data_9DRH
# 
_entry.id   9DRH 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9DRH         pdb_00009drh 10.2210/pdb9drh/pdb 
WWPDB D_1000288634 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-05 ? 
2 'Structure model' 1 1 2025-03-26 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DRH 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-25 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              niraj.tolia@nih.gov 
_pdbx_contact_author.name_first         Niraj 
_pdbx_contact_author.name_last          Tolia 
_pdbx_contact_author.name_mi            H 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-2689-1337 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Tang, W.K.'  1 ? 
'Tolia, N.H.' 2 ? 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acs Infect Dis.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2373-8227 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            11 
_citation.language                  ? 
_citation.page_first                738 
_citation.page_last                 749 
_citation.title                     
'C10-Benzoate Esters of Anhydrotetracycline Inhibit Tetracycline Destructases and Recover Tetracycline Antibacterial Activity.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acsinfecdis.4c00912 
_citation.pdbx_database_id_PubMed   39912785 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Williford, E.E.' 1  ? 
primary 'Xue, Y.P.'       2  ? 
primary 'Tang, W.K.'      3  ? 
primary 'Li, R.'          4  ? 
primary 'Jones, K.V.'     5  ? 
primary 'Blake, K.S.'     6  ? 
primary 'Blaine, H.C.'    7  ? 
primary 'Lian, X.'        8  ? 
primary 'Stallings, C.L.' 9  ? 
primary 'Tolia, N.H.'     10 ? 
primary 'Dantas, G.'      11 ? 
primary 'Wencewicz, T.A.' 12 ? 
# 
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 'Tet(X7)' 44903.766 1 ? ? ? ? 
2 non-polymer syn 
;(6aS,7S,10aS)-9-carbamoyl-7-(dimethylamino)-8,10a,12-trihydroxy-5-methyl-10,11-dioxo-6,6a,7,10,10a,11-hexahydrotetracen-1-yl pyrimidine-2-carboxylate
;
532.501   1 ? ? ? ? 
3 non-polymer syn 'FLAVIN-ADENINE DINUCLEOTIDE' 785.550   1 ? ? ? ? 
# 
_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       
;MGSSHHHHHHSSGLVPRGSHMTLLKNKKITIIGAGPVGLTMARLLQQNRVDVTVYERDKDRDARIFGGTLDLHRDSGQEA
MKRAGLLQTYYDLALPMGVNIADEKGNILTTKNVKPENRFDNPEINRNDLRTILLNSLQNDTVIWDRKLVTLEPDKEKWT
LTFEDKPSETADLVIIANGGMSKVRKFVTDTEVEETGTFNIQADIHQPEVNCPGFFQLCNGNRLMAAHQGNLLFANPNNN
GALHFGISFKTSDEWKSKTLVDFQDRNSVVDFLLKKFSDWDERYKELIRVTSSFVGLATRIFPLGKSWKSKRPLPITMIG
DAAHLMPPFAGQGVNSGLMDALILSDNLTNGKFNSIEEAIENYEQQMFAYGREAQAESIINETEMFSSDFSFQKLMNL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSSGLVPRGSHMTLLKNKKITIIGAGPVGLTMARLLQQNRVDVTVYERDKDRDARIFGGTLDLHRDSGQEA
MKRAGLLQTYYDLALPMGVNIADEKGNILTTKNVKPENRFDNPEINRNDLRTILLNSLQNDTVIWDRKLVTLEPDKEKWT
LTFEDKPSETADLVIIANGGMSKVRKFVTDTEVEETGTFNIQADIHQPEVNCPGFFQLCNGNRLMAAHQGNLLFANPNNN
GALHFGISFKTSDEWKSKTLVDFQDRNSVVDFLLKKFSDWDERYKELIRVTSSFVGLATRIFPLGKSWKSKRPLPITMIG
DAAHLMPPFAGQGVNSGLMDALILSDNLTNGKFNSIEEAIENYEQQMFAYGREAQAESIINETEMFSSDFSFQKLMNL
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 
;(6aS,7S,10aS)-9-carbamoyl-7-(dimethylamino)-8,10a,12-trihydroxy-5-methyl-10,11-dioxo-6,6a,7,10,10a,11-hexahydrotetracen-1-yl pyrimidine-2-carboxylate
;
A1BDP 
3 'FLAVIN-ADENINE DINUCLEOTIDE' FAD   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  SER n 
1 12  SER n 
1 13  GLY n 
1 14  LEU n 
1 15  VAL n 
1 16  PRO n 
1 17  ARG n 
1 18  GLY n 
1 19  SER n 
1 20  HIS n 
1 21  MET n 
1 22  THR n 
1 23  LEU n 
1 24  LEU n 
1 25  LYS n 
1 26  ASN n 
1 27  LYS n 
1 28  LYS n 
1 29  ILE n 
1 30  THR n 
1 31  ILE n 
1 32  ILE n 
1 33  GLY n 
1 34  ALA n 
1 35  GLY n 
1 36  PRO n 
1 37  VAL n 
1 38  GLY n 
1 39  LEU n 
1 40  THR n 
1 41  MET n 
1 42  ALA n 
1 43  ARG n 
1 44  LEU n 
1 45  LEU n 
1 46  GLN n 
1 47  GLN n 
1 48  ASN n 
1 49  ARG n 
1 50  VAL n 
1 51  ASP n 
1 52  VAL n 
1 53  THR n 
1 54  VAL n 
1 55  TYR n 
1 56  GLU n 
1 57  ARG n 
1 58  ASP n 
1 59  LYS n 
1 60  ASP n 
1 61  ARG n 
1 62  ASP n 
1 63  ALA n 
1 64  ARG n 
1 65  ILE n 
1 66  PHE n 
1 67  GLY n 
1 68  GLY n 
1 69  THR n 
1 70  LEU n 
1 71  ASP n 
1 72  LEU n 
1 73  HIS n 
1 74  ARG n 
1 75  ASP n 
1 76  SER n 
1 77  GLY n 
1 78  GLN n 
1 79  GLU n 
1 80  ALA n 
1 81  MET n 
1 82  LYS n 
1 83  ARG n 
1 84  ALA n 
1 85  GLY n 
1 86  LEU n 
1 87  LEU n 
1 88  GLN n 
1 89  THR n 
1 90  TYR n 
1 91  TYR n 
1 92  ASP n 
1 93  LEU n 
1 94  ALA n 
1 95  LEU n 
1 96  PRO n 
1 97  MET n 
1 98  GLY n 
1 99  VAL n 
1 100 ASN n 
1 101 ILE n 
1 102 ALA n 
1 103 ASP n 
1 104 GLU n 
1 105 LYS n 
1 106 GLY n 
1 107 ASN n 
1 108 ILE n 
1 109 LEU n 
1 110 THR n 
1 111 THR n 
1 112 LYS n 
1 113 ASN n 
1 114 VAL n 
1 115 LYS n 
1 116 PRO n 
1 117 GLU n 
1 118 ASN n 
1 119 ARG n 
1 120 PHE n 
1 121 ASP n 
1 122 ASN n 
1 123 PRO n 
1 124 GLU n 
1 125 ILE n 
1 126 ASN n 
1 127 ARG n 
1 128 ASN n 
1 129 ASP n 
1 130 LEU n 
1 131 ARG n 
1 132 THR n 
1 133 ILE n 
1 134 LEU n 
1 135 LEU n 
1 136 ASN n 
1 137 SER n 
1 138 LEU n 
1 139 GLN n 
1 140 ASN n 
1 141 ASP n 
1 142 THR n 
1 143 VAL n 
1 144 ILE n 
1 145 TRP n 
1 146 ASP n 
1 147 ARG n 
1 148 LYS n 
1 149 LEU n 
1 150 VAL n 
1 151 THR n 
1 152 LEU n 
1 153 GLU n 
1 154 PRO n 
1 155 ASP n 
1 156 LYS n 
1 157 GLU n 
1 158 LYS n 
1 159 TRP n 
1 160 THR n 
1 161 LEU n 
1 162 THR n 
1 163 PHE n 
1 164 GLU n 
1 165 ASP n 
1 166 LYS n 
1 167 PRO n 
1 168 SER n 
1 169 GLU n 
1 170 THR n 
1 171 ALA n 
1 172 ASP n 
1 173 LEU n 
1 174 VAL n 
1 175 ILE n 
1 176 ILE n 
1 177 ALA n 
1 178 ASN n 
1 179 GLY n 
1 180 GLY n 
1 181 MET n 
1 182 SER n 
1 183 LYS n 
1 184 VAL n 
1 185 ARG n 
1 186 LYS n 
1 187 PHE n 
1 188 VAL n 
1 189 THR n 
1 190 ASP n 
1 191 THR n 
1 192 GLU n 
1 193 VAL n 
1 194 GLU n 
1 195 GLU n 
1 196 THR n 
1 197 GLY n 
1 198 THR n 
1 199 PHE n 
1 200 ASN n 
1 201 ILE n 
1 202 GLN n 
1 203 ALA n 
1 204 ASP n 
1 205 ILE n 
1 206 HIS n 
1 207 GLN n 
1 208 PRO n 
1 209 GLU n 
1 210 VAL n 
1 211 ASN n 
1 212 CYS n 
1 213 PRO n 
1 214 GLY n 
1 215 PHE n 
1 216 PHE n 
1 217 GLN n 
1 218 LEU n 
1 219 CYS n 
1 220 ASN n 
1 221 GLY n 
1 222 ASN n 
1 223 ARG n 
1 224 LEU n 
1 225 MET n 
1 226 ALA n 
1 227 ALA n 
1 228 HIS n 
1 229 GLN n 
1 230 GLY n 
1 231 ASN n 
1 232 LEU n 
1 233 LEU n 
1 234 PHE n 
1 235 ALA n 
1 236 ASN n 
1 237 PRO n 
1 238 ASN n 
1 239 ASN n 
1 240 ASN n 
1 241 GLY n 
1 242 ALA n 
1 243 LEU n 
1 244 HIS n 
1 245 PHE n 
1 246 GLY n 
1 247 ILE n 
1 248 SER n 
1 249 PHE n 
1 250 LYS n 
1 251 THR n 
1 252 SER n 
1 253 ASP n 
1 254 GLU n 
1 255 TRP n 
1 256 LYS n 
1 257 SER n 
1 258 LYS n 
1 259 THR n 
1 260 LEU n 
1 261 VAL n 
1 262 ASP n 
1 263 PHE n 
1 264 GLN n 
1 265 ASP n 
1 266 ARG n 
1 267 ASN n 
1 268 SER n 
1 269 VAL n 
1 270 VAL n 
1 271 ASP n 
1 272 PHE n 
1 273 LEU n 
1 274 LEU n 
1 275 LYS n 
1 276 LYS n 
1 277 PHE n 
1 278 SER n 
1 279 ASP n 
1 280 TRP n 
1 281 ASP n 
1 282 GLU n 
1 283 ARG n 
1 284 TYR n 
1 285 LYS n 
1 286 GLU n 
1 287 LEU n 
1 288 ILE n 
1 289 ARG n 
1 290 VAL n 
1 291 THR n 
1 292 SER n 
1 293 SER n 
1 294 PHE n 
1 295 VAL n 
1 296 GLY n 
1 297 LEU n 
1 298 ALA n 
1 299 THR n 
1 300 ARG n 
1 301 ILE n 
1 302 PHE n 
1 303 PRO n 
1 304 LEU n 
1 305 GLY n 
1 306 LYS n 
1 307 SER n 
1 308 TRP n 
1 309 LYS n 
1 310 SER n 
1 311 LYS n 
1 312 ARG n 
1 313 PRO n 
1 314 LEU n 
1 315 PRO n 
1 316 ILE n 
1 317 THR n 
1 318 MET n 
1 319 ILE n 
1 320 GLY n 
1 321 ASP n 
1 322 ALA n 
1 323 ALA n 
1 324 HIS n 
1 325 LEU n 
1 326 MET n 
1 327 PRO n 
1 328 PRO n 
1 329 PHE n 
1 330 ALA n 
1 331 GLY n 
1 332 GLN n 
1 333 GLY n 
1 334 VAL n 
1 335 ASN n 
1 336 SER n 
1 337 GLY n 
1 338 LEU n 
1 339 MET n 
1 340 ASP n 
1 341 ALA n 
1 342 LEU n 
1 343 ILE n 
1 344 LEU n 
1 345 SER n 
1 346 ASP n 
1 347 ASN n 
1 348 LEU n 
1 349 THR n 
1 350 ASN n 
1 351 GLY n 
1 352 LYS n 
1 353 PHE n 
1 354 ASN n 
1 355 SER n 
1 356 ILE n 
1 357 GLU n 
1 358 GLU n 
1 359 ALA n 
1 360 ILE n 
1 361 GLU n 
1 362 ASN n 
1 363 TYR n 
1 364 GLU n 
1 365 GLN n 
1 366 GLN n 
1 367 MET n 
1 368 PHE n 
1 369 ALA n 
1 370 TYR n 
1 371 GLY n 
1 372 ARG n 
1 373 GLU n 
1 374 ALA n 
1 375 GLN n 
1 376 ALA n 
1 377 GLU n 
1 378 SER n 
1 379 ILE n 
1 380 ILE n 
1 381 ASN n 
1 382 GLU n 
1 383 THR n 
1 384 GLU n 
1 385 MET n 
1 386 PHE n 
1 387 SER n 
1 388 SER n 
1 389 ASP n 
1 390 PHE n 
1 391 SER n 
1 392 PHE n 
1 393 GLN n 
1 394 LYS n 
1 395 LEU n 
1 396 MET n 
1 397 ASN n 
1 398 LEU 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                   398 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Pseudomonas aeruginosa' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     287 
_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 
A1BDP non-polymer         . 
;(6aS,7S,10aS)-9-carbamoyl-7-(dimethylamino)-8,10a,12-trihydroxy-5-methyl-10,11-dioxo-6,6a,7,10,10a,11-hexahydrotetracen-1-yl pyrimidine-2-carboxylate
;
? 'C27 H24 N4 O8'     532.501 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'        89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'    175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'       132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'        133.103 
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'      121.158 
FAD   non-polymer         . 'FLAVIN-ADENINE DINUCLEOTIDE' ? 'C27 H33 N9 O15 P2' 785.550 
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'      146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'        147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'        75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'    156.162 
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'       131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'       131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'    147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'     149.211 
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'       165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'        115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'        105.093 
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'        119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'     204.225 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'       181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   2   ?   ?   ?   A . n 
A 1 2   GLY 2   3   ?   ?   ?   A . n 
A 1 3   SER 3   4   ?   ?   ?   A . n 
A 1 4   SER 4   5   ?   ?   ?   A . n 
A 1 5   HIS 5   6   ?   ?   ?   A . n 
A 1 6   HIS 6   7   ?   ?   ?   A . n 
A 1 7   HIS 7   8   ?   ?   ?   A . n 
A 1 8   HIS 8   9   ?   ?   ?   A . n 
A 1 9   HIS 9   10  ?   ?   ?   A . n 
A 1 10  HIS 10  11  ?   ?   ?   A . n 
A 1 11  SER 11  12  ?   ?   ?   A . n 
A 1 12  SER 12  13  ?   ?   ?   A . n 
A 1 13  GLY 13  14  ?   ?   ?   A . n 
A 1 14  LEU 14  15  ?   ?   ?   A . n 
A 1 15  VAL 15  16  ?   ?   ?   A . n 
A 1 16  PRO 16  17  ?   ?   ?   A . n 
A 1 17  ARG 17  18  ?   ?   ?   A . n 
A 1 18  GLY 18  19  ?   ?   ?   A . n 
A 1 19  SER 19  20  ?   ?   ?   A . n 
A 1 20  HIS 20  21  ?   ?   ?   A . n 
A 1 21  MET 21  22  ?   ?   ?   A . n 
A 1 22  THR 22  23  23  THR THR A . n 
A 1 23  LEU 23  24  24  LEU LEU A . n 
A 1 24  LEU 24  25  25  LEU LEU A . n 
A 1 25  LYS 25  26  26  LYS LYS A . n 
A 1 26  ASN 26  27  27  ASN ASN A . n 
A 1 27  LYS 27  28  28  LYS LYS A . n 
A 1 28  LYS 28  29  29  LYS LYS A . n 
A 1 29  ILE 29  30  30  ILE ILE A . n 
A 1 30  THR 30  31  31  THR THR A . n 
A 1 31  ILE 31  32  32  ILE ILE A . n 
A 1 32  ILE 32  33  33  ILE ILE A . n 
A 1 33  GLY 33  34  34  GLY GLY A . n 
A 1 34  ALA 34  35  35  ALA ALA A . n 
A 1 35  GLY 35  36  36  GLY GLY A . n 
A 1 36  PRO 36  37  37  PRO PRO A . n 
A 1 37  VAL 37  38  38  VAL VAL A . n 
A 1 38  GLY 38  39  39  GLY GLY A . n 
A 1 39  LEU 39  40  40  LEU LEU A . n 
A 1 40  THR 40  41  41  THR THR A . n 
A 1 41  MET 41  42  42  MET MET A . n 
A 1 42  ALA 42  43  43  ALA ALA A . n 
A 1 43  ARG 43  44  44  ARG ARG A . n 
A 1 44  LEU 44  45  45  LEU LEU A . n 
A 1 45  LEU 45  46  46  LEU LEU A . n 
A 1 46  GLN 46  47  47  GLN GLN A . n 
A 1 47  GLN 47  48  48  GLN GLN A . n 
A 1 48  ASN 48  49  49  ASN ASN A . n 
A 1 49  ARG 49  50  50  ARG ARG A . n 
A 1 50  VAL 50  51  51  VAL VAL A . n 
A 1 51  ASP 51  52  52  ASP ASP A . n 
A 1 52  VAL 52  53  53  VAL VAL A . n 
A 1 53  THR 53  54  54  THR THR A . n 
A 1 54  VAL 54  55  55  VAL VAL A . n 
A 1 55  TYR 55  56  56  TYR TYR A . n 
A 1 56  GLU 56  57  57  GLU GLU A . n 
A 1 57  ARG 57  58  58  ARG ARG A . n 
A 1 58  ASP 58  59  59  ASP ASP A . n 
A 1 59  LYS 59  60  60  LYS LYS A . n 
A 1 60  ASP 60  61  61  ASP ASP A . n 
A 1 61  ARG 61  62  62  ARG ARG A . n 
A 1 62  ASP 62  63  63  ASP ASP A . n 
A 1 63  ALA 63  64  64  ALA ALA A . n 
A 1 64  ARG 64  65  65  ARG ARG A . n 
A 1 65  ILE 65  66  66  ILE ILE A . n 
A 1 66  PHE 66  67  67  PHE PHE A . n 
A 1 67  GLY 67  68  68  GLY GLY A . n 
A 1 68  GLY 68  69  69  GLY GLY A . n 
A 1 69  THR 69  70  70  THR THR A . n 
A 1 70  LEU 70  71  71  LEU LEU A . n 
A 1 71  ASP 71  72  72  ASP ASP A . n 
A 1 72  LEU 72  73  73  LEU LEU A . n 
A 1 73  HIS 73  74  74  HIS HIS A . n 
A 1 74  ARG 74  75  75  ARG ARG A . n 
A 1 75  ASP 75  76  76  ASP ASP A . n 
A 1 76  SER 76  77  77  SER SER A . n 
A 1 77  GLY 77  78  78  GLY GLY A . n 
A 1 78  GLN 78  79  79  GLN GLN A . n 
A 1 79  GLU 79  80  80  GLU GLU A . n 
A 1 80  ALA 80  81  81  ALA ALA A . n 
A 1 81  MET 81  82  82  MET MET A . n 
A 1 82  LYS 82  83  83  LYS LYS A . n 
A 1 83  ARG 83  84  84  ARG ARG A . n 
A 1 84  ALA 84  85  85  ALA ALA A . n 
A 1 85  GLY 85  86  86  GLY GLY A . n 
A 1 86  LEU 86  87  87  LEU LEU A . n 
A 1 87  LEU 87  88  88  LEU LEU A . n 
A 1 88  GLN 88  89  89  GLN GLN A . n 
A 1 89  THR 89  90  90  THR THR A . n 
A 1 90  TYR 90  91  91  TYR TYR A . n 
A 1 91  TYR 91  92  92  TYR TYR A . n 
A 1 92  ASP 92  93  93  ASP ASP A . n 
A 1 93  LEU 93  94  94  LEU LEU A . n 
A 1 94  ALA 94  95  95  ALA ALA A . n 
A 1 95  LEU 95  96  96  LEU LEU A . n 
A 1 96  PRO 96  97  97  PRO PRO A . n 
A 1 97  MET 97  98  98  MET MET A . n 
A 1 98  GLY 98  99  99  GLY GLY A . n 
A 1 99  VAL 99  100 100 VAL VAL A . n 
A 1 100 ASN 100 101 101 ASN ASN A . n 
A 1 101 ILE 101 102 102 ILE ILE A . n 
A 1 102 ALA 102 103 103 ALA ALA A . n 
A 1 103 ASP 103 104 104 ASP ASP A . n 
A 1 104 GLU 104 105 105 GLU GLU A . n 
A 1 105 LYS 105 106 106 LYS LYS A . n 
A 1 106 GLY 106 107 107 GLY GLY A . n 
A 1 107 ASN 107 108 108 ASN ASN A . n 
A 1 108 ILE 108 109 109 ILE ILE A . n 
A 1 109 LEU 109 110 110 LEU LEU A . n 
A 1 110 THR 110 111 111 THR THR A . n 
A 1 111 THR 111 112 112 THR THR A . n 
A 1 112 LYS 112 113 113 LYS LYS A . n 
A 1 113 ASN 113 114 114 ASN ASN A . n 
A 1 114 VAL 114 115 115 VAL VAL A . n 
A 1 115 LYS 115 116 116 LYS LYS A . n 
A 1 116 PRO 116 117 117 PRO PRO A . n 
A 1 117 GLU 117 118 118 GLU GLU A . n 
A 1 118 ASN 118 119 119 ASN ASN A . n 
A 1 119 ARG 119 120 120 ARG ARG A . n 
A 1 120 PHE 120 121 121 PHE PHE A . n 
A 1 121 ASP 121 122 122 ASP ASP A . n 
A 1 122 ASN 122 123 123 ASN ASN A . n 
A 1 123 PRO 123 124 124 PRO PRO A . n 
A 1 124 GLU 124 125 125 GLU GLU A . n 
A 1 125 ILE 125 126 126 ILE ILE A . n 
A 1 126 ASN 126 127 127 ASN ASN A . n 
A 1 127 ARG 127 128 128 ARG ARG A . n 
A 1 128 ASN 128 129 129 ASN ASN A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 LEU 130 131 131 LEU LEU A . n 
A 1 131 ARG 131 132 132 ARG ARG A . n 
A 1 132 THR 132 133 133 THR THR A . n 
A 1 133 ILE 133 134 134 ILE ILE A . n 
A 1 134 LEU 134 135 135 LEU LEU A . n 
A 1 135 LEU 135 136 136 LEU LEU A . n 
A 1 136 ASN 136 137 137 ASN ASN A . n 
A 1 137 SER 137 138 138 SER SER A . n 
A 1 138 LEU 138 139 139 LEU LEU A . n 
A 1 139 GLN 139 140 140 GLN GLN A . n 
A 1 140 ASN 140 141 141 ASN ASN A . n 
A 1 141 ASP 141 142 142 ASP ASP A . n 
A 1 142 THR 142 143 143 THR THR A . n 
A 1 143 VAL 143 144 144 VAL VAL A . n 
A 1 144 ILE 144 145 145 ILE ILE A . n 
A 1 145 TRP 145 146 146 TRP TRP A . n 
A 1 146 ASP 146 147 147 ASP ASP A . n 
A 1 147 ARG 147 148 148 ARG ARG A . n 
A 1 148 LYS 148 149 149 LYS LYS A . n 
A 1 149 LEU 149 150 150 LEU LEU A . n 
A 1 150 VAL 150 151 151 VAL VAL A . n 
A 1 151 THR 151 152 152 THR THR A . n 
A 1 152 LEU 152 153 153 LEU LEU A . n 
A 1 153 GLU 153 154 154 GLU GLU A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 ASP 155 156 156 ASP ASP A . n 
A 1 156 LYS 156 157 157 LYS LYS A . n 
A 1 157 GLU 157 158 158 GLU GLU A . n 
A 1 158 LYS 158 159 159 LYS LYS A . n 
A 1 159 TRP 159 160 160 TRP TRP A . n 
A 1 160 THR 160 161 161 THR THR A . n 
A 1 161 LEU 161 162 162 LEU LEU A . n 
A 1 162 THR 162 163 163 THR THR A . n 
A 1 163 PHE 163 164 164 PHE PHE A . n 
A 1 164 GLU 164 165 165 GLU GLU A . n 
A 1 165 ASP 165 166 166 ASP ASP A . n 
A 1 166 LYS 166 167 167 LYS LYS A . n 
A 1 167 PRO 167 168 168 PRO PRO A . n 
A 1 168 SER 168 169 169 SER SER A . n 
A 1 169 GLU 169 170 170 GLU GLU A . n 
A 1 170 THR 170 171 171 THR THR A . n 
A 1 171 ALA 171 172 172 ALA ALA A . n 
A 1 172 ASP 172 173 173 ASP ASP A . n 
A 1 173 LEU 173 174 174 LEU LEU A . n 
A 1 174 VAL 174 175 175 VAL VAL A . n 
A 1 175 ILE 175 176 176 ILE ILE A . n 
A 1 176 ILE 176 177 177 ILE ILE A . n 
A 1 177 ALA 177 178 178 ALA ALA A . n 
A 1 178 ASN 178 179 179 ASN ASN A . n 
A 1 179 GLY 179 180 180 GLY GLY A . n 
A 1 180 GLY 180 181 181 GLY GLY A . n 
A 1 181 MET 181 182 182 MET MET A . n 
A 1 182 SER 182 183 183 SER SER A . n 
A 1 183 LYS 183 184 184 LYS LYS A . n 
A 1 184 VAL 184 185 185 VAL VAL A . n 
A 1 185 ARG 185 186 186 ARG ARG A . n 
A 1 186 LYS 186 187 187 LYS LYS A . n 
A 1 187 PHE 187 188 188 PHE PHE A . n 
A 1 188 VAL 188 189 189 VAL VAL A . n 
A 1 189 THR 189 190 190 THR THR A . n 
A 1 190 ASP 190 191 191 ASP ASP A . n 
A 1 191 THR 191 192 192 THR THR A . n 
A 1 192 GLU 192 193 193 GLU GLU A . n 
A 1 193 VAL 193 194 194 VAL VAL A . n 
A 1 194 GLU 194 195 195 GLU GLU A . n 
A 1 195 GLU 195 196 196 GLU GLU A . n 
A 1 196 THR 196 197 197 THR THR A . n 
A 1 197 GLY 197 198 198 GLY GLY A . n 
A 1 198 THR 198 199 199 THR THR A . n 
A 1 199 PHE 199 200 200 PHE PHE A . n 
A 1 200 ASN 200 201 201 ASN ASN A . n 
A 1 201 ILE 201 202 202 ILE ILE A . n 
A 1 202 GLN 202 203 203 GLN GLN A . n 
A 1 203 ALA 203 204 204 ALA ALA A . n 
A 1 204 ASP 204 205 205 ASP ASP A . n 
A 1 205 ILE 205 206 206 ILE ILE A . n 
A 1 206 HIS 206 207 207 HIS HIS A . n 
A 1 207 GLN 207 208 208 GLN GLN A . n 
A 1 208 PRO 208 209 209 PRO PRO A . n 
A 1 209 GLU 209 210 210 GLU GLU A . n 
A 1 210 VAL 210 211 211 VAL VAL A . n 
A 1 211 ASN 211 212 212 ASN ASN A . n 
A 1 212 CYS 212 213 213 CYS CYS A . n 
A 1 213 PRO 213 214 214 PRO PRO A . n 
A 1 214 GLY 214 215 215 GLY GLY A . n 
A 1 215 PHE 215 216 216 PHE PHE A . n 
A 1 216 PHE 216 217 217 PHE PHE A . n 
A 1 217 GLN 217 218 218 GLN GLN A . n 
A 1 218 LEU 218 219 219 LEU LEU A . n 
A 1 219 CYS 219 220 220 CYS CYS A . n 
A 1 220 ASN 220 221 221 ASN ASN A . n 
A 1 221 GLY 221 222 222 GLY GLY A . n 
A 1 222 ASN 222 223 223 ASN ASN A . n 
A 1 223 ARG 223 224 224 ARG ARG A . n 
A 1 224 LEU 224 225 225 LEU LEU A . n 
A 1 225 MET 225 226 226 MET MET A . n 
A 1 226 ALA 226 227 227 ALA ALA A . n 
A 1 227 ALA 227 228 228 ALA ALA A . n 
A 1 228 HIS 228 229 229 HIS HIS A . n 
A 1 229 GLN 229 230 230 GLN GLN A . n 
A 1 230 GLY 230 231 231 GLY GLY A . n 
A 1 231 ASN 231 232 232 ASN ASN A . n 
A 1 232 LEU 232 233 233 LEU LEU A . n 
A 1 233 LEU 233 234 234 LEU LEU A . n 
A 1 234 PHE 234 235 235 PHE PHE A . n 
A 1 235 ALA 235 236 236 ALA ALA A . n 
A 1 236 ASN 236 237 237 ASN ASN A . n 
A 1 237 PRO 237 238 238 PRO PRO A . n 
A 1 238 ASN 238 239 239 ASN ASN A . n 
A 1 239 ASN 239 240 240 ASN ASN A . n 
A 1 240 ASN 240 241 241 ASN ASN A . n 
A 1 241 GLY 241 242 242 GLY GLY A . n 
A 1 242 ALA 242 243 243 ALA ALA A . n 
A 1 243 LEU 243 244 244 LEU LEU A . n 
A 1 244 HIS 244 245 245 HIS HIS A . n 
A 1 245 PHE 245 246 246 PHE PHE A . n 
A 1 246 GLY 246 247 247 GLY GLY A . n 
A 1 247 ILE 247 248 248 ILE ILE A . n 
A 1 248 SER 248 249 249 SER SER A . n 
A 1 249 PHE 249 250 250 PHE PHE A . n 
A 1 250 LYS 250 251 251 LYS LYS A . n 
A 1 251 THR 251 252 252 THR THR A . n 
A 1 252 SER 252 253 253 SER SER A . n 
A 1 253 ASP 253 254 ?   ?   ?   A . n 
A 1 254 GLU 254 255 ?   ?   ?   A . n 
A 1 255 TRP 255 256 ?   ?   ?   A . n 
A 1 256 LYS 256 257 ?   ?   ?   A . n 
A 1 257 SER 257 258 ?   ?   ?   A . n 
A 1 258 LYS 258 259 ?   ?   ?   A . n 
A 1 259 THR 259 260 260 THR THR A . n 
A 1 260 LEU 260 261 261 LEU LEU A . n 
A 1 261 VAL 261 262 262 VAL VAL A . n 
A 1 262 ASP 262 263 263 ASP ASP A . n 
A 1 263 PHE 263 264 264 PHE PHE A . n 
A 1 264 GLN 264 265 265 GLN GLN A . n 
A 1 265 ASP 265 266 266 ASP ASP A . n 
A 1 266 ARG 266 267 267 ARG ARG A . n 
A 1 267 ASN 267 268 268 ASN ASN A . n 
A 1 268 SER 268 269 269 SER SER A . n 
A 1 269 VAL 269 270 270 VAL VAL A . n 
A 1 270 VAL 270 271 271 VAL VAL A . n 
A 1 271 ASP 271 272 272 ASP ASP A . n 
A 1 272 PHE 272 273 273 PHE PHE A . n 
A 1 273 LEU 273 274 274 LEU LEU A . n 
A 1 274 LEU 274 275 275 LEU LEU A . n 
A 1 275 LYS 275 276 276 LYS LYS A . n 
A 1 276 LYS 276 277 277 LYS LYS A . n 
A 1 277 PHE 277 278 278 PHE PHE A . n 
A 1 278 SER 278 279 279 SER SER A . n 
A 1 279 ASP 279 280 280 ASP ASP A . n 
A 1 280 TRP 280 281 281 TRP TRP A . n 
A 1 281 ASP 281 282 282 ASP ASP A . n 
A 1 282 GLU 282 283 283 GLU GLU A . n 
A 1 283 ARG 283 284 284 ARG ARG A . n 
A 1 284 TYR 284 285 285 TYR TYR A . n 
A 1 285 LYS 285 286 286 LYS LYS A . n 
A 1 286 GLU 286 287 287 GLU GLU A . n 
A 1 287 LEU 287 288 288 LEU LEU A . n 
A 1 288 ILE 288 289 289 ILE ILE A . n 
A 1 289 ARG 289 290 290 ARG ARG A . n 
A 1 290 VAL 290 291 291 VAL VAL A . n 
A 1 291 THR 291 292 292 THR THR A . n 
A 1 292 SER 292 293 293 SER SER A . n 
A 1 293 SER 293 294 294 SER SER A . n 
A 1 294 PHE 294 295 295 PHE PHE A . n 
A 1 295 VAL 295 296 296 VAL VAL A . n 
A 1 296 GLY 296 297 297 GLY GLY A . n 
A 1 297 LEU 297 298 298 LEU LEU A . n 
A 1 298 ALA 298 299 299 ALA ALA A . n 
A 1 299 THR 299 300 300 THR THR A . n 
A 1 300 ARG 300 301 301 ARG ARG A . n 
A 1 301 ILE 301 302 302 ILE ILE A . n 
A 1 302 PHE 302 303 303 PHE PHE A . n 
A 1 303 PRO 303 304 304 PRO PRO A . n 
A 1 304 LEU 304 305 305 LEU LEU A . n 
A 1 305 GLY 305 306 306 GLY GLY A . n 
A 1 306 LYS 306 307 307 LYS LYS A . n 
A 1 307 SER 307 308 308 SER SER A . n 
A 1 308 TRP 308 309 309 TRP TRP A . n 
A 1 309 LYS 309 310 310 LYS LYS A . n 
A 1 310 SER 310 311 311 SER SER A . n 
A 1 311 LYS 311 312 312 LYS LYS A . n 
A 1 312 ARG 312 313 313 ARG ARG A . n 
A 1 313 PRO 313 314 314 PRO PRO A . n 
A 1 314 LEU 314 315 315 LEU LEU A . n 
A 1 315 PRO 315 316 316 PRO PRO A . n 
A 1 316 ILE 316 317 317 ILE ILE A . n 
A 1 317 THR 317 318 318 THR THR A . n 
A 1 318 MET 318 319 319 MET MET A . n 
A 1 319 ILE 319 320 320 ILE ILE A . n 
A 1 320 GLY 320 321 321 GLY GLY A . n 
A 1 321 ASP 321 322 322 ASP ASP A . n 
A 1 322 ALA 322 323 323 ALA ALA A . n 
A 1 323 ALA 323 324 324 ALA ALA A . n 
A 1 324 HIS 324 325 325 HIS HIS A . n 
A 1 325 LEU 325 326 326 LEU LEU A . n 
A 1 326 MET 326 327 327 MET MET A . n 
A 1 327 PRO 327 328 328 PRO PRO A . n 
A 1 328 PRO 328 329 329 PRO PRO A . n 
A 1 329 PHE 329 330 330 PHE PHE A . n 
A 1 330 ALA 330 331 331 ALA ALA A . n 
A 1 331 GLY 331 332 332 GLY GLY A . n 
A 1 332 GLN 332 333 333 GLN GLN A . n 
A 1 333 GLY 333 334 334 GLY GLY A . n 
A 1 334 VAL 334 335 335 VAL VAL A . n 
A 1 335 ASN 335 336 336 ASN ASN A . n 
A 1 336 SER 336 337 337 SER SER A . n 
A 1 337 GLY 337 338 338 GLY GLY A . n 
A 1 338 LEU 338 339 339 LEU LEU A . n 
A 1 339 MET 339 340 340 MET MET A . n 
A 1 340 ASP 340 341 341 ASP ASP A . n 
A 1 341 ALA 341 342 342 ALA ALA A . n 
A 1 342 LEU 342 343 343 LEU LEU A . n 
A 1 343 ILE 343 344 344 ILE ILE A . n 
A 1 344 LEU 344 345 345 LEU LEU A . n 
A 1 345 SER 345 346 346 SER SER A . n 
A 1 346 ASP 346 347 347 ASP ASP A . n 
A 1 347 ASN 347 348 348 ASN ASN A . n 
A 1 348 LEU 348 349 349 LEU LEU A . n 
A 1 349 THR 349 350 350 THR THR A . n 
A 1 350 ASN 350 351 351 ASN ASN A . n 
A 1 351 GLY 351 352 352 GLY GLY A . n 
A 1 352 LYS 352 353 353 LYS LYS A . n 
A 1 353 PHE 353 354 354 PHE PHE A . n 
A 1 354 ASN 354 355 355 ASN ASN A . n 
A 1 355 SER 355 356 356 SER SER A . n 
A 1 356 ILE 356 357 357 ILE ILE A . n 
A 1 357 GLU 357 358 358 GLU GLU A . n 
A 1 358 GLU 358 359 359 GLU GLU A . n 
A 1 359 ALA 359 360 360 ALA ALA A . n 
A 1 360 ILE 360 361 361 ILE ILE A . n 
A 1 361 GLU 361 362 362 GLU GLU A . n 
A 1 362 ASN 362 363 363 ASN ASN A . n 
A 1 363 TYR 363 364 364 TYR TYR A . n 
A 1 364 GLU 364 365 365 GLU GLU A . n 
A 1 365 GLN 365 366 366 GLN GLN A . n 
A 1 366 GLN 366 367 367 GLN GLN A . n 
A 1 367 MET 367 368 368 MET MET A . n 
A 1 368 PHE 368 369 369 PHE PHE A . n 
A 1 369 ALA 369 370 370 ALA ALA A . n 
A 1 370 TYR 370 371 371 TYR TYR A . n 
A 1 371 GLY 371 372 372 GLY GLY A . n 
A 1 372 ARG 372 373 373 ARG ARG A . n 
A 1 373 GLU 373 374 374 GLU GLU A . n 
A 1 374 ALA 374 375 375 ALA ALA A . n 
A 1 375 GLN 375 376 376 GLN GLN A . n 
A 1 376 ALA 376 377 377 ALA ALA A . n 
A 1 377 GLU 377 378 378 GLU GLU A . n 
A 1 378 SER 378 379 379 SER SER A . n 
A 1 379 ILE 379 380 380 ILE ILE A . n 
A 1 380 ILE 380 381 381 ILE ILE A . n 
A 1 381 ASN 381 382 382 ASN ASN A . n 
A 1 382 GLU 382 383 383 GLU GLU A . n 
A 1 383 THR 383 384 384 THR THR A . n 
A 1 384 GLU 384 385 385 GLU GLU A . n 
A 1 385 MET 385 386 386 MET MET A . n 
A 1 386 PHE 386 387 387 PHE PHE A . n 
A 1 387 SER 387 388 388 SER SER A . n 
A 1 388 SER 388 389 389 SER SER A . n 
A 1 389 ASP 389 390 390 ASP ASP A . n 
A 1 390 PHE 390 391 391 PHE PHE A . n 
A 1 391 SER 391 392 392 SER SER A . n 
A 1 392 PHE 392 393 393 PHE PHE A . n 
A 1 393 GLN 393 394 ?   ?   ?   A . n 
A 1 394 LYS 394 395 ?   ?   ?   A . n 
A 1 395 LEU 395 396 ?   ?   ?   A . n 
A 1 396 MET 396 397 ?   ?   ?   A . n 
A 1 397 ASN 397 398 ?   ?   ?   A . n 
A 1 398 LEU 398 399 ?   ?   ?   A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 A1BDP ? ? A1BDP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 FAD   ? ? FAD   ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 
B 2 A1BDP 1 401 401 A1BDP ABE A . 
C 3 FAD   1 402 402 FAD   FAD A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.21.1_5286 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DRH 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     132.730 
_cell.length_a_esd                 ? 
_cell.length_b                     132.730 
_cell.length_b_esd                 ? 
_cell.length_c                     57.780 
_cell.length_c_esd                 ? 
_cell.volume                       1017924.786 
_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                         9DRH 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                92 
_symmetry.space_group_name_Hall            'P 4abw 2nw' 
_symmetry.space_group_name_H-M             'P 41 21 2' 
_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                   9DRH 
_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             2.83 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          56.59 
_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, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M Hepes, pH 7.5, 0.2 M ammonium sulfate, 16% PEG 4000 and 10% isopropanol' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            292 
# 
_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 PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-04-10 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1 
_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                        'ALS BEAMLINE 5.0.2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   5.0.2 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          121.98 
_reflns.entry_id                                       9DRH 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.3 
_reflns.d_resolution_low                               19.79 
_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                                     8118 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.79 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.99 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    3.3 
_reflns_shell.d_res_low                                     3.51 
_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                             8117 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.4 
_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               ? 
# 
_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                               149.74 
_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                                 9DRH 
_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                            3.30 
_refine.ls_d_res_low                             19.79 
_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                     8118 
_refine.ls_number_reflns_R_free                  814 
_refine.ls_number_reflns_R_work                  7304 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.66 
_refine.ls_percent_reflns_R_free                 10.03 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2395 
_refine.ls_R_factor_R_free                       0.2914 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2335 
_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                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 35.3950 
_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                            0.5723 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       3.30 
_refine_hist.d_res_low                        19.79 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               2980 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2888 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         92 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0021  ? 3041 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.4594  ? 4129 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0396  ? 454  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0051  ? 531  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 13.0649 ? 1161 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 3.30 3.51  . . 131 1185 100.00 . . . . 0.3675 . . . . . . . . . . . 0.4219 
'X-RAY DIFFRACTION' 3.51 3.77  . . 134 1204 100.00 . . . . 0.3028 . . . . . . . . . . . 0.3777 
'X-RAY DIFFRACTION' 3.77 4.15  . . 133 1194 99.77  . . . . 0.2855 . . . . . . . . . . . 0.3560 
'X-RAY DIFFRACTION' 4.15 4.75  . . 135 1196 98.89  . . . . 0.2326 . . . . . . . . . . . 0.3267 
'X-RAY DIFFRACTION' 4.75 5.95  . . 135 1221 99.34  . . . . 0.2422 . . . . . . . . . . . 0.2607 
'X-RAY DIFFRACTION' 5.95 19.79 . . 146 1304 99.93  . . . . 0.1870 . . . . . . . . . . . 0.2418 
# 
_struct.entry_id                     9DRH 
_struct.title                        'Crystal structure of Tet(X7) bound to anhydrotetracycline C10-benzoate ester' 
_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        9DRH 
_struct_keywords.text            'Inhibitor, OXIDOREDUCTASE, OXIDOREDUCTASE-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE/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 2 ? 
C N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    9DRH 
_struct_ref.pdbx_db_accession          9DRH 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9DRH 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 398 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             9DRH 
_struct_ref_seq.db_align_beg                  2 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  399 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       2 
_struct_ref_seq.pdbx_auth_seq_align_end       399 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 35  ? GLN A 47  ? GLY A 36  GLN A 48  1 ? 13 
HELX_P HELX_P2  AA2 SER A 76  ? ALA A 84  ? SER A 77  ALA A 85  1 ? 9  
HELX_P HELX_P3  AA3 LEU A 86  ? ALA A 94  ? LEU A 87  ALA A 95  1 ? 9  
HELX_P HELX_P4  AA4 LYS A 115 ? ARG A 119 ? LYS A 116 ARG A 120 5 ? 5  
HELX_P HELX_P5  AA5 ASN A 126 ? LEU A 138 ? ASN A 127 LEU A 139 1 ? 13 
HELX_P HELX_P6  AA6 GLN A 207 ? CYS A 212 ? GLN A 208 CYS A 213 1 ? 6  
HELX_P HELX_P7  AA7 CYS A 212 ? ASN A 220 ? CYS A 213 ASN A 221 1 ? 9  
HELX_P HELX_P8  AA8 ASP A 265 ? PHE A 277 ? ASP A 266 PHE A 278 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 281 ? THR A 291 ? ASP A 282 THR A 292 1 ? 11 
HELX_P HELX_P10 AB1 GLY A 320 ? LEU A 325 ? GLY A 321 LEU A 326 1 ? 6  
HELX_P HELX_P11 AB2 GLN A 332 ? ASN A 350 ? GLN A 333 ASN A 351 1 ? 19 
HELX_P HELX_P12 AB3 SER A 355 ? PHE A 386 ? SER A 356 PHE A 387 1 ? 32 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
AA3 ? 7 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 143 ? ILE A 144 ? VAL A 144 ILE A 145 
AA1 2 VAL A 52  ? TYR A 55  ? VAL A 53  TYR A 56  
AA1 3 ILE A 29  ? ILE A 32  ? ILE A 30  ILE A 33  
AA1 4 LEU A 173 ? ILE A 176 ? LEU A 174 ILE A 177 
AA1 5 ILE A 316 ? MET A 318 ? ILE A 317 MET A 319 
AA2 1 LEU A 70  ? ASP A 71  ? LEU A 71  ASP A 72  
AA2 2 GLU A 124 ? ILE A 125 ? GLU A 125 ILE A 126 
AA3 1 ILE A 108 ? THR A 111 ? ILE A 109 THR A 112 
AA3 2 VAL A 99  ? ALA A 102 ? VAL A 100 ALA A 103 
AA3 3 ARG A 223 ? HIS A 228 ? ARG A 224 HIS A 229 
AA3 4 ASN A 231 ? ASN A 239 ? ASN A 232 ASN A 240 
AA3 5 ALA A 242 ? LYS A 250 ? ALA A 243 LYS A 251 
AA3 6 GLU A 194 ? HIS A 206 ? GLU A 195 HIS A 207 
AA3 7 VAL A 295 ? ILE A 301 ? VAL A 296 ILE A 302 
AA4 1 LEU A 149 ? PRO A 154 ? LEU A 150 PRO A 155 
AA4 2 TRP A 159 ? PHE A 163 ? TRP A 160 PHE A 164 
AA4 3 LYS A 166 ? ALA A 171 ? LYS A 167 ALA A 172 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ILE A 144 ? O ILE A 145 N VAL A 54  ? N VAL A 55  
AA1 2 3 O THR A 53  ? O THR A 54  N ILE A 31  ? N ILE A 32  
AA1 3 4 N ILE A 32  ? N ILE A 33  O ILE A 175 ? O ILE A 176 
AA1 4 5 N ILE A 176 ? N ILE A 177 O THR A 317 ? O THR A 318 
AA2 1 2 N LEU A 70  ? N LEU A 71  O ILE A 125 ? O ILE A 126 
AA3 1 2 O LEU A 109 ? O LEU A 110 N ILE A 101 ? N ILE A 102 
AA3 2 3 N ASN A 100 ? N ASN A 101 O MET A 225 ? O MET A 226 
AA3 3 4 N ALA A 226 ? N ALA A 227 O LEU A 233 ? O LEU A 234 
AA3 4 5 N ASN A 239 ? N ASN A 240 O ALA A 242 ? O ALA A 243 
AA3 5 6 O LEU A 243 ? O LEU A 244 N ILE A 205 ? N ILE A 206 
AA3 6 7 N ASN A 200 ? N ASN A 201 O LEU A 297 ? O LEU A 298 
AA4 1 2 N VAL A 150 ? N VAL A 151 O THR A 162 ? O THR A 163 
AA4 2 3 N LEU A 161 ? N LEU A 162 O GLU A 169 ? O GLU A 170 
# 
_pdbx_entry_details.entry_id                   9DRH 
_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 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   LYS 
_pdbx_validate_close_contact.auth_seq_id_1    187 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   HZ2 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   LYS 
_pdbx_validate_close_contact.auth_seq_id_2    310 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.59 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ALA A 35  ? ? -95.70  32.48  
2 1 SER A 77  ? ? -131.98 -79.92 
3 1 PHE A 121 ? ? -108.82 49.21  
4 1 GLU A 158 ? ? -143.52 -22.20 
5 1 ALA A 178 ? ? -142.72 30.46  
6 1 HIS A 325 ? ? -159.73 54.58  
7 1 SER A 392 ? ? -151.28 34.68  
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 -y+1/2,x+1/2,z+1/4  
3 y+1/2,-x+1/2,z+3/4  
4 x+1/2,-y+1/2,-z+3/4 
5 -x+1/2,y+1/2,-z+1/4 
6 -x,-y,z+1/2         
7 y,x,-z              
8 -y,-x,-z+1/2        
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 4.47317122141 -37.8414667372 -3.82099654707 1.2381027779  ? -0.0690380286075 ? -0.0863061057097 ? 
1.29660992829 ? 0.063093259577   ? 1.51575121963 ? 0.923384299396 ? 0.570908424928  ? -0.164817714253 ? 0.556653574278    ? 
0.516834331489 ? 1.74410687709 ? 0.68185828698  ? 0.42492025954   ? -0.461264907896 ? -0.497010792929 ? -0.263838511244 ? 
0.674432803733  ? -0.216191929217 ? -0.555289290855 ? -3.09508699496e-05 ? 
2 'X-RAY DIFFRACTION' ? refined 12.9427007128 -43.0690562746 7.48072380092  1.30429840912 ? -0.438475689021  ? 0.119854488509   ? 
1.16029548143 ? -0.150110045965  ? 1.24955426991 ? 4.62617659177  ? -2.98567569716  ? -0.461198524791 ? 4.10054707773     ? 
-1.61658956759 ? 2.17861189721 ? 0.706556042973 ? -0.11953433965  ? -0.143605254819 ? 0.0162101731558 ? -0.154687082738 ? 
0.787135778042  ? -0.17133506652  ? 0.101237607158  ? 0.000966050241626  ? 
3 'X-RAY DIFFRACTION' ? refined 25.6914461838 -52.0477260369 16.6026678366  1.52955652551 ? -0.433164387979  ? 0.0253386114514  ? 
1.70919329565 ? -0.0767914045099 ? 1.14740452027 ? 0.589054379881 ? -1.16889073039  ? 0.950150365075  ? 2.33602297824     ? 
-1.87574019556 ? 1.49312953301 ? 0.596705552419 ? -1.1795880148   ? -0.500225317735 ? 0.0442297629137 ? -0.666735689557 ? 
0.127533109572  ? -0.809599893128 ? 1.24181395679   ? -2.04267804686e-05 ? 
4 'X-RAY DIFFRACTION' ? refined 21.5858034966 -37.0829808093 9.19153063716  1.45706724372 ? -0.505192079297  ? 0.161927047963   ? 
1.21771951446 ? -0.250728928264  ? 1.15262779682 ? 3.1937781687   ? 0.0925387601305 ? -1.29962000588  ? -0.00807566530354 ? 
0.137239460371 ? 1.60295720411 ? 0.643638956547 ? -0.476107632281 ? 0.695580066729  ? 0.303679164294  ? -0.137509745764 ? 
-0.267858229302 ? -0.933684191644 ? 0.805607926599  ? 0.00151413232874   ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 A 1   A 23  ? A 44  A 66  ? ? 
;chain 'A' and (resid   23  through   66 )
;
2 'X-RAY DIFFRACTION' 2 A 45  A 67  ? A 198 A 220 ? ? 
;chain 'A' and (resid   67  through  220 )
;
3 'X-RAY DIFFRACTION' 3 A 199 A 221 ? A 238 A 266 ? ? 
;chain 'A' and (resid  221  through  266 )
;
4 'X-RAY DIFFRACTION' 4 A 239 A 267 ? A 365 A 393 ? ? 
;chain 'A' and (resid  267  through  393 )
;
# 
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 MET 2   ? A MET 1   
2  1 Y 1 A GLY 3   ? A GLY 2   
3  1 Y 1 A SER 4   ? A SER 3   
4  1 Y 1 A SER 5   ? A SER 4   
5  1 Y 1 A HIS 6   ? A HIS 5   
6  1 Y 1 A HIS 7   ? A HIS 6   
7  1 Y 1 A HIS 8   ? A HIS 7   
8  1 Y 1 A HIS 9   ? A HIS 8   
9  1 Y 1 A HIS 10  ? A HIS 9   
10 1 Y 1 A HIS 11  ? A HIS 10  
11 1 Y 1 A SER 12  ? A SER 11  
12 1 Y 1 A SER 13  ? A SER 12  
13 1 Y 1 A GLY 14  ? A GLY 13  
14 1 Y 1 A LEU 15  ? A LEU 14  
15 1 Y 1 A VAL 16  ? A VAL 15  
16 1 Y 1 A PRO 17  ? A PRO 16  
17 1 Y 1 A ARG 18  ? A ARG 17  
18 1 Y 1 A GLY 19  ? A GLY 18  
19 1 Y 1 A SER 20  ? A SER 19  
20 1 Y 1 A HIS 21  ? A HIS 20  
21 1 Y 1 A MET 22  ? A MET 21  
22 1 Y 1 A ASP 254 ? A ASP 253 
23 1 Y 1 A GLU 255 ? A GLU 254 
24 1 Y 1 A TRP 256 ? A TRP 255 
25 1 Y 1 A LYS 257 ? A LYS 256 
26 1 Y 1 A SER 258 ? A SER 257 
27 1 Y 1 A LYS 259 ? A LYS 258 
28 1 Y 1 A GLN 394 ? A GLN 393 
29 1 Y 1 A LYS 395 ? A LYS 394 
30 1 Y 1 A LEU 396 ? A LEU 395 
31 1 Y 1 A MET 397 ? A MET 396 
32 1 Y 1 A ASN 398 ? A ASN 397 
33 1 Y 1 A LEU 399 ? A LEU 398 
# 
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 
A1BDP C1     C N N 1   
A1BDP C2     C N N 2   
A1BDP C3     C N N 3   
A1BDP C4     C N S 4   
A1BDP C5     C N N 5   
A1BDP C6     C Y N 6   
A1BDP O1     O N N 7   
A1BDP C10    C Y N 8   
A1BDP C11    C Y N 9   
A1BDP C12    C N N 10  
A1BDP C13    C N N 11  
A1BDP C15    C Y N 12  
A1BDP C17    C Y N 13  
A1BDP C18    C Y N 14  
A1BDP C19    C Y N 15  
A1BDP C1A    C Y N 16  
A1BDP C1B    C Y N 17  
A1BDP C1C    C N S 18  
A1BDP C21    C N N 19  
A1BDP C41    C N S 20  
A1BDP C42    C N N 21  
A1BDP C43    C N N 22  
A1BDP C51    C Y N 23  
A1BDP C61    C Y N 24  
A1BDP C62    C N N 25  
A1BDP C7     C Y N 26  
A1BDP C8     C Y N 27  
A1BDP C9     C Y N 28  
A1BDP N16    N Y N 29  
A1BDP N20    N Y N 30  
A1BDP N21    N N N 31  
A1BDP N4     N N N 32  
A1BDP O10    O N N 33  
A1BDP O11    O N N 34  
A1BDP O12    O N N 35  
A1BDP O14    O N N 36  
A1BDP O1C    O N N 37  
A1BDP O21    O N N 38  
A1BDP O3     O N N 39  
A1BDP H4     H N N 40  
A1BDP H5C1   H N N 41  
A1BDP H5C2   H N N 42  
A1BDP H191   H N N 43  
A1BDP H181   H N N 44  
A1BDP H171   H N N 45  
A1BDP H41    H N N 46  
A1BDP H431   H N N 47  
A1BDP H432   H N N 48  
A1BDP H433   H N N 49  
A1BDP H422   H N N 50  
A1BDP H423   H N N 51  
A1BDP H421   H N N 52  
A1BDP H622   H N N 53  
A1BDP H623   H N N 54  
A1BDP H621   H N N 55  
A1BDP H7     H N N 56  
A1BDP H8     H N N 57  
A1BDP H9     H N N 58  
A1BDP H211   H N N 59  
A1BDP H212   H N N 60  
A1BDP H11    H N N 61  
A1BDP H1C    H N N 62  
A1BDP H3     H N N 63  
ALA   N      N N N 64  
ALA   CA     C N S 65  
ALA   C      C N N 66  
ALA   O      O N N 67  
ALA   CB     C N N 68  
ALA   OXT    O N N 69  
ALA   H      H N N 70  
ALA   H2     H N N 71  
ALA   HA     H N N 72  
ALA   HB1    H N N 73  
ALA   HB2    H N N 74  
ALA   HB3    H N N 75  
ALA   HXT    H N N 76  
ARG   N      N N N 77  
ARG   CA     C N S 78  
ARG   C      C N N 79  
ARG   O      O N N 80  
ARG   CB     C N N 81  
ARG   CG     C N N 82  
ARG   CD     C N N 83  
ARG   NE     N N N 84  
ARG   CZ     C N N 85  
ARG   NH1    N N N 86  
ARG   NH2    N N N 87  
ARG   OXT    O N N 88  
ARG   H      H N N 89  
ARG   H2     H N N 90  
ARG   HA     H N N 91  
ARG   HB2    H N N 92  
ARG   HB3    H N N 93  
ARG   HG2    H N N 94  
ARG   HG3    H N N 95  
ARG   HD2    H N N 96  
ARG   HD3    H N N 97  
ARG   HE     H N N 98  
ARG   HH11   H N N 99  
ARG   HH12   H N N 100 
ARG   HH21   H N N 101 
ARG   HH22   H N N 102 
ARG   HXT    H N N 103 
ASN   N      N N N 104 
ASN   CA     C N S 105 
ASN   C      C N N 106 
ASN   O      O N N 107 
ASN   CB     C N N 108 
ASN   CG     C N N 109 
ASN   OD1    O N N 110 
ASN   ND2    N N N 111 
ASN   OXT    O N N 112 
ASN   H      H N N 113 
ASN   H2     H N N 114 
ASN   HA     H N N 115 
ASN   HB2    H N N 116 
ASN   HB3    H N N 117 
ASN   HD21   H N N 118 
ASN   HD22   H N N 119 
ASN   HXT    H N N 120 
ASP   N      N N N 121 
ASP   CA     C N S 122 
ASP   C      C N N 123 
ASP   O      O N N 124 
ASP   CB     C N N 125 
ASP   CG     C N N 126 
ASP   OD1    O N N 127 
ASP   OD2    O N N 128 
ASP   OXT    O N N 129 
ASP   H      H N N 130 
ASP   H2     H N N 131 
ASP   HA     H N N 132 
ASP   HB2    H N N 133 
ASP   HB3    H N N 134 
ASP   HD2    H N N 135 
ASP   HXT    H N N 136 
CYS   N      N N N 137 
CYS   CA     C N R 138 
CYS   C      C N N 139 
CYS   O      O N N 140 
CYS   CB     C N N 141 
CYS   SG     S N N 142 
CYS   OXT    O N N 143 
CYS   H      H N N 144 
CYS   H2     H N N 145 
CYS   HA     H N N 146 
CYS   HB2    H N N 147 
CYS   HB3    H N N 148 
CYS   HG     H N N 149 
CYS   HXT    H N N 150 
FAD   PA     P N R 151 
FAD   O1A    O N N 152 
FAD   O2A    O N N 153 
FAD   O5B    O N N 154 
FAD   C5B    C N N 155 
FAD   C4B    C N R 156 
FAD   O4B    O N N 157 
FAD   C3B    C N S 158 
FAD   O3B    O N N 159 
FAD   C2B    C N R 160 
FAD   O2B    O N N 161 
FAD   C1B    C N R 162 
FAD   N9A    N Y N 163 
FAD   C8A    C Y N 164 
FAD   N7A    N Y N 165 
FAD   C5A    C Y N 166 
FAD   C6A    C Y N 167 
FAD   N6A    N N N 168 
FAD   N1A    N Y N 169 
FAD   C2A    C Y N 170 
FAD   N3A    N Y N 171 
FAD   C4A    C Y N 172 
FAD   N1     N N N 173 
FAD   C2     C N N 174 
FAD   O2     O N N 175 
FAD   N3     N N N 176 
FAD   C4     C N N 177 
FAD   O4     O N N 178 
FAD   C4X    C N N 179 
FAD   N5     N N N 180 
FAD   C5X    C Y N 181 
FAD   C6     C Y N 182 
FAD   C7     C Y N 183 
FAD   C7M    C N N 184 
FAD   C8     C Y N 185 
FAD   C8M    C N N 186 
FAD   C9     C Y N 187 
FAD   C9A    C Y N 188 
FAD   N10    N N N 189 
FAD   C10    C N N 190 
FAD   "C1'"  C N N 191 
FAD   "C2'"  C N S 192 
FAD   "O2'"  O N N 193 
FAD   "C3'"  C N S 194 
FAD   "O3'"  O N N 195 
FAD   "C4'"  C N R 196 
FAD   "O4'"  O N N 197 
FAD   "C5'"  C N N 198 
FAD   "O5'"  O N N 199 
FAD   P      P N R 200 
FAD   O1P    O N N 201 
FAD   O2P    O N N 202 
FAD   O3P    O N N 203 
FAD   HOA2   H N N 204 
FAD   H51A   H N N 205 
FAD   H52A   H N N 206 
FAD   H4B    H N N 207 
FAD   H3B    H N N 208 
FAD   HO3A   H N N 209 
FAD   H2B    H N N 210 
FAD   HO2A   H N N 211 
FAD   H1B    H N N 212 
FAD   H8A    H N N 213 
FAD   H61A   H N N 214 
FAD   H62A   H N N 215 
FAD   H2A    H N N 216 
FAD   HN3    H N N 217 
FAD   H6     H N N 218 
FAD   HM71   H N N 219 
FAD   HM72   H N N 220 
FAD   HM73   H N N 221 
FAD   HM81   H N N 222 
FAD   HM82   H N N 223 
FAD   HM83   H N N 224 
FAD   H9     H N N 225 
FAD   "H1'1" H N N 226 
FAD   "H1'2" H N N 227 
FAD   "H2'"  H N N 228 
FAD   "HO2'" H N N 229 
FAD   "H3'"  H N N 230 
FAD   "HO3'" H N N 231 
FAD   "H4'"  H N N 232 
FAD   "HO4'" H N N 233 
FAD   "H5'1" H N N 234 
FAD   "H5'2" H N N 235 
FAD   HOP2   H N N 236 
GLN   N      N N N 237 
GLN   CA     C N S 238 
GLN   C      C N N 239 
GLN   O      O N N 240 
GLN   CB     C N N 241 
GLN   CG     C N N 242 
GLN   CD     C N N 243 
GLN   OE1    O N N 244 
GLN   NE2    N N N 245 
GLN   OXT    O N N 246 
GLN   H      H N N 247 
GLN   H2     H N N 248 
GLN   HA     H N N 249 
GLN   HB2    H N N 250 
GLN   HB3    H N N 251 
GLN   HG2    H N N 252 
GLN   HG3    H N N 253 
GLN   HE21   H N N 254 
GLN   HE22   H N N 255 
GLN   HXT    H N N 256 
GLU   N      N N N 257 
GLU   CA     C N S 258 
GLU   C      C N N 259 
GLU   O      O N N 260 
GLU   CB     C N N 261 
GLU   CG     C N N 262 
GLU   CD     C N N 263 
GLU   OE1    O N N 264 
GLU   OE2    O N N 265 
GLU   OXT    O N N 266 
GLU   H      H N N 267 
GLU   H2     H N N 268 
GLU   HA     H N N 269 
GLU   HB2    H N N 270 
GLU   HB3    H N N 271 
GLU   HG2    H N N 272 
GLU   HG3    H N N 273 
GLU   HE2    H N N 274 
GLU   HXT    H N N 275 
GLY   N      N N N 276 
GLY   CA     C N N 277 
GLY   C      C N N 278 
GLY   O      O N N 279 
GLY   OXT    O N N 280 
GLY   H      H N N 281 
GLY   H2     H N N 282 
GLY   HA2    H N N 283 
GLY   HA3    H N N 284 
GLY   HXT    H N N 285 
HIS   N      N N N 286 
HIS   CA     C N S 287 
HIS   C      C N N 288 
HIS   O      O N N 289 
HIS   CB     C N N 290 
HIS   CG     C Y N 291 
HIS   ND1    N Y N 292 
HIS   CD2    C Y N 293 
HIS   CE1    C Y N 294 
HIS   NE2    N Y N 295 
HIS   OXT    O N N 296 
HIS   H      H N N 297 
HIS   H2     H N N 298 
HIS   HA     H N N 299 
HIS   HB2    H N N 300 
HIS   HB3    H N N 301 
HIS   HD1    H N N 302 
HIS   HD2    H N N 303 
HIS   HE1    H N N 304 
HIS   HE2    H N N 305 
HIS   HXT    H N N 306 
ILE   N      N N N 307 
ILE   CA     C N S 308 
ILE   C      C N N 309 
ILE   O      O N N 310 
ILE   CB     C N S 311 
ILE   CG1    C N N 312 
ILE   CG2    C N N 313 
ILE   CD1    C N N 314 
ILE   OXT    O N N 315 
ILE   H      H N N 316 
ILE   H2     H N N 317 
ILE   HA     H N N 318 
ILE   HB     H N N 319 
ILE   HG12   H N N 320 
ILE   HG13   H N N 321 
ILE   HG21   H N N 322 
ILE   HG22   H N N 323 
ILE   HG23   H N N 324 
ILE   HD11   H N N 325 
ILE   HD12   H N N 326 
ILE   HD13   H N N 327 
ILE   HXT    H N N 328 
LEU   N      N N N 329 
LEU   CA     C N S 330 
LEU   C      C N N 331 
LEU   O      O N N 332 
LEU   CB     C N N 333 
LEU   CG     C N N 334 
LEU   CD1    C N N 335 
LEU   CD2    C N N 336 
LEU   OXT    O N N 337 
LEU   H      H N N 338 
LEU   H2     H N N 339 
LEU   HA     H N N 340 
LEU   HB2    H N N 341 
LEU   HB3    H N N 342 
LEU   HG     H N N 343 
LEU   HD11   H N N 344 
LEU   HD12   H N N 345 
LEU   HD13   H N N 346 
LEU   HD21   H N N 347 
LEU   HD22   H N N 348 
LEU   HD23   H N N 349 
LEU   HXT    H N N 350 
LYS   N      N N N 351 
LYS   CA     C N S 352 
LYS   C      C N N 353 
LYS   O      O N N 354 
LYS   CB     C N N 355 
LYS   CG     C N N 356 
LYS   CD     C N N 357 
LYS   CE     C N N 358 
LYS   NZ     N N N 359 
LYS   OXT    O N N 360 
LYS   H      H N N 361 
LYS   H2     H N N 362 
LYS   HA     H N N 363 
LYS   HB2    H N N 364 
LYS   HB3    H N N 365 
LYS   HG2    H N N 366 
LYS   HG3    H N N 367 
LYS   HD2    H N N 368 
LYS   HD3    H N N 369 
LYS   HE2    H N N 370 
LYS   HE3    H N N 371 
LYS   HZ1    H N N 372 
LYS   HZ2    H N N 373 
LYS   HZ3    H N N 374 
LYS   HXT    H N N 375 
MET   N      N N N 376 
MET   CA     C N S 377 
MET   C      C N N 378 
MET   O      O N N 379 
MET   CB     C N N 380 
MET   CG     C N N 381 
MET   SD     S N N 382 
MET   CE     C N N 383 
MET   OXT    O N N 384 
MET   H      H N N 385 
MET   H2     H N N 386 
MET   HA     H N N 387 
MET   HB2    H N N 388 
MET   HB3    H N N 389 
MET   HG2    H N N 390 
MET   HG3    H N N 391 
MET   HE1    H N N 392 
MET   HE2    H N N 393 
MET   HE3    H N N 394 
MET   HXT    H N N 395 
PHE   N      N N N 396 
PHE   CA     C N S 397 
PHE   C      C N N 398 
PHE   O      O N N 399 
PHE   CB     C N N 400 
PHE   CG     C Y N 401 
PHE   CD1    C Y N 402 
PHE   CD2    C Y N 403 
PHE   CE1    C Y N 404 
PHE   CE2    C Y N 405 
PHE   CZ     C Y N 406 
PHE   OXT    O N N 407 
PHE   H      H N N 408 
PHE   H2     H N N 409 
PHE   HA     H N N 410 
PHE   HB2    H N N 411 
PHE   HB3    H N N 412 
PHE   HD1    H N N 413 
PHE   HD2    H N N 414 
PHE   HE1    H N N 415 
PHE   HE2    H N N 416 
PHE   HZ     H N N 417 
PHE   HXT    H N N 418 
PRO   N      N N N 419 
PRO   CA     C N S 420 
PRO   C      C N N 421 
PRO   O      O N N 422 
PRO   CB     C N N 423 
PRO   CG     C N N 424 
PRO   CD     C N N 425 
PRO   OXT    O N N 426 
PRO   H      H N N 427 
PRO   HA     H N N 428 
PRO   HB2    H N N 429 
PRO   HB3    H N N 430 
PRO   HG2    H N N 431 
PRO   HG3    H N N 432 
PRO   HD2    H N N 433 
PRO   HD3    H N N 434 
PRO   HXT    H N N 435 
SER   N      N N N 436 
SER   CA     C N S 437 
SER   C      C N N 438 
SER   O      O N N 439 
SER   CB     C N N 440 
SER   OG     O N N 441 
SER   OXT    O N N 442 
SER   H      H N N 443 
SER   H2     H N N 444 
SER   HA     H N N 445 
SER   HB2    H N N 446 
SER   HB3    H N N 447 
SER   HG     H N N 448 
SER   HXT    H N N 449 
THR   N      N N N 450 
THR   CA     C N S 451 
THR   C      C N N 452 
THR   O      O N N 453 
THR   CB     C N R 454 
THR   OG1    O N N 455 
THR   CG2    C N N 456 
THR   OXT    O N N 457 
THR   H      H N N 458 
THR   H2     H N N 459 
THR   HA     H N N 460 
THR   HB     H N N 461 
THR   HG1    H N N 462 
THR   HG21   H N N 463 
THR   HG22   H N N 464 
THR   HG23   H N N 465 
THR   HXT    H N N 466 
TRP   N      N N N 467 
TRP   CA     C N S 468 
TRP   C      C N N 469 
TRP   O      O N N 470 
TRP   CB     C N N 471 
TRP   CG     C Y N 472 
TRP   CD1    C Y N 473 
TRP   CD2    C Y N 474 
TRP   NE1    N Y N 475 
TRP   CE2    C Y N 476 
TRP   CE3    C Y N 477 
TRP   CZ2    C Y N 478 
TRP   CZ3    C Y N 479 
TRP   CH2    C Y N 480 
TRP   OXT    O N N 481 
TRP   H      H N N 482 
TRP   H2     H N N 483 
TRP   HA     H N N 484 
TRP   HB2    H N N 485 
TRP   HB3    H N N 486 
TRP   HD1    H N N 487 
TRP   HE1    H N N 488 
TRP   HE3    H N N 489 
TRP   HZ2    H N N 490 
TRP   HZ3    H N N 491 
TRP   HH2    H N N 492 
TRP   HXT    H N N 493 
TYR   N      N N N 494 
TYR   CA     C N S 495 
TYR   C      C N N 496 
TYR   O      O N N 497 
TYR   CB     C N N 498 
TYR   CG     C Y N 499 
TYR   CD1    C Y N 500 
TYR   CD2    C Y N 501 
TYR   CE1    C Y N 502 
TYR   CE2    C Y N 503 
TYR   CZ     C Y N 504 
TYR   OH     O N N 505 
TYR   OXT    O N N 506 
TYR   H      H N N 507 
TYR   H2     H N N 508 
TYR   HA     H N N 509 
TYR   HB2    H N N 510 
TYR   HB3    H N N 511 
TYR   HD1    H N N 512 
TYR   HD2    H N N 513 
TYR   HE1    H N N 514 
TYR   HE2    H N N 515 
TYR   HH     H N N 516 
TYR   HXT    H N N 517 
VAL   N      N N N 518 
VAL   CA     C N S 519 
VAL   C      C N N 520 
VAL   O      O N N 521 
VAL   CB     C N N 522 
VAL   CG1    C N N 523 
VAL   CG2    C N N 524 
VAL   OXT    O N N 525 
VAL   H      H N N 526 
VAL   H2     H N N 527 
VAL   HA     H N N 528 
VAL   HB     H N N 529 
VAL   HG11   H N N 530 
VAL   HG12   H N N 531 
VAL   HG13   H N N 532 
VAL   HG21   H N N 533 
VAL   HG22   H N N 534 
VAL   HG23   H N N 535 
VAL   HXT    H N N 536 
# 
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 
A1BDP C62   C6     sing N N 1   
A1BDP C6    C61    doub Y N 2   
A1BDP C61   C7     sing Y N 3   
A1BDP C7    C8     doub Y N 4   
A1BDP C8    C9     sing Y N 5   
A1BDP C9    C10    doub Y N 6   
A1BDP C10   C1A    sing Y N 7   
A1BDP C61   C1A    sing Y N 8   
A1BDP C1A   C11    doub Y N 9   
A1BDP C11   C1B    sing Y N 10  
A1BDP C1B   C51    doub Y N 11  
A1BDP C6    C51    sing Y N 12  
A1BDP C51   C5     sing N N 13  
A1BDP C5    C41    sing N N 14  
A1BDP C41   C4     sing N N 15  
A1BDP C4    C3     sing N N 16  
A1BDP C3    C2     doub N N 17  
A1BDP C2    C1     sing N N 18  
A1BDP C1    O1     doub N N 19  
A1BDP C1    C1C    sing N N 20  
A1BDP C41   C1C    sing N N 21  
A1BDP C1C   C12    sing N N 22  
A1BDP C1B   C12    sing N N 23  
A1BDP C12   O12    doub N N 24  
A1BDP C1C   O1C    sing N N 25  
A1BDP C2    C21    sing N N 26  
A1BDP C21   O21    doub N N 27  
A1BDP C21   N21    sing N N 28  
A1BDP C3    O3     sing N N 29  
A1BDP C4    N4     sing N N 30  
A1BDP N4    C43    sing N N 31  
A1BDP N4    C42    sing N N 32  
A1BDP C11   O11    sing N N 33  
A1BDP C10   O10    sing N N 34  
A1BDP O10   C13    sing N N 35  
A1BDP C17   C18    doub Y N 36  
A1BDP C18   C19    sing Y N 37  
A1BDP C13   C15    sing N N 38  
A1BDP C15   N20    sing Y N 39  
A1BDP C19   N20    doub Y N 40  
A1BDP C15   N16    doub Y N 41  
A1BDP C17   N16    sing Y N 42  
A1BDP C13   O14    doub N N 43  
A1BDP C4    H4     sing N N 44  
A1BDP C5    H5C1   sing N N 45  
A1BDP C5    H5C2   sing N N 46  
A1BDP C17   H191   sing N N 47  
A1BDP C18   H181   sing N N 48  
A1BDP C19   H171   sing N N 49  
A1BDP C41   H41    sing N N 50  
A1BDP C42   H431   sing N N 51  
A1BDP C42   H432   sing N N 52  
A1BDP C42   H433   sing N N 53  
A1BDP C43   H422   sing N N 54  
A1BDP C43   H423   sing N N 55  
A1BDP C43   H421   sing N N 56  
A1BDP C62   H622   sing N N 57  
A1BDP C62   H623   sing N N 58  
A1BDP C62   H621   sing N N 59  
A1BDP C7    H7     sing N N 60  
A1BDP C8    H8     sing N N 61  
A1BDP C9    H9     sing N N 62  
A1BDP N21   H211   sing N N 63  
A1BDP N21   H212   sing N N 64  
A1BDP O11   H11    sing N N 65  
A1BDP O1C   H1C    sing N N 66  
A1BDP O3    H3     sing N N 67  
ALA   N     CA     sing N N 68  
ALA   N     H      sing N N 69  
ALA   N     H2     sing N N 70  
ALA   CA    C      sing N N 71  
ALA   CA    CB     sing N N 72  
ALA   CA    HA     sing N N 73  
ALA   C     O      doub N N 74  
ALA   C     OXT    sing N N 75  
ALA   CB    HB1    sing N N 76  
ALA   CB    HB2    sing N N 77  
ALA   CB    HB3    sing N N 78  
ALA   OXT   HXT    sing N N 79  
ARG   N     CA     sing N N 80  
ARG   N     H      sing N N 81  
ARG   N     H2     sing N N 82  
ARG   CA    C      sing N N 83  
ARG   CA    CB     sing N N 84  
ARG   CA    HA     sing N N 85  
ARG   C     O      doub N N 86  
ARG   C     OXT    sing N N 87  
ARG   CB    CG     sing N N 88  
ARG   CB    HB2    sing N N 89  
ARG   CB    HB3    sing N N 90  
ARG   CG    CD     sing N N 91  
ARG   CG    HG2    sing N N 92  
ARG   CG    HG3    sing N N 93  
ARG   CD    NE     sing N N 94  
ARG   CD    HD2    sing N N 95  
ARG   CD    HD3    sing N N 96  
ARG   NE    CZ     sing N N 97  
ARG   NE    HE     sing N N 98  
ARG   CZ    NH1    sing N N 99  
ARG   CZ    NH2    doub N N 100 
ARG   NH1   HH11   sing N N 101 
ARG   NH1   HH12   sing N N 102 
ARG   NH2   HH21   sing N N 103 
ARG   NH2   HH22   sing N N 104 
ARG   OXT   HXT    sing N N 105 
ASN   N     CA     sing N N 106 
ASN   N     H      sing N N 107 
ASN   N     H2     sing N N 108 
ASN   CA    C      sing N N 109 
ASN   CA    CB     sing N N 110 
ASN   CA    HA     sing N N 111 
ASN   C     O      doub N N 112 
ASN   C     OXT    sing N N 113 
ASN   CB    CG     sing N N 114 
ASN   CB    HB2    sing N N 115 
ASN   CB    HB3    sing N N 116 
ASN   CG    OD1    doub N N 117 
ASN   CG    ND2    sing N N 118 
ASN   ND2   HD21   sing N N 119 
ASN   ND2   HD22   sing N N 120 
ASN   OXT   HXT    sing N N 121 
ASP   N     CA     sing N N 122 
ASP   N     H      sing N N 123 
ASP   N     H2     sing N N 124 
ASP   CA    C      sing N N 125 
ASP   CA    CB     sing N N 126 
ASP   CA    HA     sing N N 127 
ASP   C     O      doub N N 128 
ASP   C     OXT    sing N N 129 
ASP   CB    CG     sing N N 130 
ASP   CB    HB2    sing N N 131 
ASP   CB    HB3    sing N N 132 
ASP   CG    OD1    doub N N 133 
ASP   CG    OD2    sing N N 134 
ASP   OD2   HD2    sing N N 135 
ASP   OXT   HXT    sing N N 136 
CYS   N     CA     sing N N 137 
CYS   N     H      sing N N 138 
CYS   N     H2     sing N N 139 
CYS   CA    C      sing N N 140 
CYS   CA    CB     sing N N 141 
CYS   CA    HA     sing N N 142 
CYS   C     O      doub N N 143 
CYS   C     OXT    sing N N 144 
CYS   CB    SG     sing N N 145 
CYS   CB    HB2    sing N N 146 
CYS   CB    HB3    sing N N 147 
CYS   SG    HG     sing N N 148 
CYS   OXT   HXT    sing N N 149 
FAD   PA    O1A    doub N N 150 
FAD   PA    O2A    sing N N 151 
FAD   PA    O5B    sing N N 152 
FAD   PA    O3P    sing N N 153 
FAD   O2A   HOA2   sing N N 154 
FAD   O5B   C5B    sing N N 155 
FAD   C5B   C4B    sing N N 156 
FAD   C5B   H51A   sing N N 157 
FAD   C5B   H52A   sing N N 158 
FAD   C4B   O4B    sing N N 159 
FAD   C4B   C3B    sing N N 160 
FAD   C4B   H4B    sing N N 161 
FAD   O4B   C1B    sing N N 162 
FAD   C3B   O3B    sing N N 163 
FAD   C3B   C2B    sing N N 164 
FAD   C3B   H3B    sing N N 165 
FAD   O3B   HO3A   sing N N 166 
FAD   C2B   O2B    sing N N 167 
FAD   C2B   C1B    sing N N 168 
FAD   C2B   H2B    sing N N 169 
FAD   O2B   HO2A   sing N N 170 
FAD   C1B   N9A    sing N N 171 
FAD   C1B   H1B    sing N N 172 
FAD   N9A   C8A    sing Y N 173 
FAD   N9A   C4A    sing Y N 174 
FAD   C8A   N7A    doub Y N 175 
FAD   C8A   H8A    sing N N 176 
FAD   N7A   C5A    sing Y N 177 
FAD   C5A   C6A    sing Y N 178 
FAD   C5A   C4A    doub Y N 179 
FAD   C6A   N6A    sing N N 180 
FAD   C6A   N1A    doub Y N 181 
FAD   N6A   H61A   sing N N 182 
FAD   N6A   H62A   sing N N 183 
FAD   N1A   C2A    sing Y N 184 
FAD   C2A   N3A    doub Y N 185 
FAD   C2A   H2A    sing N N 186 
FAD   N3A   C4A    sing Y N 187 
FAD   N1    C2     sing N N 188 
FAD   N1    C10    doub N N 189 
FAD   C2    O2     doub N N 190 
FAD   C2    N3     sing N N 191 
FAD   N3    C4     sing N N 192 
FAD   N3    HN3    sing N N 193 
FAD   C4    O4     doub N N 194 
FAD   C4    C4X    sing N N 195 
FAD   C4X   N5     doub N N 196 
FAD   C4X   C10    sing N N 197 
FAD   N5    C5X    sing N N 198 
FAD   C5X   C6     doub Y N 199 
FAD   C5X   C9A    sing Y N 200 
FAD   C6    C7     sing Y N 201 
FAD   C6    H6     sing N N 202 
FAD   C7    C7M    sing N N 203 
FAD   C7    C8     doub Y N 204 
FAD   C7M   HM71   sing N N 205 
FAD   C7M   HM72   sing N N 206 
FAD   C7M   HM73   sing N N 207 
FAD   C8    C8M    sing N N 208 
FAD   C8    C9     sing Y N 209 
FAD   C8M   HM81   sing N N 210 
FAD   C8M   HM82   sing N N 211 
FAD   C8M   HM83   sing N N 212 
FAD   C9    C9A    doub Y N 213 
FAD   C9    H9     sing N N 214 
FAD   C9A   N10    sing N N 215 
FAD   N10   C10    sing N N 216 
FAD   N10   "C1'"  sing N N 217 
FAD   "C1'" "C2'"  sing N N 218 
FAD   "C1'" "H1'1" sing N N 219 
FAD   "C1'" "H1'2" sing N N 220 
FAD   "C2'" "O2'"  sing N N 221 
FAD   "C2'" "C3'"  sing N N 222 
FAD   "C2'" "H2'"  sing N N 223 
FAD   "O2'" "HO2'" sing N N 224 
FAD   "C3'" "O3'"  sing N N 225 
FAD   "C3'" "C4'"  sing N N 226 
FAD   "C3'" "H3'"  sing N N 227 
FAD   "O3'" "HO3'" sing N N 228 
FAD   "C4'" "O4'"  sing N N 229 
FAD   "C4'" "C5'"  sing N N 230 
FAD   "C4'" "H4'"  sing N N 231 
FAD   "O4'" "HO4'" sing N N 232 
FAD   "C5'" "O5'"  sing N N 233 
FAD   "C5'" "H5'1" sing N N 234 
FAD   "C5'" "H5'2" sing N N 235 
FAD   "O5'" P      sing N N 236 
FAD   P     O1P    doub N N 237 
FAD   P     O2P    sing N N 238 
FAD   P     O3P    sing N N 239 
FAD   O2P   HOP2   sing N N 240 
GLN   N     CA     sing N N 241 
GLN   N     H      sing N N 242 
GLN   N     H2     sing N N 243 
GLN   CA    C      sing N N 244 
GLN   CA    CB     sing N N 245 
GLN   CA    HA     sing N N 246 
GLN   C     O      doub N N 247 
GLN   C     OXT    sing N N 248 
GLN   CB    CG     sing N N 249 
GLN   CB    HB2    sing N N 250 
GLN   CB    HB3    sing N N 251 
GLN   CG    CD     sing N N 252 
GLN   CG    HG2    sing N N 253 
GLN   CG    HG3    sing N N 254 
GLN   CD    OE1    doub N N 255 
GLN   CD    NE2    sing N N 256 
GLN   NE2   HE21   sing N N 257 
GLN   NE2   HE22   sing N N 258 
GLN   OXT   HXT    sing N N 259 
GLU   N     CA     sing N N 260 
GLU   N     H      sing N N 261 
GLU   N     H2     sing N N 262 
GLU   CA    C      sing N N 263 
GLU   CA    CB     sing N N 264 
GLU   CA    HA     sing N N 265 
GLU   C     O      doub N N 266 
GLU   C     OXT    sing N N 267 
GLU   CB    CG     sing N N 268 
GLU   CB    HB2    sing N N 269 
GLU   CB    HB3    sing N N 270 
GLU   CG    CD     sing N N 271 
GLU   CG    HG2    sing N N 272 
GLU   CG    HG3    sing N N 273 
GLU   CD    OE1    doub N N 274 
GLU   CD    OE2    sing N N 275 
GLU   OE2   HE2    sing N N 276 
GLU   OXT   HXT    sing N N 277 
GLY   N     CA     sing N N 278 
GLY   N     H      sing N N 279 
GLY   N     H2     sing N N 280 
GLY   CA    C      sing N N 281 
GLY   CA    HA2    sing N N 282 
GLY   CA    HA3    sing N N 283 
GLY   C     O      doub N N 284 
GLY   C     OXT    sing N N 285 
GLY   OXT   HXT    sing N N 286 
HIS   N     CA     sing N N 287 
HIS   N     H      sing N N 288 
HIS   N     H2     sing N N 289 
HIS   CA    C      sing N N 290 
HIS   CA    CB     sing N N 291 
HIS   CA    HA     sing N N 292 
HIS   C     O      doub N N 293 
HIS   C     OXT    sing N N 294 
HIS   CB    CG     sing N N 295 
HIS   CB    HB2    sing N N 296 
HIS   CB    HB3    sing N N 297 
HIS   CG    ND1    sing Y N 298 
HIS   CG    CD2    doub Y N 299 
HIS   ND1   CE1    doub Y N 300 
HIS   ND1   HD1    sing N N 301 
HIS   CD2   NE2    sing Y N 302 
HIS   CD2   HD2    sing N N 303 
HIS   CE1   NE2    sing Y N 304 
HIS   CE1   HE1    sing N N 305 
HIS   NE2   HE2    sing N N 306 
HIS   OXT   HXT    sing N N 307 
ILE   N     CA     sing N N 308 
ILE   N     H      sing N N 309 
ILE   N     H2     sing N N 310 
ILE   CA    C      sing N N 311 
ILE   CA    CB     sing N N 312 
ILE   CA    HA     sing N N 313 
ILE   C     O      doub N N 314 
ILE   C     OXT    sing N N 315 
ILE   CB    CG1    sing N N 316 
ILE   CB    CG2    sing N N 317 
ILE   CB    HB     sing N N 318 
ILE   CG1   CD1    sing N N 319 
ILE   CG1   HG12   sing N N 320 
ILE   CG1   HG13   sing N N 321 
ILE   CG2   HG21   sing N N 322 
ILE   CG2   HG22   sing N N 323 
ILE   CG2   HG23   sing N N 324 
ILE   CD1   HD11   sing N N 325 
ILE   CD1   HD12   sing N N 326 
ILE   CD1   HD13   sing N N 327 
ILE   OXT   HXT    sing N N 328 
LEU   N     CA     sing N N 329 
LEU   N     H      sing N N 330 
LEU   N     H2     sing N N 331 
LEU   CA    C      sing N N 332 
LEU   CA    CB     sing N N 333 
LEU   CA    HA     sing N N 334 
LEU   C     O      doub N N 335 
LEU   C     OXT    sing N N 336 
LEU   CB    CG     sing N N 337 
LEU   CB    HB2    sing N N 338 
LEU   CB    HB3    sing N N 339 
LEU   CG    CD1    sing N N 340 
LEU   CG    CD2    sing N N 341 
LEU   CG    HG     sing N N 342 
LEU   CD1   HD11   sing N N 343 
LEU   CD1   HD12   sing N N 344 
LEU   CD1   HD13   sing N N 345 
LEU   CD2   HD21   sing N N 346 
LEU   CD2   HD22   sing N N 347 
LEU   CD2   HD23   sing N N 348 
LEU   OXT   HXT    sing N N 349 
LYS   N     CA     sing N N 350 
LYS   N     H      sing N N 351 
LYS   N     H2     sing N N 352 
LYS   CA    C      sing N N 353 
LYS   CA    CB     sing N N 354 
LYS   CA    HA     sing N N 355 
LYS   C     O      doub N N 356 
LYS   C     OXT    sing N N 357 
LYS   CB    CG     sing N N 358 
LYS   CB    HB2    sing N N 359 
LYS   CB    HB3    sing N N 360 
LYS   CG    CD     sing N N 361 
LYS   CG    HG2    sing N N 362 
LYS   CG    HG3    sing N N 363 
LYS   CD    CE     sing N N 364 
LYS   CD    HD2    sing N N 365 
LYS   CD    HD3    sing N N 366 
LYS   CE    NZ     sing N N 367 
LYS   CE    HE2    sing N N 368 
LYS   CE    HE3    sing N N 369 
LYS   NZ    HZ1    sing N N 370 
LYS   NZ    HZ2    sing N N 371 
LYS   NZ    HZ3    sing N N 372 
LYS   OXT   HXT    sing N N 373 
MET   N     CA     sing N N 374 
MET   N     H      sing N N 375 
MET   N     H2     sing N N 376 
MET   CA    C      sing N N 377 
MET   CA    CB     sing N N 378 
MET   CA    HA     sing N N 379 
MET   C     O      doub N N 380 
MET   C     OXT    sing N N 381 
MET   CB    CG     sing N N 382 
MET   CB    HB2    sing N N 383 
MET   CB    HB3    sing N N 384 
MET   CG    SD     sing N N 385 
MET   CG    HG2    sing N N 386 
MET   CG    HG3    sing N N 387 
MET   SD    CE     sing N N 388 
MET   CE    HE1    sing N N 389 
MET   CE    HE2    sing N N 390 
MET   CE    HE3    sing N N 391 
MET   OXT   HXT    sing N N 392 
PHE   N     CA     sing N N 393 
PHE   N     H      sing N N 394 
PHE   N     H2     sing N N 395 
PHE   CA    C      sing N N 396 
PHE   CA    CB     sing N N 397 
PHE   CA    HA     sing N N 398 
PHE   C     O      doub N N 399 
PHE   C     OXT    sing N N 400 
PHE   CB    CG     sing N N 401 
PHE   CB    HB2    sing N N 402 
PHE   CB    HB3    sing N N 403 
PHE   CG    CD1    doub Y N 404 
PHE   CG    CD2    sing Y N 405 
PHE   CD1   CE1    sing Y N 406 
PHE   CD1   HD1    sing N N 407 
PHE   CD2   CE2    doub Y N 408 
PHE   CD2   HD2    sing N N 409 
PHE   CE1   CZ     doub Y N 410 
PHE   CE1   HE1    sing N N 411 
PHE   CE2   CZ     sing Y N 412 
PHE   CE2   HE2    sing N N 413 
PHE   CZ    HZ     sing N N 414 
PHE   OXT   HXT    sing N N 415 
PRO   N     CA     sing N N 416 
PRO   N     CD     sing N N 417 
PRO   N     H      sing N N 418 
PRO   CA    C      sing N N 419 
PRO   CA    CB     sing N N 420 
PRO   CA    HA     sing N N 421 
PRO   C     O      doub N N 422 
PRO   C     OXT    sing N N 423 
PRO   CB    CG     sing N N 424 
PRO   CB    HB2    sing N N 425 
PRO   CB    HB3    sing N N 426 
PRO   CG    CD     sing N N 427 
PRO   CG    HG2    sing N N 428 
PRO   CG    HG3    sing N N 429 
PRO   CD    HD2    sing N N 430 
PRO   CD    HD3    sing N N 431 
PRO   OXT   HXT    sing N N 432 
SER   N     CA     sing N N 433 
SER   N     H      sing N N 434 
SER   N     H2     sing N N 435 
SER   CA    C      sing N N 436 
SER   CA    CB     sing N N 437 
SER   CA    HA     sing N N 438 
SER   C     O      doub N N 439 
SER   C     OXT    sing N N 440 
SER   CB    OG     sing N N 441 
SER   CB    HB2    sing N N 442 
SER   CB    HB3    sing N N 443 
SER   OG    HG     sing N N 444 
SER   OXT   HXT    sing N N 445 
THR   N     CA     sing N N 446 
THR   N     H      sing N N 447 
THR   N     H2     sing N N 448 
THR   CA    C      sing N N 449 
THR   CA    CB     sing N N 450 
THR   CA    HA     sing N N 451 
THR   C     O      doub N N 452 
THR   C     OXT    sing N N 453 
THR   CB    OG1    sing N N 454 
THR   CB    CG2    sing N N 455 
THR   CB    HB     sing N N 456 
THR   OG1   HG1    sing N N 457 
THR   CG2   HG21   sing N N 458 
THR   CG2   HG22   sing N N 459 
THR   CG2   HG23   sing N N 460 
THR   OXT   HXT    sing N N 461 
TRP   N     CA     sing N N 462 
TRP   N     H      sing N N 463 
TRP   N     H2     sing N N 464 
TRP   CA    C      sing N N 465 
TRP   CA    CB     sing N N 466 
TRP   CA    HA     sing N N 467 
TRP   C     O      doub N N 468 
TRP   C     OXT    sing N N 469 
TRP   CB    CG     sing N N 470 
TRP   CB    HB2    sing N N 471 
TRP   CB    HB3    sing N N 472 
TRP   CG    CD1    doub Y N 473 
TRP   CG    CD2    sing Y N 474 
TRP   CD1   NE1    sing Y N 475 
TRP   CD1   HD1    sing N N 476 
TRP   CD2   CE2    doub Y N 477 
TRP   CD2   CE3    sing Y N 478 
TRP   NE1   CE2    sing Y N 479 
TRP   NE1   HE1    sing N N 480 
TRP   CE2   CZ2    sing Y N 481 
TRP   CE3   CZ3    doub Y N 482 
TRP   CE3   HE3    sing N N 483 
TRP   CZ2   CH2    doub Y N 484 
TRP   CZ2   HZ2    sing N N 485 
TRP   CZ3   CH2    sing Y N 486 
TRP   CZ3   HZ3    sing N N 487 
TRP   CH2   HH2    sing N N 488 
TRP   OXT   HXT    sing N N 489 
TYR   N     CA     sing N N 490 
TYR   N     H      sing N N 491 
TYR   N     H2     sing N N 492 
TYR   CA    C      sing N N 493 
TYR   CA    CB     sing N N 494 
TYR   CA    HA     sing N N 495 
TYR   C     O      doub N N 496 
TYR   C     OXT    sing N N 497 
TYR   CB    CG     sing N N 498 
TYR   CB    HB2    sing N N 499 
TYR   CB    HB3    sing N N 500 
TYR   CG    CD1    doub Y N 501 
TYR   CG    CD2    sing Y N 502 
TYR   CD1   CE1    sing Y N 503 
TYR   CD1   HD1    sing N N 504 
TYR   CD2   CE2    doub Y N 505 
TYR   CD2   HD2    sing N N 506 
TYR   CE1   CZ     doub Y N 507 
TYR   CE1   HE1    sing N N 508 
TYR   CE2   CZ     sing Y N 509 
TYR   CE2   HE2    sing N N 510 
TYR   CZ    OH     sing N N 511 
TYR   OH    HH     sing N N 512 
TYR   OXT   HXT    sing N N 513 
VAL   N     CA     sing N N 514 
VAL   N     H      sing N N 515 
VAL   N     H2     sing N N 516 
VAL   CA    C      sing N N 517 
VAL   CA    CB     sing N N 518 
VAL   CA    HA     sing N N 519 
VAL   C     O      doub N N 520 
VAL   C     OXT    sing N N 521 
VAL   CB    CG1    sing N N 522 
VAL   CB    CG2    sing N N 523 
VAL   CB    HB     sing N N 524 
VAL   CG1   HG11   sing N N 525 
VAL   CG1   HG12   sing N N 526 
VAL   CG1   HG13   sing N N 527 
VAL   CG2   HG21   sing N N 528 
VAL   CG2   HG22   sing N N 529 
VAL   CG2   HG23   sing N N 530 
VAL   OXT   HXT    sing N N 531 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_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   6wg9 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 41 21 2' 
_space_group.name_Hall        'P 4abw 2nw' 
_space_group.IT_number        92 
_space_group.crystal_system   tetragonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9DRH 
_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]   0.007534 
_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]   0.007534 
_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]   0.017307 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
H ? ? 0.99627 ?       ? ? 14.84254 ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 6.96715 ?       ? ? 11.43723 ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 7.96527 ?       ? ? 9.05267  ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P ? ? 9.51135 5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N      . THR   A 1 22  ? -3.91514  -22.07787 -5.72538  1.000 173.60267 ? 23  THR   A N      1 
ATOM   2    C CA     . THR   A 1 22  ? -3.81498  -21.08785 -6.79091  1.000 178.95609 ? 23  THR   A CA     1 
ATOM   3    C C      . THR   A 1 22  ? -2.39291  -21.02062 -7.33498  1.000 183.58071 ? 23  THR   A C      1 
ATOM   4    O O      . THR   A 1 22  ? -2.17311  -21.13215 -8.54065  1.000 208.64446 ? 23  THR   A O      1 
ATOM   5    C CB     . THR   A 1 22  ? -4.23085  -19.68648 -6.30282  1.000 186.32421 ? 23  THR   A CB     1 
ATOM   6    O OG1    . THR   A 1 22  ? -5.56905  -19.73060 -5.79195  1.000 187.37284 ? 23  THR   A OG1    1 
ATOM   7    C CG2    . THR   A 1 22  ? -4.15311  -18.67488 -7.44202  1.000 174.49087 ? 23  THR   A CG2    1 
ATOM   8    H HA     . THR   A 1 22  ? -4.40740  -21.34176 -7.51581  1.000 215.13778 ? 23  THR   A HA     1 
ATOM   9    H HB     . THR   A 1 22  ? -3.62813  -19.39826 -5.59957  1.000 223.97953 ? 23  THR   A HB     1 
ATOM   10   H HG1    . THR   A 1 22  ? -5.61330  -20.26864 -5.14841  1.000 225.23788 ? 23  THR   A HG1    1 
ATOM   11   H HG21   . THR   A 1 22  ? -4.57752  -17.84381 -7.17726  1.000 209.77952 ? 23  THR   A HG21   1 
ATOM   12   H HG22   . THR   A 1 22  ? -3.22602  -18.49762 -7.66561  1.000 209.77952 ? 23  THR   A HG22   1 
ATOM   13   H HG23   . THR   A 1 22  ? -4.60506  -19.02321 -8.22644  1.000 209.77952 ? 23  THR   A HG23   1 
ATOM   14   N N      . LEU   A 1 23  ? -1.42935  -20.83639 -6.42954  1.000 178.88459 ? 24  LEU   A N      1 
ATOM   15   C CA     . LEU   A 1 23  ? -0.03381  -20.71350 -6.83898  1.000 185.68481 ? 24  LEU   A CA     1 
ATOM   16   C C      . LEU   A 1 23  ? 0.40439   -21.89758 -7.69248  1.000 189.42176 ? 24  LEU   A C      1 
ATOM   17   O O      . LEU   A 1 23  ? 1.19132   -21.73767 -8.63302  1.000 187.40957 ? 24  LEU   A O      1 
ATOM   18   C CB     . LEU   A 1 23  ? 0.85561   -20.58596 -5.60077  1.000 204.45992 ? 24  LEU   A CB     1 
ATOM   19   C CG     . LEU   A 1 23  ? 2.34289   -20.30734 -5.82660  1.000 204.03364 ? 24  LEU   A CG     1 
ATOM   20   C CD1    . LEU   A 1 23  ? 2.54733   -19.03068 -6.62752  1.000 197.88349 ? 24  LEU   A CD1    1 
ATOM   21   C CD2    . LEU   A 1 23  ? 3.06944   -20.22490 -4.48753  1.000 215.46039 ? 24  LEU   A CD2    1 
ATOM   22   H H      . LEU   A 1 23  ? -1.55735  -20.77983 -5.58101  1.000 215.05197 ? 24  LEU   A H      1 
ATOM   23   H HA     . LEU   A 1 23  ? 0.06858   -19.91033 -7.37314  1.000 223.21225 ? 24  LEU   A HA     1 
ATOM   24   H HB2    . LEU   A 1 23  ? 0.51165   -19.85614 -5.06229  1.000 245.74238 ? 24  LEU   A HB2    1 
ATOM   25   H HB3    . LEU   A 1 23  ? 0.79763   -21.41872 -5.10676  1.000 245.74238 ? 24  LEU   A HB3    1 
ATOM   26   H HG     . LEU   A 1 23  ? 2.72445   -21.03622 -6.34046  1.000 245.23084 ? 24  LEU   A HG     1 
ATOM   27   H HD11   . LEU   A 1 23  ? 3.49178   -18.80960 -6.63372  1.000 237.85066 ? 24  LEU   A HD11   1 
ATOM   28   H HD12   . LEU   A 1 23  ? 2.23511   -19.17359 -7.53471  1.000 237.85066 ? 24  LEU   A HD12   1 
ATOM   29   H HD13   . LEU   A 1 23  ? 2.04247   -18.31359 -6.21305  1.000 237.85066 ? 24  LEU   A HD13   1 
ATOM   30   H HD21   . LEU   A 1 23  ? 4.01036   -20.05300 -4.64882  1.000 258.94294 ? 24  LEU   A HD21   1 
ATOM   31   H HD22   . LEU   A 1 23  ? 2.68635   -19.50355 -3.96427  1.000 258.94294 ? 24  LEU   A HD22   1 
ATOM   32   H HD23   . LEU   A 1 23  ? 2.96276   -21.06695 -4.01799  1.000 258.94294 ? 24  LEU   A HD23   1 
ATOM   33   N N      . LEU   A 1 24  ? -0.10191  -23.09378 -7.38619  1.000 192.87996 ? 25  LEU   A N      1 
ATOM   34   C CA     . LEU   A 1 24  ? 0.28598   -24.31481 -8.08029  1.000 189.38072 ? 25  LEU   A CA     1 
ATOM   35   C C      . LEU   A 1 24  ? -0.80460  -24.83342 -9.01302  1.000 195.04520 ? 25  LEU   A C      1 
ATOM   36   O O      . LEU   A 1 24  ? -0.82424  -26.02747 -9.32867  1.000 194.60515 ? 25  LEU   A O      1 
ATOM   37   C CB     . LEU   A 1 24  ? 0.65346   -25.40353 -7.06989  1.000 182.28658 ? 25  LEU   A CB     1 
ATOM   38   C CG     . LEU   A 1 24  ? 1.89744   -25.19753 -6.20595  1.000 198.80795 ? 25  LEU   A CG     1 
ATOM   39   C CD1    . LEU   A 1 24  ? 2.07341   -26.37331 -5.25198  1.000 195.28022 ? 25  LEU   A CD1    1 
ATOM   40   C CD2    . LEU   A 1 24  ? 3.13243   -25.02056 -7.06978  1.000 191.31486 ? 25  LEU   A CD2    1 
ATOM   41   H H      . LEU   A 1 24  ? -0.68388  -23.22229 -6.76620  1.000 231.84642 ? 25  LEU   A H      1 
ATOM   42   H HA     . LEU   A 1 24  ? 1.06703   -24.11417 -8.61936  1.000 227.64733 ? 25  LEU   A HA     1 
ATOM   43   H HB2    . LEU   A 1 24  ? -0.09449  -25.50295 -6.46031  1.000 219.13437 ? 25  LEU   A HB2    1 
ATOM   44   H HB3    . LEU   A 1 24  ? 0.79130   -26.22736 -7.56304  1.000 219.13437 ? 25  LEU   A HB3    1 
ATOM   45   H HG     . LEU   A 1 24  ? 1.78799   -24.38959 -5.68046  1.000 238.96001 ? 25  LEU   A HG     1 
ATOM   46   H HD11   . LEU   A 1 24  ? 2.88856   -26.24669 -4.74168  1.000 234.72673 ? 25  LEU   A HD11   1 
ATOM   47   H HD12   . LEU   A 1 24  ? 1.31101   -26.41122 -4.65347  1.000 234.72673 ? 25  LEU   A HD12   1 
ATOM   48   H HD13   . LEU   A 1 24  ? 2.13004   -27.19280 -5.76785  1.000 234.72673 ? 25  LEU   A HD13   1 
ATOM   49   H HD21   . LEU   A 1 24  ? 3.92031   -25.05386 -6.50495  1.000 229.96830 ? 25  LEU   A HD21   1 
ATOM   50   H HD22   . LEU   A 1 24  ? 3.16464   -25.73519 -7.72489  1.000 229.96830 ? 25  LEU   A HD22   1 
ATOM   51   H HD23   . LEU   A 1 24  ? 3.08338   -24.16216 -7.51881  1.000 229.96830 ? 25  LEU   A HD23   1 
ATOM   52   N N      . LYS   A 1 25  ? -1.71107  -23.96909 -9.46397  1.000 203.83914 ? 26  LYS   A N      1 
ATOM   53   C CA     . LYS   A 1 25  ? -2.82875  -24.43892 -10.27192 1.000 203.67385 ? 26  LYS   A CA     1 
ATOM   54   C C      . LYS   A 1 25  ? -2.32910  -25.06125 -11.57007 1.000 200.43039 ? 26  LYS   A C      1 
ATOM   55   O O      . LYS   A 1 25  ? -1.51254  -24.47243 -12.28484 1.000 203.05812 ? 26  LYS   A O      1 
ATOM   56   C CB     . LYS   A 1 25  ? -3.79607  -23.29642 -10.58116 1.000 202.03361 ? 26  LYS   A CB     1 
ATOM   57   C CG     . LYS   A 1 25  ? -5.00971  -23.75626 -11.38289 1.000 203.87994 ? 26  LYS   A CG     1 
ATOM   58   C CD     . LYS   A 1 25  ? -6.02915  -22.65171 -11.60160 1.000 216.86614 ? 26  LYS   A CD     1 
ATOM   59   C CE     . LYS   A 1 25  ? -7.19161  -23.15642 -12.44757 1.000 201.33402 ? 26  LYS   A CE     1 
ATOM   60   N NZ     . LYS   A 1 25  ? -8.21435  -22.10715 -12.70427 1.000 198.16206 ? 26  LYS   A NZ     1 
ATOM   61   H H      . LYS   A 1 25  ? -1.70071  -23.12160 -9.31815  1.000 244.99744 ? 26  LYS   A H      1 
ATOM   62   H HA     . LYS   A 1 25  ? -3.31100  -25.11323 -9.76829  1.000 244.79909 ? 26  LYS   A HA     1 
ATOM   63   H HB2    . LYS   A 1 25  ? -4.11290  -22.91583 -9.74709  1.000 242.83080 ? 26  LYS   A HB2    1 
ATOM   64   H HB3    . LYS   A 1 25  ? -3.33173  -22.62037 -11.09908 1.000 242.83080 ? 26  LYS   A HB3    1 
ATOM   65   H HG2    . LYS   A 1 25  ? -4.71408  -24.06631 -12.25317 1.000 245.04640 ? 26  LYS   A HG2    1 
ATOM   66   H HG3    . LYS   A 1 25  ? -5.44870  -24.47744 -10.90531 1.000 245.04640 ? 26  LYS   A HG3    1 
ATOM   67   H HD2    . LYS   A 1 25  ? -6.37597  -22.35551 -10.74552 1.000 260.62983 ? 26  LYS   A HD2    1 
ATOM   68   H HD3    . LYS   A 1 25  ? -5.60980  -21.90952 -12.06441 1.000 260.62983 ? 26  LYS   A HD3    1 
ATOM   69   H HE2    . LYS   A 1 25  ? -6.85149  -23.45937 -13.30398 1.000 241.99129 ? 26  LYS   A HE2    1 
ATOM   70   H HE3    . LYS   A 1 25  ? -7.62482  -23.89029 -11.98425 1.000 241.99129 ? 26  LYS   A HE3    1 
ATOM   71   H HZ1    . LYS   A 1 25  ? -8.86633  -22.43563 -13.21330 1.000 238.18494 ? 26  LYS   A HZ1    1 
ATOM   72   H HZ2    . LYS   A 1 25  ? -8.56231  -21.82649 -11.93468 1.000 238.18494 ? 26  LYS   A HZ2    1 
ATOM   73   H HZ3    . LYS   A 1 25  ? -7.84224  -21.41519 -13.12240 1.000 238.18494 ? 26  LYS   A HZ3    1 
ATOM   74   N N      . ASN   A 1 26  ? -2.83086  -26.25888 -11.87157 1.000 196.67145 ? 27  ASN   A N      1 
ATOM   75   C CA     . ASN   A 1 26  ? -2.50653  -26.96772 -13.10778 1.000 197.36968 ? 27  ASN   A CA     1 
ATOM   76   C C      . ASN   A 1 26  ? -1.00232  -27.15639 -13.28137 1.000 197.30011 ? 27  ASN   A C      1 
ATOM   77   O O      . ASN   A 1 26  ? -0.50695  -27.26758 -14.40561 1.000 205.99729 ? 27  ASN   A O      1 
ATOM   78   C CB     . ASN   A 1 26  ? -3.09179  -26.24702 -14.32649 1.000 203.33678 ? 27  ASN   A CB     1 
ATOM   79   C CG     . ASN   A 1 26  ? -4.60122  -26.12805 -14.26319 1.000 197.59083 ? 27  ASN   A CG     1 
ATOM   80   O OD1    . ASN   A 1 26  ? -5.25282  -26.78011 -13.44717 1.000 188.68846 ? 27  ASN   A OD1    1 
ATOM   81   N ND2    . ASN   A 1 26  ? -5.16668  -25.29819 -15.13213 1.000 199.59138 ? 27  ASN   A ND2    1 
ATOM   82   H H      . ASN   A 1 26  ? -3.37404  -26.69089 -11.36370 1.000 236.39621 ? 27  ASN   A H      1 
ATOM   83   H HA     . ASN   A 1 26  ? -2.90318  -27.85145 -13.05693 1.000 237.23409 ? 27  ASN   A HA     1 
ATOM   84   H HB2    . ASN   A 1 26  ? -2.72135  -25.35175 -14.37311 1.000 244.39460 ? 27  ASN   A HB2    1 
ATOM   85   H HB3    . ASN   A 1 26  ? -2.86267  -26.74301 -15.12799 1.000 244.39460 ? 27  ASN   A HB3    1 
ATOM   86   H HD21   . ASN   A 1 26  ? -6.02058  -25.19598 -15.13599 1.000 239.90012 ? 27  ASN   A HD21   1 
ATOM   87   H HD22   . ASN   A 1 26  ? -4.67898  -24.86297 -15.69100 1.000 239.90012 ? 27  ASN   A HD22   1 
ATOM   88   N N      . LYS   A 1 27  ? -0.26345  -27.19829 -12.17662 1.000 187.60722 ? 28  LYS   A N      1 
ATOM   89   C CA     . LYS   A 1 27  ? 1.17357   -27.44234 -12.19658 1.000 179.93136 ? 28  LYS   A CA     1 
ATOM   90   C C      . LYS   A 1 27  ? 1.43292   -28.85911 -11.70134 1.000 178.62149 ? 28  LYS   A C      1 
ATOM   91   O O      . LYS   A 1 27  ? 1.08127   -29.19808 -10.56585 1.000 189.36293 ? 28  LYS   A O      1 
ATOM   92   C CB     . LYS   A 1 27  ? 1.91874   -26.42178 -11.33652 1.000 192.36364 ? 28  LYS   A CB     1 
ATOM   93   C CG     . LYS   A 1 27  ? 1.81410   -24.98428 -11.83597 1.000 192.31102 ? 28  LYS   A CG     1 
ATOM   94   C CD     . LYS   A 1 27  ? 2.39819   -24.82113 -13.23272 1.000 168.18468 ? 28  LYS   A CD     1 
ATOM   95   C CE     . LYS   A 1 27  ? 2.17659   -23.41521 -13.76690 1.000 167.50329 ? 28  LYS   A CE     1 
ATOM   96   N NZ     . LYS   A 1 27  ? 2.81885   -22.38067 -12.91129 1.000 172.87641 ? 28  LYS   A NZ     1 
ATOM   97   H H      . LYS   A 1 27  ? -0.58085  -27.08540 -11.38534 1.000 225.51914 ? 28  LYS   A H      1 
ATOM   98   H HA     . LYS   A 1 27  ? 1.50352   -27.36746 -13.10566 1.000 216.30811 ? 28  LYS   A HA     1 
ATOM   99   H HB2    . LYS   A 1 27  ? 1.55339   -26.44810 -10.43834 1.000 231.22684 ? 28  LYS   A HB2    1 
ATOM   100  H HB3    . LYS   A 1 27  ? 2.85910   -26.65912 -11.31925 1.000 231.22684 ? 28  LYS   A HB3    1 
ATOM   101  H HG2    . LYS   A 1 27  ? 0.88018   -24.72393 -11.86617 1.000 231.16370 ? 28  LYS   A HG2    1 
ATOM   102  H HG3    . LYS   A 1 27  ? 2.30187   -24.40076 -11.23390 1.000 231.16370 ? 28  LYS   A HG3    1 
ATOM   103  H HD2    . LYS   A 1 27  ? 3.35303   -24.98951 -13.20364 1.000 202.21209 ? 28  LYS   A HD2    1 
ATOM   104  H HD3    . LYS   A 1 27  ? 1.96902   -25.44790 -13.83594 1.000 202.21209 ? 28  LYS   A HD3    1 
ATOM   105  H HE2    . LYS   A 1 27  ? 2.55632   -23.34927 -14.65705 1.000 201.39442 ? 28  LYS   A HE2    1 
ATOM   106  H HE3    . LYS   A 1 27  ? 1.22440   -23.23282 -13.79806 1.000 201.39442 ? 28  LYS   A HE3    1 
ATOM   107  H HZ1    . LYS   A 1 27  ? 2.72903   -21.57794 -13.28501 1.000 207.84216 ? 28  LYS   A HZ1    1 
ATOM   108  H HZ2    . LYS   A 1 27  ? 2.43615   -22.36967 -12.10785 1.000 207.84216 ? 28  LYS   A HZ2    1 
ATOM   109  H HZ3    . LYS   A 1 27  ? 3.68546   -22.55958 -12.81601 1.000 207.84216 ? 28  LYS   A HZ3    1 
ATOM   110  N N      . LYS   A 1 28  ? 2.04387   -29.67955 -12.55316 1.000 170.79512 ? 29  LYS   A N      1 
ATOM   111  C CA     . LYS   A 1 28  ? 2.32805   -31.07222 -12.22238 1.000 173.32190 ? 29  LYS   A CA     1 
ATOM   112  C C      . LYS   A 1 28  ? 3.62271   -31.13803 -11.42156 1.000 171.49301 ? 29  LYS   A C      1 
ATOM   113  O O      . LYS   A 1 28  ? 4.71103   -30.92428 -11.96579 1.000 165.52177 ? 29  LYS   A O      1 
ATOM   114  C CB     . LYS   A 1 28  ? 2.42391   -31.90897 -13.49450 1.000 170.74664 ? 29  LYS   A CB     1 
ATOM   115  C CG     . LYS   A 1 28  ? 2.71995   -33.37803 -13.24962 1.000 163.15385 ? 29  LYS   A CG     1 
ATOM   116  C CD     . LYS   A 1 28  ? 2.70969   -34.17723 -14.54527 1.000 175.27188 ? 29  LYS   A CD     1 
ATOM   117  C CE     . LYS   A 1 28  ? 4.01066   -34.01805 -15.31494 1.000 167.22058 ? 29  LYS   A CE     1 
ATOM   118  N NZ     . LYS   A 1 28  ? 4.20600   -35.10937 -16.31192 1.000 145.34358 ? 29  LYS   A NZ     1 
ATOM   119  H H      . LYS   A 1 28  ? 2.30686   -29.44970 -13.33904 1.000 205.34462 ? 29  LYS   A H      1 
ATOM   120  H HA     . LYS   A 1 28  ? 1.61057   -31.42765 -11.67485 1.000 208.37675 ? 29  LYS   A HA     1 
ATOM   121  H HB2    . LYS   A 1 28  ? 1.57860   -31.85351 -13.96700 1.000 205.28644 ? 29  LYS   A HB2    1 
ATOM   122  H HB3    . LYS   A 1 28  ? 3.13698   -31.55286 -14.04732 1.000 205.28644 ? 29  LYS   A HB3    1 
ATOM   123  H HG2    . LYS   A 1 28  ? 3.59740   -33.46526 -12.84544 1.000 196.17509 ? 29  LYS   A HG2    1 
ATOM   124  H HG3    . LYS   A 1 28  ? 2.04457   -33.74715 -12.65927 1.000 196.17509 ? 29  LYS   A HG3    1 
ATOM   125  H HD2    . LYS   A 1 28  ? 2.59086   -35.11791 -14.34058 1.000 210.71672 ? 29  LYS   A HD2    1 
ATOM   126  H HD3    . LYS   A 1 28  ? 1.98361   -33.86586 -15.10807 1.000 210.71672 ? 29  LYS   A HD3    1 
ATOM   127  H HE2    . LYS   A 1 28  ? 3.99938   -33.17227 -15.78973 1.000 201.05516 ? 29  LYS   A HE2    1 
ATOM   128  H HE3    . LYS   A 1 28  ? 4.75448   -34.03931 -14.69270 1.000 201.05516 ? 29  LYS   A HE3    1 
ATOM   129  H HZ1    . LYS   A 1 28  ? 5.06290   -35.15643 -16.54775 1.000 174.80277 ? 29  LYS   A HZ1    1 
ATOM   130  H HZ2    . LYS   A 1 28  ? 3.95961   -35.88950 -15.96150 1.000 174.80277 ? 29  LYS   A HZ2    1 
ATOM   131  H HZ3    . LYS   A 1 28  ? 3.71514   -34.95059 -17.03714 1.000 174.80277 ? 29  LYS   A HZ3    1 
ATOM   132  N N      . ILE   A 1 29  ? 3.50750   -31.44046 -10.13175 1.000 163.00480 ? 30  ILE   A N      1 
ATOM   133  C CA     . ILE   A 1 29  ? 4.64790   -31.50379 -9.22583  1.000 149.68151 ? 30  ILE   A CA     1 
ATOM   134  C C      . ILE   A 1 29  ? 5.11049   -32.94884 -9.12796  1.000 142.87612 ? 30  ILE   A C      1 
ATOM   135  O O      . ILE   A 1 29  ? 4.29021   -33.86971 -9.02148  1.000 150.40118 ? 30  ILE   A O      1 
ATOM   136  C CB     . ILE   A 1 29  ? 4.28600   -30.95048 -7.83416  1.000 166.95805 ? 30  ILE   A CB     1 
ATOM   137  C CG1    . ILE   A 1 29  ? 3.38932   -29.71425 -7.95516  1.000 182.23514 ? 30  ILE   A CG1    1 
ATOM   138  C CG2    . ILE   A 1 29  ? 5.54762   -30.61284 -7.05363  1.000 165.12224 ? 30  ILE   A CG2    1 
ATOM   139  C CD1    . ILE   A 1 29  ? 3.98755   -28.58529 -8.76982  1.000 169.35602 ? 30  ILE   A CD1    1 
ATOM   140  H H      . ILE   A 1 29  ? 2.75809   -31.61755 -9.74885  1.000 195.99623 ? 30  ILE   A H      1 
ATOM   141  H HA     . ILE   A 1 29  ? 5.37143   -30.96847 -9.58755  1.000 180.00828 ? 30  ILE   A HA     1 
ATOM   142  H HB     . ILE   A 1 29  ? 3.79527   -31.63748 -7.35654  1.000 200.74013 ? 30  ILE   A HB     1 
ATOM   143  H HG12   . ILE   A 1 29  ? 2.55811   -29.97534 -8.38157  1.000 219.07264 ? 30  ILE   A HG12   1 
ATOM   144  H HG13   . ILE   A 1 29  ? 3.21231   -29.37196 -7.06499  1.000 219.07264 ? 30  ILE   A HG13   1 
ATOM   145  H HG21   . ILE   A 1 29  ? 5.29700   -30.21975 -6.20300  1.000 198.53716 ? 30  ILE   A HG21   1 
ATOM   146  H HG22   . ILE   A 1 29  ? 6.05456   -31.42645 -6.90548  1.000 198.53716 ? 30  ILE   A HG22   1 
ATOM   147  H HG23   . ILE   A 1 29  ? 6.07688   -29.98208 -7.56638  1.000 198.53716 ? 30  ILE   A HG23   1 
ATOM   148  H HD11   . ILE   A 1 29  ? 3.32125   -27.88933 -8.88202  1.000 203.61769 ? 30  ILE   A HD11   1 
ATOM   149  H HD12   . ILE   A 1 29  ? 4.75935   -28.23176 -8.30053  1.000 203.61769 ? 30  ILE   A HD12   1 
ATOM   150  H HD13   . ILE   A 1 29  ? 4.25606   -28.92893 -9.63626  1.000 203.61769 ? 30  ILE   A HD13   1 
ATOM   151  N N      . THR   A 1 30  ? 6.42519   -33.15179 -9.16107  1.000 136.05027 ? 31  THR   A N      1 
ATOM   152  C CA     . THR   A 1 30  ? 7.02201   -34.47452 -9.03805  1.000 135.87912 ? 31  THR   A CA     1 
ATOM   153  C C      . THR   A 1 30  ? 8.01665   -34.47599 -7.88736  1.000 148.06108 ? 31  THR   A C      1 
ATOM   154  O O      . THR   A 1 30  ? 8.92577   -33.63994 -7.84566  1.000 150.30071 ? 31  THR   A O      1 
ATOM   155  C CB     . THR   A 1 30  ? 7.73039   -34.89508 -10.32906 1.000 157.01492 ? 31  THR   A CB     1 
ATOM   156  O OG1    . THR   A 1 30  ? 8.71352   -33.91213 -10.67875 1.000 176.38151 ? 31  THR   A OG1    1 
ATOM   157  C CG2    . THR   A 1 30  ? 6.73030   -35.05593 -11.46608 1.000 158.74884 ? 31  THR   A CG2    1 
ATOM   158  H H      . THR   A 1 30  ? 7.00344   -32.52237 -9.25626  1.000 163.65079 ? 31  THR   A H      1 
ATOM   159  H HA     . THR   A 1 30  ? 6.32125   -35.11768 -8.84785  1.000 163.44542 ? 31  THR   A HA     1 
ATOM   160  H HB     . THR   A 1 30  ? 8.16800   -35.75038 -10.19541 1.000 188.80838 ? 31  THR   A HB     1 
ATOM   161  H HG1    . THR   A 1 30  ? 9.28446   -33.84624 -10.06614 1.000 212.04828 ? 31  THR   A HG1    1 
ATOM   162  H HG21   . THR   A 1 30  ? 7.18839   -35.33704 -12.27356 1.000 190.88908 ? 31  THR   A HG21   1 
ATOM   163  H HG22   . THR   A 1 30  ? 6.06651   -35.72342 -11.23212 1.000 190.88908 ? 31  THR   A HG22   1 
ATOM   164  H HG23   . THR   A 1 30  ? 6.28234   -34.21245 -11.63571 1.000 190.88908 ? 31  THR   A HG23   1 
ATOM   165  N N      . ILE   A 1 31  ? 7.84260   -35.41507 -6.96234  1.000 140.98771 ? 32  ILE   A N      1 
ATOM   166  C CA     . ILE   A 1 31  ? 8.76279   -35.61754 -5.85011  1.000 125.39750 ? 32  ILE   A CA     1 
ATOM   167  C C      . ILE   A 1 31  ? 9.62869   -36.82568 -6.17333  1.000 125.48299 ? 32  ILE   A C      1 
ATOM   168  O O      . ILE   A 1 31  ? 9.11209   -37.88521 -6.54906  1.000 128.26727 ? 32  ILE   A O      1 
ATOM   169  C CB     . ILE   A 1 31  ? 8.00362   -35.81863 -4.52704  1.000 133.06213 ? 32  ILE   A CB     1 
ATOM   170  C CG1    . ILE   A 1 31  ? 7.14076   -34.59087 -4.21908  1.000 129.57096 ? 32  ILE   A CG1    1 
ATOM   171  C CG2    . ILE   A 1 31  ? 8.98273   -36.09344 -3.38714  1.000 146.43250 ? 32  ILE   A CG2    1 
ATOM   172  C CD1    . ILE   A 1 31  ? 6.17262   -34.78601 -3.06220  1.000 160.17468 ? 32  ILE   A CD1    1 
ATOM   173  H H      . ILE   A 1 31  ? 7.17933   -35.96249 -6.95857  1.000 169.57572 ? 32  ILE   A H      1 
ATOM   174  H HA     . ILE   A 1 31  ? 9.33489   -34.84025 -5.75304  1.000 150.86748 ? 32  ILE   A HA     1 
ATOM   175  H HB     . ILE   A 1 31  ? 7.41976   -36.58771 -4.61942  1.000 160.06502 ? 32  ILE   A HB     1 
ATOM   176  H HG12   . ILE   A 1 31  ? 7.72450   -33.84995 -3.99284  1.000 155.87563 ? 32  ILE   A HG12   1 
ATOM   177  H HG13   . ILE   A 1 31  ? 6.61831   -34.37305 -5.00680  1.000 155.87563 ? 32  ILE   A HG13   1 
ATOM   178  H HG21   . ILE   A 1 31  ? 8.49511   -36.10860 -2.54875  1.000 176.10947 ? 32  ILE   A HG21   1 
ATOM   179  H HG22   . ILE   A 1 31  ? 9.40933   -36.95156 -3.53724  1.000 176.10947 ? 32  ILE   A HG22   1 
ATOM   180  H HG23   . ILE   A 1 31  ? 9.65098   -35.39059 -3.36847  1.000 176.10947 ? 32  ILE   A HG23   1 
ATOM   181  H HD11   . ILE   A 1 31  ? 5.63007   -33.98766 -2.96635  1.000 192.60009 ? 32  ILE   A HD11   1 
ATOM   182  H HD12   . ILE   A 1 31  ? 5.60591   -35.55047 -3.25018  1.000 192.60009 ? 32  ILE   A HD12   1 
ATOM   183  H HD13   . ILE   A 1 31  ? 6.67888   -34.94143 -2.24953  1.000 192.60009 ? 32  ILE   A HD13   1 
ATOM   184  N N      . ILE   A 1 32  ? 10.94006  -36.67127 -6.03499  1.000 123.73163 ? 33  ILE   A N      1 
ATOM   185  C CA     . ILE   A 1 32  ? 11.89232  -37.73526 -6.32870  1.000 120.85064 ? 33  ILE   A CA     1 
ATOM   186  C C      . ILE   A 1 32  ? 12.24570  -38.42081 -5.01419  1.000 133.61428 ? 33  ILE   A C      1 
ATOM   187  O O      . ILE   A 1 32  ? 13.00363  -37.87631 -4.20391  1.000 139.94317 ? 33  ILE   A O      1 
ATOM   188  C CB     . ILE   A 1 32  ? 13.14808  -37.19476 -7.02595  1.000 118.65990 ? 33  ILE   A CB     1 
ATOM   189  C CG1    . ILE   A 1 32  ? 12.76860  -36.22849 -8.15161  1.000 130.35216 ? 33  ILE   A CG1    1 
ATOM   190  C CG2    . ILE   A 1 32  ? 13.98542  -38.34137 -7.56778  1.000 118.58956 ? 33  ILE   A CG2    1 
ATOM   191  C CD1    . ILE   A 1 32  ? 11.87802  -36.83300 -9.22022  1.000 157.89595 ? 33  ILE   A CD1    1 
ATOM   192  H H      . ILE   A 1 32  ? 11.31034  -35.94300 -5.76646  1.000 148.86843 ? 33  ILE   A H      1 
ATOM   193  H HA     . ILE   A 1 32  ? 11.47069  -38.38571 -6.91183  1.000 145.41124 ? 33  ILE   A HA     1 
ATOM   194  H HB     . ILE   A 1 32  ? 13.67290  -36.70755 -6.37166  1.000 142.78235 ? 33  ILE   A HB     1 
ATOM   195  H HG12   . ILE   A 1 32  ? 12.29476  -35.47492 -7.76626  1.000 156.81306 ? 33  ILE   A HG12   1 
ATOM   196  H HG13   . ILE   A 1 32  ? 13.58108  -35.92318 -8.58470  1.000 156.81306 ? 33  ILE   A HG13   1 
ATOM   197  H HG21   . ILE   A 1 32  ? 14.71072  -37.97873 -8.10006  1.000 142.69794 ? 33  ILE   A HG21   1 
ATOM   198  H HG22   . ILE   A 1 32  ? 14.34355  -38.85007 -6.82356  1.000 142.69794 ? 33  ILE   A HG22   1 
ATOM   199  H HG23   . ILE   A 1 32  ? 13.42399  -38.91014 -8.11751  1.000 142.69794 ? 33  ILE   A HG23   1 
ATOM   200  H HD11   . ILE   A 1 32  ? 11.70202  -36.16403 -9.90022  1.000 189.86561 ? 33  ILE   A HD11   1 
ATOM   201  H HD12   . ILE   A 1 32  ? 12.33077  -37.59468 -9.61489  1.000 189.86561 ? 33  ILE   A HD12   1 
ATOM   202  H HD13   . ILE   A 1 32  ? 11.04499  -37.11790 -8.81304  1.000 189.86561 ? 33  ILE   A HD13   1 
ATOM   203  N N      . GLY   A 1 33  ? 11.70765  -39.62110 -4.80388  1.000 133.47813 ? 34  GLY   A N      1 
ATOM   204  C CA     . GLY   A 1 33  ? 12.01688  -40.39777 -3.61855  1.000 123.81241 ? 34  GLY   A CA     1 
ATOM   205  C C      . GLY   A 1 33  ? 10.82285  -40.59530 -2.70808  1.000 119.35928 ? 34  GLY   A C      1 
ATOM   206  O O      . GLY   A 1 33  ? 10.25920  -39.62340 -2.19585  1.000 115.51588 ? 34  GLY   A O      1 
ATOM   207  H H      . GLY   A 1 33  ? 11.15666  -40.00637 -5.34015  1.000 160.56423 ? 34  GLY   A H      1 
ATOM   208  H HA2    . GLY   A 1 33  ? 12.34081  -41.27185 -3.88677  1.000 148.96536 ? 34  GLY   A HA2    1 
ATOM   209  H HA3    . GLY   A 1 33  ? 12.71064  -39.94507 -3.11391  1.000 148.96536 ? 34  GLY   A HA3    1 
ATOM   210  N N      . ALA   A 1 34  ? 10.42410  -41.85241 -2.50162  1.000 124.65753 ? 35  ALA   A N      1 
ATOM   211  C CA     . ALA   A 1 34  ? 9.30358   -42.19336 -1.63510  1.000 119.10944 ? 35  ALA   A CA     1 
ATOM   212  C C      . ALA   A 1 34  ? 9.75460   -42.56222 -0.22720  1.000 116.75182 ? 35  ALA   A C      1 
ATOM   213  O O      . ALA   A 1 34  ? 9.13346   -43.41059 0.42125   1.000 112.80249 ? 35  ALA   A O      1 
ATOM   214  C CB     . ALA   A 1 34  ? 8.48916   -43.33693 -2.23862  1.000 120.82932 ? 35  ALA   A CB     1 
ATOM   215  H H      . ALA   A 1 34  ? 10.79817  -42.53752 -2.86258  1.000 149.97951 ? 35  ALA   A H      1 
ATOM   216  H HA     . ALA   A 1 34  ? 8.72693   -41.41615 -1.56949  1.000 143.32180 ? 35  ALA   A HA     1 
ATOM   217  H HB1    . ALA   A 1 34  ? 7.74778   -43.54267 -1.64793  1.000 145.38565 ? 35  ALA   A HB1    1 
ATOM   218  H HB2    . ALA   A 1 34  ? 8.15422   -43.06234 -3.10655  1.000 145.38565 ? 35  ALA   A HB2    1 
ATOM   219  H HB3    . ALA   A 1 34  ? 9.06058   -44.11474 -2.33553  1.000 145.38565 ? 35  ALA   A HB3    1 
ATOM   220  N N      . GLY   A 1 35  ? 10.83634  -41.95126 0.25557   1.000 118.49073 ? 36  GLY   A N      1 
ATOM   221  C CA     . GLY   A 1 35  ? 11.22232  -42.11013 1.62522   1.000 113.02870 ? 36  GLY   A CA     1 
ATOM   222  C C      . GLY   A 1 35  ? 10.22742  -41.44379 2.55446   1.000 121.47134 ? 36  GLY   A C      1 
ATOM   223  O O      . GLY   A 1 35  ? 9.23511   -40.84428 2.11624   1.000 105.00892 ? 36  GLY   A O      1 
ATOM   224  H H      . GLY   A 1 35  ? 11.35504  -41.44112 -0.20302  1.000 142.57934 ? 36  GLY   A H      1 
ATOM   225  H HA2    . GLY   A 1 35  ? 11.26771  -43.05410 1.84376   1.000 136.02491 ? 36  GLY   A HA2    1 
ATOM   226  H HA3    . GLY   A 1 35  ? 12.09504  -41.71097 1.76640   1.000 136.02491 ? 36  GLY   A HA3    1 
ATOM   227  N N      . PRO   A 1 36  ? 10.48364  -41.54337 3.86069   1.000 119.56178 ? 37  PRO   A N      1 
ATOM   228  C CA     . PRO   A 1 36  ? 9.56243   -40.90901 4.81809   1.000 96.27123  ? 37  PRO   A CA     1 
ATOM   229  C C      . PRO   A 1 36  ? 9.36352   -39.42611 4.55796   1.000 99.62271  ? 37  PRO   A C      1 
ATOM   230  O O      . PRO   A 1 36  ? 8.24556   -38.91920 4.71196   1.000 96.70734  ? 37  PRO   A O      1 
ATOM   231  C CB     . PRO   A 1 36  ? 10.22756  -41.17634 6.17695   1.000 97.82338  ? 37  PRO   A CB     1 
ATOM   232  C CG     . PRO   A 1 36  ? 11.64547  -41.53995 5.86778   1.000 99.32546  ? 37  PRO   A CG     1 
ATOM   233  C CD     . PRO   A 1 36  ? 11.62688  -42.19122 4.52663   1.000 101.16496 ? 37  PRO   A CD     1 
ATOM   234  H HA     . PRO   A 1 36  ? 8.70187   -41.35606 4.79586   1.000 114.10943 ? 37  PRO   A HA     1 
ATOM   235  H HB2    . PRO   A 1 36  ? 10.18825  -40.37619 6.72385   1.000 117.77853 ? 37  PRO   A HB2    1 
ATOM   236  H HB3    . PRO   A 1 36  ? 9.77414   -41.90727 6.62533   1.000 117.77853 ? 37  PRO   A HB3    1 
ATOM   237  H HG2    . PRO   A 1 36  ? 12.19084  -40.73796 5.85099   1.000 119.58102 ? 37  PRO   A HG2    1 
ATOM   238  H HG3    . PRO   A 1 36  ? 11.97837  -42.15349 6.54132   1.000 119.58102 ? 37  PRO   A HG3    1 
ATOM   239  H HD2    . PRO   A 1 36  ? 12.45144  -42.01820 4.04594   1.000 121.78843 ? 37  PRO   A HD2    1 
ATOM   240  H HD3    . PRO   A 1 36  ? 11.48443  -43.14728 4.60763   1.000 121.78843 ? 37  PRO   A HD3    1 
ATOM   241  N N      . VAL   A 1 37  ? 10.41613  -38.71470 4.15225   1.000 105.88645 ? 38  VAL   A N      1 
ATOM   242  C CA     . VAL   A 1 37  ? 10.28532  -37.28520 3.89108   1.000 102.46334 ? 38  VAL   A CA     1 
ATOM   243  C C      . VAL   A 1 37  ? 9.46442   -37.04939 2.62991   1.000 117.36997 ? 38  VAL   A C      1 
ATOM   244  O O      . VAL   A 1 37  ? 8.46548   -36.32048 2.64602   1.000 121.99628 ? 38  VAL   A O      1 
ATOM   245  C CB     . VAL   A 1 37  ? 11.67291  -36.62849 3.78528   1.000 93.41707  ? 38  VAL   A CB     1 
ATOM   246  C CG1    . VAL   A 1 37  ? 11.53097  -35.15792 3.43684   1.000 106.53455 ? 38  VAL   A CG1    1 
ATOM   247  C CG2    . VAL   A 1 37  ? 12.44070  -36.79742 5.08086   1.000 116.07897 ? 38  VAL   A CG2    1 
ATOM   248  H H      . VAL   A 1 37  ? 11.20479  -39.03233 4.02289   1.000 127.45422 ? 38  VAL   A H      1 
ATOM   249  H HA     . VAL   A 1 37  ? 9.81621   -36.87962 4.63695   1.000 123.34647 ? 38  VAL   A HA     1 
ATOM   250  H HB     . VAL   A 1 37  ? 12.17596  -37.06330 3.07904   1.000 110.14813 ? 38  VAL   A HB     1 
ATOM   251  H HG11   . VAL   A 1 37  ? 12.36303  -34.70319 3.64127   1.000 128.23193 ? 38  VAL   A HG11   1 
ATOM   252  H HG12   . VAL   A 1 37  ? 11.33256  -35.07521 2.49095   1.000 128.23193 ? 38  VAL   A HG12   1 
ATOM   253  H HG13   . VAL   A 1 37  ? 10.80872  -34.77750 3.96081   1.000 128.23193 ? 38  VAL   A HG13   1 
ATOM   254  H HG21   . VAL   A 1 37  ? 13.33081  -36.42793 4.97093   1.000 139.68524 ? 38  VAL   A HG21   1 
ATOM   255  H HG22   . VAL   A 1 37  ? 11.97270  -36.32772 5.78885   1.000 139.68524 ? 38  VAL   A HG22   1 
ATOM   256  H HG23   . VAL   A 1 37  ? 12.49860  -37.74222 5.29275   1.000 139.68524 ? 38  VAL   A HG23   1 
ATOM   257  N N      . GLY   A 1 38  ? 9.87415   -37.66207 1.51767   1.000 114.93086 ? 39  GLY   A N      1 
ATOM   258  C CA     . GLY   A 1 38  ? 9.16789   -37.44587 0.26655   1.000 112.84500 ? 39  GLY   A CA     1 
ATOM   259  C C      . GLY   A 1 38  ? 7.70042   -37.81402 0.35431   1.000 121.27517 ? 39  GLY   A C      1 
ATOM   260  O O      . GLY   A 1 38  ? 6.83625   -37.08649 -0.14186  1.000 100.90762 ? 39  GLY   A O      1 
ATOM   261  H H      . GLY   A 1 38  ? 10.54570  -38.19678 1.46570   1.000 138.30751 ? 39  GLY   A H      1 
ATOM   262  H HA2    . GLY   A 1 38  ? 9.23305   -36.51004 0.01981   1.000 135.80447 ? 39  GLY   A HA2    1 
ATOM   263  H HA3    . GLY   A 1 38  ? 9.57625   -37.98497 -0.42881  1.000 135.80447 ? 39  GLY   A HA3    1 
ATOM   264  N N      . LEU   A 1 39  ? 7.39786   -38.94709 0.99014   1.000 121.71544 ? 40  LEU   A N      1 
ATOM   265  C CA     . LEU   A 1 39  ? 6.00833   -39.36710 1.13277   1.000 112.53604 ? 40  LEU   A CA     1 
ATOM   266  C C      . LEU   A 1 39  ? 5.21070   -38.34459 1.93249   1.000 131.70505 ? 40  LEU   A C      1 
ATOM   267  O O      . LEU   A 1 39  ? 4.10878   -37.94881 1.53368   1.000 126.19708 ? 40  LEU   A O      1 
ATOM   268  C CB     . LEU   A 1 39  ? 5.94773   -40.74238 1.79549   1.000 101.62465 ? 40  LEU   A CB     1 
ATOM   269  C CG     . LEU   A 1 39  ? 6.40448   -41.91874 0.93311   1.000 105.54600 ? 40  LEU   A CG     1 
ATOM   270  C CD1    . LEU   A 1 39  ? 6.50425   -43.18946 1.75980   1.000 118.47461 ? 40  LEU   A CD1    1 
ATOM   271  C CD2    . LEU   A 1 39  ? 5.45085   -42.11779 -0.23456  1.000 149.91289 ? 40  LEU   A CD2    1 
ATOM   272  H H      . LEU   A 1 39  ? 7.97163   -39.48207 1.34255   1.000 146.44899 ? 40  LEU   A H      1 
ATOM   273  H HA     . LEU   A 1 39  ? 5.60674   -39.43967 0.25280   1.000 135.43372 ? 40  LEU   A HA     1 
ATOM   274  H HB2    . LEU   A 1 39  ? 6.51503   -40.72485 2.58211   1.000 119.99722 ? 40  LEU   A HB2    1 
ATOM   275  H HB3    . LEU   A 1 39  ? 5.02851   -40.91425 2.05315   1.000 119.99722 ? 40  LEU   A HB3    1 
ATOM   276  H HG     . LEU   A 1 39  ? 7.28659   -41.72478 0.57932   1.000 127.04567 ? 40  LEU   A HG     1 
ATOM   277  H HD11   . LEU   A 1 39  ? 6.77212   -43.92153 1.18255   1.000 142.56000 ? 40  LEU   A HD11   1 
ATOM   278  H HD12   . LEU   A 1 39  ? 7.16454   -43.06057 2.45859   1.000 142.56000 ? 40  LEU   A HD12   1 
ATOM   279  H HD13   . LEU   A 1 39  ? 5.63830   -43.37869 2.15379   1.000 142.56000 ? 40  LEU   A HD13   1 
ATOM   280  H HD21   . LEU   A 1 39  ? 5.68630   -42.93641 -0.69858  1.000 180.28593 ? 40  LEU   A HD21   1 
ATOM   281  H HD22   . LEU   A 1 39  ? 4.54429   -42.17905 0.10499   1.000 180.28593 ? 40  LEU   A HD22   1 
ATOM   282  H HD23   . LEU   A 1 39  ? 5.52783   -41.36190 -0.83756  1.000 180.28593 ? 40  LEU   A HD23   1 
ATOM   283  N N      . THR   A 1 40  ? 5.75596   -37.90307 3.06961   1.000 128.53873 ? 41  THR   A N      1 
ATOM   284  C CA     . THR   A 1 40  ? 5.08412   -36.87584 3.85797   1.000 108.64789 ? 41  THR   A CA     1 
ATOM   285  C C      . THR   A 1 40  ? 4.83295   -35.62615 3.02519   1.000 133.33935 ? 41  THR   A C      1 
ATOM   286  O O      . THR   A 1 40  ? 3.74221   -35.04550 3.07380   1.000 123.05494 ? 41  THR   A O      1 
ATOM   287  C CB     . THR   A 1 40  ? 5.91585   -36.53143 5.09120   1.000 100.07943 ? 41  THR   A CB     1 
ATOM   288  O OG1    . THR   A 1 40  ? 6.13449   -37.71565 5.86626   1.000 113.79668 ? 41  THR   A OG1    1 
ATOM   289  C CG2    . THR   A 1 40  ? 5.20030   -35.48952 5.93773   1.000 135.11900 ? 41  THR   A CG2    1 
ATOM   290  H H      . THR   A 1 40  ? 6.50112   -38.17861 3.39888   1.000 154.63694 ? 41  THR   A H      1 
ATOM   291  H HA     . THR   A 1 40  ? 4.22888   -37.22156 4.15788   1.000 130.76794 ? 41  THR   A HA     1 
ATOM   292  H HB     . THR   A 1 40  ? 6.77175   -36.16557 4.81830   1.000 120.48578 ? 41  THR   A HB     1 
ATOM   293  H HG1    . THR   A 1 40  ? 6.52239   -38.29670 5.39988   1.000 136.94649 ? 41  THR   A HG1    1 
ATOM   294  H HG21   . THR   A 1 40  ? 5.59768   -35.45045 6.82173   1.000 162.53327 ? 41  THR   A HG21   1 
ATOM   295  H HG22   . THR   A 1 40  ? 5.27305   -34.61661 5.52103   1.000 162.53327 ? 41  THR   A HG22   1 
ATOM   296  H HG23   . THR   A 1 40  ? 4.26202   -35.71982 6.02426   1.000 162.53327 ? 41  THR   A HG23   1 
ATOM   297  N N      . MET   A 1 41  ? 5.83714   -35.19414 2.25756   1.000 136.27706 ? 42  MET   A N      1 
ATOM   298  C CA     . MET   A 1 41  ? 5.63895   -34.07483 1.34394   1.000 134.34249 ? 42  MET   A CA     1 
ATOM   299  C C      . MET   A 1 41  ? 4.49956   -34.36337 0.37584   1.000 135.63553 ? 42  MET   A C      1 
ATOM   300  O O      . MET   A 1 41  ? 3.64869   -33.50013 0.12587   1.000 148.02715 ? 42  MET   A O      1 
ATOM   301  C CB     . MET   A 1 41  ? 6.93218   -33.79387 0.57600   1.000 133.35402 ? 42  MET   A CB     1 
ATOM   302  C CG     . MET   A 1 41  ? 6.87273   -32.55040 -0.30074  1.000 145.46509 ? 42  MET   A CG     1 
ATOM   303  S SD     . MET   A 1 41  ? 6.89218   -31.02683 0.66320   1.000 156.55532 ? 42  MET   A SD     1 
ATOM   304  C CE     . MET   A 1 41  ? 6.16957   -29.87105 -0.49691  1.000 160.25596 ? 42  MET   A CE     1 
ATOM   305  H H      . MET   A 1 41  ? 6.62956   -35.52819 2.24864   1.000 163.92294 ? 42  MET   A H      1 
ATOM   306  H HA     . MET   A 1 41  ? 5.42225   -33.28315 1.86084   1.000 161.60146 ? 42  MET   A HA     1 
ATOM   307  H HB2    . MET   A 1 41  ? 7.65241   -33.67117 1.21405   1.000 160.41529 ? 42  MET   A HB2    1 
ATOM   308  H HB3    . MET   A 1 41  ? 7.12354   -34.55152 0.00133   1.000 160.41529 ? 42  MET   A HB3    1 
ATOM   309  H HG2    . MET   A 1 41  ? 7.64130   -32.54237 -0.89247  1.000 174.94858 ? 42  MET   A HG2    1 
ATOM   310  H HG3    . MET   A 1 41  ? 6.05397   -32.56759 -0.82059  1.000 174.94858 ? 42  MET   A HG3    1 
ATOM   311  H HE1    . MET   A 1 41  ? 6.12399   -28.99499 -0.08298  1.000 192.69762 ? 42  MET   A HE1    1 
ATOM   312  H HE2    . MET   A 1 41  ? 6.72434   -29.83290 -1.29170  1.000 192.69762 ? 42  MET   A HE2    1 
ATOM   313  H HE3    . MET   A 1 41  ? 5.27792   -30.17350 -0.73011  1.000 192.69762 ? 42  MET   A HE3    1 
ATOM   314  N N      . ALA   A 1 42  ? 4.46507   -35.57647 -0.17593  1.000 123.22917 ? 43  ALA   A N      1 
ATOM   315  C CA     . ALA   A 1 42  ? 3.41691   -35.92527 -1.12708  1.000 137.57210 ? 43  ALA   A CA     1 
ATOM   316  C C      . ALA   A 1 42  ? 2.03752   -35.82541 -0.48970  1.000 137.47297 ? 43  ALA   A C      1 
ATOM   317  O O      . ALA   A 1 42  ? 1.09103   -35.33145 -1.11388  1.000 135.98136 ? 43  ALA   A O      1 
ATOM   318  C CB     . ALA   A 1 42  ? 3.65412   -37.33325 -1.67092  1.000 145.90608 ? 43  ALA   A CB     1 
ATOM   319  H H      . ALA   A 1 42  ? 5.02937   -36.20588 -0.01781  1.000 148.26548 ? 43  ALA   A H      1 
ATOM   320  H HA     . ALA   A 1 42  ? 3.44967   -35.30369 -1.87103  1.000 165.47699 ? 43  ALA   A HA     1 
ATOM   321  H HB1    . ALA   A 1 42  ? 2.96210   -37.54278 -2.31753  1.000 175.47776 ? 43  ALA   A HB1    1 
ATOM   322  H HB2    . ALA   A 1 42  ? 4.52512   -37.36476 -2.09667  1.000 175.47776 ? 43  ALA   A HB2    1 
ATOM   323  H HB3    . ALA   A 1 42  ? 3.62222   -37.96527 -0.93578  1.000 175.47776 ? 43  ALA   A HB3    1 
ATOM   324  N N      . ARG   A 1 43  ? 1.90313   -36.28833 0.75406   1.000 131.02636 ? 44  ARG   A N      1 
ATOM   325  C CA     . ARG   A 1 43  ? 0.60843   -36.23759 1.42529   1.000 142.05888 ? 44  ARG   A CA     1 
ATOM   326  C C      . ARG   A 1 43  ? 0.18780   -34.79829 1.69664   1.000 150.10591 ? 44  ARG   A C      1 
ATOM   327  O O      . ARG   A 1 43  ? -0.94981  -34.40961 1.40704   1.000 155.58302 ? 44  ARG   A O      1 
ATOM   328  C CB     . ARG   A 1 43  ? 0.66535   -37.04567 2.72313   1.000 143.01367 ? 44  ARG   A CB     1 
ATOM   329  C CG     . ARG   A 1 43  ? -0.46684  -36.76641 3.70775   1.000 146.12069 ? 44  ARG   A CG     1 
ATOM   330  C CD     . ARG   A 1 43  ? -1.84537  -37.01525 3.10949   1.000 157.89638 ? 44  ARG   A CD     1 
ATOM   331  N NE     . ARG   A 1 43  ? -2.90387  -36.65945 4.04894   1.000 159.40994 ? 44  ARG   A NE     1 
ATOM   332  C CZ     . ARG   A 1 43  ? -4.19271  -36.91491 3.86733   1.000 156.21255 ? 44  ARG   A CZ     1 
ATOM   333  N NH1    . ARG   A 1 43  ? -4.62723  -37.55424 2.79308   1.000 140.18441 ? 44  ARG   A NH1    1 
ATOM   334  N NH2    . ARG   A 1 43  ? -5.06766  -36.52012 4.78832   1.000 153.05053 ? 44  ARG   A NH2    1 
ATOM   335  H H      . ARG   A 1 43  ? 2.53710   -36.63130 1.22315   1.000 157.62211 ? 44  ARG   A H      1 
ATOM   336  H HA     . ARG   A 1 43  ? -0.06243  -36.63921 0.85122   1.000 170.86113 ? 44  ARG   A HA     1 
ATOM   337  H HB2    . ARG   A 1 43  ? 0.62985   -37.98880 2.49920   1.000 172.00687 ? 44  ARG   A HB2    1 
ATOM   338  H HB3    . ARG   A 1 43  ? 1.49970   -36.84303 3.17445   1.000 172.00687 ? 44  ARG   A HB3    1 
ATOM   339  H HG2    . ARG   A 1 43  ? -0.36597  -37.34671 4.47845   1.000 175.73530 ? 44  ARG   A HG2    1 
ATOM   340  H HG3    . ARG   A 1 43  ? -0.42377  -35.83756 3.98394   1.000 175.73530 ? 44  ARG   A HG3    1 
ATOM   341  H HD2    . ARG   A 1 43  ? -1.95154  -36.47558 2.31049   1.000 189.86613 ? 44  ARG   A HD2    1 
ATOM   342  H HD3    . ARG   A 1 43  ? -1.93550  -37.95557 2.88910   1.000 189.86613 ? 44  ARG   A HD3    1 
ATOM   343  H HE     . ARG   A 1 43  ? -2.67551  -36.25488 4.77266   1.000 191.68240 ? 44  ARG   A HE     1 
ATOM   344  H HH11   . ARG   A 1 43  ? -4.06934  -37.81453 2.19257   1.000 168.61176 ? 44  ARG   A HH11   1 
ATOM   345  H HH12   . ARG   A 1 43  ? -5.46747  -37.70940 2.69553   1.000 168.61176 ? 44  ARG   A HH12   1 
ATOM   346  H HH21   . ARG   A 1 43  ? -4.79507  -36.10496 5.49042   1.000 184.05110 ? 44  ARG   A HH21   1 
ATOM   347  H HH22   . ARG   A 1 43  ? -5.90590  -36.68005 4.68164   1.000 184.05110 ? 44  ARG   A HH22   1 
ATOM   348  N N      . LEU   A 1 44  ? 1.09409   -33.98953 2.25195   1.000 147.26559 ? 45  LEU   A N      1 
ATOM   349  C CA     . LEU   A 1 44  ? 0.75304   -32.60242 2.55120   1.000 152.09845 ? 45  LEU   A CA     1 
ATOM   350  C C      . LEU   A 1 44  ? 0.30725   -31.86302 1.29589   1.000 161.12378 ? 45  LEU   A C      1 
ATOM   351  O O      . LEU   A 1 44  ? -0.59994  -31.02490 1.34934   1.000 166.80100 ? 45  LEU   A O      1 
ATOM   352  C CB     . LEU   A 1 44  ? 1.94363   -31.89475 3.19626   1.000 155.52943 ? 45  LEU   A CB     1 
ATOM   353  C CG     . LEU   A 1 44  ? 2.34591   -32.39145 4.58647   1.000 169.24909 ? 45  LEU   A CG     1 
ATOM   354  C CD1    . LEU   A 1 44  ? 3.58721   -31.65775 5.06984   1.000 161.41726 ? 45  LEU   A CD1    1 
ATOM   355  C CD2    . LEU   A 1 44  ? 1.20567   -32.22664 5.58604   1.000 158.47522 ? 45  LEU   A CD2    1 
ATOM   356  H H      . LEU   A 1 44  ? 1.89697   -34.21650 2.46043   1.000 177.10918 ? 45  LEU   A H      1 
ATOM   357  H HA     . LEU   A 1 44  ? 0.01899   -32.59105 3.18519   1.000 182.90861 ? 45  LEU   A HA     1 
ATOM   358  H HB2    . LEU   A 1 44  ? 2.71321   -32.00830 2.61682   1.000 187.02579 ? 45  LEU   A HB2    1 
ATOM   359  H HB3    . LEU   A 1 44  ? 1.72696   -30.95291 3.27930   1.000 187.02579 ? 45  LEU   A HB3    1 
ATOM   360  H HG     . LEU   A 1 44  ? 2.54893   -33.33825 4.52939   1.000 203.48938 ? 45  LEU   A HG     1 
ATOM   361  H HD11   . LEU   A 1 44  ? 3.89292   -32.06448 5.89568   1.000 194.09119 ? 45  LEU   A HD11   1 
ATOM   362  H HD12   . LEU   A 1 44  ? 4.27800   -31.72546 4.39226   1.000 194.09119 ? 45  LEU   A HD12   1 
ATOM   363  H HD13   . LEU   A 1 44  ? 3.36399   -30.72625 5.22272   1.000 194.09119 ? 45  LEU   A HD13   1 
ATOM   364  H HD21   . LEU   A 1 44  ? 1.53953   -32.40761 6.47861   1.000 190.56074 ? 45  LEU   A HD21   1 
ATOM   365  H HD22   . LEU   A 1 44  ? 0.87085   -31.31763 5.53611   1.000 190.56074 ? 45  LEU   A HD22   1 
ATOM   366  H HD23   . LEU   A 1 44  ? 0.49839   -32.85231 5.36427   1.000 190.56074 ? 45  LEU   A HD23   1 
ATOM   367  N N      . LEU   A 1 45  ? 0.92967   -32.16220 0.15436   1.000 153.62657 ? 46  LEU   A N      1 
ATOM   368  C CA     . LEU   A 1 45  ? 0.50743   -31.54414 -1.09726  1.000 148.52916 ? 46  LEU   A CA     1 
ATOM   369  C C      . LEU   A 1 45  ? -0.81742  -32.12525 -1.57321  1.000 150.63814 ? 46  LEU   A C      1 
ATOM   370  O O      . LEU   A 1 45  ? -1.75519  -31.38464 -1.89112  1.000 157.82007 ? 46  LEU   A O      1 
ATOM   371  C CB     . LEU   A 1 45  ? 1.58077   -31.73351 -2.16787  1.000 149.35688 ? 46  LEU   A CB     1 
ATOM   372  C CG     . LEU   A 1 45  ? 2.84714   -30.88764 -2.04715  1.000 172.39333 ? 46  LEU   A CG     1 
ATOM   373  C CD1    . LEU   A 1 45  ? 3.84085   -31.28888 -3.12765  1.000 200.53551 ? 46  LEU   A CD1    1 
ATOM   374  C CD2    . LEU   A 1 45  ? 2.52901   -29.40350 -2.14150  1.000 192.78944 ? 46  LEU   A CD2    1 
ATOM   375  H H      . LEU   A 1 45  ? 1.58786   -32.71079 0.08058   1.000 184.74236 ? 46  LEU   A H      1 
ATOM   376  H HA     . LEU   A 1 45  ? 0.39124   -30.59271 -0.94829  1.000 178.62546 ? 46  LEU   A HA     1 
ATOM   377  H HB2    . LEU   A 1 45  ? 1.85958   -32.66237 -2.14837  1.000 179.61872 ? 46  LEU   A HB2    1 
ATOM   378  H HB3    . LEU   A 1 45  ? 1.18331   -31.52441 -3.02764  1.000 179.61872 ? 46  LEU   A HB3    1 
ATOM   379  H HG     . LEU   A 1 45  ? 3.24871   -31.04364 -1.17806  1.000 207.26246 ? 46  LEU   A HG     1 
ATOM   380  H HD11   . LEU   A 1 45  ? 4.65635   -30.77638 -3.01276  1.000 241.03308 ? 46  LEU   A HD11   1 
ATOM   381  H HD12   . LEU   A 1 45  ? 4.03131   -32.23643 -3.04541  1.000 241.03308 ? 46  LEU   A HD12   1 
ATOM   382  H HD13   . LEU   A 1 45  ? 3.45352   -31.10361 -3.99745  1.000 241.03308 ? 46  LEU   A HD13   1 
ATOM   383  H HD21   . LEU   A 1 45  ? 3.35849   -28.90097 -2.12366  1.000 231.73780 ? 46  LEU   A HD21   1 
ATOM   384  H HD22   . LEU   A 1 45  ? 2.05725   -29.23382 -2.97189  1.000 231.73780 ? 46  LEU   A HD22   1 
ATOM   385  H HD23   . LEU   A 1 45  ? 1.97310   -29.15115 -1.38772  1.000 231.73780 ? 46  LEU   A HD23   1 
ATOM   386  N N      . GLN   A 1 46  ? -0.91138  -33.45587 -1.62740  1.000 147.38091 ? 47  GLN   A N      1 
ATOM   387  C CA     . GLN   A 1 46  ? -2.09977  -34.09074 -2.18675  1.000 157.03674 ? 47  GLN   A CA     1 
ATOM   388  C C      . GLN   A 1 46  ? -3.34488  -33.74357 -1.38100  1.000 166.50835 ? 47  GLN   A C      1 
ATOM   389  O O      . GLN   A 1 46  ? -4.42341  -33.53889 -1.95110  1.000 166.19899 ? 47  GLN   A O      1 
ATOM   390  C CB     . GLN   A 1 46  ? -1.90027  -35.60469 -2.24966  1.000 152.63078 ? 47  GLN   A CB     1 
ATOM   391  C CG     . GLN   A 1 46  ? -3.02879  -36.34874 -2.94436  1.000 147.22652 ? 47  GLN   A CG     1 
ATOM   392  C CD     . GLN   A 1 46  ? -2.52259  -37.50475 -3.77819  1.000 146.36014 ? 47  GLN   A CD     1 
ATOM   393  O OE1    . GLN   A 1 46  ? -2.79643  -37.58944 -4.97551  1.000 169.59236 ? 47  GLN   A OE1    1 
ATOM   394  N NE2    . GLN   A 1 46  ? -1.77318  -38.40163 -3.15004  1.000 139.84494 ? 47  GLN   A NE2    1 
ATOM   395  H H      . GLN   A 1 46  ? -0.30914  -34.00391 -1.35070  1.000 177.24756 ? 47  GLN   A H      1 
ATOM   396  H HA     . GLN   A 1 46  ? -2.23249  -33.76693 -3.09143  1.000 188.83456 ? 47  GLN   A HA     1 
ATOM   397  H HB2    . GLN   A 1 46  ? -1.08144  -35.79037 -2.73541  1.000 183.54741 ? 47  GLN   A HB2    1 
ATOM   398  H HB3    . GLN   A 1 46  ? -1.83409  -35.94735 -1.34462  1.000 183.54741 ? 47  GLN   A HB3    1 
ATOM   399  H HG2    . GLN   A 1 46  ? -3.63645  -36.70156 -2.27566  1.000 177.06230 ? 47  GLN   A HG2    1 
ATOM   400  H HG3    . GLN   A 1 46  ? -3.50007  -35.73649 -3.53083  1.000 177.06230 ? 47  GLN   A HG3    1 
ATOM   401  H HE21   . GLN   A 1 46  ? -1.59978  -38.30671 -2.31307  1.000 168.20440 ? 47  GLN   A HE21   1 
ATOM   402  H HE22   . GLN   A 1 46  ? -1.46087  -39.07787 -3.57989  1.000 168.20440 ? 47  GLN   A HE22   1 
ATOM   403  N N      . GLN   A 1 47  ? -3.21895  -33.66656 -0.05407  1.000 165.66578 ? 48  GLN   A N      1 
ATOM   404  C CA     . GLN   A 1 47  ? -4.35748  -33.28605 0.77261   1.000 165.20654 ? 48  GLN   A CA     1 
ATOM   405  C C      . GLN   A 1 47  ? -4.72538  -31.81587 0.61607   1.000 165.79873 ? 48  GLN   A C      1 
ATOM   406  O O      . GLN   A 1 47  ? -5.75654  -31.39493 1.15079   1.000 171.47443 ? 48  GLN   A O      1 
ATOM   407  C CB     . GLN   A 1 47  ? -4.07411  -33.60125 2.24452   1.000 163.81720 ? 48  GLN   A CB     1 
ATOM   408  C CG     . GLN   A 1 47  ? -3.10456  -32.65364 2.93400   1.000 166.20450 ? 48  GLN   A CG     1 
ATOM   409  C CD     . GLN   A 1 47  ? -2.79361  -33.07912 4.36010   1.000 164.25214 ? 48  GLN   A CD     1 
ATOM   410  O OE1    . GLN   A 1 47  ? -3.08088  -34.20798 4.76038   1.000 150.68154 ? 48  GLN   A OE1    1 
ATOM   411  N NE2    . GLN   A 1 47  ? -2.20839  -32.17270 5.13472   1.000 162.02701 ? 48  GLN   A NE2    1 
ATOM   412  H H      . GLN   A 1 47  ? -2.49521  -33.82774 0.38161   1.000 199.18941 ? 48  GLN   A H      1 
ATOM   413  H HA     . GLN   A 1 47  ? -5.12554  -33.81485 0.50549   1.000 198.63832 ? 48  GLN   A HA     1 
ATOM   414  H HB2    . GLN   A 1 47  ? -4.91174  -33.56476 2.73233   1.000 196.97111 ? 48  GLN   A HB2    1 
ATOM   415  H HB3    . GLN   A 1 47  ? -3.69669  -34.49311 2.29962   1.000 196.97111 ? 48  GLN   A HB3    1 
ATOM   416  H HG2    . GLN   A 1 47  ? -2.27187  -32.63439 2.43685   1.000 199.83587 ? 48  GLN   A HG2    1 
ATOM   417  H HG3    . GLN   A 1 47  ? -3.49450  -31.76593 2.96254   1.000 199.83587 ? 48  GLN   A HG3    1 
ATOM   418  H HE21   . GLN   A 1 47  ? -2.02553  -31.39295 4.82143   1.000 194.82289 ? 48  GLN   A HE21   1 
ATOM   419  H HE22   . GLN   A 1 47  ? -2.01233  -32.36555 5.94956   1.000 194.82289 ? 48  GLN   A HE22   1 
ATOM   420  N N      . ASN   A 1 48  ? -3.91155  -31.02986 -0.09134  1.000 167.33845 ? 49  ASN   A N      1 
ATOM   421  C CA     . ASN   A 1 48  ? -4.24085  -29.65299 -0.43157  1.000 174.40752 ? 49  ASN   A CA     1 
ATOM   422  C C      . ASN   A 1 48  ? -4.69487  -29.51339 -1.88173  1.000 161.61738 ? 49  ASN   A C      1 
ATOM   423  O O      . ASN   A 1 48  ? -4.60187  -28.42161 -2.45248  1.000 160.46666 ? 49  ASN   A O      1 
ATOM   424  C CB     . ASN   A 1 48  ? -3.04463  -28.73632 -0.16241  1.000 172.97778 ? 49  ASN   A CB     1 
ATOM   425  C CG     . ASN   A 1 48  ? -2.75169  -28.57828 1.31845   1.000 181.41004 ? 49  ASN   A CG     1 
ATOM   426  O OD1    . ASN   A 1 48  ? -3.54594  -28.00009 2.06107   1.000 178.24737 ? 49  ASN   A OD1    1 
ATOM   427  N ND2    . ASN   A 1 48  ? -1.60143  -29.08182 1.75276   1.000 187.76024 ? 49  ASN   A ND2    1 
ATOM   428  H H      . ASN   A 1 48  ? -3.14563  -31.28166 -0.39060  1.000 201.19661 ? 49  ASN   A H      1 
ATOM   429  H HA     . ASN   A 1 48  ? -4.96890  -29.36246 0.13977   1.000 209.67949 ? 49  ASN   A HA     1 
ATOM   430  H HB2    . ASN   A 1 48  ? -2.25678  -29.11123 -0.58625  1.000 207.96381 ? 49  ASN   A HB2    1 
ATOM   431  H HB3    . ASN   A 1 48  ? -3.23105  -27.85714 -0.52736  1.000 207.96381 ? 49  ASN   A HB3    1 
ATOM   432  H HD21   . ASN   A 1 48  ? -1.39031  -29.01724 2.58394   1.000 225.70276 ? 49  ASN   A HD21   1 
ATOM   433  H HD22   . ASN   A 1 48  ? -1.06801  -29.47234 1.20270   1.000 225.70276 ? 49  ASN   A HD22   1 
ATOM   434  N N      . ARG   A 1 49  ? -5.17626  -30.60069 -2.48782  1.000 160.23744 ? 50  ARG   A N      1 
ATOM   435  C CA     . ARG   A 1 49  ? -5.70173  -30.59099 -3.85032  1.000 162.87904 ? 50  ARG   A CA     1 
ATOM   436  C C      . ARG   A 1 49  ? -4.60811  -30.35650 -4.88748  1.000 165.41973 ? 50  ARG   A C      1 
ATOM   437  O O      . ARG   A 1 49  ? -4.86612  -29.78574 -5.94924  1.000 180.62184 ? 50  ARG   A O      1 
ATOM   438  C CB     . ARG   A 1 49  ? -6.80441  -29.53837 -4.01286  1.000 165.96907 ? 50  ARG   A CB     1 
ATOM   439  C CG     . ARG   A 1 49  ? -7.95027  -29.67496 -3.02731  1.000 168.86031 ? 50  ARG   A CG     1 
ATOM   440  C CD     . ARG   A 1 49  ? -9.09118  -28.72589 -3.36954  1.000 178.79140 ? 50  ARG   A CD     1 
ATOM   441  N NE     . ARG   A 1 49  ? -10.31781 -29.06507 -2.65597  1.000 199.37333 ? 50  ARG   A NE     1 
ATOM   442  C CZ     . ARG   A 1 49  ? -11.38203 -29.64292 -3.20159  1.000 201.94916 ? 50  ARG   A CZ     1 
ATOM   443  N NH1    . ARG   A 1 49  ? -11.42611 -29.94498 -4.49001  1.000 204.59618 ? 50  ARG   A NH1    1 
ATOM   444  N NH2    . ARG   A 1 49  ? -12.43274 -29.91924 -2.43445  1.000 194.57984 ? 50  ARG   A NH2    1 
ATOM   445  H H      . ARG   A 1 49  ? -5.20898  -31.37637 -2.11790  1.000 192.67540 ? 50  ARG   A H      1 
ATOM   446  H HA     . ARG   A 1 49  ? -6.08582  -31.46426 -4.02572  1.000 195.84532 ? 50  ARG   A HA     1 
ATOM   447  H HB2    . ARG   A 1 49  ? -6.41372  -28.65923 -3.88882  1.000 199.55335 ? 50  ARG   A HB2    1 
ATOM   448  H HB3    . ARG   A 1 49  ? -7.17492  -29.61372 -4.90613  1.000 199.55335 ? 50  ARG   A HB3    1 
ATOM   449  H HG2    . ARG   A 1 49  ? -8.29019  -30.58310 -3.05260  1.000 203.02284 ? 50  ARG   A HG2    1 
ATOM   450  H HG3    . ARG   A 1 49  ? -7.63430  -29.46372 -2.13488  1.000 203.02284 ? 50  ARG   A HG3    1 
ATOM   451  H HD2    . ARG   A 1 49  ? -8.83855  -27.82191 -3.12481  1.000 214.94015 ? 50  ARG   A HD2    1 
ATOM   452  H HD3    . ARG   A 1 49  ? -9.27145  -28.77380 -4.32144  1.000 214.94015 ? 50  ARG   A HD3    1 
ATOM   453  H HE     . ARG   A 1 49  ? -10.35458 -28.87634 -1.81774  1.000 239.63847 ? 50  ARG   A HE     1 
ATOM   454  H HH11   . ARG   A 1 49  ? -10.75427 -29.76718 -4.99658  1.000 245.90589 ? 50  ARG   A HH11   1 
ATOM   455  H HH12   . ARG   A 1 49  ? -12.12658 -30.31898 -4.82026  1.000 245.90589 ? 50  ARG   A HH12   1 
ATOM   456  H HH21   . ARG   A 1 49  ? -12.41704 -29.72388 -1.59708  1.000 233.88628 ? 50  ARG   A HH21   1 
ATOM   457  H HH22   . ARG   A 1 49  ? -13.12786 -30.29329 -2.77577  1.000 233.88628 ? 50  ARG   A HH22   1 
ATOM   458  N N      . VAL   A 1 50  ? -3.38561  -30.79598 -4.60128  1.000 157.45843 ? 51  VAL   A N      1 
ATOM   459  C CA     . VAL   A 1 50  ? -2.24491  -30.57610 -5.48336  1.000 158.31249 ? 51  VAL   A CA     1 
ATOM   460  C C      . VAL   A 1 50  ? -1.99035  -31.83404 -6.29929  1.000 166.08942 ? 51  VAL   A C      1 
ATOM   461  O O      . VAL   A 1 50  ? -2.07348  -32.95584 -5.78157  1.000 157.39151 ? 51  VAL   A O      1 
ATOM   462  C CB     . VAL   A 1 50  ? -0.98930  -30.18070 -4.68147  1.000 150.19825 ? 51  VAL   A CB     1 
ATOM   463  C CG1    . VAL   A 1 50  ? 0.21520   -30.04687 -5.60420  1.000 156.45676 ? 51  VAL   A CG1    1 
ATOM   464  C CG2    . VAL   A 1 50  ? -1.23047  -28.88664 -3.92394  1.000 171.82401 ? 51  VAL   A CG2    1 
ATOM   465  H H      . VAL   A 1 50  ? -3.18908  -31.23292 -3.88709  1.000 189.34059 ? 51  VAL   A H      1 
ATOM   466  H HA     . VAL   A 1 50  ? -2.45962  -29.85515 -6.09576  1.000 190.36545 ? 51  VAL   A HA     1 
ATOM   467  H HB     . VAL   A 1 50  ? -0.79667  -30.87846 -4.03577  1.000 180.62837 ? 51  VAL   A HB     1 
ATOM   468  H HG11   . VAL   A 1 50  ? 0.92359   -29.58078 -5.13319  1.000 188.13858 ? 51  VAL   A HG11   1 
ATOM   469  H HG12   . VAL   A 1 50  ? 0.51595   -30.93249 -5.86137  1.000 188.13858 ? 51  VAL   A HG12   1 
ATOM   470  H HG13   . VAL   A 1 50  ? -0.04477  -29.54411 -6.39194  1.000 188.13858 ? 51  VAL   A HG13   1 
ATOM   471  H HG21   . VAL   A 1 50  ? -0.40268  -28.60918 -3.50125  1.000 206.57928 ? 51  VAL   A HG21   1 
ATOM   472  H HG22   . VAL   A 1 50  ? -1.52754  -28.20605 -4.54801  1.000 206.57928 ? 51  VAL   A HG22   1 
ATOM   473  H HG23   . VAL   A 1 50  ? -1.91165  -29.03746 -3.25003  1.000 206.57928 ? 51  VAL   A HG23   1 
ATOM   474  N N      . ASP   A 1 51  ? -1.68336  -31.64715 -7.58230  1.000 156.55128 ? 52  ASP   A N      1 
ATOM   475  C CA     . ASP   A 1 51  ? -1.24900  -32.74124 -8.44445  1.000 153.50335 ? 52  ASP   A CA     1 
ATOM   476  C C      . ASP   A 1 51  ? 0.21529   -33.03015 -8.13926  1.000 154.43970 ? 52  ASP   A C      1 
ATOM   477  O O      . ASP   A 1 51  ? 1.09508   -32.22678 -8.46674  1.000 148.95732 ? 52  ASP   A O      1 
ATOM   478  C CB     . ASP   A 1 51  ? -1.44105  -32.38078 -9.91428  1.000 166.19234 ? 52  ASP   A CB     1 
ATOM   479  C CG     . ASP   A 1 51  ? -1.20107  -33.56153 -10.84370 1.000 174.15940 ? 52  ASP   A CG     1 
ATOM   480  O OD1    . ASP   A 1 51  ? -0.58525  -34.55664 -10.40604 1.000 163.02494 ? 52  ASP   A OD1    1 
ATOM   481  O OD2    . ASP   A 1 51  ? -1.62624  -33.49332 -12.01644 1.000 157.47697 ? 52  ASP   A OD2    1 
ATOM   482  H H      . ASP   A 1 51  ? -1.71958  -30.88580 -7.98059  1.000 188.25201 ? 52  ASP   A H      1 
ATOM   483  H HA     . ASP   A 1 51  ? -1.77787  -33.53330 -8.26048  1.000 184.59449 ? 52  ASP   A HA     1 
ATOM   484  H HB2    . ASP   A 1 51  ? -2.35114  -32.07313 -10.04838 1.000 199.82128 ? 52  ASP   A HB2    1 
ATOM   485  H HB3    . ASP   A 1 51  ? -0.81515  -31.67905 -10.15243 1.000 199.82128 ? 52  ASP   A HB3    1 
ATOM   486  N N      . VAL   A 1 52  ? 0.48019   -34.17125 -7.51158  1.000 148.16025 ? 53  VAL   A N      1 
ATOM   487  C CA     . VAL   A 1 52  ? 1.82056   -34.53572 -7.07491  1.000 144.48472 ? 53  VAL   A CA     1 
ATOM   488  C C      . VAL   A 1 52  ? 2.09306   -35.97461 -7.48683  1.000 144.08509 ? 53  VAL   A C      1 
ATOM   489  O O      . VAL   A 1 52  ? 1.21456   -36.83783 -7.38480  1.000 148.50116 ? 53  VAL   A O      1 
ATOM   490  C CB     . VAL   A 1 52  ? 1.98186   -34.35768 -5.54874  1.000 146.70849 ? 53  VAL   A CB     1 
ATOM   491  C CG1    . VAL   A 1 52  ? 1.07561   -35.32500 -4.79325  1.000 156.41550 ? 53  VAL   A CG1    1 
ATOM   492  C CG2    . VAL   A 1 52  ? 3.43579   -34.53607 -5.13790  1.000 143.68494 ? 53  VAL   A CG2    1 
ATOM   493  H H      . VAL   A 1 52  ? -0.11492  -34.76303 -7.32384  1.000 178.18277 ? 53  VAL   A H      1 
ATOM   494  H HA     . VAL   A 1 52  ? 2.47143   -33.96957 -7.51846  1.000 173.77213 ? 53  VAL   A HA     1 
ATOM   495  H HB     . VAL   A 1 52  ? 1.71513   -33.45607 -5.31030  1.000 176.44066 ? 53  VAL   A HB     1 
ATOM   496  H HG11   . VAL   A 1 52  ? 1.02449   -35.04984 -3.86450  1.000 188.08907 ? 53  VAL   A HG11   1 
ATOM   497  H HG12   . VAL   A 1 52  ? 0.19184   -35.30708 -5.19267  1.000 188.08907 ? 53  VAL   A HG12   1 
ATOM   498  H HG13   . VAL   A 1 52  ? 1.44774   -36.21875 -4.85345  1.000 188.08907 ? 53  VAL   A HG13   1 
ATOM   499  H HG21   . VAL   A 1 52  ? 3.51802   -34.36739 -4.18623  1.000 172.81240 ? 53  VAL   A HG21   1 
ATOM   500  H HG22   . VAL   A 1 52  ? 3.71131   -35.44437 -5.33787  1.000 172.81240 ? 53  VAL   A HG22   1 
ATOM   501  H HG23   . VAL   A 1 52  ? 3.98347   -33.90753 -5.63377  1.000 172.81240 ? 53  VAL   A HG23   1 
ATOM   502  N N      . THR   A 1 53  ? 3.31058   -36.22585 -7.96435  1.000 141.55711 ? 54  THR   A N      1 
ATOM   503  C CA     . THR   A 1 53  ? 3.76362   -37.55973 -8.33006  1.000 138.03373 ? 54  THR   A CA     1 
ATOM   504  C C      . THR   A 1 53  ? 5.05291   -37.87681 -7.58706  1.000 138.98636 ? 54  THR   A C      1 
ATOM   505  O O      . THR   A 1 53  ? 5.92318   -37.01380 -7.44050  1.000 143.46260 ? 54  THR   A O      1 
ATOM   506  C CB     . THR   A 1 53  ? 3.99726   -37.67719 -9.84121  1.000 150.19833 ? 54  THR   A CB     1 
ATOM   507  O OG1    . THR   A 1 53  ? 2.73767   -37.74776 -10.52081 1.000 174.41538 ? 54  THR   A OG1    1 
ATOM   508  C CG2    . THR   A 1 53  ? 4.82456   -38.91555 -10.16586 1.000 149.07228 ? 54  THR   A CG2    1 
ATOM   509  H H      . THR   A 1 53  ? 3.90777   -35.61948 -8.08799  1.000 170.25900 ? 54  THR   A H      1 
ATOM   510  H HA     . THR   A 1 53  ? 3.09147   -38.21059 -8.07416  1.000 166.03095 ? 54  THR   A HA     1 
ATOM   511  H HB     . THR   A 1 53  ? 4.48583   -36.89907 -10.15222 1.000 180.62847 ? 54  THR   A HB     1 
ATOM   512  H HG1    . THR   A 1 53  ? 2.33103   -38.44886 -10.30010 1.000 209.68892 ? 54  THR   A HG1    1 
ATOM   513  H HG21   . THR   A 1 53  ? 4.72486   -39.14480 -11.10310 1.000 179.27721 ? 54  THR   A HG21   1 
ATOM   514  H HG22   . THR   A 1 53  ? 5.76165   -38.74629 -9.98114  1.000 179.27721 ? 54  THR   A HG22   1 
ATOM   515  H HG23   . THR   A 1 53  ? 4.52737   -39.66415 -9.62534  1.000 179.27721 ? 54  THR   A HG23   1 
ATOM   516  N N      . VAL   A 1 54  ? 5.17281   -39.11870 -7.12442  1.000 134.36754 ? 55  VAL   A N      1 
ATOM   517  C CA     . VAL   A 1 54  ? 6.36052   -39.59550 -6.42726  1.000 134.75693 ? 55  VAL   A CA     1 
ATOM   518  C C      . VAL   A 1 54  ? 7.00667   -40.68432 -7.27345  1.000 130.59407 ? 55  VAL   A C      1 
ATOM   519  O O      . VAL   A 1 54  ? 6.32541   -41.61231 -7.72461  1.000 131.40054 ? 55  VAL   A O      1 
ATOM   520  C CB     . VAL   A 1 54  ? 6.02008   -40.12767 -5.02193  1.000 139.98719 ? 55  VAL   A CB     1 
ATOM   521  C CG1    . VAL   A 1 54  ? 7.28450   -40.57863 -4.29878  1.000 144.23062 ? 55  VAL   A CG1    1 
ATOM   522  C CG2    . VAL   A 1 54  ? 5.28550   -39.06918 -4.21244  1.000 134.37676 ? 55  VAL   A CG2    1 
ATOM   523  H H      . VAL   A 1 54  ? 4.56158   -39.71820 -7.20558  1.000 161.63152 ? 55  VAL   A H      1 
ATOM   524  H HA     . VAL   A 1 54  ? 6.99133   -38.86465 -6.33323  1.000 162.09879 ? 55  VAL   A HA     1 
ATOM   525  H HB     . VAL   A 1 54  ? 5.43524   -40.89623 -5.11233  1.000 168.37509 ? 55  VAL   A HB     1 
ATOM   526  H HG11   . VAL   A 1 54  ? 7.06380   -40.78838 -3.37780  1.000 173.46721 ? 55  VAL   A HG11   1 
ATOM   527  H HG12   . VAL   A 1 54  ? 7.63791   -41.36588 -4.74176  1.000 173.46721 ? 55  VAL   A HG12   1 
ATOM   528  H HG13   . VAL   A 1 54  ? 7.93739   -39.86183 -4.32746  1.000 173.46721 ? 55  VAL   A HG13   1 
ATOM   529  H HG21   . VAL   A 1 54  ? 5.12561   -39.40988 -3.31843  1.000 161.64258 ? 55  VAL   A HG21   1 
ATOM   530  H HG22   . VAL   A 1 54  ? 5.83232   -38.26920 -4.16867  1.000 161.64258 ? 55  VAL   A HG22   1 
ATOM   531  H HG23   . VAL   A 1 54  ? 4.44121   -38.86941 -4.64621  1.000 161.64258 ? 55  VAL   A HG23   1 
ATOM   532  N N      . TYR   A 1 55  ? 8.31526   -40.56776 -7.48667  1.000 127.67209 ? 56  TYR   A N      1 
ATOM   533  C CA     . TYR   A 1 55  ? 9.09125   -41.55401 -8.22971  1.000 127.89304 ? 56  TYR   A CA     1 
ATOM   534  C C      . TYR   A 1 55  ? 10.03661  -42.26309 -7.26745  1.000 122.78183 ? 56  TYR   A C      1 
ATOM   535  O O      . TYR   A 1 55  ? 10.86763  -41.61821 -6.61946  1.000 123.90532 ? 56  TYR   A O      1 
ATOM   536  C CB     . TYR   A 1 55  ? 9.87361   -40.89739 -9.36783  1.000 144.77573 ? 56  TYR   A CB     1 
ATOM   537  C CG     . TYR   A 1 55  ? 9.00234   -40.26665 -10.43314 1.000 158.32482 ? 56  TYR   A CG     1 
ATOM   538  C CD1    . TYR   A 1 55  ? 8.26077   -41.05197 -11.30677 1.000 157.12737 ? 56  TYR   A CD1    1 
ATOM   539  C CD2    . TYR   A 1 55  ? 8.93029   -38.88624 -10.57264 1.000 158.81414 ? 56  TYR   A CD2    1 
ATOM   540  C CE1    . TYR   A 1 55  ? 7.46532   -40.48048 -12.28418 1.000 158.84350 ? 56  TYR   A CE1    1 
ATOM   541  C CE2    . TYR   A 1 55  ? 8.13751   -38.30498 -11.54798 1.000 167.50440 ? 56  TYR   A CE2    1 
ATOM   542  C CZ     . TYR   A 1 55  ? 7.40655   -39.10753 -12.39990 1.000 170.01151 ? 56  TYR   A CZ     1 
ATOM   543  O OH     . TYR   A 1 55  ? 6.61567   -38.53948 -13.37293 1.000 153.67691 ? 56  TYR   A OH     1 
ATOM   544  H H      . TYR   A 1 55  ? 8.78709   -39.90739 -7.20228  1.000 153.59697 ? 56  TYR   A H      1 
ATOM   545  H HA     . TYR   A 1 55  ? 8.49136   -42.21244 -8.61377  1.000 153.86211 ? 56  TYR   A HA     1 
ATOM   546  H HB2    . TYR   A 1 55  ? 10.43602  -40.19994 -8.99613  1.000 174.12135 ? 56  TYR   A HB2    1 
ATOM   547  H HB3    . TYR   A 1 55  ? 10.42222  -41.57226 -9.79735  1.000 174.12135 ? 56  TYR   A HB3    1 
ATOM   548  H HD1    . TYR   A 1 55  ? 8.29963   -41.97825 -11.23340 1.000 188.94332 ? 56  TYR   A HD1    1 
ATOM   549  H HD2    . TYR   A 1 55  ? 9.42317   -38.34299 -10.00093 1.000 190.96744 ? 56  TYR   A HD2    1 
ATOM   550  H HE1    . TYR   A 1 55  ? 6.97282   -41.01953 -12.86017 1.000 191.00267 ? 56  TYR   A HE1    1 
ATOM   551  H HE2    . TYR   A 1 55  ? 8.09797   -37.37930 -11.62835 1.000 201.39575 ? 56  TYR   A HE2    1 
ATOM   552  H HH     . TYR   A 1 55  ? 5.99920   -38.09299 -13.01766 1.000 184.80276 ? 56  TYR   A HH     1 
ATOM   553  N N      . GLU   A 1 56  ? 9.91359   -43.58592 -7.18600  1.000 126.17360 ? 57  GLU   A N      1 
ATOM   554  C CA     . GLU   A 1 56  ? 10.66172  -44.40337 -6.24107  1.000 119.27760 ? 57  GLU   A CA     1 
ATOM   555  C C      . GLU   A 1 56  ? 11.32569  -45.55172 -6.98283  1.000 124.30876 ? 57  GLU   A C      1 
ATOM   556  O O      . GLU   A 1 56  ? 10.69446  -46.20924 -7.81466  1.000 141.61697 ? 57  GLU   A O      1 
ATOM   557  C CB     . GLU   A 1 56  ? 9.73188   -44.94058 -5.14320  1.000 127.36582 ? 57  GLU   A CB     1 
ATOM   558  C CG     . GLU   A 1 56  ? 10.32591  -46.03015 -4.25876  1.000 137.27882 ? 57  GLU   A CG     1 
ATOM   559  C CD     . GLU   A 1 56  ? 11.51736  -45.55380 -3.45384  1.000 136.22389 ? 57  GLU   A CD     1 
ATOM   560  O OE1    . GLU   A 1 56  ? 11.77653  -44.33454 -3.44747  1.000 133.33404 ? 57  GLU   A OE1    1 
ATOM   561  O OE2    . GLU   A 1 56  ? 12.19094  -46.39735 -2.82425  1.000 135.99474 ? 57  GLU   A OE2    1 
ATOM   562  H H      . GLU   A 1 56  ? 9.38504   -44.04551 -7.68502  1.000 151.79880 ? 57  GLU   A H      1 
ATOM   563  H HA     . GLU   A 1 56  ? 11.36184  -43.87947 -5.82124  1.000 143.52359 ? 57  GLU   A HA     1 
ATOM   564  H HB2    . GLU   A 1 56  ? 9.48358   -44.20233 -4.56507  1.000 153.22945 ? 57  GLU   A HB2    1 
ATOM   565  H HB3    . GLU   A 1 56  ? 8.94154   -45.31078 -5.56654  1.000 153.22945 ? 57  GLU   A HB3    1 
ATOM   566  H HG2    . GLU   A 1 56  ? 9.64753   -46.33584 -3.63646  1.000 165.12505 ? 57  GLU   A HG2    1 
ATOM   567  H HG3    . GLU   A 1 56  ? 10.61832  -46.76625 -4.81872  1.000 165.12505 ? 57  GLU   A HG3    1 
ATOM   568  N N      . ARG   A 1 57  ? 12.59928  -45.80109 -6.66974  1.000 112.83319 ? 58  ARG   A N      1 
ATOM   569  C CA     . ARG   A 1 57  ? 13.33787  -46.82876 -7.39405  1.000 120.48470 ? 58  ARG   A CA     1 
ATOM   570  C C      . ARG   A 1 57  ? 12.99222  -48.23359 -6.91601  1.000 122.35140 ? 58  ARG   A C      1 
ATOM   571  O O      . ARG   A 1 57  ? 13.11030  -49.18891 -7.69125  1.000 117.29311 ? 58  ARG   A O      1 
ATOM   572  C CB     . ARG   A 1 57  ? 14.84353  -46.58825 -7.27022  1.000 128.54355 ? 58  ARG   A CB     1 
ATOM   573  C CG     . ARG   A 1 57  ? 15.47614  -47.10457 -5.98788  1.000 135.25339 ? 58  ARG   A CG     1 
ATOM   574  C CD     . ARG   A 1 57  ? 16.96279  -46.78002 -5.95815  1.000 149.92395 ? 58  ARG   A CD     1 
ATOM   575  N NE     . ARG   A 1 57  ? 17.47969  -46.67283 -4.59935  1.000 149.66992 ? 58  ARG   A NE     1 
ATOM   576  C CZ     . ARG   A 1 57  ? 18.73399  -46.36594 -4.29799  1.000 151.38005 ? 58  ARG   A CZ     1 
ATOM   577  N NH1    . ARG   A 1 57  ? 19.63581  -46.13911 -5.23971  1.000 154.60381 ? 58  ARG   A NH1    1 
ATOM   578  N NH2    . ARG   A 1 57  ? 19.09246  -46.28435 -3.01972  1.000 154.13820 ? 58  ARG   A NH2    1 
ATOM   579  H H      . ARG   A 1 57  ? 13.04609  -45.39723 -6.05585  1.000 135.79030 ? 58  ARG   A H      1 
ATOM   580  H HA     . ARG   A 1 57  ? 13.10354  -46.76868 -8.33340  1.000 144.97211 ? 58  ARG   A HA     1 
ATOM   581  H HB2    . ARG   A 1 57  ? 15.28655  -47.03067 -8.01110  1.000 154.64273 ? 58  ARG   A HB2    1 
ATOM   582  H HB3    . ARG   A 1 57  ? 15.00556  -45.63269 -7.30960  1.000 154.64273 ? 58  ARG   A HB3    1 
ATOM   583  H HG2    . ARG   A 1 57  ? 15.05252  -46.68304 -5.22384  1.000 162.69454 ? 58  ARG   A HG2    1 
ATOM   584  H HG3    . ARG   A 1 57  ? 15.36899  -48.06731 -5.93732  1.000 162.69454 ? 58  ARG   A HG3    1 
ATOM   585  H HD2    . ARG   A 1 57  ? 17.45111  -47.48479 -6.41174  1.000 180.29921 ? 58  ARG   A HD2    1 
ATOM   586  H HD3    . ARG   A 1 57  ? 17.11205  -45.93224 -6.40524  1.000 180.29921 ? 58  ARG   A HD3    1 
ATOM   587  H HE     . ARG   A 1 57  ? 16.93492  -46.81829 -3.95000  1.000 179.99437 ? 58  ARG   A HE     1 
ATOM   588  H HH11   . ARG   A 1 57  ? 19.41355  -46.18936 -6.06898  1.000 185.91504 ? 58  ARG   A HH11   1 
ATOM   589  H HH12   . ARG   A 1 57  ? 20.44409  -45.94148 -5.02239  1.000 185.91504 ? 58  ARG   A HH12   1 
ATOM   590  H HH21   . ARG   A 1 57  ? 18.51352  -46.42988 -2.40065  1.000 185.35631 ? 58  ARG   A HH21   1 
ATOM   591  H HH22   . ARG   A 1 57  ? 19.90317  -46.08606 -2.81230  1.000 185.35631 ? 58  ARG   A HH22   1 
ATOM   592  N N      . ASP   A 1 58  ? 12.57624  -48.38672 -5.65972  1.000 140.73340 ? 59  ASP   A N      1 
ATOM   593  C CA     . ASP   A 1 58  ? 12.17020  -49.69775 -5.16996  1.000 143.11122 ? 59  ASP   A CA     1 
ATOM   594  C C      . ASP   A 1 58  ? 11.11412  -50.29214 -6.09158  1.000 132.00946 ? 59  ASP   A C      1 
ATOM   595  O O      . ASP   A 1 58  ? 10.18847  -49.60376 -6.52905  1.000 130.69202 ? 59  ASP   A O      1 
ATOM   596  C CB     . ASP   A 1 58  ? 11.63108  -49.59637 -3.74316  1.000 141.68210 ? 59  ASP   A CB     1 
ATOM   597  C CG     . ASP   A 1 58  ? 12.71236  -49.26694 -2.73539  1.000 135.18073 ? 59  ASP   A CG     1 
ATOM   598  O OD1    . ASP   A 1 58  ? 13.90241  -49.49054 -3.04402  1.000 140.06972 ? 59  ASP   A OD1    1 
ATOM   599  O OD2    . ASP   A 1 58  ? 12.37055  -48.78802 -1.63349  1.000 141.22625 ? 59  ASP   A OD2    1 
ATOM   600  H H      . ASP   A 1 58  ? 12.52118  -47.75428 -5.07956  1.000 169.27055 ? 59  ASP   A H      1 
ATOM   601  H HA     . ASP   A 1 58  ? 12.93915  -50.28875 -5.15145  1.000 172.12393 ? 59  ASP   A HA     1 
ATOM   602  H HB2    . ASP   A 1 58  ? 10.96194  -48.89508 -3.70638  1.000 170.40899 ? 59  ASP   A HB2    1 
ATOM   603  H HB3    . ASP   A 1 58  ? 11.23542  -50.44590 -3.49285  1.000 170.40899 ? 59  ASP   A HB3    1 
ATOM   604  N N      . LYS   A 1 59  ? 11.25425  -51.58628 -6.37895  1.000 136.42244 ? 60  LYS   A N      1 
ATOM   605  C CA     . LYS   A 1 59  ? 10.46721  -52.18125 -7.45274  1.000 141.78895 ? 60  LYS   A CA     1 
ATOM   606  C C      . LYS   A 1 59  ? 8.98476   -52.24147 -7.09940  1.000 141.83649 ? 60  LYS   A C      1 
ATOM   607  O O      . LYS   A 1 59  ? 8.13088   -52.02855 -7.96770  1.000 158.91674 ? 60  LYS   A O      1 
ATOM   608  C CB     . LYS   A 1 59  ? 11.00587  -53.57137 -7.78825  1.000 150.55886 ? 60  LYS   A CB     1 
ATOM   609  C CG     . LYS   A 1 59  ? 10.47704  -54.11835 -9.10591  1.000 176.41221 ? 60  LYS   A CG     1 
ATOM   610  C CD     . LYS   A 1 59  ? 11.33142  -55.25681 -9.63896  1.000 178.00207 ? 60  LYS   A CD     1 
ATOM   611  C CE     . LYS   A 1 59  ? 10.80022  -55.75878 -10.97451 1.000 160.14217 ? 60  LYS   A CE     1 
ATOM   612  N NZ     . LYS   A 1 59  ? 11.65128  -56.83459 -11.55762 1.000 181.60300 ? 60  LYS   A NZ     1 
ATOM   613  H H      . LYS   A 1 59  ? 11.78635  -52.12844 -5.97579  1.000 164.09740 ? 60  LYS   A H      1 
ATOM   614  H HA     . LYS   A 1 59  ? 10.55503  -51.62752 -8.24430  1.000 170.53721 ? 60  LYS   A HA     1 
ATOM   615  H HB2    . LYS   A 1 59  ? 11.97284  -53.52659 -7.85044  1.000 181.06111 ? 60  LYS   A HB2    1 
ATOM   616  H HB3    . LYS   A 1 59  ? 10.74683  -54.18655 -7.08443  1.000 181.06111 ? 60  LYS   A HB3    1 
ATOM   617  H HG2    . LYS   A 1 59  ? 9.57635   -54.45319 -8.97343  1.000 212.08512 ? 60  LYS   A HG2    1 
ATOM   618  H HG3    . LYS   A 1 59  ? 10.47321  -53.40855 -9.76702  1.000 212.08512 ? 60  LYS   A HG3    1 
ATOM   619  H HD2    . LYS   A 1 59  ? 12.24095  -54.94532 -9.76791  1.000 213.99296 ? 60  LYS   A HD2    1 
ATOM   620  H HD3    . LYS   A 1 59  ? 11.31927  -55.99305 -9.00753  1.000 213.99296 ? 60  LYS   A HD3    1 
ATOM   621  H HE2    . LYS   A 1 59  ? 9.90782   -56.11688 -10.84687 1.000 192.56107 ? 60  LYS   A HE2    1 
ATOM   622  H HE3    . LYS   A 1 59  ? 10.77475  -55.02090 -11.60362 1.000 192.56107 ? 60  LYS   A HE3    1 
ATOM   623  H HZ1    . LYS   A 1 59  ? 11.26921  -57.16026 -12.29251 1.000 218.31407 ? 60  LYS   A HZ1    1 
ATOM   624  H HZ2    . LYS   A 1 59  ? 12.45204  -56.50847 -11.76866 1.000 218.31407 ? 60  LYS   A HZ2    1 
ATOM   625  H HZ3    . LYS   A 1 59  ? 11.75401  -57.49414 -10.96894 1.000 218.31407 ? 60  LYS   A HZ3    1 
ATOM   626  N N      . ASP   A 1 60  ? 8.65223   -52.52521 -5.84158  1.000 123.81615 ? 61  ASP   A N      1 
ATOM   627  C CA     . ASP   A 1 60  ? 7.25692   -52.54719 -5.42420  1.000 128.81745 ? 61  ASP   A CA     1 
ATOM   628  C C      . ASP   A 1 60  ? 7.15848   -52.11580 -3.96803  1.000 141.96221 ? 61  ASP   A C      1 
ATOM   629  O O      . ASP   A 1 60  ? 8.15551   -52.05636 -3.24366  1.000 149.62651 ? 61  ASP   A O      1 
ATOM   630  C CB     . ASP   A 1 60  ? 6.62597   -53.93252 -5.62410  1.000 124.69174 ? 61  ASP   A CB     1 
ATOM   631  C CG     . ASP   A 1 60  ? 7.40845   -55.03730 -4.94214  1.000 124.47492 ? 61  ASP   A CG     1 
ATOM   632  O OD1    . ASP   A 1 60  ? 7.70923   -54.90180 -3.73794  1.000 151.07270 ? 61  ASP   A OD1    1 
ATOM   633  O OD2    . ASP   A 1 60  ? 7.71239   -56.04899 -5.60817  1.000 120.24189 ? 61  ASP   A OD2    1 
ATOM   634  H H      . ASP   A 1 60  ? 9.21454   -52.70701 -5.21680  1.000 148.96985 ? 61  ASP   A H      1 
ATOM   635  H HA     . ASP   A 1 60  ? 6.76499   -51.90699 -5.96183  1.000 154.97141 ? 61  ASP   A HA     1 
ATOM   636  H HB2    . ASP   A 1 60  ? 5.72927   -53.92779 -5.25421  1.000 150.02056 ? 61  ASP   A HB2    1 
ATOM   637  H HB3    . ASP   A 1 60  ? 6.59236   -54.13058 -6.57306  1.000 150.02056 ? 61  ASP   A HB3    1 
ATOM   638  N N      . ARG   A 1 61  ? 5.92732   -51.81743 -3.54397  1.000 143.64357 ? 62  ARG   A N      1 
ATOM   639  C CA     . ARG   A 1 61  ? 5.69663   -51.34266 -2.18559  1.000 131.87273 ? 62  ARG   A CA     1 
ATOM   640  C C      . ARG   A 1 61  ? 6.02618   -52.39710 -1.13987  1.000 119.44389 ? 62  ARG   A C      1 
ATOM   641  O O      . ARG   A 1 61  ? 6.23322   -52.04918 0.02710   1.000 151.50982 ? 62  ARG   A O      1 
ATOM   642  C CB     . ARG   A 1 61  ? 4.24354   -50.89419 -2.02825  1.000 137.18816 ? 62  ARG   A CB     1 
ATOM   643  C CG     . ARG   A 1 61  ? 3.22654   -52.01070 -2.19149  1.000 148.23712 ? 62  ARG   A CG     1 
ATOM   644  C CD     . ARG   A 1 61  ? 1.84359   -51.44637 -2.47936  1.000 158.17597 ? 62  ARG   A CD     1 
ATOM   645  N NE     . ARG   A 1 61  ? 1.22739   -50.86500 -1.29247  1.000 171.62910 ? 62  ARG   A NE     1 
ATOM   646  C CZ     . ARG   A 1 61  ? 0.34105   -49.87752 -1.30906  1.000 169.06808 ? 62  ARG   A CZ     1 
ATOM   647  N NH1    . ARG   A 1 61  ? -0.01995  -49.28875 -2.43840  1.000 166.10210 ? 62  ARG   A NH1    1 
ATOM   648  N NH2    . ARG   A 1 61  ? -0.19143  -49.46535 -0.16206  1.000 162.91203 ? 62  ARG   A NH2    1 
ATOM   649  H H      . ARG   A 1 61  ? 5.21570   -51.88198 -4.02255  1.000 172.76275 ? 62  ARG   A H      1 
ATOM   650  H HA     . ARG   A 1 61  ? 6.26803   -50.57554 -2.02459  1.000 158.63775 ? 62  ARG   A HA     1 
ATOM   651  H HB2    . ARG   A 1 61  ? 4.12904   -50.51918 -1.14103  1.000 165.01627 ? 62  ARG   A HB2    1 
ATOM   652  H HB3    . ARG   A 1 61  ? 4.05218   -50.22122 -2.70011  1.000 165.01627 ? 62  ARG   A HB3    1 
ATOM   653  H HG2    . ARG   A 1 61  ? 3.48680   -52.57978 -2.93265  1.000 178.27502 ? 62  ARG   A HG2    1 
ATOM   654  H HG3    . ARG   A 1 61  ? 3.18242   -52.53046 -1.37369  1.000 178.27502 ? 62  ARG   A HG3    1 
ATOM   655  H HD2    . ARG   A 1 61  ? 1.91693   -50.75188 -3.15256  1.000 190.20164 ? 62  ARG   A HD2    1 
ATOM   656  H HD3    . ARG   A 1 61  ? 1.26910   -52.15938 -2.79948  1.000 190.20164 ? 62  ARG   A HD3    1 
ATOM   657  H HE     . ARG   A 1 61  ? 1.45459   -51.18489 -0.52719  1.000 206.34539 ? 62  ARG   A HE     1 
ATOM   658  H HH11   . ARG   A 1 61  ? 0.32186   -49.54442 -3.18499  1.000 199.71300 ? 62  ARG   A HH11   1 
ATOM   659  H HH12   . ARG   A 1 61  ? -0.59630  -48.65058 -2.42549  1.000 199.71300 ? 62  ARG   A HH12   1 
ATOM   660  H HH21   . ARG   A 1 61  ? 0.03971   -49.83796 0.57776   1.000 195.88491 ? 62  ARG   A HH21   1 
ATOM   661  H HH22   . ARG   A 1 61  ? -0.76686  -48.82623 -0.16024  1.000 195.88491 ? 62  ARG   A HH22   1 
ATOM   662  N N      . ASP   A 1 62  ? 6.08291   -53.66791 -1.52363  1.000 118.34286 ? 63  ASP   A N      1 
ATOM   663  C CA     . ASP   A 1 62  ? 6.43251   -54.72165 -0.58226  1.000 117.05653 ? 63  ASP   A CA     1 
ATOM   664  C C      . ASP   A 1 62  ? 7.91832   -54.75661 -0.25958  1.000 112.76653 ? 63  ASP   A C      1 
ATOM   665  O O      . ASP   A 1 62  ? 8.33155   -55.55433 0.58820   1.000 121.28814 ? 63  ASP   A O      1 
ATOM   666  C CB     . ASP   A 1 62  ? 5.99970   -56.07856 -1.13380  1.000 124.32015 ? 63  ASP   A CB     1 
ATOM   667  C CG     . ASP   A 1 62  ? 4.53987   -56.10311 -1.52212  1.000 136.07391 ? 63  ASP   A CG     1 
ATOM   668  O OD1    . ASP   A 1 62  ? 3.75144   -55.35740 -0.90358  1.000 131.26126 ? 63  ASP   A OD1    1 
ATOM   669  O OD2    . ASP   A 1 62  ? 4.18182   -56.85957 -2.44880  1.000 150.18505 ? 63  ASP   A OD2    1 
ATOM   670  H H      . ASP   A 1 62  ? 5.92330   -53.94349 -2.32249  1.000 142.40190 ? 63  ASP   A H      1 
ATOM   671  H HA     . ASP   A 1 62  ? 5.95167   -54.56719 0.24589   1.000 140.85831 ? 63  ASP   A HA     1 
ATOM   672  H HB2    . ASP   A 1 62  ? 6.52510   -56.28260 -1.92324  1.000 149.57465 ? 63  ASP   A HB2    1 
ATOM   673  H HB3    . ASP   A 1 62  ? 6.14268   -56.75717 -0.45561  1.000 149.57465 ? 63  ASP   A HB3    1 
ATOM   674  N N      . ALA   A 1 63  ? 8.72647   -53.92935 -0.91328  1.000 109.97408 ? 64  ALA   A N      1 
ATOM   675  C CA     . ALA   A 1 63  ? 10.15091  -53.88571 -0.61688  1.000 139.29234 ? 64  ALA   A CA     1 
ATOM   676  C C      . ALA   A 1 63  ? 10.37055  -53.50174 0.84024   1.000 139.37634 ? 64  ALA   A C      1 
ATOM   677  O O      . ALA   A 1 63  ? 9.88819   -52.45950 1.29686   1.000 126.05025 ? 64  ALA   A O      1 
ATOM   678  C CB     . ALA   A 1 63  ? 10.84559  -52.89188 -1.54532  1.000 152.86596 ? 64  ALA   A CB     1 
ATOM   679  H H      . ALA   A 1 63  ? 8.47512   -53.38559 -1.53034  1.000 130.01654 ? 64  ALA   A H      1 
ATOM   680  H HA     . ALA   A 1 63  ? 10.53978  -54.76176 -0.76591  1.000 167.54128 ? 64  ALA   A HA     1 
ATOM   681  H HB1    . ALA   A 1 63  ? 11.79394  -52.87946 -1.34189  1.000 183.82962 ? 64  ALA   A HB1    1 
ATOM   682  H HB2    . ALA   A 1 63  ? 10.70808  -53.16927 -2.46459  1.000 183.82962 ? 64  ALA   A HB2    1 
ATOM   683  H HB3    . ALA   A 1 63  ? 10.46571  -52.01039 -1.40545  1.000 183.82962 ? 64  ALA   A HB3    1 
ATOM   684  N N      . ARG   A 1 64  ? 11.09569  -54.34460 1.57187   1.000 127.21149 ? 65  ARG   A N      1 
ATOM   685  C CA     . ARG   A 1 64  ? 11.37075  -54.08090 2.97619   1.000 123.33760 ? 65  ARG   A CA     1 
ATOM   686  C C      . ARG   A 1 64  ? 12.42872  -52.99333 3.11974   1.000 119.67864 ? 65  ARG   A C      1 
ATOM   687  O O      . ARG   A 1 64  ? 13.41150  -52.95892 2.37295   1.000 114.52472 ? 65  ARG   A O      1 
ATOM   688  C CB     . ARG   A 1 64  ? 11.83738  -55.35372 3.68319   1.000 131.12312 ? 65  ARG   A CB     1 
ATOM   689  C CG     . ARG   A 1 64  ? 10.77851  -56.44018 3.79054   1.000 143.38449 ? 65  ARG   A CG     1 
ATOM   690  C CD     . ARG   A 1 64  ? 11.31145  -57.65291 4.53970   1.000 171.31981 ? 65  ARG   A CD     1 
ATOM   691  N NE     . ARG   A 1 64  ? 10.36469  -58.76213 4.54209   1.000 192.43446 ? 65  ARG   A NE     1 
ATOM   692  C CZ     . ARG   A 1 64  ? 10.59869  -59.94719 5.09045   1.000 206.54034 ? 65  ARG   A CZ     1 
ATOM   693  N NH1    . ARG   A 1 64  ? 11.74370  -60.21475 5.69780   1.000 199.85064 ? 65  ARG   A NH1    1 
ATOM   694  N NH2    . ARG   A 1 64  ? 9.66062   -60.88808 5.02682   1.000 207.55826 ? 65  ARG   A NH2    1 
ATOM   695  H H      . ARG   A 1 64  ? 11.43870  -55.07564 1.27605   1.000 153.04426 ? 65  ARG   A H      1 
ATOM   696  H HA     . ARG   A 1 64  ? 10.55691  -53.77614 3.40710   1.000 148.39559 ? 65  ARG   A HA     1 
ATOM   697  H HB2    . ARG   A 1 64  ? 12.58727  -55.72313 3.19116   1.000 157.73822 ? 65  ARG   A HB2    1 
ATOM   698  H HB3    . ARG   A 1 64  ? 12.11297  -55.12324 4.58420   1.000 157.73822 ? 65  ARG   A HB3    1 
ATOM   699  H HG2    . ARG   A 1 64  ? 10.01023  -56.09567 4.27216   1.000 172.45186 ? 65  ARG   A HG2    1 
ATOM   700  H HG3    . ARG   A 1 64  ? 10.51347  -56.72162 2.90090   1.000 172.45186 ? 65  ARG   A HG3    1 
ATOM   701  H HD2    . ARG   A 1 64  ? 12.12922  -57.95523 4.11456   1.000 205.97424 ? 65  ARG   A HD2    1 
ATOM   702  H HD3    . ARG   A 1 64  ? 11.48831  -57.40528 5.46074   1.000 205.97424 ? 65  ARG   A HD3    1 
ATOM   703  H HE     . ARG   A 1 64  ? 9.60292   -58.63968 4.16220   1.000 231.31183 ? 65  ARG   A HE     1 
ATOM   704  H HH11   . ARG   A 1 64  ? 12.35689  -59.61351 5.74363   1.000 240.21124 ? 65  ARG   A HH11   1 
ATOM   705  H HH12   . ARG   A 1 64  ? 11.87455  -60.98986 6.04663   1.000 240.21124 ? 65  ARG   A HH12   1 
ATOM   706  H HH21   . ARG   A 1 64  ? 8.91344   -60.72445 4.63370   1.000 249.46038 ? 65  ARG   A HH21   1 
ATOM   707  H HH22   . ARG   A 1 64  ? 9.80130   -61.66004 5.37881   1.000 249.46038 ? 65  ARG   A HH22   1 
ATOM   708  N N      . ILE   A 1 65  ? 12.22232  -52.10617 4.08916   1.000 123.64541 ? 66  ILE   A N      1 
ATOM   709  C CA     . ILE   A 1 65  ? 13.16285  -51.03520 4.39720   1.000 104.70771 ? 66  ILE   A CA     1 
ATOM   710  C C      . ILE   A 1 65  ? 14.04729  -51.50091 5.54328   1.000 103.33640 ? 66  ILE   A C      1 
ATOM   711  O O      . ILE   A 1 65  ? 13.56765  -51.70151 6.66640   1.000 122.58233 ? 66  ILE   A O      1 
ATOM   712  C CB     . ILE   A 1 65  ? 12.43683  -49.73298 4.76791   1.000 99.97313  ? 66  ILE   A CB     1 
ATOM   713  C CG1    . ILE   A 1 65  ? 11.41863  -49.35833 3.69123   1.000 111.73250 ? 66  ILE   A CG1    1 
ATOM   714  C CG2    . ILE   A 1 65  ? 13.43955  -48.60287 4.95550   1.000 118.49728 ? 66  ILE   A CG2    1 
ATOM   715  C CD1    . ILE   A 1 65  ? 10.63283  -48.09477 4.00306   1.000 107.82244 ? 66  ILE   A CD1    1 
ATOM   716  H H      . ILE   A 1 65  ? 11.52645  -52.10506 4.59450   1.000 148.76497 ? 66  ILE   A H      1 
ATOM   717  H HA     . ILE   A 1 65  ? 13.71819  -50.86732 3.61982   1.000 126.03972 ? 66  ILE   A HA     1 
ATOM   718  H HB     . ILE   A 1 65  ? 11.96472  -49.87800 5.60277   1.000 120.20542 ? 66  ILE   A HB     1 
ATOM   719  H HG12   . ILE   A 1 65  ? 11.88800  -49.21589 2.85439   1.000 134.46947 ? 66  ILE   A HG12   1 
ATOM   720  H HG13   . ILE   A 1 65  ? 10.78384  -50.08557 3.59596   1.000 134.46947 ? 66  ILE   A HG13   1 
ATOM   721  H HG21   . ILE   A 1 65  ? 12.97495  -47.82129 5.29340   1.000 142.58721 ? 66  ILE   A HG21   1 
ATOM   722  H HG22   . ILE   A 1 65  ? 14.11767  -48.88434 5.58940   1.000 142.58721 ? 66  ILE   A HG22   1 
ATOM   723  H HG23   . ILE   A 1 65  ? 13.85003  -48.39972 4.10044   1.000 142.58721 ? 66  ILE   A HG23   1 
ATOM   724  H HD11   . ILE   A 1 65  ? 9.92952   -47.98939 3.34340   1.000 129.77740 ? 66  ILE   A HD11   1 
ATOM   725  H HD12   . ILE   A 1 65  ? 10.24611  -48.17396 4.88911   1.000 129.77740 ? 66  ILE   A HD12   1 
ATOM   726  H HD13   . ILE   A 1 65  ? 11.23317  -47.33354 3.97100   1.000 129.77740 ? 66  ILE   A HD13   1 
ATOM   727  N N      . PHE   A 1 66  ? 15.33664  -51.65559 5.26915   1.000 99.87148  ? 67  PHE   A N      1 
ATOM   728  C CA     . PHE   A 1 66  ? 16.27565  -52.03885 6.30776   1.000 99.13498  ? 67  PHE   A CA     1 
ATOM   729  C C      . PHE   A 1 66  ? 16.61170  -50.83868 7.18307   1.000 107.37670 ? 67  PHE   A C      1 
ATOM   730  O O      . PHE   A 1 66  ? 16.64310  -49.69315 6.72498   1.000 97.21649  ? 67  PHE   A O      1 
ATOM   731  C CB     . PHE   A 1 66  ? 17.55348  -52.61475 5.70322   1.000 98.91678  ? 67  PHE   A CB     1 
ATOM   732  C CG     . PHE   A 1 66  ? 18.62787  -52.89319 6.71663   1.000 119.50760 ? 67  PHE   A CG     1 
ATOM   733  C CD1    . PHE   A 1 66  ? 18.58864  -54.04032 7.49051   1.000 121.83212 ? 67  PHE   A CD1    1 
ATOM   734  C CD2    . PHE   A 1 66  ? 19.67851  -52.00757 6.89390   1.000 111.30452 ? 67  PHE   A CD2    1 
ATOM   735  C CE1    . PHE   A 1 66  ? 19.57811  -54.30012 8.42271   1.000 111.78440 ? 67  PHE   A CE1    1 
ATOM   736  C CE2    . PHE   A 1 66  ? 20.67145  -52.26185 7.82327   1.000 102.17065 ? 67  PHE   A CE2    1 
ATOM   737  C CZ     . PHE   A 1 66  ? 20.62104  -53.40905 8.58821   1.000 108.99938 ? 67  PHE   A CZ     1 
ATOM   738  H H      . PHE   A 1 66  ? 15.68888  -51.54448 4.49250   1.000 117.89343 ? 67  PHE   A H      1 
ATOM   739  H HA     . PHE   A 1 66  ? 15.87718  -52.72636 6.86405   1.000 117.00962 ? 67  PHE   A HA     1 
ATOM   740  H HB2    . PHE   A 1 66  ? 17.34006  -53.45080 5.26009   1.000 116.91821 ? 67  PHE   A HB2    1 
ATOM   741  H HB3    . PHE   A 1 66  ? 17.90873  -51.98026 5.06125   1.000 116.91821 ? 67  PHE   A HB3    1 
ATOM   742  H HD1    . PHE   A 1 66  ? 17.88909  -54.64358 7.38275   1.000 146.58902 ? 67  PHE   A HD1    1 
ATOM   743  H HD2    . PHE   A 1 66  ? 19.71681  -51.23230 6.38167   1.000 133.95590 ? 67  PHE   A HD2    1 
ATOM   744  H HE1    . PHE   A 1 66  ? 19.54104  -55.07388 8.93731   1.000 134.53176 ? 67  PHE   A HE1    1 
ATOM   745  H HE2    . PHE   A 1 66  ? 21.37214  -51.66013 7.93225   1.000 122.99525 ? 67  PHE   A HE2    1 
ATOM   746  H HZ     . PHE   A 1 66  ? 21.28730  -53.58207 9.21357   1.000 131.18972 ? 67  PHE   A HZ     1 
ATOM   747  N N      . GLY   A 1 67  ? 16.85274  -51.11120 8.45737   1.000 122.28161 ? 68  GLY   A N      1 
ATOM   748  C CA     . GLY   A 1 67  ? 17.23879  -50.09138 9.40650   1.000 132.48231 ? 68  GLY   A CA     1 
ATOM   749  C C      . GLY   A 1 67  ? 16.44973  -50.19848 10.69480  1.000 120.11032 ? 68  GLY   A C      1 
ATOM   750  O O      . GLY   A 1 67  ? 15.52117  -50.99325 10.83258  1.000 123.47950 ? 68  GLY   A O      1 
ATOM   751  H H      . GLY   A 1 67  ? 16.79680  -51.89836 8.79920   1.000 147.12840 ? 68  GLY   A H      1 
ATOM   752  H HA2    . GLY   A 1 67  ? 18.18197  -50.18225 9.61396   1.000 159.36925 ? 68  GLY   A HA2    1 
ATOM   753  H HA3    . GLY   A 1 67  ? 17.08317  -49.21481 9.02139   1.000 159.36925 ? 68  GLY   A HA3    1 
ATOM   754  N N      . GLY   A 1 68  ? 16.86119  -49.37739 11.65602  1.000 112.08505 ? 69  GLY   A N      1 
ATOM   755  C CA     . GLY   A 1 68  ? 16.21304  -49.32454 12.94606  1.000 120.41370 ? 69  GLY   A CA     1 
ATOM   756  C C      . GLY   A 1 68  ? 14.89694  -48.58035 12.88615  1.000 118.22749 ? 69  GLY   A C      1 
ATOM   757  O O      . GLY   A 1 68  ? 14.35578  -48.27572 11.82117  1.000 114.38648 ? 69  GLY   A O      1 
ATOM   758  H H      . GLY   A 1 68  ? 17.52437  -48.83554 11.57731  1.000 134.89254 ? 69  GLY   A H      1 
ATOM   759  H HA2    . GLY   A 1 68  ? 16.04248  -50.22667 13.25908  1.000 144.88692 ? 69  GLY   A HA2    1 
ATOM   760  H HA3    . GLY   A 1 68  ? 16.79249  -48.87440 13.58050  1.000 144.88692 ? 69  GLY   A HA3    1 
ATOM   761  N N      . THR   A 1 69  ? 14.37714  -48.28704 14.06784  1.000 126.76130 ? 70  THR   A N      1 
ATOM   762  C CA     . THR   A 1 69  ? 13.13007  -47.55595 14.20761  1.000 111.37568 ? 70  THR   A CA     1 
ATOM   763  C C      . THR   A 1 69  ? 13.39195  -46.05372 14.18792  1.000 102.97259 ? 70  THR   A C      1 
ATOM   764  O O      . THR   A 1 69  ? 14.51795  -45.59155 14.38274  1.000 122.36485 ? 70  THR   A O      1 
ATOM   765  C CB     . THR   A 1 69  ? 12.42612  -47.94747 15.50471  1.000 115.99624 ? 70  THR   A CB     1 
ATOM   766  O OG1    . THR   A 1 69  ? 13.30247  -47.71896 16.61597  1.000 146.29977 ? 70  THR   A OG1    1 
ATOM   767  C CG2    . THR   A 1 69  ? 12.02735  -49.40873 15.47304  1.000 112.09896 ? 70  THR   A CG2    1 
ATOM   768  H H      . THR   A 1 69  ? 14.73546  -48.50513 14.81861  1.000 152.50403 ? 70  THR   A H      1 
ATOM   769  H HA     . THR   A 1 69  ? 12.54205  -47.77256 13.46719  1.000 134.04128 ? 70  THR   A HA     1 
ATOM   770  H HB     . THR   A 1 69  ? 11.62360  -47.41301 15.61063  1.000 139.58595 ? 70  THR   A HB     1 
ATOM   771  H HG1    . THR   A 1 69  ? 12.91966  -47.93277 17.33245  1.000 175.95019 ? 70  THR   A HG1    1 
ATOM   772  H HG21   . THR   A 1 69  ? 11.55264  -49.64078 16.28649  1.000 134.90922 ? 70  THR   A HG21   1 
ATOM   773  H HG22   . THR   A 1 69  ? 11.45005  -49.57866 14.71229  1.000 134.90922 ? 70  THR   A HG22   1 
ATOM   774  H HG23   . THR   A 1 69  ? 12.81739  -49.96670 15.39954  1.000 134.90922 ? 70  THR   A HG23   1 
ATOM   775  N N      . LEU   A 1 70  ? 12.32801  -45.29132 13.94940  1.000 104.84546 ? 71  LEU   A N      1 
ATOM   776  C CA     . LEU   A 1 70  ? 12.40334  -43.84037 13.83261  1.000 120.17398 ? 71  LEU   A CA     1 
ATOM   777  C C      . LEU   A 1 70  ? 11.51779  -43.19718 14.89148  1.000 131.59506 ? 71  LEU   A C      1 
ATOM   778  O O      . LEU   A 1 70  ? 10.36349  -43.59999 15.07219  1.000 125.07362 ? 71  LEU   A O      1 
ATOM   779  C CB     . LEU   A 1 70  ? 11.98477  -43.38026 12.42998  1.000 118.84581 ? 71  LEU   A CB     1 
ATOM   780  C CG     . LEU   A 1 70  ? 12.95791  -43.68865 11.28624  1.000 111.80915 ? 71  LEU   A CG     1 
ATOM   781  C CD1    . LEU   A 1 70  ? 12.31241  -43.37734 9.94403   1.000 123.02265 ? 71  LEU   A CD1    1 
ATOM   782  C CD2    . LEU   A 1 70  ? 14.26443  -42.92081 11.43125  1.000 133.50047 ? 71  LEU   A CD2    1 
ATOM   783  H H      . LEU   A 1 70  ? 11.53204  -45.60114 13.84915  1.000 126.20502 ? 71  LEU   A H      1 
ATOM   784  H HA     . LEU   A 1 70  ? 13.31539  -43.54980 13.98959  1.000 144.59925 ? 71  LEU   A HA     1 
ATOM   785  H HB2    . LEU   A 1 70  ? 11.14359  -43.81115 12.21166  1.000 143.00545 ? 71  LEU   A HB2    1 
ATOM   786  H HB3    . LEU   A 1 70  ? 11.86833  -42.41754 12.45253  1.000 143.00545 ? 71  LEU   A HB3    1 
ATOM   787  H HG     . LEU   A 1 70  ? 13.17270  -44.63394 11.32067  1.000 134.56146 ? 71  LEU   A HG     1 
ATOM   788  H HD11   . LEU   A 1 70  ? 12.97442  -43.48346 9.24305   1.000 148.01765 ? 71  LEU   A HD11   1 
ATOM   789  H HD12   . LEU   A 1 70  ? 11.57517  -43.99064 9.79835   1.000 148.01765 ? 71  LEU   A HD12   1 
ATOM   790  H HD13   . LEU   A 1 70  ? 11.98572  -42.46407 9.95497   1.000 148.01765 ? 71  LEU   A HD13   1 
ATOM   791  H HD21   . LEU   A 1 70  ? 14.80743  -43.06944 10.64133  1.000 160.59104 ? 71  LEU   A HD21   1 
ATOM   792  H HD22   . LEU   A 1 70  ? 14.06671  -41.97569 11.52368  1.000 160.59104 ? 71  LEU   A HD22   1 
ATOM   793  H HD23   . LEU   A 1 70  ? 14.73225  -43.23947 12.21897  1.000 160.59104 ? 71  LEU   A HD23   1 
ATOM   794  N N      . ASP   A 1 71  ? 12.06450  -42.20304 15.58804  1.000 137.36332 ? 72  ASP   A N      1 
ATOM   795  C CA     . ASP   A 1 71  ? 11.36713  -41.47135 16.63762  1.000 119.34725 ? 72  ASP   A CA     1 
ATOM   796  C C      . ASP   A 1 71  ? 10.98976  -40.08661 16.13470  1.000 120.25763 ? 72  ASP   A C      1 
ATOM   797  O O      . ASP   A 1 71  ? 11.82620  -39.38298 15.55988  1.000 134.53717 ? 72  ASP   A O      1 
ATOM   798  C CB     . ASP   A 1 71  ? 12.24917  -41.35174 17.87914  1.000 153.75275 ? 72  ASP   A CB     1 
ATOM   799  C CG     . ASP   A 1 71  ? 12.33523  -42.64126 18.65164  1.000 179.34035 ? 72  ASP   A CG     1 
ATOM   800  O OD1    . ASP   A 1 71  ? 11.29990  -43.05891 19.20807  1.000 177.96043 ? 72  ASP   A OD1    1 
ATOM   801  O OD2    . ASP   A 1 71  ? 13.42986  -43.24159 18.69103  1.000 190.99854 ? 72  ASP   A OD2    1 
ATOM   802  H H      . ASP   A 1 71  ? 12.86901  -41.92542 15.46433  1.000 165.22645 ? 72  ASP   A H      1 
ATOM   803  H HA     . ASP   A 1 71  ? 10.55121  -41.94007 16.87315  1.000 143.60717 ? 72  ASP   A HA     1 
ATOM   804  H HB2    . ASP   A 1 71  ? 13.14659  -41.10305 17.60770  1.000 184.89377 ? 72  ASP   A HB2    1 
ATOM   805  H HB3    . ASP   A 1 71  ? 11.88011  -40.67335 18.46607  1.000 184.89377 ? 72  ASP   A HB3    1 
ATOM   806  N N      . LEU   A 1 72  ? 9.73851   -39.69437 16.36138  1.000 110.20118 ? 73  LEU   A N      1 
ATOM   807  C CA     . LEU   A 1 72  ? 9.22850   -38.40245 15.91985  1.000 142.82515 ? 73  LEU   A CA     1 
ATOM   808  C C      . LEU   A 1 72  ? 9.24461   -37.42736 17.09173  1.000 146.66632 ? 73  LEU   A C      1 
ATOM   809  O O      . LEU   A 1 72  ? 8.65041   -37.69994 18.14053  1.000 149.93077 ? 73  LEU   A O      1 
ATOM   810  C CB     . LEU   A 1 72  ? 7.81420   -38.53647 15.35473  1.000 147.82281 ? 73  LEU   A CB     1 
ATOM   811  C CG     . LEU   A 1 72  ? 7.63743   -39.35997 14.07657  1.000 118.33512 ? 73  LEU   A CG     1 
ATOM   812  C CD1    . LEU   A 1 72  ? 6.21513   -39.21562 13.55618  1.000 126.66874 ? 73  LEU   A CD1    1 
ATOM   813  C CD2    . LEU   A 1 72  ? 8.63183   -38.95386 13.00645  1.000 120.52451 ? 73  LEU   A CD2    1 
ATOM   814  H H      . LEU   A 1 72  ? 9.15550   -40.17022 16.77764  1.000 132.63188 ? 73  LEU   A H      1 
ATOM   815  H HA     . LEU   A 1 72  ? 9.80569   -38.05348 15.22273  1.000 171.78065 ? 73  LEU   A HA     1 
ATOM   816  H HB2    . LEU   A 1 72  ? 7.26155   -38.95222 16.03490  1.000 177.77784 ? 73  LEU   A HB2    1 
ATOM   817  H HB3    . LEU   A 1 72  ? 7.48679   -37.64418 15.16100  1.000 177.77784 ? 73  LEU   A HB3    1 
ATOM   818  H HG     . LEU   A 1 72  ? 7.80445   -40.29208 14.28673  1.000 142.39261 ? 73  LEU   A HG     1 
ATOM   819  H HD11   . LEU   A 1 72  ? 6.10010   -39.79483 12.78664  1.000 152.39295 ? 73  LEU   A HD11   1 
ATOM   820  H HD12   . LEU   A 1 72  ? 5.59498   -39.47005 14.25732  1.000 152.39295 ? 73  LEU   A HD12   1 
ATOM   821  H HD13   . LEU   A 1 72  ? 6.06459   -38.29211 13.30054  1.000 152.39295 ? 73  LEU   A HD13   1 
ATOM   822  H HD21   . LEU   A 1 72  ? 8.40340   -39.40157 12.17682  1.000 145.01989 ? 73  LEU   A HD21   1 
ATOM   823  H HD22   . LEU   A 1 72  ? 8.59064   -37.99230 12.88563  1.000 145.01989 ? 73  LEU   A HD22   1 
ATOM   824  H HD23   . LEU   A 1 72  ? 9.52281   -39.21397 13.28823  1.000 145.01989 ? 73  LEU   A HD23   1 
ATOM   825  N N      . HIS   A 1 73  ? 9.92880   -36.30041 16.91172  1.000 142.53893 ? 74  HIS   A N      1 
ATOM   826  C CA     . HIS   A 1 73  ? 9.95460   -35.24387 17.91212  1.000 142.60505 ? 74  HIS   A CA     1 
ATOM   827  C C      . HIS   A 1 73  ? 8.64230   -34.46694 17.88502  1.000 155.33507 ? 74  HIS   A C      1 
ATOM   828  O O      . HIS   A 1 73  ? 7.99352   -34.33673 16.84336  1.000 161.01250 ? 74  HIS   A O      1 
ATOM   829  C CB     . HIS   A 1 73  ? 11.14126  -34.31336 17.65924  1.000 139.96981 ? 74  HIS   A CB     1 
ATOM   830  C CG     . HIS   A 1 73  ? 11.22267  -33.15755 18.60707  1.000 190.37110 ? 74  HIS   A CG     1 
ATOM   831  N ND1    . HIS   A 1 73  ? 11.37071  -33.31654 19.96831  1.000 204.31168 ? 74  HIS   A ND1    1 
ATOM   832  C CD2    . HIS   A 1 73  ? 11.18659  -31.82196 18.38635  1.000 181.20954 ? 74  HIS   A CD2    1 
ATOM   833  C CE1    . HIS   A 1 73  ? 11.41640  -32.12914 20.54589  1.000 185.79179 ? 74  HIS   A CE1    1 
ATOM   834  N NE2    . HIS   A 1 73  ? 11.30699  -31.20540 19.60804  1.000 182.96692 ? 74  HIS   A NE2    1 
ATOM   835  H H      . HIS   A 1 73  ? 10.39162  -36.12312 16.20889  1.000 171.43718 ? 74  HIS   A H      1 
ATOM   836  H HA     . HIS   A 1 73  ? 10.05918  -35.61983 18.80016  1.000 171.51653 ? 74  HIS   A HA     1 
ATOM   837  H HB2    . HIS   A 1 73  ? 11.96107  -34.82445 17.74640  1.000 168.35425 ? 74  HIS   A HB2    1 
ATOM   838  H HB3    . HIS   A 1 73  ? 11.06839  -33.95375 16.76131  1.000 168.35425 ? 74  HIS   A HB3    1 
ATOM   839  H HD2    . HIS   A 1 73  ? 11.09705  -31.40091 17.56197  1.000 217.84192 ? 74  HIS   A HD2    1 
ATOM   840  H HE1    . HIS   A 1 73  ? 11.50971  -31.97068 21.45753  1.000 223.34062 ? 74  HIS   A HE1    1 
ATOM   841  N N      . ARG   A 1 74  ? 8.25454   -33.94574 19.05148  1.000 154.08068 ? 75  ARG   A N      1 
ATOM   842  C CA     . ARG   A 1 74  ? 6.91615   -33.38144 19.20128  1.000 148.75249 ? 75  ARG   A CA     1 
ATOM   843  C C      . ARG   A 1 74  ? 6.75680   -32.07947 18.42341  1.000 147.93413 ? 75  ARG   A C      1 
ATOM   844  O O      . ARG   A 1 74  ? 5.69401   -31.82568 17.84383  1.000 132.53899 ? 75  ARG   A O      1 
ATOM   845  C CB     . ARG   A 1 74  ? 6.61140   -33.16492 20.68400  1.000 169.16607 ? 75  ARG   A CB     1 
ATOM   846  C CG     . ARG   A 1 74  ? 6.57397   -34.45571 21.49599  1.000 185.36446 ? 75  ARG   A CG     1 
ATOM   847  C CD     . ARG   A 1 74  ? 6.29376   -34.19393 22.97028  1.000 164.63868 ? 75  ARG   A CD     1 
ATOM   848  N NE     . ARG   A 1 74  ? 5.01154   -33.53075 23.17757  1.000 168.10065 ? 75  ARG   A NE     1 
ATOM   849  C CZ     . ARG   A 1 74  ? 3.85565   -34.15829 23.35431  1.000 187.65289 ? 75  ARG   A CZ     1 
ATOM   850  N NH1    . ARG   A 1 74  ? 3.77589   -35.47971 23.35265  1.000 184.12334 ? 75  ARG   A NH1    1 
ATOM   851  N NH2    . ARG   A 1 74  ? 2.75089   -33.44098 23.53770  1.000 199.12916 ? 75  ARG   A NH2    1 
ATOM   852  H H      . ARG   A 1 74  ? 8.74064   -33.90771 19.75990  1.000 185.28728 ? 75  ARG   A H      1 
ATOM   853  H HA     . ARG   A 1 74  ? 6.27226   -34.01290 18.84413  1.000 178.89346 ? 75  ARG   A HA     1 
ATOM   854  H HB2    . ARG   A 1 74  ? 7.29847   -32.59533 21.06400  1.000 203.38976 ? 75  ARG   A HB2    1 
ATOM   855  H HB3    . ARG   A 1 74  ? 5.74417   -32.73810 20.76538  1.000 203.38976 ? 75  ARG   A HB3    1 
ATOM   856  H HG2    . ARG   A 1 74  ? 5.87188   -35.02957 21.15154  1.000 222.82782 ? 75  ARG   A HG2    1 
ATOM   857  H HG3    . ARG   A 1 74  ? 7.43207   -34.90248 21.42551  1.000 222.82782 ? 75  ARG   A HG3    1 
ATOM   858  H HD2    . ARG   A 1 74  ? 6.27742   -35.03892 23.44632  1.000 197.95688 ? 75  ARG   A HD2    1 
ATOM   859  H HD3    . ARG   A 1 74  ? 6.99074   -33.62358 23.33058  1.000 197.95688 ? 75  ARG   A HD3    1 
ATOM   860  H HE     . ARG   A 1 74  ? 5.00393   -32.67082 23.18588  1.000 202.11126 ? 75  ARG   A HE     1 
ATOM   861  H HH11   . ARG   A 1 74  ? 4.48418   -35.95310 23.23504  1.000 221.33848 ? 75  ARG   A HH11   1 
ATOM   862  H HH12   . ARG   A 1 74  ? 3.01578   -35.86476 23.46917  1.000 221.33848 ? 75  ARG   A HH12   1 
ATOM   863  H HH21   . ARG   A 1 74  ? 2.79151   -32.58195 23.54067  1.000 239.34546 ? 75  ARG   A HH21   1 
ATOM   864  H HH22   . ARG   A 1 74  ? 1.99586   -33.83616 23.65331  1.000 239.34546 ? 75  ARG   A HH22   1 
ATOM   865  N N      . ASP   A 1 75  ? 7.79035   -31.24016 18.40034  1.000 161.20708 ? 76  ASP   A N      1 
ATOM   866  C CA     . ASP   A 1 75  ? 7.70299   -29.94827 17.73012  1.000 170.34005 ? 76  ASP   A CA     1 
ATOM   867  C C      . ASP   A 1 75  ? 7.94767   -30.03151 16.22920  1.000 171.90628 ? 76  ASP   A C      1 
ATOM   868  O O      . ASP   A 1 75  ? 7.81820   -29.01149 15.54341  1.000 182.72889 ? 76  ASP   A O      1 
ATOM   869  C CB     . ASP   A 1 75  ? 8.70365   -28.96564 18.34561  1.000 173.96664 ? 76  ASP   A CB     1 
ATOM   870  C CG     . ASP   A 1 75  ? 8.35386   -28.59198 19.77067  1.000 181.34806 ? 76  ASP   A CG     1 
ATOM   871  O OD1    . ASP   A 1 75  ? 7.15150   -28.42628 20.06523  1.000 182.27257 ? 76  ASP   A OD1    1 
ATOM   872  O OD2    . ASP   A 1 75  ? 9.28257   -28.46262 20.59589  1.000 186.58130 ? 76  ASP   A OD2    1 
ATOM   873  H H      . ASP   A 1 75  ? 8.55259   -31.39745 18.76619  1.000 193.83896 ? 76  ASP   A H      1 
ATOM   874  H HA     . ASP   A 1 75  ? 6.80854   -29.59925 17.86810  1.000 204.79853 ? 76  ASP   A HA     1 
ATOM   875  H HB2    . ASP   A 1 75  ? 9.58450   -29.37182 18.34929  1.000 209.15044 ? 76  ASP   A HB2    1 
ATOM   876  H HB3    . ASP   A 1 75  ? 8.71531   -28.15286 17.81632  1.000 209.15044 ? 76  ASP   A HB3    1 
ATOM   877  N N      . SER   A 1 76  ? 8.29545   -31.20620 15.70449  1.000 166.61391 ? 77  SER   A N      1 
ATOM   878  C CA     . SER   A 1 76  ? 8.61262   -31.34451 14.28892  1.000 153.16604 ? 77  SER   A CA     1 
ATOM   879  C C      . SER   A 1 76  ? 7.88267   -32.53146 13.67338  1.000 147.82138 ? 77  SER   A C      1 
ATOM   880  O O      . SER   A 1 76  ? 6.85374   -32.35799 13.01221  1.000 155.96955 ? 77  SER   A O      1 
ATOM   881  C CB     . SER   A 1 76  ? 10.12398  -31.49717 14.09849  1.000 146.01697 ? 77  SER   A CB     1 
ATOM   882  O OG     . SER   A 1 76  ? 10.62221  -32.59347 14.84485  1.000 144.54981 ? 77  SER   A OG     1 
ATOM   883  H H      . SER   A 1 76  ? 8.35458   -31.93902 16.15068  1.000 200.32717 ? 77  SER   A H      1 
ATOM   884  H HA     . SER   A 1 76  ? 8.32215   -30.54439 13.82381  1.000 184.18972 ? 77  SER   A HA     1 
ATOM   885  H HB2    . SER   A 1 76  ? 10.30957  -31.64593 13.15811  1.000 175.61083 ? 77  SER   A HB2    1 
ATOM   886  H HB3    . SER   A 1 76  ? 10.56288  -30.68602 14.39901  1.000 175.61083 ? 77  SER   A HB3    1 
ATOM   887  H HG     . SER   A 1 76  ? 11.45740  -32.53745 14.91497  1.000 173.85024 ? 77  SER   A HG     1 
ATOM   888  N N      . GLY   A 1 77  ? 8.41031   -33.73903 13.88490  1.000 132.18189 ? 78  GLY   A N      1 
ATOM   889  C CA     . GLY   A 1 77  ? 7.82292   -34.91453 13.26054  1.000 132.89938 ? 78  GLY   A CA     1 
ATOM   890  C C      . GLY   A 1 77  ? 6.34447   -35.06330 13.55476  1.000 143.78738 ? 78  GLY   A C      1 
ATOM   891  O O      . GLY   A 1 77  ? 5.52983   -35.23698 12.64490  1.000 147.01982 ? 78  GLY   A O      1 
ATOM   892  H H      . GLY   A 1 77  ? 9.09667   -33.89883 14.37782  1.000 159.00874 ? 78  GLY   A H      1 
ATOM   893  H HA2    . GLY   A 1 77  ? 7.93630   -34.85503 12.29902  1.000 159.86972 ? 78  GLY   A HA2    1 
ATOM   894  H HA3    . GLY   A 1 77  ? 8.27779   -35.70800 13.58366  1.000 159.86972 ? 78  GLY   A HA3    1 
ATOM   895  N N      . GLN   A 1 78  ? 5.97440   -34.99781 14.83609  1.000 137.91710 ? 79  GLN   A N      1 
ATOM   896  C CA     . GLN   A 1 78  ? 4.57000   -35.15119 15.20249  1.000 149.63688 ? 79  GLN   A CA     1 
ATOM   897  C C      . GLN   A 1 78  ? 3.71770   -34.04284 14.59681  1.000 147.84708 ? 79  GLN   A C      1 
ATOM   898  O O      . GLN   A 1 78  ? 2.57914   -34.28295 14.17715  1.000 139.03533 ? 79  GLN   A O      1 
ATOM   899  C CB     . GLN   A 1 78  ? 4.41981   -35.16951 16.72379  1.000 149.97585 ? 79  GLN   A CB     1 
ATOM   900  C CG     . GLN   A 1 78  ? 5.02492   -36.39275 17.39252  1.000 141.11238 ? 79  GLN   A CG     1 
ATOM   901  C CD     . GLN   A 1 78  ? 4.61688   -36.52449 18.85011  1.000 163.85127 ? 79  GLN   A CD     1 
ATOM   902  O OE1    . GLN   A 1 78  ? 3.70387   -35.84195 19.31596  1.000 158.16201 ? 79  GLN   A OE1    1 
ATOM   903  N NE2    . GLN   A 1 78  ? 5.29260   -37.40777 19.57706  1.000 171.44100 ? 79  GLN   A NE2    1 
ATOM   904  H H      . GLN   A 1 78  ? 6.50759   -34.86796 15.49824  1.000 165.89099 ? 79  GLN   A H      1 
ATOM   905  H HA     . GLN   A 1 78  ? 4.25076   -36.00037 14.85915  1.000 179.95472 ? 79  GLN   A HA     1 
ATOM   906  H HB2    . GLN   A 1 78  ? 4.86024   -34.38607 17.08868  1.000 180.36149 ? 79  GLN   A HB2    1 
ATOM   907  H HB3    . GLN   A 1 78  ? 3.47502   -35.15110 16.94272  1.000 180.36149 ? 79  GLN   A HB3    1 
ATOM   908  H HG2    . GLN   A 1 78  ? 4.72814   -37.18877 16.92435  1.000 169.72533 ? 79  GLN   A HG2    1 
ATOM   909  H HG3    . GLN   A 1 78  ? 5.99204   -36.32757 17.35600  1.000 169.72533 ? 79  GLN   A HG3    1 
ATOM   910  H HE21   . GLN   A 1 78  ? 5.92349   -37.86819 19.21708  1.000 206.11967 ? 79  GLN   A HE21   1 
ATOM   911  H HE22   . GLN   A 1 78  ? 5.09909   -37.51908 20.40758  1.000 206.11967 ? 79  GLN   A HE22   1 
ATOM   912  N N      . GLU   A 1 79  ? 4.25036   -32.82030 14.54186  1.000 142.65616 ? 80  GLU   A N      1 
ATOM   913  C CA     . GLU   A 1 79  ? 3.49487   -31.72034 13.95293  1.000 143.49284 ? 80  GLU   A CA     1 
ATOM   914  C C      . GLU   A 1 79  ? 3.23484   -31.97002 12.47288  1.000 145.23540 ? 80  GLU   A C      1 
ATOM   915  O O      . GLU   A 1 79  ? 2.16495   -31.62803 11.95558  1.000 156.19178 ? 80  GLU   A O      1 
ATOM   916  C CB     . GLU   A 1 79  ? 4.24219   -30.40280 14.15729  1.000 153.43110 ? 80  GLU   A CB     1 
ATOM   917  C CG     . GLU   A 1 79  ? 3.49595   -29.18408 13.64026  1.000 161.94943 ? 80  GLU   A CG     1 
ATOM   918  C CD     . GLU   A 1 79  ? 2.13493   -29.01185 14.28933  1.000 171.97851 ? 80  GLU   A CD     1 
ATOM   919  O OE1    . GLU   A 1 79  ? 1.99416   -29.34710 15.48523  1.000 152.21568 ? 80  GLU   A OE1    1 
ATOM   920  O OE2    . GLU   A 1 79  ? 1.20293   -28.54870 13.59870  1.000 180.86594 ? 80  GLU   A OE2    1 
ATOM   921  H H      . GLU   A 1 79  ? 5.03112   -32.60748 14.83293  1.000 171.57786 ? 80  GLU   A H      1 
ATOM   922  H HA     . GLU   A 1 79  ? 2.63791   -31.64801 14.40159  1.000 172.58188 ? 80  GLU   A HA     1 
ATOM   923  H HB2    . GLU   A 1 79  ? 4.39406   -30.27532 15.10680  1.000 184.50779 ? 80  GLU   A HB2    1 
ATOM   924  H HB3    . GLU   A 1 79  ? 5.09039   -30.45039 13.68910  1.000 184.50779 ? 80  GLU   A HB3    1 
ATOM   925  H HG2    . GLU   A 1 79  ? 4.02017   -28.38953 13.82674  1.000 194.72978 ? 80  GLU   A HG2    1 
ATOM   926  H HG3    . GLU   A 1 79  ? 3.36287   -29.27684 12.68392  1.000 194.72978 ? 80  GLU   A HG3    1 
ATOM   927  N N      . ALA   A 1 80  ? 4.20053   -32.57258 11.77540  1.000 145.75929 ? 81  ALA   A N      1 
ATOM   928  C CA     . ALA   A 1 80  ? 4.00078   -32.89329 10.36639  1.000 141.76299 ? 81  ALA   A CA     1 
ATOM   929  C C      . ALA   A 1 80  ? 2.92291   -33.95523 10.19318  1.000 147.04514 ? 81  ALA   A C      1 
ATOM   930  O O      . ALA   A 1 80  ? 2.06802   -33.84281 9.30631   1.000 147.13247 ? 81  ALA   A O      1 
ATOM   931  C CB     . ALA   A 1 80  ? 5.31629   -33.35867 9.74378   1.000 127.15369 ? 81  ALA   A CB     1 
ATOM   932  H H      . ALA   A 1 80  ? 4.96710   -32.80174 12.09076  1.000 175.30162 ? 81  ALA   A H      1 
ATOM   933  H HA     . ALA   A 1 80  ? 3.71434   -32.09261 9.89975   1.000 170.50606 ? 81  ALA   A HA     1 
ATOM   934  H HB1    . ALA   A 1 80  ? 5.16607   -33.56953 8.80897   1.000 152.97490 ? 81  ALA   A HB1    1 
ATOM   935  H HB2    . ALA   A 1 80  ? 5.97138   -32.64751 9.82133   1.000 152.97490 ? 81  ALA   A HB2    1 
ATOM   936  H HB3    . ALA   A 1 80  ? 5.62707   -34.14750 10.21501  1.000 152.97490 ? 81  ALA   A HB3    1 
ATOM   937  N N      . MET   A 1 81  ? 2.94978   -34.99636 11.02874  1.000 140.30026 ? 82  MET   A N      1 
ATOM   938  C CA     . MET   A 1 81  ? 1.90817   -36.01535 10.96920  1.000 138.10596 ? 82  MET   A CA     1 
ATOM   939  C C      . MET   A 1 81  ? 0.55035   -35.42843 11.33006  1.000 144.20812 ? 82  MET   A C      1 
ATOM   940  O O      . MET   A 1 81  ? -0.47055  -35.78854 10.73176  1.000 151.63294 ? 82  MET   A O      1 
ATOM   941  C CB     . MET   A 1 81  ? 2.25302   -37.17099 11.90658  1.000 135.40415 ? 82  MET   A CB     1 
ATOM   942  C CG     . MET   A 1 81  ? 3.54030   -37.90450 11.55790  1.000 128.37601 ? 82  MET   A CG     1 
ATOM   943  S SD     . MET   A 1 81  ? 3.46783   -38.78837 9.98478   1.000 116.67157 ? 82  MET   A SD     1 
ATOM   944  C CE     . MET   A 1 81  ? 4.14076   -37.56592 8.86048   1.000 130.56014 ? 82  MET   A CE     1 
ATOM   945  H H      . MET   A 1 81  ? 3.55096   -35.13194 11.62857  1.000 168.75079 ? 82  MET   A H      1 
ATOM   946  H HA     . MET   A 1 81  ? 1.86988   -36.36642 10.06577  1.000 166.11762 ? 82  MET   A HA     1 
ATOM   947  H HB2    . MET   A 1 81  ? 2.34987   -36.82078 12.80595  1.000 162.87545 ? 82  MET   A HB2    1 
ATOM   948  H HB3    . MET   A 1 81  ? 1.53058   -37.81766 11.87837  1.000 162.87545 ? 82  MET   A HB3    1 
ATOM   949  H HG2    . MET   A 1 81  ? 4.26238   -37.25924 11.50197  1.000 154.44168 ? 82  MET   A HG2    1 
ATOM   950  H HG3    . MET   A 1 81  ? 3.72851   -38.55353 12.25378  1.000 154.44168 ? 82  MET   A HG3    1 
ATOM   951  H HE1    . MET   A 1 81  ? 4.22988   -37.96219 7.97961   1.000 157.06263 ? 82  MET   A HE1    1 
ATOM   952  H HE2    . MET   A 1 81  ? 3.53838   -36.80660 8.82220   1.000 157.06263 ? 82  MET   A HE2    1 
ATOM   953  H HE3    . MET   A 1 81  ? 5.00979   -37.28269 9.18523   1.000 157.06263 ? 82  MET   A HE3    1 
ATOM   954  N N      . LYS   A 1 82  ? 0.51880   -34.52610 12.31297  1.000 137.74278 ? 83  LYS   A N      1 
ATOM   955  C CA     . LYS   A 1 82  ? -0.73124  -33.86878 12.67591  1.000 144.99785 ? 83  LYS   A CA     1 
ATOM   956  C C      . LYS   A 1 82  ? -1.33413  -33.15139 11.47598  1.000 150.65522 ? 83  LYS   A C      1 
ATOM   957  O O      . LYS   A 1 82  ? -2.50743  -33.35103 11.14111  1.000 150.78033 ? 83  LYS   A O      1 
ATOM   958  C CB     . LYS   A 1 82  ? -0.48876  -32.88640 13.82166  1.000 149.25120 ? 83  LYS   A CB     1 
ATOM   959  C CG     . LYS   A 1 82  ? -1.72808  -32.11803 14.25783  1.000 169.63220 ? 83  LYS   A CG     1 
ATOM   960  C CD     . LYS   A 1 82  ? -1.39198  -31.03544 15.27916  1.000 197.63642 ? 83  LYS   A CD     1 
ATOM   961  C CE     . LYS   A 1 82  ? -0.72778  -31.61490 16.52145  1.000 188.27408 ? 83  LYS   A CE     1 
ATOM   962  N NZ     . LYS   A 1 82  ? -0.68690  -30.63483 17.64060  1.000 178.45480 ? 83  LYS   A NZ     1 
ATOM   963  H H      . LYS   A 1 82  ? 1.19956   -34.28130 12.77799  1.000 165.68181 ? 83  LYS   A H      1 
ATOM   964  H HA     . LYS   A 1 82  ? -1.36364  -34.53853 12.97991  1.000 174.38790 ? 83  LYS   A HA     1 
ATOM   965  H HB2    . LYS   A 1 82  ? -0.16340  -33.38069 14.59025  1.000 179.49190 ? 83  LYS   A HB2    1 
ATOM   966  H HB3    . LYS   A 1 82  ? 0.17502   -32.23806 13.53892  1.000 179.49190 ? 83  LYS   A HB3    1 
ATOM   967  H HG2    . LYS   A 1 82  ? -2.12948  -31.69189 13.48441  1.000 203.94911 ? 83  LYS   A HG2    1 
ATOM   968  H HG3    . LYS   A 1 82  ? -2.35977  -32.73248 14.66320  1.000 203.94911 ? 83  LYS   A HG3    1 
ATOM   969  H HD2    . LYS   A 1 82  ? -0.78178  -30.39635 14.87900  1.000 237.55417 ? 83  LYS   A HD2    1 
ATOM   970  H HD3    . LYS   A 1 82  ? -2.20844  -30.58849 15.55215  1.000 237.55417 ? 83  LYS   A HD3    1 
ATOM   971  H HE2    . LYS   A 1 82  ? -1.22729  -32.39195 16.81742  1.000 226.31936 ? 83  LYS   A HE2    1 
ATOM   972  H HE3    . LYS   A 1 82  ? 0.18372   -31.86827 16.30728  1.000 226.31936 ? 83  LYS   A HE3    1 
ATOM   973  H HZ1    . LYS   A 1 82  ? -0.35904  -31.02157 18.37207  1.000 214.53624 ? 83  LYS   A HZ1    1 
ATOM   974  H HZ2    . LYS   A 1 82  ? -0.16924  -29.94465 17.42205  1.000 214.53624 ? 83  LYS   A HZ2    1 
ATOM   975  H HZ3    . LYS   A 1 82  ? -1.50733  -30.33689 17.81443  1.000 214.53624 ? 83  LYS   A HZ3    1 
ATOM   976  N N      . ARG   A 1 83  ? -0.54059  -32.30788 10.81299  1.000 150.33187 ? 84  ARG   A N      1 
ATOM   977  C CA     . ARG   A 1 83  ? -1.05479  -31.57069 9.66576   1.000 136.92100 ? 84  ARG   A CA     1 
ATOM   978  C C      . ARG   A 1 83  ? -1.44928  -32.51296 8.53875   1.000 145.97555 ? 84  ARG   A C      1 
ATOM   979  O O      . ARG   A 1 83  ? -2.34422  -32.19512 7.74725   1.000 158.66927 ? 84  ARG   A O      1 
ATOM   980  C CB     . ARG   A 1 83  ? -0.01524  -30.55841 9.18664   1.000 144.30928 ? 84  ARG   A CB     1 
ATOM   981  C CG     . ARG   A 1 83  ? -0.60721  -29.41537 8.37196   1.000 167.89662 ? 84  ARG   A CG     1 
ATOM   982  C CD     . ARG   A 1 83  ? 0.25969   -28.16559 8.43770   1.000 174.78626 ? 84  ARG   A CD     1 
ATOM   983  N NE     . ARG   A 1 83  ? 0.53430   -27.76293 9.81246   1.000 164.87204 ? 84  ARG   A NE     1 
ATOM   984  C CZ     . ARG   A 1 83  ? 1.37661   -26.79974 10.16007  1.000 178.00142 ? 84  ARG   A CZ     1 
ATOM   985  N NH1    . ARG   A 1 83  ? 2.04552   -26.10500 9.25341   1.000 169.42927 ? 84  ARG   A NH1    1 
ATOM   986  N NH2    . ARG   A 1 83  ? 1.55448   -26.52891 11.45013  1.000 164.95374 ? 84  ARG   A NH2    1 
ATOM   987  H H      . ARG   A 1 83  ? 0.28253   -32.14913 11.00499  1.000 180.78871 ? 84  ARG   A H      1 
ATOM   988  H HA     . ARG   A 1 83  ? -1.84550  -31.07601 9.93217   1.000 164.69567 ? 84  ARG   A HA     1 
ATOM   989  H HB2    . ARG   A 1 83  ? 0.42618   -30.17405 9.96016   1.000 173.56161 ? 84  ARG   A HB2    1 
ATOM   990  H HB3    . ARG   A 1 83  ? 0.63257   -31.01631 8.62846   1.000 173.56161 ? 84  ARG   A HB3    1 
ATOM   991  H HG2    . ARG   A 1 83  ? -0.67802  -29.68715 7.44351   1.000 201.86642 ? 84  ARG   A HG2    1 
ATOM   992  H HG3    . ARG   A 1 83  ? -1.48495  -29.19462 8.72088   1.000 201.86642 ? 84  ARG   A HG3    1 
ATOM   993  H HD2    . ARG   A 1 83  ? 1.10657   -28.34107 7.99848   1.000 210.13398 ? 84  ARG   A HD2    1 
ATOM   994  H HD3    . ARG   A 1 83  ? -0.19909  -27.43517 7.99395   1.000 210.13398 ? 84  ARG   A HD3    1 
ATOM   995  H HE     . ARG   A 1 83  ? 0.12109   -28.17926 10.44138  1.000 198.23692 ? 84  ARG   A HE     1 
ATOM   996  H HH11   . ARG   A 1 83  ? 1.93859   -26.27427 8.41704   1.000 203.70560 ? 84  ARG   A HH11   1 
ATOM   997  H HH12   . ARG   A 1 83  ? 2.58703   -25.48436 9.50073   1.000 203.70560 ? 84  ARG   A HH12   1 
ATOM   998  H HH21   . ARG   A 1 83  ? 1.12578   -26.97627 12.04652  1.000 198.33496 ? 84  ARG   A HH21   1 
ATOM   999  H HH22   . ARG   A 1 83  ? 2.09819   -25.90643 11.68784  1.000 198.33496 ? 84  ARG   A HH22   1 
ATOM   1000 N N      . ALA   A 1 84  ? -0.80355  -33.67337 8.45345   1.000 144.01803 ? 85  ALA   A N      1 
ATOM   1001 C CA     . ALA   A 1 84  ? -1.18980  -34.69497 7.49195   1.000 152.75250 ? 85  ALA   A CA     1 
ATOM   1002 C C      . ALA   A 1 84  ? -2.36852  -35.53149 7.96955   1.000 159.63518 ? 85  ALA   A C      1 
ATOM   1003 O O      . ALA   A 1 84  ? -2.84862  -36.38301 7.21422   1.000 170.54612 ? 85  ALA   A O      1 
ATOM   1004 C CB     . ALA   A 1 84  ? 0.00044   -35.60883 7.19121   1.000 147.06073 ? 85  ALA   A CB     1 
ATOM   1005 H H      . ALA   A 1 84  ? -0.13362  -33.89209 8.94636   1.000 173.21210 ? 85  ALA   A H      1 
ATOM   1006 H HA     . ALA   A 1 84  ? -1.44670  -34.26146 6.66311   1.000 183.69347 ? 85  ALA   A HA     1 
ATOM   1007 H HB1    . ALA   A 1 84  ? -0.26997  -36.27591 6.54099   1.000 176.86334 ? 85  ALA   A HB1    1 
ATOM   1008 H HB2    . ALA   A 1 84  ? 0.72677   -35.07420 6.83411   1.000 176.86334 ? 85  ALA   A HB2    1 
ATOM   1009 H HB3    . ALA   A 1 84  ? 0.28133   -36.04210 8.01236   1.000 176.86334 ? 85  ALA   A HB3    1 
ATOM   1010 N N      . GLY   A 1 85  ? -2.84482  -35.30894 9.19288   1.000 150.81000 ? 86  GLY   A N      1 
ATOM   1011 C CA     . GLY   A 1 85  ? -3.94946  -36.08440 9.71622   1.000 150.21197 ? 86  GLY   A CA     1 
ATOM   1012 C C      . GLY   A 1 85  ? -3.58892  -37.49095 10.12665  1.000 158.88243 ? 86  GLY   A C      1 
ATOM   1013 O O      . GLY   A 1 85  ? -4.48101  -38.32836 10.27901  1.000 180.70693 ? 86  GLY   A O      1 
ATOM   1014 H H      . GLY   A 1 85  ? -2.54200  -34.71377 9.73480   1.000 181.36247 ? 86  GLY   A H      1 
ATOM   1015 H HA2    . GLY   A 1 85  ? -4.30805  -35.63040 10.49481  1.000 180.64484 ? 86  GLY   A HA2    1 
ATOM   1016 H HA3    . GLY   A 1 85  ? -4.64018  -36.14077 9.03752   1.000 180.64484 ? 86  GLY   A HA3    1 
ATOM   1017 N N      . LEU   A 1 86  ? -2.30089  -37.77631 10.31637  1.000 143.03128 ? 87  LEU   A N      1 
ATOM   1018 C CA     . LEU   A 1 86  ? -1.83481  -39.12070 10.62438  1.000 148.47986 ? 87  LEU   A CA     1 
ATOM   1019 C C      . LEU   A 1 86  ? -1.29524  -39.24983 12.04248  1.000 145.34029 ? 87  LEU   A C      1 
ATOM   1020 O O      . LEU   A 1 86  ? -0.77448  -40.31153 12.40022  1.000 145.04939 ? 87  LEU   A O      1 
ATOM   1021 C CB     . LEU   A 1 86  ? -0.75484  -39.53972 9.62430   1.000 148.94503 ? 87  LEU   A CB     1 
ATOM   1022 C CG     . LEU   A 1 86  ? -1.17225  -39.58169 8.15431   1.000 150.08641 ? 87  LEU   A CG     1 
ATOM   1023 C CD1    . LEU   A 1 86  ? 0.01960   -39.92321 7.27043   1.000 151.89355 ? 87  LEU   A CD1    1 
ATOM   1024 C CD2    . LEU   A 1 86  ? -2.29954  -40.58043 7.94849   1.000 150.60856 ? 87  LEU   A CD2    1 
ATOM   1025 H H      . LEU   A 1 86  ? -1.66902  -37.19475 10.27028  1.000 172.02801 ? 87  LEU   A H      1 
ATOM   1026 H HA     . LEU   A 1 86  ? -2.58620  -39.72824 10.53951  1.000 178.56631 ? 87  LEU   A HA     1 
ATOM   1027 H HB2    . LEU   A 1 86  ? -0.01911  -38.91152 9.69472   1.000 179.12451 ? 87  LEU   A HB2    1 
ATOM   1028 H HB3    . LEU   A 1 86  ? -0.45407  -40.43085 9.86161   1.000 179.12451 ? 87  LEU   A HB3    1 
ATOM   1029 H HG     . LEU   A 1 86  ? -1.49737  -38.70618 7.89225   1.000 180.49416 ? 87  LEU   A HG     1 
ATOM   1030 H HD11   . LEU   A 1 86  ? -0.26668  -39.93170 6.34368   1.000 182.66273 ? 87  LEU   A HD11   1 
ATOM   1031 H HD12   . LEU   A 1 86  ? 0.70929   -39.25307 7.39747   1.000 182.66273 ? 87  LEU   A HD12   1 
ATOM   1032 H HD13   . LEU   A 1 86  ? 0.35777   -40.79738 7.52018   1.000 182.66273 ? 87  LEU   A HD13   1 
ATOM   1033 H HD21   . LEU   A 1 86  ? -2.46263  -40.68104 6.99761   1.000 181.12074 ? 87  LEU   A HD21   1 
ATOM   1034 H HD22   . LEU   A 1 86  ? -2.04003  -41.43294 8.33161   1.000 181.12074 ? 87  LEU   A HD22   1 
ATOM   1035 H HD23   . LEU   A 1 86  ? -3.09855  -40.24979 8.38798   1.000 181.12074 ? 87  LEU   A HD23   1 
ATOM   1036 N N      . LEU   A 1 87  ? -1.41146  -38.20311 12.86109  1.000 144.69634 ? 88  LEU   A N      1 
ATOM   1037 C CA     . LEU   A 1 87  ? -0.78885  -38.23060 14.18091  1.000 149.79281 ? 88  LEU   A CA     1 
ATOM   1038 C C      . LEU   A 1 87  ? -1.31996  -39.39013 15.01506  1.000 142.45410 ? 88  LEU   A C      1 
ATOM   1039 O O      . LEU   A 1 87  ? -0.54452  -40.15824 15.59582  1.000 124.38152 ? 88  LEU   A O      1 
ATOM   1040 C CB     . LEU   A 1 87  ? -1.01703  -36.89971 14.89734  1.000 148.20104 ? 88  LEU   A CB     1 
ATOM   1041 C CG     . LEU   A 1 87  ? -0.28703  -36.74283 16.23418  1.000 159.65021 ? 88  LEU   A CG     1 
ATOM   1042 C CD1    . LEU   A 1 87  ? 1.22247   -36.82626 16.04096  1.000 144.41687 ? 88  LEU   A CD1    1 
ATOM   1043 C CD2    . LEU   A 1 87  ? -0.66440  -35.43287 16.91396  1.000 160.08710 ? 88  LEU   A CD2    1 
ATOM   1044 H H      . LEU   A 1 87  ? -1.83776  -37.47881 12.67872  1.000 174.02608 ? 88  LEU   A H      1 
ATOM   1045 H HA     . LEU   A 1 87  ? 0.16725   -38.35237 14.07164  1.000 180.14184 ? 88  LEU   A HA     1 
ATOM   1046 H HB2    . LEU   A 1 87  ? -0.71488  -36.18444 14.31597  1.000 178.23172 ? 88  LEU   A HB2    1 
ATOM   1047 H HB3    . LEU   A 1 87  ? -1.96651  -36.80623 15.07241  1.000 178.23172 ? 88  LEU   A HB3    1 
ATOM   1048 H HG     . LEU   A 1 87  ? -0.55748  -37.46967 16.81681  1.000 191.97072 ? 88  LEU   A HG     1 
ATOM   1049 H HD11   . LEU   A 1 87  ? 1.66047   -36.61372 16.87994  1.000 173.69072 ? 88  LEU   A HD11   1 
ATOM   1050 H HD12   . LEU   A 1 87  ? 1.45620   -37.72616 15.76448  1.000 173.69072 ? 88  LEU   A HD12   1 
ATOM   1051 H HD13   . LEU   A 1 87  ? 1.48907   -36.19075 15.35835  1.000 173.69072 ? 88  LEU   A HD13   1 
ATOM   1052 H HD21   . LEU   A 1 87  ? -0.48397  -35.50674 17.86416  1.000 192.49499 ? 88  LEU   A HD21   1 
ATOM   1053 H HD22   . LEU   A 1 87  ? -0.13578  -34.71499 16.53172  1.000 192.49499 ? 88  LEU   A HD22   1 
ATOM   1054 H HD23   . LEU   A 1 87  ? -1.60816  -35.26217 16.76877  1.000 192.49499 ? 88  LEU   A HD23   1 
ATOM   1055 N N      . GLN   A 1 88  ? -2.64488  -39.53573 15.08635  1.000 152.09584 ? 89  GLN   A N      1 
ATOM   1056 C CA     . GLN   A 1 88  ? -3.21213  -40.62230 15.87690  1.000 153.14085 ? 89  GLN   A CA     1 
ATOM   1057 C C      . GLN   A 1 88  ? -2.83675  -41.97967 15.29962  1.000 146.90980 ? 89  GLN   A C      1 
ATOM   1058 O O      . GLN   A 1 88  ? -2.64254  -42.94223 16.05135  1.000 129.97340 ? 89  GLN   A O      1 
ATOM   1059 C CB     . GLN   A 1 88  ? -4.73150  -40.48239 15.95885  1.000 154.30315 ? 89  GLN   A CB     1 
ATOM   1060 C CG     . GLN   A 1 88  ? -5.37425  -41.41241 16.97541  1.000 148.86207 ? 89  GLN   A CG     1 
ATOM   1061 C CD     . GLN   A 1 88  ? -4.85482  -41.18258 18.38366  1.000 155.77593 ? 89  GLN   A CD     1 
ATOM   1062 O OE1    . GLN   A 1 88  ? -5.04273  -40.11100 18.96051  1.000 161.30403 ? 89  GLN   A OE1    1 
ATOM   1063 N NE2    . GLN   A 1 88  ? -4.18595  -42.18674 18.93886  1.000 145.73212 ? 89  GLN   A NE2    1 
ATOM   1064 H H      . GLN   A 1 88  ? -3.22107  -39.03078 14.69566  1.000 182.90548 ? 89  GLN   A H      1 
ATOM   1065 H HA     . GLN   A 1 88  ? -2.86138  -40.56766 16.77961  1.000 184.15949 ? 89  GLN   A HA     1 
ATOM   1066 H HB2    . GLN   A 1 88  ? -4.94818  -39.57127 16.21145  1.000 185.55425 ? 89  GLN   A HB2    1 
ATOM   1067 H HB3    . GLN   A 1 88  ? -5.11124  -40.68489 15.08954  1.000 185.55425 ? 89  GLN   A HB3    1 
ATOM   1068 H HG2    . GLN   A 1 88  ? -6.33269  -41.26322 16.98005  1.000 179.02495 ? 89  GLN   A HG2    1 
ATOM   1069 H HG3    . GLN   A 1 88  ? -5.18268  -42.33114 16.73017  1.000 179.02495 ? 89  GLN   A HG3    1 
ATOM   1070 H HE21   . GLN   A 1 88  ? -4.06732  -42.91798 18.50203  1.000 175.26901 ? 89  GLN   A HE21   1 
ATOM   1071 H HE22   . GLN   A 1 88  ? -3.87148  -42.10572 19.73519  1.000 175.26901 ? 89  GLN   A HE22   1 
ATOM   1072 N N      . THR   A 1 89  ? -2.73232  -42.07902 13.97222  1.000 146.48692 ? 90  THR   A N      1 
ATOM   1073 C CA     . THR   A 1 89  ? -2.27484  -43.32313 13.36464  1.000 140.32537 ? 90  THR   A CA     1 
ATOM   1074 C C      . THR   A 1 89  ? -0.85112  -43.64439 13.79974  1.000 134.40991 ? 90  THR   A C      1 
ATOM   1075 O O      . THR   A 1 89  ? -0.51986  -44.80533 14.06786  1.000 125.67822 ? 90  THR   A O      1 
ATOM   1076 C CB     . THR   A 1 89  ? -2.35928  -43.22878 11.84137  1.000 136.03852 ? 90  THR   A CB     1 
ATOM   1077 O OG1    . THR   A 1 89  ? -3.66293  -42.77349 11.45774  1.000 140.15879 ? 90  THR   A OG1    1 
ATOM   1078 C CG2    . THR   A 1 89  ? -2.09248  -44.58848 11.20915  1.000 148.99890 ? 90  THR   A CG2    1 
ATOM   1079 H H      . THR   A 1 89  ? -2.91710  -41.45163 13.41379  1.000 176.17478 ? 90  THR   A H      1 
ATOM   1080 H HA     . THR   A 1 89  ? -2.85475  -44.04615 13.65073  1.000 168.78091 ? 90  THR   A HA     1 
ATOM   1081 H HB     . THR   A 1 89  ? -1.69226  -42.60315 11.51799  1.000 163.63670 ? 90  THR   A HB     1 
ATOM   1082 H HG1    . THR   A 1 89  ? -3.72761  -42.75992 10.62034  1.000 168.58102 ? 90  THR   A HG1    1 
ATOM   1083 H HG21   . THR   A 1 89  ? -2.23843  -44.54334 10.25125  1.000 179.18915 ? 90  THR   A HG21   1 
ATOM   1084 H HG22   . THR   A 1 89  ? -1.17552  -44.85753 11.37554  1.000 179.18915 ? 90  THR   A HG22   1 
ATOM   1085 H HG23   . THR   A 1 89  ? -2.68916  -45.25310 11.58751  1.000 179.18915 ? 90  THR   A HG23   1 
ATOM   1086 N N      . TYR   A 1 90  ? 0.00379   -42.62297 13.88020  1.000 138.40010 ? 91  TYR   A N      1 
ATOM   1087 C CA     . TYR   A 1 90  ? 1.36902   -42.82728 14.35189  1.000 130.48777 ? 91  TYR   A CA     1 
ATOM   1088 C C      . TYR   A 1 90  ? 1.37798   -43.37348 15.77359  1.000 129.24073 ? 91  TYR   A C      1 
ATOM   1089 O O      . TYR   A 1 90  ? 2.04717   -44.37188 16.06313  1.000 123.89673 ? 91  TYR   A O      1 
ATOM   1090 C CB     . TYR   A 1 90  ? 2.14321   -41.51184 14.26545  1.000 119.34791 ? 91  TYR   A CB     1 
ATOM   1091 C CG     . TYR   A 1 90  ? 3.43696   -41.49394 15.04333  1.000 117.24751 ? 91  TYR   A CG     1 
ATOM   1092 C CD1    . TYR   A 1 90  ? 4.52100   -42.26431 14.64746  1.000 122.45655 ? 91  TYR   A CD1    1 
ATOM   1093 C CD2    . TYR   A 1 90  ? 3.58013   -40.69036 16.16469  1.000 119.71662 ? 91  TYR   A CD2    1 
ATOM   1094 C CE1    . TYR   A 1 90  ? 5.70790   -42.24324 15.35553  1.000 117.00370 ? 91  TYR   A CE1    1 
ATOM   1095 C CE2    . TYR   A 1 90  ? 4.76127   -40.66172 16.87662  1.000 116.75553 ? 91  TYR   A CE2    1 
ATOM   1096 C CZ     . TYR   A 1 90  ? 5.82182   -41.43828 16.46678  1.000 111.09985 ? 91  TYR   A CZ     1 
ATOM   1097 O OH     . TYR   A 1 90  ? 6.99928   -41.41211 17.17552  1.000 126.58063 ? 91  TYR   A OH     1 
ATOM   1098 H H      . TYR   A 1 90  ? -0.18161  -41.81010 13.66933  1.000 166.47059 ? 91  TYR   A H      1 
ATOM   1099 H HA     . TYR   A 1 90  ? 1.81147   -43.47584 13.78223  1.000 156.97579 ? 91  TYR   A HA     1 
ATOM   1100 H HB2    . TYR   A 1 90  ? 2.35844   -41.34065 13.33525  1.000 143.60796 ? 91  TYR   A HB2    1 
ATOM   1101 H HB3    . TYR   A 1 90  ? 1.58288   -40.80026 14.61271  1.000 143.60796 ? 91  TYR   A HB3    1 
ATOM   1102 H HD1    . TYR   A 1 90  ? 4.44778   -42.80366 13.89337  1.000 147.33833 ? 91  TYR   A HD1    1 
ATOM   1103 H HD2    . TYR   A 1 90  ? 2.86707   -40.16140 16.44155  1.000 144.05041 ? 91  TYR   A HD2    1 
ATOM   1104 H HE1    . TYR   A 1 90  ? 6.42482   -42.76929 15.08314  1.000 140.79491 ? 91  TYR   A HE1    1 
ATOM   1105 H HE2    . TYR   A 1 90  ? 4.84080   -40.12101 17.62908  1.000 140.49710 ? 91  TYR   A HE2    1 
ATOM   1106 H HH     . TYR   A 1 90  ? 7.53890   -41.97146 16.85687  1.000 152.28723 ? 91  TYR   A HH     1 
ATOM   1107 N N      . TYR   A 1 91  ? 0.63320   -42.73239 16.67796  1.000 137.58936 ? 92  TYR   A N      1 
ATOM   1108 C CA     . TYR   A 1 91  ? 0.54960   -43.23448 18.04539  1.000 132.88556 ? 92  TYR   A CA     1 
ATOM   1109 C C      . TYR   A 1 91  ? -0.03127  -44.64248 18.07381  1.000 134.67683 ? 92  TYR   A C      1 
ATOM   1110 O O      . TYR   A 1 91  ? 0.42792   -45.49691 18.84021  1.000 137.23525 ? 92  TYR   A O      1 
ATOM   1111 C CB     . TYR   A 1 91  ? -0.29735  -42.29614 18.90778  1.000 141.65558 ? 92  TYR   A CB     1 
ATOM   1112 C CG     . TYR   A 1 91  ? 0.36094   -40.97455 19.25344  1.000 137.24058 ? 92  TYR   A CG     1 
ATOM   1113 C CD1    . TYR   A 1 91  ? 1.71436   -40.90231 19.56329  1.000 133.48623 ? 92  TYR   A CD1    1 
ATOM   1114 C CD2    . TYR   A 1 91  ? -0.37655  -39.79782 19.27339  1.000 135.28082 ? 92  TYR   A CD2    1 
ATOM   1115 C CE1    . TYR   A 1 91  ? 2.31294   -39.69618 19.87960  1.000 125.77474 ? 92  TYR   A CE1    1 
ATOM   1116 C CE2    . TYR   A 1 91  ? 0.21395   -38.58850 19.58722  1.000 127.18130 ? 92  TYR   A CE2    1 
ATOM   1117 C CZ     . TYR   A 1 91  ? 1.55788   -38.54342 19.88965  1.000 122.94916 ? 92  TYR   A CZ     1 
ATOM   1118 O OH     . TYR   A 1 91  ? 2.14892   -37.34138 20.20448  1.000 125.20449 ? 92  TYR   A OH     1 
ATOM   1119 H H      . TYR   A 1 91  ? 0.17671   -42.01944 16.52658  1.000 165.49771 ? 92  TYR   A H      1 
ATOM   1120 H HA     . TYR   A 1 91  ? 1.44355   -43.26058 18.42099  1.000 159.85314 ? 92  TYR   A HA     1 
ATOM   1121 H HB2    . TYR   A 1 91  ? -1.11737  -42.09627 18.42975  1.000 170.37717 ? 92  TYR   A HB2    1 
ATOM   1122 H HB3    . TYR   A 1 91  ? -0.50120  -42.74650 19.74236  1.000 170.37717 ? 92  TYR   A HB3    1 
ATOM   1123 H HD1    . TYR   A 1 91  ? 2.22627   -41.67872 19.55777  1.000 160.57395 ? 92  TYR   A HD1    1 
ATOM   1124 H HD2    . TYR   A 1 91  ? -1.28408  -39.82421 19.07192  1.000 162.72746 ? 92  TYR   A HD2    1 
ATOM   1125 H HE1    . TYR   A 1 91  ? 3.21954   -39.66334 20.08428  1.000 151.32016 ? 92  TYR   A HE1    1 
ATOM   1126 H HE2    . TYR   A 1 91  ? -0.29301  -37.80886 19.59431  1.000 153.00804 ? 92  TYR   A HE2    1 
ATOM   1127 H HH     . TYR   A 1 91  ? 1.60196   -36.71396 20.09142  1.000 150.63586 ? 92  TYR   A HH     1 
ATOM   1128 N N      . ASP   A 1 92  ? -1.04156  -44.90396 17.24054  1.000 133.01003 ? 93  ASP   A N      1 
ATOM   1129 C CA     . ASP   A 1 92  ? -1.67059  -46.21996 17.23785  1.000 130.69138 ? 93  ASP   A CA     1 
ATOM   1130 C C      . ASP   A 1 92  ? -0.67079  -47.30968 16.87306  1.000 127.73747 ? 93  ASP   A C      1 
ATOM   1131 O O      . ASP   A 1 92  ? -0.70964  -48.41068 17.43406  1.000 141.96080 ? 93  ASP   A O      1 
ATOM   1132 C CB     . ASP   A 1 92  ? -2.85413  -46.23092 16.27107  1.000 132.85266 ? 93  ASP   A CB     1 
ATOM   1133 C CG     . ASP   A 1 92  ? -4.01232  -45.38902 16.76266  1.000 140.23321 ? 93  ASP   A CG     1 
ATOM   1134 O OD1    . ASP   A 1 92  ? -4.18434  -45.28047 17.99502  1.000 148.01247 ? 93  ASP   A OD1    1 
ATOM   1135 O OD2    . ASP   A 1 92  ? -4.74794  -44.83472 15.91922  1.000 153.05799 ? 93  ASP   A OD2    1 
ATOM   1136 H H      . ASP   A 1 92  ? -1.37415  -44.34528 16.67764  1.000 160.00250 ? 93  ASP   A H      1 
ATOM   1137 H HA     . ASP   A 1 92  ? -2.00669  -46.40822 18.12807  1.000 157.22012 ? 93  ASP   A HA     1 
ATOM   1138 H HB2    . ASP   A 1 92  ? -2.56716  -45.87720 15.41466  1.000 159.81366 ? 93  ASP   A HB2    1 
ATOM   1139 H HB3    . ASP   A 1 92  ? -3.16839  -47.14245 16.16503  1.000 159.81366 ? 93  ASP   A HB3    1 
ATOM   1140 N N      . LEU   A 1 93  ? 0.23934   -47.01761 15.94389  1.000 124.89603 ? 94  LEU   A N      1 
ATOM   1141 C CA     . LEU   A 1 93  ? 1.19912   -48.01001 15.47637  1.000 133.90020 ? 94  LEU   A CA     1 
ATOM   1142 C C      . LEU   A 1 93  ? 2.53505   -47.94452 16.20454  1.000 134.78239 ? 94  LEU   A C      1 
ATOM   1143 O O      . LEU   A 1 93  ? 3.19011   -48.98073 16.36220  1.000 129.10172 ? 94  LEU   A O      1 
ATOM   1144 C CB     . LEU   A 1 93  ? 1.44334   -47.84215 13.97308  1.000 150.55915 ? 94  LEU   A CB     1 
ATOM   1145 C CG     . LEU   A 1 93  ? 0.32029   -48.27931 13.02957  1.000 155.04407 ? 94  LEU   A CG     1 
ATOM   1146 C CD1    . LEU   A 1 93  ? 0.69233   -47.95116 11.59057  1.000 140.04006 ? 94  LEU   A CD1    1 
ATOM   1147 C CD2    . LEU   A 1 93  ? 0.02009   -49.76420 13.17294  1.000 167.10098 ? 94  LEU   A CD2    1 
ATOM   1148 H H      . LEU   A 1 93  ? 0.32005   -46.24808 15.56850  1.000 150.26571 ? 94  LEU   A H      1 
ATOM   1149 H HA     . LEU   A 1 93  ? 0.82119   -48.89032 15.62842  1.000 161.07071 ? 94  LEU   A HA     1 
ATOM   1150 H HB2    . LEU   A 1 93  ? 1.60626   -46.90154 13.80105  1.000 181.06145 ? 94  LEU   A HB2    1 
ATOM   1151 H HB3    . LEU   A 1 93  ? 2.22743   -48.36294 13.73879  1.000 181.06145 ? 94  LEU   A HB3    1 
ATOM   1152 H HG     . LEU   A 1 93  ? -0.48750  -47.79601 13.26364  1.000 186.44336 ? 94  LEU   A HG     1 
ATOM   1153 H HD11   . LEU   A 1 93  ? -0.09820  -48.03041 11.03408  1.000 168.43854 ? 94  LEU   A HD11   1 
ATOM   1154 H HD12   . LEU   A 1 93  ? 1.03459   -47.04438 11.55181  1.000 168.43854 ? 94  LEU   A HD12   1 
ATOM   1155 H HD13   . LEU   A 1 93  ? 1.37217   -48.57444 11.29016  1.000 168.43854 ? 94  LEU   A HD13   1 
ATOM   1156 H HD21   . LEU   A 1 93  ? -0.65073  -50.01537 12.51886  1.000 200.91164 ? 94  LEU   A HD21   1 
ATOM   1157 H HD22   . LEU   A 1 93  ? 0.83529   -50.26735 13.02064  1.000 200.91164 ? 94  LEU   A HD22   1 
ATOM   1158 H HD23   . LEU   A 1 93  ? -0.31120  -49.93438 14.06859  1.000 200.91164 ? 94  LEU   A HD23   1 
ATOM   1159 N N      . ALA   A 1 94  ? 2.95426   -46.76541 16.65547  1.000 138.26648 ? 95  ALA   A N      1 
ATOM   1160 C CA     . ALA   A 1 94  ? 4.25841   -46.63021 17.28656  1.000 129.81255 ? 95  ALA   A CA     1 
ATOM   1161 C C      . ALA   A 1 94  ? 4.25407   -47.25181 18.68129  1.000 125.18953 ? 95  ALA   A C      1 
ATOM   1162 O O      . ALA   A 1 94  ? 3.21148   -47.39934 19.32476  1.000 133.32292 ? 95  ALA   A O      1 
ATOM   1163 C CB     . ALA   A 1 94  ? 4.66056   -45.15916 17.36865  1.000 132.36159 ? 95  ALA   A CB     1 
ATOM   1164 H H      . ALA   A 1 94  ? 2.50409   -46.03420 16.60756  1.000 166.31024 ? 95  ALA   A H      1 
ATOM   1165 H HA     . ALA   A 1 94  ? 4.92192   -47.09625 16.75414  1.000 156.16553 ? 95  ALA   A HA     1 
ATOM   1166 H HB1    . ALA   A 1 94  ? 5.57365   -45.09887 17.69041  1.000 159.22438 ? 95  ALA   A HB1    1 
ATOM   1167 H HB2    . ALA   A 1 94  ? 4.59433   -44.76390 16.48532  1.000 159.22438 ? 95  ALA   A HB2    1 
ATOM   1168 H HB3    . ALA   A 1 94  ? 4.06316   -44.70217 17.98116  1.000 159.22438 ? 95  ALA   A HB3    1 
ATOM   1169 N N      . LEU   A 1 95  ? 5.44754   -47.60993 19.15135  1.000 131.67186 ? 96  LEU   A N      1 
ATOM   1170 C CA     . LEU   A 1 95  ? 5.61332   -48.31859 20.41500  1.000 135.82912 ? 96  LEU   A CA     1 
ATOM   1171 C C      . LEU   A 1 95  ? 6.56372   -47.53908 21.31350  1.000 147.47427 ? 96  LEU   A C      1 
ATOM   1172 O O      . LEU   A 1 95  ? 7.74005   -47.35959 20.95518  1.000 153.32542 ? 96  LEU   A O      1 
ATOM   1173 C CB     . LEU   A 1 95  ? 6.14964   -49.73414 20.18174  1.000 128.41855 ? 96  LEU   A CB     1 
ATOM   1174 C CG     . LEU   A 1 95  ? 5.35247   -50.61344 19.21842  1.000 169.46502 ? 96  LEU   A CG     1 
ATOM   1175 C CD1    . LEU   A 1 95  ? 6.17877   -51.82464 18.81194  1.000 182.08604 ? 96  LEU   A CD1    1 
ATOM   1176 C CD2    . LEU   A 1 95  ? 4.03539   -51.04466 19.84331  1.000 150.69403 ? 96  LEU   A CD2    1 
ATOM   1177 H H      . LEU   A 1 95  ? 6.18947   -47.44960 18.74708  1.000 158.39670 ? 96  LEU   A H      1 
ATOM   1178 H HA     . LEU   A 1 95  ? 4.75203   -48.38256 20.85657  1.000 163.38541 ? 96  LEU   A HA     1 
ATOM   1179 H HB2    . LEU   A 1 95  ? 7.04804   -49.66012 19.82354  1.000 154.49273 ? 96  LEU   A HB2    1 
ATOM   1180 H HB3    . LEU   A 1 95  ? 6.16993   -50.19265 21.03629  1.000 154.49273 ? 96  LEU   A HB3    1 
ATOM   1181 H HG     . LEU   A 1 95  ? 5.14428   -50.10340 18.42004  1.000 203.74850 ? 96  LEU   A HG     1 
ATOM   1182 H HD11   . LEU   A 1 95  ? 5.68090   -52.34216 18.15987  1.000 218.89371 ? 96  LEU   A HD11   1 
ATOM   1183 H HD12   . LEU   A 1 95  ? 7.01476   -51.52110 18.42480  1.000 218.89371 ? 96  LEU   A HD12   1 
ATOM   1184 H HD13   . LEU   A 1 95  ? 6.35515   -52.36484 19.59805  1.000 218.89371 ? 96  LEU   A HD13   1 
ATOM   1185 H HD21   . LEU   A 1 95  ? 3.63121   -51.72912 19.28738  1.000 181.22331 ? 96  LEU   A HD21   1 
ATOM   1186 H HD22   . LEU   A 1 95  ? 4.20730   -51.39778 20.73024  1.000 181.22331 ? 96  LEU   A HD22   1 
ATOM   1187 H HD23   . LEU   A 1 95  ? 3.44687   -50.27581 19.90173  1.000 181.22331 ? 96  LEU   A HD23   1 
ATOM   1188 N N      . PRO   A 1 96  ? 6.11716   -47.05957 22.47391  1.000 159.62174 ? 97  PRO   A N      1 
ATOM   1189 C CA     . PRO   A 1 96  ? 7.04545   -46.38842 23.39172  1.000 158.13843 ? 97  PRO   A CA     1 
ATOM   1190 C C      . PRO   A 1 96  ? 8.05953   -47.37235 23.95322  1.000 152.65618 ? 97  PRO   A C      1 
ATOM   1191 O O      . PRO   A 1 96  ? 7.73672   -48.52603 24.24578  1.000 148.99144 ? 97  PRO   A O      1 
ATOM   1192 C CB     . PRO   A 1 96  ? 6.12997   -45.83376 24.49083  1.000 162.66025 ? 97  PRO   A CB     1 
ATOM   1193 C CG     . PRO   A 1 96  ? 4.74322   -45.88078 23.91626  1.000 157.76095 ? 97  PRO   A CG     1 
ATOM   1194 C CD     . PRO   A 1 96  ? 4.72815   -47.02308 22.96522  1.000 167.19377 ? 97  PRO   A CD     1 
ATOM   1195 H HA     . PRO   A 1 96  ? 7.50280   -45.65471 22.95194  1.000 190.15658 ? 97  PRO   A HA     1 
ATOM   1196 H HB2    . PRO   A 1 96  ? 6.19471   -46.38906 25.28352  1.000 195.58277 ? 97  PRO   A HB2    1 
ATOM   1197 H HB3    . PRO   A 1 96  ? 6.38573   -44.92233 24.70245  1.000 195.58277 ? 97  PRO   A HB3    1 
ATOM   1198 H HG2    . PRO   A 1 96  ? 4.09979   -46.01984 24.62869  1.000 189.70361 ? 97  PRO   A HG2    1 
ATOM   1199 H HG3    . PRO   A 1 96  ? 4.55307   -45.04881 23.45521  1.000 189.70361 ? 97  PRO   A HG3    1 
ATOM   1200 H HD2    . PRO   A 1 96  ? 4.49895   -47.84919 23.41899  1.000 201.02299 ? 97  PRO   A HD2    1 
ATOM   1201 H HD3    . PRO   A 1 96  ? 4.10717   -46.86072 22.23795  1.000 201.02299 ? 97  PRO   A HD3    1 
ATOM   1202 N N      . MET   A 1 97  ? 9.29629   -46.90461 24.10683  1.000 145.22144 ? 98  MET   A N      1 
ATOM   1203 C CA     . MET   A 1 97  ? 10.40103  -47.77150 24.48776  1.000 155.35460 ? 98  MET   A CA     1 
ATOM   1204 C C      . MET   A 1 97  ? 11.30764  -47.06262 25.47975  1.000 138.88891 ? 98  MET   A C      1 
ATOM   1205 O O      . MET   A 1 97  ? 11.61276  -45.87757 25.31969  1.000 129.58138 ? 98  MET   A O      1 
ATOM   1206 C CB     . MET   A 1 97  ? 11.21789  -48.19498 23.25777  1.000 160.29309 ? 98  MET   A CB     1 
ATOM   1207 C CG     . MET   A 1 97  ? 10.48780  -49.13423 22.31393  1.000 136.16225 ? 98  MET   A CG     1 
ATOM   1208 S SD     . MET   A 1 97  ? 10.77174  -50.86812 22.71032  1.000 161.02472 ? 98  MET   A SD     1 
ATOM   1209 C CE     . MET   A 1 97  ? 12.53248  -51.00261 22.40583  1.000 115.73881 ? 98  MET   A CE     1 
ATOM   1210 H H      . MET   A 1 97  ? 9.51941   -46.08169 23.99444  1.000 174.65619 ? 98  MET   A H      1 
ATOM   1211 H HA     . MET   A 1 97  ? 10.04173  -48.56556 24.91352  1.000 186.81599 ? 98  MET   A HA     1 
ATOM   1212 H HB2    . MET   A 1 97  ? 11.45529  -47.39996 22.75528  1.000 192.74218 ? 98  MET   A HB2    1 
ATOM   1213 H HB3    . MET   A 1 97  ? 12.02037  -48.64817 23.56031  1.000 192.74218 ? 98  MET   A HB3    1 
ATOM   1214 H HG2    . MET   A 1 97  ? 9.53458   -48.96433 22.37215  1.000 163.78517 ? 98  MET   A HG2    1 
ATOM   1215 H HG3    . MET   A 1 97  ? 10.79798  -48.97779 21.40827  1.000 163.78517 ? 98  MET   A HG3    1 
ATOM   1216 H HE1    . MET   A 1 97  ? 12.76908  -51.94022 22.32965  1.000 136.93422 ? 98  MET   A HE1    1 
ATOM   1217 H HE2    . MET   A 1 97  ? 12.74661  -50.53934 21.58095  1.000 136.93422 ? 98  MET   A HE2    1 
ATOM   1218 H HE3    . MET   A 1 97  ? 13.01266  -50.59937 23.14591  1.000 136.93422 ? 98  MET   A HE3    1 
ATOM   1219 N N      . GLY   A 1 98  ? 11.72831  -47.79602 26.50891  1.000 137.72021 ? 99  GLY   A N      1 
ATOM   1220 C CA     . GLY   A 1 98  ? 12.72517  -47.30568 27.43155  1.000 148.74804 ? 99  GLY   A CA     1 
ATOM   1221 C C      . GLY   A 1 98  ? 14.12464  -47.47589 26.88248  1.000 136.26074 ? 99  GLY   A C      1 
ATOM   1222 O O      . GLY   A 1 98  ? 14.34134  -47.94379 25.76542  1.000 154.22400 ? 99  GLY   A O      1 
ATOM   1223 H H      . GLY   A 1 98  ? 11.44378  -48.58740 26.68883  1.000 165.65472 ? 99  GLY   A H      1 
ATOM   1224 H HA2    . GLY   A 1 98  ? 12.57278  -46.36307 27.60234  1.000 178.88812 ? 99  GLY   A HA2    1 
ATOM   1225 H HA3    . GLY   A 1 98  ? 12.66003  -47.79272 28.26788  1.000 178.88812 ? 99  GLY   A HA3    1 
ATOM   1226 N N      . VAL   A 1 99  ? 15.09782  -47.08293 27.69654  1.000 141.78483 ? 100 VAL   A N      1 
ATOM   1227 C CA     . VAL   A 1 99  ? 16.50316  -47.16061 27.32268  1.000 140.93600 ? 100 VAL   A CA     1 
ATOM   1228 C C      . VAL   A 1 99  ? 17.29867  -47.65614 28.51961  1.000 145.01837 ? 100 VAL   A C      1 
ATOM   1229 O O      . VAL   A 1 99  ? 17.08004  -47.21438 29.65218  1.000 162.22413 ? 100 VAL   A O      1 
ATOM   1230 C CB     . VAL   A 1 99  ? 17.03764  -45.79711 26.83824  1.000 147.52105 ? 100 VAL   A CB     1 
ATOM   1231 C CG1    . VAL   A 1 99  ? 18.51109  -45.90410 26.48348  1.000 145.87144 ? 100 VAL   A CG1    1 
ATOM   1232 C CG2    . VAL   A 1 99  ? 16.22557  -45.29793 25.64917  1.000 151.72365 ? 100 VAL   A CG2    1 
ATOM   1233 H H      . VAL   A 1 99  ? 14.96585  -46.76253 28.48364  1.000 170.53226 ? 100 VAL   A H      1 
ATOM   1234 H HA     . VAL   A 1 99  ? 16.60562  -47.80246 26.60266  1.000 169.51367 ? 100 VAL   A HA     1 
ATOM   1235 H HB     . VAL   A 1 99  ? 16.94732  -45.14819 27.55353  1.000 177.41574 ? 100 VAL   A HB     1 
ATOM   1236 H HG11   . VAL   A 1 99  ? 18.76318  -45.13658 25.94658  1.000 175.43620 ? 100 VAL   A HG11   1 
ATOM   1237 H HG12   . VAL   A 1 99  ? 19.03239  -45.92126 27.30132  1.000 175.43620 ? 100 VAL   A HG12   1 
ATOM   1238 H HG13   . VAL   A 1 99  ? 18.65649  -46.72117 25.98134  1.000 175.43620 ? 100 VAL   A HG13   1 
ATOM   1239 H HG21   . VAL   A 1 99  ? 16.60769  -44.46412 25.33350  1.000 182.45885 ? 100 VAL   A HG21   1 
ATOM   1240 H HG22   . VAL   A 1 99  ? 16.25596  -45.96354 24.94424  1.000 182.45885 ? 100 VAL   A HG22   1 
ATOM   1241 H HG23   . VAL   A 1 99  ? 15.30824  -45.15580 25.93058  1.000 182.45885 ? 100 VAL   A HG23   1 
ATOM   1242 N N      . ASN   A 1 100 ? 18.21322  -48.58570 28.26748  1.000 142.03889 ? 101 ASN   A N      1 
ATOM   1243 C CA     . ASN   A 1 100 ? 19.16360  -49.05362 29.26400  1.000 149.60244 ? 101 ASN   A CA     1 
ATOM   1244 C C      . ASN   A 1 100 ? 20.57073  -48.71771 28.79546  1.000 139.48782 ? 101 ASN   A C      1 
ATOM   1245 O O      . ASN   A 1 100 ? 20.90714  -48.91610 27.62521  1.000 149.78465 ? 101 ASN   A O      1 
ATOM   1246 C CB     . ASN   A 1 100 ? 19.03672  -50.56214 29.49766  1.000 158.92322 ? 101 ASN   A CB     1 
ATOM   1247 C CG     . ASN   A 1 100 ? 17.81195  -50.92504 30.31237  1.000 166.84788 ? 101 ASN   A CG     1 
ATOM   1248 O OD1    . ASN   A 1 100 ? 16.99709  -50.06560 30.64632  1.000 169.93071 ? 101 ASN   A OD1    1 
ATOM   1249 N ND2    . ASN   A 1 100 ? 17.67347  -52.20602 30.63327  1.000 166.36806 ? 101 ASN   A ND2    1 
ATOM   1250 H H      . ASN   A 1 100 ? 18.30379  -48.97019 27.50357  1.000 170.83714 ? 101 ASN   A H      1 
ATOM   1251 H HA     . ASN   A 1 100 ? 18.99833  -48.60981 30.11054  1.000 179.91339 ? 101 ASN   A HA     1 
ATOM   1252 H HB2    . ASN   A 1 100 ? 18.97098  -51.01086 28.64021  1.000 191.09833 ? 101 ASN   A HB2    1 
ATOM   1253 H HB3    . ASN   A 1 100 ? 19.81987  -50.87524 29.97677  1.000 191.09833 ? 101 ASN   A HB3    1 
ATOM   1254 H HD21   . ASN   A 1 100 ? 16.99483  -52.46271 31.09496  1.000 200.03214 ? 101 ASN   A HD21   1 
ATOM   1255 H HD22   . ASN   A 1 100 ? 18.26242  -52.77900 30.37943  1.000 200.03214 ? 101 ASN   A HD22   1 
ATOM   1256 N N      . ILE   A 1 101 ? 21.38455  -48.19551 29.70443  1.000 137.16129 ? 102 ILE   A N      1 
ATOM   1257 C CA     . ILE   A 1 101 ? 22.78996  -47.92206 29.43484  1.000 130.59869 ? 102 ILE   A CA     1 
ATOM   1258 C C      . ILE   A 1 101 ? 23.59985  -49.02588 30.09553  1.000 132.39180 ? 102 ILE   A C      1 
ATOM   1259 O O      . ILE   A 1 101 ? 23.49769  -49.23765 31.30956  1.000 168.01645 ? 102 ILE   A O      1 
ATOM   1260 C CB     . ILE   A 1 101 ? 23.21222  -46.54132 29.95699  1.000 135.50340 ? 102 ILE   A CB     1 
ATOM   1261 C CG1    . ILE   A 1 101 ? 22.32408  -45.44232 29.36977  1.000 137.41968 ? 102 ILE   A CG1    1 
ATOM   1262 C CG2    . ILE   A 1 101 ? 24.67575  -46.28559 29.62153  1.000 133.09873 ? 102 ILE   A CG2    1 
ATOM   1263 C CD1    . ILE   A 1 101 ? 22.60366  -45.13145 27.92620  1.000 151.51922 ? 102 ILE   A CD1    1 
ATOM   1264 H H      . ILE   A 1 101 ? 21.14018  -47.98659 30.50207  1.000 164.98402 ? 102 ILE   A H      1 
ATOM   1265 H HA     . ILE   A 1 101 ? 22.94738  -47.93991 28.47787  1.000 154.76608 ? 102 ILE   A HA     1 
ATOM   1266 H HB     . ILE   A 1 101 ? 23.10266  -46.53030 30.92072  1.000 162.99455 ? 102 ILE   A HB     1 
ATOM   1267 H HG12   . ILE   A 1 101 ? 21.39798  -45.72304 29.43640  1.000 165.29409 ? 102 ILE   A HG12   1 
ATOM   1268 H HG13   . ILE   A 1 101 ? 22.46122  -44.62771 29.87820  1.000 165.29409 ? 102 ILE   A HG13   1 
ATOM   1269 H HG21   . ILE   A 1 101 ? 24.86898  -45.34358 29.74879  1.000 157.76612 ? 102 ILE   A HG21   1 
ATOM   1270 H HG22   . ILE   A 1 101 ? 25.23249  -46.81981 30.20937  1.000 157.76612 ? 102 ILE   A HG22   1 
ATOM   1271 H HG23   . ILE   A 1 101 ? 24.83613  -46.53430 28.69778  1.000 157.76612 ? 102 ILE   A HG23   1 
ATOM   1272 H HD11   . ILE   A 1 101 ? 21.89452  -44.56631 27.58178  1.000 182.21354 ? 102 ILE   A HD11   1 
ATOM   1273 H HD12   . ILE   A 1 101 ? 23.45477  -44.67066 27.86150  1.000 182.21354 ? 102 ILE   A HD12   1 
ATOM   1274 H HD13   . ILE   A 1 101 ? 22.63795  -45.96142 27.42533  1.000 182.21354 ? 102 ILE   A HD13   1 
ATOM   1275 N N      . ALA   A 1 102 ? 24.39764  -49.73136 29.30578  1.000 130.41408 ? 103 ALA   A N      1 
ATOM   1276 C CA     . ALA   A 1 102 ? 25.16837  -50.86494 29.78651  1.000 135.83637 ? 103 ALA   A CA     1 
ATOM   1277 C C      . ALA   A 1 102 ? 26.65514  -50.60231 29.59210  1.000 145.70504 ? 103 ALA   A C      1 
ATOM   1278 O O      . ALA   A 1 102 ? 27.06457  -49.65361 28.91802  1.000 155.46194 ? 103 ALA   A O      1 
ATOM   1279 C CB     . ALA   A 1 102 ? 24.75456  -52.15423 29.06464  1.000 159.81563 ? 103 ALA   A CB     1 
ATOM   1280 H H      . ALA   A 1 102 ? 24.51031  -49.56743 28.46911  1.000 156.88737 ? 103 ALA   A H      1 
ATOM   1281 H HA     . ALA   A 1 102 ? 25.00649  -50.98214 30.73570  1.000 163.39411 ? 103 ALA   A HA     1 
ATOM   1282 H HB1    . ALA   A 1 102 ? 25.28156  -52.89212 29.40915  1.000 192.16922 ? 103 ALA   A HB1    1 
ATOM   1283 H HB2    . ALA   A 1 102 ? 23.81201  -52.31754 29.22534  1.000 192.16922 ? 103 ALA   A HB2    1 
ATOM   1284 H HB3    . ALA   A 1 102 ? 24.91463  -52.04905 28.11374  1.000 192.16922 ? 103 ALA   A HB3    1 
ATOM   1285 N N      . ASP   A 1 103 ? 27.46294  -51.45616 30.20903  1.000 152.11398 ? 104 ASP   A N      1 
ATOM   1286 C CA     . ASP   A 1 103 ? 28.90913  -51.44132 30.06098  1.000 162.93123 ? 104 ASP   A CA     1 
ATOM   1287 C C      . ASP   A 1 103 ? 29.34346  -52.65988 29.25218  1.000 148.14388 ? 104 ASP   A C      1 
ATOM   1288 O O      . ASP   A 1 103 ? 28.52483  -53.48625 28.84036  1.000 147.29768 ? 104 ASP   A O      1 
ATOM   1289 C CB     . ASP   A 1 103 ? 29.59183  -51.40365 31.43121  1.000 191.73923 ? 104 ASP   A CB     1 
ATOM   1290 C CG     . ASP   A 1 103 ? 29.32941  -52.65227 32.25966  1.000 166.00885 ? 104 ASP   A CG     1 
ATOM   1291 O OD1    . ASP   A 1 103 ? 28.62443  -53.56573 31.78037  1.000 158.29225 ? 104 ASP   A OD1    1 
ATOM   1292 O OD2    . ASP   A 1 103 ? 29.83447  -52.71793 33.40036  1.000 166.65368 ? 104 ASP   A OD2    1 
ATOM   1293 H H      . ASP   A 1 103 ? 27.18423  -52.07489 30.73733  1.000 182.92725 ? 104 ASP   A H      1 
ATOM   1294 H HA     . ASP   A 1 103 ? 29.17487  -50.64272 29.57876  1.000 195.90794 ? 104 ASP   A HA     1 
ATOM   1295 H HB2    . ASP   A 1 103 ? 30.55023  -51.32520 31.30391  1.000 230.47755 ? 104 ASP   A HB2    1 
ATOM   1296 H HB3    . ASP   A 1 103 ? 29.25953  -50.63976 31.92814  1.000 230.47755 ? 104 ASP   A HB3    1 
ATOM   1297 N N      . GLU   A 1 104 ? 30.65389  -52.76826 29.02282  1.000 150.57270 ? 105 GLU   A N      1 
ATOM   1298 C CA     . GLU   A 1 104 ? 31.16705  -53.88241 28.23520  1.000 161.79084 ? 105 GLU   A CA     1 
ATOM   1299 C C      . GLU   A 1 104 ? 31.02926  -55.21454 28.96095  1.000 156.65570 ? 105 GLU   A C      1 
ATOM   1300 O O      . GLU   A 1 104 ? 31.04589  -56.26494 28.31093  1.000 157.86601 ? 105 GLU   A O      1 
ATOM   1301 C CB     . GLU   A 1 104 ? 32.63406  -53.64278 27.85909  1.000 170.51694 ? 105 GLU   A CB     1 
ATOM   1302 C CG     . GLU   A 1 104 ? 33.63878  -53.79158 28.99685  1.000 170.79198 ? 105 GLU   A CG     1 
ATOM   1303 C CD     . GLU   A 1 104 ? 33.60934  -52.62790 29.96563  1.000 180.71363 ? 105 GLU   A CD     1 
ATOM   1304 O OE1    . GLU   A 1 104 ? 32.78497  -51.71021 29.76810  1.000 164.22689 ? 105 GLU   A OE1    1 
ATOM   1305 O OE2    . GLU   A 1 104 ? 34.41172  -52.63029 30.92347  1.000 188.11421 ? 105 GLU   A OE2    1 
ATOM   1306 H H      . GLU   A 1 104 ? 31.25224  -52.21996 29.30732  1.000 181.07771 ? 105 GLU   A H      1 
ATOM   1307 H HA     . GLU   A 1 104 ? 30.65713  -53.93528 27.41174  1.000 194.53948 ? 105 GLU   A HA     1 
ATOM   1308 H HB2    . GLU   A 1 104 ? 32.88048  -54.28117 27.17160  1.000 205.01080 ? 105 GLU   A HB2    1 
ATOM   1309 H HB3    . GLU   A 1 104 ? 32.71721  -52.73873 27.51750  1.000 205.01080 ? 105 GLU   A HB3    1 
ATOM   1310 H HG2    . GLU   A 1 104 ? 33.43559  -54.59963 29.49349  1.000 205.34085 ? 105 GLU   A HG2    1 
ATOM   1311 H HG3    . GLU   A 1 104 ? 34.53227  -53.84752 28.62341  1.000 205.34085 ? 105 GLU   A HG3    1 
ATOM   1312 N N      . LYS   A 1 105 ? 30.89226  -55.19677 30.28277  1.000 154.18391 ? 106 LYS   A N      1 
ATOM   1313 C CA     . LYS   A 1 105 ? 30.79159  -56.41634 31.07096  1.000 160.00838 ? 106 LYS   A CA     1 
ATOM   1314 C C      . LYS   A 1 105 ? 29.36376  -56.93263 31.18596  1.000 162.31146 ? 106 LYS   A C      1 
ATOM   1315 O O      . LYS   A 1 105 ? 29.14522  -57.96875 31.82187  1.000 165.09968 ? 106 LYS   A O      1 
ATOM   1316 C CB     . LYS   A 1 105 ? 31.37318  -56.17634 32.46735  1.000 173.50145 ? 106 LYS   A CB     1 
ATOM   1317 C CG     . LYS   A 1 105 ? 32.84852  -55.80631 32.44969  1.000 173.91943 ? 106 LYS   A CG     1 
ATOM   1318 C CD     . LYS   A 1 105 ? 33.30105  -55.22452 33.77624  1.000 198.76806 ? 106 LYS   A CD     1 
ATOM   1319 C CE     . LYS   A 1 105 ? 34.77493  -54.85038 33.73784  1.000 205.43216 ? 106 LYS   A CE     1 
ATOM   1320 N NZ     . LYS   A 1 105 ? 35.28009  -54.42589 35.07425  1.000 237.77140 ? 106 LYS   A NZ     1 
ATOM   1321 H H      . LYS   A 1 105 ? 30.85457  -54.47742 30.75257  1.000 185.41117 ? 106 LYS   A H      1 
ATOM   1322 H HA     . LYS   A 1 105 ? 31.31645  -57.11120 30.64366  1.000 192.40052 ? 106 LYS   A HA     1 
ATOM   1323 H HB2    . LYS   A 1 105 ? 30.88853  -55.44898 32.88803  1.000 208.59221 ? 106 LYS   A HB2    1 
ATOM   1324 H HB3    . LYS   A 1 105 ? 31.27547  -56.98685 32.99119  1.000 208.59221 ? 106 LYS   A HB3    1 
ATOM   1325 H HG2    . LYS   A 1 105 ? 33.37553  -56.60090 32.27138  1.000 209.09379 ? 106 LYS   A HG2    1 
ATOM   1326 H HG3    . LYS   A 1 105 ? 33.00382  -55.14329 31.75891  1.000 209.09379 ? 106 LYS   A HG3    1 
ATOM   1327 H HD2    . LYS   A 1 105 ? 32.78709  -54.42500 33.96992  1.000 238.91214 ? 106 LYS   A HD2    1 
ATOM   1328 H HD3    . LYS   A 1 105 ? 33.17000  -55.88125 34.47798  1.000 238.91214 ? 106 LYS   A HD3    1 
ATOM   1329 H HE2    . LYS   A 1 105 ? 35.29163  -55.61886 33.44914  1.000 246.90907 ? 106 LYS   A HE2    1 
ATOM   1330 H HE3    . LYS   A 1 105 ? 34.90109  -54.11427 33.11886  1.000 246.90907 ? 106 LYS   A HE3    1 
ATOM   1331 H HZ1    . LYS   A 1 105 ? 34.77220  -53.77040 35.39750  1.000 285.71616 ? 106 LYS   A HZ1    1 
ATOM   1332 H HZ2    . LYS   A 1 105 ? 35.25951  -55.11286 35.63971  1.000 285.71616 ? 106 LYS   A HZ2    1 
ATOM   1333 H HZ3    . LYS   A 1 105 ? 36.11806  -54.13431 35.00436  1.000 285.71616 ? 106 LYS   A HZ3    1 
ATOM   1334 N N      . GLY   A 1 106 ? 28.39375  -56.24975 30.58302  1.000 162.31360 ? 107 GLY   A N      1 
ATOM   1335 C CA     . GLY   A 1 106 ? 27.01512  -56.68391 30.62440  1.000 169.17525 ? 107 GLY   A CA     1 
ATOM   1336 C C      . GLY   A 1 106 ? 26.18882  -56.10539 31.75123  1.000 158.24448 ? 107 GLY   A C      1 
ATOM   1337 O O      . GLY   A 1 106 ? 25.01075  -56.46348 31.87938  1.000 159.14297 ? 107 GLY   A O      1 
ATOM   1338 H H      . GLY   A 1 106 ? 28.51763  -55.52331 30.13970  1.000 195.16680 ? 107 GLY   A H      1 
ATOM   1339 H HA2    . GLY   A 1 106 ? 26.58811  -56.43596 29.78948  1.000 203.40077 ? 107 GLY   A HA2    1 
ATOM   1340 H HA3    . GLY   A 1 106 ? 26.99805  -57.64968 30.71321  1.000 203.40077 ? 107 GLY   A HA3    1 
ATOM   1341 N N      . ASN   A 1 107 ? 26.76033  -55.23005 32.57204  1.000 163.85599 ? 108 ASN   A N      1 
ATOM   1342 C CA     . ASN   A 1 107 ? 26.01208  -54.60197 33.65018  1.000 168.71039 ? 108 ASN   A CA     1 
ATOM   1343 C C      . ASN   A 1 107 ? 25.16197  -53.46234 33.10832  1.000 163.44680 ? 108 ASN   A C      1 
ATOM   1344 O O      . ASN   A 1 107 ? 25.57968  -52.73271 32.20526  1.000 173.67654 ? 108 ASN   A O      1 
ATOM   1345 C CB     . ASN   A 1 107 ? 26.96256  -54.06907 34.72139  1.000 171.26046 ? 108 ASN   A CB     1 
ATOM   1346 C CG     . ASN   A 1 107 ? 27.81147  -55.15844 35.34135  1.000 175.13626 ? 108 ASN   A CG     1 
ATOM   1347 O OD1    . ASN   A 1 107 ? 27.32722  -56.25392 35.62525  1.000 176.36660 ? 108 ASN   A OD1    1 
ATOM   1348 N ND2    . ASN   A 1 107 ? 29.08941  -54.86457 35.54980  1.000 176.10686 ? 108 ASN   A ND2    1 
ATOM   1349 H HA     . ASN   A 1 107 ? 25.42729  -55.25827 34.06028  1.000 202.84294 ? 108 ASN   A HA     1 
ATOM   1350 H HB2    . ASN   A 1 107 ? 27.55743  -53.41624 34.32034  1.000 205.90302 ? 108 ASN   A HB2    1 
ATOM   1351 H HB3    . ASN   A 1 107 ? 26.44290  -53.65452 35.42779  1.000 205.90302 ? 108 ASN   A HB3    1 
ATOM   1352 H HD21   . ASN   A 1 107 ? 29.61362  -55.44963 35.89979  1.000 211.71870 ? 108 ASN   A HD21   1 
ATOM   1353 H HD22   . ASN   A 1 107 ? 29.39292  -54.08915 35.33484  1.000 211.71870 ? 108 ASN   A HD22   1 
ATOM   1354 N N      . ILE   A 1 108 ? 23.96512  -53.31114 33.66538  1.000 156.45145 ? 109 ILE   A N      1 
ATOM   1355 C CA     . ILE   A 1 108 ? 23.08643  -52.19813 33.32610  1.000 155.09047 ? 109 ILE   A CA     1 
ATOM   1356 C C      . ILE   A 1 108 ? 23.46568  -51.02792 34.22557  1.000 157.08513 ? 109 ILE   A C      1 
ATOM   1357 O O      . ILE   A 1 108 ? 23.28522  -51.08546 35.44419  1.000 172.68801 ? 109 ILE   A O      1 
ATOM   1358 C CB     . ILE   A 1 108 ? 21.60770  -52.57171 33.48396  1.000 164.94435 ? 109 ILE   A CB     1 
ATOM   1359 C CG1    . ILE   A 1 108 ? 21.20878  -53.58391 32.40502  1.000 167.09121 ? 109 ILE   A CG1    1 
ATOM   1360 C CG2    . ILE   A 1 108 ? 20.73320  -51.31865 33.41614  1.000 157.85529 ? 109 ILE   A CG2    1 
ATOM   1361 C CD1    . ILE   A 1 108 ? 19.79882  -54.12504 32.54500  1.000 172.35096 ? 109 ILE   A CD1    1 
ATOM   1362 H H      . ILE   A 1 108 ? 23.63525  -53.84784 34.25082  1.000 188.13221 ? 109 ILE   A H      1 
ATOM   1363 H HA     . ILE   A 1 108 ? 23.23225  -51.94116 32.40219  1.000 186.49904 ? 109 ILE   A HA     1 
ATOM   1364 H HB     . ILE   A 1 108 ? 21.47578  -52.98265 34.35265  1.000 198.32369 ? 109 ILE   A HB     1 
ATOM   1365 H HG12   . ILE   A 1 108 ? 21.27320  -53.15366 31.53805  1.000 200.89992 ? 109 ILE   A HG12   1 
ATOM   1366 H HG13   . ILE   A 1 108 ? 21.81788  -54.33764 32.44741  1.000 200.89992 ? 109 ILE   A HG13   1 
ATOM   1367 H HG21   . ILE   A 1 108 ? 19.80176  -51.58565 33.37106  1.000 189.81682 ? 109 ILE   A HG21   1 
ATOM   1368 H HG22   . ILE   A 1 108 ? 20.88585  -50.78363 34.21072  1.000 189.81682 ? 109 ILE   A HG22   1 
ATOM   1369 H HG23   . ILE   A 1 108 ? 20.97032  -50.81052 32.62464  1.000 189.81682 ? 109 ILE   A HG23   1 
ATOM   1370 H HD11   . ILE   A 1 108 ? 19.68239  -54.47471 33.44226  1.000 207.21163 ? 109 ILE   A HD11   1 
ATOM   1371 H HD12   . ILE   A 1 108 ? 19.16739  -53.40616 32.38562  1.000 207.21163 ? 109 ILE   A HD12   1 
ATOM   1372 H HD13   . ILE   A 1 108 ? 19.66596  -54.83227 31.89456  1.000 207.21163 ? 109 ILE   A HD13   1 
ATOM   1373 N N      . LEU   A 1 109 ? 23.99404  -49.96223 33.62389  1.000 152.99242 ? 110 LEU   A N      1 
ATOM   1374 C CA     . LEU   A 1 109 ? 24.41693  -48.80753 34.40654  1.000 160.23016 ? 110 LEU   A CA     1 
ATOM   1375 C C      . LEU   A 1 109 ? 23.22545  -47.96891 34.85251  1.000 165.71395 ? 110 LEU   A C      1 
ATOM   1376 O O      . LEU   A 1 109 ? 23.18729  -47.50064 35.99569  1.000 179.09232 ? 110 LEU   A O      1 
ATOM   1377 C CB     . LEU   A 1 109 ? 25.39559  -47.95594 33.59818  1.000 158.02595 ? 110 LEU   A CB     1 
ATOM   1378 C CG     . LEU   A 1 109 ? 26.61112  -48.69667 33.03459  1.000 158.11739 ? 110 LEU   A CG     1 
ATOM   1379 C CD1    . LEU   A 1 109 ? 27.58757  -47.71463 32.39977  1.000 156.61939 ? 110 LEU   A CD1    1 
ATOM   1380 C CD2    . LEU   A 1 109 ? 27.29787  -49.52343 34.10814  1.000 161.03102 ? 110 LEU   A CD2    1 
ATOM   1381 H H      . LEU   A 1 109 ? 24.11601  -49.88541 32.77605  1.000 183.98137 ? 110 LEU   A H      1 
ATOM   1382 H HA     . LEU   A 1 109 ? 24.87791  -49.12029 35.20063  1.000 192.66666 ? 110 LEU   A HA     1 
ATOM   1383 H HB2    . LEU   A 1 109 ? 24.91636  -47.57394 32.84631  1.000 190.02161 ? 110 LEU   A HB2    1 
ATOM   1384 H HB3    . LEU   A 1 109 ? 25.72925  -47.24913 34.17263  1.000 190.02161 ? 110 LEU   A HB3    1 
ATOM   1385 H HG     . LEU   A 1 109 ? 26.30850  -49.30940 32.34620  1.000 190.13134 ? 110 LEU   A HG     1 
ATOM   1386 H HD11   . LEU   A 1 109 ? 28.39819  -48.18830 32.15601  1.000 188.33374 ? 110 LEU   A HD11   1 
ATOM   1387 H HD12   . LEU   A 1 109 ? 27.17885  -47.32966 31.60879  1.000 188.33374 ? 110 LEU   A HD12   1 
ATOM   1388 H HD13   . LEU   A 1 109 ? 27.79289  -47.01520 33.03972  1.000 188.33374 ? 110 LEU   A HD13   1 
ATOM   1389 H HD21   . LEU   A 1 109 ? 28.16281  -49.81337 33.77842  1.000 193.62770 ? 110 LEU   A HD21   1 
ATOM   1390 H HD22   . LEU   A 1 109 ? 27.41241  -48.97782 34.90192  1.000 193.62770 ? 110 LEU   A HD22   1 
ATOM   1391 H HD23   . LEU   A 1 109 ? 26.74669  -50.29472 34.31361  1.000 193.62770 ? 110 LEU   A HD23   1 
ATOM   1392 N N      . THR   A 1 110 ? 22.24696  -47.77019 33.97289  1.000 156.78962 ? 111 THR   A N      1 
ATOM   1393 C CA     . THR   A 1 110 ? 21.05655  -47.00570 34.30823  1.000 165.02048 ? 111 THR   A CA     1 
ATOM   1394 C C      . THR   A 1 110 ? 19.85123  -47.61335 33.60887  1.000 161.01571 ? 111 THR   A C      1 
ATOM   1395 O O      . THR   A 1 110 ? 19.96654  -48.18771 32.52365  1.000 155.11089 ? 111 THR   A O      1 
ATOM   1396 C CB     . THR   A 1 110 ? 21.18971  -45.52917 33.90890  1.000 171.76170 ? 111 THR   A CB     1 
ATOM   1397 O OG1    . THR   A 1 110 ? 21.52980  -45.43643 32.51996  1.000 152.11387 ? 111 THR   A OG1    1 
ATOM   1398 C CG2    . THR   A 1 110 ? 22.25671  -44.83778 34.74896  1.000 173.03268 ? 111 THR   A CG2    1 
ATOM   1399 H H      . THR   A 1 110 ? 22.25245  -48.07255 33.16782  1.000 188.53801 ? 111 THR   A H      1 
ATOM   1400 H HA     . THR   A 1 110 ? 20.91251  -47.05021 35.26645  1.000 198.41505 ? 111 THR   A HA     1 
ATOM   1401 H HB     . THR   A 1 110 ? 20.34692  -45.07426 34.06267  1.000 206.50451 ? 111 THR   A HB     1 
ATOM   1402 H HG1    . THR   A 1 110 ? 21.48741  -44.63669 32.26657  1.000 182.92712 ? 111 THR   A HG1    1 
ATOM   1403 H HG21   . THR   A 1 110 ? 22.20950  -43.87750 34.62040  1.000 208.02968 ? 111 THR   A HG21   1 
ATOM   1404 H HG22   . THR   A 1 110 ? 22.11980  -45.03673 35.68841  1.000 208.02968 ? 111 THR   A HG22   1 
ATOM   1405 H HG23   . THR   A 1 110 ? 23.13771  -45.14756 34.48672  1.000 208.02968 ? 111 THR   A HG23   1 
ATOM   1406 N N      . THR   A 1 111 ? 18.69228  -47.48156 34.24869  1.000 178.55166 ? 112 THR   A N      1 
ATOM   1407 C CA     . THR   A 1 111 ? 17.41587  -47.91989 33.69523  1.000 173.90991 ? 112 THR   A CA     1 
ATOM   1408 C C      . THR   A 1 111 ? 16.55656  -46.68243 33.46545  1.000 174.03586 ? 112 THR   A C      1 
ATOM   1409 O O      . THR   A 1 111 ? 16.16601  -46.00487 34.42269  1.000 178.16066 ? 112 THR   A O      1 
ATOM   1410 C CB     . THR   A 1 111 ? 16.71640  -48.90573 34.62916  1.000 180.18947 ? 112 THR   A CB     1 
ATOM   1411 O OG1    . THR   A 1 111 ? 17.48131  -50.11454 34.71269  1.000 179.96045 ? 112 THR   A OG1    1 
ATOM   1412 C CG2    . THR   A 1 111 ? 15.31538  -49.22479 34.12154  1.000 181.70482 ? 112 THR   A CG2    1 
ATOM   1413 H H      . THR   A 1 111 ? 18.61883  -47.12968 35.02997  1.000 214.65247 ? 112 THR   A H      1 
ATOM   1414 H HA     . THR   A 1 111 ? 17.56699  -48.36338 32.84588  1.000 209.08236 ? 112 THR   A HA     1 
ATOM   1415 H HB     . THR   A 1 111 ? 16.63709  -48.51299 35.51254  1.000 216.61783 ? 112 THR   A HB     1 
ATOM   1416 H HG1    . THR   A 1 111 ? 17.09396  -50.66552 35.21466  1.000 216.34301 ? 112 THR   A HG1    1 
ATOM   1417 H HG21   . THR   A 1 111 ? 14.97902  -50.02402 34.55628  1.000 218.43625 ? 112 THR   A HG21   1 
ATOM   1418 H HG22   . THR   A 1 111 ? 14.71668  -48.48621 34.31375  1.000 218.43625 ? 112 THR   A HG22   1 
ATOM   1419 H HG23   . THR   A 1 111 ? 15.33544  -49.37254 33.16307  1.000 218.43625 ? 112 THR   A HG23   1 
ATOM   1420 N N      . LYS   A 1 112 ? 16.26778  -46.38817 32.19719  1.000 173.77094 ? 113 LYS   A N      1 
ATOM   1421 C CA     . LYS   A 1 112 ? 15.44898  -45.24392 31.81746  1.000 178.86744 ? 113 LYS   A CA     1 
ATOM   1422 C C      . LYS   A 1 112 ? 14.02090  -45.65216 31.47072  1.000 176.80764 ? 113 LYS   A C      1 
ATOM   1423 O O      . LYS   A 1 112 ? 13.40480  -45.05770 30.58058  1.000 188.00131 ? 113 LYS   A O      1 
ATOM   1424 C CB     . LYS   A 1 112 ? 16.08834  -44.50682 30.64048  1.000 174.64442 ? 113 LYS   A CB     1 
ATOM   1425 C CG     . LYS   A 1 112 ? 17.52217  -44.05860 30.89053  1.000 172.67816 ? 113 LYS   A CG     1 
ATOM   1426 C CD     . LYS   A 1 112 ? 18.12353  -43.40517 29.65461  1.000 196.69403 ? 113 LYS   A CD     1 
ATOM   1427 C CE     . LYS   A 1 112 ? 19.48592  -42.79492 29.94801  1.000 205.93473 ? 113 LYS   A CE     1 
ATOM   1428 N NZ     . LYS   A 1 112 ? 19.99781  -41.99778 28.79584  1.000 185.99448 ? 113 LYS   A NZ     1 
ATOM   1429 H H      . LYS   A 1 112 ? 16.54280  -46.84950 31.52553  1.000 208.91560 ? 113 LYS   A H      1 
ATOM   1430 H HA     . LYS   A 1 112 ? 15.40746  -44.63152 32.56856  1.000 215.03140 ? 113 LYS   A HA     1 
ATOM   1431 H HB2    . LYS   A 1 112 ? 16.09440  -45.09733 29.87096  1.000 209.96377 ? 113 LYS   A HB2    1 
ATOM   1432 H HB3    . LYS   A 1 112 ? 15.56190  -43.71536 30.44718  1.000 209.96377 ? 113 LYS   A HB3    1 
ATOM   1433 H HG2    . LYS   A 1 112 ? 17.53575  -43.41297 31.61433  1.000 207.60426 ? 113 LYS   A HG2    1 
ATOM   1434 H HG3    . LYS   A 1 112 ? 18.06408  -44.82885 31.12282  1.000 207.60426 ? 113 LYS   A HG3    1 
ATOM   1435 H HD2    . LYS   A 1 112 ? 18.23281  -44.07317 28.95982  1.000 236.42331 ? 113 LYS   A HD2    1 
ATOM   1436 H HD3    . LYS   A 1 112 ? 17.53412  -42.69916 29.34630  1.000 236.42331 ? 113 LYS   A HD3    1 
ATOM   1437 H HE2    . LYS   A 1 112 ? 19.41401  -42.20663 30.71589  1.000 247.51215 ? 113 LYS   A HE2    1 
ATOM   1438 H HE3    . LYS   A 1 112 ? 20.12111  -43.50454 30.13207  1.000 247.51215 ? 113 LYS   A HE3    1 
ATOM   1439 H HZ1    . LYS   A 1 112 ? 20.86079  -41.81394 28.91235  1.000 223.58385 ? 113 LYS   A HZ1    1 
ATOM   1440 H HZ2    . LYS   A 1 112 ? 19.89991  -42.45759 28.04014  1.000 223.58385 ? 113 LYS   A HZ2    1 
ATOM   1441 H HZ3    . LYS   A 1 112 ? 19.54611  -41.23378 28.72966  1.000 223.58385 ? 113 LYS   A HZ3    1 
ATOM   1442 N N      . ASN   A 1 113 ? 13.49160  -46.65883 32.16479  1.000 173.03728 ? 114 ASN   A N      1 
ATOM   1443 C CA     . ASN   A 1 113 ? 12.16538  -47.19871 31.88355  1.000 172.02155 ? 114 ASN   A CA     1 
ATOM   1444 C C      . ASN   A 1 113 ? 11.14902  -46.08296 31.68895  1.000 178.49720 ? 114 ASN   A C      1 
ATOM   1445 O O      . ASN   A 1 113 ? 10.89093  -45.29749 32.60513  1.000 184.92775 ? 114 ASN   A O      1 
ATOM   1446 C CB     . ASN   A 1 113 ? 11.73988  -48.11633 33.03234  1.000 178.27649 ? 114 ASN   A CB     1 
ATOM   1447 C CG     . ASN   A 1 113 ? 10.69164  -49.12726 32.61462  1.000 179.04898 ? 114 ASN   A CG     1 
ATOM   1448 O OD1    . ASN   A 1 113 ? 10.32262  -49.20866 31.44378  1.000 182.92988 ? 114 ASN   A OD1    1 
ATOM   1449 N ND2    . ASN   A 1 113 ? 10.21548  -49.91489 33.57152  1.000 192.75630 ? 114 ASN   A ND2    1 
ATOM   1450 H H      . ASN   A 1 113 ? 13.88925  -47.05409 32.81689  1.000 208.03520 ? 114 ASN   A H      1 
ATOM   1451 H HA     . ASN   A 1 113 ? 12.19727  -47.71835 31.06510  1.000 206.81634 ? 114 ASN   A HA     1 
ATOM   1452 H HB2    . ASN   A 1 113 ? 12.51551  -48.60288 33.35260  1.000 214.32225 ? 114 ASN   A HB2    1 
ATOM   1453 H HB3    . ASN   A 1 113 ? 11.36831  -47.57653 33.74750  1.000 214.32225 ? 114 ASN   A HB3    1 
ATOM   1454 H HD21   . ASN   A 1 113 ? 9.61858   -50.50530 33.38515  1.000 231.69803 ? 114 ASN   A HD21   1 
ATOM   1455 H HD22   . ASN   A 1 113 ? 10.50395  -49.83467 34.37771  1.000 231.69803 ? 114 ASN   A HD22   1 
ATOM   1456 N N      . VAL   A 1 114 ? 10.58113  -46.01866 30.48407  1.000 186.91447 ? 115 VAL   A N      1 
ATOM   1457 C CA     . VAL   A 1 114 ? 9.64426   -44.96823 30.09906  1.000 188.25288 ? 115 VAL   A CA     1 
ATOM   1458 C C      . VAL   A 1 114 ? 8.64689   -44.69531 31.21346  1.000 192.68251 ? 115 VAL   A C      1 
ATOM   1459 O O      . VAL   A 1 114 ? 7.97457   -45.61109 31.70014  1.000 215.59110 ? 115 VAL   A O      1 
ATOM   1460 C CB     . VAL   A 1 114 ? 8.89709   -45.34495 28.80447  1.000 184.87425 ? 115 VAL   A CB     1 
ATOM   1461 C CG1    . VAL   A 1 114 ? 7.68465   -44.44948 28.60067  1.000 187.65635 ? 115 VAL   A CG1    1 
ATOM   1462 C CG2    . VAL   A 1 114 ? 9.82049   -45.25162 27.61276  1.000 190.23258 ? 115 VAL   A CG2    1 
ATOM   1463 H H      . VAL   A 1 114 ? 10.72752  -46.58806 29.85641  1.000 224.68783 ? 115 VAL   A H      1 
ATOM   1464 H HA     . VAL   A 1 114 ? 10.15607  -44.15674 29.95612  1.000 226.29392 ? 115 VAL   A HA     1 
ATOM   1465 H HB     . VAL   A 1 114 ? 8.58829   -46.26107 28.88354  1.000 222.23957 ? 115 VAL   A HB     1 
ATOM   1466 H HG11   . VAL   A 1 114 ? 7.39395   -44.51673 27.67771  1.000 225.57809 ? 115 VAL   A HG11   1 
ATOM   1467 H HG12   . VAL   A 1 114 ? 6.97400   -44.74039 29.19333  1.000 225.57809 ? 115 VAL   A HG12   1 
ATOM   1468 H HG13   . VAL   A 1 114 ? 7.93078   -43.53353 28.80404  1.000 225.57809 ? 115 VAL   A HG13   1 
ATOM   1469 H HG21   . VAL   A 1 114 ? 9.30960   -45.41237 26.80403  1.000 228.66957 ? 115 VAL   A HG21   1 
ATOM   1470 H HG22   . VAL   A 1 114 ? 10.21242  -44.36473 27.58563  1.000 228.66957 ? 115 VAL   A HG22   1 
ATOM   1471 H HG23   . VAL   A 1 114 ? 10.51864  -45.91921 27.70116  1.000 228.66957 ? 115 VAL   A HG23   1 
ATOM   1472 N N      . LYS   A 1 115 ? 8.54166   -43.43501 31.62080  1.000 199.78764 ? 116 LYS   A N      1 
ATOM   1473 C CA     . LYS   A 1 115 ? 7.46152   -43.04553 32.50575  1.000 198.06884 ? 116 LYS   A CA     1 
ATOM   1474 C C      . LYS   A 1 115 ? 6.13257   -43.13937 31.75885  1.000 196.73095 ? 116 LYS   A C      1 
ATOM   1475 O O      . LYS   A 1 115 ? 6.07048   -42.87870 30.55424  1.000 192.56011 ? 116 LYS   A O      1 
ATOM   1476 C CB     . LYS   A 1 115 ? 7.64807   -41.61943 33.00516  1.000 193.20524 ? 116 LYS   A CB     1 
ATOM   1477 C CG     . LYS   A 1 115 ? 8.95279   -41.33786 33.70457  1.000 195.34272 ? 116 LYS   A CG     1 
ATOM   1478 C CD     . LYS   A 1 115 ? 9.02170   -39.86308 34.03965  1.000 197.07712 ? 116 LYS   A CD     1 
ATOM   1479 C CE     . LYS   A 1 115 ? 10.24421  -39.52623 34.84495  1.000 201.84442 ? 116 LYS   A CE     1 
ATOM   1480 N NZ     . LYS   A 1 115 ? 10.16019  -38.13940 35.37940  1.000 206.87158 ? 116 LYS   A NZ     1 
ATOM   1481 H H      . LYS   A 1 115 ? 9.07637   -42.79846 31.40059  1.000 240.13564 ? 116 LYS   A H      1 
ATOM   1482 H HA     . LYS   A 1 115 ? 7.44762   -43.63514 33.27586  1.000 238.07308 ? 116 LYS   A HA     1 
ATOM   1483 H HB2    . LYS   A 1 115 ? 7.59460   -41.02091 32.24370  1.000 232.23676 ? 116 LYS   A HB2    1 
ATOM   1484 H HB3    . LYS   A 1 115 ? 6.93605   -41.42142 33.63342  1.000 232.23676 ? 116 LYS   A HB3    1 
ATOM   1485 H HG2    . LYS   A 1 115 ? 9.00557   -41.85100 34.52603  1.000 234.80173 ? 116 LYS   A HG2    1 
ATOM   1486 H HG3    . LYS   A 1 115 ? 9.69563   -41.56457 33.12346  1.000 234.80173 ? 116 LYS   A HG3    1 
ATOM   1487 H HD2    . LYS   A 1 115 ? 9.04982   -39.34954 33.21722  1.000 236.88301 ? 116 LYS   A HD2    1 
ATOM   1488 H HD3    . LYS   A 1 115 ? 8.23997   -39.61639 34.55825  1.000 236.88301 ? 116 LYS   A HD3    1 
ATOM   1489 H HE2    . LYS   A 1 115 ? 10.31889  -40.14017 35.59222  1.000 242.60377 ? 116 LYS   A HE2    1 
ATOM   1490 H HE3    . LYS   A 1 115 ? 11.03115  -39.59196 34.28165  1.000 242.60377 ? 116 LYS   A HE3    1 
ATOM   1491 H HZ1    . LYS   A 1 115 ? 10.97316  -37.84435 35.58944  1.000 248.63636 ? 116 LYS   A HZ1    1 
ATOM   1492 H HZ2    . LYS   A 1 115 ? 9.80566   -37.59851 34.76796  1.000 248.63636 ? 116 LYS   A HZ2    1 
ATOM   1493 H HZ3    . LYS   A 1 115 ? 9.65020   -38.12459 36.10864  1.000 248.63636 ? 116 LYS   A HZ3    1 
ATOM   1494 N N      . PRO   A 1 116 ? 5.05079   -43.50483 32.44931  1.000 196.03818 ? 117 PRO   A N      1 
ATOM   1495 C CA     . PRO   A 1 116 ? 3.73358   -43.44113 31.79369  1.000 194.06838 ? 117 PRO   A CA     1 
ATOM   1496 C C      . PRO   A 1 116 ? 3.40575   -42.05643 31.25951  1.000 185.86114 ? 117 PRO   A C      1 
ATOM   1497 O O      . PRO   A 1 116 ? 2.81402   -41.93258 30.17946  1.000 180.02415 ? 117 PRO   A O      1 
ATOM   1498 C CB     . PRO   A 1 116 ? 2.76378   -43.87643 32.90531  1.000 189.26622 ? 117 PRO   A CB     1 
ATOM   1499 C CG     . PRO   A 1 116 ? 3.54012   -43.79032 34.18446  1.000 196.24141 ? 117 PRO   A CG     1 
ATOM   1500 C CD     . PRO   A 1 116 ? 4.96658   -44.02781 33.82389  1.000 189.19350 ? 117 PRO   A CD     1 
ATOM   1501 H HA     . PRO   A 1 116 ? 3.69176   -44.08509 31.06948  1.000 233.27252 ? 117 PRO   A HA     1 
ATOM   1502 H HB2    . PRO   A 1 116 ? 2.00051   -43.27818 32.92540  1.000 227.50993 ? 117 PRO   A HB2    1 
ATOM   1503 H HB3    . PRO   A 1 116 ? 2.46824   -44.78595 32.74303  1.000 227.50993 ? 117 PRO   A HB3    1 
ATOM   1504 H HG2    . PRO   A 1 116 ? 3.42807   -42.90929 34.57450  1.000 235.88017 ? 117 PRO   A HG2    1 
ATOM   1505 H HG3    . PRO   A 1 116 ? 3.22594   -44.46900 34.80218  1.000 235.88017 ? 117 PRO   A HG3    1 
ATOM   1506 H HD2    . PRO   A 1 116 ? 5.55972   -43.54068 34.41699  1.000 227.42267 ? 117 PRO   A HD2    1 
ATOM   1507 H HD3    . PRO   A 1 116 ? 5.17721   -44.97436 33.84809  1.000 227.42267 ? 117 PRO   A HD3    1 
ATOM   1508 N N      . GLU   A 1 117 ? 3.79407   -41.00499 31.98794  1.000 196.64332 ? 118 GLU   A N      1 
ATOM   1509 C CA     . GLU   A 1 117 ? 3.46974   -39.63843 31.59386  1.000 186.48233 ? 118 GLU   A CA     1 
ATOM   1510 C C      . GLU   A 1 117 ? 4.26598   -39.16346 30.38295  1.000 176.60606 ? 118 GLU   A C      1 
ATOM   1511 O O      . GLU   A 1 117 ? 3.81657   -38.24582 29.68842  1.000 175.15702 ? 118 GLU   A O      1 
ATOM   1512 C CB     . GLU   A 1 117 ? 3.70346   -38.68902 32.77487  1.000 208.40850 ? 118 GLU   A CB     1 
ATOM   1513 C CG     . GLU   A 1 117 ? 5.09369   -38.78102 33.39653  1.000 215.84095 ? 118 GLU   A CG     1 
ATOM   1514 C CD     . GLU   A 1 117 ? 5.22406   -37.95558 34.66235  1.000 206.10174 ? 118 GLU   A CD     1 
ATOM   1515 O OE1    . GLU   A 1 117 ? 4.20241   -37.40385 35.12338  1.000 212.96997 ? 118 GLU   A OE1    1 
ATOM   1516 O OE2    . GLU   A 1 117 ? 6.34869   -37.86099 35.19690  1.000 208.58563 ? 118 GLU   A OE2    1 
ATOM   1517 H H      . GLU   A 1 117 ? 4.24776   -41.05935 32.71651  1.000 236.36246 ? 118 GLU   A H      1 
ATOM   1518 H HA     . GLU   A 1 117 ? 2.53063   -39.60421 31.35345  1.000 224.16926 ? 118 GLU   A HA     1 
ATOM   1519 H HB2    . GLU   A 1 117 ? 3.58006   -37.77740 32.46725  1.000 250.48068 ? 118 GLU   A HB2    1 
ATOM   1520 H HB3    . GLU   A 1 117 ? 3.05810   -38.89512 33.46908  1.000 250.48068 ? 118 GLU   A HB3    1 
ATOM   1521 H HG2    . GLU   A 1 117 ? 5.27932   -39.70627 33.62096  1.000 259.39961 ? 118 GLU   A HG2    1 
ATOM   1522 H HG3    . GLU   A 1 117 ? 5.74792   -38.45685 32.75795  1.000 259.39961 ? 118 GLU   A HG3    1 
ATOM   1523 N N      . ASN   A 1 118 ? 5.43238   -39.74964 30.11738  1.000 174.41427 ? 119 ASN   A N      1 
ATOM   1524 C CA     . ASN   A 1 118 ? 6.21966   -39.42769 28.93310  1.000 192.35051 ? 119 ASN   A CA     1 
ATOM   1525 C C      . ASN   A 1 118 ? 6.11978   -40.50391 27.86075  1.000 184.02010 ? 119 ASN   A C      1 
ATOM   1526 O O      . ASN   A 1 118 ? 6.87784   -40.47303 26.88522  1.000 158.40367 ? 119 ASN   A O      1 
ATOM   1527 C CB     . ASN   A 1 118 ? 7.68252   -39.20432 29.31676  1.000 187.28109 ? 119 ASN   A CB     1 
ATOM   1528 C CG     . ASN   A 1 118 ? 7.86330   -38.02088 30.24212  1.000 196.04436 ? 119 ASN   A CG     1 
ATOM   1529 O OD1    . ASN   A 1 118 ? 8.20413   -38.18031 31.41304  1.000 208.62888 ? 119 ASN   A OD1    1 
ATOM   1530 N ND2    . ASN   A 1 118 ? 7.63227   -36.82191 29.72049  1.000 176.87582 ? 119 ASN   A ND2    1 
ATOM   1531 N N      . ARG   A 1 119 ? 5.18863   -41.44459 28.01937  1.000 187.76796 ? 120 ARG   A N      1 
ATOM   1532 C CA     . ARG   A 1 119 ? 5.09300   -42.57989 27.10915  1.000 177.03325 ? 120 ARG   A CA     1 
ATOM   1533 C C      . ARG   A 1 119 ? 4.77673   -42.14100 25.68489  1.000 169.16916 ? 120 ARG   A C      1 
ATOM   1534 O O      . ARG   A 1 119 ? 5.24195   -42.77009 24.72711  1.000 151.69414 ? 120 ARG   A O      1 
ATOM   1535 C CB     . ARG   A 1 119 ? 4.03552   -43.54705 27.64848  1.000 172.29472 ? 120 ARG   A CB     1 
ATOM   1536 C CG     . ARG   A 1 119 ? 3.60265   -44.64429 26.70800  1.000 168.14792 ? 120 ARG   A CG     1 
ATOM   1537 C CD     . ARG   A 1 119 ? 2.45920   -45.45940 27.31179  1.000 171.07766 ? 120 ARG   A CD     1 
ATOM   1538 N NE     . ARG   A 1 119 ? 1.78159   -46.28669 26.31898  1.000 201.63117 ? 120 ARG   A NE     1 
ATOM   1539 C CZ     . ARG   A 1 119 ? 2.13433   -47.52452 25.99400  1.000 208.48776 ? 120 ARG   A CZ     1 
ATOM   1540 N NH1    . ARG   A 1 119 ? 3.14886   -48.13442 26.58514  1.000 210.78863 ? 120 ARG   A NH1    1 
ATOM   1541 N NH2    . ARG   A 1 119 ? 1.45373   -48.16490 25.04751  1.000 199.58130 ? 120 ARG   A NH2    1 
ATOM   1542 H H      . ARG   A 1 119 ? 4.60034   -41.44802 28.64666  1.000 225.71202 ? 120 ARG   A H      1 
ATOM   1543 H HA     . ARG   A 1 119 ? 5.94227   -43.04682 27.06905  1.000 212.83037 ? 120 ARG   A HA     1 
ATOM   1544 H HB2    . ARG   A 1 119 ? 4.39257   -43.97454 28.44263  1.000 207.14413 ? 120 ARG   A HB2    1 
ATOM   1545 H HB3    . ARG   A 1 119 ? 3.24360   -43.03478 27.87506  1.000 207.14413 ? 120 ARG   A HB3    1 
ATOM   1546 H HG2    . ARG   A 1 119 ? 3.29553   -44.25400 25.87478  1.000 202.16797 ? 120 ARG   A HG2    1 
ATOM   1547 H HG3    . ARG   A 1 119 ? 4.34956   -45.23993 26.53991  1.000 202.16797 ? 120 ARG   A HG3    1 
ATOM   1548 H HD2    . ARG   A 1 119 ? 2.81443   -46.04412 27.99940  1.000 205.68367 ? 120 ARG   A HD2    1 
ATOM   1549 H HD3    . ARG   A 1 119 ? 1.80592   -44.85404 27.69607  1.000 205.68367 ? 120 ARG   A HD3    1 
ATOM   1550 H HE     . ARG   A 1 119 ? 1.10309   -45.94702 25.91418  1.000 242.34788 ? 120 ARG   A HE     1 
ATOM   1551 H HH11   . ARG   A 1 119 ? 3.59769   -47.72846 27.19617  1.000 253.33683 ? 120 ARG   A HH11   1 
ATOM   1552 H HH12   . ARG   A 1 119 ? 3.35945   -48.93680 26.35834  1.000 253.33683 ? 120 ARG   A HH12   1 
ATOM   1553 H HH21   . ARG   A 1 119 ? 0.79449   -47.77673 24.65465  1.000 239.88803 ? 120 ARG   A HH21   1 
ATOM   1554 H HH22   . ARG   A 1 119 ? 1.67290   -48.96711 24.82839  1.000 239.88803 ? 120 ARG   A HH22   1 
ATOM   1555 N N      . PHE   A 1 120 ? 4.00749   -41.06621 25.52024  1.000 159.66447 ? 121 PHE   A N      1 
ATOM   1556 C CA     . PHE   A 1 120 ? 3.63647   -40.59771 24.19063  1.000 143.17401 ? 121 PHE   A CA     1 
ATOM   1557 C C      . PHE   A 1 120 ? 4.35969   -39.30144 23.86194  1.000 145.22930 ? 121 PHE   A C      1 
ATOM   1558 O O      . PHE   A 1 120 ? 3.74473   -38.32343 23.42433  1.000 152.60713 ? 121 PHE   A O      1 
ATOM   1559 C CB     . PHE   A 1 120 ? 2.12355   -40.42456 24.09759  1.000 145.52553 ? 121 PHE   A CB     1 
ATOM   1560 C CG     . PHE   A 1 120 ? 1.36967   -41.69489 24.33253  1.000 155.51401 ? 121 PHE   A CG     1 
ATOM   1561 C CD1    . PHE   A 1 120 ? 1.08434   -42.55060 23.28267  1.000 166.52983 ? 121 PHE   A CD1    1 
ATOM   1562 C CD2    . PHE   A 1 120 ? 0.96989   -42.04906 25.60819  1.000 156.23880 ? 121 PHE   A CD2    1 
ATOM   1563 C CE1    . PHE   A 1 120 ? 0.40007   -43.72792 23.50046  1.000 161.85622 ? 121 PHE   A CE1    1 
ATOM   1564 C CE2    . PHE   A 1 120 ? 0.28627   -43.22403 25.83078  1.000 157.26012 ? 121 PHE   A CE2    1 
ATOM   1565 C CZ     . PHE   A 1 120 ? 0.00251   -44.06323 24.77629  1.000 154.99249 ? 121 PHE   A CZ     1 
ATOM   1566 H H      . PHE   A 1 120 ? 3.68871   -40.59242 26.16328  1.000 191.98783 ? 121 PHE   A H      1 
ATOM   1567 H HA     . PHE   A 1 120 ? 3.89800   -41.25545 23.52739  1.000 172.19929 ? 121 PHE   A HA     1 
ATOM   1568 H HB2    . PHE   A 1 120 ? 1.83943   -39.78102 24.76545  1.000 175.02110 ? 121 PHE   A HB2    1 
ATOM   1569 H HB3    . PHE   A 1 120 ? 1.89816   -40.10346 23.21046  1.000 175.02110 ? 121 PHE   A HB3    1 
ATOM   1570 H HD1    . PHE   A 1 120 ? 1.35691   -42.32930 22.42150  1.000 200.22626 ? 121 PHE   A HD1    1 
ATOM   1571 H HD2    . PHE   A 1 120 ? 1.16474   -41.48776 26.32364  1.000 187.87703 ? 121 PHE   A HD2    1 
ATOM   1572 H HE1    . PHE   A 1 120 ? 0.20750   -44.29396 22.78813  1.000 194.61793 ? 121 PHE   A HE1    1 
ATOM   1573 H HE2    . PHE   A 1 120 ? 0.01681   -43.45024 26.69166  1.000 189.10262 ? 121 PHE   A HE2    1 
ATOM   1574 H HZ     . PHE   A 1 120 ? -0.45805  -44.85727 24.92560  1.000 186.38146 ? 121 PHE   A HZ     1 
ATOM   1575 N N      . ASP   A 1 121 ? 5.67247   -39.29526 24.07557  1.000 155.11207 ? 122 ASP   A N      1 
ATOM   1576 C CA     . ASP   A 1 121 ? 6.53946   -38.19155 23.69310  1.000 167.13271 ? 122 ASP   A CA     1 
ATOM   1577 C C      . ASP   A 1 121 ? 7.37806   -38.51839 22.46833  1.000 161.94771 ? 122 ASP   A C      1 
ATOM   1578 O O      . ASP   A 1 121 ? 7.45871   -37.71219 21.53688  1.000 165.35238 ? 122 ASP   A O      1 
ATOM   1579 C CB     . ASP   A 1 121 ? 7.46041   -37.82053 24.86387  1.000 172.47733 ? 122 ASP   A CB     1 
ATOM   1580 C CG     . ASP   A 1 121 ? 6.70275   -37.24320 26.04096  1.000 179.54437 ? 122 ASP   A CG     1 
ATOM   1581 O OD1    . ASP   A 1 121 ? 5.48598   -36.99704 25.90410  1.000 168.22166 ? 122 ASP   A OD1    1 
ATOM   1582 O OD2    . ASP   A 1 121 ? 7.32458   -37.03715 27.10428  1.000 183.96312 ? 122 ASP   A OD2    1 
ATOM   1583 H H      . ASP   A 1 121 ? 6.09549   -39.94182 24.45321  1.000 186.52496 ? 122 ASP   A H      1 
ATOM   1584 H HA     . ASP   A 1 121 ? 5.99285   -37.41706 23.48746  1.000 200.94973 ? 122 ASP   A HA     1 
ATOM   1585 H HB2    . ASP   A 1 121 ? 7.92422   -38.61690 25.16648  1.000 207.36326 ? 122 ASP   A HB2    1 
ATOM   1586 H HB3    . ASP   A 1 121 ? 8.10140   -37.15692 24.56444  1.000 207.36326 ? 122 ASP   A HB3    1 
ATOM   1587 N N      . ASN   A 1 122 ? 8.00161   -39.69408 22.44561  1.000 165.14898 ? 123 ASN   A N      1 
ATOM   1588 C CA     . ASN   A 1 122 ? 8.88010   -40.08937 21.35374  1.000 153.54447 ? 123 ASN   A CA     1 
ATOM   1589 C C      . ASN   A 1 122 ? 8.78842   -41.59177 21.12608  1.000 145.65228 ? 123 ASN   A C      1 
ATOM   1590 O O      . ASN   A 1 122 ? 9.78174   -42.31108 21.29529  1.000 132.74080 ? 123 ASN   A O      1 
ATOM   1591 C CB     . ASN   A 1 122 ? 10.31803  -39.67332 21.65855  1.000 155.29281 ? 123 ASN   A CB     1 
ATOM   1592 C CG     . ASN   A 1 122 ? 10.47762  -38.16907 21.74012  1.000 175.47801 ? 123 ASN   A CG     1 
ATOM   1593 O OD1    . ASN   A 1 122 ? 10.12384  -37.44641 20.80830  1.000 182.79253 ? 123 ASN   A OD1    1 
ATOM   1594 N ND2    . ASN   A 1 122 ? 10.98966  -37.68647 22.86613  1.000 202.22072 ? 123 ASN   A ND2    1 
ATOM   1595 H HA     . ASN   A 1 122 ? 8.60222   -39.64859 20.53558  1.000 184.64384 ? 123 ASN   A HA     1 
ATOM   1596 H HB2    . ASN   A 1 122 ? 10.58418  -40.05156 22.51119  1.000 186.74184 ? 123 ASN   A HB2    1 
ATOM   1597 H HB3    . ASN   A 1 122 ? 10.89943  -40.00059 20.95445  1.000 186.74184 ? 123 ASN   A HB3    1 
ATOM   1598 H HD21   . ASN   A 1 122 ? 11.09961  -36.83868 22.95983  1.000 243.05533 ? 123 ASN   A HD21   1 
ATOM   1599 H HD22   . ASN   A 1 122 ? 11.21137  -38.22166 23.50175  1.000 243.05533 ? 123 ASN   A HD22   1 
ATOM   1600 N N      . PRO   A 1 123 ? 7.61951   -42.09935 20.74637  1.000 139.64762 ? 124 PRO   A N      1 
ATOM   1601 C CA     . PRO   A 1 123 ? 7.49321   -43.53004 20.44968  1.000 130.30900 ? 124 PRO   A CA     1 
ATOM   1602 C C      . PRO   A 1 123 ? 8.21294   -43.87127 19.15425  1.000 134.85472 ? 124 PRO   A C      1 
ATOM   1603 O O      . PRO   A 1 123 ? 8.66619   -43.00048 18.40938  1.000 147.45183 ? 124 PRO   A O      1 
ATOM   1604 C CB     . PRO   A 1 123 ? 5.98114   -43.74144 20.34232  1.000 134.98342 ? 124 PRO   A CB     1 
ATOM   1605 C CG     . PRO   A 1 123 ? 5.44606   -42.40971 19.93086  1.000 124.75437 ? 124 PRO   A CG     1 
ATOM   1606 C CD     . PRO   A 1 123 ? 6.35302   -41.37215 20.54323  1.000 124.79195 ? 124 PRO   A CD     1 
ATOM   1607 H HA     . PRO   A 1 123 ? 7.83803   -44.07789 21.17209  1.000 156.76127 ? 124 PRO   A HA     1 
ATOM   1608 H HB2    . PRO   A 1 123 ? 5.78680   -44.41722 19.67415  1.000 162.37057 ? 124 PRO   A HB2    1 
ATOM   1609 H HB3    . PRO   A 1 123 ? 5.62162   -44.01161 21.20176  1.000 162.37057 ? 124 PRO   A HB3    1 
ATOM   1610 H HG2    . PRO   A 1 123 ? 5.45522   -42.34178 18.96328  1.000 150.09571 ? 124 PRO   A HG2    1 
ATOM   1611 H HG3    . PRO   A 1 123 ? 4.53999   -42.30826 20.26199  1.000 150.09571 ? 124 PRO   A HG3    1 
ATOM   1612 H HD2    . PRO   A 1 123 ? 6.47842   -40.62417 19.93850  1.000 150.14081 ? 124 PRO   A HD2    1 
ATOM   1613 H HD3    . PRO   A 1 123 ? 5.99622   -41.05876 21.38903  1.000 150.14081 ? 124 PRO   A HD3    1 
ATOM   1614 N N      . GLU   A 1 124 ? 8.30858   -45.17052 18.88559  1.000 136.21784 ? 125 GLU   A N      1 
ATOM   1615 C CA     . GLU   A 1 124 ? 9.14568   -45.69139 17.81141  1.000 135.29644 ? 125 GLU   A CA     1 
ATOM   1616 C C      . GLU   A 1 124 ? 8.28357   -46.45641 16.82235  1.000 138.42371 ? 125 GLU   A C      1 
ATOM   1617 O O      . GLU   A 1 124 ? 7.64499   -47.45040 17.18637  1.000 128.29233 ? 125 GLU   A O      1 
ATOM   1618 C CB     . GLU   A 1 124 ? 10.24783  -46.59022 18.37485  1.000 150.40996 ? 125 GLU   A CB     1 
ATOM   1619 C CG     . GLU   A 1 124 ? 11.24925  -45.84379 19.23610  1.000 169.25137 ? 125 GLU   A CG     1 
ATOM   1620 C CD     . GLU   A 1 124 ? 12.14489  -46.75999 20.03260  1.000 191.03596 ? 125 GLU   A CD     1 
ATOM   1621 O OE1    . GLU   A 1 124 ? 12.20942  -47.96115 19.69779  1.000 198.50737 ? 125 GLU   A OE1    1 
ATOM   1622 O OE2    . GLU   A 1 124 ? 12.77938  -46.27426 20.99523  1.000 195.62206 ? 125 GLU   A OE2    1 
ATOM   1623 H H      . GLU   A 1 124 ? 7.88874   -45.78141 19.32165  1.000 163.85188 ? 125 GLU   A H      1 
ATOM   1624 H HA     . GLU   A 1 124 ? 9.55534   -44.95169 17.33610  1.000 162.74620 ? 125 GLU   A HA     1 
ATOM   1625 H HB2    . GLU   A 1 124 ? 9.84070   -47.28047 18.92138  1.000 180.88242 ? 125 GLU   A HB2    1 
ATOM   1626 H HB3    . GLU   A 1 124 ? 10.73139  -46.99346 17.63697  1.000 180.88242 ? 125 GLU   A HB3    1 
ATOM   1627 H HG2    . GLU   A 1 124 ? 11.81241  -45.29947 18.66384  1.000 203.49211 ? 125 GLU   A HG2    1 
ATOM   1628 H HG3    . GLU   A 1 124 ? 10.76782  -45.27963 19.86127  1.000 203.49211 ? 125 GLU   A HG3    1 
ATOM   1629 N N      . ILE   A 1 125 ? 8.27438   -45.99636 15.57332  1.000 136.74323 ? 126 ILE   A N      1 
ATOM   1630 C CA     . ILE   A 1 125 ? 7.49815   -46.60771 14.50320  1.000 119.20229 ? 126 ILE   A CA     1 
ATOM   1631 C C      . ILE   A 1 125 ? 8.46712   -47.23650 13.51329  1.000 105.91636 ? 126 ILE   A C      1 
ATOM   1632 O O      . ILE   A 1 125 ? 9.37988   -46.56672 13.01498  1.000 113.26348 ? 126 ILE   A O      1 
ATOM   1633 C CB     . ILE   A 1 125 ? 6.58044   -45.58062 13.81336  1.000 110.54104 ? 126 ILE   A CB     1 
ATOM   1634 C CG1    . ILE   A 1 125 ? 5.66218   -46.28214 12.81178  1.000 120.15967 ? 126 ILE   A CG1    1 
ATOM   1635 C CG2    . ILE   A 1 125 ? 7.40153   -44.50265 13.11545  1.000 113.45377 ? 126 ILE   A CG2    1 
ATOM   1636 C CD1    . ILE   A 1 125 ? 4.51635   -45.41880 12.32334  1.000 128.77999 ? 126 ILE   A CD1    1 
ATOM   1637 H H      . ILE   A 1 125 ? 8.72457   -45.31013 15.31640  1.000 164.48234 ? 126 ILE   A H      1 
ATOM   1638 H HA     . ILE   A 1 125 ? 6.93945   -47.31083 14.86978  1.000 143.43322 ? 126 ILE   A HA     1 
ATOM   1639 H HB     . ILE   A 1 125 ? 6.03579   -45.15584 14.49441  1.000 133.03972 ? 126 ILE   A HB     1 
ATOM   1640 H HG12   . ILE   A 1 125 ? 6.18623   -46.54340 12.03846  1.000 144.58208 ? 126 ILE   A HG12   1 
ATOM   1641 H HG13   . ILE   A 1 125 ? 5.28131   -47.06740 13.23511  1.000 144.58208 ? 126 ILE   A HG13   1 
ATOM   1642 H HG21   . ILE   A 1 125 ? 6.82513   -43.74996 12.91020  1.000 136.53499 ? 126 ILE   A HG21   1 
ATOM   1643 H HG22   . ILE   A 1 125 ? 8.11766   -44.21966 13.70534  1.000 136.53499 ? 126 ILE   A HG22   1 
ATOM   1644 H HG23   . ILE   A 1 125 ? 7.77215   -44.86829 12.29701  1.000 136.53499 ? 126 ILE   A HG23   1 
ATOM   1645 H HD11   . ILE   A 1 125 ? 3.95448   -45.94436 11.73260  1.000 154.92646 ? 126 ILE   A HD11   1 
ATOM   1646 H HD12   . ILE   A 1 125 ? 4.00102   -45.11613 13.08736  1.000 154.92646 ? 126 ILE   A HD12   1 
ATOM   1647 H HD13   . ILE   A 1 125 ? 4.87728   -44.65620 11.84472  1.000 154.92646 ? 126 ILE   A HD13   1 
ATOM   1648 N N      . ASN   A 1 126 ? 8.27997   -48.52867 13.24958  1.000 117.10147 ? 127 ASN   A N      1 
ATOM   1649 C CA     . ASN   A 1 126 ? 9.07136   -49.22799 12.24645  1.000 112.39245 ? 127 ASN   A CA     1 
ATOM   1650 C C      . ASN   A 1 126 ? 8.99824   -48.49972 10.91012  1.000 116.17534 ? 127 ASN   A C      1 
ATOM   1651 O O      . ASN   A 1 126 ? 7.95521   -47.95679 10.53709  1.000 118.45926 ? 127 ASN   A O      1 
ATOM   1652 C CB     . ASN   A 1 126 ? 8.55921   -50.66445 12.11025  1.000 126.85215 ? 127 ASN   A CB     1 
ATOM   1653 C CG     . ASN   A 1 126 ? 9.03179   -51.33566 10.84504  1.000 131.05518 ? 127 ASN   A CG     1 
ATOM   1654 O OD1    . ASN   A 1 126 ? 8.51225   -51.07512 9.76195   1.000 131.23209 ? 127 ASN   A OD1    1 
ATOM   1655 N ND2    . ASN   A 1 126 ? 10.01015  -52.22085 10.97505  1.000 138.92160 ? 127 ASN   A ND2    1 
ATOM   1656 H H      . ASN   A 1 126 ? 7.69674   -49.02470 13.64126  1.000 140.91223 ? 127 ASN   A H      1 
ATOM   1657 H HA     . ASN   A 1 126 ? 10.00275  -49.25997 12.51553  1.000 135.26141 ? 127 ASN   A HA     1 
ATOM   1658 H HB2    . ASN   A 1 126 ? 8.87771   -51.18621 12.86339  1.000 152.61305 ? 127 ASN   A HB2    1 
ATOM   1659 H HB3    . ASN   A 1 126 ? 7.58931   -50.65446 12.10005  1.000 152.61305 ? 127 ASN   A HB3    1 
ATOM   1660 H HD21   . ASN   A 1 126 ? 10.31426  -52.63044 10.28269  1.000 167.09639 ? 127 ASN   A HD21   1 
ATOM   1661 H HD22   . ASN   A 1 126 ? 10.34069  -52.38547 11.75173  1.000 167.09639 ? 127 ASN   A HD22   1 
ATOM   1662 N N      . ARG   A 1 127 ? 10.12079  -48.49212 10.18532  1.000 118.36523 ? 128 ARG   A N      1 
ATOM   1663 C CA     . ARG   A 1 127 ? 10.20108  -47.70699 8.95636   1.000 121.05192 ? 128 ARG   A CA     1 
ATOM   1664 C C      . ARG   A 1 127 ? 9.15314   -48.14677 7.93997   1.000 116.94350 ? 128 ARG   A C      1 
ATOM   1665 O O      . ARG   A 1 127 ? 8.53933   -47.30767 7.26984   1.000 112.08548 ? 128 ARG   A O      1 
ATOM   1666 C CB     . ARG   A 1 127 ? 11.60363  -47.81286 8.35574   1.000 119.72025 ? 128 ARG   A CB     1 
ATOM   1667 C CG     . ARG   A 1 127 ? 12.69673  -47.16863 9.19626   1.000 128.45882 ? 128 ARG   A CG     1 
ATOM   1668 C CD     . ARG   A 1 127 ? 14.06002  -47.29778 8.53150   1.000 116.63784 ? 128 ARG   A CD     1 
ATOM   1669 N NE     . ARG   A 1 127 ? 15.11929  -46.67937 9.32111   1.000 125.74811 ? 128 ARG   A NE     1 
ATOM   1670 C CZ     . ARG   A 1 127 ? 15.55110  -45.43365 9.16672   1.000 124.43549 ? 128 ARG   A CZ     1 
ATOM   1671 N NH1    . ARG   A 1 127 ? 15.03168  -44.62689 8.25581   1.000 131.81079 ? 128 ARG   A NH1    1 
ATOM   1672 N NH2    . ARG   A 1 127 ? 16.53253  -44.98753 9.94463   1.000 129.55351 ? 128 ARG   A NH2    1 
ATOM   1673 H H      . ARG   A 1 127 ? 10.83698  -48.92606 10.38121  1.000 142.42875 ? 128 ARG   A H      1 
ATOM   1674 H HA     . ARG   A 1 127 ? 10.03311  -46.77689 9.17457   1.000 145.65278 ? 128 ARG   A HA     1 
ATOM   1675 H HB2    . ARG   A 1 127 ? 11.82650  -48.75137 8.25365   1.000 144.05477 ? 128 ARG   A HB2    1 
ATOM   1676 H HB3    . ARG   A 1 127 ? 11.60321  -47.37587 7.48975   1.000 144.05477 ? 128 ARG   A HB3    1 
ATOM   1677 H HG2    . ARG   A 1 127 ? 12.50098  -46.22540 9.30984   1.000 154.54106 ? 128 ARG   A HG2    1 
ATOM   1678 H HG3    . ARG   A 1 127 ? 12.73664  -47.60568 10.06130  1.000 154.54106 ? 128 ARG   A HG3    1 
ATOM   1679 H HD2    . ARG   A 1 127 ? 14.27360  -48.23774 8.42306   1.000 140.35588 ? 128 ARG   A HD2    1 
ATOM   1680 H HD3    . ARG   A 1 127 ? 14.03466  -46.86129 7.66562   1.000 140.35588 ? 128 ARG   A HD3    1 
ATOM   1681 H HE     . ARG   A 1 127 ? 15.49149  -47.15711 9.93172   1.000 151.28820 ? 128 ARG   A HE     1 
ATOM   1682 H HH11   . ARG   A 1 127 ? 14.39810  -44.90580 7.74552   1.000 158.56341 ? 128 ARG   A HH11   1 
ATOM   1683 H HH12   . ARG   A 1 127 ? 15.32762  -43.82357 8.17398   1.000 158.56341 ? 128 ARG   A HH12   1 
ATOM   1684 H HH21   . ARG   A 1 127 ? 16.87916  -45.50411 10.53843  1.000 155.85468 ? 128 ARG   A HH21   1 
ATOM   1685 H HH22   . ARG   A 1 127 ? 16.82078  -44.18236 9.85407   1.000 155.85468 ? 128 ARG   A HH22   1 
ATOM   1686 N N      . ASN   A 1 128 ? 8.93665   -49.45770 7.80427   1.000 128.28882 ? 129 ASN   A N      1 
ATOM   1687 C CA     . ASN   A 1 128 ? 7.93568   -49.94027 6.85677   1.000 115.06492 ? 129 ASN   A CA     1 
ATOM   1688 C C      . ASN   A 1 128 ? 6.53127   -49.52613 7.27826   1.000 117.04939 ? 129 ASN   A C      1 
ATOM   1689 O O      . ASN   A 1 128 ? 5.69824   -49.18613 6.43001   1.000 117.42000 ? 129 ASN   A O      1 
ATOM   1690 C CB     . ASN   A 1 128 ? 8.02734   -51.45985 6.71922   1.000 111.46877 ? 129 ASN   A CB     1 
ATOM   1691 C CG     . ASN   A 1 128 ? 9.13698   -51.89316 5.78357   1.000 106.93646 ? 129 ASN   A CG     1 
ATOM   1692 O OD1    . ASN   A 1 128 ? 10.17292  -52.39551 6.21957   1.000 105.91327 ? 129 ASN   A OD1    1 
ATOM   1693 N ND2    . ASN   A 1 128 ? 8.92162   -51.70739 4.48567   1.000 122.24891 ? 129 ASN   A ND2    1 
ATOM   1694 H H      . ASN   A 1 128 ? 9.34795   -50.07436 8.24034   1.000 154.33706 ? 129 ASN   A H      1 
ATOM   1695 H HA     . ASN   A 1 128 ? 8.11769   -49.54976 5.98771   1.000 138.46837 ? 129 ASN   A HA     1 
ATOM   1696 H HB2    . ASN   A 1 128 ? 8.20115   -51.84698 7.59147   1.000 134.15300 ? 129 ASN   A HB2    1 
ATOM   1697 H HB3    . ASN   A 1 128 ? 7.18863   -51.79728 6.36764   1.000 134.15300 ? 129 ASN   A HB3    1 
ATOM   1698 H HD21   . ASN   A 1 128 ? 9.52097   -51.93682 3.91318   1.000 147.08916 ? 129 ASN   A HD21   1 
ATOM   1699 H HD22   . ASN   A 1 128 ? 8.18289   -51.35771 4.21809   1.000 147.08916 ? 129 ASN   A HD22   1 
ATOM   1700 N N      . ASP   A 1 129 ? 6.24628   -49.55254 8.58229   1.000 122.29262 ? 130 ASP   A N      1 
ATOM   1701 C CA     . ASP   A 1 129 ? 4.94977   -49.08112 9.05731   1.000 120.21482 ? 130 ASP   A CA     1 
ATOM   1702 C C      . ASP   A 1 129 ? 4.71693   -47.62967 8.65684   1.000 114.65292 ? 130 ASP   A C      1 
ATOM   1703 O O      . ASP   A 1 129 ? 3.62703   -47.27063 8.19646   1.000 112.59460 ? 130 ASP   A O      1 
ATOM   1704 C CB     . ASP   A 1 129 ? 4.85625   -49.23859 10.57556  1.000 123.72084 ? 130 ASP   A CB     1 
ATOM   1705 C CG     . ASP   A 1 129 ? 4.75640   -50.69164 11.01019  1.000 133.03923 ? 130 ASP   A CG     1 
ATOM   1706 O OD1    . ASP   A 1 129 ? 4.59052   -51.56763 10.13575  1.000 130.76094 ? 130 ASP   A OD1    1 
ATOM   1707 O OD2    . ASP   A 1 129 ? 4.84395   -50.95861 12.22833  1.000 132.96397 ? 130 ASP   A OD2    1 
ATOM   1708 H H      . ASP   A 1 129 ? 6.77642   -49.83315 9.19858   1.000 147.14161 ? 130 ASP   A H      1 
ATOM   1709 H HA     . ASP   A 1 129 ? 4.25247   -49.62340 8.65655   1.000 144.64825 ? 130 ASP   A HA     1 
ATOM   1710 H HB2    . ASP   A 1 129 ? 5.65005   -48.85755 10.98248  1.000 148.85547 ? 130 ASP   A HB2    1 
ATOM   1711 H HB3    . ASP   A 1 129 ? 4.06552   -48.77531 10.89340  1.000 148.85547 ? 130 ASP   A HB3    1 
ATOM   1712 N N      . LEU   A 1 130 ? 5.73408   -46.78079 8.81970   1.000 113.20258 ? 131 LEU   A N      1 
ATOM   1713 C CA     . LEU   A 1 130 ? 5.59135   -45.37701 8.44865   1.000 112.53831 ? 131 LEU   A CA     1 
ATOM   1714 C C      . LEU   A 1 130 ? 5.34633   -45.22584 6.95337   1.000 117.97827 ? 131 LEU   A C      1 
ATOM   1715 O O      . LEU   A 1 130 ? 4.50209   -44.42596 6.53209   1.000 119.70336 ? 131 LEU   A O      1 
ATOM   1716 C CB     . LEU   A 1 130 ? 6.83725   -44.60123 8.86900   1.000 115.04394 ? 131 LEU   A CB     1 
ATOM   1717 C CG     . LEU   A 1 130 ? 6.81271   -43.09400 8.61645   1.000 126.23883 ? 131 LEU   A CG     1 
ATOM   1718 C CD1    . LEU   A 1 130 ? 5.66514   -42.43804 9.36374   1.000 117.52162 ? 131 LEU   A CD1    1 
ATOM   1719 C CD2    . LEU   A 1 130 ? 8.14146   -42.46883 9.01825   1.000 120.80145 ? 131 LEU   A CD2    1 
ATOM   1720 H H      . LEU   A 1 130 ? 6.50486   -46.99069 9.13819   1.000 136.23357 ? 131 LEU   A H      1 
ATOM   1721 H HA     . LEU   A 1 130 ? 4.82887   -45.00241 8.91683   1.000 135.43644 ? 131 LEU   A HA     1 
ATOM   1722 H HB2    . LEU   A 1 130 ? 6.96491   -44.72955 9.82196   1.000 138.44320 ? 131 LEU   A HB2    1 
ATOM   1723 H HB3    . LEU   A 1 130 ? 7.59485   -44.96067 8.38141   1.000 138.44320 ? 131 LEU   A HB3    1 
ATOM   1724 H HG     . LEU   A 1 130 ? 6.67597   -42.93642 7.66915   1.000 151.87706 ? 131 LEU   A HG     1 
ATOM   1725 H HD11   . LEU   A 1 130 ? 5.76279   -41.47449 9.30958   1.000 141.41642 ? 131 LEU   A HD11   1 
ATOM   1726 H HD12   . LEU   A 1 130 ? 4.82738   -42.70901 8.95678   1.000 141.41642 ? 131 LEU   A HD12   1 
ATOM   1727 H HD13   . LEU   A 1 130 ? 5.68926   -42.72135 10.29114  1.000 141.41642 ? 131 LEU   A HD13   1 
ATOM   1728 H HD21   . LEU   A 1 130 ? 8.15480   -41.54278 8.72990   1.000 145.35221 ? 131 LEU   A HD21   1 
ATOM   1729 H HD22   . LEU   A 1 130 ? 8.23403   -42.51634 9.98266   1.000 145.35221 ? 131 LEU   A HD22   1 
ATOM   1730 H HD23   . LEU   A 1 130 ? 8.86244   -42.95834 8.59224   1.000 145.35221 ? 131 LEU   A HD23   1 
ATOM   1731 N N      . ARG   A 1 131 ? 6.08373   -45.97900 6.13401   1.000 126.31281 ? 132 ARG   A N      1 
ATOM   1732 C CA     . ARG   A 1 131 ? 5.83563   -45.96479 4.69643   1.000 126.13647 ? 132 ARG   A CA     1 
ATOM   1733 C C      . ARG   A 1 131 ? 4.39970   -46.36439 4.38426   1.000 123.75335 ? 132 ARG   A C      1 
ATOM   1734 O O      . ARG   A 1 131 ? 3.76661   -45.78948 3.49072   1.000 131.31810 ? 132 ARG   A O      1 
ATOM   1735 C CB     . ARG   A 1 131 ? 6.81752   -46.89927 3.98771   1.000 124.16386 ? 132 ARG   A CB     1 
ATOM   1736 C CG     . ARG   A 1 131 ? 6.37869   -47.32653 2.59534   1.000 112.82998 ? 132 ARG   A CG     1 
ATOM   1737 C CD     . ARG   A 1 131 ? 7.49459   -48.04195 1.84540   1.000 122.93584 ? 132 ARG   A CD     1 
ATOM   1738 N NE     . ARG   A 1 131 ? 8.46356   -47.10671 1.28480   1.000 132.07885 ? 132 ARG   A NE     1 
ATOM   1739 C CZ     . ARG   A 1 131 ? 9.46996   -47.45174 0.49238   1.000 143.42051 ? 132 ARG   A CZ     1 
ATOM   1740 N NH1    . ARG   A 1 131 ? 9.69159   -48.71506 0.16534   1.000 133.91784 ? 132 ARG   A NH1    1 
ATOM   1741 N NH2    . ARG   A 1 131 ? 10.27097  -46.50473 0.01161   1.000 140.29658 ? 132 ARG   A NH2    1 
ATOM   1742 H H      . ARG   A 1 131 ? 6.72284   -46.49788 6.38281   1.000 151.96585 ? 132 ARG   A H      1 
ATOM   1743 H HA     . ARG   A 1 131 ? 5.97899   -45.06593 4.36118   1.000 151.75423 ? 132 ARG   A HA     1 
ATOM   1744 H HB2    . ARG   A 1 131 ? 7.67009   -46.44486 3.90084   1.000 149.38710 ? 132 ARG   A HB2    1 
ATOM   1745 H HB3    . ARG   A 1 131 ? 6.92231   -47.70188 4.52226   1.000 149.38710 ? 132 ARG   A HB3    1 
ATOM   1746 H HG2    . ARG   A 1 131 ? 5.62517   -47.93289 2.66911   1.000 135.78645 ? 132 ARG   A HG2    1 
ATOM   1747 H HG3    . ARG   A 1 131 ? 6.12436   -46.54187 2.08492   1.000 135.78645 ? 132 ARG   A HG3    1 
ATOM   1748 H HD2    . ARG   A 1 131 ? 7.96219   -48.63256 2.45649   1.000 147.91348 ? 132 ARG   A HD2    1 
ATOM   1749 H HD3    . ARG   A 1 131 ? 7.11160   -48.55457 1.11641   1.000 147.91348 ? 132 ARG   A HD3    1 
ATOM   1750 H HE     . ARG   A 1 131 ? 8.37636   -46.27408 1.48161   1.000 158.88510 ? 132 ARG   A HE     1 
ATOM   1751 H HH11   . ARG   A 1 131 ? 9.17724   -49.33421 0.46813   1.000 161.09187 ? 132 ARG   A HH11   1 
ATOM   1752 H HH12   . ARG   A 1 131 ? 10.34995  -48.91670 -0.34994  1.000 161.09187 ? 132 ARG   A HH12   1 
ATOM   1753 H HH21   . ARG   A 1 131 ? 10.13317  -45.68068 0.21544   1.000 168.74636 ? 132 ARG   A HH21   1 
ATOM   1754 H HH22   . ARG   A 1 131 ? 10.92661  -46.71655 -0.50304  1.000 168.74636 ? 132 ARG   A HH22   1 
ATOM   1755 N N      . THR   A 1 132 ? 3.86475   -47.34277 5.11596   1.000 122.34529 ? 133 THR   A N      1 
ATOM   1756 C CA     . THR   A 1 132 ? 2.53074   -47.84589 4.81072   1.000 124.46688 ? 133 THR   A CA     1 
ATOM   1757 C C      . THR   A 1 132 ? 1.45823   -46.81155 5.13188   1.000 126.50238 ? 133 THR   A C      1 
ATOM   1758 O O      . THR   A 1 132 ? 0.54296   -46.58934 4.33230   1.000 135.58684 ? 133 THR   A O      1 
ATOM   1759 C CB     . THR   A 1 132 ? 2.27117   -49.14603 5.57075   1.000 136.26722 ? 133 THR   A CB     1 
ATOM   1760 O OG1    . THR   A 1 132 ? 3.17371   -50.15879 5.10814   1.000 133.22015 ? 133 THR   A OG1    1 
ATOM   1761 C CG2    . THR   A 1 132 ? 0.83604   -49.61425 5.36202   1.000 149.98023 ? 133 THR   A CG2    1 
ATOM   1762 H H      . THR   A 1 132 ? 4.24876   -47.72521 5.78369   1.000 147.20482 ? 133 THR   A H      1 
ATOM   1763 H HA     . THR   A 1 132 ? 2.48448   -48.03783 3.86103   1.000 149.75072 ? 133 THR   A HA     1 
ATOM   1764 H HB     . THR   A 1 132 ? 2.40739   -48.99828 6.51970   1.000 163.91113 ? 133 THR   A HB     1 
ATOM   1765 H HG1    . THR   A 1 132 ? 3.96697   -49.89314 5.18410   1.000 160.25465 ? 133 THR   A HG1    1 
ATOM   1766 H HG21   . THR   A 1 132 ? 0.75108   -50.54667 5.61555   1.000 180.36674 ? 133 THR   A HG21   1 
ATOM   1767 H HG22   . THR   A 1 132 ? 0.23182   -49.08409 5.90493   1.000 180.36674 ? 133 THR   A HG22   1 
ATOM   1768 H HG23   . THR   A 1 132 ? 0.58794   -49.51778 4.42926   1.000 180.36674 ? 133 THR   A HG23   1 
ATOM   1769 N N      . ILE   A 1 133 ? 1.54761   -46.16607 6.29802   1.000 115.03713 ? 134 ILE   A N      1 
ATOM   1770 C CA     . ILE   A 1 133 ? 0.52458   -45.18834 6.65521   1.000 117.57119 ? 134 ILE   A CA     1 
ATOM   1771 C C      . ILE   A 1 133 ? 0.59639   -43.98269 5.72773   1.000 133.23108 ? 134 ILE   A C      1 
ATOM   1772 O O      . ILE   A 1 133 ? -0.43208  -43.39998 5.36512   1.000 155.91869 ? 134 ILE   A O      1 
ATOM   1773 C CB     . ILE   A 1 133 ? 0.65076   -44.77477 8.13284   1.000 138.44359 ? 134 ILE   A CB     1 
ATOM   1774 C CG1    . ILE   A 1 133 ? 1.95257   -44.01247 8.38987   1.000 144.46436 ? 134 ILE   A CG1    1 
ATOM   1775 C CG2    . ILE   A 1 133 ? 0.57246   -46.00214 9.02523   1.000 145.37142 ? 134 ILE   A CG2    1 
ATOM   1776 C CD1    . ILE   A 1 133 ? 2.01334   -43.37269 9.76823   1.000 148.49538 ? 134 ILE   A CD1    1 
ATOM   1777 H H      . ILE   A 1 133 ? 2.17144   -46.27402 6.88006   1.000 138.43502 ? 134 ILE   A H      1 
ATOM   1778 H HA     . ILE   A 1 133 ? -0.34351  -45.60628 6.54269   1.000 141.47590 ? 134 ILE   A HA     1 
ATOM   1779 H HB     . ILE   A 1 133 ? -0.08685  -44.17985 8.34000   1.000 166.52277 ? 134 ILE   A HB     1 
ATOM   1780 H HG12   . ILE   A 1 133 ? 2.69731   -44.62940 8.31467   1.000 173.74771 ? 134 ILE   A HG12   1 
ATOM   1781 H HG13   . ILE   A 1 133 ? 2.03834   -43.30685 7.72984   1.000 173.74771 ? 134 ILE   A HG13   1 
ATOM   1782 H HG21   . ILE   A 1 133 ? 0.50003   -45.71654 9.94940   1.000 174.83618 ? 134 ILE   A HG21   1 
ATOM   1783 H HG22   . ILE   A 1 133 ? -0.20747  -46.52315 8.77794   1.000 174.83618 ? 134 ILE   A HG22   1 
ATOM   1784 H HG23   . ILE   A 1 133 ? 1.37599   -46.53196 8.90476   1.000 174.83618 ? 134 ILE   A HG23   1 
ATOM   1785 H HD11   . ILE   A 1 133 ? 2.86143   -42.91204 9.86547   1.000 178.58493 ? 134 ILE   A HD11   1 
ATOM   1786 H HD12   . ILE   A 1 133 ? 1.28209   -42.74144 9.85591   1.000 178.58493 ? 134 ILE   A HD12   1 
ATOM   1787 H HD13   . ILE   A 1 133 ? 1.93437   -44.06604 10.44198  1.000 178.58493 ? 134 ILE   A HD13   1 
ATOM   1788 N N      . LEU   A 1 134 ? 1.80659   -43.58992 5.32580   1.000 127.51941 ? 135 LEU   A N      1 
ATOM   1789 C CA     . LEU   A 1 134 ? 1.94480   -42.47195 4.39910   1.000 127.08208 ? 135 LEU   A CA     1 
ATOM   1790 C C      . LEU   A 1 134 ? 1.35166   -42.82265 3.04074   1.000 129.24389 ? 135 LEU   A C      1 
ATOM   1791 O O      . LEU   A 1 134 ? 0.58168   -42.04318 2.46768   1.000 128.04961 ? 135 LEU   A O      1 
ATOM   1792 C CB     . LEU   A 1 134 ? 3.41627   -42.08020 4.26959   1.000 119.89614 ? 135 LEU   A CB     1 
ATOM   1793 C CG     . LEU   A 1 134 ? 4.03823   -41.45761 5.52147   1.000 114.96433 ? 135 LEU   A CG     1 
ATOM   1794 C CD1    . LEU   A 1 134 ? 5.55446   -41.44222 5.42918   1.000 107.79917 ? 135 LEU   A CD1    1 
ATOM   1795 C CD2    . LEU   A 1 134 ? 3.50778   -40.04738 5.73077   1.000 123.99858 ? 135 LEU   A CD2    1 
ATOM   1796 H H      . LEU   A 1 134 ? 2.54874   -43.94846 5.57131   1.000 153.41376 ? 135 LEU   A H      1 
ATOM   1797 H HA     . LEU   A 1 134 ? 1.46454   -41.70525 4.74900   1.000 152.88896 ? 135 LEU   A HA     1 
ATOM   1798 H HB2    . LEU   A 1 134 ? 3.92689   -42.87708 4.05713   1.000 144.26583 ? 135 LEU   A HB2    1 
ATOM   1799 H HB3    . LEU   A 1 134 ? 3.49790   -41.43272 3.55195   1.000 144.26583 ? 135 LEU   A HB3    1 
ATOM   1800 H HG     . LEU   A 1 134 ? 3.79349   -41.99690 6.28970   1.000 138.34767 ? 135 LEU   A HG     1 
ATOM   1801 H HD11   . LEU   A 1 134 ? 5.91837   -41.11074 6.26500   1.000 129.74947 ? 135 LEU   A HD11   1 
ATOM   1802 H HD12   . LEU   A 1 134 ? 5.87008   -42.34477 5.26583   1.000 129.74947 ? 135 LEU   A HD12   1 
ATOM   1803 H HD13   . LEU   A 1 134 ? 5.82053   -40.86155 4.69916   1.000 129.74947 ? 135 LEU   A HD13   1 
ATOM   1804 H HD21   . LEU   A 1 134 ? 3.93323   -39.66281 6.51307   1.000 149.18876 ? 135 LEU   A HD21   1 
ATOM   1805 H HD22   . LEU   A 1 134 ? 3.71213   -39.51356 4.94707   1.000 149.18876 ? 135 LEU   A HD22   1 
ATOM   1806 H HD23   . LEU   A 1 134 ? 2.54761   -40.08746 5.86252   1.000 149.18876 ? 135 LEU   A HD23   1 
ATOM   1807 N N      . LEU   A 1 135 ? 1.68940   -44.00305 2.51502   1.000 132.49824 ? 136 LEU   A N      1 
ATOM   1808 C CA     . LEU   A 1 135 ? 1.09885   -44.44306 1.25584   1.000 128.40854 ? 136 LEU   A CA     1 
ATOM   1809 C C      . LEU   A 1 135 ? -0.42128  -44.48052 1.34749   1.000 129.50645 ? 136 LEU   A C      1 
ATOM   1810 O O      . LEU   A 1 135 ? -1.11779  -44.03846 0.42635   1.000 139.99176 ? 136 LEU   A O      1 
ATOM   1811 C CB     . LEU   A 1 135 ? 1.64157   -45.81995 0.86933   1.000 126.07251 ? 136 LEU   A CB     1 
ATOM   1812 C CG     . LEU   A 1 135 ? 3.08917   -45.88741 0.37793   1.000 134.64508 ? 136 LEU   A CG     1 
ATOM   1813 C CD1    . LEU   A 1 135 ? 3.51983   -47.33371 0.15975   1.000 122.98157 ? 136 LEU   A CD1    1 
ATOM   1814 C CD2    . LEU   A 1 135 ? 3.26481   -45.08555 -0.90160  1.000 150.72879 ? 136 LEU   A CD2    1 
ATOM   1815 H H      . LEU   A 1 135 ? 2.24826   -44.55644 2.86291   1.000 159.38836 ? 136 LEU   A H      1 
ATOM   1816 H HA     . LEU   A 1 135 ? 1.34807   -43.81551 0.55945   1.000 154.48072 ? 136 LEU   A HA     1 
ATOM   1817 H HB2    . LEU   A 1 135 ? 1.58132   -46.39350 1.64927   1.000 151.67748 ? 136 LEU   A HB2    1 
ATOM   1818 H HB3    . LEU   A 1 135 ? 1.08492   -46.17006 0.15626   1.000 151.67748 ? 136 LEU   A HB3    1 
ATOM   1819 H HG     . LEU   A 1 135 ? 3.66293   -45.50000 1.05735   1.000 161.96457 ? 136 LEU   A HG     1 
ATOM   1820 H HD11   . LEU   A 1 135 ? 4.44960   -47.34814 -0.11631  1.000 147.96836 ? 136 LEU   A HD11   1 
ATOM   1821 H HD12   . LEU   A 1 135 ? 3.41373   -47.82351 0.99026   1.000 147.96836 ? 136 LEU   A HD12   1 
ATOM   1822 H HD13   . LEU   A 1 135 ? 2.96375   -47.72813 -0.53025  1.000 147.96836 ? 136 LEU   A HD13   1 
ATOM   1823 H HD21   . LEU   A 1 135 ? 4.16560   -45.21799 -1.23616  1.000 181.26502 ? 136 LEU   A HD21   1 
ATOM   1824 H HD22   . LEU   A 1 135 ? 2.61977   -45.39259 -1.55777  1.000 181.26502 ? 136 LEU   A HD22   1 
ATOM   1825 H HD23   . LEU   A 1 135 ? 3.11851   -44.14633 -0.70829  1.000 181.26502 ? 136 LEU   A HD23   1 
ATOM   1826 N N      . ASN   A 1 136 ? -0.95542  -44.99905 2.45639   1.000 130.41835 ? 137 ASN   A N      1 
ATOM   1827 C CA     . ASN   A 1 136 ? -2.40352  -45.12035 2.58715   1.000 147.73891 ? 137 ASN   A CA     1 
ATOM   1828 C C      . ASN   A 1 136 ? -3.08632  -43.75941 2.59138   1.000 147.13543 ? 137 ASN   A C      1 
ATOM   1829 O O      . ASN   A 1 136 ? -4.25888  -43.65336 2.21286   1.000 134.05967 ? 137 ASN   A O      1 
ATOM   1830 C CB     . ASN   A 1 136 ? -2.75230  -45.89436 3.85827   1.000 136.39959 ? 137 ASN   A CB     1 
ATOM   1831 C CG     . ASN   A 1 136 ? -2.45509  -47.37476 3.73543   1.000 130.54656 ? 137 ASN   A CG     1 
ATOM   1832 O OD1    . ASN   A 1 136 ? -2.34042  -47.90604 2.63054   1.000 143.48590 ? 137 ASN   A OD1    1 
ATOM   1833 N ND2    . ASN   A 1 136 ? -2.33534  -48.05146 4.87120   1.000 138.24558 ? 137 ASN   A ND2    1 
ATOM   1834 H H      . ASN   A 1 136 ? -0.50794  -45.28228 3.13399   1.000 156.89249 ? 137 ASN   A H      1 
ATOM   1835 H HA     . ASN   A 1 136 ? -2.74242  -45.62020 1.82808   1.000 177.67717 ? 137 ASN   A HA     1 
ATOM   1836 H HB2    . ASN   A 1 136 ? -2.23073  -45.54286 4.59673   1.000 164.06998 ? 137 ASN   A HB2    1 
ATOM   1837 H HB3    . ASN   A 1 136 ? -3.69912  -45.79166 4.04233   1.000 164.06998 ? 137 ASN   A HB3    1 
ATOM   1838 H HD21   . ASN   A 1 136 ? -2.16678  -48.89459 4.85366   1.000 166.28516 ? 137 ASN   A HD21   1 
ATOM   1839 H HD22   . ASN   A 1 136 ? -2.42632  -47.64671 5.62452   1.000 166.28516 ? 137 ASN   A HD22   1 
ATOM   1840 N N      . SER   A 1 137 ? -2.37881  -42.71153 3.01164   1.000 134.30917 ? 138 SER   A N      1 
ATOM   1841 C CA     . SER   A 1 137 ? -2.94255  -41.36901 2.99905   1.000 140.84047 ? 138 SER   A CA     1 
ATOM   1842 C C      . SER   A 1 137 ? -2.93291  -40.74107 1.61163   1.000 148.71600 ? 138 SER   A C      1 
ATOM   1843 O O      . SER   A 1 137 ? -3.55925  -39.69276 1.41939   1.000 138.52222 ? 138 SER   A O      1 
ATOM   1844 C CB     . SER   A 1 137 ? -2.17672  -40.47061 3.97313   1.000 152.15926 ? 138 SER   A CB     1 
ATOM   1845 O OG     . SER   A 1 137 ? -0.88052  -40.17177 3.48494   1.000 143.58303 ? 138 SER   A OG     1 
ATOM   1846 H H      . SER   A 1 137 ? -1.57244  -42.75459 3.30748   1.000 161.56148 ? 138 SER   A H      1 
ATOM   1847 H HA     . SER   A 1 137 ? -3.86387  -41.41444 3.29904   1.000 169.39904 ? 138 SER   A HA     1 
ATOM   1848 H HB2    . SER   A 1 137 ? -2.66769  -39.64205 4.08860   1.000 182.98159 ? 138 SER   A HB2    1 
ATOM   1849 H HB3    . SER   A 1 137 ? -2.09403  -40.92861 4.82418   1.000 182.98159 ? 138 SER   A HB3    1 
ATOM   1850 H HG     . SER   A 1 137 ? -0.50995  -39.60496 3.98193   1.000 172.69010 ? 138 SER   A HG     1 
ATOM   1851 N N      . LEU   A 1 138 ? -2.24480  -41.35058 0.65181   1.000 143.88446 ? 139 LEU   A N      1 
ATOM   1852 C CA     . LEU   A 1 138 ? -2.18979  -40.85121 -0.71166  1.000 143.68022 ? 139 LEU   A CA     1 
ATOM   1853 C C      . LEU   A 1 138 ? -3.24687  -41.53371 -1.57398  1.000 149.33009 ? 139 LEU   A C      1 
ATOM   1854 O O      . LEU   A 1 138 ? -3.69816  -42.64537 -1.28778  1.000 151.42741 ? 139 LEU   A O      1 
ATOM   1855 C CB     . LEU   A 1 138 ? -0.80496  -41.08671 -1.31583  1.000 139.81775 ? 139 LEU   A CB     1 
ATOM   1856 C CG     . LEU   A 1 138 ? 0.38769   -40.50525 -0.55772  1.000 137.86334 ? 139 LEU   A CG     1 
ATOM   1857 C CD1    . LEU   A 1 138 ? 1.68659   -40.86063 -1.26229  1.000 134.42522 ? 139 LEU   A CD1    1 
ATOM   1858 C CD2    . LEU   A 1 138 ? 0.25533   -39.00124 -0.41144  1.000 145.74711 ? 139 LEU   A CD2    1 
ATOM   1859 H H      . LEU   A 1 138 ? -1.79171  -42.07179 0.77077   1.000 173.05182 ? 139 LEU   A H      1 
ATOM   1860 H HA     . LEU   A 1 138 ? -2.36368  -39.89693 -0.70768  1.000 172.80673 ? 139 LEU   A HA     1 
ATOM   1861 H HB2    . LEU   A 1 138 ? -0.66355  -42.04453 -1.37487  1.000 168.17178 ? 139 LEU   A HB2    1 
ATOM   1862 H HB3    . LEU   A 1 138 ? -0.79528  -40.69462 -2.20300  1.000 168.17178 ? 139 LEU   A HB3    1 
ATOM   1863 H HG     . LEU   A 1 138 ? 0.40926   -40.88828 0.33319   1.000 165.82648 ? 139 LEU   A HG     1 
ATOM   1864 H HD11   . LEU   A 1 138 ? 2.42797   -40.47000 -0.77376  1.000 161.70074 ? 139 LEU   A HD11   1 
ATOM   1865 H HD12   . LEU   A 1 138 ? 1.77864   -41.82594 -1.28690  1.000 161.70074 ? 139 LEU   A HD12   1 
ATOM   1866 H HD13   . LEU   A 1 138 ? 1.66284   -40.50748 -2.16540  1.000 161.70074 ? 139 LEU   A HD13   1 
ATOM   1867 H HD21   . LEU   A 1 138 ? 1.06805   -38.64973 -0.01544  1.000 175.28700 ? 139 LEU   A HD21   1 
ATOM   1868 H HD22   . LEU   A 1 138 ? 0.11831   -38.60952 -1.28818  1.000 175.28700 ? 139 LEU   A HD22   1 
ATOM   1869 H HD23   . LEU   A 1 138 ? -0.50304  -38.80512 0.16067   1.000 175.28700 ? 139 LEU   A HD23   1 
ATOM   1870 N N      . GLN   A 1 139 ? -3.63882  -40.84690 -2.64323  1.000 151.31256 ? 140 GLN   A N      1 
ATOM   1871 C CA     . GLN   A 1 139 ? -4.53447  -41.43987 -3.62448  1.000 154.51503 ? 140 GLN   A CA     1 
ATOM   1872 C C      . GLN   A 1 139 ? -3.81915  -42.55043 -4.38639  1.000 155.39689 ? 140 GLN   A C      1 
ATOM   1873 O O      . GLN   A 1 139 ? -2.59251  -42.55233 -4.52314  1.000 149.76472 ? 140 GLN   A O      1 
ATOM   1874 C CB     . GLN   A 1 139 ? -5.04198  -40.37492 -4.59480  1.000 152.80872 ? 140 GLN   A CB     1 
ATOM   1875 C CG     . GLN   A 1 139 ? -5.94814  -39.33678 -3.94959  1.000 156.70516 ? 140 GLN   A CG     1 
ATOM   1876 C CD     . GLN   A 1 139 ? -6.38159  -38.25599 -4.92046  1.000 160.14602 ? 140 GLN   A CD     1 
ATOM   1877 O OE1    . GLN   A 1 139 ? -5.70574  -37.99153 -5.91517  1.000 161.32344 ? 140 GLN   A OE1    1 
ATOM   1878 N NE2    . GLN   A 1 139 ? -7.51718  -37.62732 -4.63821  1.000 164.43844 ? 140 GLN   A NE2    1 
ATOM   1879 H H      . GLN   A 1 139 ? -3.40059  -40.03995 -2.82122  1.000 181.96554 ? 140 GLN   A H      1 
ATOM   1880 H HA     . GLN   A 1 139 ? -5.30475  -41.82366 -3.17697  1.000 185.80851 ? 140 GLN   A HA     1 
ATOM   1881 H HB2    . GLN   A 1 139 ? -4.27966  -39.90859 -4.97203  1.000 183.76093 ? 140 GLN   A HB2    1 
ATOM   1882 H HB3    . GLN   A 1 139 ? -5.54632  -40.81065 -5.29956  1.000 183.76093 ? 140 GLN   A HB3    1 
ATOM   1883 H HG2    . GLN   A 1 139 ? -6.74504  -39.77674 -3.61449  1.000 188.43666 ? 140 GLN   A HG2    1 
ATOM   1884 H HG3    . GLN   A 1 139 ? -5.47216  -38.91127 -3.21933  1.000 188.43666 ? 140 GLN   A HG3    1 
ATOM   1885 H HE21   . GLN   A 1 139 ? -7.96395  -37.84140 -3.93524  1.000 197.71660 ? 140 GLN   A HE21   1 
ATOM   1886 H HE22   . GLN   A 1 139 ? -7.80561  -37.00621 -5.15843  1.000 197.71660 ? 140 GLN   A HE22   1 
ATOM   1887 N N      . ASN   A 1 140 ? -4.60297  -43.50371 -4.88413  1.000 165.60171 ? 141 ASN   A N      1 
ATOM   1888 C CA     . ASN   A 1 140 ? -4.02946  -44.65987 -5.55837  1.000 160.22280 ? 141 ASN   A CA     1 
ATOM   1889 C C      . ASN   A 1 140 ? -3.12769  -44.22468 -6.70605  1.000 151.07274 ? 141 ASN   A C      1 
ATOM   1890 O O      . ASN   A 1 140 ? -3.42963  -43.27475 -7.43364  1.000 156.44588 ? 141 ASN   A O      1 
ATOM   1891 C CB     . ASN   A 1 140 ? -5.13858  -45.57536 -6.07897  1.000 157.19868 ? 141 ASN   A CB     1 
ATOM   1892 C CG     . ASN   A 1 140 ? -5.82243  -46.34947 -4.96928  1.000 161.40932 ? 141 ASN   A CG     1 
ATOM   1893 O OD1    . ASN   A 1 140 ? -5.31794  -47.37495 -4.51139  1.000 167.00216 ? 141 ASN   A OD1    1 
ATOM   1894 N ND2    . ASN   A 1 140 ? -6.97704  -45.86222 -4.53095  1.000 157.24773 ? 141 ASN   A ND2    1 
ATOM   1895 H H      . ASN   A 1 140 ? -5.46204  -43.50356 -4.84426  1.000 199.11252 ? 141 ASN   A H      1 
ATOM   1896 H HA     . ASN   A 1 140 ? -3.49268  -45.16216 -4.92554  1.000 192.65783 ? 141 ASN   A HA     1 
ATOM   1897 H HB2    . ASN   A 1 140 ? -5.80924  -45.03707 -6.52768  1.000 189.02889 ? 141 ASN   A HB2    1 
ATOM   1898 H HB3    . ASN   A 1 140 ? -4.75621  -46.21468 -6.70023  1.000 189.02889 ? 141 ASN   A HB3    1 
ATOM   1899 H HD21   . ASN   A 1 140 ? -7.40321  -46.26586 -3.90242  1.000 189.08775 ? 141 ASN   A HD21   1 
ATOM   1900 H HD22   . ASN   A 1 140 ? -7.29877  -45.14295 -4.87554  1.000 189.08775 ? 141 ASN   A HD22   1 
ATOM   1901 N N      . ASP   A 1 141 ? -2.00504  -44.92631 -6.85503  1.000 150.10276 ? 142 ASP   A N      1 
ATOM   1902 C CA     . ASP   A 1 141 ? -1.05135  -44.71576 -7.93781  1.000 152.64899 ? 142 ASP   A CA     1 
ATOM   1903 C C      . ASP   A 1 141 ? -0.35902  -43.36187 -7.86339  1.000 144.38371 ? 142 ASP   A C      1 
ATOM   1904 O O      . ASP   A 1 141 ? 0.15041   -42.87039 -8.87585  1.000 147.84058 ? 142 ASP   A O      1 
ATOM   1905 C CB     . ASP   A 1 141 ? -1.73068  -44.87765 -9.30216  1.000 155.80738 ? 142 ASP   A CB     1 
ATOM   1906 C CG     . ASP   A 1 141 ? -2.32227  -46.25897 -9.49409  1.000 154.15992 ? 142 ASP   A CG     1 
ATOM   1907 O OD1    . ASP   A 1 141 ? -1.63370  -47.24922 -9.16956  1.000 145.41279 ? 142 ASP   A OD1    1 
ATOM   1908 O OD2    . ASP   A 1 141 ? -3.47769  -46.35524 -9.95857  1.000 176.38377 ? 142 ASP   A OD2    1 
ATOM   1909 H H      . ASP   A 1 141 ? -1.76708  -45.55456 -6.31811  1.000 180.51378 ? 142 ASP   A H      1 
ATOM   1910 H HA     . ASP   A 1 141 ? -0.35788  -45.38943 -7.85928  1.000 183.56926 ? 142 ASP   A HA     1 
ATOM   1911 H HB2    . ASP   A 1 141 ? -2.44831  -44.22947 -9.37809  1.000 187.35932 ? 142 ASP   A HB2    1 
ATOM   1912 H HB3    . ASP   A 1 141 ? -1.07547  -44.73072 -10.00217 1.000 187.35932 ? 142 ASP   A HB3    1 
ATOM   1913 N N      . THR   A 1 142 ? -0.32742  -42.73972 -6.68322  1.000 145.85340 ? 143 THR   A N      1 
ATOM   1914 C CA     . THR   A 1 142 ? 0.44753   -41.51452 -6.52488  1.000 144.40580 ? 143 THR   A CA     1 
ATOM   1915 C C      . THR   A 1 142 ? 1.94356   -41.79237 -6.59248  1.000 132.19014 ? 143 THR   A C      1 
ATOM   1916 O O      . THR   A 1 142 ? 2.71653   -40.92641 -7.01786  1.000 130.45875 ? 143 THR   A O      1 
ATOM   1917 C CB     . THR   A 1 142 ? 0.10073   -40.83701 -5.19956  1.000 149.16022 ? 143 THR   A CB     1 
ATOM   1918 O OG1    . THR   A 1 142 ? -1.29436  -40.51050 -5.17727  1.000 154.50811 ? 143 THR   A OG1    1 
ATOM   1919 C CG2    . THR   A 1 142 ? 0.92163   -39.56851 -5.01443  1.000 152.09598 ? 143 THR   A CG2    1 
ATOM   1920 H H      . THR   A 1 142 ? -0.73784  -43.00223 -5.97453  1.000 175.41455 ? 143 THR   A H      1 
ATOM   1921 H HA     . THR   A 1 142 ? 0.21583   -40.90475 -7.24280  1.000 173.67743 ? 143 THR   A HA     1 
ATOM   1922 H HB     . THR   A 1 142 ? 0.30280   -41.43917 -4.46644  1.000 179.38273 ? 143 THR   A HB     1 
ATOM   1923 H HG1    . THR   A 1 142 ? -1.75396  -41.20663 -5.27615  1.000 185.80021 ? 143 THR   A HG1    1 
ATOM   1924 H HG21   . THR   A 1 142 ? 0.54865   -39.03385 -4.29614  1.000 182.90565 ? 143 THR   A HG21   1 
ATOM   1925 H HG22   . THR   A 1 142 ? 1.83852   -39.79588 -4.79419  1.000 182.90565 ? 143 THR   A HG22   1 
ATOM   1926 H HG23   . THR   A 1 142 ? 0.91442   -39.04641 -5.83190  1.000 182.90565 ? 143 THR   A HG23   1 
ATOM   1927 N N      . VAL   A 1 143 ? 2.36561   -42.98389 -6.17859  1.000 127.99285 ? 144 VAL   A N      1 
ATOM   1928 C CA     . VAL   A 1 143 ? 3.76644   -43.38628 -6.20012  1.000 134.45402 ? 144 VAL   A CA     1 
ATOM   1929 C C      . VAL   A 1 143 ? 3.97691   -44.33901 -7.36776  1.000 132.68393 ? 144 VAL   A C      1 
ATOM   1930 O O      . VAL   A 1 143 ? 3.23010   -45.31347 -7.52658  1.000 127.01568 ? 144 VAL   A O      1 
ATOM   1931 C CB     . VAL   A 1 143 ? 4.17397   -44.04883 -4.87251  1.000 155.53303 ? 144 VAL   A CB     1 
ATOM   1932 C CG1    . VAL   A 1 143 ? 5.58580   -44.61065 -4.96648  1.000 142.98948 ? 144 VAL   A CG1    1 
ATOM   1933 C CG2    . VAL   A 1 143 ? 4.06410   -43.05655 -3.72194  1.000 143.89540 ? 144 VAL   A CG2    1 
ATOM   1934 H H      . VAL   A 1 143 ? 1.84237   -43.59367 -5.87200  1.000 153.98189 ? 144 VAL   A H      1 
ATOM   1935 H HA     . VAL   A 1 143 ? 4.32323   -42.60388 -6.33698  1.000 161.73529 ? 144 VAL   A HA     1 
ATOM   1936 H HB     . VAL   A 1 143 ? 3.56865   -44.78507 -4.69240  1.000 187.03010 ? 144 VAL   A HB     1 
ATOM   1937 H HG11   . VAL   A 1 143 ? 5.90153   -44.82225 -4.07404  1.000 171.97784 ? 144 VAL   A HG11   1 
ATOM   1938 H HG12   . VAL   A 1 143 ? 5.57069   -45.41328 -5.51096  1.000 171.97784 ? 144 VAL   A HG12   1 
ATOM   1939 H HG13   . VAL   A 1 143 ? 6.16375   -43.94606 -5.37291  1.000 171.97784 ? 144 VAL   A HG13   1 
ATOM   1940 H HG21   . VAL   A 1 143 ? 4.13525   -43.53727 -2.88245  1.000 173.06495 ? 144 VAL   A HG21   1 
ATOM   1941 H HG22   . VAL   A 1 143 ? 4.78238   -42.40865 -3.79400  1.000 173.06495 ? 144 VAL   A HG22   1 
ATOM   1942 H HG23   . VAL   A 1 143 ? 3.20634   -42.60660 -3.77378  1.000 173.06495 ? 144 VAL   A HG23   1 
ATOM   1943 N N      . ILE   A 1 144 ? 4.99338   -44.06466 -8.17973  1.000 131.81999 ? 145 ILE   A N      1 
ATOM   1944 C CA     . ILE   A 1 144 ? 5.34320   -44.90191 -9.32099  1.000 130.51986 ? 145 ILE   A CA     1 
ATOM   1945 C C      . ILE   A 1 144 ? 6.59004   -45.69281 -8.95014  1.000 128.44998 ? 145 ILE   A C      1 
ATOM   1946 O O      . ILE   A 1 144 ? 7.68780   -45.13329 -8.85841  1.000 129.47875 ? 145 ILE   A O      1 
ATOM   1947 C CB     . ILE   A 1 144 ? 5.57833   -44.07020 -10.58789 1.000 144.09554 ? 145 ILE   A CB     1 
ATOM   1948 C CG1    . ILE   A 1 144 ? 4.43958   -43.06928 -10.79540 1.000 139.95237 ? 145 ILE   A CG1    1 
ATOM   1949 C CG2    . ILE   A 1 144 ? 5.71886   -44.98638 -11.79531 1.000 152.02251 ? 145 ILE   A CG2    1 
ATOM   1950 C CD1    . ILE   A 1 144 ? 3.05591   -43.69054 -10.79626 1.000 141.80840 ? 145 ILE   A CD1    1 
ATOM   1951 H H      . ILE   A 1 144 ? 5.50743   -43.38150 -8.08678  1.000 158.57446 ? 145 ILE   A H      1 
ATOM   1952 H HA     . ILE   A 1 144 ? 4.61769   -45.52320 -9.48989  1.000 157.01430 ? 145 ILE   A HA     1 
ATOM   1953 H HB     . ILE   A 1 144 ? 6.40185   -43.56920 -10.47970 1.000 173.30511 ? 145 ILE   A HB     1 
ATOM   1954 H HG12   . ILE   A 1 144 ? 4.46760   -42.41524 -10.07961 1.000 168.33332 ? 145 ILE   A HG12   1 
ATOM   1955 H HG13   . ILE   A 1 144 ? 4.56507   -42.63014 -11.65115 1.000 168.33332 ? 145 ILE   A HG13   1 
ATOM   1956 H HG21   . ILE   A 1 144 ? 5.80178   -44.44409 -12.59527 1.000 182.81748 ? 145 ILE   A HG21   1 
ATOM   1957 H HG22   . ILE   A 1 144 ? 6.51065   -45.53565 -11.68450 1.000 182.81748 ? 145 ILE   A HG22   1 
ATOM   1958 H HG23   . ILE   A 1 144 ? 4.93162   -45.54965 -11.85766 1.000 182.81748 ? 145 ILE   A HG23   1 
ATOM   1959 H HD11   . ILE   A 1 144 ? 2.40432   -43.00999 -11.02688 1.000 170.56056 ? 145 ILE   A HD11   1 
ATOM   1960 H HD12   . ILE   A 1 144 ? 3.03170   -44.40672 -11.45002 1.000 170.56056 ? 145 ILE   A HD12   1 
ATOM   1961 H HD13   . ILE   A 1 144 ? 2.86742   -44.04296 -9.91242  1.000 170.56056 ? 145 ILE   A HD13   1 
ATOM   1962 N N      . TRP   A 1 145 ? 6.43000   -46.99733 -8.75738  1.000 130.92851 ? 146 TRP   A N      1 
ATOM   1963 C CA     . TRP   A 1 145 ? 7.53198   -47.83571 -8.31840  1.000 140.48782 ? 146 TRP   A CA     1 
ATOM   1964 C C      . TRP   A 1 145 ? 8.40948   -48.23592 -9.50274  1.000 138.13049 ? 146 TRP   A C      1 
ATOM   1965 O O      . TRP   A 1 145 ? 8.03803   -48.08965 -10.66976 1.000 130.70087 ? 146 TRP   A O      1 
ATOM   1966 C CB     . TRP   A 1 145 ? 6.99757   -49.07249 -7.59662  1.000 144.96669 ? 146 TRP   A CB     1 
ATOM   1967 C CG     . TRP   A 1 145 ? 6.14934   -48.73101 -6.40982  1.000 141.10250 ? 146 TRP   A CG     1 
ATOM   1968 C CD1    . TRP   A 1 145 ? 4.79610   -48.55029 -6.39197  1.000 150.09535 ? 146 TRP   A CD1    1 
ATOM   1969 C CD2    . TRP   A 1 145 ? 6.59977   -48.51747 -5.06741  1.000 139.78449 ? 146 TRP   A CD2    1 
ATOM   1970 N NE1    . TRP   A 1 145 ? 4.37650   -48.24016 -5.12086  1.000 126.33478 ? 146 TRP   A NE1    1 
ATOM   1971 C CE2    . TRP   A 1 145 ? 5.46477   -48.21425 -4.28906  1.000 131.70218 ? 146 TRP   A CE2    1 
ATOM   1972 C CE3    . TRP   A 1 145 ? 7.85206   -48.55466 -4.44760  1.000 138.88392 ? 146 TRP   A CE3    1 
ATOM   1973 C CZ2    . TRP   A 1 145 ? 5.54493   -47.95042 -2.92350  1.000 148.85011 ? 146 TRP   A CZ2    1 
ATOM   1974 C CZ3    . TRP   A 1 145 ? 7.92859   -48.29440 -3.09139  1.000 143.86263 ? 146 TRP   A CZ3    1 
ATOM   1975 C CH2    . TRP   A 1 145 ? 6.78290   -47.99300 -2.34508  1.000 147.59256 ? 146 TRP   A CH2    1 
ATOM   1976 H H      . TRP   A 1 145 ? 5.69021   -47.41983 -8.87486  1.000 157.50468 ? 146 TRP   A H      1 
ATOM   1977 H HA     . TRP   A 1 145 ? 8.08574   -47.33889 -7.69596  1.000 168.97585 ? 146 TRP   A HA     1 
ATOM   1978 H HB2    . TRP   A 1 145 ? 6.45599   -49.58877 -8.21390  1.000 174.35050 ? 146 TRP   A HB2    1 
ATOM   1979 H HB3    . TRP   A 1 145 ? 7.74655   -49.60533 -7.28675  1.000 174.35050 ? 146 TRP   A HB3    1 
ATOM   1980 H HD1    . TRP   A 1 145 ? 4.23906   -48.62612 -7.13282  1.000 180.50490 ? 146 TRP   A HD1    1 
ATOM   1981 H HE1    . TRP   A 1 145 ? 3.56349   -48.08728 -4.88581  1.000 151.99221 ? 146 TRP   A HE1    1 
ATOM   1982 H HE3    . TRP   A 1 145 ? 8.61816   -48.75041 -4.93716  1.000 167.05118 ? 146 TRP   A HE3    1 
ATOM   1983 H HZ2    . TRP   A 1 145 ? 4.78540   -47.75290 -2.42451  1.000 179.01060 ? 146 TRP   A HZ2    1 
ATOM   1984 H HZ3    . TRP   A 1 145 ? 8.75598   -48.32007 -2.66751  1.000 173.02563 ? 146 TRP   A HZ3    1 
ATOM   1985 H HH2    . TRP   A 1 145 ? 6.86594   -47.81785 -1.43551  1.000 177.50154 ? 146 TRP   A HH2    1 
ATOM   1986 N N      . ASP   A 1 146 ? 9.60235   -48.73851 -9.18232  1.000 140.14053 ? 147 ASP   A N      1 
ATOM   1987 C CA     . ASP   A 1 146 ? 10.55646  -49.20064 -10.18936 1.000 134.42326 ? 147 ASP   A CA     1 
ATOM   1988 C C      . ASP   A 1 146 ? 10.93542  -48.07303 -11.14684 1.000 134.72166 ? 147 ASP   A C      1 
ATOM   1989 O O      . ASP   A 1 146 ? 11.00442  -48.26103 -12.36296 1.000 142.81772 ? 147 ASP   A O      1 
ATOM   1990 C CB     . ASP   A 1 146 ? 9.99926   -50.40154 -10.95758 1.000 155.93931 ? 147 ASP   A CB     1 
ATOM   1991 C CG     . ASP   A 1 146 ? 11.03049  -51.04314 -11.86866 1.000 169.75919 ? 147 ASP   A CG     1 
ATOM   1992 O OD1    . ASP   A 1 146 ? 12.22004  -50.67312 -11.77506 1.000 151.73602 ? 147 ASP   A OD1    1 
ATOM   1993 O OD2    . ASP   A 1 146 ? 10.65068  -51.91220 -12.68270 1.000 163.32495 ? 147 ASP   A OD2    1 
ATOM   1994 H H      . ASP   A 1 146 ? 9.88639   -48.82338 -8.37503  1.000 168.55911 ? 147 ASP   A H      1 
ATOM   1995 H HA     . ASP   A 1 146 ? 11.36784  -49.48247 -9.73866  1.000 161.69838 ? 147 ASP   A HA     1 
ATOM   1996 H HB2    . ASP   A 1 146 ? 9.70040   -51.07187 -10.32337 1.000 187.51765 ? 147 ASP   A HB2    1 
ATOM   1997 H HB3    . ASP   A 1 146 ? 9.25484   -50.10854 -11.50611 1.000 187.51765 ? 147 ASP   A HB3    1 
ATOM   1998 N N      . ARG   A 1 147 ? 11.18694  -46.88830 -10.59364 1.000 132.86335 ? 148 ARG   A N      1 
ATOM   1999 C CA     . ARG   A 1 147 ? 11.54875  -45.70868 -11.37833 1.000 143.26508 ? 148 ARG   A CA     1 
ATOM   2000 C C      . ARG   A 1 147 ? 12.77451  -45.05851 -10.74234 1.000 141.39014 ? 148 ARG   A C      1 
ATOM   2001 O O      . ARG   A 1 147 ? 12.65064  -44.27935 -9.79271  1.000 148.25953 ? 148 ARG   A O      1 
ATOM   2002 C CB     . ARG   A 1 147 ? 10.38240  -44.72802 -11.45964 1.000 145.24328 ? 148 ARG   A CB     1 
ATOM   2003 C CG     . ARG   A 1 147 ? 9.19738   -45.23096 -12.27107 1.000 154.53016 ? 148 ARG   A CG     1 
ATOM   2004 C CD     . ARG   A 1 147 ? 9.57330   -45.46743 -13.73143 1.000 169.14937 ? 148 ARG   A CD     1 
ATOM   2005 N NE     . ARG   A 1 147 ? 8.41902   -45.82129 -14.55090 1.000 151.76396 ? 148 ARG   A NE     1 
ATOM   2006 C CZ     . ARG   A 1 147 ? 7.91287   -47.04333 -14.65010 1.000 153.82663 ? 148 ARG   A CZ     1 
ATOM   2007 N NH1    . ARG   A 1 147 ? 8.42986   -48.06305 -13.98439 1.000 155.85721 ? 148 ARG   A NH1    1 
ATOM   2008 N NH2    . ARG   A 1 147 ? 6.85920   -47.24706 -15.43530 1.000 163.62910 ? 148 ARG   A NH2    1 
ATOM   2009 H H      . ARG   A 1 147 ? 11.15369  -46.73966 -9.74724  1.000 159.82650 ? 148 ARG   A H      1 
ATOM   2010 H HA     . ARG   A 1 147 ? 11.78786  -45.98718 -12.27619 1.000 172.30857 ? 148 ARG   A HA     1 
ATOM   2011 H HB2    . ARG   A 1 147 ? 10.06706  -44.54650 -10.56046 1.000 174.68241 ? 148 ARG   A HB2    1 
ATOM   2012 H HB3    . ARG   A 1 147 ? 10.69518  -43.90830 -11.87332 1.000 174.68241 ? 148 ARG   A HB3    1 
ATOM   2013 H HG2    . ARG   A 1 147 ? 8.88611   -46.07027 -11.89749 1.000 185.82667 ? 148 ARG   A HG2    1 
ATOM   2014 H HG3    . ARG   A 1 147 ? 8.48661   -44.57147 -12.24303 1.000 185.82667 ? 148 ARG   A HG3    1 
ATOM   2015 H HD2    . ARG   A 1 147 ? 9.96374   -44.65706 -14.09441 1.000 203.36971 ? 148 ARG   A HD2    1 
ATOM   2016 H HD3    . ARG   A 1 147 ? 10.21288  -46.19500 -13.78124 1.000 203.36971 ? 148 ARG   A HD3    1 
ATOM   2017 H HE     . ARG   A 1 147 ? 8.04049   -45.19378 -15.00095 1.000 182.50723 ? 148 ARG   A HE     1 
ATOM   2018 H HH11   . ARG   A 1 147 ? 9.11019   -47.94181 -13.47247 1.000 187.41913 ? 148 ARG   A HH11   1 
ATOM   2019 H HH12   . ARG   A 1 147 ? 8.08561   -48.84716 -14.06357 1.000 187.41913 ? 148 ARG   A HH12   1 
ATOM   2020 H HH21   . ARG   A 1 147 ? 6.51436   -46.59071 -15.87107 1.000 196.74539 ? 148 ARG   A HH21   1 
ATOM   2021 H HH22   . ARG   A 1 147 ? 6.52260   -48.03516 -15.50734 1.000 196.74539 ? 148 ARG   A HH22   1 
ATOM   2022 N N      . LYS   A 1 148 ? 13.95342  -45.37366 -11.27380 1.000 138.68946 ? 149 LYS   A N      1 
ATOM   2023 C CA     . LYS   A 1 148 ? 15.21601  -44.82527 -10.79061 1.000 134.67227 ? 149 LYS   A CA     1 
ATOM   2024 C C      . LYS   A 1 148 ? 15.59786  -43.63753 -11.66720 1.000 141.83336 ? 149 LYS   A C      1 
ATOM   2025 O O      . LYS   A 1 148 ? 15.97669  -43.81349 -12.82851 1.000 173.16122 ? 149 LYS   A O      1 
ATOM   2026 C CB     . LYS   A 1 148 ? 16.30777  -45.89400 -10.81133 1.000 130.14908 ? 149 LYS   A CB     1 
ATOM   2027 C CG     . LYS   A 1 148 ? 17.69396  -45.39615 -10.41745 1.000 130.76843 ? 149 LYS   A CG     1 
ATOM   2028 C CD     . LYS   A 1 148 ? 18.77409  -46.43438 -10.71041 1.000 120.06683 ? 149 LYS   A CD     1 
ATOM   2029 C CE     . LYS   A 1 148 ? 18.55950  -47.72525 -9.92918  1.000 154.45554 ? 149 LYS   A CE     1 
ATOM   2030 N NZ     . LYS   A 1 148 ? 19.59271  -48.75213 -10.25362 1.000 167.86742 ? 149 LYS   A NZ     1 
ATOM   2031 H H      . LYS   A 1 148 ? 14.04886  -45.91781 -11.93289 1.000 166.81782 ? 149 LYS   A H      1 
ATOM   2032 H HA     . LYS   A 1 148 ? 15.10505  -44.51147 -9.87950  1.000 161.99720 ? 149 LYS   A HA     1 
ATOM   2033 H HB2    . LYS   A 1 148 ? 16.06244  -46.59723 -10.18989 1.000 156.56936 ? 149 LYS   A HB2    1 
ATOM   2034 H HB3    . LYS   A 1 148 ? 16.37076  -46.25280 -11.71032 1.000 156.56936 ? 149 LYS   A HB3    1 
ATOM   2035 H HG2    . LYS   A 1 148 ? 17.90054  -44.59299 -10.92060 1.000 157.31259 ? 149 LYS   A HG2    1 
ATOM   2036 H HG3    . LYS   A 1 148 ? 17.70705  -45.20455 -9.46665  1.000 157.31259 ? 149 LYS   A HG3    1 
ATOM   2037 H HD2    . LYS   A 1 148 ? 18.76195  -46.64852 -11.65640 1.000 144.47067 ? 149 LYS   A HD2    1 
ATOM   2038 H HD3    . LYS   A 1 148 ? 19.63939  -46.07232 -10.46330 1.000 144.47067 ? 149 LYS   A HD3    1 
ATOM   2039 H HE2    . LYS   A 1 148 ? 18.60853  -47.53554 -8.97918  1.000 185.73712 ? 149 LYS   A HE2    1 
ATOM   2040 H HE3    . LYS   A 1 148 ? 17.68870  -48.09115 -10.14991 1.000 185.73712 ? 149 LYS   A HE3    1 
ATOM   2041 H HZ1    . LYS   A 1 148 ? 19.40436  -49.51568 -9.83694  1.000 201.83138 ? 149 LYS   A HZ1    1 
ATOM   2042 H HZ2    . LYS   A 1 148 ? 19.61094  -48.89889 -11.13125 1.000 201.83138 ? 149 LYS   A HZ2    1 
ATOM   2043 H HZ3    . LYS   A 1 148 ? 20.39503  -48.47016 -9.99120  1.000 201.83138 ? 149 LYS   A HZ3    1 
ATOM   2044 N N      . LEU   A 1 149 ? 15.50819  -42.43344 -11.10992 1.000 140.59507 ? 150 LEU   A N      1 
ATOM   2045 C CA     . LEU   A 1 149 ? 15.89527  -41.23719 -11.84610 1.000 140.37864 ? 150 LEU   A CA     1 
ATOM   2046 C C      . LEU   A 1 149 ? 17.39776  -41.24651 -12.09715 1.000 147.85615 ? 150 LEU   A C      1 
ATOM   2047 O O      . LEU   A 1 149 ? 18.19016  -41.44496 -11.17176 1.000 161.16318 ? 150 LEU   A O      1 
ATOM   2048 C CB     . LEU   A 1 149 ? 15.49623  -39.98653 -11.06765 1.000 141.48787 ? 150 LEU   A CB     1 
ATOM   2049 C CG     . LEU   A 1 149 ? 15.75137  -38.64392 -11.75162 1.000 125.05481 ? 150 LEU   A CG     1 
ATOM   2050 C CD1    . LEU   A 1 149 ? 14.82388  -38.46842 -12.93579 1.000 146.12767 ? 150 LEU   A CD1    1 
ATOM   2051 C CD2    . LEU   A 1 149 ? 15.58050  -37.49702 -10.76893 1.000 148.22098 ? 150 LEU   A CD2    1 
ATOM   2052 H H      . LEU   A 1 149 ? 15.22766  -42.28358 -10.31090 1.000 169.10455 ? 150 LEU   A H      1 
ATOM   2053 H HA     . LEU   A 1 149 ? 15.43873  -41.21901 -12.70175 1.000 168.84484 ? 150 LEU   A HA     1 
ATOM   2054 H HB2    . LEU   A 1 149 ? 14.54472  -40.03708 -10.88606 1.000 170.17592 ? 150 LEU   A HB2    1 
ATOM   2055 H HB3    . LEU   A 1 149 ? 15.99310  -39.98045 -10.23459 1.000 170.17592 ? 150 LEU   A HB3    1 
ATOM   2056 H HG     . LEU   A 1 149 ? 16.66550  -38.62649 -12.07560 1.000 150.45624 ? 150 LEU   A HG     1 
ATOM   2057 H HD11   . LEU   A 1 149 ? 14.99544  -37.60646 -13.34627 1.000 175.74367 ? 150 LEU   A HD11   1 
ATOM   2058 H HD12   . LEU   A 1 149 ? 14.99051  -39.17840 -13.57538 1.000 175.74367 ? 150 LEU   A HD12   1 
ATOM   2059 H HD13   . LEU   A 1 149 ? 13.90546  -38.51061 -12.62656 1.000 175.74367 ? 150 LEU   A HD13   1 
ATOM   2060 H HD21   . LEU   A 1 149 ? 15.81947  -36.66611 -11.20867 1.000 178.25564 ? 150 LEU   A HD21   1 
ATOM   2061 H HD22   . LEU   A 1 149 ? 14.65516  -37.46405 -10.47986 1.000 178.25564 ? 150 LEU   A HD22   1 
ATOM   2062 H HD23   . LEU   A 1 149 ? 16.16035  -37.64603 -10.00573 1.000 178.25564 ? 150 LEU   A HD23   1 
ATOM   2063 N N      . VAL   A 1 150 ? 17.78912  -41.02825 -13.34897 1.000 158.17229 ? 151 VAL   A N      1 
ATOM   2064 C CA     . VAL   A 1 150 ? 19.18661  -41.06372 -13.76359 1.000 159.56729 ? 151 VAL   A CA     1 
ATOM   2065 C C      . VAL   A 1 150 ? 19.71900  -39.66130 -14.03997 1.000 146.26408 ? 151 VAL   A C      1 
ATOM   2066 O O      . VAL   A 1 150 ? 20.79081  -39.28941 -13.56014 1.000 130.96197 ? 151 VAL   A O      1 
ATOM   2067 C CB     . VAL   A 1 150 ? 19.37076  -41.97813 -14.99643 1.000 173.05469 ? 151 VAL   A CB     1 
ATOM   2068 C CG1    . VAL   A 1 150 ? 20.83232  -42.03065 -15.41227 1.000 184.53765 ? 151 VAL   A CG1    1 
ATOM   2069 C CG2    . VAL   A 1 150 ? 18.85049  -43.37694 -14.70451 1.000 176.88919 ? 151 VAL   A CG2    1 
ATOM   2070 H H      . VAL   A 1 150 ? 17.24732  -40.85272 -13.99336 1.000 190.19721 ? 151 VAL   A H      1 
ATOM   2071 H HA     . VAL   A 1 150 ? 19.71187  -41.43551 -13.03780 1.000 191.87121 ? 151 VAL   A HA     1 
ATOM   2072 H HB     . VAL   A 1 150 ? 18.85989  -41.61089 -15.73470 1.000 208.05610 ? 151 VAL   A HB     1 
ATOM   2073 H HG11   . VAL   A 1 150 ? 20.95443  -42.75448 -16.04636 1.000 221.83565 ? 151 VAL   A HG11   1 
ATOM   2074 H HG12   . VAL   A 1 150 ? 21.07414  -41.18617 -15.82370 1.000 221.83565 ? 151 VAL   A HG12   1 
ATOM   2075 H HG13   . VAL   A 1 150 ? 21.37908  -42.18403 -14.62588 1.000 221.83565 ? 151 VAL   A HG13   1 
ATOM   2076 H HG21   . VAL   A 1 150 ? 19.04494  -43.95069 -15.46207 1.000 212.65750 ? 151 VAL   A HG21   1 
ATOM   2077 H HG22   . VAL   A 1 150 ? 19.29006  -43.71792 -13.90990 1.000 212.65750 ? 151 VAL   A HG22   1 
ATOM   2078 H HG23   . VAL   A 1 150 ? 17.89234  -43.33366 -14.55968 1.000 212.65750 ? 151 VAL   A HG23   1 
ATOM   2079 N N      . THR   A 1 151 ? 18.98096  -38.86964 -14.81685 1.000 160.53332 ? 152 THR   A N      1 
ATOM   2080 C CA     . THR   A 1 151 ? 19.37277  -37.50415 -15.12922 1.000 147.52569 ? 152 THR   A CA     1 
ATOM   2081 C C      . THR   A 1 151 ? 18.14421  -36.60823 -15.10670 1.000 147.60690 ? 152 THR   A C      1 
ATOM   2082 O O      . THR   A 1 151 ? 17.02289  -37.05679 -15.35845 1.000 152.86086 ? 152 THR   A O      1 
ATOM   2083 C CB     . THR   A 1 151 ? 20.05041  -37.39103 -16.50327 1.000 179.92443 ? 152 THR   A CB     1 
ATOM   2084 O OG1    . THR   A 1 151 ? 19.14635  -37.83194 -17.52476 1.000 181.50367 ? 152 THR   A OG1    1 
ATOM   2085 C CG2    . THR   A 1 151 ? 21.31893  -38.22627 -16.55049 1.000 180.49605 ? 152 THR   A CG2    1 
ATOM   2086 H H      . THR   A 1 151 ? 18.23805  -39.10776 -15.17876 1.000 193.03045 ? 152 THR   A H      1 
ATOM   2087 H HA     . THR   A 1 151 ? 19.99876  -37.19922 -14.45390 1.000 177.42130 ? 152 THR   A HA     1 
ATOM   2088 H HB     . THR   A 1 151 ? 20.29327  -36.46616 -16.66617 1.000 216.29979 ? 152 THR   A HB     1 
ATOM   2089 H HG1    . THR   A 1 151 ? 19.51760  -37.78495 -18.27681 1.000 218.19488 ? 152 THR   A HG1    1 
ATOM   2090 H HG21   . THR   A 1 151 ? 21.78586  -38.07340 -17.38685 1.000 216.98574 ? 152 THR   A HG21   1 
ATOM   2091 H HG22   . THR   A 1 151 ? 21.90315  -37.98413 -15.81498 1.000 216.98574 ? 152 THR   A HG22   1 
ATOM   2092 H HG23   . THR   A 1 151 ? 21.09866  -39.16833 -16.48055 1.000 216.98574 ? 152 THR   A HG23   1 
ATOM   2093 N N      . LEU   A 1 152 ? 18.37445  -35.33102 -14.81256 1.000 149.51684 ? 153 LEU   A N      1 
ATOM   2094 C CA     . LEU   A 1 152 ? 17.32452  -34.31789 -14.75875 1.000 164.45608 ? 153 LEU   A CA     1 
ATOM   2095 C C      . LEU   A 1 152 ? 17.80841  -33.11644 -15.55831 1.000 165.52813 ? 153 LEU   A C      1 
ATOM   2096 O O      . LEU   A 1 152 ? 18.78667  -32.46817 -15.17322 1.000 164.62888 ? 153 LEU   A O      1 
ATOM   2097 C CB     . LEU   A 1 152 ? 17.01032  -33.93288 -13.31310 1.000 157.39197 ? 153 LEU   A CB     1 
ATOM   2098 C CG     . LEU   A 1 152 ? 15.89787  -32.91143 -13.07745 1.000 165.64955 ? 153 LEU   A CG     1 
ATOM   2099 C CD1    . LEU   A 1 152 ? 14.57507  -33.40521 -13.63270 1.000 175.89774 ? 153 LEU   A CD1    1 
ATOM   2100 C CD2    . LEU   A 1 152 ? 15.77317  -32.61016 -11.59027 1.000 185.58810 ? 153 LEU   A CD2    1 
ATOM   2101 H H      . LEU   A 1 152 ? 19.15543  -35.01781 -14.63490 1.000 179.81067 ? 153 LEU   A H      1 
ATOM   2102 H HA     . LEU   A 1 152 ? 16.51023  -34.65466 -15.16424 1.000 197.73776 ? 153 LEU   A HA     1 
ATOM   2103 H HB2    . LEU   A 1 152 ? 16.75386  -34.74039 -12.84081 1.000 189.26084 ? 153 LEU   A HB2    1 
ATOM   2104 H HB3    . LEU   A 1 152 ? 17.81771  -33.56275 -12.92322 1.000 189.26084 ? 153 LEU   A HB3    1 
ATOM   2105 H HG     . LEU   A 1 152 ? 16.12147  -32.09036 -13.54301 1.000 199.16994 ? 153 LEU   A HG     1 
ATOM   2106 H HD11   . LEU   A 1 152 ? 13.88407  -32.75649 -13.42633 1.000 211.46776 ? 153 LEU   A HD11   1 
ATOM   2107 H HD12   . LEU   A 1 152 ? 14.65500  -33.50893 -14.59382 1.000 211.46776 ? 153 LEU   A HD12   1 
ATOM   2108 H HD13   . LEU   A 1 152 ? 14.36012  -34.25856 -13.22466 1.000 211.46776 ? 153 LEU   A HD13   1 
ATOM   2109 H HD21   . LEU   A 1 152 ? 15.05849  -31.96801 -11.45698 1.000 223.09620 ? 153 LEU   A HD21   1 
ATOM   2110 H HD22   . LEU   A 1 152 ? 15.57135  -33.43262 -11.11727 1.000 223.09620 ? 153 LEU   A HD22   1 
ATOM   2111 H HD23   . LEU   A 1 152 ? 16.61209  -32.24237 -11.27113 1.000 223.09620 ? 153 LEU   A HD23   1 
ATOM   2112 N N      . GLU   A 1 153 ? 17.13368  -32.82323 -16.67079 1.000 168.77430 ? 154 GLU   A N      1 
ATOM   2113 C CA     . GLU   A 1 153 ? 17.56867  -31.76825 -17.57400 1.000 168.92210 ? 154 GLU   A CA     1 
ATOM   2114 C C      . GLU   A 1 153 ? 16.43199  -30.79518 -17.85424 1.000 171.98066 ? 154 GLU   A C      1 
ATOM   2115 O O      . GLU   A 1 153 ? 15.29862  -31.21724 -18.11503 1.000 168.63279 ? 154 GLU   A O      1 
ATOM   2116 C CB     . GLU   A 1 153 ? 18.08030  -32.36405 -18.89330 1.000 175.90904 ? 154 GLU   A CB     1 
ATOM   2117 C CG     . GLU   A 1 153 ? 19.25472  -33.31415 -18.71633 1.000 194.06071 ? 154 GLU   A CG     1 
ATOM   2118 C CD     . GLU   A 1 153 ? 20.41719  -32.67169 -17.98252 1.000 194.66377 ? 154 GLU   A CD     1 
ATOM   2119 O OE1    . GLU   A 1 153 ? 20.61390  -31.44757 -18.13616 1.000 182.93429 ? 154 GLU   A OE1    1 
ATOM   2120 O OE2    . GLU   A 1 153 ? 21.12651  -33.38775 -17.24391 1.000 190.74864 ? 154 GLU   A OE2    1 
ATOM   2121 H H      . GLU   A 1 153 ? 16.41673  -33.22629 -16.92203 1.000 202.91963 ? 154 GLU   A H      1 
ATOM   2122 H HA     . GLU   A 1 153 ? 18.28762  -31.26794 -17.15722 1.000 203.09699 ? 154 GLU   A HA     1 
ATOM   2123 H HB2    . GLU   A 1 153 ? 17.35916  -32.85832 -19.31347 1.000 211.48132 ? 154 GLU   A HB2    1 
ATOM   2124 H HB3    . GLU   A 1 153 ? 18.36805  -31.64078 -19.47207 1.000 211.48132 ? 154 GLU   A HB3    1 
ATOM   2125 H HG2    . GLU   A 1 153 ? 18.96444  -34.08486 -18.20385 1.000 233.26332 ? 154 GLU   A HG2    1 
ATOM   2126 H HG3    . GLU   A 1 153 ? 19.56897  -33.59574 -19.58975 1.000 233.26332 ? 154 GLU   A HG3    1 
ATOM   2127 N N      . PRO   A 1 154 ? 16.70339  -29.49280 -17.82181 1.000 172.72323 ? 155 PRO   A N      1 
ATOM   2128 C CA     . PRO   A 1 154 ? 15.62783  -28.50860 -17.95742 1.000 174.05265 ? 155 PRO   A CA     1 
ATOM   2129 C C      . PRO   A 1 154 ? 15.28340  -28.20982 -19.40841 1.000 187.86416 ? 155 PRO   A C      1 
ATOM   2130 O O      . PRO   A 1 154 ? 16.06883  -28.43066 -20.33188 1.000 203.62688 ? 155 PRO   A O      1 
ATOM   2131 C CB     . PRO   A 1 154 ? 16.20894  -27.26807 -17.26910 1.000 171.31899 ? 155 PRO   A CB     1 
ATOM   2132 C CG     . PRO   A 1 154 ? 17.66954  -27.36977 -17.53689 1.000 172.46577 ? 155 PRO   A CG     1 
ATOM   2133 C CD     . PRO   A 1 154 ? 17.99767  -28.84632 -17.52768 1.000 172.65018 ? 155 PRO   A CD     1 
ATOM   2134 H HA     . PRO   A 1 154 ? 14.82926  -28.81022 -17.49676 1.000 209.25365 ? 155 PRO   A HA     1 
ATOM   2135 H HB2    . PRO   A 1 154 ? 15.83494  -26.46214 -17.65832 1.000 205.97325 ? 155 PRO   A HB2    1 
ATOM   2136 H HB3    . PRO   A 1 154 ? 16.02284  -27.29415 -16.31747 1.000 205.97325 ? 155 PRO   A HB3    1 
ATOM   2137 H HG2    . PRO   A 1 154 ? 17.87012  -26.97986 -18.40213 1.000 207.34940 ? 155 PRO   A HG2    1 
ATOM   2138 H HG3    . PRO   A 1 154 ? 18.16141  -26.90540 -16.84167 1.000 207.34940 ? 155 PRO   A HG3    1 
ATOM   2139 H HD2    . PRO   A 1 154 ? 18.65111  -29.05763 -18.21270 1.000 207.57069 ? 155 PRO   A HD2    1 
ATOM   2140 H HD3    . PRO   A 1 154 ? 18.32870  -29.11958 -16.65783 1.000 207.57069 ? 155 PRO   A HD3    1 
ATOM   2141 N N      . ASP   A 1 155 ? 14.07418  -27.69264 -19.58686 1.000 204.03415 ? 156 ASP   A N      1 
ATOM   2142 C CA     . ASP   A 1 155 ? 13.57384  -27.21122 -20.86566 1.000 204.73855 ? 156 ASP   A CA     1 
ATOM   2143 C C      . ASP   A 1 155 ? 13.24552  -25.72409 -20.71935 1.000 202.04945 ? 156 ASP   A C      1 
ATOM   2144 O O      . ASP   A 1 155 ? 13.52928  -25.10508 -19.69021 1.000 209.10734 ? 156 ASP   A O      1 
ATOM   2145 C CB     . ASP   A 1 155 ? 12.35990  -28.03270 -21.30270 1.000 199.62387 ? 156 ASP   A CB     1 
ATOM   2146 C CG     . ASP   A 1 155 ? 12.08887  -27.92399 -22.78294 1.000 200.48692 ? 156 ASP   A CG     1 
ATOM   2147 O OD1    . ASP   A 1 155 ? 12.94497  -28.36972 -23.57452 1.000 230.51032 ? 156 ASP   A OD1    1 
ATOM   2148 O OD2    . ASP   A 1 155 ? 11.02345  -27.38933 -23.15347 1.000 204.73897 ? 156 ASP   A OD2    1 
ATOM   2149 H H      . ASP   A 1 155 ? 13.50016  -27.60677 -18.95225 1.000 245.23145 ? 156 ASP   A H      1 
ATOM   2150 H HA     . ASP   A 1 155 ? 14.25703  -27.31361 -21.54659 1.000 246.07674 ? 156 ASP   A HA     1 
ATOM   2151 H HB2    . ASP   A 1 155 ? 12.51765  -28.96670 -21.09376 1.000 239.93912 ? 156 ASP   A HB2    1 
ATOM   2152 H HB3    . ASP   A 1 155 ? 11.57524  -27.71477 -20.82926 1.000 239.93912 ? 156 ASP   A HB3    1 
ATOM   2153 N N      . LYS   A 1 156 ? 12.64523  -25.14435 -21.75997 1.000 196.84958 ? 157 LYS   A N      1 
ATOM   2154 C CA     . LYS   A 1 156 ? 12.20928  -23.75667 -21.66247 1.000 202.21186 ? 157 LYS   A CA     1 
ATOM   2155 C C      . LYS   A 1 156 ? 11.05314  -23.58230 -20.68462 1.000 199.30017 ? 157 LYS   A C      1 
ATOM   2156 O O      . LYS   A 1 156 ? 10.83594  -22.46697 -20.19933 1.000 197.51975 ? 157 LYS   A O      1 
ATOM   2157 C CB     . LYS   A 1 156 ? 11.79912  -23.22454 -23.03755 1.000 207.71058 ? 157 LYS   A CB     1 
ATOM   2158 C CG     . LYS   A 1 156 ? 12.91865  -22.54469 -23.82091 1.000 208.22899 ? 157 LYS   A CG     1 
ATOM   2159 C CD     . LYS   A 1 156 ? 13.43932  -21.30501 -23.10376 1.000 212.66272 ? 157 LYS   A CD     1 
ATOM   2160 C CE     . LYS   A 1 156 ? 14.32382  -20.46224 -24.00926 1.000 216.91099 ? 157 LYS   A CE     1 
ATOM   2161 N NZ     . LYS   A 1 156 ? 14.86481  -19.26566 -23.30305 1.000 217.78096 ? 157 LYS   A NZ     1 
ATOM   2162 H H      . LYS   A 1 156 ? 12.48361  -25.52509 -22.51397 1.000 236.60997 ? 157 LYS   A H      1 
ATOM   2163 H HA     . LYS   A 1 156 ? 12.95754  -23.22528 -21.34841 1.000 243.04471 ? 157 LYS   A HA     1 
ATOM   2164 H HB2    . LYS   A 1 156 ? 11.47880  -23.96784 -23.57216 1.000 249.64316 ? 157 LYS   A HB2    1 
ATOM   2165 H HB3    . LYS   A 1 156 ? 11.09056  -22.57321 -22.91665 1.000 249.64316 ? 157 LYS   A HB3    1 
ATOM   2166 H HG2    . LYS   A 1 156 ? 13.65634  -23.16522 -23.92888 1.000 250.26525 ? 157 LYS   A HG2    1 
ATOM   2167 H HG3    . LYS   A 1 156 ? 12.58282  -22.27415 -24.68978 1.000 250.26525 ? 157 LYS   A HG3    1 
ATOM   2168 H HD2    . LYS   A 1 156 ? 12.68885  -20.76032 -22.81914 1.000 255.58573 ? 157 LYS   A HD2    1 
ATOM   2169 H HD3    . LYS   A 1 156 ? 13.96321  -21.57632 -22.33380 1.000 255.58573 ? 157 LYS   A HD3    1 
ATOM   2170 H HE2    . LYS   A 1 156 ? 15.07240  -20.99871 -24.31376 1.000 260.68365 ? 157 LYS   A HE2    1 
ATOM   2171 H HE3    . LYS   A 1 156 ? 13.80395  -20.15656 -24.76899 1.000 260.68365 ? 157 LYS   A HE3    1 
ATOM   2172 H HZ1    . LYS   A 1 156 ? 15.69836  -19.10531 -23.57061 1.000 261.72762 ? 157 LYS   A HZ1    1 
ATOM   2173 H HZ2    . LYS   A 1 156 ? 14.36198  -18.55343 -23.48195 1.000 261.72762 ? 157 LYS   A HZ2    1 
ATOM   2174 H HZ3    . LYS   A 1 156 ? 14.86542  -19.40538 -22.42409 1.000 261.72762 ? 157 LYS   A HZ3    1 
ATOM   2175 N N      . GLU   A 1 157 ? 10.31048  -24.64960 -20.38154 1.000 193.49961 ? 158 GLU   A N      1 
ATOM   2176 C CA     . GLU   A 1 157 ? 9.15978   -24.53052 -19.48943 1.000 205.10973 ? 158 GLU   A CA     1 
ATOM   2177 C C      . GLU   A 1 157 ? 8.94263   -25.72003 -18.56398 1.000 215.41145 ? 158 GLU   A C      1 
ATOM   2178 O O      . GLU   A 1 157 ? 8.29081   -25.54366 -17.52876 1.000 208.81292 ? 158 GLU   A O      1 
ATOM   2179 C CB     . GLU   A 1 157 ? 7.87909   -24.30303 -20.30429 1.000 198.02438 ? 158 GLU   A CB     1 
ATOM   2180 C CG     . GLU   A 1 157 ? 6.88567   -23.36527 -19.63491 1.000 207.07237 ? 158 GLU   A CG     1 
ATOM   2181 C CD     . GLU   A 1 157 ? 5.65438   -23.11118 -20.48121 1.000 221.80151 ? 158 GLU   A CD     1 
ATOM   2182 O OE1    . GLU   A 1 157 ? 5.37832   -23.91993 -21.39189 1.000 237.23188 ? 158 GLU   A OE1    1 
ATOM   2183 O OE2    . GLU   A 1 157 ? 4.96368   -22.09961 -20.23621 1.000 222.57319 ? 158 GLU   A OE2    1 
ATOM   2184 H H      . GLU   A 1 157 ? 10.45230  -25.44453 -20.67745 1.000 232.59000 ? 158 GLU   A H      1 
ATOM   2185 H HA     . GLU   A 1 157 ? 9.29627   -23.75516 -18.92278 1.000 246.52215 ? 158 GLU   A HA     1 
ATOM   2186 H HB2    . GLU   A 1 157 ? 8.11916   -23.91743 -21.16137 1.000 238.01973 ? 158 GLU   A HB2    1 
ATOM   2187 H HB3    . GLU   A 1 157 ? 7.43781   -25.15667 -20.43647 1.000 238.01973 ? 158 GLU   A HB3    1 
ATOM   2188 H HG2    . GLU   A 1 157 ? 6.59692   -23.75763 -18.79612 1.000 248.87731 ? 158 GLU   A HG2    1 
ATOM   2189 H HG3    . GLU   A 1 157 ? 7.31769   -22.51241 -19.47091 1.000 248.87731 ? 158 GLU   A HG3    1 
ATOM   2190 N N      . LYS   A 1 158 ? 9.44870   -26.91412 -18.87239 1.000 196.29915 ? 159 LYS   A N      1 
ATOM   2191 C CA     . LYS   A 1 158 ? 9.24510   -28.07492 -18.01781 1.000 184.33422 ? 159 LYS   A CA     1 
ATOM   2192 C C      . LYS   A 1 158 ? 10.54536  -28.85050 -17.87218 1.000 184.06289 ? 159 LYS   A C      1 
ATOM   2193 O O      . LYS   A 1 158 ? 11.46135  -28.73624 -18.68938 1.000 182.61541 ? 159 LYS   A O      1 
ATOM   2194 C CB     . LYS   A 1 158 ? 8.15339   -29.00848 -18.56368 1.000 179.29644 ? 159 LYS   A CB     1 
ATOM   2195 C CG     . LYS   A 1 158 ? 6.74718   -28.61208 -18.15953 1.000 174.32774 ? 159 LYS   A CG     1 
ATOM   2196 C CD     . LYS   A 1 158 ? 5.71045   -29.58991 -18.68512 1.000 175.75324 ? 159 LYS   A CD     1 
ATOM   2197 C CE     . LYS   A 1 158 ? 4.32019   -28.97435 -18.66463 1.000 178.92263 ? 159 LYS   A CE     1 
ATOM   2198 N NZ     . LYS   A 1 158 ? 3.30808   -29.85459 -19.30789 1.000 184.87946 ? 159 LYS   A NZ     1 
ATOM   2199 H H      . LYS   A 1 158 ? 9.91590   -27.07464 -19.57635 1.000 235.94945 ? 159 LYS   A H      1 
ATOM   2200 H HA     . LYS   A 1 158 ? 8.97766   -27.76116 -17.13978 1.000 221.59153 ? 159 LYS   A HA     1 
ATOM   2201 H HB2    . LYS   A 1 158 ? 8.19500   -29.00267 -19.53277 1.000 215.54620 ? 159 LYS   A HB2    1 
ATOM   2202 H HB3    . LYS   A 1 158 ? 8.31509   -29.90483 -18.23005 1.000 215.54620 ? 159 LYS   A HB3    1 
ATOM   2203 H HG2    . LYS   A 1 158 ? 6.68519   -28.59551 -17.19165 1.000 209.58375 ? 159 LYS   A HG2    1 
ATOM   2204 H HG3    . LYS   A 1 158 ? 6.54623   -27.73422 -18.51992 1.000 209.58375 ? 159 LYS   A HG3    1 
ATOM   2205 H HD2    . LYS   A 1 158 ? 5.92660   -29.82927 -19.59994 1.000 211.29436 ? 159 LYS   A HD2    1 
ATOM   2206 H HD3    . LYS   A 1 158 ? 5.70289   -30.38355 -18.12748 1.000 211.29436 ? 159 LYS   A HD3    1 
ATOM   2207 H HE2    . LYS   A 1 158 ? 4.05086   -28.82594 -17.74467 1.000 215.09762 ? 159 LYS   A HE2    1 
ATOM   2208 H HE3    . LYS   A 1 158 ? 4.33748   -28.13198 -19.14526 1.000 215.09762 ? 159 LYS   A HE3    1 
ATOM   2209 H HZ1    . LYS   A 1 158 ? 2.51570   -29.44951 -19.31942 1.000 222.24582 ? 159 LYS   A HZ1    1 
ATOM   2210 H HZ2    . LYS   A 1 158 ? 3.55123   -30.03738 -20.14429 1.000 222.24582 ? 159 LYS   A HZ2    1 
ATOM   2211 H HZ3    . LYS   A 1 158 ? 3.23602   -30.61725 -18.85482 1.000 222.24582 ? 159 LYS   A HZ3    1 
ATOM   2212 N N      . TRP   A 1 159 ? 10.61063  -29.64458 -16.80904 1.000 191.33556 ? 160 TRP   A N      1 
ATOM   2213 C CA     . TRP   A 1 159 ? 11.72923  -30.54730 -16.59882 1.000 188.66695 ? 160 TRP   A CA     1 
ATOM   2214 C C      . TRP   A 1 159 ? 11.54224  -31.81815 -17.41866 1.000 189.92079 ? 160 TRP   A C      1 
ATOM   2215 O O      . TRP   A 1 159 ? 10.42117  -32.20031 -17.76375 1.000 182.02601 ? 160 TRP   A O      1 
ATOM   2216 C CB     . TRP   A 1 159 ? 11.85959  -30.90007 -15.11772 1.000 169.77499 ? 160 TRP   A CB     1 
ATOM   2217 C CG     . TRP   A 1 159 ? 12.34789  -29.77014 -14.26539 1.000 171.81128 ? 160 TRP   A CG     1 
ATOM   2218 C CD1    . TRP   A 1 159 ? 11.58988  -28.91616 -13.51751 1.000 170.51373 ? 160 TRP   A CD1    1 
ATOM   2219 C CD2    . TRP   A 1 159 ? 13.70960  -29.37358 -14.06995 1.000 163.35951 ? 160 TRP   A CD2    1 
ATOM   2220 N NE1    . TRP   A 1 159 ? 12.39656  -28.01328 -12.86830 1.000 161.48434 ? 160 TRP   A NE1    1 
ATOM   2221 C CE2    . TRP   A 1 159 ? 13.70257  -28.27390 -13.19030 1.000 160.74107 ? 160 TRP   A CE2    1 
ATOM   2222 C CE3    . TRP   A 1 159 ? 14.93410  -29.84282 -14.55281 1.000 164.81792 ? 160 TRP   A CE3    1 
ATOM   2223 C CZ2    . TRP   A 1 159 ? 14.87202  -27.63376 -12.78652 1.000 163.26370 ? 160 TRP   A CZ2    1 
ATOM   2224 C CZ3    . TRP   A 1 159 ? 16.09362  -29.20827 -14.14919 1.000 163.61909 ? 160 TRP   A CZ3    1 
ATOM   2225 C CH2    . TRP   A 1 159 ? 16.05468  -28.11549 -13.27527 1.000 164.59438 ? 160 TRP   A CH2    1 
ATOM   2226 H H      . TRP   A 1 159 ? 10.01356  -29.67793 -16.19098 1.000 229.99314 ? 160 TRP   A H      1 
ATOM   2227 H HA     . TRP   A 1 159 ? 12.55268  -30.11836 -16.87962 1.000 226.79081 ? 160 TRP   A HA     1 
ATOM   2228 H HB2    . TRP   A 1 159 ? 10.98907  -31.16727 -14.78353 1.000 204.12046 ? 160 TRP   A HB2    1 
ATOM   2229 H HB3    . TRP   A 1 159 ? 12.48912  -31.63236 -15.02633 1.000 204.12046 ? 160 TRP   A HB3    1 
ATOM   2230 H HD1    . TRP   A 1 159 ? 10.66224  -28.94179 -13.45633 1.000 205.00694 ? 160 TRP   A HD1    1 
ATOM   2231 H HE1    . TRP   A 1 159 ? 12.12592  -27.38669 -12.34510 1.000 194.17167 ? 160 TRP   A HE1    1 
ATOM   2232 H HE3    . TRP   A 1 159 ? 14.96811  -30.56782 -15.13429 1.000 198.17197 ? 160 TRP   A HE3    1 
ATOM   2233 H HZ2    . TRP   A 1 159 ? 14.84927  -26.90682 -12.20691 1.000 196.30691 ? 160 TRP   A HZ2    1 
ATOM   2234 H HZ3    . TRP   A 1 159 ? 16.91418  -29.51265 -14.46373 1.000 196.73338 ? 160 TRP   A HZ3    1 
ATOM   2235 H HH2    . TRP   A 1 159 ? 16.85112  -27.70794 -13.02137 1.000 197.90373 ? 160 TRP   A HH2    1 
ATOM   2236 N N      . THR   A 1 160 ? 12.65938  -32.46500 -17.74263 1.000 178.54315 ? 161 THR   A N      1 
ATOM   2237 C CA     . THR   A 1 160 ? 12.65999  -33.77007 -18.39317 1.000 167.79469 ? 161 THR   A CA     1 
ATOM   2238 C C      . THR   A 1 160 ? 13.33961  -34.76649 -17.46406 1.000 163.42717 ? 161 THR   A C      1 
ATOM   2239 O O      . THR   A 1 160 ? 14.53358  -34.63405 -17.17489 1.000 160.02105 ? 161 THR   A O      1 
ATOM   2240 C CB     . THR   A 1 160 ? 13.37252  -33.71889 -19.74533 1.000 181.08165 ? 161 THR   A CB     1 
ATOM   2241 O OG1    . THR   A 1 160 ? 12.66497  -32.83832 -20.62729 1.000 205.84993 ? 161 THR   A OG1    1 
ATOM   2242 C CG2    . THR   A 1 160 ? 13.44224  -35.10849 -20.36493 1.000 193.55997 ? 161 THR   A CG2    1 
ATOM   2243 H H      . THR   A 1 160 ? 13.44863  -32.15885 -17.59110 1.000 214.64225 ? 161 THR   A H      1 
ATOM   2244 H HA     . THR   A 1 160 ? 11.74661  -34.05809 -18.54709 1.000 201.74410 ? 161 THR   A HA     1 
ATOM   2245 H HB     . THR   A 1 160 ? 14.27814  -33.39367 -19.62291 1.000 217.68845 ? 161 THR   A HB     1 
ATOM   2246 H HG1    . THR   A 1 160 ? 13.04112  -32.82054 -21.37815 1.000 247.41038 ? 161 THR   A HG1    1 
ATOM   2247 H HG21   . THR   A 1 160 ? 13.70521  -35.04361 -21.29635 1.000 232.66243 ? 161 THR   A HG21   1 
ATOM   2248 H HG22   . THR   A 1 160 ? 14.09233  -35.65068 -19.89132 1.000 232.66243 ? 161 THR   A HG22   1 
ATOM   2249 H HG23   . THR   A 1 160 ? 12.57473  -35.53923 -20.31202 1.000 232.66243 ? 161 THR   A HG23   1 
ATOM   2250 N N      . LEU   A 1 161 ? 12.57980  -35.76002 -17.00560 1.000 167.11831 ? 162 LEU   A N      1 
ATOM   2251 C CA     . LEU   A 1 161 ? 13.04368  -36.72823 -16.01934 1.000 170.68890 ? 162 LEU   A CA     1 
ATOM   2252 C C      . LEU   A 1 161 ? 13.34442  -38.05392 -16.70667 1.000 163.74994 ? 162 LEU   A C      1 
ATOM   2253 O O      . LEU   A 1 161 ? 12.43810  -38.68957 -17.25224 1.000 166.31849 ? 162 LEU   A O      1 
ATOM   2254 C CB     . LEU   A 1 161 ? 11.99361  -36.93747 -14.92789 1.000 175.12574 ? 162 LEU   A CB     1 
ATOM   2255 C CG     . LEU   A 1 161 ? 11.80543  -35.83407 -13.88717 1.000 177.64593 ? 162 LEU   A CG     1 
ATOM   2256 C CD1    . LEU   A 1 161 ? 11.33410  -34.53641 -14.52135 1.000 178.99430 ? 162 LEU   A CD1    1 
ATOM   2257 C CD2    . LEU   A 1 161 ? 10.82356  -36.29942 -12.81836 1.000 184.64731 ? 162 LEU   A CD2    1 
ATOM   2258 H H      . LEU   A 1 161 ? 11.76941  -35.89584 -17.25941 1.000 200.93244 ? 162 LEU   A H      1 
ATOM   2259 H HA     . LEU   A 1 161 ? 13.86061  -36.39646 -15.61503 1.000 205.21715 ? 162 LEU   A HA     1 
ATOM   2260 H HB2    . LEU   A 1 161 ? 11.13569  -37.05687 -15.36449 1.000 210.54135 ? 162 LEU   A HB2    1 
ATOM   2261 H HB3    . LEU   A 1 161 ? 12.23253  -37.74135 -14.44045 1.000 210.54135 ? 162 LEU   A HB3    1 
ATOM   2262 H HG     . LEU   A 1 161 ? 12.66140  -35.64795 -13.47055 1.000 213.56558 ? 162 LEU   A HG     1 
ATOM   2263 H HD11   . LEU   A 1 161 ? 11.06331  -33.92264 -13.82074 1.000 215.18363 ? 162 LEU   A HD11   1 
ATOM   2264 H HD12   . LEU   A 1 161 ? 12.06265  -34.15258 -15.03398 1.000 215.18363 ? 162 LEU   A HD12   1 
ATOM   2265 H HD13   . LEU   A 1 161 ? 10.58244  -34.72482 -15.10478 1.000 215.18363 ? 162 LEU   A HD13   1 
ATOM   2266 H HD21   . LEU   A 1 161 ? 10.74281  -35.60914 -12.14167 1.000 221.96724 ? 162 LEU   A HD21   1 
ATOM   2267 H HD22   . LEU   A 1 161 ? 9.96063   -36.46069 -13.23097 1.000 221.96724 ? 162 LEU   A HD22   1 
ATOM   2268 H HD23   . LEU   A 1 161 ? 11.15690  -37.11767 -12.41805 1.000 221.96724 ? 162 LEU   A HD23   1 
ATOM   2269 N N      . THR   A 1 162 ? 14.60203  -38.48327 -16.64690 1.000 156.20847 ? 163 THR   A N      1 
ATOM   2270 C CA     . THR   A 1 162 ? 15.04456  -39.71713 -17.28291 1.000 151.15064 ? 163 THR   A CA     1 
ATOM   2271 C C      . THR   A 1 162 ? 15.17746  -40.81925 -16.24088 1.000 158.74756 ? 163 THR   A C      1 
ATOM   2272 O O      . THR   A 1 162 ? 15.84898  -40.63617 -15.22134 1.000 167.88668 ? 163 THR   A O      1 
ATOM   2273 C CB     . THR   A 1 162 ? 16.38357  -39.51110 -17.99330 1.000 155.19549 ? 163 THR   A CB     1 
ATOM   2274 O OG1    . THR   A 1 162 ? 16.24941  -38.48336 -18.98234 1.000 163.54877 ? 163 THR   A OG1    1 
ATOM   2275 C CG2    . THR   A 1 162 ? 16.84540  -40.80176 -18.65742 1.000 150.96412 ? 163 THR   A CG2    1 
ATOM   2276 H H      . THR   A 1 162 ? 15.23054  -38.06625 -16.23378 1.000 187.84064 ? 163 THR   A H      1 
ATOM   2277 H HA     . THR   A 1 162 ? 14.38342  -39.99247 -17.93711 1.000 181.77124 ? 163 THR   A HA     1 
ATOM   2278 H HB     . THR   A 1 162 ? 17.05583  -39.24827 -17.34531 1.000 186.62506 ? 163 THR   A HB     1 
ATOM   2279 H HG1    . THR   A 1 162 ? 16.99695  -38.31779 -19.32784 1.000 196.64899 ? 163 THR   A HG1    1 
ATOM   2280 H HG21   . THR   A 1 162 ? 17.61260  -40.62691 -19.22464 1.000 181.54741 ? 163 THR   A HG21   1 
ATOM   2281 H HG22   . THR   A 1 162 ? 17.09495  -41.45160 -17.98189 1.000 181.54741 ? 163 THR   A HG22   1 
ATOM   2282 H HG23   . THR   A 1 162 ? 16.13043  -41.17011 -19.19967 1.000 181.54741 ? 163 THR   A HG23   1 
ATOM   2283 N N      . PHE   A 1 163 ? 14.54984  -41.96208 -16.50505 1.000 155.85972 ? 164 PHE   A N      1 
ATOM   2284 C CA     . PHE   A 1 163 ? 14.60608  -43.11461 -15.61852 1.000 161.56721 ? 164 PHE   A CA     1 
ATOM   2285 C C      . PHE   A 1 163 ? 15.31848  -44.26612 -16.31509 1.000 173.22796 ? 164 PHE   A C      1 
ATOM   2286 O O      . PHE   A 1 163 ? 15.20568  -44.44450 -17.53191 1.000 201.86286 ? 164 PHE   A O      1 
ATOM   2287 C CB     . PHE   A 1 163 ? 13.20084  -43.54483 -15.18357 1.000 162.32770 ? 164 PHE   A CB     1 
ATOM   2288 C CG     . PHE   A 1 163 ? 12.45236  -42.48353 -14.42520 1.000 163.93581 ? 164 PHE   A CG     1 
ATOM   2289 C CD1    . PHE   A 1 163 ? 12.59362  -42.36381 -13.05155 1.000 171.34454 ? 164 PHE   A CD1    1 
ATOM   2290 C CD2    . PHE   A 1 163 ? 11.61263  -41.60181 -15.08582 1.000 167.55251 ? 164 PHE   A CD2    1 
ATOM   2291 C CE1    . PHE   A 1 163 ? 11.90829  -41.38739 -12.35053 1.000 140.78363 ? 164 PHE   A CE1    1 
ATOM   2292 C CE2    . PHE   A 1 163 ? 10.92481  -40.62325 -14.39021 1.000 165.74775 ? 164 PHE   A CE2    1 
ATOM   2293 C CZ     . PHE   A 1 163 ? 11.07398  -40.51650 -13.02064 1.000 151.33963 ? 164 PHE   A CZ     1 
ATOM   2294 H H      . PHE   A 1 163 ? 14.07441  -42.09454 -17.20934 1.000 187.42213 ? 164 PHE   A H      1 
ATOM   2295 H HA     . PHE   A 1 163 ? 15.11055  -42.89172 -14.82056 1.000 194.27113 ? 164 PHE   A HA     1 
ATOM   2296 H HB2    . PHE   A 1 163 ? 12.68323  -43.76534 -15.97373 1.000 195.18371 ? 164 PHE   A HB2    1 
ATOM   2297 H HB3    . PHE   A 1 163 ? 13.27630  -44.32248 -14.60871 1.000 195.18371 ? 164 PHE   A HB3    1 
ATOM   2298 H HD1    . PHE   A 1 163 ? 13.15614  -42.94715 -12.59529 1.000 206.00392 ? 164 PHE   A HD1    1 
ATOM   2299 H HD2    . PHE   A 1 163 ? 11.50997  -41.66836 -16.00774 1.000 201.45348 ? 164 PHE   A HD2    1 
ATOM   2300 H HE1    . PHE   A 1 163 ? 12.00993  -41.31821 -11.42870 1.000 169.33083 ? 164 PHE   A HE1    1 
ATOM   2301 H HE2    . PHE   A 1 163 ? 10.36254  -40.03782 -14.84410 1.000 199.28777 ? 164 PHE   A HE2    1 
ATOM   2302 H HZ     . PHE   A 1 163 ? 10.61296  -39.85900 -12.55155 1.000 181.99803 ? 164 PHE   A HZ     1 
ATOM   2303 N N      . GLU   A 1 164 ? 16.05602  -45.04745 -15.52941 1.000 166.92916 ? 165 GLU   A N      1 
ATOM   2304 C CA     . GLU   A 1 164 ? 16.87072  -46.12211 -16.08265 1.000 173.93040 ? 165 GLU   A CA     1 
ATOM   2305 C C      . GLU   A 1 164 ? 15.97927  -47.18975 -16.70483 1.000 180.25237 ? 165 GLU   A C      1 
ATOM   2306 O O      . GLU   A 1 164 ? 15.20053  -47.84534 -16.00460 1.000 185.98829 ? 165 GLU   A O      1 
ATOM   2307 C CB     . GLU   A 1 164 ? 17.75296  -46.73024 -14.99534 1.000 171.91741 ? 165 GLU   A CB     1 
ATOM   2308 C CG     . GLU   A 1 164 ? 18.79329  -47.70916 -15.52183 1.000 176.31888 ? 165 GLU   A CG     1 
ATOM   2309 C CD     . GLU   A 1 164 ? 19.76426  -48.16663 -14.45104 1.000 162.91003 ? 165 GLU   A CD     1 
ATOM   2310 O OE1    . GLU   A 1 164 ? 19.31503  -48.76811 -13.45249 1.000 155.36664 ? 165 GLU   A OE1    1 
ATOM   2311 O OE2    . GLU   A 1 164 ? 20.97831  -47.91629 -14.60625 1.000 175.53028 ? 165 GLU   A OE2    1 
ATOM   2312 H H      . GLU   A 1 164 ? 16.10111  -44.97495 -14.67365 1.000 200.70546 ? 165 GLU   A H      1 
ATOM   2313 H HA     . GLU   A 1 164 ? 17.44445  -45.76003 -16.77593 1.000 209.10695 ? 165 GLU   A HA     1 
ATOM   2314 H HB2    . GLU   A 1 164 ? 18.22393  -46.01474 -14.54020 1.000 206.69136 ? 165 GLU   A HB2    1 
ATOM   2315 H HB3    . GLU   A 1 164 ? 17.18859  -47.20791 -14.36747 1.000 206.69136 ? 165 GLU   A HB3    1 
ATOM   2316 H HG2    . GLU   A 1 164 ? 18.34123  -48.49303 -15.87126 1.000 211.97312 ? 165 GLU   A HG2    1 
ATOM   2317 H HG3    . GLU   A 1 164 ? 19.30392  -47.27934 -16.22569 1.000 211.97312 ? 165 GLU   A HG3    1 
ATOM   2318 N N      . ASP   A 1 165 ? 16.09549  -47.36558 -18.02110 1.000 168.17470 ? 166 ASP   A N      1 
ATOM   2319 C CA     . ASP   A 1 165 ? 15.34851  -48.39292 -18.74235 1.000 168.33386 ? 166 ASP   A CA     1 
ATOM   2320 C C      . ASP   A 1 165 ? 13.84612  -48.24935 -18.52683 1.000 171.47063 ? 166 ASP   A C      1 
ATOM   2321 O O      . ASP   A 1 165 ? 13.11741  -49.24250 -18.46143 1.000 188.08908 ? 166 ASP   A O      1 
ATOM   2322 C CB     . ASP   A 1 165 ? 15.81223  -49.79368 -18.33483 1.000 173.33389 ? 166 ASP   A CB     1 
ATOM   2323 C CG     . ASP   A 1 165 ? 17.31060  -49.97218 -18.47312 1.000 172.66944 ? 166 ASP   A CG     1 
ATOM   2324 O OD1    . ASP   A 1 165 ? 17.90716  -49.33011 -19.36338 1.000 175.14154 ? 166 ASP   A OD1    1 
ATOM   2325 O OD2    . ASP   A 1 165 ? 17.89262  -50.75106 -17.68931 1.000 171.49004 ? 166 ASP   A OD2    1 
ATOM   2326 H H      . ASP   A 1 165 ? 16.60888  -46.89443 -18.52514 1.000 202.20011 ? 166 ASP   A H      1 
ATOM   2327 H HA     . ASP   A 1 165 ? 15.51683  -48.28316 -19.69131 1.000 202.39111 ? 166 ASP   A HA     1 
ATOM   2328 H HB2    . ASP   A 1 165 ? 15.57505  -49.94873 -17.40714 1.000 208.39114 ? 166 ASP   A HB2    1 
ATOM   2329 H HB3    . ASP   A 1 165 ? 15.37743  -50.44917 -18.90244 1.000 208.39114 ? 166 ASP   A HB3    1 
ATOM   2330 N N      . LYS   A 1 166 ? 13.37472  -47.01194 -18.40968 1.000 163.74600 ? 167 LYS   A N      1 
ATOM   2331 C CA     . LYS   A 1 166 ? 11.95941  -46.72578 -18.23545 1.000 163.85858 ? 167 LYS   A CA     1 
ATOM   2332 C C      . LYS   A 1 166 ? 11.65720  -45.40551 -18.92260 1.000 164.58090 ? 167 LYS   A C      1 
ATOM   2333 O O      . LYS   A 1 166 ? 12.55181  -44.56192 -19.05921 1.000 162.69059 ? 167 LYS   A O      1 
ATOM   2334 C CB     . LYS   A 1 166 ? 11.57321  -46.66084 -16.75083 1.000 173.29042 ? 167 LYS   A CB     1 
ATOM   2335 C CG     . LYS   A 1 166 ? 11.55326  -48.01647 -16.04694 1.000 176.52629 ? 167 LYS   A CG     1 
ATOM   2336 C CD     . LYS   A 1 166 ? 10.40184  -48.88880 -16.53371 1.000 173.89085 ? 167 LYS   A CD     1 
ATOM   2337 C CE     . LYS   A 1 166 ? 10.33453  -50.21233 -15.77994 1.000 181.69857 ? 167 LYS   A CE     1 
ATOM   2338 N NZ     . LYS   A 1 166 ? 11.49937  -51.09406 -16.07297 1.000 174.36421 ? 167 LYS   A NZ     1 
ATOM   2339 H H      . LYS   A 1 166 ? 13.86768  -46.30751 -18.42875 1.000 196.88568 ? 167 LYS   A H      1 
ATOM   2340 H HA     . LYS   A 1 166 ? 11.42561  -47.41986 -18.65282 1.000 197.02077 ? 167 LYS   A HA     1 
ATOM   2341 H HB2    . LYS   A 1 166 ? 12.21445  -46.09893 -16.28827 1.000 208.33898 ? 167 LYS   A HB2    1 
ATOM   2342 H HB3    . LYS   A 1 166 ? 10.68448  -46.27899 -16.67839 1.000 208.33898 ? 167 LYS   A HB3    1 
ATOM   2343 H HG2    . LYS   A 1 166 ? 12.38464  -48.48286 -16.22636 1.000 212.22201 ? 167 LYS   A HG2    1 
ATOM   2344 H HG3    . LYS   A 1 166 ? 11.44865  -47.88022 -15.09228 1.000 212.22201 ? 167 LYS   A HG3    1 
ATOM   2345 H HD2    . LYS   A 1 166 ? 9.56438   -48.41885 -16.39689 1.000 209.05949 ? 167 LYS   A HD2    1 
ATOM   2346 H HD3    . LYS   A 1 166 ? 10.52345  -49.08241 -17.47638 1.000 209.05949 ? 167 LYS   A HD3    1 
ATOM   2347 H HE2    . LYS   A 1 166 ? 10.32400  -50.03446 -14.82645 1.000 218.42875 ? 167 LYS   A HE2    1 
ATOM   2348 H HE3    . LYS   A 1 166 ? 9.52736   -50.68414 -16.03835 1.000 218.42875 ? 167 LYS   A HE3    1 
ATOM   2349 H HZ1    . LYS   A 1 166 ? 11.23708  -51.94388 -16.10632 1.000 209.62752 ? 167 LYS   A HZ1    1 
ATOM   2350 H HZ2    . LYS   A 1 166 ? 11.85982  -50.87210 -16.85586 1.000 209.62752 ? 167 LYS   A HZ2    1 
ATOM   2351 H HZ3    . LYS   A 1 166 ? 12.11511  -51.00659 -15.43633 1.000 209.62752 ? 167 LYS   A HZ3    1 
ATOM   2352 N N      . PRO   A 1 167 ? 10.41993  -45.19606 -19.36800 1.000 172.08669 ? 168 PRO   A N      1 
ATOM   2353 C CA     . PRO   A 1 167 ? 10.11024  -43.96918 -20.11142 1.000 180.20184 ? 168 PRO   A CA     1 
ATOM   2354 C C      . PRO   A 1 167 ? 10.31070  -42.72870 -19.25589 1.000 171.61859 ? 168 PRO   A C      1 
ATOM   2355 O O      . PRO   A 1 167 ? 10.03338  -42.72461 -18.05520 1.000 170.08458 ? 168 PRO   A O      1 
ATOM   2356 C CB     . PRO   A 1 167 ? 8.63986   -44.15267 -20.50834 1.000 187.45559 ? 168 PRO   A CB     1 
ATOM   2357 C CG     . PRO   A 1 167 ? 8.09746   -45.14838 -19.53844 1.000 178.53287 ? 168 PRO   A CG     1 
ATOM   2358 C CD     . PRO   A 1 167 ? 9.23906   -46.06375 -19.20870 1.000 175.54797 ? 168 PRO   A CD     1 
ATOM   2359 H HA     . PRO   A 1 167 ? 10.66012  -43.90553 -20.90797 1.000 216.63268 ? 168 PRO   A HA     1 
ATOM   2360 H HB2    . PRO   A 1 167 ? 8.17066   -43.30679 -20.43597 1.000 225.33718 ? 168 PRO   A HB2    1 
ATOM   2361 H HB3    . PRO   A 1 167 ? 8.58279   -44.48702 -21.41711 1.000 225.33718 ? 168 PRO   A HB3    1 
ATOM   2362 H HG2    . PRO   A 1 167 ? 7.78243   -44.69180 -18.74270 1.000 214.62991 ? 168 PRO   A HG2    1 
ATOM   2363 H HG3    . PRO   A 1 167 ? 7.36941   -45.64118 -19.94831 1.000 214.62991 ? 168 PRO   A HG3    1 
ATOM   2364 H HD2    . PRO   A 1 167 ? 9.16938   -46.38935 -18.29765 1.000 211.04803 ? 168 PRO   A HD2    1 
ATOM   2365 H HD3    . PRO   A 1 167 ? 9.27291   -46.81091 -19.82637 1.000 211.04803 ? 168 PRO   A HD3    1 
ATOM   2366 N N      . SER   A 1 168 ? 10.79673  -41.66832 -19.89243 1.000 167.91426 ? 169 SER   A N      1 
ATOM   2367 C CA     . SER   A 1 168 ? 11.03576  -40.41423 -19.20009 1.000 173.34291 ? 169 SER   A CA     1 
ATOM   2368 C C      . SER   A 1 168 ? 9.72551   -39.65444 -19.01410 1.000 172.78079 ? 169 SER   A C      1 
ATOM   2369 O O      . SER   A 1 168 ? 8.71572   -39.92959 -19.66747 1.000 176.41799 ? 169 SER   A O      1 
ATOM   2370 C CB     . SER   A 1 168 ? 12.04469  -39.56347 -19.97162 1.000 173.79070 ? 169 SER   A CB     1 
ATOM   2371 O OG     . SER   A 1 168 ? 13.25918  -40.27086 -20.15916 1.000 169.69231 ? 169 SER   A OG     1 
ATOM   2372 H H      . SER   A 1 168 ? 10.99626  -41.65202 -20.72881 1.000 201.88758 ? 169 SER   A H      1 
ATOM   2373 H HA     . SER   A 1 168 ? 11.40744  -40.58945 -18.32143 1.000 208.40196 ? 169 SER   A HA     1 
ATOM   2374 H HB2    . SER   A 1 168 ? 11.67197  -39.33985 -20.83878 1.000 208.93931 ? 169 SER   A HB2    1 
ATOM   2375 H HB3    . SER   A 1 168 ? 12.22496  -38.75357 -19.46915 1.000 208.93931 ? 169 SER   A HB3    1 
ATOM   2376 H HG     . SER   A 1 168 ? 13.74488  -39.86622 -20.71230 1.000 204.02124 ? 169 SER   A HG     1 
ATOM   2377 N N      . GLU   A 1 169 ? 9.75319   -38.68799 -18.09948 1.000 177.61514 ? 170 GLU   A N      1 
ATOM   2378 C CA     . GLU   A 1 169 ? 8.57246   -37.91846 -17.74169 1.000 167.24622 ? 170 GLU   A CA     1 
ATOM   2379 C C      . GLU   A 1 169 ? 8.95994   -36.45412 -17.60986 1.000 165.71623 ? 170 GLU   A C      1 
ATOM   2380 O O      . GLU   A 1 169 ? 10.14025  -36.09543 -17.63492 1.000 161.70867 ? 170 GLU   A O      1 
ATOM   2381 C CB     . GLU   A 1 169 ? 7.94778   -38.42842 -16.43818 1.000 174.31715 ? 170 GLU   A CB     1 
ATOM   2382 C CG     . GLU   A 1 169 ? 7.52381   -39.88727 -16.48434 1.000 165.03239 ? 170 GLU   A CG     1 
ATOM   2383 C CD     . GLU   A 1 169 ? 6.33644   -40.12393 -17.39495 1.000 164.92189 ? 170 GLU   A CD     1 
ATOM   2384 O OE1    . GLU   A 1 169 ? 5.84113   -39.14845 -17.99698 1.000 171.11734 ? 170 GLU   A OE1    1 
ATOM   2385 O OE2    . GLU   A 1 169 ? 5.89589   -41.28691 -17.50575 1.000 162.52959 ? 170 GLU   A OE2    1 
ATOM   2386 H H      . GLU   A 1 169 ? 10.45917  -38.45741 -17.66586 1.000 213.52864 ? 170 GLU   A H      1 
ATOM   2387 H HA     . GLU   A 1 169 ? 7.91176   -37.99639 -18.44759 1.000 201.08594 ? 170 GLU   A HA     1 
ATOM   2388 H HB2    . GLU   A 1 169 ? 8.59714   -38.33241 -15.72403 1.000 209.57105 ? 170 GLU   A HB2    1 
ATOM   2389 H HB3    . GLU   A 1 169 ? 7.15933   -37.89813 -16.24317 1.000 209.57105 ? 170 GLU   A HB3    1 
ATOM   2390 H HG2    . GLU   A 1 169 ? 8.26424   -40.42141 -16.81199 1.000 198.42934 ? 170 GLU   A HG2    1 
ATOM   2391 H HG3    . GLU   A 1 169 ? 7.27818   -40.17348 -15.59067 1.000 198.42934 ? 170 GLU   A HG3    1 
ATOM   2392 N N      . THR   A 1 170 ? 7.95055   -35.60478 -17.46996 1.000 164.24487 ? 171 THR   A N      1 
ATOM   2393 C CA     . THR   A 1 170 ? 8.14612   -34.16831 -17.34294 1.000 164.46312 ? 171 THR   A CA     1 
ATOM   2394 C C      . THR   A 1 170 ? 7.56171   -33.67930 -16.02235 1.000 163.91368 ? 171 THR   A C      1 
ATOM   2395 O O      . THR   A 1 170 ? 6.95592   -34.43817 -15.26301 1.000 180.12125 ? 171 THR   A O      1 
ATOM   2396 C CB     . THR   A 1 170 ? 7.50790   -33.41901 -18.51449 1.000 171.23047 ? 171 THR   A CB     1 
ATOM   2397 O OG1    . THR   A 1 170 ? 6.09796   -33.67431 -18.53467 1.000 176.49115 ? 171 THR   A OG1    1 
ATOM   2398 C CG2    . THR   A 1 170 ? 8.12736   -33.85921 -19.82837 1.000 172.49973 ? 171 THR   A CG2    1 
ATOM   2399 H H      . THR   A 1 170 ? 7.12474   -35.84361 -17.44538 1.000 197.48431 ? 171 THR   A H      1 
ATOM   2400 H HA     . THR   A 1 170 ? 9.09954   -33.98977 -17.34465 1.000 197.74621 ? 171 THR   A HA     1 
ATOM   2401 H HB     . THR   A 1 170 ? 7.65910   -32.46614 -18.41411 1.000 205.86704 ? 171 THR   A HB     1 
ATOM   2402 H HG1    . THR   A 1 170 ? 5.73752   -33.35058 -17.84847 1.000 212.17985 ? 171 THR   A HG1    1 
ATOM   2403 H HG21   . THR   A 1 170 ? 7.74426   -33.35307 -20.56183 1.000 207.39015 ? 171 THR   A HG21   1 
ATOM   2404 H HG22   . THR   A 1 170 ? 9.08566   -33.71018 -19.80975 1.000 207.39015 ? 171 THR   A HG22   1 
ATOM   2405 H HG23   . THR   A 1 170 ? 7.95835   -34.80304 -19.97509 1.000 207.39015 ? 171 THR   A HG23   1 
ATOM   2406 N N      . ALA   A 1 171 ? 7.76429   -32.38923 -15.75333 1.000 167.41191 ? 172 ALA   A N      1 
ATOM   2407 C CA     . ALA   A 1 171 ? 7.24469   -31.76052 -14.54611 1.000 177.95686 ? 172 ALA   A CA     1 
ATOM   2408 C C      . ALA   A 1 171 ? 7.52309   -30.26287 -14.55550 1.000 178.99959 ? 172 ALA   A C      1 
ATOM   2409 O O      . ALA   A 1 171 ? 8.48752   -29.81110 -15.18261 1.000 182.02854 ? 172 ALA   A O      1 
ATOM   2410 C CB     . ALA   A 1 171 ? 7.86096   -32.39428 -13.29723 1.000 173.13330 ? 172 ALA   A CB     1 
ATOM   2411 H H      . ALA   A 1 171 ? 8.20468   -31.85307 -16.26145 1.000 201.28476 ? 172 ALA   A H      1 
ATOM   2412 H HA     . ALA   A 1 171 ? 6.28480   -31.89655 -14.51421 1.000 213.93870 ? 172 ALA   A HA     1 
ATOM   2413 H HB1    . ALA   A 1 171 ? 7.46823   -31.98649 -12.50959 1.000 208.15043 ? 172 ALA   A HB1    1 
ATOM   2414 H HB2    . ALA   A 1 171 ? 7.67734   -33.34672 -13.30304 1.000 208.15043 ? 172 ALA   A HB2    1 
ATOM   2415 H HB3    . ALA   A 1 171 ? 8.81890   -32.24203 -13.30577 1.000 208.15043 ? 172 ALA   A HB3    1 
ATOM   2416 N N      . ASP   A 1 172 ? 6.69352   -29.48803 -13.85566 1.000 178.18927 ? 173 ASP   A N      1 
ATOM   2417 C CA     . ASP   A 1 172 ? 6.93210   -28.05697 -13.71137 1.000 183.49864 ? 173 ASP   A CA     1 
ATOM   2418 C C      . ASP   A 1 172 ? 7.80299   -27.73526 -12.50600 1.000 174.68603 ? 173 ASP   A C      1 
ATOM   2419 O O      . ASP   A 1 172 ? 8.58998   -26.78207 -12.55389 1.000 172.80934 ? 173 ASP   A O      1 
ATOM   2420 C CB     . ASP   A 1 172 ? 5.60125   -27.30966 -13.59400 1.000 188.22585 ? 173 ASP   A CB     1 
ATOM   2421 C CG     . ASP   A 1 172 ? 4.69437   -27.54800 -14.78397 1.000 185.29016 ? 173 ASP   A CG     1 
ATOM   2422 O OD1    . ASP   A 1 172 ? 5.16317   -27.41242 -15.93336 1.000 179.01287 ? 173 ASP   A OD1    1 
ATOM   2423 O OD2    . ASP   A 1 172 ? 3.51211   -27.88402 -14.56881 1.000 184.87764 ? 173 ASP   A OD2    1 
ATOM   2424 H H      . ASP   A 1 172 ? 5.98608   -29.76937 -13.45569 1.000 214.21759 ? 173 ASP   A H      1 
ATOM   2425 H HA     . ASP   A 1 172 ? 7.38399   -27.73067 -14.50524 1.000 220.58884 ? 173 ASP   A HA     1 
ATOM   2426 H HB2    . ASP   A 1 172 ? 5.13758   -27.61135 -12.79719 1.000 226.26149 ? 173 ASP   A HB2    1 
ATOM   2427 H HB3    . ASP   A 1 172 ? 5.77658   -26.35744 -13.53531 1.000 226.26149 ? 173 ASP   A HB3    1 
ATOM   2428 N N      . LEU   A 1 173 ? 7.68342   -28.51514 -11.43326 1.000 171.85730 ? 174 LEU   A N      1 
ATOM   2429 C CA     . LEU   A 1 173 ? 8.46746   -28.32227 -10.22153 1.000 162.51901 ? 174 LEU   A CA     1 
ATOM   2430 C C      . LEU   A 1 173 ? 8.91201   -29.67890 -9.70065  1.000 153.31293 ? 174 LEU   A C      1 
ATOM   2431 O O      . LEU   A 1 173 ? 8.08396   -30.57356 -9.50363  1.000 144.40054 ? 174 LEU   A O      1 
ATOM   2432 C CB     . LEU   A 1 173 ? 7.65834   -27.58235 -9.15030  1.000 172.34924 ? 174 LEU   A CB     1 
ATOM   2433 C CG     . LEU   A 1 173 ? 8.20655   -27.62117 -7.72131  1.000 170.97465 ? 174 LEU   A CG     1 
ATOM   2434 C CD1    . LEU   A 1 173 ? 9.61835   -27.06174 -7.65197  1.000 173.48672 ? 174 LEU   A CD1    1 
ATOM   2435 C CD2    . LEU   A 1 173 ? 7.28419   -26.85755 -6.78099  1.000 162.88473 ? 174 LEU   A CD2    1 
ATOM   2436 H H      . LEU   A 1 173 ? 7.13970   -29.17965 -11.38421 1.000 206.61923 ? 174 LEU   A H      1 
ATOM   2437 H HA     . LEU   A 1 173 ? 9.25766   -27.79733 -10.42384 1.000 195.41328 ? 174 LEU   A HA     1 
ATOM   2438 H HB2    . LEU   A 1 173 ? 7.60397   -26.64880 -9.40804  1.000 207.20956 ? 174 LEU   A HB2    1 
ATOM   2439 H HB3    . LEU   A 1 173 ? 6.77023   -27.97156 -9.12412  1.000 207.20956 ? 174 LEU   A HB3    1 
ATOM   2440 H HG     . LEU   A 1 173 ? 8.24667   -28.54625 -7.43232  1.000 205.56005 ? 174 LEU   A HG     1 
ATOM   2441 H HD11   . LEU   A 1 173 ? 9.95104   -27.15551 -6.74565  1.000 208.57453 ? 174 LEU   A HD11   1 
ATOM   2442 H HD12   . LEU   A 1 173 ? 10.18448  -27.55632 -8.26498  1.000 208.57453 ? 174 LEU   A HD12   1 
ATOM   2443 H HD13   . LEU   A 1 173 ? 9.59938   -26.12473 -7.90207  1.000 208.57453 ? 174 LEU   A HD13   1 
ATOM   2444 H HD21   . LEU   A 1 173 ? 7.65822   -26.87792 -5.88623  1.000 195.85214 ? 174 LEU   A HD21   1 
ATOM   2445 H HD22   . LEU   A 1 173 ? 7.20973   -25.94030 -7.08758  1.000 195.85214 ? 174 LEU   A HD22   1 
ATOM   2446 H HD23   . LEU   A 1 173 ? 6.41066   -27.27928 -6.78403  1.000 195.85214 ? 174 LEU   A HD23   1 
ATOM   2447 N N      . VAL   A 1 174 ? 10.21481  -29.82308 -9.47595  1.000 147.90743 ? 175 VAL   A N      1 
ATOM   2448 C CA     . VAL   A 1 174 ? 10.80472  -31.05237 -8.96294  1.000 147.67094 ? 175 VAL   A CA     1 
ATOM   2449 C C      . VAL   A 1 174 ? 11.24806  -30.81552 -7.52722  1.000 141.17115 ? 175 VAL   A C      1 
ATOM   2450 O O      . VAL   A 1 174 ? 11.83941  -29.77629 -7.21154  1.000 141.43260 ? 175 VAL   A O      1 
ATOM   2451 C CB     . VAL   A 1 174 ? 11.99094  -31.51407 -9.83195  1.000 154.53371 ? 175 VAL   A CB     1 
ATOM   2452 C CG1    . VAL   A 1 174 ? 12.65830  -32.73699 -9.22002  1.000 161.28326 ? 175 VAL   A CG1    1 
ATOM   2453 C CG2    . VAL   A 1 174 ? 11.52582  -31.80934 -11.24777 1.000 143.62172 ? 175 VAL   A CG2    1 
ATOM   2454 H H      . VAL   A 1 174 ? 10.79323  -29.20272 -9.61799  1.000 177.87939 ? 175 VAL   A H      1 
ATOM   2455 H HA     . VAL   A 1 174 ? 10.13377  -31.75287 -8.96619  1.000 177.59560 ? 175 VAL   A HA     1 
ATOM   2456 H HB     . VAL   A 1 174 ? 12.64814  -30.80169 -9.87072  1.000 185.83092 ? 175 VAL   A HB     1 
ATOM   2457 H HG11   . VAL   A 1 174 ? 13.33467  -33.06704 -9.83197  1.000 193.93039 ? 175 VAL   A HG11   1 
ATOM   2458 H HG12   . VAL   A 1 174 ? 13.06874  -32.48468 -8.37813  1.000 193.93039 ? 175 VAL   A HG12   1 
ATOM   2459 H HG13   . VAL   A 1 174 ? 11.98699  -33.42067 -9.06895  1.000 193.93039 ? 175 VAL   A HG13   1 
ATOM   2460 H HG21   . VAL   A 1 174 ? 12.27369  -32.15390 -11.76047 1.000 172.73653 ? 175 VAL   A HG21   1 
ATOM   2461 H HG22   . VAL   A 1 174 ? 10.81506  -32.46865 -11.21564 1.000 172.73653 ? 175 VAL   A HG22   1 
ATOM   2462 H HG23   . VAL   A 1 174 ? 11.19865  -30.98959 -11.65011 1.000 172.73653 ? 175 VAL   A HG23   1 
ATOM   2463 N N      . ILE   A 1 175 ? 10.96401  -31.78336 -6.66059  1.000 144.14195 ? 176 ILE   A N      1 
ATOM   2464 C CA     . ILE   A 1 175 ? 11.36445  -31.74373 -5.25886  1.000 137.25034 ? 176 ILE   A CA     1 
ATOM   2465 C C      . ILE   A 1 175 ? 12.24008  -32.96276 -5.01196  1.000 129.36745 ? 176 ILE   A C      1 
ATOM   2466 O O      . ILE   A 1 175 ? 11.75542  -34.10121 -5.04236  1.000 130.72199 ? 176 ILE   A O      1 
ATOM   2467 C CB     . ILE   A 1 175 ? 10.15755  -31.72301 -4.31239  1.000 121.78599 ? 176 ILE   A CB     1 
ATOM   2468 C CG1    . ILE   A 1 175 ? 9.31938   -30.46829 -4.57082  1.000 123.01103 ? 176 ILE   A CG1    1 
ATOM   2469 C CG2    . ILE   A 1 175 ? 10.61893  -31.77143 -2.86108  1.000 128.59135 ? 176 ILE   A CG2    1 
ATOM   2470 C CD1    . ILE   A 1 175 ? 8.04693   -30.39048 -3.75648  1.000 156.83976 ? 176 ILE   A CD1    1 
ATOM   2471 H H      . ILE   A 1 175 ? 10.52693  -32.49423 -6.86848  1.000 173.36081 ? 176 ILE   A H      1 
ATOM   2472 H HA     . ILE   A 1 175 ? 11.89061  -30.94599 -5.09252  1.000 165.09088 ? 176 ILE   A HA     1 
ATOM   2473 H HB     . ILE   A 1 175 ? 9.61099   -32.50587 -4.48358  1.000 146.53366 ? 176 ILE   A HB     1 
ATOM   2474 H HG12   . ILE   A 1 175 ? 9.85439   -29.68854 -4.35482  1.000 148.00371 ? 176 ILE   A HG12   1 
ATOM   2475 H HG13   . ILE   A 1 175 ? 9.06982   -30.45016 -5.50799  1.000 148.00371 ? 176 ILE   A HG13   1 
ATOM   2476 H HG21   . ILE   A 1 175 ? 9.84180   -31.74001 -2.28144  1.000 154.70010 ? 176 ILE   A HG21   1 
ATOM   2477 H HG22   . ILE   A 1 175 ? 11.10906  -32.59526 -2.71284  1.000 154.70010 ? 176 ILE   A HG22   1 
ATOM   2478 H HG23   . ILE   A 1 175 ? 11.19281  -31.00913 -2.68654  1.000 154.70010 ? 176 ILE   A HG23   1 
ATOM   2479 H HD11   . ILE   A 1 175 ? 7.52793   -29.62684 -4.05379  1.000 188.59818 ? 176 ILE   A HD11   1 
ATOM   2480 H HD12   . ILE   A 1 175 ? 7.53872   -31.20647 -3.88599  1.000 188.59818 ? 176 ILE   A HD12   1 
ATOM   2481 H HD13   . ILE   A 1 175 ? 8.27723   -30.28938 -2.81966  1.000 188.59818 ? 176 ILE   A HD13   1 
ATOM   2482 N N      . ILE   A 1 176 ? 13.52365  -32.72768 -4.76198  1.000 134.92068 ? 177 ILE   A N      1 
ATOM   2483 C CA     . ILE   A 1 176 ? 14.49111  -33.80881 -4.61294  1.000 127.95143 ? 177 ILE   A CA     1 
ATOM   2484 C C      . ILE   A 1 176 ? 14.39318  -34.36408 -3.19859  1.000 126.51111 ? 177 ILE   A C      1 
ATOM   2485 O O      . ILE   A 1 176 ? 14.57411  -33.63286 -2.21949  1.000 142.07764 ? 177 ILE   A O      1 
ATOM   2486 C CB     . ILE   A 1 176 ? 15.91421  -33.31904 -4.91664  1.000 150.50423 ? 177 ILE   A CB     1 
ATOM   2487 C CG1    . ILE   A 1 176 ? 15.97785  -32.69676 -6.31625  1.000 160.80921 ? 177 ILE   A CG1    1 
ATOM   2488 C CG2    . ILE   A 1 176 ? 16.91209  -34.46063 -4.78313  1.000 143.74161 ? 177 ILE   A CG2    1 
ATOM   2489 C CD1    . ILE   A 1 176 ? 15.54234  -33.62648 -7.43890  1.000 152.32166 ? 177 ILE   A CD1    1 
ATOM   2490 H H      . ILE   A 1 176 ? 13.86290  -31.94241 -4.67328  1.000 162.29528 ? 177 ILE   A H      1 
ATOM   2491 H HA     . ILE   A 1 176 ? 14.27161  -34.52058 -5.23432  1.000 153.93219 ? 177 ILE   A HA     1 
ATOM   2492 H HB     . ILE   A 1 176 ? 16.14794  -32.63536 -4.26945  1.000 180.99555 ? 177 ILE   A HB     1 
ATOM   2493 H HG12   . ILE   A 1 176 ? 15.39645  -31.92057 -6.33629  1.000 193.36152 ? 177 ILE   A HG12   1 
ATOM   2494 H HG13   . ILE   A 1 176 ? 16.89327  -32.43028 -6.49484  1.000 193.36152 ? 177 ILE   A HG13   1 
ATOM   2495 H HG21   . ILE   A 1 176 ? 17.76172  -34.18310 -5.15998  1.000 172.88040 ? 177 ILE   A HG21   1 
ATOM   2496 H HG22   . ILE   A 1 176 ? 17.02153  -34.67618 -3.84373  1.000 172.88040 ? 177 ILE   A HG22   1 
ATOM   2497 H HG23   . ILE   A 1 176 ? 16.57414  -35.23318 -5.26257  1.000 172.88040 ? 177 ILE   A HG23   1 
ATOM   2498 H HD11   . ILE   A 1 176 ? 15.68969  -33.18475 -8.28982  1.000 183.17646 ? 177 ILE   A HD11   1 
ATOM   2499 H HD12   . ILE   A 1 176 ? 16.06571  -34.44196 -7.39453  1.000 183.17646 ? 177 ILE   A HD12   1 
ATOM   2500 H HD13   . ILE   A 1 176 ? 14.60040  -33.83170 -7.33148  1.000 183.17646 ? 177 ILE   A HD13   1 
ATOM   2501 N N      . ALA   A 1 177 ? 14.10936  -35.66453 -3.09029  1.000 124.08530 ? 178 ALA   A N      1 
ATOM   2502 C CA     . ALA   A 1 177 ? 14.00389  -36.32710 -1.79699  1.000 123.31817 ? 178 ALA   A CA     1 
ATOM   2503 C C      . ALA   A 1 177 ? 14.57109  -37.73992 -1.85148  1.000 120.55330 ? 178 ALA   A C      1 
ATOM   2504 O O      . ALA   A 1 177 ? 14.10987  -38.62485 -1.12246  1.000 126.69251 ? 178 ALA   A O      1 
ATOM   2505 C CB     . ALA   A 1 177 ? 12.54947  -36.37357 -1.32147  1.000 122.41738 ? 178 ALA   A CB     1 
ATOM   2506 H H      . ALA   A 1 177 ? 13.97290  -36.18645 -3.76005  1.000 149.29284 ? 178 ALA   A H      1 
ATOM   2507 H HA     . ALA   A 1 177 ? 14.51973  -35.82117 -1.14981  1.000 148.37227 ? 178 ALA   A HA     1 
ATOM   2508 H HB1    . ALA   A 1 177 ? 12.51207  -36.82402 -0.46323  1.000 147.29133 ? 178 ALA   A HB1    1 
ATOM   2509 H HB2    . ALA   A 1 177 ? 12.21675  -35.46664 -1.23382  1.000 147.29133 ? 178 ALA   A HB2    1 
ATOM   2510 H HB3    . ALA   A 1 177 ? 12.01952  -36.85879 -1.97309  1.000 147.29133 ? 178 ALA   A HB3    1 
ATOM   2511 N N      . ASN   A 1 178 ? 15.56956  -37.97247 -2.70806  1.000 126.18566 ? 179 ASN   A N      1 
ATOM   2512 C CA     . ASN   A 1 178 ? 16.08697  -39.31405 -2.95056  1.000 125.64337 ? 179 ASN   A CA     1 
ATOM   2513 C C      . ASN   A 1 178 ? 17.28131  -39.66191 -2.06863  1.000 124.10177 ? 179 ASN   A C      1 
ATOM   2514 O O      . ASN   A 1 178 ? 18.10773  -40.49875 -2.45677  1.000 121.92795 ? 179 ASN   A O      1 
ATOM   2515 C CB     . ASN   A 1 178 ? 16.45368  -39.47774 -4.42642  1.000 130.41615 ? 179 ASN   A CB     1 
ATOM   2516 C CG     . ASN   A 1 178 ? 17.55791  -38.54178 -4.85958  1.000 134.26094 ? 179 ASN   A CG     1 
ATOM   2517 O OD1    . ASN   A 1 178 ? 17.59205  -37.37679 -4.46373  1.000 134.34377 ? 179 ASN   A OD1    1 
ATOM   2518 N ND2    . ASN   A 1 178 ? 18.47306  -39.04793 -5.67794  1.000 134.62966 ? 179 ASN   A ND2    1 
ATOM   2519 H H      . ASN   A 1 178 ? 15.96522  -37.35976 -3.16374  1.000 151.81327 ? 179 ASN   A H      1 
ATOM   2520 H HA     . ASN   A 1 178 ? 15.38073  -39.94614 -2.74420  1.000 151.16252 ? 179 ASN   A HA     1 
ATOM   2521 H HB2    . ASN   A 1 178 ? 16.75407  -40.38738 -4.57879  1.000 156.88984 ? 179 ASN   A HB2    1 
ATOM   2522 H HB3    . ASN   A 1 178 ? 15.67177  -39.29124 -4.96930  1.000 156.88984 ? 179 ASN   A HB3    1 
ATOM   2523 H HD21   . ASN   A 1 178 ? 19.12244  -38.55613 -5.95369  1.000 161.94607 ? 179 ASN   A HD21   1 
ATOM   2524 H HD22   . ASN   A 1 178 ? 18.41635  -39.86753 -5.93219  1.000 161.94607 ? 179 ASN   A HD22   1 
ATOM   2525 N N      . GLY   A 1 179 ? 17.39924  -39.04487 -0.89639  1.000 117.86907 ? 180 GLY   A N      1 
ATOM   2526 C CA     . GLY   A 1 179 ? 18.34455  -39.48713 0.11167   1.000 125.34300 ? 180 GLY   A CA     1 
ATOM   2527 C C      . GLY   A 1 179 ? 19.58742  -38.62208 0.18293   1.000 117.39084 ? 180 GLY   A C      1 
ATOM   2528 O O      . GLY   A 1 179 ? 19.78572  -37.67436 -0.58232  1.000 109.25031 ? 180 GLY   A O      1 
ATOM   2529 H H      . GLY   A 1 179 ? 16.93517  -38.35964 -0.66253  1.000 141.83335 ? 180 GLY   A H      1 
ATOM   2530 H HA2    . GLY   A 1 179 ? 17.91414  -39.47022 0.98078   1.000 150.80207 ? 180 GLY   A HA2    1 
ATOM   2531 H HA3    . GLY   A 1 179 ? 18.61962  -40.39587 -0.08688  1.000 150.80207 ? 180 GLY   A HA3    1 
ATOM   2532 N N      . GLY   A 1 180 ? 20.44951  -38.98587 1.13778   1.000 108.09545 ? 181 GLY   A N      1 
ATOM   2533 C CA     . GLY   A 1 180 ? 21.65846  -38.22410 1.39296   1.000 113.01595 ? 181 GLY   A CA     1 
ATOM   2534 C C      . GLY   A 1 180 ? 22.76268  -38.43534 0.38269   1.000 112.24572 ? 181 GLY   A C      1 
ATOM   2535 O O      . GLY   A 1 180 ? 23.69075  -37.62355 0.31716   1.000 104.06787 ? 181 GLY   A O      1 
ATOM   2536 H H      . GLY   A 1 180 ? 20.35132  -39.67104 1.64818   1.000 130.10501 ? 181 GLY   A H      1 
ATOM   2537 H HA2    . GLY   A 1 180 ? 21.43662  -37.27981 1.39653   1.000 136.00960 ? 181 GLY   A HA2    1 
ATOM   2538 H HA3    . GLY   A 1 180 ? 22.00364  -38.47070 2.26528   1.000 136.00960 ? 181 GLY   A HA3    1 
ATOM   2539 N N      . MET   A 1 181 ? 22.69137  -39.51152 -0.40164  1.000 127.07856 ? 182 MET   A N      1 
ATOM   2540 C CA     . MET   A 1 181 ? 23.65714  -39.77780 -1.45789  1.000 133.54250 ? 182 MET   A CA     1 
ATOM   2541 C C      . MET   A 1 181 ? 23.11590  -39.41636 -2.83817  1.000 121.65125 ? 182 MET   A C      1 
ATOM   2542 O O      . MET   A 1 181 ? 23.60587  -39.93730 -3.84601  1.000 116.06308 ? 182 MET   A O      1 
ATOM   2543 C CB     . MET   A 1 181 ? 24.08022  -41.24777 -1.42569  1.000 117.03249 ? 182 MET   A CB     1 
ATOM   2544 C CG     . MET   A 1 181 ? 24.71976  -41.68827 -0.11498  1.000 115.45229 ? 182 MET   A CG     1 
ATOM   2545 S SD     . MET   A 1 181 ? 26.27578  -40.85003 0.25343   1.000 227.93900 ? 182 MET   A SD     1 
ATOM   2546 C CE     . MET   A 1 181 ? 27.33137  -41.47784 -1.05200  1.000 164.87325 ? 182 MET   A CE     1 
ATOM   2547 H H      . MET   A 1 181 ? 22.07874  -40.11158 -0.33674  1.000 152.88474 ? 182 MET   A H      1 
ATOM   2548 H HA     . MET   A 1 181 ? 24.44700  -39.24083 -1.28856  1.000 160.64147 ? 182 MET   A HA     1 
ATOM   2549 H HB2    . MET   A 1 181 ? 23.29514  -41.79908 -1.56928  1.000 140.82946 ? 182 MET   A HB2    1 
ATOM   2550 H HB3    . MET   A 1 181 ? 24.72614  -41.39957 -2.13325  1.000 140.82946 ? 182 MET   A HB3    1 
ATOM   2551 H HG2    . MET   A 1 181 ? 24.10419  -41.50142 0.61100   1.000 138.93322 ? 182 MET   A HG2    1 
ATOM   2552 H HG3    . MET   A 1 181 ? 24.90028  -42.64025 -0.16018  1.000 138.93322 ? 182 MET   A HG3    1 
ATOM   2553 H HE1    . MET   A 1 181 ? 28.21726  -41.09531 -0.95321  1.000 198.23837 ? 182 MET   A HE1    1 
ATOM   2554 H HE2    . MET   A 1 181 ? 27.37871  -42.44419 -0.98257  1.000 198.23837 ? 182 MET   A HE2    1 
ATOM   2555 H HE3    . MET   A 1 181 ? 26.95608  -41.22586 -1.91023  1.000 198.23837 ? 182 MET   A HE3    1 
ATOM   2556 N N      . SER   A 1 182 ? 22.12181  -38.53294 -2.90114  1.000 115.43636 ? 183 SER   A N      1 
ATOM   2557 C CA     . SER   A 1 182 ? 21.53258  -38.15029 -4.17600  1.000 118.46793 ? 183 SER   A CA     1 
ATOM   2558 C C      . SER   A 1 182 ? 22.59924  -37.61986 -5.12656  1.000 125.54605 ? 183 SER   A C      1 
ATOM   2559 O O      . SER   A 1 182 ? 23.56932  -36.97785 -4.71508  1.000 138.08596 ? 183 SER   A O      1 
ATOM   2560 C CB     . SER   A 1 182 ? 20.45147  -37.09061 -3.96048  1.000 120.72982 ? 183 SER   A CB     1 
ATOM   2561 O OG     . SER   A 1 182 ? 19.89319  -36.66956 -5.19226  1.000 112.48777 ? 183 SER   A OG     1 
ATOM   2562 H H      . SER   A 1 182 ? 21.77210  -38.14199 -2.21963  1.000 138.91411 ? 183 SER   A H      1 
ATOM   2563 H HA     . SER   A 1 182 ? 21.12215  -38.92746 -4.58642  1.000 142.55199 ? 183 SER   A HA     1 
ATOM   2564 H HB2    . SER   A 1 182 ? 19.74792  -37.46715 -3.40900  1.000 145.26626 ? 183 SER   A HB2    1 
ATOM   2565 H HB3    . SER   A 1 182 ? 20.84680  -36.32420 -3.51637  1.000 145.26626 ? 183 SER   A HB3    1 
ATOM   2566 H HG     . SER   A 1 182 ? 19.35355  -36.03904 -5.06251  1.000 135.37579 ? 183 SER   A HG     1 
ATOM   2567 N N      . LYS   A 1 183 ? 22.41085  -37.90048 -6.41574  1.000 123.05168 ? 184 LYS   A N      1 
ATOM   2568 C CA     . LYS   A 1 183 ? 23.31844  -37.44454 -7.45718  1.000 118.17508 ? 184 LYS   A CA     1 
ATOM   2569 C C      . LYS   A 1 183 ? 22.69198  -36.40465 -8.37523  1.000 122.07819 ? 184 LYS   A C      1 
ATOM   2570 O O      . LYS   A 1 183 ? 23.33224  -35.99432 -9.34864  1.000 143.91748 ? 184 LYS   A O      1 
ATOM   2571 C CB     . LYS   A 1 183 ? 23.80251  -38.63570 -8.29280  1.000 116.25876 ? 184 LYS   A CB     1 
ATOM   2572 C CG     . LYS   A 1 183 ? 24.57590  -39.68292 -7.50564  1.000 115.10886 ? 184 LYS   A CG     1 
ATOM   2573 C CD     . LYS   A 1 183 ? 25.10361  -40.78260 -8.42040  1.000 112.54361 ? 184 LYS   A CD     1 
ATOM   2574 C CE     . LYS   A 1 183 ? 25.56602  -41.99823 -7.63380  1.000 110.82466 ? 184 LYS   A CE     1 
ATOM   2575 N NZ     . LYS   A 1 183 ? 25.30203  -43.26313 -8.37344  1.000 111.77586 ? 184 LYS   A NZ     1 
ATOM   2576 H H      . LYS   A 1 183 ? 21.75001  -38.36299 -6.71402  1.000 148.05248 ? 184 LYS   A H      1 
ATOM   2577 H HA     . LYS   A 1 183 ? 24.09232  -37.04042 -7.03445  1.000 142.20056 ? 184 LYS   A HA     1 
ATOM   2578 H HB2    . LYS   A 1 183 ? 23.03019  -39.07359 -8.68352  1.000 139.90099 ? 184 LYS   A HB2    1 
ATOM   2579 H HB3    . LYS   A 1 183 ? 24.38621  -38.30511 -8.99344  1.000 139.90099 ? 184 LYS   A HB3    1 
ATOM   2580 H HG2    . LYS   A 1 183 ? 25.33108  -39.26254 -7.06532  1.000 138.52110 ? 184 LYS   A HG2    1 
ATOM   2581 H HG3    . LYS   A 1 183 ? 23.99078  -40.08781 -6.84640  1.000 138.52110 ? 184 LYS   A HG3    1 
ATOM   2582 H HD2    . LYS   A 1 183 ? 24.39817  -41.06237 -9.02454  1.000 133.09998 ? 184 LYS   A HD2    1 
ATOM   2583 H HD3    . LYS   A 1 183 ? 25.85849  -40.44332 -8.92630  1.000 133.09998 ? 184 LYS   A HD3    1 
ATOM   2584 H HE2    . LYS   A 1 183 ? 26.52046  -41.93256 -7.47374  1.000 131.03724 ? 184 LYS   A HE2    1 
ATOM   2585 H HE3    . LYS   A 1 183 ? 25.08974  -42.03406 -6.78954  1.000 131.03724 ? 184 LYS   A HE3    1 
ATOM   2586 H HZ1    . LYS   A 1 183 ? 25.45997  -43.96263 -7.84632  1.000 132.17868 ? 184 LYS   A HZ1    1 
ATOM   2587 H HZ2    . LYS   A 1 183 ? 24.45333  -43.28831 -8.64022  1.000 132.17868 ? 184 LYS   A HZ2    1 
ATOM   2588 H HZ3    . LYS   A 1 183 ? 25.83088  -43.31429 -9.08745  1.000 132.17868 ? 184 LYS   A HZ3    1 
ATOM   2589 N N      . VAL   A 1 184 ? 21.46509  -35.96737 -8.09460  1.000 114.74127 ? 185 VAL   A N      1 
ATOM   2590 C CA     . VAL   A 1 184 ? 20.76454  -35.01837 -8.95201  1.000 115.12298 ? 185 VAL   A CA     1 
ATOM   2591 C C      . VAL   A 1 184 ? 20.57444  -33.70351 -8.20650  1.000 119.34027 ? 185 VAL   A C      1 
ATOM   2592 O O      . VAL   A 1 184 ? 19.48065  -33.12710 -8.20982  1.000 115.00775 ? 185 VAL   A O      1 
ATOM   2593 C CB     . VAL   A 1 184 ? 19.41206  -35.58949 -9.41938  1.000 115.13193 ? 185 VAL   A CB     1 
ATOM   2594 C CG1    . VAL   A 1 184 ? 19.63007  -36.78048 -10.33805 1.000 116.32704 ? 185 VAL   A CG1    1 
ATOM   2595 C CG2    . VAL   A 1 184 ? 18.55369  -35.99153 -8.22381  1.000 146.20386 ? 185 VAL   A CG2    1 
ATOM   2596 H H      . VAL   A 1 184 ? 21.01312  -36.20965 -7.40422  1.000 138.08000 ? 185 VAL   A H      1 
ATOM   2597 H HA     . VAL   A 1 184 ? 21.30894  -34.84245 -9.73532  1.000 136.19522 ? 185 VAL   A HA     1 
ATOM   2598 H HB     . VAL   A 1 184 ? 18.93825  -34.90230 -9.91351  1.000 136.20597 ? 185 VAL   A HB     1 
ATOM   2599 H HG11   . VAL   A 1 184 ? 18.76780  -37.14042 -10.59849 1.000 137.64010 ? 185 VAL   A HG11   1 
ATOM   2600 H HG12   . VAL   A 1 184 ? 20.11748  -36.48799 -11.12404 1.000 137.64010 ? 185 VAL   A HG12   1 
ATOM   2601 H HG13   . VAL   A 1 184 ? 20.14082  -37.45544 -9.86427  1.000 137.64010 ? 185 VAL   A HG13   1 
ATOM   2602 H HG21   . VAL   A 1 184 ? 17.67528  -36.25480 -8.54000  1.000 175.83511 ? 185 VAL   A HG21   1 
ATOM   2603 H HG22   . VAL   A 1 184 ? 18.97722  -36.73488 -7.76670  1.000 175.83511 ? 185 VAL   A HG22   1 
ATOM   2604 H HG23   . VAL   A 1 184 ? 18.47558  -35.23454 -7.62234  1.000 175.83511 ? 185 VAL   A HG23   1 
ATOM   2605 N N      . ARG   A 1 185 ? 21.63997  -33.21810 -7.56806  1.000 121.27036 ? 186 ARG   A N      1 
ATOM   2606 C CA     . ARG   A 1 185 ? 21.59681  -31.97673 -6.80806  1.000 130.17159 ? 186 ARG   A CA     1 
ATOM   2607 C C      . ARG   A 1 185 ? 22.23947  -30.80225 -7.53116  1.000 132.99582 ? 186 ARG   A C      1 
ATOM   2608 O O      . ARG   A 1 185 ? 22.08924  -29.66200 -7.07893  1.000 125.10235 ? 186 ARG   A O      1 
ATOM   2609 C CB     . ARG   A 1 185 ? 22.31103  -32.15180 -5.46304  1.000 137.82704 ? 186 ARG   A CB     1 
ATOM   2610 C CG     . ARG   A 1 185 ? 21.70686  -33.18989 -4.54375  1.000 140.40879 ? 186 ARG   A CG     1 
ATOM   2611 C CD     . ARG   A 1 185 ? 22.78380  -33.82854 -3.68902  1.000 127.49865 ? 186 ARG   A CD     1 
ATOM   2612 N NE     . ARG   A 1 185 ? 22.33737  -34.08268 -2.32604  1.000 116.38372 ? 186 ARG   A NE     1 
ATOM   2613 C CZ     . ARG   A 1 185 ? 22.89736  -34.96538 -1.51097  1.000 122.84773 ? 186 ARG   A CZ     1 
ATOM   2614 N NH1    . ARG   A 1 185 ? 23.89555  -35.73834 -1.90916  1.000 112.37472 ? 186 ARG   A NH1    1 
ATOM   2615 N NH2    . ARG   A 1 185 ? 22.44110  -35.07992 -0.26721  1.000 125.37387 ? 186 ARG   A NH2    1 
ATOM   2616 H H      . ARG   A 1 185 ? 22.41106  -33.59887 -7.56225  1.000 145.91490 ? 186 ARG   A H      1 
ATOM   2617 H HA     . ARG   A 1 185 ? 20.66549  -31.76236 -6.64194  1.000 156.59638 ? 186 ARG   A HA     1 
ATOM   2618 H HB2    . ARG   A 1 185 ? 23.22834  -32.41581 -5.63549  1.000 165.78292 ? 186 ARG   A HB2    1 
ATOM   2619 H HB3    . ARG   A 1 185 ? 22.29271  -31.30304 -4.99382  1.000 165.78292 ? 186 ARG   A HB3    1 
ATOM   2620 H HG2    . ARG   A 1 185 ? 21.05708  -32.76875 -3.95952  1.000 168.88102 ? 186 ARG   A HG2    1 
ATOM   2621 H HG3    . ARG   A 1 185 ? 21.27900  -33.88241 -5.07124  1.000 168.88102 ? 186 ARG   A HG3    1 
ATOM   2622 H HD2    . ARG   A 1 185 ? 23.04107  -34.67625 -4.08412  1.000 153.38885 ? 186 ARG   A HD2    1 
ATOM   2623 H HD3    . ARG   A 1 185 ? 23.55008  -33.23516 -3.64869  1.000 153.38885 ? 186 ARG   A HD3    1 
ATOM   2624 H HE     . ARG   A 1 185 ? 21.66750  -33.63108 -2.03120  1.000 140.05093 ? 186 ARG   A HE     1 
ATOM   2625 H HH11   . ARG   A 1 185 ? 24.19487  -35.67421 -2.71284  1.000 135.24014 ? 186 ARG   A HH11   1 
ATOM   2626 H HH12   . ARG   A 1 185 ? 24.24471  -36.30461 -1.36417  1.000 135.24014 ? 186 ARG   A HH12   1 
ATOM   2627 H HH21   . ARG   A 1 185 ? 21.79049  -34.58474 -0.00055  1.000 150.83912 ? 186 ARG   A HH21   1 
ATOM   2628 H HH22   . ARG   A 1 185 ? 22.79662  -35.64918 0.27052   1.000 150.83912 ? 186 ARG   A HH22   1 
ATOM   2629 N N      . LYS   A 1 186 ? 22.94898  -31.05161 -8.63362  1.000 134.18651 ? 187 LYS   A N      1 
ATOM   2630 C CA     . LYS   A 1 186 ? 23.82871  -30.03264 -9.19761  1.000 136.23359 ? 187 LYS   A CA     1 
ATOM   2631 C C      . LYS   A 1 186 ? 23.07932  -28.74493 -9.51904  1.000 136.87883 ? 187 LYS   A C      1 
ATOM   2632 O O      . LYS   A 1 186 ? 23.60815  -27.64683 -9.31215  1.000 139.65503 ? 187 LYS   A O      1 
ATOM   2633 C CB     . LYS   A 1 186 ? 24.51809  -30.57638 -10.44846 1.000 141.99204 ? 187 LYS   A CB     1 
ATOM   2634 C CG     . LYS   A 1 186 ? 25.55602  -31.65754 -10.16862 1.000 153.82715 ? 187 LYS   A CG     1 
ATOM   2635 C CD     . LYS   A 1 186 ? 26.70259  -31.13431 -9.31190  1.000 157.84478 ? 187 LYS   A CD     1 
ATOM   2636 C CE     . LYS   A 1 186 ? 27.69432  -32.23414 -8.97212  1.000 157.46112 ? 187 LYS   A CE     1 
ATOM   2637 N NZ     . LYS   A 1 186 ? 28.66762  -31.79173 -7.93557  1.000 159.84530 ? 187 LYS   A NZ     1 
ATOM   2638 H H      . LYS   A 1 186 ? 22.93826  -31.79379 -9.06796  1.000 161.41429 ? 187 LYS   A H      1 
ATOM   2639 H HA     . LYS   A 1 186 ? 24.50832  -29.81771 -8.53971  1.000 163.87077 ? 187 LYS   A HA     1 
ATOM   2640 H HB2    . LYS   A 1 186 ? 23.84461  -30.95885 -11.03244 1.000 170.78092 ? 187 LYS   A HB2    1 
ATOM   2641 H HB3    . LYS   A 1 186 ? 24.96920  -29.84422 -10.89717 1.000 170.78092 ? 187 LYS   A HB3    1 
ATOM   2642 H HG2    . LYS   A 1 186 ? 25.13396  -32.39150 -9.69526  1.000 184.98305 ? 187 LYS   A HG2    1 
ATOM   2643 H HG3    . LYS   A 1 186 ? 25.92433  -31.97274 -11.00880 1.000 184.98305 ? 187 LYS   A HG3    1 
ATOM   2644 H HD2    . LYS   A 1 186 ? 27.17379  -30.43865 -9.79659  1.000 189.80420 ? 187 LYS   A HD2    1 
ATOM   2645 H HD3    . LYS   A 1 186 ? 26.34699  -30.77825 -8.48264  1.000 189.80420 ? 187 LYS   A HD3    1 
ATOM   2646 H HE2    . LYS   A 1 186 ? 27.21438  -33.00476 -8.63051  1.000 189.34381 ? 187 LYS   A HE2    1 
ATOM   2647 H HE3    . LYS   A 1 186 ? 28.18875  -32.47824 -9.77015  1.000 189.34381 ? 187 LYS   A HE3    1 
ATOM   2648 H HZ1    . LYS   A 1 186 ? 29.14105  -32.48746 -7.64587  1.000 192.20483 ? 187 LYS   A HZ1    1 
ATOM   2649 H HZ2    . LYS   A 1 186 ? 29.22328  -31.18681 -8.27821  1.000 192.20483 ? 187 LYS   A HZ2    1 
ATOM   2650 H HZ3    . LYS   A 1 186 ? 28.23540  -31.42963 -7.24697  1.000 192.20483 ? 187 LYS   A HZ3    1 
ATOM   2651 N N      . PHE   A 1 187 ? 21.85101  -28.85121 -10.02754 1.000 133.95130 ? 188 PHE   A N      1 
ATOM   2652 C CA     . PHE   A 1 187 ? 21.11828  -27.64913 -10.40895 1.000 131.43236 ? 188 PHE   A CA     1 
ATOM   2653 C C      . PHE   A 1 187 ? 20.74580  -26.78536 -9.21147  1.000 147.45102 ? 188 PHE   A C      1 
ATOM   2654 O O      . PHE   A 1 187 ? 20.44453  -25.60035 -9.39269  1.000 136.94745 ? 188 PHE   A O      1 
ATOM   2655 C CB     . PHE   A 1 187 ? 19.86266  -28.02369 -11.19550 1.000 137.08864 ? 188 PHE   A CB     1 
ATOM   2656 C CG     . PHE   A 1 187 ? 20.13739  -28.36503 -12.62846 1.000 149.81258 ? 188 PHE   A CG     1 
ATOM   2657 C CD1    . PHE   A 1 187 ? 20.49547  -27.37491 -13.52719 1.000 146.70486 ? 188 PHE   A CD1    1 
ATOM   2658 C CD2    . PHE   A 1 187 ? 20.04940  -29.67110 -13.07702 1.000 159.87865 ? 188 PHE   A CD2    1 
ATOM   2659 C CE1    . PHE   A 1 187 ? 20.75737  -27.67856 -14.84532 1.000 150.70145 ? 188 PHE   A CE1    1 
ATOM   2660 C CE2    . PHE   A 1 187 ? 20.31001  -29.98102 -14.39726 1.000 162.23962 ? 188 PHE   A CE2    1 
ATOM   2661 C CZ     . PHE   A 1 187 ? 20.66530  -28.98293 -15.28178 1.000 158.53843 ? 188 PHE   A CZ     1 
ATOM   2662 H H      . PHE   A 1 187 ? 21.43121  -29.59038 -10.15796 1.000 161.13203 ? 188 PHE   A H      1 
ATOM   2663 H HA     . PHE   A 1 187 ? 21.68479  -27.11660 -10.98892 1.000 158.10931 ? 188 PHE   A HA     1 
ATOM   2664 H HB2    . PHE   A 1 187 ? 19.45128  -28.79714 -10.77902 1.000 164.89683 ? 188 PHE   A HB2    1 
ATOM   2665 H HB3    . PHE   A 1 187 ? 19.24842  -27.27309 -11.18095 1.000 164.89683 ? 188 PHE   A HB3    1 
ATOM   2666 H HD1    . PHE   A 1 187 ? 20.56007  -26.49353 -13.23754 1.000 176.43630 ? 188 PHE   A HD1    1 
ATOM   2667 H HD2    . PHE   A 1 187 ? 19.81243  -30.34678 -12.48356 1.000 192.24485 ? 188 PHE   A HD2    1 
ATOM   2668 H HE1    . PHE   A 1 187 ? 20.99597  -27.00440 -15.43987 1.000 181.23221 ? 188 PHE   A HE1    1 
ATOM   2669 H HE2    . PHE   A 1 187 ? 20.24618  -30.86141 -14.69005 1.000 195.07801 ? 188 PHE   A HE2    1 
ATOM   2670 H HZ     . PHE   A 1 187 ? 20.84234  -29.19005 -16.17097 1.000 190.63659 ? 188 PHE   A HZ     1 
ATOM   2671 N N      . VAL   A 1 188 ? 20.76445  -27.33947 -8.00390  1.000 158.87314 ? 189 VAL   A N      1 
ATOM   2672 C CA     . VAL   A 1 188 ? 20.47830  -26.58315 -6.78868  1.000 139.97598 ? 189 VAL   A CA     1 
ATOM   2673 C C      . VAL   A 1 188 ? 21.75745  -26.15904 -6.08108  1.000 142.17213 ? 189 VAL   A C      1 
ATOM   2674 O O      . VAL   A 1 188 ? 21.88578  -25.01363 -5.64909  1.000 149.07241 ? 189 VAL   A O      1 
ATOM   2675 C CB     . VAL   A 1 188 ? 19.57084  -27.40507 -5.84693  1.000 140.04987 ? 189 VAL   A CB     1 
ATOM   2676 C CG1    . VAL   A 1 188 ? 19.53685  -26.77365 -4.46513  1.000 151.76806 ? 189 VAL   A CG1    1 
ATOM   2677 C CG2    . VAL   A 1 188 ? 18.17064  -27.50920 -6.42170  1.000 142.86783 ? 189 VAL   A CG2    1 
ATOM   2678 H H      . VAL   A 1 188 ? 20.94361  -28.16810 -7.85946  1.000 191.03824 ? 189 VAL   A H      1 
ATOM   2679 H HA     . VAL   A 1 188 ? 19.99851  -25.77822 -7.03925  1.000 168.36165 ? 189 VAL   A HA     1 
ATOM   2680 H HB     . VAL   A 1 188 ? 19.93036  -28.30199 -5.76220  1.000 168.45031 ? 189 VAL   A HB     1 
ATOM   2681 H HG11   . VAL   A 1 188 ? 18.76298  -27.10695 -3.98457  1.000 182.51214 ? 189 VAL   A HG11   1 
ATOM   2682 H HG12   . VAL   A 1 188 ? 20.34858  -27.01028 -3.98973  1.000 182.51214 ? 189 VAL   A HG12   1 
ATOM   2683 H HG13   . VAL   A 1 188 ? 19.47780  -25.81007 -4.55959  1.000 182.51214 ? 189 VAL   A HG13   1 
ATOM   2684 H HG21   . VAL   A 1 188 ? 17.62759  -28.05660 -5.83318  1.000 171.83186 ? 189 VAL   A HG21   1 
ATOM   2685 H HG22   . VAL   A 1 188 ? 17.79041  -26.61946 -6.49018  1.000 171.83186 ? 189 VAL   A HG22   1 
ATOM   2686 H HG23   . VAL   A 1 188 ? 18.21956  -27.91656 -7.30065  1.000 171.83186 ? 189 VAL   A HG23   1 
ATOM   2687 N N      . THR   A 1 189 ? 22.71365  -27.07499 -5.94400  1.000 139.31687 ? 190 THR   A N      1 
ATOM   2688 C CA     . THR   A 1 189 ? 23.95318  -26.77653 -5.24516  1.000 142.70749 ? 190 THR   A CA     1 
ATOM   2689 C C      . THR   A 1 189 ? 25.06130  -27.67792 -5.76392  1.000 144.50196 ? 190 THR   A C      1 
ATOM   2690 O O      . THR   A 1 189 ? 24.81564  -28.81055 -6.18757  1.000 148.45958 ? 190 THR   A O      1 
ATOM   2691 C CB     . THR   A 1 189 ? 23.81286  -26.96499 -3.72894  1.000 144.78603 ? 190 THR   A CB     1 
ATOM   2692 O OG1    . THR   A 1 189 ? 25.06227  -26.67422 -3.08967  1.000 150.55030 ? 190 THR   A OG1    1 
ATOM   2693 C CG2    . THR   A 1 189 ? 23.40629  -28.39585 -3.40109  1.000 144.48506 ? 190 THR   A CG2    1 
ATOM   2694 H H      . THR   A 1 189 ? 22.66508  -27.87769 -6.24883  1.000 167.57072 ? 190 THR   A H      1 
ATOM   2695 H HA     . THR   A 1 189 ? 24.19558  -25.85478 -5.42552  1.000 171.63946 ? 190 THR   A HA     1 
ATOM   2696 H HB     . THR   A 1 189 ? 23.12785  -26.36572 -3.39349  1.000 174.13370 ? 190 THR   A HB     1 
ATOM   2697 H HG1    . THR   A 1 189 ? 24.99801  -26.80183 -2.26191  1.000 181.05083 ? 190 THR   A HG1    1 
ATOM   2698 H HG21   . THR   A 1 189 ? 23.20333  -28.47478 -2.45585  1.000 173.77254 ? 190 THR   A HG21   1 
ATOM   2699 H HG22   . THR   A 1 189 ? 22.62067  -28.64319 -3.91346  1.000 173.77254 ? 190 THR   A HG22   1 
ATOM   2700 H HG23   . THR   A 1 189 ? 24.12920  -29.00453 -3.61974  1.000 173.77254 ? 190 THR   A HG23   1 
ATOM   2701 N N      . ASP   A 1 190 ? 26.28527  -27.15981 -5.72181  1.000 148.40640 ? 191 ASP   A N      1 
ATOM   2702 C CA     . ASP   A 1 190 ? 27.47600  -27.94148 -6.01893  1.000 154.49784 ? 191 ASP   A CA     1 
ATOM   2703 C C      . ASP   A 1 190 ? 28.03146  -28.64613 -4.79004  1.000 157.99223 ? 191 ASP   A C      1 
ATOM   2704 O O      . ASP   A 1 190 ? 29.06277  -29.31926 -4.89172  1.000 154.45988 ? 191 ASP   A O      1 
ATOM   2705 C CB     . ASP   A 1 190 ? 28.55903  -27.04319 -6.62150  1.000 142.14121 ? 191 ASP   A CB     1 
ATOM   2706 C CG     . ASP   A 1 190 ? 28.18342  -26.51997 -7.99041  1.000 165.42752 ? 191 ASP   A CG     1 
ATOM   2707 O OD1    . ASP   A 1 190 ? 27.39886  -27.19524 -8.68949  1.000 168.80335 ? 191 ASP   A OD1    1 
ATOM   2708 O OD2    . ASP   A 1 190 ? 28.67378  -25.43581 -8.36871  1.000 176.25718 ? 191 ASP   A OD2    1 
ATOM   2709 H H      . ASP   A 1 190 ? 26.45292  -26.34096 -5.51937  1.000 178.47815 ? 191 ASP   A H      1 
ATOM   2710 H HA     . ASP   A 1 190 ? 27.24883  -28.61605 -6.67791  1.000 185.78788 ? 191 ASP   A HA     1 
ATOM   2711 H HB2    . ASP   A 1 190 ? 28.70082  -26.28212 -6.03707  1.000 170.95992 ? 191 ASP   A HB2    1 
ATOM   2712 H HB3    . ASP   A 1 190 ? 29.38027  -27.55195 -6.70885  1.000 170.95992 ? 191 ASP   A HB3    1 
ATOM   2713 N N      . THR   A 1 191 ? 27.37675  -28.50499 -3.63973  1.000 148.67870 ? 192 THR   A N      1 
ATOM   2714 C CA     . THR   A 1 191 ? 27.88201  -29.09913 -2.41108  1.000 141.24986 ? 192 THR   A CA     1 
ATOM   2715 C C      . THR   A 1 191 ? 28.03962  -30.60574 -2.57224  1.000 141.60126 ? 192 THR   A C      1 
ATOM   2716 O O      . THR   A 1 191 ? 27.22474  -31.27007 -3.21918  1.000 141.56025 ? 192 THR   A O      1 
ATOM   2717 C CB     . THR   A 1 191 ? 26.93997  -28.78243 -1.24822  1.000 126.40423 ? 192 THR   A CB     1 
ATOM   2718 O OG1    . THR   A 1 191 ? 26.87391  -27.36308 -1.05730  1.000 123.66663 ? 192 THR   A OG1    1 
ATOM   2719 C CG2    . THR   A 1 191 ? 27.42715  -29.44001 0.03162   1.000 128.17587 ? 192 THR   A CG2    1 
ATOM   2720 H H      . THR   A 1 191 ? 26.64022  -28.07097 -3.54614  1.000 178.80491 ? 192 THR   A H      1 
ATOM   2721 H HA     . THR   A 1 191 ? 28.75291  -28.72554 -2.20401  1.000 169.89030 ? 192 THR   A HA     1 
ATOM   2722 H HB     . THR   A 1 191 ? 26.05469  -29.12473 -1.44825  1.000 152.07555 ? 192 THR   A HB     1 
ATOM   2723 H HG1    . THR   A 1 191 ? 26.40045  -27.18514 -0.38665  1.000 148.79042 ? 192 THR   A HG1    1 
ATOM   2724 H HG21   . THR   A 1 191 ? 26.98881  -29.03891 0.79835   1.000 154.20151 ? 192 THR   A HG21   1 
ATOM   2725 H HG22   . THR   A 1 191 ? 27.22584  -30.38874 0.01458   1.000 154.20151 ? 192 THR   A HG22   1 
ATOM   2726 H HG23   . THR   A 1 191 ? 28.38599  -29.32321 0.12043   1.000 154.20151 ? 192 THR   A HG23   1 
ATOM   2727 N N      . GLU   A 1 192 ? 29.10574  -31.13936 -1.98422  1.000 130.69366 ? 193 GLU   A N      1 
ATOM   2728 C CA     . GLU   A 1 192 ? 29.42913  -32.55392 -2.05889  1.000 136.66641 ? 193 GLU   A CA     1 
ATOM   2729 C C      . GLU   A 1 192 ? 29.27200  -33.20366 -0.69058  1.000 134.18845 ? 193 GLU   A C      1 
ATOM   2730 O O      . GLU   A 1 192 ? 29.52168  -32.58096 0.34559   1.000 139.23840 ? 193 GLU   A O      1 
ATOM   2731 C CB     . GLU   A 1 192 ? 30.86235  -32.76492 -2.55745  1.000 159.07642 ? 193 GLU   A CB     1 
ATOM   2732 C CG     . GLU   A 1 192 ? 31.14378  -32.18958 -3.93631  1.000 181.68100 ? 193 GLU   A CG     1 
ATOM   2733 C CD     . GLU   A 1 192 ? 30.66177  -33.08852 -5.05716  1.000 180.09378 ? 193 GLU   A CD     1 
ATOM   2734 O OE1    . GLU   A 1 192 ? 30.49768  -34.30450 -4.82123  1.000 160.89155 ? 193 GLU   A OE1    1 
ATOM   2735 O OE2    . GLU   A 1 192 ? 30.44777  -32.57800 -6.17639  1.000 184.82022 ? 193 GLU   A OE2    1 
ATOM   2736 H H      . GLU   A 1 192 ? 29.67209  -30.68546 -1.52290  1.000 157.22286 ? 193 GLU   A H      1 
ATOM   2737 H HA     . GLU   A 1 192 ? 28.81993  -32.98763 -2.67667  1.000 164.39016 ? 193 GLU   A HA     1 
ATOM   2738 H HB2    . GLU   A 1 192 ? 31.47174  -32.34052 -1.93340  1.000 191.28218 ? 193 GLU   A HB2    1 
ATOM   2739 H HB3    . GLU   A 1 192 ? 31.03821  -33.71804 -2.59667  1.000 191.28218 ? 193 GLU   A HB3    1 
ATOM   2740 H HG2    . GLU   A 1 192 ? 30.69098  -31.33592 -4.02091  1.000 218.40767 ? 193 GLU   A HG2    1 
ATOM   2741 H HG3    . GLU   A 1 192 ? 32.10076  -32.06914 -4.03911  1.000 218.40767 ? 193 GLU   A HG3    1 
ATOM   2742 N N      . VAL   A 1 193 ? 28.85016  -34.46876 -0.70039  1.000 127.22336 ? 194 VAL   A N      1 
ATOM   2743 C CA     . VAL   A 1 193 ? 28.82154  -35.25921 0.52192   1.000 118.71940 ? 194 VAL   A CA     1 
ATOM   2744 C C      . VAL   A 1 193 ? 30.24659  -35.48990 1.01276   1.000 122.67595 ? 194 VAL   A C      1 
ATOM   2745 O O      . VAL   A 1 193 ? 31.18942  -35.63176 0.22196   1.000 116.78129 ? 194 VAL   A O      1 
ATOM   2746 C CB     . VAL   A 1 193 ? 28.09434  -36.59508 0.28252   1.000 109.72090 ? 194 VAL   A CB     1 
ATOM   2747 C CG1    . VAL   A 1 193 ? 28.33771  -37.55154 1.43650   1.000 116.54192 ? 194 VAL   A CG1    1 
ATOM   2748 C CG2    . VAL   A 1 193 ? 26.60419  -36.36097 0.08825   1.000 111.50652 ? 194 VAL   A CG2    1 
ATOM   2749 H H      . VAL   A 1 193 ? 28.57718  -34.88808 -1.39985  1.000 153.05850 ? 194 VAL   A H      1 
ATOM   2750 H HA     . VAL   A 1 193 ? 28.33710  -34.77076 1.20575   1.000 142.85375 ? 194 VAL   A HA     1 
ATOM   2751 H HB     . VAL   A 1 193 ? 28.44634  -37.00192 -0.52462  1.000 132.05555 ? 194 VAL   A HB     1 
ATOM   2752 H HG11   . VAL   A 1 193 ? 27.69559  -38.27685 1.38630   1.000 140.24078 ? 194 VAL   A HG11   1 
ATOM   2753 H HG12   . VAL   A 1 193 ? 29.23943  -37.90291 1.37065   1.000 140.24078 ? 194 VAL   A HG12   1 
ATOM   2754 H HG13   . VAL   A 1 193 ? 28.22994  -37.07163 2.27254   1.000 140.24078 ? 194 VAL   A HG13   1 
ATOM   2755 H HG21   . VAL   A 1 193 ? 26.16660  -37.21452 -0.05617  1.000 134.19829 ? 194 VAL   A HG21   1 
ATOM   2756 H HG22   . VAL   A 1 193 ? 26.24518  -35.93540 0.88255   1.000 134.19829 ? 194 VAL   A HG22   1 
ATOM   2757 H HG23   . VAL   A 1 193 ? 26.47252  -35.78713 -0.68265  1.000 134.19829 ? 194 VAL   A HG23   1 
ATOM   2758 N N      . GLU   A 1 194 ? 30.40768  -35.52783 2.33417   1.000 126.56958 ? 195 GLU   A N      1 
ATOM   2759 C CA     . GLU   A 1 194 ? 31.70485  -35.75717 2.95175   1.000 126.90531 ? 195 GLU   A CA     1 
ATOM   2760 C C      . GLU   A 1 194 ? 31.53414  -36.69345 4.13978   1.000 110.84480 ? 195 GLU   A C      1 
ATOM   2761 O O      . GLU   A 1 194 ? 30.48702  -36.70830 4.79184   1.000 110.27097 ? 195 GLU   A O      1 
ATOM   2762 C CB     . GLU   A 1 194 ? 32.35749  -34.44795 3.42192   1.000 131.92818 ? 195 GLU   A CB     1 
ATOM   2763 C CG     . GLU   A 1 194 ? 32.02015  -33.21946 2.57984   1.000 155.07414 ? 195 GLU   A CG     1 
ATOM   2764 C CD     . GLU   A 1 194 ? 32.62035  -33.26637 1.18071   1.000 172.56531 ? 195 GLU   A CD     1 
ATOM   2765 O OE1    . GLU   A 1 194 ? 33.31466  -34.25375 0.85724   1.000 152.82519 ? 195 GLU   A OE1    1 
ATOM   2766 O OE2    . GLU   A 1 194 ? 32.39838  -32.31261 0.40215   1.000 162.84065 ? 195 GLU   A OE2    1 
ATOM   2767 H H      . GLU   A 1 194 ? 29.76887  -35.42149 2.90005   1.000 152.27397 ? 195 GLU   A H      1 
ATOM   2768 H HA     . GLU   A 1 194 ? 32.29537  -36.17614 2.30627   1.000 152.67684 ? 195 GLU   A HA     1 
ATOM   2769 H HB2    . GLU   A 1 194 ? 32.06516  -34.26782 4.32911   1.000 158.70428 ? 195 GLU   A HB2    1 
ATOM   2770 H HB3    . GLU   A 1 194 ? 33.32075  -34.56001 3.39984   1.000 158.70428 ? 195 GLU   A HB3    1 
ATOM   2771 H HG2    . GLU   A 1 194 ? 31.05653  -33.15602 2.48860   1.000 186.47944 ? 195 GLU   A HG2    1 
ATOM   2772 H HG3    . GLU   A 1 194 ? 32.36397  -32.42925 3.02510   1.000 186.47944 ? 195 GLU   A HG3    1 
ATOM   2773 N N      . GLU   A 1 195 ? 32.57810  -37.46879 4.41996   1.000 111.29159 ? 196 GLU   A N      1 
ATOM   2774 C CA     . GLU   A 1 195 ? 32.57184  -38.40623 5.53439   1.000 112.86020 ? 196 GLU   A CA     1 
ATOM   2775 C C      . GLU   A 1 195 ? 32.99777  -37.69664 6.81357   1.000 121.03509 ? 196 GLU   A C      1 
ATOM   2776 O O      . GLU   A 1 195 ? 33.88822  -36.84221 6.79536   1.000 125.99935 ? 196 GLU   A O      1 
ATOM   2777 C CB     . GLU   A 1 195 ? 33.50353  -39.58550 5.24845   1.000 121.10253 ? 196 GLU   A CB     1 
ATOM   2778 C CG     . GLU   A 1 195 ? 33.10266  -40.41176 4.03284   1.000 125.96011 ? 196 GLU   A CG     1 
ATOM   2779 C CD     . GLU   A 1 195 ? 34.04623  -41.57172 3.77156   1.000 154.74147 ? 196 GLU   A CD     1 
ATOM   2780 O OE1    . GLU   A 1 195 ? 34.83621  -41.91527 4.67592   1.000 166.74725 ? 196 GLU   A OE1    1 
ATOM   2781 O OE2    . GLU   A 1 195 ? 33.99905  -42.13828 2.65883   1.000 177.38452 ? 196 GLU   A OE2    1 
ATOM   2782 H H      . GLU   A 1 195 ? 33.31194  -37.46907 3.97154   1.000 131.59756 ? 196 GLU   A H      1 
ATOM   2783 H HA     . GLU   A 1 195 ? 31.67621  -38.75569 5.66336   1.000 135.82271 ? 196 GLU   A HA     1 
ATOM   2784 H HB2    . GLU   A 1 195 ? 34.39776  -39.24410 5.09129   1.000 145.71350 ? 196 GLU   A HB2    1 
ATOM   2785 H HB3    . GLU   A 1 195 ? 33.50410  -40.17502 6.01875   1.000 145.71350 ? 196 GLU   A HB3    1 
ATOM   2786 H HG2    . GLU   A 1 195 ? 32.21459  -40.77452 4.17652   1.000 151.54261 ? 196 GLU   A HG2    1 
ATOM   2787 H HG3    . GLU   A 1 195 ? 33.10503  -39.84113 3.24844   1.000 151.54261 ? 196 GLU   A HG3    1 
ATOM   2788 N N      . THR   A 1 196 ? 32.35831  -38.06064 7.92777   1.000 133.66624 ? 197 THR   A N      1 
ATOM   2789 C CA     . THR   A 1 196 ? 32.59043  -37.39138 9.20206   1.000 124.85620 ? 197 THR   A CA     1 
ATOM   2790 C C      . THR   A 1 196 ? 33.62841  -38.08406 10.07630  1.000 118.00987 ? 197 THR   A C      1 
ATOM   2791 O O      . THR   A 1 196 ? 34.01108  -37.52518 11.10972  1.000 123.60246 ? 197 THR   A O      1 
ATOM   2792 C CB     . THR   A 1 196 ? 31.28304  -37.28013 9.99378   1.000 122.87860 ? 197 THR   A CB     1 
ATOM   2793 O OG1    . THR   A 1 196 ? 30.75563  -38.59066 10.23456  1.000 138.23020 ? 197 THR   A OG1    1 
ATOM   2794 C CG2    . THR   A 1 196 ? 30.26171  -36.44519 9.23298   1.000 127.53928 ? 197 THR   A CG2    1 
ATOM   2795 H H      . THR   A 1 196 ? 31.78170  -38.69743 7.96804   1.000 160.78996 ? 197 THR   A H      1 
ATOM   2796 H HA     . THR   A 1 196 ? 32.91030  -36.49594 9.01027   1.000 150.21792 ? 197 THR   A HA     1 
ATOM   2797 H HB     . THR   A 1 196 ? 31.45388  -36.84278 10.84257  1.000 147.84479 ? 197 THR   A HB     1 
ATOM   2798 H HG1    . THR   A 1 196 ? 31.25676  -39.00942 10.76286  1.000 166.26671 ? 197 THR   A HG1    1 
ATOM   2799 H HG21   . THR   A 1 196 ? 29.45864  -36.33667 9.76609   1.000 153.43760 ? 197 THR   A HG21   1 
ATOM   2800 H HG22   . THR   A 1 196 ? 30.62957  -35.56951 9.03609   1.000 153.43760 ? 197 THR   A HG22   1 
ATOM   2801 H HG23   . THR   A 1 196 ? 30.02940  -36.88370 8.39953   1.000 153.43760 ? 197 THR   A HG23   1 
ATOM   2802 N N      . GLY   A 1 197 ? 34.07904  -39.28134 9.70708   1.000 120.75737 ? 198 GLY   A N      1 
ATOM   2803 C CA     . GLY   A 1 197 ? 35.15637  -39.94826 10.41094  1.000 121.95853 ? 198 GLY   A CA     1 
ATOM   2804 C C      . GLY   A 1 197 ? 34.74944  -41.14970 11.23334  1.000 121.13620 ? 198 GLY   A C      1 
ATOM   2805 O O      . GLY   A 1 197 ? 35.62150  -41.77883 11.84451  1.000 133.15124 ? 198 GLY   A O      1 
ATOM   2806 H H      . GLY   A 1 197 ? 33.76850  -39.72908 9.04172   1.000 145.29932 ? 198 GLY   A H      1 
ATOM   2807 H HA2    . GLY   A 1 197 ? 35.81145  -40.24636 9.76063   1.000 146.74071 ? 198 GLY   A HA2    1 
ATOM   2808 H HA3    . GLY   A 1 197 ? 35.57422  -39.31045 11.01052  1.000 146.74071 ? 198 GLY   A HA3    1 
ATOM   2809 N N      . THR   A 1 198 ? 33.46610  -41.48979 11.28000  1.000 137.66846 ? 199 THR   A N      1 
ATOM   2810 C CA     . THR   A 1 198 ? 32.99129  -42.66177 11.99697  1.000 131.55919 ? 199 THR   A CA     1 
ATOM   2811 C C      . THR   A 1 198 ? 32.29174  -43.60530 11.02762  1.000 122.17578 ? 199 THR   A C      1 
ATOM   2812 O O      . THR   A 1 198 ? 31.87051  -43.21063 9.93675   1.000 115.61348 ? 199 THR   A O      1 
ATOM   2813 C CB     . THR   A 1 198 ? 32.03577  -42.27370 13.12968  1.000 110.29277 ? 199 THR   A CB     1 
ATOM   2814 O OG1    . THR   A 1 198 ? 30.89092  -41.60651 12.58563  1.000 111.54909 ? 199 THR   A OG1    1 
ATOM   2815 C CG2    . THR   A 1 198 ? 32.73306  -41.35504 14.11533  1.000 115.91926 ? 199 THR   A CG2    1 
ATOM   2816 H H      . THR   A 1 198 ? 32.83888  -41.04537 10.89439  1.000 165.59262 ? 199 THR   A H      1 
ATOM   2817 H HA     . THR   A 1 198 ? 33.74569  -43.12924 12.38847  1.000 158.26150 ? 199 THR   A HA     1 
ATOM   2818 H HB     . THR   A 1 198 ? 31.74883  -43.07115 13.60153  1.000 132.74180 ? 199 THR   A HB     1 
ATOM   2819 H HG1    . THR   A 1 198 ? 31.12700  -40.89764 12.20174  1.000 134.24938 ? 199 THR   A HG1    1 
ATOM   2820 H HG21   . THR   A 1 198 ? 32.12439  -41.11263 14.83064  1.000 139.49358 ? 199 THR   A HG21   1 
ATOM   2821 H HG22   . THR   A 1 198 ? 33.50483  -41.80208 14.49666  1.000 139.49358 ? 199 THR   A HG22   1 
ATOM   2822 H HG23   . THR   A 1 198 ? 33.02739  -40.54772 13.66531  1.000 139.49358 ? 199 THR   A HG23   1 
ATOM   2823 N N      . PHE   A 1 199 ? 32.17075  -44.86362 11.44224  1.000 127.29278 ? 200 PHE   A N      1 
ATOM   2824 C CA     . PHE   A 1 199 ? 31.58760  -45.91124 10.61774  1.000 122.00592 ? 200 PHE   A CA     1 
ATOM   2825 C C      . PHE   A 1 199 ? 30.57102  -46.68940 11.43688  1.000 119.47183 ? 200 PHE   A C      1 
ATOM   2826 O O      . PHE   A 1 199 ? 30.76116  -46.89588 12.63759  1.000 124.48614 ? 200 PHE   A O      1 
ATOM   2827 C CB     . PHE   A 1 199 ? 32.66788  -46.85581 10.08564  1.000 127.97312 ? 200 PHE   A CB     1 
ATOM   2828 C CG     . PHE   A 1 199 ? 32.20291  -47.73044 8.96286   1.000 127.98832 ? 200 PHE   A CG     1 
ATOM   2829 C CD1    . PHE   A 1 199 ? 32.26331  -47.28489 7.65417   1.000 114.32784 ? 200 PHE   A CD1    1 
ATOM   2830 C CD2    . PHE   A 1 199 ? 31.70390  -48.99642 9.21424   1.000 123.60318 ? 200 PHE   A CD2    1 
ATOM   2831 C CE1    . PHE   A 1 199 ? 31.83574  -48.08384 6.61901   1.000 121.89513 ? 200 PHE   A CE1    1 
ATOM   2832 C CE2    . PHE   A 1 199 ? 31.27513  -49.80100 8.18132   1.000 115.51630 ? 200 PHE   A CE2    1 
ATOM   2833 C CZ     . PHE   A 1 199 ? 31.34121  -49.34411 6.88154   1.000 121.49970 ? 200 PHE   A CZ     1 
ATOM   2834 H H      . PHE   A 1 199 ? 32.42604  -45.13877 12.21601  1.000 153.14181 ? 200 PHE   A H      1 
ATOM   2835 H HA     . PHE   A 1 199 ? 31.12750  -45.51767 9.85991   1.000 146.79758 ? 200 PHE   A HA     1 
ATOM   2836 H HB2    . PHE   A 1 199 ? 33.41251  -46.32635 9.75991   1.000 153.95821 ? 200 PHE   A HB2    1 
ATOM   2837 H HB3    . PHE   A 1 199 ? 32.96176  -47.43241 10.80818  1.000 153.95821 ? 200 PHE   A HB3    1 
ATOM   2838 H HD1    . PHE   A 1 199 ? 32.59663  -46.43592 7.47237   1.000 137.58388 ? 200 PHE   A HD1    1 
ATOM   2839 H HD2    . PHE   A 1 199 ? 31.65747  -49.30735 10.08950  1.000 148.71429 ? 200 PHE   A HD2    1 
ATOM   2840 H HE1    . PHE   A 1 199 ? 31.88016  -47.77436 5.74314   1.000 146.66463 ? 200 PHE   A HE1    1 
ATOM   2841 H HE2    . PHE   A 1 199 ? 30.94176  -50.65059 8.36010   1.000 139.01003 ? 200 PHE   A HE2    1 
ATOM   2842 H HZ     . PHE   A 1 199 ? 31.05248  -49.88556 6.18271   1.000 146.19011 ? 200 PHE   A HZ     1 
ATOM   2843 N N      . ASN   A 1 200 ? 29.49560  -47.12173 10.78330  1.000 120.92257 ? 201 ASN   A N      1 
ATOM   2844 C CA     . ASN   A 1 200 ? 28.40411  -47.82795 11.43900  1.000 112.92326 ? 201 ASN   A CA     1 
ATOM   2845 C C      . ASN   A 1 200 ? 28.17681  -49.16660 10.75462  1.000 105.14949 ? 201 ASN   A C      1 
ATOM   2846 O O      . ASN   A 1 200 ? 28.14655  -49.24202 9.52210   1.000 122.05083 ? 201 ASN   A O      1 
ATOM   2847 C CB     . ASN   A 1 200 ? 27.11713  -46.99996 11.40581  1.000 115.46820 ? 201 ASN   A CB     1 
ATOM   2848 C CG     . ASN   A 1 200 ? 27.34935  -45.55145 11.77758  1.000 123.03146 ? 201 ASN   A CG     1 
ATOM   2849 O OD1    . ASN   A 1 200 ? 27.49590  -45.21486 12.95303  1.000 127.54533 ? 201 ASN   A OD1    1 
ATOM   2850 N ND2    . ASN   A 1 200 ? 27.38139  -44.68237 10.77430  1.000 127.56054 ? 201 ASN   A ND2    1 
ATOM   2851 H H      . ASN   A 1 200 ? 29.37491  -47.01387 9.93867   1.000 145.49756 ? 201 ASN   A H      1 
ATOM   2852 H HA     . ASN   A 1 200 ? 28.64290  -47.99600 12.36401  1.000 135.89839 ? 201 ASN   A HA     1 
ATOM   2853 H HB2    . ASN   A 1 200 ? 26.74726  -47.02492 10.50944  1.000 138.95231 ? 201 ASN   A HB2    1 
ATOM   2854 H HB3    . ASN   A 1 200 ? 26.48291  -47.37458 12.03695  1.000 138.95231 ? 201 ASN   A HB3    1 
ATOM   2855 H HD21   . ASN   A 1 200 ? 27.51043  -43.84704 10.93295  1.000 153.46311 ? 201 ASN   A HD21   1 
ATOM   2856 H HD22   . ASN   A 1 200 ? 27.27310  -44.95479 9.96580   1.000 153.46311 ? 201 ASN   A HD22   1 
ATOM   2857 N N      . ILE   A 1 201 ? 28.01439  -50.21527 11.55485  1.000 98.50716  ? 202 ILE   A N      1 
ATOM   2858 C CA     . ILE   A 1 201 ? 27.67706  -51.54685 11.06675  1.000 98.07161  ? 202 ILE   A CA     1 
ATOM   2859 C C      . ILE   A 1 201 ? 26.34608  -51.93119 11.69297  1.000 97.93931  ? 202 ILE   A C      1 
ATOM   2860 O O      . ILE   A 1 201 ? 26.22812  -51.98455 12.92224  1.000 112.01867 ? 202 ILE   A O      1 
ATOM   2861 C CB     . ILE   A 1 201 ? 28.76516  -52.57564 11.40683  1.000 98.93239  ? 202 ILE   A CB     1 
ATOM   2862 C CG1    . ILE   A 1 201 ? 30.09285  -52.17018 10.76416  1.000 99.37255  ? 202 ILE   A CG1    1 
ATOM   2863 C CG2    . ILE   A 1 201 ? 28.35339  -53.96511 10.93623  1.000 107.46400 ? 202 ILE   A CG2    1 
ATOM   2864 C CD1    . ILE   A 1 201 ? 31.26962  -53.00061 11.22298  1.000 117.35484 ? 202 ILE   A CD1    1 
ATOM   2865 H H      . ILE   A 1 201 ? 28.09715  -50.17812 12.41005  1.000 116.25624 ? 202 ILE   A H      1 
ATOM   2866 H HA     . ILE   A 1 201 ? 27.57520  -51.52719 10.10232  1.000 115.73358 ? 202 ILE   A HA     1 
ATOM   2867 H HB     . ILE   A 1 201 ? 28.87621  -52.59630 12.37023  1.000 116.76652 ? 202 ILE   A HB     1 
ATOM   2868 H HG12   . ILE   A 1 201 ? 30.01713  -52.26989 9.80227   1.000 117.29471 ? 202 ILE   A HG12   1 
ATOM   2869 H HG13   . ILE   A 1 201 ? 30.27813  -51.24478 10.98821  1.000 117.29471 ? 202 ILE   A HG13   1 
ATOM   2870 H HG21   . ILE   A 1 201 ? 29.08357  -54.58273 11.09837  1.000 129.34727 ? 202 ILE   A HG21   1 
ATOM   2871 H HG22   . ILE   A 1 201 ? 27.56704  -54.24564 11.43005  1.000 129.34727 ? 202 ILE   A HG22   1 
ATOM   2872 H HG23   . ILE   A 1 201 ? 28.15352  -53.93092 9.98766   1.000 129.34727 ? 202 ILE   A HG23   1 
ATOM   2873 H HD11   . ILE   A 1 201 ? 32.09031  -52.57355 10.93145  1.000 141.21627 ? 202 ILE   A HD11   1 
ATOM   2874 H HD12   . ILE   A 1 201 ? 31.25449  -53.06211 12.19091  1.000 141.21627 ? 202 ILE   A HD12   1 
ATOM   2875 H HD13   . ILE   A 1 201 ? 31.20162  -53.88666 10.83414  1.000 141.21627 ? 202 ILE   A HD13   1 
ATOM   2876 N N      . GLN   A 1 202 ? 25.34981  -52.19482 10.85359  1.000 97.63188  ? 203 GLN   A N      1 
ATOM   2877 C CA     . GLN   A 1 202 ? 23.99307  -52.46855 11.29770  1.000 99.98801  ? 203 GLN   A CA     1 
ATOM   2878 C C      . GLN   A 1 202 ? 23.59787  -53.88805 10.91594  1.000 97.90638  ? 203 GLN   A C      1 
ATOM   2879 O O      . GLN   A 1 202 ? 24.22333  -54.51937 10.06090  1.000 102.56580 ? 203 GLN   A O      1 
ATOM   2880 C CB     . GLN   A 1 202 ? 23.00384  -51.47040 10.68320  1.000 105.41474 ? 203 GLN   A CB     1 
ATOM   2881 C CG     . GLN   A 1 202 ? 23.45077  -50.02163 10.77489  1.000 119.49085 ? 203 GLN   A CG     1 
ATOM   2882 C CD     . GLN   A 1 202 ? 23.78038  -49.60516 12.19141  1.000 129.82168 ? 203 GLN   A CD     1 
ATOM   2883 O OE1    . GLN   A 1 202 ? 24.94854  -49.47241 12.55790  1.000 133.25150 ? 203 GLN   A OE1    1 
ATOM   2884 N NE2    . GLN   A 1 202 ? 22.74939  -49.39479 12.99824  1.000 139.62204 ? 203 GLN   A NE2    1 
ATOM   2885 H H      . GLN   A 1 202 ? 25.44053  -52.22087 9.99879   1.000 117.54873 ? 203 GLN   A H      1 
ATOM   2886 H HA     . GLN   A 1 202 ? 23.94692  -52.39251 12.26361  1.000 120.37608 ? 203 GLN   A HA     1 
ATOM   2887 H HB2    . GLN   A 1 202 ? 22.88878  -51.68485 9.74423   1.000 126.88816 ? 203 GLN   A HB2    1 
ATOM   2888 H HB3    . GLN   A 1 202 ? 22.15567  -51.54751 11.14748  1.000 126.88816 ? 203 GLN   A HB3    1 
ATOM   2889 H HG2    . GLN   A 1 202 ? 24.24599  -49.90034 10.23284  1.000 143.77949 ? 203 GLN   A HG2    1 
ATOM   2890 H HG3    . GLN   A 1 202 ? 22.73799  -49.44895 10.45103  1.000 143.77949 ? 203 GLN   A HG3    1 
ATOM   2891 H HE21   . GLN   A 1 202 ? 21.94697  -49.49684 12.70615  1.000 167.93691 ? 203 GLN   A HE21   1 
ATOM   2892 H HE22   . GLN   A 1 202 ? 22.88312  -49.15630 13.81361  1.000 167.93691 ? 203 GLN   A HE22   1 
ATOM   2893 N N      . ALA   A 1 203 ? 22.54528  -54.38764 11.55838  1.000 107.57669 ? 204 ALA   A N      1 
ATOM   2894 C CA     . ALA   A 1 203 ? 22.04290  -55.71853 11.24612  1.000 111.53059 ? 204 ALA   A CA     1 
ATOM   2895 C C      . ALA   A 1 203 ? 20.72969  -55.95157 11.97596  1.000 105.39377 ? 204 ALA   A C      1 
ATOM   2896 O O      . ALA   A 1 203 ? 20.39557  -55.25279 12.93723  1.000 100.75716 ? 204 ALA   A O      1 
ATOM   2897 C CB     . ALA   A 1 203 ? 23.05556  -56.80660 11.62094  1.000 134.49484 ? 204 ALA   A CB     1 
ATOM   2898 H H      . ALA   A 1 203 ? 22.10885  -53.97659 12.17495  1.000 129.48250 ? 204 ALA   A H      1 
ATOM   2899 H HA     . ALA   A 1 203 ? 21.86636  -55.76563 10.29349  1.000 134.22718 ? 204 ALA   A HA     1 
ATOM   2900 H HB1    . ALA   A 1 203 ? 22.68060  -57.67480 11.40523  1.000 161.78428 ? 204 ALA   A HB1    1 
ATOM   2901 H HB2    . ALA   A 1 203 ? 23.87242  -56.66472 11.11744  1.000 161.78428 ? 204 ALA   A HB2    1 
ATOM   2902 H HB3    . ALA   A 1 203 ? 23.23952  -56.75274 12.57181  1.000 161.78428 ? 204 ALA   A HB3    1 
ATOM   2903 N N      . ASP   A 1 204 ? 19.99167  -56.95034 11.49609  1.000 113.78445 ? 205 ASP   A N      1 
ATOM   2904 C CA     . ASP   A 1 204 ? 18.75678  -57.41267 12.10985  1.000 103.43742 ? 205 ASP   A CA     1 
ATOM   2905 C C      . ASP   A 1 204 ? 18.90769  -58.87951 12.48350  1.000 105.04988 ? 205 ASP   A C      1 
ATOM   2906 O O      . ASP   A 1 204 ? 19.49347  -59.66291 11.72906  1.000 105.35137 ? 205 ASP   A O      1 
ATOM   2907 C CB     . ASP   A 1 204 ? 17.56022  -57.25264 11.16241  1.000 114.65692 ? 205 ASP   A CB     1 
ATOM   2908 C CG     . ASP   A 1 204 ? 17.13897  -55.81001 10.98846  1.000 106.70707 ? 205 ASP   A CG     1 
ATOM   2909 O OD1    . ASP   A 1 204 ? 16.96377  -55.11604 12.00960  1.000 102.04456 ? 205 ASP   A OD1    1 
ATOM   2910 O OD2    . ASP   A 1 204 ? 16.98287  -55.37039 9.82956   1.000 117.96756 ? 205 ASP   A OD2    1 
ATOM   2911 H H      . ASP   A 1 204 ? 20.19725  -57.39130 10.78694  1.000 136.93181 ? 205 ASP   A H      1 
ATOM   2912 H HA     . ASP   A 1 204 ? 18.58042  -56.89352 12.91003  1.000 124.51537 ? 205 ASP   A HA     1 
ATOM   2913 H HB2    . ASP   A 1 204 ? 17.79918  -57.60243 10.28980  1.000 137.97877 ? 205 ASP   A HB2    1 
ATOM   2914 H HB3    . ASP   A 1 204 ? 16.80501  -57.74423 11.52143  1.000 137.97877 ? 205 ASP   A HB3    1 
ATOM   2915 N N      . ILE   A 1 205 ? 18.38045  -59.24688 13.64753  1.000 112.31426 ? 206 ILE   A N      1 
ATOM   2916 C CA     . ILE   A 1 205 ? 18.30338  -60.63737 14.07987  1.000 118.73063 ? 206 ILE   A CA     1 
ATOM   2917 C C      . ILE   A 1 205 ? 16.83883  -60.95740 14.33343  1.000 116.74283 ? 206 ILE   A C      1 
ATOM   2918 O O      . ILE   A 1 205 ? 16.19635  -60.32083 15.17834  1.000 116.83987 ? 206 ILE   A O      1 
ATOM   2919 C CB     . ILE   A 1 205 ? 19.14844  -60.90394 15.33490  1.000 114.54463 ? 206 ILE   A CB     1 
ATOM   2920 C CG1    . ILE   A 1 205 ? 20.63546  -60.90553 14.97588  1.000 122.36980 ? 206 ILE   A CG1    1 
ATOM   2921 C CG2    . ILE   A 1 205 ? 18.74594  -62.23086 15.96740  1.000 118.22508 ? 206 ILE   A CG2    1 
ATOM   2922 C CD1    . ILE   A 1 205 ? 21.55864  -60.85645 16.17271  1.000 138.19636 ? 206 ILE   A CD1    1 
ATOM   2923 H H      . ILE   A 1 205 ? 18.05252  -58.69329 14.21814  1.000 135.16758 ? 206 ILE   A H      1 
ATOM   2924 H HA     . ILE   A 1 205 ? 18.63103  -61.21250 13.37081  1.000 142.86723 ? 206 ILE   A HA     1 
ATOM   2925 H HB     . ILE   A 1 205 ? 18.98743  -60.19519 15.97727  1.000 137.84402 ? 206 ILE   A HB     1 
ATOM   2926 H HG12   . ILE   A 1 205 ? 20.83515  -61.71653 14.48262  1.000 147.23423 ? 206 ILE   A HG12   1 
ATOM   2927 H HG13   . ILE   A 1 205 ? 20.82333  -60.12840 14.42662  1.000 147.23423 ? 206 ILE   A HG13   1 
ATOM   2928 H HG21   . ILE   A 1 205 ? 19.45023  -62.52091 16.56802  1.000 142.26057 ? 206 ILE   A HG21   1 
ATOM   2929 H HG22   . ILE   A 1 205 ? 17.92008  -62.10776 16.46106  1.000 142.26057 ? 206 ILE   A HG22   1 
ATOM   2930 H HG23   . ILE   A 1 205 ? 18.61731  -62.88875 15.26631  1.000 142.26057 ? 206 ILE   A HG23   1 
ATOM   2931 H HD11   . ILE   A 1 205 ? 22.47665  -60.81638 15.86200  1.000 166.22611 ? 206 ILE   A HD11   1 
ATOM   2932 H HD12   . ILE   A 1 205 ? 21.35260  -60.06768 16.69834  1.000 166.22611 ? 206 ILE   A HD12   1 
ATOM   2933 H HD13   . ILE   A 1 205 ? 21.42499  -61.65456 16.70756  1.000 166.22611 ? 206 ILE   A HD13   1 
ATOM   2934 N N      . HIS   A 1 206 ? 16.31260  -61.93331 13.60105  1.000 117.41595 ? 207 HIS   A N      1 
ATOM   2935 C CA     . HIS   A 1 206 ? 14.93271  -62.36299 13.76543  1.000 132.36701 ? 207 HIS   A CA     1 
ATOM   2936 C C      . HIS   A 1 206 ? 14.84056  -63.42674 14.84893  1.000 137.95662 ? 207 HIS   A C      1 
ATOM   2937 O O      . HIS   A 1 206 ? 15.72960  -64.27233 14.98537  1.000 131.27176 ? 207 HIS   A O      1 
ATOM   2938 C CB     . HIS   A 1 206 ? 14.38035  -62.90356 12.44838  1.000 136.56654 ? 207 HIS   A CB     1 
ATOM   2939 C CG     . HIS   A 1 206 ? 14.18803  -61.85066 11.40438  1.000 127.54262 ? 207 HIS   A CG     1 
ATOM   2940 N ND1    . HIS   A 1 206 ? 13.00036  -61.68345 10.72622  1.000 145.76307 ? 207 HIS   A ND1    1 
ATOM   2941 C CD2    . HIS   A 1 206 ? 15.02811  -60.89919 10.93314  1.000 115.75855 ? 207 HIS   A CD2    1 
ATOM   2942 C CE1    . HIS   A 1 206 ? 13.11996  -60.68003 9.87529   1.000 159.54049 ? 207 HIS   A CE1    1 
ATOM   2943 N NE2    . HIS   A 1 206 ? 14.34031  -60.18645 9.98182   1.000 128.94150 ? 207 HIS   A NE2    1 
ATOM   2944 H H      . HIS   A 1 206 ? 16.74176  -62.36669 12.99475  1.000 141.28962 ? 207 HIS   A H      1 
ATOM   2945 H HA     . HIS   A 1 206 ? 14.38659  -61.60788 14.03462  1.000 159.23088 ? 207 HIS   A HA     1 
ATOM   2946 H HB2    . HIS   A 1 206 ? 14.99992  -63.56148 12.09600  1.000 164.27032 ? 207 HIS   A HB2    1 
ATOM   2947 H HB3    . HIS   A 1 206 ? 13.51863  -63.31597 12.61648  1.000 164.27032 ? 207 HIS   A HB3    1 
ATOM   2948 H HD2    . HIS   A 1 206 ? 15.90635  -60.75526 11.20308  1.000 139.30073 ? 207 HIS   A HD2    1 
ATOM   2949 H HE1    . HIS   A 1 206 ? 12.45744  -60.37336 9.29917   1.000 191.83906 ? 207 HIS   A HE1    1 
ATOM   2950 N N      . GLN   A 1 207 ? 13.75449  -63.38063 15.61575  1.000 133.41052 ? 208 GLN   A N      1 
ATOM   2951 C CA     . GLN   A 1 207 ? 13.58941  -64.29086 16.74003  1.000 134.93129 ? 208 GLN   A CA     1 
ATOM   2952 C C      . GLN   A 1 207 ? 14.79060  -64.15888 17.66814  1.000 139.24969 ? 208 GLN   A C      1 
ATOM   2953 O O      . GLN   A 1 207 ? 15.44678  -65.15956 17.98460  1.000 151.80794 ? 208 GLN   A O      1 
ATOM   2954 C CB     . GLN   A 1 207 ? 13.43401  -65.72547 16.24126  1.000 130.80768 ? 208 GLN   A CB     1 
ATOM   2955 C CG     . GLN   A 1 207 ? 12.21019  -65.92686 15.36757  1.000 144.08628 ? 208 GLN   A CG     1 
ATOM   2956 C CD     . GLN   A 1 207 ? 12.37923  -67.06425 14.38276  1.000 189.39208 ? 208 GLN   A CD     1 
ATOM   2957 O OE1    . GLN   A 1 207 ? 12.77009  -66.85153 13.23482  1.000 186.70212 ? 208 GLN   A OE1    1 
ATOM   2958 N NE2    . GLN   A 1 207 ? 12.08512  -68.28091 14.82561  1.000 189.99983 ? 208 GLN   A NE2    1 
ATOM   2959 H H      . GLN   A 1 207 ? 13.10176  -62.83191 15.50419  1.000 160.48310 ? 208 GLN   A H      1 
ATOM   2960 H HA     . GLN   A 1 207 ? 12.79037  -64.06586 17.24184  1.000 162.30802 ? 208 GLN   A HA     1 
ATOM   2961 H HB2    . GLN   A 1 207 ? 14.21596  -65.96223 15.71839  1.000 157.35969 ? 208 GLN   A HB2    1 
ATOM   2962 H HB3    . GLN   A 1 207 ? 13.35494  -66.31670 17.00618  1.000 157.35969 ? 208 GLN   A HB3    1 
ATOM   2963 H HG2    . GLN   A 1 207 ? 11.44776  -66.12890 15.93218  1.000 173.29400 ? 208 GLN   A HG2    1 
ATOM   2964 H HG3    . GLN   A 1 207 ? 12.04385  -65.11499 14.86349  1.000 173.29400 ? 208 GLN   A HG3    1 
ATOM   2965 H HE21   . GLN   A 1 207 ? 11.81455  -68.39030 15.63458  1.000 228.39027 ? 208 GLN   A HE21   1 
ATOM   2966 H HE22   . GLN   A 1 207 ? 12.16519  -68.95957 14.30350  1.000 228.39027 ? 208 GLN   A HE22   1 
ATOM   2967 N N      . PRO   A 1 208 ? 15.10956  -62.94346 18.12098  1.000 126.03508 ? 209 PRO   A N      1 
ATOM   2968 C CA     . PRO   A 1 208 ? 16.30715  -62.76756 18.95891  1.000 128.02839 ? 209 PRO   A CA     1 
ATOM   2969 C C      . PRO   A 1 208 ? 16.23926  -63.52527 20.26809  1.000 132.95898 ? 209 PRO   A C      1 
ATOM   2970 O O      . PRO   A 1 208 ? 17.27916  -63.96313 20.77787  1.000 122.16715 ? 209 PRO   A O      1 
ATOM   2971 C CB     . PRO   A 1 208 ? 16.35185  -61.24943 19.18558  1.000 127.68473 ? 209 PRO   A CB     1 
ATOM   2972 C CG     . PRO   A 1 208 ? 14.93488  -60.80013 19.00922  1.000 123.88624 ? 209 PRO   A CG     1 
ATOM   2973 C CD     . PRO   A 1 208 ? 14.36165  -61.68579 17.94665  1.000 124.85868 ? 209 PRO   A CD     1 
ATOM   2974 H HA     . PRO   A 1 208 ? 17.09835  -63.04327 18.47015  1.000 154.02454 ? 209 PRO   A HA     1 
ATOM   2975 H HB2    . PRO   A 1 208 ? 16.66969  -61.05692 20.08158  1.000 153.61214 ? 209 PRO   A HB2    1 
ATOM   2976 H HB3    . PRO   A 1 208 ? 16.93370  -60.83311 18.53057  1.000 153.61214 ? 209 PRO   A HB3    1 
ATOM   2977 H HG2    . PRO   A 1 208 ? 14.45096  -60.90509 19.84331  1.000 149.05396 ? 209 PRO   A HG2    1 
ATOM   2978 H HG3    . PRO   A 1 208 ? 14.91731  -59.87133 18.73008  1.000 149.05396 ? 209 PRO   A HG3    1 
ATOM   2979 H HD2    . PRO   A 1 208 ? 13.41219  -61.82547 18.08773  1.000 150.22089 ? 209 PRO   A HD2    1 
ATOM   2980 H HD3    . PRO   A 1 208 ? 14.51453  -61.31172 17.06483  1.000 150.22089 ? 209 PRO   A HD3    1 
ATOM   2981 N N      . GLU   A 1 209 ? 15.03968  -63.68957 20.83195  1.000 146.37676 ? 210 GLU   A N      1 
ATOM   2982 C CA     . GLU   A 1 209 ? 14.89612  -64.45541 22.06356  1.000 139.04535 ? 210 GLU   A CA     1 
ATOM   2983 C C      . GLU   A 1 209 ? 15.49304  -65.84945 21.92611  1.000 136.67981 ? 210 GLU   A C      1 
ATOM   2984 O O      . GLU   A 1 209 ? 15.90837  -66.44953 22.92365  1.000 141.64935 ? 210 GLU   A O      1 
ATOM   2985 C CB     . GLU   A 1 209 ? 13.41720  -64.54452 22.45818  1.000 138.59106 ? 210 GLU   A CB     1 
ATOM   2986 C CG     . GLU   A 1 209 ? 12.53338  -65.34178 21.50075  1.000 140.14940 ? 210 GLU   A CG     1 
ATOM   2987 C CD     . GLU   A 1 209 ? 12.20803  -64.59214 20.22623  1.000 142.80618 ? 210 GLU   A CD     1 
ATOM   2988 O OE1    . GLU   A 1 209 ? 12.61190  -63.41651 20.10553  1.000 161.90069 ? 210 GLU   A OE1    1 
ATOM   2989 O OE2    . GLU   A 1 209 ? 11.54786  -65.18052 19.34503  1.000 143.15193 ? 210 GLU   A OE2    1 
ATOM   2990 H H      . GLU   A 1 209 ? 14.30342  -63.37038 20.52269  1.000 176.04259 ? 210 GLU   A H      1 
ATOM   2991 H HA     . GLU   A 1 209 ? 15.36673  -63.99619 22.77669  1.000 167.24489 ? 210 GLU   A HA     1 
ATOM   2992 H HB2    . GLU   A 1 209 ? 13.35788  -64.96892 23.32839  1.000 166.69975 ? 210 GLU   A HB2    1 
ATOM   2993 H HB3    . GLU   A 1 209 ? 13.05777  -63.64467 22.50272  1.000 166.69975 ? 210 GLU   A HB3    1 
ATOM   2994 H HG2    . GLU   A 1 209 ? 12.99301  -66.16022 21.25622  1.000 168.56975 ? 210 GLU   A HG2    1 
ATOM   2995 H HG3    . GLU   A 1 209 ? 11.69705  -65.55108 21.94532  1.000 168.56975 ? 210 GLU   A HG3    1 
ATOM   2996 N N      . VAL   A 1 210 ? 15.54815  -66.37677 20.70675  1.000 136.80618 ? 211 VAL   A N      1 
ATOM   2997 C CA     . VAL   A 1 210 ? 16.10020  -67.70642 20.46807  1.000 140.79117 ? 211 VAL   A CA     1 
ATOM   2998 C C      . VAL   A 1 210 ? 17.57392  -67.63809 20.09552  1.000 144.85339 ? 211 VAL   A C      1 
ATOM   2999 O O      . VAL   A 1 210 ? 18.39837  -68.38033 20.63518  1.000 153.58522 ? 211 VAL   A O      1 
ATOM   3000 C CB     . VAL   A 1 210 ? 15.28403  -68.42184 19.36983  1.000 140.22185 ? 211 VAL   A CB     1 
ATOM   3001 C CG1    . VAL   A 1 210 ? 16.05822  -69.61314 18.81825  1.000 145.46960 ? 211 VAL   A CG1    1 
ATOM   3002 C CG2    . VAL   A 1 210 ? 13.93849  -68.86124 19.91088  1.000 141.74469 ? 211 VAL   A CG2    1 
ATOM   3003 H H      . VAL   A 1 210 ? 15.27012  -65.98160 19.99531  1.000 164.55789 ? 211 VAL   A H      1 
ATOM   3004 H HA     . VAL   A 1 210 ? 16.02482  -68.21929 21.28794  1.000 169.33988 ? 211 VAL   A HA     1 
ATOM   3005 H HB     . VAL   A 1 210 ? 15.12796  -67.80149 18.64065  1.000 168.65669 ? 211 VAL   A HB     1 
ATOM   3006 H HG11   . VAL   A 1 210 ? 15.44580  -70.19367 18.33990  1.000 174.95399 ? 211 VAL   A HG11   1 
ATOM   3007 H HG12   . VAL   A 1 210 ? 16.74691  -69.29075 18.21603  1.000 174.95399 ? 211 VAL   A HG12   1 
ATOM   3008 H HG13   . VAL   A 1 210 ? 16.46321  -70.09552 19.55594  1.000 174.95399 ? 211 VAL   A HG13   1 
ATOM   3009 H HG21   . VAL   A 1 210 ? 13.45979  -69.33989 19.21616  1.000 170.48410 ? 211 VAL   A HG21   1 
ATOM   3010 H HG22   . VAL   A 1 210 ? 14.07968  -69.44151 20.67524  1.000 170.48410 ? 211 VAL   A HG22   1 
ATOM   3011 H HG23   . VAL   A 1 210 ? 13.43476  -68.07702 20.17950  1.000 170.48410 ? 211 VAL   A HG23   1 
ATOM   3012 N N      . ASN   A 1 211 ? 17.92704  -66.75092 19.16578  1.000 142.25414 ? 212 ASN   A N      1 
ATOM   3013 C CA     . ASN   A 1 211 ? 19.27397  -66.75905 18.60760  1.000 144.75684 ? 212 ASN   A CA     1 
ATOM   3014 C C      . ASN   A 1 211 ? 20.28134  -66.09972 19.54189  1.000 144.32746 ? 212 ASN   A C      1 
ATOM   3015 O O      . ASN   A 1 211 ? 21.40989  -66.58492 19.67663  1.000 154.99159 ? 212 ASN   A O      1 
ATOM   3016 C CB     . ASN   A 1 211 ? 19.26602  -66.07435 17.24045  1.000 143.34557 ? 212 ASN   A CB     1 
ATOM   3017 C CG     . ASN   A 1 211 ? 18.52897  -66.88615 16.19121  1.000 139.65311 ? 212 ASN   A CG     1 
ATOM   3018 O OD1    . ASN   A 1 211 ? 18.69202  -68.10354 16.10806  1.000 144.08712 ? 212 ASN   A OD1    1 
ATOM   3019 N ND2    . ASN   A 1 211 ? 17.70428  -66.21808 15.39315  1.000 144.50905 ? 212 ASN   A ND2    1 
ATOM   3020 H H      . ASN   A 1 211 ? 17.41087  -66.14192 18.84595  1.000 171.09544 ? 212 ASN   A H      1 
ATOM   3021 H HA     . ASN   A 1 211 ? 19.55868  -67.67783 18.48239  1.000 174.09868 ? 212 ASN   A HA     1 
ATOM   3022 H HB2    . ASN   A 1 211 ? 18.82627  -65.21334 17.31917  1.000 172.40515 ? 212 ASN   A HB2    1 
ATOM   3023 H HB3    . ASN   A 1 211 ? 20.18057  -65.95359 16.94057  1.000 172.40515 ? 212 ASN   A HB3    1 
ATOM   3024 H HD21   . ASN   A 1 211 ? 17.26443  -66.63513 14.78307  1.000 173.80133 ? 212 ASN   A HD21   1 
ATOM   3025 H HD22   . ASN   A 1 211 ? 17.61004  -65.36836 15.48637  1.000 173.80133 ? 212 ASN   A HD22   1 
ATOM   3026 N N      . CYS   A 1 212 ? 19.89875  -65.00895 20.20016  1.000 126.83355 ? 213 CYS   A N      1 
ATOM   3027 C CA     . CYS   A 1 212 ? 20.77582  -64.30171 21.13471  1.000 131.81449 ? 213 CYS   A CA     1 
ATOM   3028 C C      . CYS   A 1 212 ? 20.04485  -64.08444 22.45419  1.000 151.04638 ? 213 CYS   A C      1 
ATOM   3029 O O      . CYS   A 1 212 ? 19.80518  -62.94836 22.87378  1.000 152.05466 ? 213 CYS   A O      1 
ATOM   3030 C CB     . CYS   A 1 212 ? 21.23966  -62.97656 20.53517  1.000 127.70499 ? 213 CYS   A CB     1 
ATOM   3031 S SG     . CYS   A 1 212 ? 19.88421  -61.90813 20.00205  1.000 135.09194 ? 213 CYS   A SG     1 
ATOM   3032 H H      . CYS   A 1 212 ? 19.12068  -64.65114 20.12161  1.000 152.59074 ? 213 CYS   A H      1 
ATOM   3033 H HA     . CYS   A 1 212 ? 21.56084  -64.84374 21.31038  1.000 158.56785 ? 213 CYS   A HA     1 
ATOM   3034 H HB2    . CYS   A 1 212 ? 21.75241  -62.49450 21.20270  1.000 153.63646 ? 213 CYS   A HB2    1 
ATOM   3035 H HB3    . CYS   A 1 212 ? 21.79387  -63.16136 19.76083  1.000 153.63646 ? 213 CYS   A HB3    1 
ATOM   3036 H HG     . CYS   A 1 212 ? 19.20490  -61.63501 20.95280  1.000 162.50080 ? 213 CYS   A HG     1 
ATOM   3037 N N      . PRO   A 1 213 ? 19.68329  -65.16796 23.14546  1.000 150.48876 ? 214 PRO   A N      1 
ATOM   3038 C CA     . PRO   A 1 213 ? 18.89546  -65.00890 24.37923  1.000 134.75700 ? 214 PRO   A CA     1 
ATOM   3039 C C      . PRO   A 1 213 ? 19.61080  -64.20892 25.45041  1.000 135.42513 ? 214 PRO   A C      1 
ATOM   3040 O O      . PRO   A 1 213 ? 18.98383  -63.37635 26.11731  1.000 132.51292 ? 214 PRO   A O      1 
ATOM   3041 C CB     . PRO   A 1 213 ? 18.64390  -66.45865 24.81930  1.000 140.31808 ? 214 PRO   A CB     1 
ATOM   3042 C CG     . PRO   A 1 213 ? 19.74326  -67.24856 24.18902  1.000 140.12701 ? 214 PRO   A CG     1 
ATOM   3043 C CD     . PRO   A 1 213 ? 20.04136  -66.57320 22.88488  1.000 147.90750 ? 214 PRO   A CD     1 
ATOM   3044 H HA     . PRO   A 1 213 ? 18.04844  -64.58255 24.17506  1.000 162.09887 ? 214 PRO   A HA     1 
ATOM   3045 H HB2    . PRO   A 1 213 ? 18.68143  -66.52155 25.78653  1.000 168.77217 ? 214 PRO   A HB2    1 
ATOM   3046 H HB3    . PRO   A 1 213 ? 17.77681  -66.75481 24.50097  1.000 168.77217 ? 214 PRO   A HB3    1 
ATOM   3047 H HG2    . PRO   A 1 213 ? 20.52323  -67.24057 24.76564  1.000 168.54289 ? 214 PRO   A HG2    1 
ATOM   3048 H HG3    . PRO   A 1 213 ? 19.44780  -68.16089 24.04323  1.000 168.54289 ? 214 PRO   A HG3    1 
ATOM   3049 H HD2    . PRO   A 1 213 ? 20.98151  -66.65453 22.66035  1.000 177.87947 ? 214 PRO   A HD2    1 
ATOM   3050 H HD3    . PRO   A 1 213 ? 19.49688  -66.94227 22.17198  1.000 177.87947 ? 214 PRO   A HD3    1 
ATOM   3051 N N      . GLY   A 1 214 ? 20.91121  -64.43998 25.63652  1.000 139.95985 ? 215 GLY   A N      1 
ATOM   3052 C CA     . GLY   A 1 214 ? 21.64258  -63.69842 26.65031  1.000 140.86251 ? 215 GLY   A CA     1 
ATOM   3053 C C      . GLY   A 1 214 ? 21.54844  -62.19916 26.45001  1.000 143.97685 ? 215 GLY   A C      1 
ATOM   3054 O O      . GLY   A 1 214 ? 21.15369  -61.46058 27.35590  1.000 144.68068 ? 215 GLY   A O      1 
ATOM   3055 H H      . GLY   A 1 214 ? 21.38102  -65.01004 25.19617  1.000 168.34229 ? 215 GLY   A H      1 
ATOM   3056 H HA2    . GLY   A 1 214 ? 21.28421  -63.91283 27.52581  1.000 169.42549 ? 215 GLY   A HA2    1 
ATOM   3057 H HA3    . GLY   A 1 214 ? 22.57828  -63.95243 26.62122  1.000 169.42549 ? 215 GLY   A HA3    1 
ATOM   3058 N N      . PHE   A 1 215 ? 21.90796  -61.72745 25.25467  1.000 133.35690 ? 216 PHE   A N      1 
ATOM   3059 C CA     . PHE   A 1 215 ? 21.82973  -60.29749 24.98715  1.000 129.72587 ? 216 PHE   A CA     1 
ATOM   3060 C C      . PHE   A 1 215 ? 20.38639  -59.81699 24.91213  1.000 135.22799 ? 216 PHE   A C      1 
ATOM   3061 O O      . PHE   A 1 215 ? 20.09605  -58.67482 25.28490  1.000 138.64871 ? 216 PHE   A O      1 
ATOM   3062 C CB     . PHE   A 1 215 ? 22.55973  -59.96042 23.69101  1.000 120.51047 ? 216 PHE   A CB     1 
ATOM   3063 C CG     . PHE   A 1 215 ? 22.50139  -58.50555 23.33170  1.000 122.24749 ? 216 PHE   A CG     1 
ATOM   3064 C CD1    . PHE   A 1 215 ? 23.42701  -57.61553 23.84460  1.000 123.61112 ? 216 PHE   A CD1    1 
ATOM   3065 C CD2    . PHE   A 1 215 ? 21.51536  -58.02515 22.48729  1.000 129.25171 ? 216 PHE   A CD2    1 
ATOM   3066 C CE1    . PHE   A 1 215 ? 23.37248  -56.27467 23.51795  1.000 126.36645 ? 216 PHE   A CE1    1 
ATOM   3067 C CE2    . PHE   A 1 215 ? 21.45690  -56.68519 22.15837  1.000 121.05496 ? 216 PHE   A CE2    1 
ATOM   3068 C CZ     . PHE   A 1 215 ? 22.38557  -55.81020 22.67382  1.000 117.64440 ? 216 PHE   A CZ     1 
ATOM   3069 H H      . PHE   A 1 215 ? 22.19343  -62.20485 24.59878  1.000 160.41875 ? 216 PHE   A H      1 
ATOM   3070 H HA     . PHE   A 1 215 ? 22.26950  -59.82571 25.71168  1.000 156.06151 ? 216 PHE   A HA     1 
ATOM   3071 H HB2    . PHE   A 1 215 ? 23.49344  -60.20590 23.78503  1.000 145.00303 ? 216 PHE   A HB2    1 
ATOM   3072 H HB3    . PHE   A 1 215 ? 22.15629  -60.46196 22.96534  1.000 145.00303 ? 216 PHE   A HB3    1 
ATOM   3073 H HD1    . PHE   A 1 215 ? 24.09346  -57.92311 24.41567  1.000 148.72381 ? 216 PHE   A HD1    1 
ATOM   3074 H HD2    . PHE   A 1 215 ? 20.88452  -58.61196 22.13718  1.000 155.49252 ? 216 PHE   A HD2    1 
ATOM   3075 H HE1    . PHE   A 1 215 ? 24.00119  -55.68503 23.86717  1.000 152.03021 ? 216 PHE   A HE1    1 
ATOM   3076 H HE2    . PHE   A 1 215 ? 20.79049  -56.37440 21.58899  1.000 145.65642 ? 216 PHE   A HE2    1 
ATOM   3077 H HZ     . PHE   A 1 215 ? 22.34778  -54.90748 22.45342  1.000 141.56375 ? 216 PHE   A HZ     1 
ATOM   3078 N N      . PHE   A 1 216 ? 19.47340  -60.66165 24.42947  1.000 136.26151 ? 217 PHE   A N      1 
ATOM   3079 C CA     . PHE   A 1 216 ? 18.07026  -60.26745 24.35889  1.000 140.45600 ? 217 PHE   A CA     1 
ATOM   3080 C C      . PHE   A 1 216 ? 17.52882  -59.94314 25.74443  1.000 136.92958 ? 217 PHE   A C      1 
ATOM   3081 O O      . PHE   A 1 216 ? 16.91835  -58.88909 25.95686  1.000 135.78523 ? 217 PHE   A O      1 
ATOM   3082 C CB     . PHE   A 1 216 ? 17.24751  -61.37722 23.70482  1.000 139.72933 ? 217 PHE   A CB     1 
ATOM   3083 C CG     . PHE   A 1 216 ? 15.78787  -61.05230 23.57356  1.000 129.15171 ? 217 PHE   A CG     1 
ATOM   3084 C CD1    . PHE   A 1 216 ? 15.34964  -60.14592 22.62433  1.000 140.26086 ? 217 PHE   A CD1    1 
ATOM   3085 C CD2    . PHE   A 1 216 ? 14.85314  -61.65825 24.39313  1.000 131.64869 ? 217 PHE   A CD2    1 
ATOM   3086 C CE1    . PHE   A 1 216 ? 14.00702  -59.84689 22.49972  1.000 140.71393 ? 217 PHE   A CE1    1 
ATOM   3087 C CE2    . PHE   A 1 216 ? 13.50972  -61.36262 24.27044  1.000 144.97254 ? 217 PHE   A CE2    1 
ATOM   3088 C CZ     . PHE   A 1 216 ? 13.08786  -60.45622 23.32276  1.000 126.00280 ? 217 PHE   A CZ     1 
ATOM   3089 H H      . PHE   A 1 216 ? 19.63894  -61.45495 24.14160  1.000 163.90429 ? 217 PHE   A H      1 
ATOM   3090 H HA     . PHE   A 1 216 ? 17.99327  -59.47249 23.80843  1.000 168.93767 ? 217 PHE   A HA     1 
ATOM   3091 H HB2    . PHE   A 1 216 ? 17.59568  -61.53970 22.81416  1.000 168.06567 ? 217 PHE   A HB2    1 
ATOM   3092 H HB3    . PHE   A 1 216 ? 17.32452  -62.18068 24.24281  1.000 168.06567 ? 217 PHE   A HB3    1 
ATOM   3093 H HD1    . PHE   A 1 216 ? 15.96635  -59.73326 22.06372  1.000 168.70350 ? 217 PHE   A HD1    1 
ATOM   3094 H HD2    . PHE   A 1 216 ? 15.13234  -62.27162 25.03400  1.000 158.36890 ? 217 PHE   A HD2    1 
ATOM   3095 H HE1    . PHE   A 1 216 ? 13.72431  -59.23403 21.85989  1.000 169.24718 ? 217 PHE   A HE1    1 
ATOM   3096 H HE2    . PHE   A 1 216 ? 12.88993  -61.77540 24.82755  1.000 174.35752 ? 217 PHE   A HE2    1 
ATOM   3097 H HZ     . PHE   A 1 216 ? 12.18340  -60.25646 23.23935  1.000 149.25101 ? 217 PHE   A HZ     1 
ATOM   3098 N N      . GLN   A 1 217 ? 17.75026  -60.84133 26.70591  1.000 142.46670 ? 218 GLN   A N      1 
ATOM   3099 C CA     . GLN   A 1 217 ? 17.28378  -60.59266 28.06418  1.000 156.23673 ? 218 GLN   A CA     1 
ATOM   3100 C C      . GLN   A 1 217 ? 17.96023  -59.37306 28.67137  1.000 142.45619 ? 218 GLN   A C      1 
ATOM   3101 O O      . GLN   A 1 217 ? 17.35734  -58.67614 29.49454  1.000 148.27654 ? 218 GLN   A O      1 
ATOM   3102 C CB     . GLN   A 1 217 ? 17.52721  -61.82572 28.93287  1.000 171.05456 ? 218 GLN   A CB     1 
ATOM   3103 C CG     . GLN   A 1 217 ? 16.58546  -62.97697 28.63038  1.000 178.78158 ? 218 GLN   A CG     1 
ATOM   3104 C CD     . GLN   A 1 217 ? 17.15406  -64.31801 29.04374  1.000 177.91188 ? 218 GLN   A CD     1 
ATOM   3105 O OE1    . GLN   A 1 217 ? 17.38264  -64.57268 30.22633  1.000 163.83183 ? 218 GLN   A OE1    1 
ATOM   3106 N NE2    . GLN   A 1 217 ? 17.39425  -65.18344 28.06494  1.000 170.71183 ? 218 GLN   A NE2    1 
ATOM   3107 H H      . GLN   A 1 217 ? 18.16120  -61.58902 26.59778  1.000 171.35052 ? 218 GLN   A H      1 
ATOM   3108 H HA     . GLN   A 1 217 ? 16.32865  -60.42476 28.04311  1.000 187.87455 ? 218 GLN   A HA     1 
ATOM   3109 H HB2    . GLN   A 1 217 ? 18.43395  -62.13740 28.78596  1.000 205.65594 ? 218 GLN   A HB2    1 
ATOM   3110 H HB3    . GLN   A 1 217 ? 17.40732  -61.58078 29.86374  1.000 205.65594 ? 218 GLN   A HB3    1 
ATOM   3111 H HG2    . GLN   A 1 217 ? 15.75456  -62.84138 29.11217  1.000 214.92837 ? 218 GLN   A HG2    1 
ATOM   3112 H HG3    . GLN   A 1 217 ? 16.41486  -63.00415 27.67588  1.000 214.92837 ? 218 GLN   A HG3    1 
ATOM   3113 H HE21   . GLN   A 1 217 ? 17.22659  -64.96774 27.24948  1.000 205.24467 ? 218 GLN   A HE21   1 
ATOM   3114 H HE22   . GLN   A 1 217 ? 17.71742  -65.95940 28.24673  1.000 205.24467 ? 218 GLN   A HE22   1 
ATOM   3115 N N      . LEU   A 1 218 ? 19.20390  -59.09354 28.27893  1.000 136.38823 ? 219 LEU   A N      1 
ATOM   3116 C CA     . LEU   A 1 218 ? 19.89249  -57.92829 28.82210  1.000 136.69474 ? 219 LEU   A CA     1 
ATOM   3117 C C      . LEU   A 1 218 ? 19.17026  -56.64397 28.43682  1.000 139.07340 ? 219 LEU   A C      1 
ATOM   3118 O O      . LEU   A 1 218 ? 19.02871  -55.73146 29.25893  1.000 142.23924 ? 219 LEU   A O      1 
ATOM   3119 C CB     . LEU   A 1 218 ? 21.34100  -57.90489 28.34008  1.000 132.47853 ? 219 LEU   A CB     1 
ATOM   3120 C CG     . LEU   A 1 218 ? 22.23758  -56.83101 28.95746  1.000 137.74602 ? 219 LEU   A CG     1 
ATOM   3121 C CD1    . LEU   A 1 218 ? 22.42115  -57.04544 30.45374  1.000 166.49589 ? 219 LEU   A CD1    1 
ATOM   3122 C CD2    . LEU   A 1 218 ? 23.58481  -56.80914 28.25464  1.000 152.20344 ? 219 LEU   A CD2    1 
ATOM   3123 H H      . LEU   A 1 218 ? 19.65960  -59.55285 27.71239  1.000 164.05635 ? 219 LEU   A H      1 
ATOM   3124 H HA     . LEU   A 1 218 ? 19.90508  -57.98743 29.79021  1.000 164.42416 ? 219 LEU   A HA     1 
ATOM   3125 H HB2    . LEU   A 1 218 ? 21.74115  -58.76466 28.54396  1.000 159.36470 ? 219 LEU   A HB2    1 
ATOM   3126 H HB3    . LEU   A 1 218 ? 21.33793  -57.75944 27.38105  1.000 159.36470 ? 219 LEU   A HB3    1 
ATOM   3127 H HG     . LEU   A 1 218 ? 21.80951  -55.96834 28.84152  1.000 165.68569 ? 219 LEU   A HG     1 
ATOM   3128 H HD11   . LEU   A 1 218 ? 22.85983  -56.26774 30.83274  1.000 200.18554 ? 219 LEU   A HD11   1 
ATOM   3129 H HD12   . LEU   A 1 218 ? 21.55087  -57.16725 30.86443  1.000 200.18554 ? 219 LEU   A HD12   1 
ATOM   3130 H HD13   . LEU   A 1 218 ? 22.96698  -57.83475 30.59503  1.000 200.18554 ? 219 LEU   A HD13   1 
ATOM   3131 H HD21   . LEU   A 1 218 ? 24.14304  -56.12906 28.66302  1.000 183.03460 ? 219 LEU   A HD21   1 
ATOM   3132 H HD22   . LEU   A 1 218 ? 24.00311  -57.67947 28.34654  1.000 183.03460 ? 219 LEU   A HD22   1 
ATOM   3133 H HD23   . LEU   A 1 218 ? 23.44817  -56.60524 27.31621  1.000 183.03460 ? 219 LEU   A HD23   1 
ATOM   3134 N N      . CYS   A 1 219 ? 18.70066  -56.55640 27.19048  1.000 147.31911 ? 220 CYS   A N      1 
ATOM   3135 C CA     . CYS   A 1 219 ? 17.87879  -55.41877 26.79404  1.000 146.75837 ? 220 CYS   A CA     1 
ATOM   3136 C C      . CYS   A 1 219 ? 16.62625  -55.33130 27.65677  1.000 136.46487 ? 220 CYS   A C      1 
ATOM   3137 O O      . CYS   A 1 219 ? 16.20941  -54.23649 28.05301  1.000 135.12357 ? 220 CYS   A O      1 
ATOM   3138 C CB     . CYS   A 1 219 ? 17.50948  -55.53272 25.31474  1.000 131.44971 ? 220 CYS   A CB     1 
ATOM   3139 S SG     . CYS   A 1 219 ? 18.92262  -55.49121 24.17966  1.000 125.16577 ? 220 CYS   A SG     1 
ATOM   3140 H H      . CYS   A 1 219 ? 18.84190  -57.13278 26.56804  1.000 177.17340 ? 220 CYS   A H      1 
ATOM   3141 H HA     . CYS   A 1 219 ? 18.38641  -54.60066 26.91198  1.000 176.50051 ? 220 CYS   A HA     1 
ATOM   3142 H HB2    . CYS   A 1 219 ? 17.04717  -56.37411 25.17605  1.000 158.13012 ? 220 CYS   A HB2    1 
ATOM   3143 H HB3    . CYS   A 1 219 ? 16.92694  -54.79217 25.08422  1.000 158.13012 ? 220 CYS   A HB3    1 
ATOM   3144 H HG     . CYS   A 1 219 ? 19.66761  -56.39221 24.45018  1.000 150.58939 ? 220 CYS   A HG     1 
ATOM   3145 N N      . ASN   A 1 220 ? 16.02423  -56.47756 27.96515  1.000 129.12369 ? 221 ASN   A N      1 
ATOM   3146 C CA     . ASN   A 1 220 ? 14.83256  -56.56084 28.80624  1.000 132.43150 ? 221 ASN   A CA     1 
ATOM   3147 C C      . ASN   A 1 220 ? 13.81145  -55.48668 28.43650  1.000 138.15153 ? 221 ASN   A C      1 
ATOM   3148 O O      . ASN   A 1 220 ? 13.31486  -54.74061 29.28248  1.000 147.37993 ? 221 ASN   A O      1 
ATOM   3149 C CB     . ASN   A 1 220 ? 15.20540  -56.46802 30.28617  1.000 138.64622 ? 221 ASN   A CB     1 
ATOM   3150 C CG     . ASN   A 1 220 ? 14.04537  -56.81141 31.19864  1.000 129.99351 ? 221 ASN   A CG     1 
ATOM   3151 O OD1    . ASN   A 1 220 ? 12.98075  -57.22309 30.73775  1.000 131.42106 ? 221 ASN   A OD1    1 
ATOM   3152 N ND2    . ASN   A 1 220 ? 14.24866  -56.65509 32.50023  1.000 144.46647 ? 221 ASN   A ND2    1 
ATOM   3153 H H      . ASN   A 1 220 ? 16.29601  -57.24578 27.69025  1.000 155.33890 ? 221 ASN   A H      1 
ATOM   3154 H HA     . ASN   A 1 220 ? 14.41649  -57.42272 28.64828  1.000 159.30827 ? 221 ASN   A HA     1 
ATOM   3155 H HB2    . ASN   A 1 220 ? 15.92766  -57.08864 30.47080  1.000 166.76594 ? 221 ASN   A HB2    1 
ATOM   3156 H HB3    . ASN   A 1 220 ? 15.48755  -55.56171 30.48590  1.000 166.76594 ? 221 ASN   A HB3    1 
ATOM   3157 H HD21   . ASN   A 1 220 ? 13.62025  -56.83690 33.05848  1.000 173.75023 ? 221 ASN   A HD21   1 
ATOM   3158 H HD22   . ASN   A 1 220 ? 15.00886  -56.37193 32.78576  1.000 173.75023 ? 221 ASN   A HD22   1 
ATOM   3159 N N      . GLY   A 1 221 ? 13.49835  -55.40818 27.14349  1.000 136.80014 ? 222 GLY   A N      1 
ATOM   3160 C CA     . GLY   A 1 221 ? 12.48250  -54.51044 26.64092  1.000 132.56363 ? 222 GLY   A CA     1 
ATOM   3161 C C      . GLY   A 1 221 ? 12.97922  -53.12738 26.26817  1.000 141.01237 ? 222 GLY   A C      1 
ATOM   3162 O O      . GLY   A 1 221 ? 12.38690  -52.48229 25.39610  1.000 169.90021 ? 222 GLY   A O      1 
ATOM   3163 H H      . GLY   A 1 221 ? 13.87444  -55.87970 26.53044  1.000 164.55064 ? 222 GLY   A H      1 
ATOM   3164 H HA2    . GLY   A 1 221 ? 12.08419  -54.90451 25.84911  1.000 159.46683 ? 222 GLY   A HA2    1 
ATOM   3165 H HA3    . GLY   A 1 221 ? 11.79777  -54.40525 27.31988  1.000 159.46683 ? 222 GLY   A HA3    1 
ATOM   3166 N N      . ASN   A 1 222 ? 14.04985  -52.65652 26.89928  1.000 137.39186 ? 223 ASN   A N      1 
ATOM   3167 C CA     . ASN   A 1 222 ? 14.61226  -51.34432 26.61311  1.000 151.01619 ? 223 ASN   A CA     1 
ATOM   3168 C C      . ASN   A 1 222 ? 15.76220  -51.46098 25.61584  1.000 146.10796 ? 223 ASN   A C      1 
ATOM   3169 O O      . ASN   A 1 222 ? 16.23604  -52.55208 25.29070  1.000 123.13812 ? 223 ASN   A O      1 
ATOM   3170 C CB     . ASN   A 1 222 ? 15.07366  -50.67181 27.90978  1.000 153.30436 ? 223 ASN   A CB     1 
ATOM   3171 C CG     . ASN   A 1 222 ? 13.91196  -50.25903 28.78642  1.000 161.36393 ? 223 ASN   A CG     1 
ATOM   3172 O OD1    . ASN   A 1 222 ? 12.75911  -50.56161 28.48104  1.000 154.75778 ? 223 ASN   A OD1    1 
ATOM   3173 N ND2    . ASN   A 1 222 ? 14.20648  -49.56932 29.88205  1.000 178.00491 ? 223 ASN   A ND2    1 
ATOM   3174 H H      . ASN   A 1 222 ? 14.47543  -53.08833 27.50921  1.000 165.26071 ? 223 ASN   A H      1 
ATOM   3175 H HA     . ASN   A 1 222 ? 13.93175  -50.78185 26.21133  1.000 181.60990 ? 223 ASN   A HA     1 
ATOM   3176 H HB2    . ASN   A 1 222 ? 15.62477  -51.29278 28.41136  1.000 184.35570 ? 223 ASN   A HB2    1 
ATOM   3177 H HB3    . ASN   A 1 222 ? 15.58452  -49.87672 27.69125  1.000 184.35570 ? 223 ASN   A HB3    1 
ATOM   3178 H HD21   . ASN   A 1 222 ? 13.57839  -49.31317 30.41072  1.000 213.99636 ? 223 ASN   A HD21   1 
ATOM   3179 H HD22   . ASN   A 1 222 ? 15.02533  -49.37873 30.06304  1.000 213.99636 ? 223 ASN   A HD22   1 
ATOM   3180 N N      . ARG   A 1 223 ? 16.20778  -50.30670 25.12681  1.000 142.12647 ? 224 ARG   A N      1 
ATOM   3181 C CA     . ARG   A 1 223 ? 17.22623  -50.22648 24.08756  1.000 136.57107 ? 224 ARG   A CA     1 
ATOM   3182 C C      . ARG   A 1 223 ? 18.59027  -50.02642 24.73651  1.000 137.22611 ? 224 ARG   A C      1 
ATOM   3183 O O      . ARG   A 1 223 ? 18.80940  -49.03310 25.43632  1.000 157.49727 ? 224 ARG   A O      1 
ATOM   3184 C CB     . ARG   A 1 223 ? 16.91335  -49.08803 23.11801  1.000 135.40042 ? 224 ARG   A CB     1 
ATOM   3185 C CG     . ARG   A 1 223 ? 15.66971  -49.31204 22.27484  1.000 147.10381 ? 224 ARG   A CG     1 
ATOM   3186 C CD     . ARG   A 1 223 ? 15.61071  -48.30599 21.13992  1.000 166.65710 ? 224 ARG   A CD     1 
ATOM   3187 N NE     . ARG   A 1 223 ? 15.76233  -46.95819 21.67238  1.000 155.36151 ? 224 ARG   A NE     1 
ATOM   3188 C CZ     . ARG   A 1 223 ? 16.71452  -46.09879 21.33024  1.000 160.91493 ? 224 ARG   A CZ     1 
ATOM   3189 N NH1    . ARG   A 1 223 ? 17.50302  -46.31118 20.28741  1.000 168.25823 ? 224 ARG   A NH1    1 
ATOM   3190 N NH2    . ARG   A 1 223 ? 16.87644  -44.99281 22.05062  1.000 173.59972 ? 224 ARG   A NH2    1 
ATOM   3191 H H      . ARG   A 1 223 ? 15.92696  -49.53731 25.38906  1.000 170.94224 ? 224 ARG   A H      1 
ATOM   3192 H HA     . ARG   A 1 223 ? 17.24949  -51.05793 23.58850  1.000 164.27576 ? 224 ARG   A HA     1 
ATOM   3193 H HB2    . ARG   A 1 223 ? 16.78013  -48.27395 23.62834  1.000 162.87098 ? 224 ARG   A HB2    1 
ATOM   3194 H HB3    . ARG   A 1 223 ? 17.66382  -48.98112 22.51280  1.000 162.87098 ? 224 ARG   A HB3    1 
ATOM   3195 H HG2    . ARG   A 1 223 ? 15.68987  -50.20481 21.89609  1.000 176.91505 ? 224 ARG   A HG2    1 
ATOM   3196 H HG3    . ARG   A 1 223 ? 14.87898  -49.20328 22.82604  1.000 176.91505 ? 224 ARG   A HG3    1 
ATOM   3197 H HD2    . ARG   A 1 223 ? 16.32990  -48.47709 20.51192  1.000 200.37899 ? 224 ARG   A HD2    1 
ATOM   3198 H HD3    . ARG   A 1 223 ? 14.75428  -48.36978 20.68896  1.000 200.37899 ? 224 ARG   A HD3    1 
ATOM   3199 H HE     . ARG   A 1 223 ? 15.18742  -46.69790 22.25662  1.000 186.82428 ? 224 ARG   A HE     1 
ATOM   3200 H HH11   . ARG   A 1 223 ? 17.40513  -47.02097 19.81180  1.000 202.30034 ? 224 ARG   A HH11   1 
ATOM   3201 H HH12   . ARG   A 1 223 ? 18.11289  -45.73928 20.08591  1.000 202.30034 ? 224 ARG   A HH12   1 
ATOM   3202 H HH21   . ARG   A 1 223 ? 16.36793  -44.84233 22.72766  1.000 208.71014 ? 224 ARG   A HH21   1 
ATOM   3203 H HH22   . ARG   A 1 223 ? 17.48966  -44.42803 21.83946  1.000 208.71014 ? 224 ARG   A HH22   1 
ATOM   3204 N N      . LEU   A 1 224 ? 19.50417  -50.96192 24.49306  1.000 128.82241 ? 225 LEU   A N      1 
ATOM   3205 C CA     . LEU   A 1 224 ? 20.80104  -50.98353 25.15914  1.000 131.68463 ? 225 LEU   A CA     1 
ATOM   3206 C C      . LEU   A 1 224 ? 21.80047  -50.13146 24.38391  1.000 128.70923 ? 225 LEU   A C      1 
ATOM   3207 O O      . LEU   A 1 224 ? 22.03352  -50.36741 23.19450  1.000 130.79859 ? 225 LEU   A O      1 
ATOM   3208 C CB     . LEU   A 1 224 ? 21.29812  -52.42454 25.28550  1.000 137.32248 ? 225 LEU   A CB     1 
ATOM   3209 C CG     . LEU   A 1 224 ? 22.54871  -52.65861 26.13380  1.000 145.83160 ? 225 LEU   A CG     1 
ATOM   3210 C CD1    . LEU   A 1 224 ? 22.51901  -54.05630 26.73273  1.000 152.75895 ? 225 LEU   A CD1    1 
ATOM   3211 C CD2    . LEU   A 1 224 ? 23.82497  -52.46549 25.32885  1.000 148.46965 ? 225 LEU   A CD2    1 
ATOM   3212 H H      . LEU   A 1 224 ? 19.39355  -51.60699 23.93517  1.000 154.97736 ? 225 LEU   A H      1 
ATOM   3213 H HA     . LEU   A 1 224 ? 20.71557  -50.60078 26.04632  1.000 158.41203 ? 225 LEU   A HA     1 
ATOM   3214 H HB2    . LEU   A 1 224 ? 20.58620  -52.95178 25.68056  1.000 165.17745 ? 225 LEU   A HB2    1 
ATOM   3215 H HB3    . LEU   A 1 224 ? 21.49673  -52.75053 24.39377  1.000 165.17745 ? 225 LEU   A HB3    1 
ATOM   3216 H HG     . LEU   A 1 224 ? 22.55560  -52.00338 26.84900  1.000 175.38839 ? 225 LEU   A HG     1 
ATOM   3217 H HD11   . LEU   A 1 224 ? 23.29549  -54.17234 27.30238  1.000 183.70121 ? 225 LEU   A HD11   1 
ATOM   3218 H HD12   . LEU   A 1 224 ? 21.70772  -54.15916 27.25439  1.000 183.70121 ? 225 LEU   A HD12   1 
ATOM   3219 H HD13   . LEU   A 1 224 ? 22.53531  -54.70806 26.01451  1.000 183.70121 ? 225 LEU   A HD13   1 
ATOM   3220 H HD21   . LEU   A 1 224 ? 24.58397  -52.72951 25.87210  1.000 178.55405 ? 225 LEU   A HD21   1 
ATOM   3221 H HD22   . LEU   A 1 224 ? 23.78164  -53.01586 24.53128  1.000 178.55405 ? 225 LEU   A HD22   1 
ATOM   3222 H HD23   . LEU   A 1 224 ? 23.90416  -51.53081 25.08185  1.000 178.55405 ? 225 LEU   A HD23   1 
ATOM   3223 N N      . MET   A 1 225 ? 22.38632  -49.14212 25.05996  1.000 136.58944 ? 226 MET   A N      1 
ATOM   3224 C CA     . MET   A 1 225 ? 23.46080  -48.31791 24.51468  1.000 138.55903 ? 226 MET   A CA     1 
ATOM   3225 C C      . MET   A 1 225 ? 24.69236  -48.50071 25.39011  1.000 131.66230 ? 226 MET   A C      1 
ATOM   3226 O O      . MET   A 1 225 ? 24.63603  -48.26094 26.60016  1.000 159.30948 ? 226 MET   A O      1 
ATOM   3227 C CB     . MET   A 1 225 ? 23.05137  -46.84510 24.46105  1.000 134.34392 ? 226 MET   A CB     1 
ATOM   3228 C CG     . MET   A 1 225 ? 21.91957  -46.56053 23.49594  1.000 139.32120 ? 226 MET   A CG     1 
ATOM   3229 S SD     . MET   A 1 225 ? 21.48637  -44.81345 23.44017  1.000 141.06976 ? 226 MET   A SD     1 
ATOM   3230 C CE     . MET   A 1 225 ? 20.43021  -44.78836 21.99474  1.000 164.02597 ? 226 MET   A CE     1 
ATOM   3231 H H      . MET   A 1 225 ? 22.16965  -48.92382 25.86308  1.000 164.29780 ? 226 MET   A H      1 
ATOM   3232 H HA     . MET   A 1 225 ? 23.66171  -48.60433 23.60997  1.000 166.66131 ? 226 MET   A HA     1 
ATOM   3233 H HB2    . MET   A 1 225 ? 22.76286  -46.56941 25.34516  1.000 161.60318 ? 226 MET   A HB2    1 
ATOM   3234 H HB3    . MET   A 1 225 ? 23.81709  -46.31866 24.18278  1.000 161.60318 ? 226 MET   A HB3    1 
ATOM   3235 H HG2    . MET   A 1 225 ? 22.18683  -46.83329 22.60427  1.000 167.57591 ? 226 MET   A HG2    1 
ATOM   3236 H HG3    . MET   A 1 225 ? 21.13378  -47.05708 23.77321  1.000 167.57591 ? 226 MET   A HG3    1 
ATOM   3237 H HE1    . MET   A 1 225 ? 20.11490  -43.88257 21.84970  1.000 197.22163 ? 226 MET   A HE1    1 
ATOM   3238 H HE2    . MET   A 1 225 ? 20.93997  -45.08825 21.22590  1.000 197.22163 ? 226 MET   A HE2    1 
ATOM   3239 H HE3    . MET   A 1 225 ? 19.67688  -45.38097 22.14373  1.000 197.22163 ? 226 MET   A HE3    1 
ATOM   3240 N N      . ALA   A 1 226 ? 25.79796  -48.92878 24.78469  1.000 128.12697 ? 227 ALA   A N      1 
ATOM   3241 C CA     . ALA   A 1 226 ? 27.01942  -49.22116 25.52011  1.000 130.32835 ? 227 ALA   A CA     1 
ATOM   3242 C C      . ALA   A 1 226 ? 28.21236  -48.66703 24.75998  1.000 133.03813 ? 227 ALA   A C      1 
ATOM   3243 O O      . ALA   A 1 226 ? 28.23224  -48.68573 23.52706  1.000 163.12212 ? 227 ALA   A O      1 
ATOM   3244 C CB     . ALA   A 1 226 ? 27.18726  -50.72974 25.73586  1.000 137.80850 ? 227 ALA   A CB     1 
ATOM   3245 H H      . ALA   A 1 226 ? 25.86352  -49.05853 23.93707  1.000 151.80001 ? 227 ALA   A H      1 
ATOM   3246 H HA     . ALA   A 1 226 ? 26.99029  -48.78910 26.38808  1.000 154.61034 ? 227 ALA   A HA     1 
ATOM   3247 H HB1    . ALA   A 1 226 ? 28.00155  -50.88820 26.23857  1.000 165.76067 ? 227 ALA   A HB1    1 
ATOM   3248 H HB2    . ALA   A 1 226 ? 26.42290  -51.06506 26.23004  1.000 165.76067 ? 227 ALA   A HB2    1 
ATOM   3249 H HB3    . ALA   A 1 226 ? 27.24105  -51.16820 24.87228  1.000 165.76067 ? 227 ALA   A HB3    1 
ATOM   3250 N N      . ALA   A 1 227 ? 29.20790  -48.18177 25.50091  1.000 141.73120 ? 228 ALA   A N      1 
ATOM   3251 C CA     . ALA   A 1 227 ? 30.40194  -47.58926 24.91215  1.000 150.55242 ? 228 ALA   A CA     1 
ATOM   3252 C C      . ALA   A 1 227 ? 31.62840  -48.02333 25.69912  1.000 154.71288 ? 228 ALA   A C      1 
ATOM   3253 O O      . ALA   A 1 227 ? 31.66471  -47.87401 26.92365  1.000 188.61404 ? 228 ALA   A O      1 
ATOM   3254 C CB     . ALA   A 1 227 ? 30.30671  -46.05863 24.89593  1.000 146.99371 ? 228 ALA   A CB     1 
ATOM   3255 H H      . ALA   A 1 227 ? 29.21275  -48.18548 26.36089  1.000 170.46791 ? 228 ALA   A H      1 
ATOM   3256 H HA     . ALA   A 1 227 ? 30.49966  -47.90716 24.00094  1.000 181.05338 ? 228 ALA   A HA     1 
ATOM   3257 H HB1    . ALA   A 1 227 ? 31.08413  -45.69866 24.44102  1.000 176.78292 ? 228 ALA   A HB1    1 
ATOM   3258 H HB2    . ALA   A 1 227 ? 29.49871  -45.79744 24.42710  1.000 176.78292 ? 228 ALA   A HB2    1 
ATOM   3259 H HB3    . ALA   A 1 227 ? 30.27848  -45.73428 25.80966  1.000 176.78292 ? 228 ALA   A HB3    1 
ATOM   3260 N N      . HIS   A 1 228 ? 32.63019  -48.55125 24.99657  1.000 162.12072 ? 229 HIS   A N      1 
ATOM   3261 C CA     . HIS   A 1 228 ? 33.88534  -48.94913 25.63241  1.000 169.11860 ? 229 HIS   A CA     1 
ATOM   3262 C C      . HIS   A 1 228 ? 34.98293  -48.94843 24.58093  1.000 173.39237 ? 229 HIS   A C      1 
ATOM   3263 O O      . HIS   A 1 228 ? 34.88382  -49.67299 23.58537  1.000 167.38415 ? 229 HIS   A O      1 
ATOM   3264 C CB     . HIS   A 1 228 ? 33.76168  -50.32941 26.28227  1.000 173.75203 ? 229 HIS   A CB     1 
ATOM   3265 C CG     . HIS   A 1 228 ? 34.99980  -50.77409 26.99947  1.000 180.81813 ? 229 HIS   A CG     1 
ATOM   3266 N ND1    . HIS   A 1 228 ? 35.62231  -50.00451 27.95888  1.000 185.44757 ? 229 HIS   A ND1    1 
ATOM   3267 C CD2    . HIS   A 1 228 ? 35.72936  -51.91056 26.89832  1.000 181.05682 ? 229 HIS   A CD2    1 
ATOM   3268 C CE1    . HIS   A 1 228 ? 36.68227  -50.64675 28.41642  1.000 194.86915 ? 229 HIS   A CE1    1 
ATOM   3269 N NE2    . HIS   A 1 228 ? 36.76967  -51.80597 27.78951  1.000 187.73315 ? 229 HIS   A NE2    1 
ATOM   3270 H H      . HIS   A 1 228 ? 32.60779  -48.68968 24.14808  1.000 194.93534 ? 229 HIS   A H      1 
ATOM   3271 H HA     . HIS   A 1 228 ? 34.11306  -48.30371 26.31979  1.000 203.33279 ? 229 HIS   A HA     1 
ATOM   3272 H HB2    . HIS   A 1 228 ? 33.03816  -50.30611 26.92793  1.000 208.89290 ? 229 HIS   A HB2    1 
ATOM   3273 H HB3    . HIS   A 1 228 ? 33.56916  -50.98281 25.59169  1.000 208.89290 ? 229 HIS   A HB3    1 
ATOM   3274 H HD2    . HIS   A 1 228 ? 35.55814  -52.62773 26.33153  1.000 217.65866 ? 229 HIS   A HD2    1 
ATOM   3275 H HE1    . HIS   A 1 228 ? 37.26735  -50.33556 29.06891  1.000 234.23345 ? 229 HIS   A HE1    1 
ATOM   3276 N N      . GLN   A 1 229 ? 36.02314  -48.14096 24.80061  1.000 186.39309 ? 230 GLN   A N      1 
ATOM   3277 C CA     . GLN   A 1 229 ? 37.17809  -48.07051 23.90431  1.000 178.32470 ? 230 GLN   A CA     1 
ATOM   3278 C C      . GLN   A 1 229 ? 36.79354  -47.50391 22.53887  1.000 184.86476 ? 230 GLN   A C      1 
ATOM   3279 O O      . GLN   A 1 229 ? 37.23380  -47.99999 21.50104  1.000 204.39695 ? 230 GLN   A O      1 
ATOM   3280 C CB     . GLN   A 1 229 ? 37.84058  -49.44118 23.74430  1.000 181.92609 ? 230 GLN   A CB     1 
ATOM   3281 C CG     . GLN   A 1 229 ? 38.38525  -50.02645 25.03203  1.000 197.88151 ? 230 GLN   A CG     1 
ATOM   3282 C CD     . GLN   A 1 229 ? 38.93117  -51.42743 24.84271  1.000 202.35959 ? 230 GLN   A CD     1 
ATOM   3283 O OE1    . GLN   A 1 229 ? 38.27658  -52.28649 24.25059  1.000 198.68166 ? 230 GLN   A OE1    1 
ATOM   3284 N NE2    . GLN   A 1 229 ? 40.14089  -51.66304 25.33722  1.000 213.58326 ? 230 GLN   A NE2    1 
ATOM   3285 H H      . GLN   A 1 229 ? 36.08394  -47.61314 25.47686  1.000 224.06218 ? 230 GLN   A H      1 
ATOM   3286 H HA     . GLN   A 1 229 ? 37.82645  -47.46488 24.29641  1.000 214.38011 ? 230 GLN   A HA     1 
ATOM   3287 H HB2    . GLN   A 1 229 ? 37.18399  -50.06321 23.39376  1.000 218.70178 ? 230 GLN   A HB2    1 
ATOM   3288 H HB3    . GLN   A 1 229 ? 38.58145  -49.35628 23.12398  1.000 218.70178 ? 230 GLN   A HB3    1 
ATOM   3289 H HG2    . GLN   A 1 229 ? 39.10517  -49.46357 25.35726  1.000 237.84828 ? 230 GLN   A HG2    1 
ATOM   3290 H HG3    . GLN   A 1 229 ? 37.67279  -50.06656 25.68906  1.000 237.84828 ? 230 GLN   A HG3    1 
ATOM   3291 H HE21   . GLN   A 1 229 ? 40.57066  -51.03600 25.73935  1.000 256.69039 ? 230 GLN   A HE21   1 
ATOM   3292 H HE22   . GLN   A 1 229 ? 40.49454  -52.44267 25.25534  1.000 256.69039 ? 230 GLN   A HE22   1 
ATOM   3293 N N      . GLY   A 1 230 ? 35.97290  -46.45631 22.53631  1.000 189.33169 ? 231 GLY   A N      1 
ATOM   3294 C CA     . GLY   A 1 230 ? 35.54710  -45.83655 21.29993  1.000 190.68379 ? 231 GLY   A CA     1 
ATOM   3295 C C      . GLY   A 1 230 ? 34.63961  -46.67934 20.43399  1.000 168.28585 ? 231 GLY   A C      1 
ATOM   3296 O O      . GLY   A 1 230 ? 34.30120  -46.25197 19.32358  1.000 149.70906 ? 231 GLY   A O      1 
ATOM   3297 H H      . GLY   A 1 230 ? 35.65098  -46.08909 23.24420  1.000 227.58850 ? 231 GLY   A H      1 
ATOM   3298 H HA2    . GLY   A 1 230 ? 35.07308  -45.01739 21.51246  1.000 229.21102 ? 231 GLY   A HA2    1 
ATOM   3299 H HA3    . GLY   A 1 230 ? 36.33426  -45.61918 20.77645  1.000 229.21102 ? 231 GLY   A HA3    1 
ATOM   3300 N N      . ASN   A 1 231 ? 34.24336  -47.86325 20.89501  1.000 166.93367 ? 232 ASN   A N      1 
ATOM   3301 C CA     . ASN   A 1 231 ? 33.28627  -48.70994 20.19096  1.000 153.54286 ? 232 ASN   A CA     1 
ATOM   3302 C C      . ASN   A 1 231 ? 31.94028  -48.59540 20.89171  1.000 144.18022 ? 232 ASN   A C      1 
ATOM   3303 O O      . ASN   A 1 231 ? 31.79279  -49.03485 22.03568  1.000 146.41768 ? 232 ASN   A O      1 
ATOM   3304 C CB     . ASN   A 1 231 ? 33.74705  -50.16342 20.16977  1.000 154.88804 ? 232 ASN   A CB     1 
ATOM   3305 C CG     . ASN   A 1 231 ? 35.04597  -50.35370 19.42372  1.000 162.67621 ? 232 ASN   A CG     1 
ATOM   3306 O OD1    . ASN   A 1 231 ? 35.38049  -49.58163 18.52550  1.000 154.66299 ? 232 ASN   A OD1    1 
ATOM   3307 N ND2    . ASN   A 1 231 ? 35.78849  -51.38977 19.79030  1.000 170.66654 ? 232 ASN   A ND2    1 
ATOM   3308 H H      . ASN   A 1 231 ? 34.52281  -48.20549 21.63283  1.000 200.71088 ? 232 ASN   A H      1 
ATOM   3309 H HA     . ASN   A 1 231 ? 33.20153  -48.39732 19.27664  1.000 184.64190 ? 232 ASN   A HA     1 
ATOM   3310 H HB2    . ASN   A 1 231 ? 33.87777  -50.46690 21.08176  1.000 186.25612 ? 232 ASN   A HB2    1 
ATOM   3311 H HB3    . ASN   A 1 231 ? 33.06918  -50.70359 19.73432  1.000 186.25612 ? 232 ASN   A HB3    1 
ATOM   3312 H HD21   . ASN   A 1 231 ? 36.53773  -51.54253 19.39673  1.000 205.19032 ? 232 ASN   A HD21   1 
ATOM   3313 H HD22   . ASN   A 1 231 ? 35.52069  -51.90881 20.42156  1.000 205.19032 ? 232 ASN   A HD22   1 
ATOM   3314 N N      . LEU   A 1 232 ? 30.95949  -48.01850 20.20768  1.000 145.02654 ? 233 LEU   A N      1 
ATOM   3315 C CA     . LEU   A 1 232 ? 29.62368  -47.85389 20.76029  1.000 140.11847 ? 233 LEU   A CA     1 
ATOM   3316 C C      . LEU   A 1 232 ? 28.68458  -48.89903 20.17533  1.000 136.57558 ? 233 LEU   A C      1 
ATOM   3317 O O      . LEU   A 1 232 ? 28.73996  -49.20031 18.97943  1.000 151.43783 ? 233 LEU   A O      1 
ATOM   3318 C CB     . LEU   A 1 232 ? 29.07855  -46.45320 20.47502  1.000 150.97208 ? 233 LEU   A CB     1 
ATOM   3319 C CG     . LEU   A 1 232 ? 29.42722  -45.33594 21.46169  1.000 150.10339 ? 233 LEU   A CG     1 
ATOM   3320 C CD1    . LEU   A 1 232 ? 30.92811  -45.09673 21.51287  1.000 143.99237 ? 233 LEU   A CD1    1 
ATOM   3321 C CD2    . LEU   A 1 232 ? 28.68713  -44.04812 21.10954  1.000 128.99448 ? 233 LEU   A CD2    1 
ATOM   3322 H H      . LEU   A 1 232 ? 31.04597  -47.71014 19.40954  1.000 174.42232 ? 233 LEU   A H      1 
ATOM   3323 H HA     . LEU   A 1 232 ? 29.65951  -47.97554 21.72196  1.000 168.53264 ? 233 LEU   A HA     1 
ATOM   3324 H HB2    . LEU   A 1 232 ? 29.41571  -46.17603 19.60876  1.000 181.55697 ? 233 LEU   A HB2    1 
ATOM   3325 H HB3    . LEU   A 1 232 ? 28.11066  -46.51242 20.45085  1.000 181.55697 ? 233 LEU   A HB3    1 
ATOM   3326 H HG     . LEU   A 1 232 ? 29.14312  -45.61126 22.34735  1.000 180.51454 ? 233 LEU   A HG     1 
ATOM   3327 H HD11   . LEU   A 1 232 ? 31.10952  -44.35550 22.11168  1.000 173.18131 ? 233 LEU   A HD11   1 
ATOM   3328 H HD12   . LEU   A 1 232 ? 31.36491  -45.89937 21.83825  1.000 173.18131 ? 233 LEU   A HD12   1 
ATOM   3329 H HD13   . LEU   A 1 232 ? 31.24496  -44.88627 20.62056  1.000 173.18131 ? 233 LEU   A HD13   1 
ATOM   3330 H HD21   . LEU   A 1 232 ? 28.82011  -43.40273 21.82135  1.000 154.33885 ? 233 LEU   A HD21   1 
ATOM   3331 H HD22   . LEU   A 1 232 ? 29.03997  -43.69889 20.27621  1.000 154.33885 ? 233 LEU   A HD22   1 
ATOM   3332 H HD23   . LEU   A 1 232 ? 27.74198  -44.24349 21.01250  1.000 154.33885 ? 233 LEU   A HD23   1 
ATOM   3333 N N      . LEU   A 1 233 ? 27.82419  -49.44942 21.02655  1.000 134.30808 ? 234 LEU   A N      1 
ATOM   3334 C CA     . LEU   A 1 233 ? 26.80743  -50.40603 20.61633  1.000 140.32594 ? 234 LEU   A CA     1 
ATOM   3335 C C      . LEU   A 1 233 ? 25.43005  -49.84095 20.92728  1.000 137.66747 ? 234 LEU   A C      1 
ATOM   3336 O O      . LEU   A 1 233 ? 25.24068  -49.16062 21.93932  1.000 155.32370 ? 234 LEU   A O      1 
ATOM   3337 C CB     . LEU   A 1 233 ? 26.99043  -51.75432 21.32046  1.000 126.76370 ? 234 LEU   A CB     1 
ATOM   3338 C CG     . LEU   A 1 233 ? 25.96289  -52.82597 20.94807  1.000 132.26418 ? 234 LEU   A CG     1 
ATOM   3339 C CD1    . LEU   A 1 233 ? 26.58895  -54.21168 21.02174  1.000 120.88765 ? 234 LEU   A CD1    1 
ATOM   3340 C CD2    . LEU   A 1 233 ? 24.72640  -52.76129 21.83654  1.000 145.96087 ? 234 LEU   A CD2    1 
ATOM   3341 H H      . LEU   A 1 233 ? 27.81138  -49.27816 21.86923  1.000 161.56017 ? 234 LEU   A H      1 
ATOM   3342 H HA     . LEU   A 1 233 ? 26.87093  -50.55790 19.66040  1.000 168.78159 ? 234 LEU   A HA     1 
ATOM   3343 H HB2    . LEU   A 1 233 ? 27.86764  -52.10105 21.09420  1.000 152.50691 ? 234 LEU   A HB2    1 
ATOM   3344 H HB3    . LEU   A 1 233 ? 26.92727  -51.61064 22.27768  1.000 152.50691 ? 234 LEU   A HB3    1 
ATOM   3345 H HG     . LEU   A 1 233 ? 25.67418  -52.65925 20.03716  1.000 159.10748 ? 234 LEU   A HG     1 
ATOM   3346 H HD11   . LEU   A 1 233 ? 25.91554  -54.87452 20.80248  1.000 143.11283 ? 234 LEU   A HD11   1 
ATOM   3347 H HD12   . LEU   A 1 233 ? 27.32107  -54.26157 20.38739  1.000 143.11283 ? 234 LEU   A HD12   1 
ATOM   3348 H HD13   . LEU   A 1 233 ? 26.91983  -54.36131 21.92120  1.000 143.11283 ? 234 LEU   A HD13   1 
ATOM   3349 H HD21   . LEU   A 1 233 ? 24.29238  -53.62878 21.83735  1.000 175.54352 ? 234 LEU   A HD21   1 
ATOM   3350 H HD22   . LEU   A 1 233 ? 24.99709  -52.52601 22.73780  1.000 175.54352 ? 234 LEU   A HD22   1 
ATOM   3351 H HD23   . LEU   A 1 233 ? 24.12105  -52.08888 21.48680  1.000 175.54352 ? 234 LEU   A HD23   1 
ATOM   3352 N N      . PHE   A 1 234 ? 24.47371  -50.12477 20.04993  1.000 119.22022 ? 235 PHE   A N      1 
ATOM   3353 C CA     . PHE   A 1 234 ? 23.09776  -49.68721 20.21973  1.000 120.84011 ? 235 PHE   A CA     1 
ATOM   3354 C C      . PHE   A 1 234 ? 22.19202  -50.81505 19.75612  1.000 118.28078 ? 235 PHE   A C      1 
ATOM   3355 O O      . PHE   A 1 234 ? 22.56369  -51.59720 18.87938  1.000 132.92790 ? 235 PHE   A O      1 
ATOM   3356 C CB     . PHE   A 1 234 ? 22.81695  -48.41047 19.42825  1.000 128.43273 ? 235 PHE   A CB     1 
ATOM   3357 C CG     . PHE   A 1 234 ? 23.96814  -47.44961 19.40099  1.000 142.52519 ? 235 PHE   A CG     1 
ATOM   3358 C CD1    . PHE   A 1 234 ? 24.99810  -47.61414 18.49108  1.000 149.37091 ? 235 PHE   A CD1    1 
ATOM   3359 C CD2    . PHE   A 1 234 ? 24.01694  -46.37705 20.27535  1.000 148.45189 ? 235 PHE   A CD2    1 
ATOM   3360 C CE1    . PHE   A 1 234 ? 26.05329  -46.73350 18.45879  1.000 157.15177 ? 235 PHE   A CE1    1 
ATOM   3361 C CE2    . PHE   A 1 234 ? 25.07196  -45.49193 20.24441  1.000 146.18779 ? 235 PHE   A CE2    1 
ATOM   3362 C CZ     . PHE   A 1 234 ? 26.08434  -45.66704 19.33137  1.000 156.71251 ? 235 PHE   A CZ     1 
ATOM   3363 H H      . PHE   A 1 234 ? 24.60213  -50.58037 19.33192  1.000 142.55708 ? 235 PHE   A H      1 
ATOM   3364 H HA     . PHE   A 1 234 ? 22.90739  -49.49804 21.15186  1.000 145.39860 ? 235 PHE   A HA     1 
ATOM   3365 H HB2    . PHE   A 1 234 ? 22.61065  -48.65109 18.51149  1.000 154.50974 ? 235 PHE   A HB2    1 
ATOM   3366 H HB3    . PHE   A 1 234 ? 22.06067  -47.95477 19.82985  1.000 154.50974 ? 235 PHE   A HB3    1 
ATOM   3367 H HD1    . PHE   A 1 234 ? 24.97610  -48.32791 17.89530  1.000 179.63557 ? 235 PHE   A HD1    1 
ATOM   3368 H HD2    . PHE   A 1 234 ? 23.33015  -46.25294 20.89002  1.000 178.53274 ? 235 PHE   A HD2    1 
ATOM   3369 H HE1    . PHE   A 1 234 ? 26.74481  -46.85713 17.84936  1.000 188.97259 ? 235 PHE   A HE1    1 
ATOM   3370 H HE2    . PHE   A 1 234 ? 25.09919  -44.77788 20.83963  1.000 175.81582 ? 235 PHE   A HE2    1 
ATOM   3371 H HZ     . PHE   A 1 234 ? 26.79207  -45.06440 19.30228  1.000 188.44548 ? 235 PHE   A HZ     1 
ATOM   3372 N N      . ALA   A 1 235 ? 21.00516  -50.90731 20.35060  1.000 125.12572 ? 236 ALA   A N      1 
ATOM   3373 C CA     . ALA   A 1 235 ? 20.13894  -52.03643 20.04647  1.000 128.14519 ? 236 ALA   A CA     1 
ATOM   3374 C C      . ALA   A 1 235 ? 18.68847  -51.70892 20.36468  1.000 124.79615 ? 236 ALA   A C      1 
ATOM   3375 O O      . ALA   A 1 235 ? 18.39249  -51.08154 21.38417  1.000 133.35007 ? 236 ALA   A O      1 
ATOM   3376 C CB     . ALA   A 1 235 ? 20.57619  -53.28307 20.82790  1.000 121.72730 ? 236 ALA   A CB     1 
ATOM   3377 H H      . ALA   A 1 235 ? 20.68957  -50.34317 20.91784  1.000 150.54134 ? 236 ALA   A H      1 
ATOM   3378 H HA     . ALA   A 1 235 ? 20.18817  -52.21214 19.09379  1.000 154.16470 ? 236 ALA   A HA     1 
ATOM   3379 H HB1    . ALA   A 1 235 ? 19.98675  -54.01979 20.60271  1.000 146.46322 ? 236 ALA   A HB1    1 
ATOM   3380 H HB2    . ALA   A 1 235 ? 21.48906  -53.50378 20.58531  1.000 146.46322 ? 236 ALA   A HB2    1 
ATOM   3381 H HB3    . ALA   A 1 235 ? 20.52264  -53.09513 21.77801  1.000 146.46322 ? 236 ALA   A HB3    1 
ATOM   3382 N N      . ASN   A 1 236 ? 17.79788  -52.14625 19.48015  1.000 116.06431 ? 237 ASN   A N      1 
ATOM   3383 C CA     . ASN   A 1 236 ? 16.35319  -52.12516 19.71118  1.000 112.70481 ? 237 ASN   A CA     1 
ATOM   3384 C C      . ASN   A 1 236 ? 15.86301  -53.56662 19.72127  1.000 112.28870 ? 237 ASN   A C      1 
ATOM   3385 O O      . ASN   A 1 236 ? 15.79637  -54.19971 18.65021  1.000 121.88622 ? 237 ASN   A O      1 
ATOM   3386 C CB     . ASN   A 1 236 ? 15.63514  -51.31878 18.62946  1.000 111.05775 ? 237 ASN   A CB     1 
ATOM   3387 C CG     . ASN   A 1 236 ? 14.12774  -51.27121 18.83267  1.000 112.36500 ? 237 ASN   A CG     1 
ATOM   3388 O OD1    . ASN   A 1 236 ? 13.55110  -52.11132 19.52299  1.000 120.34612 ? 237 ASN   A OD1    1 
ATOM   3389 N ND2    . ASN   A 1 236 ? 13.48165  -50.28687 18.21824  1.000 117.92814 ? 237 ASN   A ND2    1 
ATOM   3390 H H      . ASN   A 1 236 ? 18.01065  -52.47095 18.71275  1.000 139.66764 ? 237 ASN   A H      1 
ATOM   3391 H HA     . ASN   A 1 236 ? 16.15536  -51.70704 20.56379  1.000 133.29342 ? 237 ASN   A HA     1 
ATOM   3392 H HB2    . ASN   A 1 236 ? 15.96811  -50.40780 18.64108  1.000 131.31695 ? 237 ASN   A HB2    1 
ATOM   3393 H HB3    . ASN   A 1 236 ? 15.80853  -51.72439 17.76556  1.000 131.31695 ? 237 ASN   A HB3    1 
ATOM   3394 H HD21   . ASN   A 1 236 ? 12.62862  -50.21516 18.30064  1.000 141.90423 ? 237 ASN   A HD21   1 
ATOM   3395 H HD22   . ASN   A 1 236 ? 13.91632  -49.72118 17.73797  1.000 141.90423 ? 237 ASN   A HD22   1 
ATOM   3396 N N      . PRO   A 1 237 ? 15.50643  -54.13489 20.87754  1.000 121.96821 ? 238 PRO   A N      1 
ATOM   3397 C CA     . PRO   A 1 237 ? 15.15210  -55.56296 20.90619  1.000 127.15244 ? 238 PRO   A CA     1 
ATOM   3398 C C      . PRO   A 1 237 ? 13.85859  -55.89526 20.18546  1.000 130.08036 ? 238 PRO   A C      1 
ATOM   3399 O O      . PRO   A 1 237 ? 13.65683  -57.06325 19.83032  1.000 127.47670 ? 238 PRO   A O      1 
ATOM   3400 C CB     . PRO   A 1 237 ? 15.04065  -55.86583 22.40715  1.000 115.53026 ? 238 PRO   A CB     1 
ATOM   3401 C CG     . PRO   A 1 237 ? 14.66559  -54.56029 23.01687  1.000 133.07258 ? 238 PRO   A CG     1 
ATOM   3402 C CD     . PRO   A 1 237 ? 15.38555  -53.51226 22.20892  1.000 138.28648 ? 238 PRO   A CD     1 
ATOM   3403 H HA     . PRO   A 1 237 ? 15.87195  -56.08627 20.52037  1.000 152.97340 ? 238 PRO   A HA     1 
ATOM   3404 H HB2    . PRO   A 1 237 ? 14.35513  -56.53433 22.56227  1.000 137.93204 ? 238 PRO   A HB2    1 
ATOM   3405 H HB3    . PRO   A 1 237 ? 15.89294  -56.17932 22.74808  1.000 137.93204 ? 238 PRO   A HB3    1 
ATOM   3406 H HG2    . PRO   A 1 237 ? 13.70499  -54.43697 22.96270  1.000 160.07757 ? 238 PRO   A HG2    1 
ATOM   3407 H HG3    . PRO   A 1 237 ? 14.95132  -54.53700 23.94354  1.000 160.07757 ? 238 PRO   A HG3    1 
ATOM   3408 H HD2    . PRO   A 1 237 ? 14.86542  -52.69485 22.16191  1.000 166.33424 ? 238 PRO   A HD2    1 
ATOM   3409 H HD3    . PRO   A 1 237 ? 16.26062  -53.32754 22.58446  1.000 166.33424 ? 238 PRO   A HD3    1 
ATOM   3410 N N      . ASN   A 1 238 ? 12.97611  -54.91984 19.95546  1.000 123.98581 ? 239 ASN   A N      1 
ATOM   3411 C CA     . ASN   A 1 238 ? 11.65288  -55.17363 19.38238  1.000 131.23475 ? 239 ASN   A CA     1 
ATOM   3412 C C      . ASN   A 1 238 ? 11.39937  -54.17123 18.25966  1.000 130.42671 ? 239 ASN   A C      1 
ATOM   3413 O O      . ASN   A 1 238 ? 10.76587  -53.13206 18.46179  1.000 116.12899 ? 239 ASN   A O      1 
ATOM   3414 C CB     . ASN   A 1 238 ? 10.57676  -55.09986 20.46354  1.000 136.89651 ? 239 ASN   A CB     1 
ATOM   3415 C CG     . ASN   A 1 238 ? 9.18667   -55.36417 19.92226  1.000 133.60150 ? 239 ASN   A CG     1 
ATOM   3416 O OD1    . ASN   A 1 238 ? 9.02449   -55.93180 18.84085  1.000 110.44717 ? 239 ASN   A OD1    1 
ATOM   3417 N ND2    . ASN   A 1 238 ? 8.17248   -54.95369 20.67517  1.000 127.58238 ? 239 ASN   A ND2    1 
ATOM   3418 H H      . ASN   A 1 238 ? 13.12466  -54.09018 20.12632  1.000 149.17344 ? 239 ASN   A H      1 
ATOM   3419 H HA     . ASN   A 1 238 ? 11.65015  -56.06052 18.98953  1.000 157.87217 ? 239 ASN   A HA     1 
ATOM   3420 H HB2    . ASN   A 1 238 ? 10.76561  -55.76488 21.14397  1.000 164.66629 ? 239 ASN   A HB2    1 
ATOM   3421 H HB3    . ASN   A 1 238 ? 10.58265  -54.21279 20.85595  1.000 164.66629 ? 239 ASN   A HB3    1 
ATOM   3422 H HD21   . ASN   A 1 238 ? 7.36334   -55.07994 20.41259  1.000 153.48932 ? 239 ASN   A HD21   1 
ATOM   3423 H HD22   . ASN   A 1 238 ? 8.32492   -54.56163 21.42527  1.000 153.48932 ? 239 ASN   A HD22   1 
ATOM   3424 N N      . ASN   A 1 239 ? 11.90115  -54.49357 17.07046  1.000 129.92326 ? 240 ASN   A N      1 
ATOM   3425 C CA     . ASN   A 1 239 ? 11.59774  -53.75675 15.84725  1.000 119.22803 ? 240 ASN   A CA     1 
ATOM   3426 C C      . ASN   A 1 239 ? 10.71900  -54.66678 14.99209  1.000 125.99064 ? 240 ASN   A C      1 
ATOM   3427 O O      . ASN   A 1 239 ? 11.19102  -55.34617 14.07930  1.000 119.89643 ? 240 ASN   A O      1 
ATOM   3428 C CB     . ASN   A 1 239 ? 12.87031  -53.34317 15.11180  1.000 113.71222 ? 240 ASN   A CB     1 
ATOM   3429 C CG     . ASN   A 1 239 ? 12.58205  -52.52955 13.86574  1.000 120.02600 ? 240 ASN   A CG     1 
ATOM   3430 O OD1    . ASN   A 1 239 ? 11.45910  -52.06839 13.65863  1.000 116.07847 ? 240 ASN   A OD1    1 
ATOM   3431 N ND2    . ASN   A 1 239 ? 13.59802  -52.34425 13.03022  1.000 130.74285 ? 240 ASN   A ND2    1 
ATOM   3432 H H      . ASN   A 1 239 ? 12.43577  -55.15519 16.94383  1.000 156.29839 ? 240 ASN   A H      1 
ATOM   3433 H HA     . ASN   A 1 239 ? 11.11260  -52.94654 16.06887  1.000 143.46410 ? 240 ASN   A HA     1 
ATOM   3434 H HB2    . ASN   A 1 239 ? 13.41743  -52.80356 15.70372  1.000 136.84513 ? 240 ASN   A HB2    1 
ATOM   3435 H HB3    . ASN   A 1 239 ? 13.35571  -54.13967 14.84558  1.000 136.84513 ? 240 ASN   A HB3    1 
ATOM   3436 H HD21   . ASN   A 1 239 ? 13.48439  -51.88934 12.30929  1.000 157.28189 ? 240 ASN   A HD21   1 
ATOM   3437 H HD22   . ASN   A 1 239 ? 14.36939  -52.67918 13.21025  1.000 157.28189 ? 240 ASN   A HD22   1 
ATOM   3438 N N      . ASN   A 1 240 ? 9.42341   -54.68214 15.30517  1.000 126.53470 ? 241 ASN   A N      1 
ATOM   3439 C CA     . ASN   A 1 240 ? 8.46687   -55.56476 14.63893  1.000 116.02779 ? 241 ASN   A CA     1 
ATOM   3440 C C      . ASN   A 1 240 ? 8.91350   -57.02288 14.74453  1.000 128.30975 ? 241 ASN   A C      1 
ATOM   3441 O O      . ASN   A 1 240 ? 9.00939   -57.74623 13.75018  1.000 118.87545 ? 241 ASN   A O      1 
ATOM   3442 C CB     . ASN   A 1 240 ? 8.26311   -55.15373 13.17814  1.000 115.01984 ? 241 ASN   A CB     1 
ATOM   3443 C CG     . ASN   A 1 240 ? 7.26047   -54.02261 13.02368  1.000 122.47338 ? 241 ASN   A CG     1 
ATOM   3444 O OD1    . ASN   A 1 240 ? 6.86987   -53.38449 14.00181  1.000 137.69925 ? 241 ASN   A OD1    1 
ATOM   3445 N ND2    . ASN   A 1 240 ? 6.83865   -53.77001 11.78915  1.000 135.48135 ? 241 ASN   A ND2    1 
ATOM   3446 H H      . ASN   A 1 240 ? 9.06924   -54.18290 15.90926  1.000 152.23212 ? 241 ASN   A H      1 
ATOM   3447 H HA     . ASN   A 1 240 ? 7.61041   -55.48691 15.08761  1.000 139.62382 ? 241 ASN   A HA     1 
ATOM   3448 H HB2    . ASN   A 1 240 ? 9.11056   -54.85623 12.81178  1.000 138.41427 ? 241 ASN   A HB2    1 
ATOM   3449 H HB3    . ASN   A 1 240 ? 7.93477   -55.91682 12.67736  1.000 138.41427 ? 241 ASN   A HB3    1 
ATOM   3450 H HD21   . ASN   A 1 240 ? 6.27083   -53.13943 11.64934  1.000 162.96809 ? 241 ASN   A HD21   1 
ATOM   3451 H HD22   . ASN   A 1 240 ? 7.13347   -54.23712 11.12999  1.000 162.96809 ? 241 ASN   A HD22   1 
ATOM   3452 N N      . GLY   A 1 241 ? 9.19847   -57.45232 15.97445  1.000 138.48013 ? 242 GLY   A N      1 
ATOM   3453 C CA     . GLY   A 1 241 ? 9.53810   -58.82687 16.25585  1.000 142.93550 ? 242 GLY   A CA     1 
ATOM   3454 C C      . GLY   A 1 241 ? 11.00062  -59.18305 16.08889  1.000 130.39229 ? 242 GLY   A C      1 
ATOM   3455 O O      . GLY   A 1 241 ? 11.42443  -60.23682 16.57517  1.000 130.54829 ? 242 GLY   A O      1 
ATOM   3456 H H      . GLY   A 1 241 ? 9.19904   -56.94772 16.67085  1.000 166.56663 ? 242 GLY   A H      1 
ATOM   3457 H HA2    . GLY   A 1 241 ? 9.29114   -59.02390 17.17295  1.000 171.91307 ? 242 GLY   A HA2    1 
ATOM   3458 H HA3    . GLY   A 1 241 ? 9.02736   -59.39851 15.66148  1.000 171.91307 ? 242 GLY   A HA3    1 
ATOM   3459 N N      . ALA   A 1 242 ? 11.77997  -58.34460 15.41486  1.000 125.81387 ? 243 ALA   A N      1 
ATOM   3460 C CA     . ALA   A 1 242 ? 13.19982  -58.58121 15.21458  1.000 106.32010 ? 243 ALA   A CA     1 
ATOM   3461 C C      . ALA   A 1 242 ? 14.00747  -57.57999 16.02685  1.000 111.08632 ? 243 ALA   A C      1 
ATOM   3462 O O      . ALA   A 1 242 ? 13.53571  -56.48266 16.33796  1.000 120.96564 ? 243 ALA   A O      1 
ATOM   3463 C CB     . ALA   A 1 242 ? 13.57371  -58.46887 13.73506  1.000 130.04069 ? 243 ALA   A CB     1 
ATOM   3464 H H      . ALA   A 1 242 ? 11.49983  -57.61478 15.05641  1.000 151.36711 ? 243 ALA   A H      1 
ATOM   3465 H HA     . ALA   A 1 242 ? 13.42668  -59.47531 15.51462  1.000 126.44134 ? 243 ALA   A HA     1 
ATOM   3466 H HB1    . ALA   A 1 242 ? 14.52605  -58.62502 13.63726  1.000 156.43930 ? 243 ALA   A HB1    1 
ATOM   3467 H HB2    . ALA   A 1 242 ? 13.07632  -59.13277 13.23234  1.000 156.43930 ? 243 ALA   A HB2    1 
ATOM   3468 H HB3    . ALA   A 1 242 ? 13.35027  -57.57925 13.41953  1.000 156.43930 ? 243 ALA   A HB3    1 
ATOM   3469 N N      . LEU   A 1 243 ? 15.23015  -57.96820 16.36950  1.000 107.89623 ? 244 LEU   A N      1 
ATOM   3470 C CA     . LEU   A 1 243 ? 16.15281  -57.09705 17.08176  1.000 108.90164 ? 244 LEU   A CA     1 
ATOM   3471 C C      . LEU   A 1 243 ? 17.07976  -56.44284 16.06941  1.000 109.47690 ? 244 LEU   A C      1 
ATOM   3472 O O      . LEU   A 1 243 ? 17.77485  -57.13764 15.31975  1.000 116.29977 ? 244 LEU   A O      1 
ATOM   3473 C CB     . LEU   A 1 243 ? 16.96387  -57.87100 18.11914  1.000 119.69367 ? 244 LEU   A CB     1 
ATOM   3474 C CG     . LEU   A 1 243 ? 17.93348  -57.03297 18.96077  1.000 129.77872 ? 244 LEU   A CG     1 
ATOM   3475 C CD1    . LEU   A 1 243 ? 18.15541  -57.69628 20.31461  1.000 113.80400 ? 244 LEU   A CD1    1 
ATOM   3476 C CD2    . LEU   A 1 243 ? 19.27196  -56.80864 18.25400  1.000 122.26301 ? 244 LEU   A CD2    1 
ATOM   3477 H H      . LEU   A 1 243 ? 15.55283  -58.74639 16.19657  1.000 127.52312 ? 244 LEU   A H      1 
ATOM   3478 H HA     . LEU   A 1 243 ? 15.65014  -56.40955 17.54606  1.000 128.72961 ? 244 LEU   A HA     1 
ATOM   3479 H HB2    . LEU   A 1 243 ? 16.34506  -58.29879 18.73148  1.000 144.02287 ? 244 LEU   A HB2    1 
ATOM   3480 H HB3    . LEU   A 1 243 ? 17.48909  -58.54196 17.65562  1.000 144.02287 ? 244 LEU   A HB3    1 
ATOM   3481 H HG     . LEU   A 1 243 ? 17.53647  -56.15802 19.09394  1.000 156.12494 ? 244 LEU   A HG     1 
ATOM   3482 H HD11   . LEU   A 1 243 ? 18.68646  -57.10628 20.87209  1.000 136.95527 ? 244 LEU   A HD11   1 
ATOM   3483 H HD12   . LEU   A 1 243 ? 17.29477  -57.85919 20.73133  1.000 136.95527 ? 244 LEU   A HD12   1 
ATOM   3484 H HD13   . LEU   A 1 243 ? 18.62297  -58.53576 20.18213  1.000 136.95527 ? 244 LEU   A HD13   1 
ATOM   3485 H HD21   . LEU   A 1 243 ? 19.94133  -56.56922 18.91393  1.000 147.10608 ? 244 LEU   A HD21   1 
ATOM   3486 H HD22   . LEU   A 1 243 ? 19.53120  -57.62659 17.80161  1.000 147.10608 ? 244 LEU   A HD22   1 
ATOM   3487 H HD23   . LEU   A 1 243 ? 19.17208  -56.09122 17.60884  1.000 147.10608 ? 244 LEU   A HD23   1 
ATOM   3488 N N      . HIS   A 1 244 ? 17.09012  -55.11491 16.05219  1.000 117.09978 ? 245 HIS   A N      1 
ATOM   3489 C CA     . HIS   A 1 244 ? 18.01716  -54.34651 15.23709  1.000 115.88548 ? 245 HIS   A CA     1 
ATOM   3490 C C      . HIS   A 1 244 ? 19.05047  -53.69715 16.14354  1.000 115.37010 ? 245 HIS   A C      1 
ATOM   3491 O O      . HIS   A 1 244 ? 18.69347  -53.03510 17.12376  1.000 119.28493 ? 245 HIS   A O      1 
ATOM   3492 C CB     . HIS   A 1 244 ? 17.29818  -53.27243 14.42352  1.000 113.04428 ? 245 HIS   A CB     1 
ATOM   3493 C CG     . HIS   A 1 244 ? 18.21464  -52.48407 13.54290  1.000 108.87278 ? 245 HIS   A CG     1 
ATOM   3494 N ND1    . HIS   A 1 244 ? 18.90083  -53.05132 12.49170  1.000 109.07917 ? 245 HIS   A ND1    1 
ATOM   3495 C CD2    . HIS   A 1 244 ? 18.57869  -51.18079 13.57021  1.000 109.72486 ? 245 HIS   A CD2    1 
ATOM   3496 C CE1    . HIS   A 1 244 ? 19.63595  -52.12775 11.89954  1.000 110.34341 ? 245 HIS   A CE1    1 
ATOM   3497 N NE2    . HIS   A 1 244 ? 19.45736  -50.98323 12.53334  1.000 105.74371 ? 245 HIS   A NE2    1 
ATOM   3498 H H      . HIS   A 1 244 ? 16.55555  -54.62678 16.51649  1.000 140.91020 ? 245 HIS   A H      1 
ATOM   3499 H HA     . HIS   A 1 244 ? 18.46447  -54.94319 14.61678  1.000 139.45305 ? 245 HIS   A HA     1 
ATOM   3500 H HB2    . HIS   A 1 244 ? 16.63528  -53.69866 13.85801  1.000 136.04361 ? 245 HIS   A HB2    1 
ATOM   3501 H HB3    . HIS   A 1 244 ? 16.86595  -52.65409 15.03321  1.000 136.04361 ? 245 HIS   A HB3    1 
ATOM   3502 H HD2    . HIS   A 1 244 ? 18.28820  -50.53911 14.17747  1.000 132.06031 ? 245 HIS   A HD2    1 
ATOM   3503 H HE1    . HIS   A 1 244 ? 20.18596  -52.26084 11.16152  1.000 132.80256 ? 245 HIS   A HE1    1 
ATOM   3504 N N      . PHE   A 1 245 ? 20.32332  -53.88485 15.81216  1.000 118.14601 ? 246 PHE   A N      1 
ATOM   3505 C CA     . PHE   A 1 245 ? 21.41402  -53.30294 16.57397  1.000 116.74506 ? 246 PHE   A CA     1 
ATOM   3506 C C      . PHE   A 1 245 ? 22.43153  -52.72175 15.60734  1.000 115.47054 ? 246 PHE   A C      1 
ATOM   3507 O O      . PHE   A 1 245 ? 22.43015  -53.02927 14.41353  1.000 142.51681 ? 246 PHE   A O      1 
ATOM   3508 C CB     . PHE   A 1 245 ? 22.08394  -54.33953 17.47758  1.000 120.13895 ? 246 PHE   A CB     1 
ATOM   3509 C CG     . PHE   A 1 245 ? 23.03639  -55.24356 16.75511  1.000 113.61869 ? 246 PHE   A CG     1 
ATOM   3510 C CD1    . PHE   A 1 245 ? 22.58567  -56.39609 16.13428  1.000 111.40626 ? 246 PHE   A CD1    1 
ATOM   3511 C CD2    . PHE   A 1 245 ? 24.38643  -54.94301 16.70207  1.000 113.88893 ? 246 PHE   A CD2    1 
ATOM   3512 C CE1    . PHE   A 1 245 ? 23.46451  -57.23089 15.47065  1.000 111.39856 ? 246 PHE   A CE1    1 
ATOM   3513 C CE2    . PHE   A 1 245 ? 25.26790  -55.77231 16.04221  1.000 114.53786 ? 246 PHE   A CE2    1 
ATOM   3514 C CZ     . PHE   A 1 245 ? 24.80636  -56.91880 15.42546  1.000 112.51497 ? 246 PHE   A CZ     1 
ATOM   3515 H H      . PHE   A 1 245 ? 20.58181  -54.35334 15.13889  1.000 142.16569 ? 246 PHE   A H      1 
ATOM   3516 H HA     . PHE   A 1 245 ? 21.07419  -52.58651 17.13266  1.000 140.48454 ? 246 PHE   A HA     1 
ATOM   3517 H HB2    . PHE   A 1 245 ? 22.58226  -53.87562 18.16850  1.000 144.55721 ? 246 PHE   A HB2    1 
ATOM   3518 H HB3    . PHE   A 1 245 ? 21.39675  -54.89369 17.87954  1.000 144.55721 ? 246 PHE   A HB3    1 
ATOM   3519 H HD1    . PHE   A 1 245 ? 21.68131  -56.61087 16.16422  1.000 134.00508 ? 246 PHE   A HD1    1 
ATOM   3520 H HD2    . PHE   A 1 245 ? 24.70247  -54.17271 17.11639  1.000 137.05718 ? 246 PHE   A HD2    1 
ATOM   3521 H HE1    . PHE   A 1 245 ? 23.15123  -58.00177 15.05532  1.000 131.72592 ? 246 PHE   A HE1    1 
ATOM   3522 H HE2    . PHE   A 1 245 ? 26.17284  -55.55999 16.01230  1.000 137.83590 ? 246 PHE   A HE2    1 
ATOM   3523 H HZ     . PHE   A 1 245 ? 25.40010  -57.47938 14.98034  1.000 133.06560 ? 246 PHE   A HZ     1 
ATOM   3524 N N      . GLY   A 1 246 ? 23.30990  -51.88775 16.13852  1.000 123.68739 ? 247 GLY   A N      1 
ATOM   3525 C CA     . GLY   A 1 246 ? 24.34682  -51.27473 15.32840  1.000 119.03669 ? 247 GLY   A CA     1 
ATOM   3526 C C      . GLY   A 1 246 ? 25.57619  -50.98488 16.15397  1.000 115.12521 ? 247 GLY   A C      1 
ATOM   3527 O O      . GLY   A 1 246 ? 25.49065  -50.67978 17.34729  1.000 131.30973 ? 247 GLY   A O      1 
ATOM   3528 H H      . GLY   A 1 246 ? 23.32694  -51.65990 16.96761  1.000 148.81533 ? 247 GLY   A H      1 
ATOM   3529 H HA2    . GLY   A 1 246 ? 24.59187  -51.87173 14.60422  1.000 143.23449 ? 247 GLY   A HA2    1 
ATOM   3530 H HA3    . GLY   A 1 246 ? 24.01980  -50.44177 14.95406  1.000 143.23449 ? 247 GLY   A HA3    1 
ATOM   3531 N N      . ILE   A 1 247 ? 26.73154  -51.07888 15.50681  1.000 115.62841 ? 248 ILE   A N      1 
ATOM   3532 C CA     . ILE   A 1 247 ? 28.02327  -50.84665 16.13717  1.000 117.89241 ? 248 ILE   A CA     1 
ATOM   3533 C C      . ILE   A 1 247 ? 28.72393  -49.73677 15.37136  1.000 118.32547 ? 248 ILE   A C      1 
ATOM   3534 O O      . ILE   A 1 247 ? 28.77560  -49.76640 14.13627  1.000 122.03028 ? 248 ILE   A O      1 
ATOM   3535 C CB     . ILE   A 1 247 ? 28.87734  -52.12713 16.15944  1.000 118.51365 ? 248 ILE   A CB     1 
ATOM   3536 C CG1    . ILE   A 1 247 ? 28.25289  -53.14813 17.11149  1.000 118.45867 ? 248 ILE   A CG1    1 
ATOM   3537 C CG2    . ILE   A 1 247 ? 30.31025  -51.80123 16.55051  1.000 120.85931 ? 248 ILE   A CG2    1 
ATOM   3538 C CD1    . ILE   A 1 247 ? 28.85761  -54.53038 17.01628  1.000 118.65612 ? 248 ILE   A CD1    1 
ATOM   3539 H H      . ILE   A 1 247 ? 26.79366  -51.28284 14.67366  1.000 136.80173 ? 248 ILE   A H      1 
ATOM   3540 H HA     . ILE   A 1 247 ? 27.89384  -50.55320 17.05261  1.000 139.51854 ? 248 ILE   A HA     1 
ATOM   3541 H HB     . ILE   A 1 247 ? 28.89621  -52.51418 15.27021  1.000 140.26402 ? 248 ILE   A HB     1 
ATOM   3542 H HG12   . ILE   A 1 247 ? 28.37158  -52.83664 18.02242  1.000 140.19805 ? 248 ILE   A HG12   1 
ATOM   3543 H HG13   . ILE   A 1 247 ? 27.30767  -53.22532 16.90777  1.000 140.19805 ? 248 ILE   A HG13   1 
ATOM   3544 H HG21   . ILE   A 1 247 ? 30.76564  -52.62231 16.79414  1.000 143.64218 ? 248 ILE   A HG21   1 
ATOM   3545 H HG22   . ILE   A 1 247 ? 30.75701  -51.38656 15.79596  1.000 143.64218 ? 248 ILE   A HG22   1 
ATOM   3546 H HG23   . ILE   A 1 247 ? 30.30083  -51.19179 17.30509  1.000 143.64218 ? 248 ILE   A HG23   1 
ATOM   3547 H HD11   . ILE   A 1 247 ? 28.30276  -55.15266 17.51208  1.000 140.43499 ? 248 ILE   A HD11   1 
ATOM   3548 H HD12   . ILE   A 1 247 ? 28.89800  -54.79386 16.08363  1.000 140.43499 ? 248 ILE   A HD12   1 
ATOM   3549 H HD13   . ILE   A 1 247 ? 29.75106  -54.51088 17.39348  1.000 140.43499 ? 248 ILE   A HD13   1 
ATOM   3550 N N      . SER   A 1 248 ? 29.25846  -48.76134 16.09919  1.000 131.22009 ? 249 SER   A N      1 
ATOM   3551 C CA     . SER   A 1 248 ? 29.90681  -47.61128 15.48888  1.000 136.75394 ? 249 SER   A CA     1 
ATOM   3552 C C      . SER   A 1 248 ? 31.25189  -47.34970 16.14985  1.000 143.47315 ? 249 SER   A C      1 
ATOM   3553 O O      . SER   A 1 248 ? 31.47558  -47.69844 17.31262  1.000 137.60563 ? 249 SER   A O      1 
ATOM   3554 C CB     . SER   A 1 248 ? 29.02261  -46.36193 15.58280  1.000 133.94338 ? 249 SER   A CB     1 
ATOM   3555 O OG     . SER   A 1 248 ? 27.87528  -46.49722 14.76268  1.000 120.41366 ? 249 SER   A OG     1 
ATOM   3556 H H      . SER   A 1 248 ? 29.25685  -48.74518 16.95904  1.000 157.85458 ? 249 SER   A H      1 
ATOM   3557 H HA     . SER   A 1 248 ? 30.07602  -47.79834 14.55225  1.000 164.49520 ? 249 SER   A HA     1 
ATOM   3558 H HB2    . SER   A 1 248 ? 28.74107  -46.24218 16.50329  1.000 161.12253 ? 249 SER   A HB2    1 
ATOM   3559 H HB3    . SER   A 1 248 ? 29.53239  -45.59084 15.28880  1.000 161.12253 ? 249 SER   A HB3    1 
ATOM   3560 H HG     . SER   A 1 248 ? 28.10108  -46.73754 13.99012  1.000 144.88686 ? 249 SER   A HG     1 
ATOM   3561 N N      . PHE   A 1 249 ? 32.14515  -46.72484 15.38750  1.000 130.49619 ? 250 PHE   A N      1 
ATOM   3562 C CA     . PHE   A 1 249 ? 33.50853  -46.46389 15.82683  1.000 140.25611 ? 250 PHE   A CA     1 
ATOM   3563 C C      . PHE   A 1 249 ? 34.13719  -45.47110 14.86147  1.000 132.61511 ? 250 PHE   A C      1 
ATOM   3564 O O      . PHE   A 1 249 ? 33.63166  -45.24961 13.75801  1.000 125.97215 ? 250 PHE   A O      1 
ATOM   3565 C CB     . PHE   A 1 249 ? 34.33132  -47.75430 15.88521  1.000 140.90652 ? 250 PHE   A CB     1 
ATOM   3566 C CG     . PHE   A 1 249 ? 34.15032  -48.63432 14.68418  1.000 131.13031 ? 250 PHE   A CG     1 
ATOM   3567 C CD1    . PHE   A 1 249 ? 34.92711  -48.45432 13.55391  1.000 141.50533 ? 250 PHE   A CD1    1 
ATOM   3568 C CD2    . PHE   A 1 249 ? 33.19215  -49.63353 14.68063  1.000 138.05339 ? 250 PHE   A CD2    1 
ATOM   3569 C CE1    . PHE   A 1 249 ? 34.75580  -49.25966 12.44222  1.000 150.82232 ? 250 PHE   A CE1    1 
ATOM   3570 C CE2    . PHE   A 1 249 ? 33.01641  -50.44206 13.57407  1.000 131.94128 ? 250 PHE   A CE2    1 
ATOM   3571 C CZ     . PHE   A 1 249 ? 33.79960  -50.25481 12.45299  1.000 127.20727 ? 250 PHE   A CZ     1 
ATOM   3572 H H      . PHE   A 1 249 ? 31.98048  -46.43643 14.59421  1.000 156.98589 ? 250 PHE   A H      1 
ATOM   3573 H HA     . PHE   A 1 249 ? 33.49835  -46.06624 16.71151  1.000 168.69780 ? 250 PHE   A HA     1 
ATOM   3574 H HB2    . PHE   A 1 249 ? 35.27151  -47.52336 15.94530  1.000 169.47830 ? 250 PHE   A HB2    1 
ATOM   3575 H HB3    . PHE   A 1 249 ? 34.06347  -48.26094 16.66781  1.000 169.47830 ? 250 PHE   A HB3    1 
ATOM   3576 H HD1    . PHE   A 1 249 ? 35.57189  -47.78425 13.54118  1.000 170.19687 ? 250 PHE   A HD1    1 
ATOM   3577 H HD2    . PHE   A 1 249 ? 32.66009  -49.76218 15.43247  1.000 166.05454 ? 250 PHE   A HD2    1 
ATOM   3578 H HE1    . PHE   A 1 249 ? 35.28460  -49.13058 11.68816  1.000 181.37725 ? 250 PHE   A HE1    1 
ATOM   3579 H HE2    . PHE   A 1 249 ? 32.37115  -51.11171 13.58459  1.000 158.72001 ? 250 PHE   A HE2    1 
ATOM   3580 H HZ     . PHE   A 1 249 ? 33.68325  -50.79775 11.70694  1.000 153.03920 ? 250 PHE   A HZ     1 
ATOM   3581 N N      . LYS   A 1 250 ? 35.24294  -44.87198 15.29335  1.000 152.69901 ? 251 LYS   A N      1 
ATOM   3582 C CA     . LYS   A 1 250 ? 35.99220  -43.98251 14.41875  1.000 140.37366 ? 251 LYS   A CA     1 
ATOM   3583 C C      . LYS   A 1 250 ? 36.65634  -44.79025 13.31293  1.000 150.60901 ? 251 LYS   A C      1 
ATOM   3584 O O      . LYS   A 1 250 ? 37.20908  -45.86726 13.55476  1.000 147.63621 ? 251 LYS   A O      1 
ATOM   3585 C CB     . LYS   A 1 250 ? 37.04155  -43.20580 15.21186  1.000 153.07771 ? 251 LYS   A CB     1 
ATOM   3586 C CG     . LYS   A 1 250 ? 36.45839  -42.12986 16.11518  1.000 155.66119 ? 251 LYS   A CG     1 
ATOM   3587 C CD     . LYS   A 1 250 ? 37.54577  -41.35315 16.85122  1.000 188.52788 ? 251 LYS   A CD     1 
ATOM   3588 C CE     . LYS   A 1 250 ? 38.24533  -42.20076 17.90937  1.000 206.97206 ? 251 LYS   A CE     1 
ATOM   3589 N NZ     . LYS   A 1 250 ? 37.33480  -42.58898 19.02534  1.000 189.19455 ? 251 LYS   A NZ     1 
ATOM   3590 H H      . LYS   A 1 250 ? 35.57596  -44.96389 16.08091  1.000 183.62929 ? 251 LYS   A H      1 
ATOM   3591 H HA     . LYS   A 1 250 ? 35.39234  -43.33516 14.01625  1.000 168.83886 ? 251 LYS   A HA     1 
ATOM   3592 H HB2    . LYS   A 1 250 ? 37.53215  -43.82782 15.77159  1.000 184.08372 ? 251 LYS   A HB2    1 
ATOM   3593 H HB3    . LYS   A 1 250 ? 37.64563  -42.77298 14.58844  1.000 184.08372 ? 251 LYS   A HB3    1 
ATOM   3594 H HG2    . LYS   A 1 250 ? 35.94904  -41.50302 15.57803  1.000 187.18390 ? 251 LYS   A HG2    1 
ATOM   3595 H HG3    . LYS   A 1 250 ? 35.88236  -42.54498 16.77607  1.000 187.18390 ? 251 LYS   A HG3    1 
ATOM   3596 H HD2    . LYS   A 1 250 ? 38.21301  -41.05664 16.21265  1.000 226.62393 ? 251 LYS   A HD2    1 
ATOM   3597 H HD3    . LYS   A 1 250 ? 37.14648  -40.58768 17.29340  1.000 226.62393 ? 251 LYS   A HD3    1 
ATOM   3598 H HE2    . LYS   A 1 250 ? 38.57765  -43.01301 17.49620  1.000 248.75695 ? 251 LYS   A HE2    1 
ATOM   3599 H HE3    . LYS   A 1 250 ? 38.98228  -41.69418 18.28511  1.000 248.75695 ? 251 LYS   A HE3    1 
ATOM   3600 H HZ1    . LYS   A 1 250 ? 37.76401  -43.11744 19.59859  1.000 227.42393 ? 251 LYS   A HZ1    1 
ATOM   3601 H HZ2    . LYS   A 1 250 ? 37.05468  -41.86247 19.45640  1.000 227.42393 ? 251 LYS   A HZ2    1 
ATOM   3602 H HZ3    . LYS   A 1 250 ? 36.62831  -43.02469 18.70422  1.000 227.42393 ? 251 LYS   A HZ3    1 
ATOM   3603 N N      . THR   A 1 251 ? 36.59450  -44.26683 12.09213  1.000 154.88805 ? 252 THR   A N      1 
ATOM   3604 C CA     . THR   A 1 251 ? 37.10744  -44.96906 10.92484  1.000 154.39496 ? 252 THR   A CA     1 
ATOM   3605 C C      . THR   A 1 251 ? 38.55169  -44.55700 10.67055  1.000 162.09033 ? 252 THR   A C      1 
ATOM   3606 O O      . THR   A 1 251 ? 38.88353  -43.36798 10.71718  1.000 159.97304 ? 252 THR   A O      1 
ATOM   3607 C CB     . THR   A 1 251 ? 36.24135  -44.67702 9.69770   1.000 152.07459 ? 252 THR   A CB     1 
ATOM   3608 O OG1    . THR   A 1 251 ? 36.54862  -45.61440 8.65746   1.000 175.11966 ? 252 THR   A OG1    1 
ATOM   3609 C CG2    . THR   A 1 251 ? 36.47980  -43.26134 9.18631   1.000 171.17982 ? 252 THR   A CG2    1 
ATOM   3610 H H      . THR   A 1 251 ? 36.25555  -43.49680 11.91389  1.000 186.25613 ? 252 THR   A H      1 
ATOM   3611 H HA     . THR   A 1 251 ? 37.08846  -45.92538 11.08604  1.000 185.66443 ? 252 THR   A HA     1 
ATOM   3612 H HB     . THR   A 1 251 ? 35.30600  -44.75636 9.94211   1.000 182.87998 ? 252 THR   A HB     1 
ATOM   3613 H HG1    . THR   A 1 251 ? 36.44857  -46.39936 8.93931   1.000 210.53407 ? 252 THR   A HG1    1 
ATOM   3614 H HG21   . THR   A 1 251 ? 35.70073  -42.94848 8.70045   1.000 205.80625 ? 252 THR   A HG21   1 
ATOM   3615 H HG22   . THR   A 1 251 ? 36.64726  -42.66326 9.93139   1.000 205.80625 ? 252 THR   A HG22   1 
ATOM   3616 H HG23   . THR   A 1 251 ? 37.24715  -43.24774 8.59310   1.000 205.80625 ? 252 THR   A HG23   1 
ATOM   3617 N N      . SER   A 1 252 ? 39.40559  -45.54346 10.41503  1.000 174.29590 ? 253 SER   A N      1 
ATOM   3618 C CA     . SER   A 1 252 ? 40.81540  -45.29450 10.13418  1.000 174.35355 ? 253 SER   A CA     1 
ATOM   3619 C C      . SER   A 1 252 ? 41.46576  -44.46672 11.23869  1.000 178.32602 ? 253 SER   A C      1 
ATOM   3620 O O      . SER   A 1 252 ? 42.27469  -44.97561 12.01435  1.000 187.16555 ? 253 SER   A O      1 
ATOM   3621 C CB     . SER   A 1 252 ? 40.97432  -44.59027 8.78510   1.000 165.22842 ? 253 SER   A CB     1 
ATOM   3622 O OG     . SER   A 1 252 ? 42.34156  -44.41125 8.46144   1.000 176.10621 ? 253 SER   A OG     1 
ATOM   3623 N N      . THR   A 1 259 ? 41.40561  -51.46892 4.15208   1.000 180.57585 ? 260 THR   A N      1 
ATOM   3624 C CA     . THR   A 1 259 ? 40.18719  -52.05575 4.69821   1.000 186.07526 ? 260 THR   A CA     1 
ATOM   3625 C C      . THR   A 1 259 ? 40.20335  -53.57370 4.53862   1.000 188.53585 ? 260 THR   A C      1 
ATOM   3626 O O      . THR   A 1 259 ? 40.25995  -54.09233 3.42352   1.000 190.23313 ? 260 THR   A O      1 
ATOM   3627 C CB     . THR   A 1 259 ? 38.93303  -51.48340 4.01558   1.000 171.65787 ? 260 THR   A CB     1 
ATOM   3628 O OG1    . THR   A 1 259 ? 38.98872  -51.74362 2.60762   1.000 186.44054 ? 260 THR   A OG1    1 
ATOM   3629 C CG2    . THR   A 1 259 ? 38.83538  -49.98226 4.24965   1.000 173.30273 ? 260 THR   A CG2    1 
ATOM   3630 H HA     . THR   A 1 259 ? 40.12771  -51.85294 5.64491   1.000 223.68078 ? 260 THR   A HA     1 
ATOM   3631 H HB     . THR   A 1 259 ? 38.14221  -51.90297 4.38903   1.000 206.37991 ? 260 THR   A HB     1 
ATOM   3632 H HG1    . THR   A 1 259 ? 39.69966  -51.43271 2.28590   1.000 224.11912 ? 260 THR   A HG1    1 
ATOM   3633 H HG21   . THR   A 1 259 ? 38.02265  -49.63618 3.84892   1.000 208.35375 ? 260 THR   A HG21   1 
ATOM   3634 H HG22   . THR   A 1 259 ? 38.82155  -49.79510 5.20133   1.000 208.35375 ? 260 THR   A HG22   1 
ATOM   3635 H HG23   . THR   A 1 259 ? 39.59811  -49.53414 3.85175   1.000 208.35375 ? 260 THR   A HG23   1 
ATOM   3636 N N      . LEU   A 1 260 ? 40.14676  -54.27962 5.66667   1.000 188.27275 ? 261 LEU   A N      1 
ATOM   3637 C CA     . LEU   A 1 260 ? 40.24766  -55.73109 5.69766   1.000 191.34585 ? 261 LEU   A CA     1 
ATOM   3638 C C      . LEU   A 1 260 ? 38.89160  -56.42781 5.72044   1.000 170.47176 ? 261 LEU   A C      1 
ATOM   3639 O O      . LEU   A 1 260 ? 38.84190  -57.65005 5.89201   1.000 166.13902 ? 261 LEU   A O      1 
ATOM   3640 C CB     . LEU   A 1 260 ? 41.06139  -56.17131 6.91841   1.000 194.61106 ? 261 LEU   A CB     1 
ATOM   3641 C CG     . LEU   A 1 260 ? 42.58587  -56.11464 6.81617   1.000 211.48901 ? 261 LEU   A CG     1 
ATOM   3642 C CD1    . LEU   A 1 260 ? 43.07235  -54.70070 6.53960   1.000 199.96191 ? 261 LEU   A CD1    1 
ATOM   3643 C CD2    . LEU   A 1 260 ? 43.21291  -56.66692 8.09256   1.000 170.76504 ? 261 LEU   A CD2    1 
ATOM   3644 H H      . LEU   A 1 260 ? 40.04770  -53.92810 6.44527   1.000 226.31777 ? 261 LEU   A H      1 
ATOM   3645 H HA     . LEU   A 1 260 ? 40.71158  -56.01455 4.89434   1.000 230.00549 ? 261 LEU   A HA     1 
ATOM   3646 H HB2    . LEU   A 1 260 ? 40.80971  -55.60187 7.66224   1.000 233.92374 ? 261 LEU   A HB2    1 
ATOM   3647 H HB3    . LEU   A 1 260 ? 40.82824  -57.09271 7.11226   1.000 233.92374 ? 261 LEU   A HB3    1 
ATOM   3648 H HG     . LEU   A 1 260 ? 42.87166  -56.66325 6.06900   1.000 254.17728 ? 261 LEU   A HG     1 
ATOM   3649 H HD11   . LEU   A 1 260 ? 44.03989  -54.68102 6.60579   1.000 240.34476 ? 261 LEU   A HD11   1 
ATOM   3650 H HD12   . LEU   A 1 260 ? 42.79653  -54.44082 5.64669   1.000 240.34476 ? 261 LEU   A HD12   1 
ATOM   3651 H HD13   . LEU   A 1 260 ? 42.68373  -54.09935 7.19401   1.000 240.34476 ? 261 LEU   A HD13   1 
ATOM   3652 H HD21   . LEU   A 1 260 ? 44.17881  -56.63386 8.00981   1.000 205.30852 ? 261 LEU   A HD21   1 
ATOM   3653 H HD22   . LEU   A 1 260 ? 42.92665  -56.12561 8.84485   1.000 205.30852 ? 261 LEU   A HD22   1 
ATOM   3654 H HD23   . LEU   A 1 260 ? 42.92266  -57.58425 8.21568   1.000 205.30852 ? 261 LEU   A HD23   1 
ATOM   3655 N N      . VAL   A 1 261 ? 37.79668  -55.69264 5.54334   1.000 161.69920 ? 262 VAL   A N      1 
ATOM   3656 C CA     . VAL   A 1 261 ? 36.45426  -56.22022 5.75756   1.000 152.52695 ? 262 VAL   A CA     1 
ATOM   3657 C C      . VAL   A 1 261 ? 35.67964  -56.17985 4.44927   1.000 152.95059 ? 262 VAL   A C      1 
ATOM   3658 O O      . VAL   A 1 261 ? 35.59904  -55.13221 3.79710   1.000 157.30553 ? 262 VAL   A O      1 
ATOM   3659 C CB     . VAL   A 1 261 ? 35.71166  -55.43690 6.85661   1.000 150.28983 ? 262 VAL   A CB     1 
ATOM   3660 C CG1    . VAL   A 1 261 ? 34.21326  -55.68342 6.77513   1.000 129.88576 ? 262 VAL   A CG1    1 
ATOM   3661 C CG2    . VAL   A 1 261 ? 36.24256  -55.82959 8.22612   1.000 153.38831 ? 262 VAL   A CG2    1 
ATOM   3662 H H      . VAL   A 1 261 ? 37.80801  -54.86953 5.29441   1.000 194.42951 ? 262 VAL   A H      1 
ATOM   3663 H HA     . VAL   A 1 261 ? 36.52456  -57.14960 6.02627   1.000 183.42281 ? 262 VAL   A HA     1 
ATOM   3664 H HB     . VAL   A 1 261 ? 35.86508  -54.48813 6.72550   1.000 180.73827 ? 262 VAL   A HB     1 
ATOM   3665 H HG11   . VAL   A 1 261 ? 33.80755  -55.44593 7.62360   1.000 156.25338 ? 262 VAL   A HG11   1 
ATOM   3666 H HG12   . VAL   A 1 261 ? 33.84128  -55.13612 6.06591   1.000 156.25338 ? 262 VAL   A HG12   1 
ATOM   3667 H HG13   . VAL   A 1 261 ? 34.05747  -56.62178 6.58512   1.000 156.25338 ? 262 VAL   A HG13   1 
ATOM   3668 H HG21   . VAL   A 1 261 ? 35.77140  -55.32164 8.90501   1.000 184.45644 ? 262 VAL   A HG21   1 
ATOM   3669 H HG22   . VAL   A 1 261 ? 36.09545  -56.77875 8.36158   1.000 184.45644 ? 262 VAL   A HG22   1 
ATOM   3670 H HG23   . VAL   A 1 261 ? 37.19164  -55.63307 8.26514   1.000 184.45644 ? 262 VAL   A HG23   1 
ATOM   3671 N N      . ASP   A 1 262 ? 35.11066  -57.32333 4.07603   1.000 155.72298 ? 263 ASP   A N      1 
ATOM   3672 C CA     . ASP   A 1 262 ? 34.18857  -57.44288 2.95410   1.000 149.95938 ? 263 ASP   A CA     1 
ATOM   3673 C C      . ASP   A 1 262 ? 32.81758  -57.79541 3.51576   1.000 142.53835 ? 263 ASP   A C      1 
ATOM   3674 O O      . ASP   A 1 262 ? 32.66263  -58.83213 4.17018   1.000 146.84401 ? 263 ASP   A O      1 
ATOM   3675 C CB     . ASP   A 1 262 ? 34.65984  -58.51131 1.96898   1.000 148.39234 ? 263 ASP   A CB     1 
ATOM   3676 C CG     . ASP   A 1 262 ? 33.79541  -58.58072 0.72705   1.000 148.73946 ? 263 ASP   A CG     1 
ATOM   3677 O OD1    . ASP   A 1 262 ? 32.67270  -58.03376 0.74781   1.000 150.26594 ? 263 ASP   A OD1    1 
ATOM   3678 O OD2    . ASP   A 1 262 ? 34.23796  -59.18635 -0.27120  1.000 146.38294 ? 263 ASP   A OD2    1 
ATOM   3679 H H      . ASP   A 1 262 ? 35.25022  -58.07247 4.47467   1.000 187.25805 ? 263 ASP   A H      1 
ATOM   3680 H HA     . ASP   A 1 262 ? 34.13057  -56.60070 2.47633   1.000 180.34173 ? 263 ASP   A HA     1 
ATOM   3681 H HB2    . ASP   A 1 262 ? 35.56731  -58.30888 1.69254   1.000 178.46128 ? 263 ASP   A HB2    1 
ATOM   3682 H HB3    . ASP   A 1 262 ? 34.63102  -59.37782 2.40398   1.000 178.46128 ? 263 ASP   A HB3    1 
ATOM   3683 N N      . PHE   A 1 263 ? 31.82699  -56.94138 3.25847   1.000 133.04085 ? 264 PHE   A N      1 
ATOM   3684 C CA     . PHE   A 1 263 ? 30.51375  -57.12205 3.86517   1.000 130.57880 ? 264 PHE   A CA     1 
ATOM   3685 C C      . PHE   A 1 263 ? 29.66164  -58.16592 3.15894   1.000 137.65372 ? 264 PHE   A C      1 
ATOM   3686 O O      . PHE   A 1 263 ? 28.60810  -58.53657 3.68853   1.000 140.90077 ? 264 PHE   A O      1 
ATOM   3687 C CB     . PHE   A 1 263 ? 29.77402  -55.78641 3.91533   1.000 122.79662 ? 264 PHE   A CB     1 
ATOM   3688 C CG     . PHE   A 1 263 ? 30.19756  -54.91885 5.05885   1.000 112.60182 ? 264 PHE   A CG     1 
ATOM   3689 C CD1    . PHE   A 1 263 ? 31.29510  -54.08581 4.94177   1.000 123.68434 ? 264 PHE   A CD1    1 
ATOM   3690 C CD2    . PHE   A 1 263 ? 29.51190  -54.95325 6.26021   1.000 111.29110 ? 264 PHE   A CD2    1 
ATOM   3691 C CE1    . PHE   A 1 263 ? 31.69372  -53.29329 5.99655   1.000 114.30176 ? 264 PHE   A CE1    1 
ATOM   3692 C CE2    . PHE   A 1 263 ? 29.90584  -54.16305 7.31865   1.000 127.54532 ? 264 PHE   A CE2    1 
ATOM   3693 C CZ     . PHE   A 1 263 ? 31.00108  -53.33375 7.18736   1.000 130.39411 ? 264 PHE   A CZ     1 
ATOM   3694 H H      . PHE   A 1 263 ? 31.89172  -56.25739 2.74121   1.000 160.03949 ? 264 PHE   A H      1 
ATOM   3695 H HA     . PHE   A 1 263 ? 30.63503  -57.42572 4.77839   1.000 157.08503 ? 264 PHE   A HA     1 
ATOM   3696 H HB2    . PHE   A 1 263 ? 29.94624  -55.30124 3.09323   1.000 147.74641 ? 264 PHE   A HB2    1 
ATOM   3697 H HB3    . PHE   A 1 263 ? 28.82358  -55.95733 4.00680   1.000 147.74641 ? 264 PHE   A HB3    1 
ATOM   3698 H HD1    . PHE   A 1 263 ? 31.76956  -54.06004 4.14232   1.000 148.81168 ? 264 PHE   A HD1    1 
ATOM   3699 H HD2    . PHE   A 1 263 ? 28.77725  -55.51564 6.35455   1.000 132.43127 ? 264 PHE   A HD2    1 
ATOM   3700 H HE1    . PHE   A 1 263 ? 32.42938  -52.73177 5.90483   1.000 137.05010 ? 264 PHE   A HE1    1 
ATOM   3701 H HE2    . PHE   A 1 263 ? 29.43439  -54.18871 8.11988   1.000 153.44485 ? 264 PHE   A HE2    1 
ATOM   3702 H HZ     . PHE   A 1 263 ? 31.27141  -52.80288 7.90150   1.000 156.86340 ? 264 PHE   A HZ     1 
ATOM   3703 N N      . GLN   A 1 264 ? 30.08003  -58.64749 1.98870   1.000 155.08704 ? 265 GLN   A N      1 
ATOM   3704 C CA     . GLN   A 1 264 ? 29.48760  -59.85568 1.43233   1.000 150.75092 ? 265 GLN   A CA     1 
ATOM   3705 C C      . GLN   A 1 264 ? 29.99863  -61.11097 2.12508   1.000 151.19833 ? 265 GLN   A C      1 
ATOM   3706 O O      . GLN   A 1 264 ? 29.49191  -62.20326 1.84885   1.000 156.95741 ? 265 GLN   A O      1 
ATOM   3707 C CB     . GLN   A 1 264 ? 29.76947  -59.95867 -0.06870  1.000 152.99455 ? 265 GLN   A CB     1 
ATOM   3708 C CG     . GLN   A 1 264 ? 29.13164  -58.86062 -0.90617  1.000 175.65832 ? 265 GLN   A CG     1 
ATOM   3709 C CD     . GLN   A 1 264 ? 27.67696  -58.61826 -0.54978  1.000 174.58880 ? 265 GLN   A CD     1 
ATOM   3710 O OE1    . GLN   A 1 264 ? 26.80778  -59.44565 -0.82740  1.000 174.57419 ? 265 GLN   A OE1    1 
ATOM   3711 N NE2    . GLN   A 1 264 ? 27.40774  -57.48143 0.08219   1.000 163.64934 ? 265 GLN   A NE2    1 
ATOM   3712 H H      . GLN   A 1 264 ? 30.69818  -58.29494 1.50579   1.000 186.49492 ? 265 GLN   A H      1 
ATOM   3713 H HA     . GLN   A 1 264 ? 28.52493  -59.80636 1.54070   1.000 181.29158 ? 265 GLN   A HA     1 
ATOM   3714 H HB2    . GLN   A 1 264 ? 30.72849  -59.91309 -0.20692  1.000 183.98393 ? 265 GLN   A HB2    1 
ATOM   3715 H HB3    . GLN   A 1 264 ? 29.42801  -60.80793 -0.38973  1.000 183.98393 ? 265 GLN   A HB3    1 
ATOM   3716 H HG2    . GLN   A 1 264 ? 29.61688  -58.03284 -0.76401  1.000 211.18045 ? 265 GLN   A HG2    1 
ATOM   3717 H HG3    . GLN   A 1 264 ? 29.17286  -59.11285 -1.84190  1.000 211.18045 ? 265 GLN   A HG3    1 
ATOM   3718 H HE21   . GLN   A 1 264 ? 28.04248  -56.93126 0.26668   1.000 196.76968 ? 265 GLN   A HE21   1 
ATOM   3719 H HE22   . GLN   A 1 264 ? 26.59870  -57.29553 0.30689   1.000 196.76968 ? 265 GLN   A HE22   1 
ATOM   3720 N N      . ASP   A 1 265 ? 30.98122  -60.97420 3.01264   1.000 149.14687 ? 266 ASP   A N      1 
ATOM   3721 C CA     . ASP   A 1 265 ? 31.58800  -62.08365 3.74293   1.000 149.42147 ? 266 ASP   A CA     1 
ATOM   3722 C C      . ASP   A 1 265 ? 31.37204  -61.81647 5.22905   1.000 138.04972 ? 266 ASP   A C      1 
ATOM   3723 O O      . ASP   A 1 265 ? 32.16722  -61.12372 5.86859   1.000 135.52805 ? 266 ASP   A O      1 
ATOM   3724 C CB     . ASP   A 1 265 ? 33.07345  -62.21191 3.39428   1.000 149.67660 ? 266 ASP   A CB     1 
ATOM   3725 C CG     . ASP   A 1 265 ? 33.77708  -63.28443 4.20332   1.000 162.48273 ? 266 ASP   A CG     1 
ATOM   3726 O OD1    . ASP   A 1 265 ? 33.10247  -63.99612 4.97644   1.000 165.53726 ? 266 ASP   A OD1    1 
ATOM   3727 O OD2    . ASP   A 1 265 ? 35.01117  -63.41761 4.06029   1.000 164.91818 ? 266 ASP   A OD2    1 
ATOM   3728 H H      . ASP   A 1 265 ? 31.32778  -60.21413 3.21705   1.000 179.36671 ? 266 ASP   A H      1 
ATOM   3729 H HA     . ASP   A 1 265 ? 31.14728  -62.91584 3.51026   1.000 179.69624 ? 266 ASP   A HA     1 
ATOM   3730 H HB2    . ASP   A 1 265 ? 33.15895  -62.44030 2.45543   1.000 180.00239 ? 266 ASP   A HB2    1 
ATOM   3731 H HB3    . ASP   A 1 265 ? 33.51363  -61.36586 3.57132   1.000 180.00239 ? 266 ASP   A HB3    1 
ATOM   3732 N N      . ARG   A 1 266 ? 30.28905  -62.36949 5.77906   1.000 132.18373 ? 267 ARG   A N      1 
ATOM   3733 C CA     . ARG   A 1 266 ? 30.01542  -62.18275 7.19764   1.000 136.75769 ? 267 ARG   A CA     1 
ATOM   3734 C C      . ARG   A 1 266 ? 31.14587  -62.71394 8.06821   1.000 148.12943 ? 267 ARG   A C      1 
ATOM   3735 O O      . ARG   A 1 266 ? 31.28429  -62.27995 9.21666   1.000 150.11939 ? 267 ARG   A O      1 
ATOM   3736 C CB     . ARG   A 1 266 ? 28.69934  -62.86252 7.58166   1.000 125.07834 ? 267 ARG   A CB     1 
ATOM   3737 C CG     . ARG   A 1 266 ? 28.76835  -64.37816 7.64743   1.000 132.99917 ? 267 ARG   A CG     1 
ATOM   3738 C CD     . ARG   A 1 266 ? 27.43907  -64.97312 8.08354   1.000 134.07153 ? 267 ARG   A CD     1 
ATOM   3739 N NE     . ARG   A 1 266 ? 27.14937  -64.69323 9.48451   1.000 119.78268 ? 267 ARG   A NE     1 
ATOM   3740 C CZ     . ARG   A 1 266 ? 27.63713  -65.39021 10.50151  1.000 122.56497 ? 267 ARG   A CZ     1 
ATOM   3741 N NH1    . ARG   A 1 266 ? 28.45750  -66.41086 10.30986  1.000 142.35974 ? 267 ARG   A NH1    1 
ATOM   3742 N NH2    . ARG   A 1 266 ? 27.29679  -65.05223 11.74194  1.000 145.04958 ? 267 ARG   A NH2    1 
ATOM   3743 H H      . ARG   A 1 266 ? 29.71049  -62.84715 5.35869   1.000 159.01095 ? 267 ARG   A H      1 
ATOM   3744 H HA     . ARG   A 1 266 ? 29.91775  -61.23351 7.37177   1.000 164.49970 ? 267 ARG   A HA     1 
ATOM   3745 H HB2    . ARG   A 1 266 ? 28.43096  -62.54331 8.45744   1.000 150.48448 ? 267 ARG   A HB2    1 
ATOM   3746 H HB3    . ARG   A 1 266 ? 28.02706  -62.62829 6.92282   1.000 150.48448 ? 267 ARG   A HB3    1 
ATOM   3747 H HG2    . ARG   A 1 266 ? 28.98709  -64.72897 6.76995   1.000 159.98948 ? 267 ARG   A HG2    1 
ATOM   3748 H HG3    . ARG   A 1 266 ? 29.44651  -64.64215 8.28876   1.000 159.98948 ? 267 ARG   A HG3    1 
ATOM   3749 H HD2    . ARG   A 1 266 ? 26.72726  -64.59317 7.54514   1.000 161.27631 ? 267 ARG   A HD2    1 
ATOM   3750 H HD3    . ARG   A 1 266 ? 27.46622  -65.93560 7.96613   1.000 161.27631 ? 267 ARG   A HD3    1 
ATOM   3751 H HE     . ARG   A 1 266 ? 26.62807  -64.03294 9.66302   1.000 144.12969 ? 267 ARG   A HE     1 
ATOM   3752 H HH11   . ARG   A 1 266 ? 28.68556  -66.63522 9.51158   1.000 171.22216 ? 267 ARG   A HH11   1 
ATOM   3753 H HH12   . ARG   A 1 266 ? 28.76254  -66.84975 10.98360  1.000 171.22216 ? 267 ARG   A HH12   1 
ATOM   3754 H HH21   . ARG   A 1 266 ? 26.76644  -64.38877 11.87669  1.000 174.44997 ? 267 ARG   A HH21   1 
ATOM   3755 H HH22   . ARG   A 1 266 ? 27.60706  -65.49714 12.40932  1.000 174.44997 ? 267 ARG   A HH22   1 
ATOM   3756 N N      . ASN   A 1 267 ? 31.95549  -63.64200 7.55222   1.000 144.51496 ? 268 ASN   A N      1 
ATOM   3757 C CA     . ASN   A 1 267 ? 33.07074  -64.16172 8.33642   1.000 145.12420 ? 268 ASN   A CA     1 
ATOM   3758 C C      . ASN   A 1 267 ? 34.11722  -63.08058 8.57459   1.000 150.53708 ? 268 ASN   A C      1 
ATOM   3759 O O      . ASN   A 1 267 ? 34.60670  -62.91215 9.69772   1.000 150.27510 ? 268 ASN   A O      1 
ATOM   3760 C CB     . ASN   A 1 267 ? 33.69390  -65.36840 7.63384   1.000 153.53693 ? 268 ASN   A CB     1 
ATOM   3761 C CG     . ASN   A 1 267 ? 32.67602  -66.44138 7.30968   1.000 161.03480 ? 268 ASN   A CG     1 
ATOM   3762 O OD1    . ASN   A 1 267 ? 32.11123  -67.06832 8.20515   1.000 167.52059 ? 268 ASN   A OD1    1 
ATOM   3763 N ND2    . ASN   A 1 267 ? 32.44056  -66.66326 6.02257   1.000 156.60133 ? 268 ASN   A ND2    1 
ATOM   3764 H H      . ASN   A 1 267 ? 31.88043  -63.97977 6.76489   1.000 173.80842 ? 268 ASN   A H      1 
ATOM   3765 H HA     . ASN   A 1 267 ? 32.73642  -64.45785 9.19749   1.000 174.53951 ? 268 ASN   A HA     1 
ATOM   3766 H HB2    . ASN   A 1 267 ? 34.09859  -65.07658 6.80200   1.000 184.63479 ? 268 ASN   A HB2    1 
ATOM   3767 H HB3    . ASN   A 1 267 ? 34.36819  -65.75829 8.21196   1.000 184.63479 ? 268 ASN   A HB3    1 
ATOM   3768 H HD21   . ASN   A 1 267 ? 31.87078  -67.26271 5.78677   1.000 188.31207 ? 268 ASN   A HD21   1 
ATOM   3769 H HD22   . ASN   A 1 267 ? 32.85776  -66.20758 5.42432   1.000 188.31207 ? 268 ASN   A HD22   1 
ATOM   3770 N N      . SER   A 1 268 ? 34.47236  -62.33401 7.52531   1.000 142.57669 ? 269 SER   A N      1 
ATOM   3771 C CA     . SER   A 1 268 ? 35.44580  -61.25958 7.68414   1.000 149.88831 ? 269 SER   A CA     1 
ATOM   3772 C C      . SER   A 1 268 ? 34.93729  -60.18336 8.63313   1.000 146.09029 ? 269 SER   A C      1 
ATOM   3773 O O      . SER   A 1 268 ? 35.73319  -59.54276 9.32917   1.000 137.27788 ? 269 SER   A O      1 
ATOM   3774 C CB     . SER   A 1 268 ? 35.77898  -60.64441 6.32474   1.000 141.54098 ? 269 SER   A CB     1 
ATOM   3775 O OG     . SER   A 1 268 ? 34.70147  -59.86274 5.83866   1.000 134.75892 ? 269 SER   A OG     1 
ATOM   3776 H H      . SER   A 1 268 ? 34.16866  -62.42922 6.72638   1.000 171.48249 ? 269 SER   A H      1 
ATOM   3777 H HA     . SER   A 1 268 ? 36.26136  -61.63197 8.05441   1.000 180.25645 ? 269 SER   A HA     1 
ATOM   3778 H HB2    . SER   A 1 268 ? 36.56082  -60.07808 6.41902   1.000 170.23965 ? 269 SER   A HB2    1 
ATOM   3779 H HB3    . SER   A 1 268 ? 35.96020  -61.35763 5.69278   1.000 170.23965 ? 269 SER   A HB3    1 
ATOM   3780 H HG     . SER   A 1 268 ? 34.02357  -60.34598 5.72667   1.000 162.10117 ? 269 SER   A HG     1 
ATOM   3781 N N      . VAL   A 1 269 ? 33.62097  -59.96923 8.67507   1.000 141.14009 ? 270 VAL   A N      1 
ATOM   3782 C CA     . VAL   A 1 269 ? 33.06433  -58.95621 9.56431   1.000 129.69974 ? 270 VAL   A CA     1 
ATOM   3783 C C      . VAL   A 1 269 ? 33.11898  -59.43059 11.01091  1.000 148.78384 ? 270 VAL   A C      1 
ATOM   3784 O O      . VAL   A 1 269 ? 33.47181  -58.66590 11.91745  1.000 158.33185 ? 270 VAL   A O      1 
ATOM   3785 C CB     . VAL   A 1 269 ? 31.62736  -58.60757 9.13632   1.000 111.94248 ? 270 VAL   A CB     1 
ATOM   3786 C CG1    . VAL   A 1 269 ? 31.06789  -57.50111 10.00889  1.000 119.48275 ? 270 VAL   A CG1    1 
ATOM   3787 C CG2    . VAL   A 1 269 ? 31.59209  -58.20158 7.67285   1.000 122.30752 ? 270 VAL   A CG2    1 
ATOM   3788 H H      . VAL   A 1 269 ? 33.03823  -60.39200 8.20467   1.000 169.75858 ? 270 VAL   A H      1 
ATOM   3789 H HA     . VAL   A 1 269 ? 33.60273  -58.15245 9.49357   1.000 156.03015 ? 270 VAL   A HA     1 
ATOM   3790 H HB     . VAL   A 1 269 ? 31.06832  -59.39258 9.24645   1.000 134.72145 ? 270 VAL   A HB     1 
ATOM   3791 H HG11   . VAL   A 1 269 ? 30.26656  -57.14592 9.59342   1.000 143.76978 ? 270 VAL   A HG11   1 
ATOM   3792 H HG12   . VAL   A 1 269 ? 30.85414  -57.86517 10.88220  1.000 143.76978 ? 270 VAL   A HG12   1 
ATOM   3793 H HG13   . VAL   A 1 269 ? 31.73337  -56.80083 10.09630  1.000 143.76978 ? 270 VAL   A HG13   1 
ATOM   3794 H HG21   . VAL   A 1 269 ? 30.68659  -57.94501 7.43804   1.000 147.15949 ? 270 VAL   A HG21   1 
ATOM   3795 H HG22   . VAL   A 1 269 ? 32.19355  -57.45255 7.53834   1.000 147.15949 ? 270 VAL   A HG22   1 
ATOM   3796 H HG23   . VAL   A 1 269 ? 31.87414  -58.95400 7.12951   1.000 147.15949 ? 270 VAL   A HG23   1 
ATOM   3797 N N      . VAL   A 1 270 ? 32.77985  -60.69850 11.25133  1.000 140.14512 ? 271 VAL   A N      1 
ATOM   3798 C CA     . VAL   A 1 270 ? 32.79275  -61.22428 12.61404  1.000 147.88913 ? 271 VAL   A CA     1 
ATOM   3799 C C      . VAL   A 1 270 ? 34.20546  -61.18186 13.18324  1.000 140.81542 ? 271 VAL   A C      1 
ATOM   3800 O O      . VAL   A 1 270 ? 34.42954  -60.70080 14.30048  1.000 132.68642 ? 271 VAL   A O      1 
ATOM   3801 C CB     . VAL   A 1 270 ? 32.21036  -62.64863 12.64304  1.000 145.60425 ? 271 VAL   A CB     1 
ATOM   3802 C CG1    . VAL   A 1 270 ? 32.51106  -63.32307 13.97200  1.000 154.42154 ? 271 VAL   A CG1    1 
ATOM   3803 C CG2    . VAL   A 1 270 ? 30.70969  -62.60681 12.39473  1.000 135.48486 ? 271 VAL   A CG2    1 
ATOM   3804 H H      . VAL   A 1 270 ? 32.54190  -61.26633 10.65087  1.000 168.56461 ? 271 VAL   A H      1 
ATOM   3805 H HA     . VAL   A 1 270 ? 32.23164  -60.66102 13.16974  1.000 177.85742 ? 271 VAL   A HA     1 
ATOM   3806 H HB     . VAL   A 1 270 ? 32.62449  -63.17276 11.93970  1.000 175.11558 ? 271 VAL   A HB     1 
ATOM   3807 H HG11   . VAL   A 1 270 ? 31.91090  -64.07642 14.08676  1.000 185.69632 ? 271 VAL   A HG11   1 
ATOM   3808 H HG12   . VAL   A 1 270 ? 33.43105  -63.63052 13.96909  1.000 185.69632 ? 271 VAL   A HG12   1 
ATOM   3809 H HG13   . VAL   A 1 270 ? 32.37863  -62.68255 14.68831  1.000 185.69632 ? 271 VAL   A HG13   1 
ATOM   3810 H HG21   . VAL   A 1 270 ? 30.36617  -63.51386 12.38279  1.000 162.97230 ? 271 VAL   A HG21   1 
ATOM   3811 H HG22   . VAL   A 1 270 ? 30.28581  -62.10191 13.10627  1.000 162.97230 ? 271 VAL   A HG22   1 
ATOM   3812 H HG23   . VAL   A 1 270 ? 30.54276  -62.17861 11.54051  1.000 162.97230 ? 271 VAL   A HG23   1 
ATOM   3813 N N      . ASP   A 1 271 ? 35.18099  -61.68481 12.42167  1.000 144.02624 ? 272 ASP   A N      1 
ATOM   3814 C CA     . ASP   A 1 271 ? 36.56990  -61.61725 12.86379  1.000 154.11943 ? 272 ASP   A CA     1 
ATOM   3815 C C      . ASP   A 1 271 ? 36.95811  -60.19040 13.22414  1.000 152.16389 ? 272 ASP   A C      1 
ATOM   3816 O O      . ASP   A 1 271 ? 37.65837  -59.95705 14.21623  1.000 172.53501 ? 272 ASP   A O      1 
ATOM   3817 C CB     . ASP   A 1 271 ? 37.49858  -62.15936 11.77546  1.000 173.05995 ? 272 ASP   A CB     1 
ATOM   3818 C CG     . ASP   A 1 271 ? 37.36396  -63.65803 11.58443  1.000 185.78007 ? 272 ASP   A CG     1 
ATOM   3819 O OD1    . ASP   A 1 271 ? 36.57242  -64.28460 12.31866  1.000 181.38106 ? 272 ASP   A OD1    1 
ATOM   3820 O OD2    . ASP   A 1 271 ? 38.05083  -64.21073 10.69948  1.000 201.56456 ? 272 ASP   A OD2    1 
ATOM   3821 H H      . ASP   A 1 271 ? 35.06500  -62.06343 11.65826  1.000 173.22195 ? 272 ASP   A H      1 
ATOM   3822 H HA     . ASP   A 1 271 ? 36.67487  -62.17354 13.65146  1.000 185.33379 ? 272 ASP   A HA     1 
ATOM   3823 H HB2    . ASP   A 1 271 ? 37.28390  -61.72888 10.93314  1.000 208.06241 ? 272 ASP   A HB2    1 
ATOM   3824 H HB3    . ASP   A 1 271 ? 38.41771  -61.96930 12.02038  1.000 208.06241 ? 272 ASP   A HB3    1 
ATOM   3825 N N      . PHE   A 1 272 ? 36.50534  -59.22019 12.42960  1.000 139.57623 ? 273 PHE   A N      1 
ATOM   3826 C CA     . PHE   A 1 272 ? 36.82565  -57.82560 12.70861  1.000 151.78760 ? 273 PHE   A CA     1 
ATOM   3827 C C      . PHE   A 1 272 ? 36.14811  -57.35202 13.98853  1.000 157.32917 ? 273 PHE   A C      1 
ATOM   3828 O O      . PHE   A 1 272 ? 36.79000  -56.74804 14.85665  1.000 156.41602 ? 273 PHE   A O      1 
ATOM   3829 C CB     . PHE   A 1 272 ? 36.41294  -56.95283 11.52374  1.000 135.74925 ? 273 PHE   A CB     1 
ATOM   3830 C CG     . PHE   A 1 272 ? 36.45306  -55.48266 11.81358  1.000 135.69121 ? 273 PHE   A CG     1 
ATOM   3831 C CD1    . PHE   A 1 272 ? 37.64454  -54.78179 11.74570  1.000 140.83539 ? 273 PHE   A CD1    1 
ATOM   3832 C CD2    . PHE   A 1 272 ? 35.29772  -54.80028 12.15291  1.000 132.66935 ? 273 PHE   A CD2    1 
ATOM   3833 C CE1    . PHE   A 1 272 ? 37.68294  -53.42760 12.01308  1.000 149.25864 ? 273 PHE   A CE1    1 
ATOM   3834 C CE2    . PHE   A 1 272 ? 35.32991  -53.44653 12.42072  1.000 137.48580 ? 273 PHE   A CE2    1 
ATOM   3835 C CZ     . PHE   A 1 272 ? 36.52394  -52.75925 12.35072  1.000 142.01772 ? 273 PHE   A CZ     1 
ATOM   3836 H H      . PHE   A 1 272 ? 36.01733  -59.34277 11.73215  1.000 167.88194 ? 273 PHE   A H      1 
ATOM   3837 H HA     . PHE   A 1 272 ? 37.78438  -57.74026 12.82883  1.000 182.53559 ? 273 PHE   A HA     1 
ATOM   3838 H HB2    . PHE   A 1 272 ? 37.01643  -57.12533 10.78419  1.000 163.28957 ? 273 PHE   A HB2    1 
ATOM   3839 H HB3    . PHE   A 1 272 ? 35.50453  -57.17997 11.27057  1.000 163.28957 ? 273 PHE   A HB3    1 
ATOM   3840 H HD1    . PHE   A 1 272 ? 38.42803  -55.22783 11.51747  1.000 169.39294 ? 273 PHE   A HD1    1 
ATOM   3841 H HD2    . PHE   A 1 272 ? 34.49027  -55.25920 12.20104  1.000 159.59370 ? 273 PHE   A HD2    1 
ATOM   3842 H HE1    . PHE   A 1 272 ? 38.48917  -52.96648 11.96565  1.000 179.50084 ? 273 PHE   A HE1    1 
ATOM   3843 H HE2    . PHE   A 1 272 ? 34.54744  -52.99828 12.64811  1.000 165.37343 ? 273 PHE   A HE2    1 
ATOM   3844 H HZ     . PHE   A 1 272 ? 36.54772  -51.84715 12.53076  1.000 170.81173 ? 273 PHE   A HZ     1 
ATOM   3845 N N      . LEU   A 1 273 ? 34.84831  -57.62270 14.12668  1.000 139.83266 ? 274 LEU   A N      1 
ATOM   3846 C CA     . LEU   A 1 273 ? 34.11430  -57.12423 15.28457  1.000 147.88919 ? 274 LEU   A CA     1 
ATOM   3847 C C      . LEU   A 1 273 ? 34.56923  -57.80293 16.57077  1.000 165.78175 ? 274 LEU   A C      1 
ATOM   3848 O O      . LEU   A 1 273 ? 34.63635  -57.16036 17.62494  1.000 173.89808 ? 274 LEU   A O      1 
ATOM   3849 C CB     . LEU   A 1 273 ? 32.61470  -57.32208 15.07795  1.000 117.52685 ? 274 LEU   A CB     1 
ATOM   3850 C CG     . LEU   A 1 273 ? 31.96986  -56.39729 14.04606  1.000 122.39099 ? 274 LEU   A CG     1 
ATOM   3851 C CD1    . LEU   A 1 273 ? 30.50082  -56.73860 13.87444  1.000 124.22675 ? 274 LEU   A CD1    1 
ATOM   3852 C CD2    . LEU   A 1 273 ? 32.13643  -54.93941 14.44787  1.000 124.13320 ? 274 LEU   A CD2    1 
ATOM   3853 H H      . LEU   A 1 273 ? 34.37848  -58.08423 13.57364  1.000 168.18967 ? 274 LEU   A H      1 
ATOM   3854 H HA     . LEU   A 1 273 ? 34.28574  -56.17358 15.37276  1.000 177.85750 ? 274 LEU   A HA     1 
ATOM   3855 H HB2    . LEU   A 1 273 ? 32.46494  -58.23422 14.78388  1.000 141.42269 ? 274 LEU   A HB2    1 
ATOM   3856 H HB3    . LEU   A 1 273 ? 32.16717  -57.16882 15.92479  1.000 141.42269 ? 274 LEU   A HB3    1 
ATOM   3857 H HG     . LEU   A 1 273 ? 32.41274  -56.52248 13.19220  1.000 147.25965 ? 274 LEU   A HG     1 
ATOM   3858 H HD11   . LEU   A 1 273 ? 30.10860  -56.13020 13.22875  1.000 149.46258 ? 274 LEU   A HD11   1 
ATOM   3859 H HD12   . LEU   A 1 273 ? 30.42379  -57.65209 13.55741  1.000 149.46258 ? 274 LEU   A HD12   1 
ATOM   3860 H HD13   . LEU   A 1 273 ? 30.05318  -56.64655 14.73003  1.000 149.46258 ? 274 LEU   A HD13   1 
ATOM   3861 H HD21   . LEU   A 1 273 ? 31.51048  -54.39869 13.94120  1.000 149.35032 ? 274 LEU   A HD21   1 
ATOM   3862 H HD22   . LEU   A 1 273 ? 31.95713  -54.85097 15.39704  1.000 149.35032 ? 274 LEU   A HD22   1 
ATOM   3863 H HD23   . LEU   A 1 273 ? 33.04541  -54.66071 14.25557  1.000 149.35032 ? 274 LEU   A HD23   1 
ATOM   3864 N N      . LEU   A 1 274 ? 34.88546  -59.09813 16.50989  1.000 154.11919 ? 275 LEU   A N      1 
ATOM   3865 C CA     . LEU   A 1 274 ? 35.30151  -59.80027 17.71908  1.000 142.79339 ? 275 LEU   A CA     1 
ATOM   3866 C C      . LEU   A 1 274 ? 36.64139  -59.28733 18.23377  1.000 158.24605 ? 275 LEU   A C      1 
ATOM   3867 O O      . LEU   A 1 274 ? 36.89041  -59.32296 19.44417  1.000 165.12305 ? 275 LEU   A O      1 
ATOM   3868 C CB     . LEU   A 1 274 ? 35.36234  -61.30457 17.45748  1.000 138.12579 ? 275 LEU   A CB     1 
ATOM   3869 C CG     . LEU   A 1 274 ? 34.00508  -61.99110 17.27475  1.000 130.24331 ? 275 LEU   A CG     1 
ATOM   3870 C CD1    . LEU   A 1 274 ? 34.18844  -63.45327 16.90315  1.000 135.31379 ? 275 LEU   A CD1    1 
ATOM   3871 C CD2    . LEU   A 1 274 ? 33.15589  -61.86890 18.53048  1.000 130.87591 ? 275 LEU   A CD2    1 
ATOM   3872 H H      . LEU   A 1 274 ? 34.86730  -59.57993 15.79775  1.000 185.33350 ? 275 LEU   A H      1 
ATOM   3873 H HA     . LEU   A 1 274 ? 34.64140  -59.64813 18.41335  1.000 171.74254 ? 275 LEU   A HA     1 
ATOM   3874 H HB2    . LEU   A 1 274 ? 35.87447  -61.45318 16.64720  1.000 166.14142 ? 275 LEU   A HB2    1 
ATOM   3875 H HB3    . LEU   A 1 274 ? 35.80296  -61.72798 18.21079  1.000 166.14142 ? 275 LEU   A HB3    1 
ATOM   3876 H HG     . LEU   A 1 274 ? 33.53374  -61.54884 16.55147  1.000 156.68244 ? 275 LEU   A HG     1 
ATOM   3877 H HD11   . LEU   A 1 274 ? 33.31613  -63.86243 16.79114  1.000 162.76702 ? 275 LEU   A HD11   1 
ATOM   3878 H HD12   . LEU   A 1 274 ? 34.68845  -63.50803 16.07376  1.000 162.76702 ? 275 LEU   A HD12   1 
ATOM   3879 H HD13   . LEU   A 1 274 ? 34.67506  -63.90086 17.61292  1.000 162.76702 ? 275 LEU   A HD13   1 
ATOM   3880 H HD21   . LEU   A 1 274 ? 32.38709  -62.45489 18.45007  1.000 157.44157 ? 275 LEU   A HD21   1 
ATOM   3881 H HD22   . LEU   A 1 274 ? 33.68921  -62.12646 19.29867  1.000 157.44157 ? 275 LEU   A HD22   1 
ATOM   3882 H HD23   . LEU   A 1 274 ? 32.86235  -60.94922 18.62495  1.000 157.44157 ? 275 LEU   A HD23   1 
ATOM   3883 N N      . LYS   A 1 275 ? 37.51058  -58.80250 17.34302  1.000 151.94870 ? 276 LYS   A N      1 
ATOM   3884 C CA     . LYS   A 1 275 ? 38.76153  -58.20222 17.79618  1.000 170.19747 ? 276 LYS   A CA     1 
ATOM   3885 C C      . LYS   A 1 275 ? 38.50662  -56.88784 18.52408  1.000 169.84078 ? 276 LYS   A C      1 
ATOM   3886 O O      . LYS   A 1 275 ? 39.09479  -56.63241 19.58151  1.000 171.77951 ? 276 LYS   A O      1 
ATOM   3887 C CB     . LYS   A 1 275 ? 39.70312  -57.98522 16.61263  1.000 170.02818 ? 276 LYS   A CB     1 
ATOM   3888 C CG     . LYS   A 1 275 ? 40.40271  -59.24774 16.13987  1.000 159.45709 ? 276 LYS   A CG     1 
ATOM   3889 C CD     . LYS   A 1 275 ? 41.30511  -58.96528 14.95162  1.000 151.00612 ? 276 LYS   A CD     1 
ATOM   3890 C CE     . LYS   A 1 275 ? 41.88650  -60.24644 14.38218  1.000 154.43902 ? 276 LYS   A CE     1 
ATOM   3891 N NZ     . LYS   A 1 275 ? 42.42062  -60.04392 13.00802  1.000 175.30604 ? 276 LYS   A NZ     1 
ATOM   3892 H H      . LYS   A 1 275 ? 37.40071  -58.80953 16.49010  1.000 182.72891 ? 276 LYS   A H      1 
ATOM   3893 H HA     . LYS   A 1 275 ? 39.19471  -58.81243 18.41335  1.000 204.62743 ? 276 LYS   A HA     1 
ATOM   3894 H HB2    . LYS   A 1 275 ? 39.19010  -57.63547 15.86738  1.000 204.42429 ? 276 LYS   A HB2    1 
ATOM   3895 H HB3    . LYS   A 1 275 ? 40.38720  -57.34845 16.87236  1.000 204.42429 ? 276 LYS   A HB3    1 
ATOM   3896 H HG2    . LYS   A 1 275 ? 40.94713  -59.60323 16.85969  1.000 191.73898 ? 276 LYS   A HG2    1 
ATOM   3897 H HG3    . LYS   A 1 275 ? 39.73927  -59.90242 15.87128  1.000 191.73898 ? 276 LYS   A HG3    1 
ATOM   3898 H HD2    . LYS   A 1 275 ? 40.79211  -58.52658 14.25500  1.000 181.59782 ? 276 LYS   A HD2    1 
ATOM   3899 H HD3    . LYS   A 1 275 ? 42.03821  -58.39556 15.23249  1.000 181.59782 ? 276 LYS   A HD3    1 
ATOM   3900 H HE2    . LYS   A 1 275 ? 42.61285  -60.54873 14.94958  1.000 185.71730 ? 276 LYS   A HE2    1 
ATOM   3901 H HE3    . LYS   A 1 275 ? 41.19282  -60.92328 14.34243  1.000 185.71730 ? 276 LYS   A HE3    1 
ATOM   3902 H HZ1    . LYS   A 1 275 ? 42.76346  -60.80507 12.69945  1.000 210.75772 ? 276 LYS   A HZ1    1 
ATOM   3903 H HZ2    . LYS   A 1 275 ? 41.76803  -59.77946 12.46369  1.000 210.75772 ? 276 LYS   A HZ2    1 
ATOM   3904 H HZ3    . LYS   A 1 275 ? 43.05813  -59.42295 13.01767  1.000 210.75772 ? 276 LYS   A HZ3    1 
ATOM   3905 N N      . LYS   A 1 276 ? 37.63210  -56.04212 17.97400  1.000 156.61265 ? 277 LYS   A N      1 
ATOM   3906 C CA     . LYS   A 1 276 ? 37.28411  -54.79765 18.65022  1.000 156.05824 ? 277 LYS   A CA     1 
ATOM   3907 C C      . LYS   A 1 276 ? 36.52726  -55.06581 19.94482  1.000 171.54426 ? 277 LYS   A C      1 
ATOM   3908 O O      . LYS   A 1 276 ? 36.71900  -54.35934 20.94163  1.000 185.89155 ? 277 LYS   A O      1 
ATOM   3909 C CB     . LYS   A 1 276 ? 36.45036  -53.91281 17.72476  1.000 146.34811 ? 277 LYS   A CB     1 
ATOM   3910 C CG     . LYS   A 1 276 ? 37.26213  -52.96095 16.86527  1.000 174.88030 ? 277 LYS   A CG     1 
ATOM   3911 C CD     . LYS   A 1 276 ? 36.35258  -52.04579 16.05516  1.000 151.19325 ? 277 LYS   A CD     1 
ATOM   3912 C CE     . LYS   A 1 276 ? 37.12734  -50.90615 15.41012  1.000 166.85957 ? 277 LYS   A CE     1 
ATOM   3913 N NZ     . LYS   A 1 276 ? 37.65473  -49.94521 16.42429  1.000 224.36017 ? 277 LYS   A NZ     1 
ATOM   3914 H H      . LYS   A 1 276 ? 37.23356  -56.16527 17.22194  1.000 188.32565 ? 277 LYS   A H      1 
ATOM   3915 H HA     . LYS   A 1 276 ? 38.10208  -54.32398 18.86809  1.000 187.66036 ? 277 LYS   A HA     1 
ATOM   3916 H HB2    . LYS   A 1 276 ? 35.94025  -54.48328 17.12874  1.000 176.00820 ? 277 LYS   A HB2    1 
ATOM   3917 H HB3    . LYS   A 1 276 ? 35.84961  -53.37811 18.26706  1.000 176.00820 ? 277 LYS   A HB3    1 
ATOM   3918 H HG2    . LYS   A 1 276 ? 37.82333  -52.41081 17.43386  1.000 210.24683 ? 277 LYS   A HG2    1 
ATOM   3919 H HG3    . LYS   A 1 276 ? 37.81194  -53.47044 16.24961  1.000 210.24683 ? 277 LYS   A HG3    1 
ATOM   3920 H HD2    . LYS   A 1 276 ? 35.92616  -52.55950 15.35149  1.000 181.82237 ? 277 LYS   A HD2    1 
ATOM   3921 H HD3    . LYS   A 1 276 ? 35.68036  -51.66291 16.64033  1.000 181.82237 ? 277 LYS   A HD3    1 
ATOM   3922 H HE2    . LYS   A 1 276 ? 37.87950  -51.26997 14.91738  1.000 200.62196 ? 277 LYS   A HE2    1 
ATOM   3923 H HE3    . LYS   A 1 276 ? 36.54053  -50.42093 14.80919  1.000 200.62196 ? 277 LYS   A HE3    1 
ATOM   3924 H HZ1    . LYS   A 1 276 ? 37.99309  -49.22921 16.01814  1.000 269.62267 ? 277 LYS   A HZ1    1 
ATOM   3925 H HZ2    . LYS   A 1 276 ? 36.99935  -49.68617 16.96788  1.000 269.62267 ? 277 LYS   A HZ2    1 
ATOM   3926 H HZ3    . LYS   A 1 276 ? 38.29424  -50.33261 16.90703  1.000 269.62267 ? 277 LYS   A HZ3    1 
ATOM   3927 N N      . PHE   A 1 277 ? 35.66394  -56.08111 19.94972  1.000 163.32333 ? 278 PHE   A N      1 
ATOM   3928 C CA     . PHE   A 1 277 ? 34.83196  -56.40088 21.10093  1.000 166.60088 ? 278 PHE   A CA     1 
ATOM   3929 C C      . PHE   A 1 277 ? 35.42506  -57.51138 21.96191  1.000 165.75016 ? 278 PHE   A C      1 
ATOM   3930 O O      . PHE   A 1 277 ? 34.69691  -58.14826 22.73113  1.000 160.79100 ? 278 PHE   A O      1 
ATOM   3931 C CB     . PHE   A 1 277 ? 33.42539  -56.78151 20.63381  1.000 161.70515 ? 278 PHE   A CB     1 
ATOM   3932 C CG     . PHE   A 1 277 ? 32.53795  -55.59926 20.36041  1.000 155.40411 ? 278 PHE   A CG     1 
ATOM   3933 C CD1    . PHE   A 1 277 ? 32.91770  -54.62201 19.45464  1.000 154.30032 ? 278 PHE   A CD1    1 
ATOM   3934 C CD2    . PHE   A 1 277 ? 31.32091  -55.46754 21.00819  1.000 149.72987 ? 278 PHE   A CD2    1 
ATOM   3935 C CE1    . PHE   A 1 277 ? 32.10128  -53.53317 19.20524  1.000 151.88597 ? 278 PHE   A CE1    1 
ATOM   3936 C CE2    . PHE   A 1 277 ? 30.50034  -54.38211 20.76141  1.000 141.87814 ? 278 PHE   A CE2    1 
ATOM   3937 C CZ     . PHE   A 1 277 ? 30.89109  -53.41439 19.85955  1.000 143.04386 ? 278 PHE   A CZ     1 
ATOM   3938 H H      . PHE   A 1 277 ? 35.54215  -56.60863 19.28153  1.000 196.37847 ? 278 PHE   A H      1 
ATOM   3939 H HA     . PHE   A 1 277 ? 34.76100  -55.61068 21.65901  1.000 200.31153 ? 278 PHE   A HA     1 
ATOM   3940 H HB2    . PHE   A 1 277 ? 33.49715  -57.29394 19.81334  1.000 194.43665 ? 278 PHE   A HB2    1 
ATOM   3941 H HB3    . PHE   A 1 277 ? 33.00186  -57.31658 21.32317  1.000 194.43665 ? 278 PHE   A HB3    1 
ATOM   3942 H HD1    . PHE   A 1 277 ? 33.73051  -54.69879 19.00929  1.000 185.55086 ? 278 PHE   A HD1    1 
ATOM   3943 H HD2    . PHE   A 1 277 ? 31.05209  -56.11730 21.61684  1.000 180.06631 ? 278 PHE   A HD2    1 
ATOM   3944 H HE1    . PHE   A 1 277 ? 32.36740  -52.88166 18.59728  1.000 182.65364 ? 278 PHE   A HE1    1 
ATOM   3945 H HE2    . PHE   A 1 277 ? 29.68565  -54.30469 21.20320  1.000 170.64424 ? 278 PHE   A HE2    1 
ATOM   3946 H HZ     . PHE   A 1 277 ? 30.34074  -52.68356 19.69253  1.000 172.04311 ? 278 PHE   A HZ     1 
ATOM   3947 N N      . SER   A 1 278 ? 36.73371  -57.75023 21.85733  1.000 167.51294 ? 279 SER   A N      1 
ATOM   3948 C CA     . SER   A 1 278 ? 37.35595  -58.78484 22.67611  1.000 180.36234 ? 279 SER   A CA     1 
ATOM   3949 C C      . SER   A 1 278 ? 37.15126  -58.50622 24.16043  1.000 184.97192 ? 279 SER   A C      1 
ATOM   3950 O O      . SER   A 1 278 ? 36.97152  -59.43586 24.95611  1.000 181.62944 ? 279 SER   A O      1 
ATOM   3951 C CB     . SER   A 1 278 ? 38.84608  -58.88479 22.35088  1.000 178.59036 ? 279 SER   A CB     1 
ATOM   3952 O OG     . SER   A 1 278 ? 39.54294  -57.73102 22.78825  1.000 182.00625 ? 279 SER   A OG     1 
ATOM   3953 H H      . SER   A 1 278 ? 37.27146  -57.33487 21.33016  1.000 201.40600 ? 279 SER   A H      1 
ATOM   3954 H HA     . SER   A 1 278 ? 36.94497  -59.63868 22.46885  1.000 216.82528 ? 279 SER   A HA     1 
ATOM   3955 H HB2    . SER   A 1 278 ? 39.21415  -59.66298 22.79793  1.000 214.69890 ? 279 SER   A HB2    1 
ATOM   3956 H HB3    . SER   A 1 278 ? 38.95338  -58.97206 21.39079  1.000 214.69890 ? 279 SER   A HB3    1 
ATOM   3957 H HG     . SER   A 1 278 ? 40.36776  -57.82883 22.66293  1.000 218.79797 ? 279 SER   A HG     1 
ATOM   3958 N N      . ASP   A 1 279 ? 37.16852  -57.22971 24.55102  1.000 181.56925 ? 280 ASP   A N      1 
ATOM   3959 C CA     . ASP   A 1 279 ? 36.99874  -56.85838 25.94985  1.000 187.73525 ? 280 ASP   A CA     1 
ATOM   3960 C C      . ASP   A 1 279 ? 35.56175  -56.99297 26.43575  1.000 184.19548 ? 280 ASP   A C      1 
ATOM   3961 O O      . ASP   A 1 279 ? 35.32887  -56.91307 27.64658  1.000 187.34379 ? 280 ASP   A O      1 
ATOM   3962 C CB     . ASP   A 1 279 ? 37.46461  -55.41600 26.16936  1.000 186.13437 ? 280 ASP   A CB     1 
ATOM   3963 C CG     . ASP   A 1 279 ? 38.97396  -55.29131 26.23925  1.000 187.74815 ? 280 ASP   A CG     1 
ATOM   3964 O OD1    . ASP   A 1 279 ? 39.66824  -56.31641 26.07537  1.000 186.93651 ? 280 ASP   A OD1    1 
ATOM   3965 O OD2    . ASP   A 1 279 ? 39.46676  -54.16535 26.46319  1.000 183.71436 ? 280 ASP   A OD2    1 
ATOM   3966 H H      . ASP   A 1 279 ? 37.27741  -56.56078 24.02161  1.000 218.27357 ? 280 ASP   A H      1 
ATOM   3967 H HA     . ASP   A 1 279 ? 37.55246  -57.44765 26.48562  1.000 225.67277 ? 280 ASP   A HA     1 
ATOM   3968 H HB2    . ASP   A 1 279 ? 37.15213  -54.86738 25.43297  1.000 223.75172 ? 280 ASP   A HB2    1 
ATOM   3969 H HB3    . ASP   A 1 279 ? 37.09762  -55.08911 27.00564  1.000 223.75172 ? 280 ASP   A HB3    1 
ATOM   3970 N N      . TRP   A 1 280 ? 34.60416  -57.19536 25.53911  1.000 180.17125 ? 281 TRP   A N      1 
ATOM   3971 C CA     . TRP   A 1 280 ? 33.19606  -57.15673 25.90069  1.000 171.78841 ? 281 TRP   A CA     1 
ATOM   3972 C C      . TRP   A 1 280 ? 32.71569  -58.51986 26.38994  1.000 164.07569 ? 281 TRP   A C      1 
ATOM   3973 O O      . TRP   A 1 280 ? 33.31004  -59.56214 26.10403  1.000 158.95844 ? 281 TRP   A O      1 
ATOM   3974 C CB     . TRP   A 1 280 ? 32.35679  -56.69099 24.70944  1.000 161.07369 ? 281 TRP   A CB     1 
ATOM   3975 C CG     . TRP   A 1 280 ? 32.59517  -55.25391 24.34200  1.000 153.82595 ? 281 TRP   A CG     1 
ATOM   3976 C CD1    . TRP   A 1 280 ? 33.78588  -54.68273 23.99663  1.000 158.70938 ? 281 TRP   A CD1    1 
ATOM   3977 C CD2    . TRP   A 1 280 ? 31.61696  -54.20862 24.27827  1.000 143.15238 ? 281 TRP   A CD2    1 
ATOM   3978 N NE1    . TRP   A 1 280 ? 33.61079  -53.34808 23.72475  1.000 158.48313 ? 281 TRP   A NE1    1 
ATOM   3979 C CE2    . TRP   A 1 280 ? 32.28808  -53.03205 23.88983  1.000 146.50603 ? 281 TRP   A CE2    1 
ATOM   3980 C CE3    . TRP   A 1 280 ? 30.23971  -54.15321 24.51201  1.000 144.06902 ? 281 TRP   A CE3    1 
ATOM   3981 C CZ2    . TRP   A 1 280 ? 31.62972  -51.81553 23.73045  1.000 146.45151 ? 281 TRP   A CZ2    1 
ATOM   3982 C CZ3    . TRP   A 1 280 ? 29.58804  -52.94334 24.35319  1.000 141.32456 ? 281 TRP   A CZ3    1 
ATOM   3983 C CH2    . TRP   A 1 280 ? 30.28328  -51.79160 23.96647  1.000 141.37593 ? 281 TRP   A CH2    1 
ATOM   3984 H H      . TRP   A 1 280 ? 34.74721  -57.35849 24.70693  1.000 216.59597 ? 281 TRP   A H      1 
ATOM   3985 H HA     . TRP   A 1 280 ? 33.06967  -56.52677 26.62738  1.000 206.53656 ? 281 TRP   A HA     1 
ATOM   3986 H HB2    . TRP   A 1 280 ? 32.57675  -57.23643 23.93807  1.000 193.67890 ? 281 TRP   A HB2    1 
ATOM   3987 H HB3    . TRP   A 1 280 ? 31.41729  -56.79068 24.92921  1.000 193.67890 ? 281 TRP   A HB3    1 
ATOM   3988 H HD1    . TRP   A 1 280 ? 34.59860  -55.13262 23.95190  1.000 190.84172 ? 281 TRP   A HD1    1 
ATOM   3989 H HE1    . TRP   A 1 280 ? 34.23036  -52.80010 23.48929  1.000 190.57023 ? 281 TRP   A HE1    1 
ATOM   3990 H HE3    . TRP   A 1 280 ? 29.77114  -54.91431 24.76907  1.000 173.27329 ? 281 TRP   A HE3    1 
ATOM   3991 H HZ2    . TRP   A 1 280 ? 32.08841  -51.04849 23.47324  1.000 176.13228 ? 281 TRP   A HZ2    1 
ATOM   3992 H HZ3    . TRP   A 1 280 ? 28.67199  -52.89431 24.50602  1.000 169.97994 ? 281 TRP   A HZ3    1 
ATOM   3993 H HH2    . TRP   A 1 280 ? 29.81876  -50.99198 23.86786  1.000 170.04158 ? 281 TRP   A HH2    1 
ATOM   3994 N N      . ASP   A 1 281 ? 31.62079  -58.49351 27.14531  1.000 158.86585 ? 282 ASP   A N      1 
ATOM   3995 C CA     . ASP   A 1 281 ? 31.07198  -59.70585 27.73331  1.000 156.72418 ? 282 ASP   A CA     1 
ATOM   3996 C C      . ASP   A 1 281 ? 30.64467  -60.68344 26.64107  1.000 152.28407 ? 282 ASP   A C      1 
ATOM   3997 O O      . ASP   A 1 281 ? 30.34870  -60.30242 25.50751  1.000 155.33752 ? 282 ASP   A O      1 
ATOM   3998 C CB     . ASP   A 1 281 ? 29.89139  -59.35610 28.64096  1.000 163.55176 ? 282 ASP   A CB     1 
ATOM   3999 C CG     . ASP   A 1 281 ? 29.26679  -60.57570 29.29206  1.000 169.65091 ? 282 ASP   A CG     1 
ATOM   4000 O OD1    . ASP   A 1 281 ? 28.61931  -61.36996 28.57735  1.000 176.39513 ? 282 ASP   A OD1    1 
ATOM   4001 O OD2    . ASP   A 1 281 ? 29.43023  -60.74401 30.51918  1.000 158.00822 ? 282 ASP   A OD2    1 
ATOM   4002 H H      . ASP   A 1 281 ? 31.17596  -57.78167 27.33242  1.000 191.02949 ? 282 ASP   A H      1 
ATOM   4003 H HA     . ASP   A 1 281 ? 31.74502  -60.14768 28.27433  1.000 188.45949 ? 282 ASP   A HA     1 
ATOM   4004 H HB2    . ASP   A 1 281 ? 30.19932  -58.76504 29.34575  1.000 196.65258 ? 282 ASP   A HB2    1 
ATOM   4005 H HB3    . ASP   A 1 281 ? 29.20737  -58.91499 28.11329  1.000 196.65258 ? 282 ASP   A HB3    1 
ATOM   4006 N N      . GLU   A 1 282 ? 30.62103  -61.97112 27.00349  1.000 156.03513 ? 283 GLU   A N      1 
ATOM   4007 C CA     . GLU   A 1 282 ? 30.28526  -63.01322 26.03764  1.000 154.95406 ? 283 GLU   A CA     1 
ATOM   4008 C C      . GLU   A 1 282 ? 28.89525  -62.81418 25.44576  1.000 148.26364 ? 283 GLU   A C      1 
ATOM   4009 O O      . GLU   A 1 282 ? 28.65338  -63.19481 24.29439  1.000 140.89466 ? 283 GLU   A O      1 
ATOM   4010 C CB     . GLU   A 1 282 ? 30.38245  -64.38819 26.70240  1.000 160.46898 ? 283 GLU   A CB     1 
ATOM   4011 C CG     . GLU   A 1 282 ? 30.15625  -65.56237 25.75917  1.000 175.54506 ? 283 GLU   A CG     1 
ATOM   4012 C CD     . GLU   A 1 282 ? 31.29823  -65.75371 24.77901  1.000 186.42219 ? 283 GLU   A CD     1 
ATOM   4013 O OE1    . GLU   A 1 282 ? 32.38558  -65.18386 25.00977  1.000 171.52328 ? 283 GLU   A OE1    1 
ATOM   4014 O OE2    . GLU   A 1 282 ? 31.10850  -66.47288 23.77524  1.000 186.19209 ? 283 GLU   A OE2    1 
ATOM   4015 H H      . GLU   A 1 282 ? 30.79394  -62.26184 27.79417  1.000 187.63262 ? 283 GLU   A H      1 
ATOM   4016 H HA     . GLU   A 1 282 ? 30.92541  -62.97817 25.30971  1.000 186.33534 ? 283 GLU   A HA     1 
ATOM   4017 H HB2    . GLU   A 1 282 ? 31.26909  -64.48512 27.08368  1.000 192.95324 ? 283 GLU   A HB2    1 
ATOM   4018 H HB3    . GLU   A 1 282 ? 29.71280  -64.44115 27.40216  1.000 192.95324 ? 283 GLU   A HB3    1 
ATOM   4019 H HG2    . GLU   A 1 282 ? 30.06917  -66.37530 26.28115  1.000 211.04454 ? 283 GLU   A HG2    1 
ATOM   4020 H HG3    . GLU   A 1 282 ? 29.34579  -65.40706 25.24933  1.000 211.04454 ? 283 GLU   A HG3    1 
ATOM   4021 N N      . ARG   A 1 283 ? 27.96722  -62.23778 26.21354  1.000 145.57997 ? 284 ARG   A N      1 
ATOM   4022 C CA     . ARG   A 1 283 ? 26.63003  -61.98604 25.68493  1.000 156.20706 ? 284 ARG   A CA     1 
ATOM   4023 C C      . ARG   A 1 283 ? 26.68732  -61.10556 24.44303  1.000 154.22230 ? 284 ARG   A C      1 
ATOM   4024 O O      . ARG   A 1 283 ? 25.91808  -61.30582 23.49479  1.000 136.08955 ? 284 ARG   A O      1 
ATOM   4025 C CB     . ARG   A 1 283 ? 25.75412  -61.34481 26.76006  1.000 161.97759 ? 284 ARG   A CB     1 
ATOM   4026 C CG     . ARG   A 1 283 ? 25.19047  -62.33626 27.76632  1.000 151.06199 ? 284 ARG   A CG     1 
ATOM   4027 C CD     . ARG   A 1 283 ? 24.54014  -61.62863 28.94280  1.000 144.70420 ? 284 ARG   A CD     1 
ATOM   4028 N NE     . ARG   A 1 283 ? 25.53158  -61.06658 29.85255  1.000 154.16122 ? 284 ARG   A NE     1 
ATOM   4029 C CZ     . ARG   A 1 283 ? 25.24147  -60.38384 30.95193  1.000 167.26861 ? 284 ARG   A CZ     1 
ATOM   4030 N NH1    . ARG   A 1 283 ? 23.98979  -60.14343 31.30719  1.000 172.66912 ? 284 ARG   A NH1    1 
ATOM   4031 N NH2    . ARG   A 1 283 ? 26.23258  -59.93142 31.71462  1.000 158.44672 ? 284 ARG   A NH2    1 
ATOM   4032 H H      . ARG   A 1 283 ? 28.08547  -61.98826 27.02801  1.000 175.08643 ? 284 ARG   A H      1 
ATOM   4033 H HA     . ARG   A 1 283 ? 26.22628  -62.83194 25.43522  1.000 187.83894 ? 284 ARG   A HA     1 
ATOM   4034 H HB2    . ARG   A 1 283 ? 26.28531  -60.69696 27.24896  1.000 194.76358 ? 284 ARG   A HB2    1 
ATOM   4035 H HB3    . ARG   A 1 283 ? 25.00575  -60.90288 26.32933  1.000 194.76358 ? 284 ARG   A HB3    1 
ATOM   4036 H HG2    . ARG   A 1 283 ? 24.51953  -62.88691 27.33329  1.000 181.66486 ? 284 ARG   A HG2    1 
ATOM   4037 H HG3    . ARG   A 1 283 ? 25.90868  -62.89334 28.10506  1.000 181.66486 ? 284 ARG   A HG3    1 
ATOM   4038 H HD2    . ARG   A 1 283 ? 23.98508  -60.90450 28.61347  1.000 174.03551 ? 284 ARG   A HD2    1 
ATOM   4039 H HD3    . ARG   A 1 283 ? 23.99856  -62.26294 29.43802  1.000 174.03551 ? 284 ARG   A HD3    1 
ATOM   4040 H HE     . ARG   A 1 283 ? 26.36189  -61.18612 29.66307  1.000 185.38393 ? 284 ARG   A HE     1 
ATOM   4041 H HH11   . ARG   A 1 283 ? 23.34180  -60.43210 30.82100  1.000 207.59342 ? 284 ARG   A HH11   1 
ATOM   4042 H HH12   . ARG   A 1 283 ? 23.82422  -59.69850 32.02428  1.000 207.59342 ? 284 ARG   A HH12   1 
ATOM   4043 H HH21   . ARG   A 1 283 ? 27.04952  -60.08280 31.49261  1.000 190.52653 ? 284 ARG   A HH21   1 
ATOM   4044 H HH22   . ARG   A 1 283 ? 26.05655  -59.48748 32.42984  1.000 190.52653 ? 284 ARG   A HH22   1 
ATOM   4045 N N      . TYR   A 1 284 ? 27.58881  -60.12110 24.43084  1.000 151.61017 ? 285 TYR   A N      1 
ATOM   4046 C CA     . TYR   A 1 284 ? 27.79730  -59.32805 23.22477  1.000 140.46454 ? 285 TYR   A CA     1 
ATOM   4047 C C      . TYR   A 1 284 ? 28.44267  -60.16582 22.12804  1.000 136.54155 ? 285 TYR   A C      1 
ATOM   4048 O O      . TYR   A 1 284 ? 28.02493  -60.11346 20.96674  1.000 139.02617 ? 285 TYR   A O      1 
ATOM   4049 C CB     . TYR   A 1 284 ? 28.65856  -58.10537 23.53414  1.000 146.17569 ? 285 TYR   A CB     1 
ATOM   4050 C CG     . TYR   A 1 284 ? 28.03989  -57.14119 24.51859  1.000 147.64837 ? 285 TYR   A CG     1 
ATOM   4051 C CD1    . TYR   A 1 284 ? 27.05369  -56.24934 24.12037  1.000 146.00377 ? 285 TYR   A CD1    1 
ATOM   4052 C CD2    . TYR   A 1 284 ? 28.45242  -57.11225 25.84350  1.000 155.48523 ? 285 TYR   A CD2    1 
ATOM   4053 C CE1    . TYR   A 1 284 ? 26.48932  -55.36172 25.01595  1.000 146.36034 ? 285 TYR   A CE1    1 
ATOM   4054 C CE2    . TYR   A 1 284 ? 27.89454  -56.22781 26.74647  1.000 154.07379 ? 285 TYR   A CE2    1 
ATOM   4055 C CZ     . TYR   A 1 284 ? 26.91410  -55.35459 26.32731  1.000 147.26345 ? 285 TYR   A CZ     1 
ATOM   4056 O OH     . TYR   A 1 284 ? 26.35558  -54.47173 27.22248  1.000 142.78318 ? 285 TYR   A OH     1 
ATOM   4057 H H      . TYR   A 1 284 ? 28.08348  -59.89744 25.09783  1.000 182.32267 ? 285 TYR   A H      1 
ATOM   4058 H HA     . TYR   A 1 284 ? 26.93549  -59.01528 22.90799  1.000 168.94792 ? 285 TYR   A HA     1 
ATOM   4059 H HB2    . TYR   A 1 284 ? 29.50112  -58.40685 23.90842  1.000 175.80129 ? 285 TYR   A HB2    1 
ATOM   4060 H HB3    . TYR   A 1 284 ? 28.81659  -57.62110 22.70866  1.000 175.80129 ? 285 TYR   A HB3    1 
ATOM   4061 H HD1    . TYR   A 1 284 ? 26.76791  -56.24931 23.23536  1.000 175.59500 ? 285 TYR   A HD1    1 
ATOM   4062 H HD2    . TYR   A 1 284 ? 29.11589  -57.69838 26.12839  1.000 186.97275 ? 285 TYR   A HD2    1 
ATOM   4063 H HE1    . TYR   A 1 284 ? 25.82666  -54.77242 24.73575  1.000 176.02288 ? 285 TYR   A HE1    1 
ATOM   4064 H HE2    . TYR   A 1 284 ? 28.17891  -56.22173 27.63190  1.000 185.27902 ? 285 TYR   A HE2    1 
ATOM   4065 H HH     . TYR   A 1 284 ? 26.76244  -54.51072 27.95634  1.000 171.73029 ? 285 TYR   A HH     1 
ATOM   4066 N N      . LYS   A 1 285 ? 29.47481  -60.94066 22.47743  1.000 141.05184 ? 286 LYS   A N      1 
ATOM   4067 C CA     . LYS   A 1 285 ? 30.08647  -61.83345 21.49843  1.000 141.07958 ? 286 LYS   A CA     1 
ATOM   4068 C C      . LYS   A 1 285 ? 29.04625  -62.76578 20.89197  1.000 145.29462 ? 286 LYS   A C      1 
ATOM   4069 O O      . LYS   A 1 285 ? 29.06541  -63.02824 19.68442  1.000 136.72115 ? 286 LYS   A O      1 
ATOM   4070 C CB     . LYS   A 1 285 ? 31.21743  -62.63204 22.14846  1.000 147.76373 ? 286 LYS   A CB     1 
ATOM   4071 C CG     . LYS   A 1 285 ? 32.41104  -61.78100 22.55832  1.000 148.83143 ? 286 LYS   A CG     1 
ATOM   4072 C CD     . LYS   A 1 285 ? 33.48308  -62.59833 23.26395  1.000 149.31541 ? 286 LYS   A CD     1 
ATOM   4073 C CE     . LYS   A 1 285 ? 34.57524  -61.69826 23.82448  1.000 163.16803 ? 286 LYS   A CE     1 
ATOM   4074 N NZ     . LYS   A 1 285 ? 35.67225  -62.46716 24.47509  1.000 172.35358 ? 286 LYS   A NZ     1 
ATOM   4075 H H      . LYS   A 1 285 ? 29.83079  -60.96587 23.25990  1.000 169.65267 ? 286 LYS   A H      1 
ATOM   4076 H HA     . LYS   A 1 285 ? 30.47242  -61.30379 20.78331  1.000 169.68597 ? 286 LYS   A HA     1 
ATOM   4077 H HB2    . LYS   A 1 285 ? 30.87491  -63.06554 22.94575  1.000 177.70694 ? 286 LYS   A HB2    1 
ATOM   4078 H HB3    . LYS   A 1 285 ? 31.53142  -63.29843 21.51740  1.000 177.70694 ? 286 LYS   A HB3    1 
ATOM   4079 H HG2    . LYS   A 1 285 ? 32.80626  -61.38375 21.76656  1.000 178.98819 ? 286 LYS   A HG2    1 
ATOM   4080 H HG3    . LYS   A 1 285 ? 32.11323  -61.08532 23.16515  1.000 178.98819 ? 286 LYS   A HG3    1 
ATOM   4081 H HD2    . LYS   A 1 285 ? 33.08347  -63.08988 23.99851  1.000 179.56897 ? 286 LYS   A HD2    1 
ATOM   4082 H HD3    . LYS   A 1 285 ? 33.88702  -63.21465 22.63317  1.000 179.56897 ? 286 LYS   A HD3    1 
ATOM   4083 H HE2    . LYS   A 1 285 ? 34.96025  -61.17900 23.10127  1.000 196.19210 ? 286 LYS   A HE2    1 
ATOM   4084 H HE3    . LYS   A 1 285 ? 34.18842  -61.10636 24.48850  1.000 196.19210 ? 286 LYS   A HE3    1 
ATOM   4085 H HZ1    . LYS   A 1 285 ? 36.30712  -61.91139 24.75821  1.000 207.21477 ? 286 LYS   A HZ1    1 
ATOM   4086 H HZ2    . LYS   A 1 285 ? 35.35428  -62.92119 25.17141  1.000 207.21477 ? 286 LYS   A HZ2    1 
ATOM   4087 H HZ3    . LYS   A 1 285 ? 36.02800  -63.04038 23.89461  1.000 207.21477 ? 286 LYS   A HZ3    1 
ATOM   4088 N N      . GLU   A 1 286 ? 28.11906  -63.26462 21.71300  1.000 157.70125 ? 287 GLU   A N      1 
ATOM   4089 C CA     . GLU   A 1 286 ? 27.04044  -64.09555 21.18841  1.000 148.57022 ? 287 GLU   A CA     1 
ATOM   4090 C C      . GLU   A 1 286 ? 26.22270  -63.34034 20.14853  1.000 141.40791 ? 287 GLU   A C      1 
ATOM   4091 O O      . GLU   A 1 286 ? 25.82594  -63.91006 19.12546  1.000 147.11792 ? 287 GLU   A O      1 
ATOM   4092 C CB     . GLU   A 1 286 ? 26.14263  -64.57009 22.33144  1.000 159.68379 ? 287 GLU   A CB     1 
ATOM   4093 C CG     . GLU   A 1 286 ? 24.95359  -65.41076 21.88589  1.000 165.48639 ? 287 GLU   A CG     1 
ATOM   4094 C CD     . GLU   A 1 286 ? 24.17633  -65.98659 23.05634  1.000 172.59045 ? 287 GLU   A CD     1 
ATOM   4095 O OE1    . GLU   A 1 286 ? 24.26223  -65.41965 24.16685  1.000 151.49027 ? 287 GLU   A OE1    1 
ATOM   4096 O OE2    . GLU   A 1 286 ? 23.48481  -67.00995 22.86732  1.000 176.30033 ? 287 GLU   A OE2    1 
ATOM   4097 H H      . GLU   A 1 286 ? 28.09374  -63.13803 22.56326  1.000 189.63197 ? 287 GLU   A H      1 
ATOM   4098 H HA     . GLU   A 1 286 ? 27.42532  -64.87722 20.76209  1.000 178.67474 ? 287 GLU   A HA     1 
ATOM   4099 H HB2    . GLU   A 1 286 ? 26.67305  -65.10958 22.93848  1.000 192.01102 ? 287 GLU   A HB2    1 
ATOM   4100 H HB3    . GLU   A 1 286 ? 25.79531  -63.79252 22.79583  1.000 192.01102 ? 287 GLU   A HB3    1 
ATOM   4101 H HG2    . GLU   A 1 286 ? 24.34979  -64.85609 21.36756  1.000 198.97413 ? 287 GLU   A HG2    1 
ATOM   4102 H HG3    . GLU   A 1 286 ? 25.27292  -66.14942 21.34431  1.000 198.97413 ? 287 GLU   A HG3    1 
ATOM   4103 N N      . LEU   A 1 287 ? 25.95597  -62.05598 20.39594  1.000 141.52240 ? 288 LEU   A N      1 
ATOM   4104 C CA     . LEU   A 1 287 ? 25.18667  -61.26144 19.44323  1.000 131.74396 ? 288 LEU   A CA     1 
ATOM   4105 C C      . LEU   A 1 287 ? 25.87600  -61.20874 18.08399  1.000 130.72338 ? 288 LEU   A C      1 
ATOM   4106 O O      . LEU   A 1 287 ? 25.22926  -61.37465 17.04275  1.000 123.68554 ? 288 LEU   A O      1 
ATOM   4107 C CB     . LEU   A 1 287 ? 24.97995  -59.85175 19.99970  1.000 121.14286 ? 288 LEU   A CB     1 
ATOM   4108 C CG     . LEU   A 1 287 ? 24.18538  -58.86721 19.14185  1.000 106.27597 ? 288 LEU   A CG     1 
ATOM   4109 C CD1    . LEU   A 1 287 ? 22.73266  -59.29312 19.02403  1.000 105.21580 ? 288 LEU   A CD1    1 
ATOM   4110 C CD2    . LEU   A 1 287 ? 24.29003  -57.46547 19.72326  1.000 107.74546 ? 288 LEU   A CD2    1 
ATOM   4111 H H      . LEU   A 1 287 ? 26.20603  -61.62790 21.09866  1.000 170.21735 ? 288 LEU   A H      1 
ATOM   4112 H HA     . LEU   A 1 287 ? 24.31586  -61.67000 19.31805  1.000 158.48322 ? 288 LEU   A HA     1 
ATOM   4113 H HB2    . LEU   A 1 287 ? 24.50985  -59.93186 20.84439  1.000 145.76190 ? 288 LEU   A HB2    1 
ATOM   4114 H HB3    . LEU   A 1 287 ? 25.85468  -59.45774 20.14291  1.000 145.76190 ? 288 LEU   A HB3    1 
ATOM   4115 H HG     . LEU   A 1 287 ? 24.55816  -58.85732 18.24639  1.000 127.92163 ? 288 LEU   A HG     1 
ATOM   4116 H HD11   . LEU   A 1 287 ? 22.26339  -58.66150 18.45680  1.000 126.64943 ? 288 LEU   A HD11   1 
ATOM   4117 H HD12   . LEU   A 1 287 ? 22.69432  -60.18024 18.63357  1.000 126.64943 ? 288 LEU   A HD12   1 
ATOM   4118 H HD13   . LEU   A 1 287 ? 22.33386  -59.30337 19.90820  1.000 126.64943 ? 288 LEU   A HD13   1 
ATOM   4119 H HD21   . LEU   A 1 287 ? 23.76285  -56.85835 19.18068  1.000 129.68502 ? 288 LEU   A HD21   1 
ATOM   4120 H HD22   . LEU   A 1 287 ? 23.95223  -57.47468 20.63250  1.000 129.68502 ? 288 LEU   A HD22   1 
ATOM   4121 H HD23   . LEU   A 1 287 ? 25.22018  -57.19032 19.71873  1.000 129.68502 ? 288 LEU   A HD23   1 
ATOM   4122 N N      . ILE   A 1 288 ? 27.19037  -60.98141 18.07308  1.000 133.22718 ? 289 ILE   A N      1 
ATOM   4123 C CA     . ILE   A 1 288 ? 27.91353  -60.87108 16.81038  1.000 116.87732 ? 289 ILE   A CA     1 
ATOM   4124 C C      . ILE   A 1 288 ? 27.92507  -62.20649 16.07673  1.000 122.45769 ? 289 ILE   A C      1 
ATOM   4125 O O      . ILE   A 1 288 ? 27.73342  -62.26084 14.85618  1.000 132.71829 ? 289 ILE   A O      1 
ATOM   4126 C CB     . ILE   A 1 288 ? 29.34259  -60.35524 17.06294  1.000 116.77225 ? 289 ILE   A CB     1 
ATOM   4127 C CG1    . ILE   A 1 288 ? 29.30312  -58.90662 17.55226  1.000 111.16552 ? 289 ILE   A CG1    1 
ATOM   4128 C CG2    . ILE   A 1 288 ? 30.18366  -60.47429 15.79973  1.000 119.12852 ? 289 ILE   A CG2    1 
ATOM   4129 C CD1    . ILE   A 1 288 ? 30.61029  -58.42342 18.15370  1.000 148.83047 ? 289 ILE   A CD1    1 
ATOM   4130 H H      . ILE   A 1 288 ? 27.67937  -60.88856 18.77441  1.000 160.26309 ? 289 ILE   A H      1 
ATOM   4131 H HA     . ILE   A 1 288 ? 27.45216  -60.22868 16.24882  1.000 140.64326 ? 289 ILE   A HA     1 
ATOM   4132 H HB     . ILE   A 1 288 ? 29.74991  -60.90211 17.75281  1.000 140.51717 ? 289 ILE   A HB     1 
ATOM   4133 H HG12   . ILE   A 1 288 ? 29.09287  -58.33011 16.80104  1.000 133.78909 ? 289 ILE   A HG12   1 
ATOM   4134 H HG13   . ILE   A 1 288 ? 28.61738  -58.82699 18.23367  1.000 133.78909 ? 289 ILE   A HG13   1 
ATOM   4135 H HG21   . ILE   A 1 288 ? 30.98560  -59.93836 15.90260  1.000 143.34470 ? 289 ILE   A HG21   1 
ATOM   4136 H HG22   . ILE   A 1 288 ? 30.42259  -61.40483 15.66594  1.000 143.34470 ? 289 ILE   A HG22   1 
ATOM   4137 H HG23   . ILE   A 1 288 ? 29.66624  -60.15375 15.04445  1.000 143.34470 ? 289 ILE   A HG23   1 
ATOM   4138 H HD11   . ILE   A 1 288 ? 30.51797  -57.49018 18.40157  1.000 178.98703 ? 289 ILE   A HD11   1 
ATOM   4139 H HD12   . ILE   A 1 288 ? 30.81249  -58.95579 18.93893  1.000 178.98703 ? 289 ILE   A HD12   1 
ATOM   4140 H HD13   . ILE   A 1 288 ? 31.31630  -58.52269 17.49598  1.000 178.98703 ? 289 ILE   A HD13   1 
ATOM   4141 N N      . ARG   A 1 289 ? 28.14631  -63.30380 16.80382  1.000 129.02557 ? 290 ARG   A N      1 
ATOM   4142 C CA     . ARG   A 1 289 ? 28.31645  -64.59759 16.15147  1.000 132.89443 ? 290 ARG   A CA     1 
ATOM   4143 C C      . ARG   A 1 289 ? 27.05508  -65.04119 15.42174  1.000 124.16502 ? 290 ARG   A C      1 
ATOM   4144 O O      . ARG   A 1 289 ? 27.13755  -65.80994 14.45691  1.000 126.94416 ? 290 ARG   A O      1 
ATOM   4145 C CB     . ARG   A 1 289 ? 28.72135  -65.65563 17.18029  1.000 151.44552 ? 290 ARG   A CB     1 
ATOM   4146 C CG     . ARG   A 1 289 ? 30.07668  -65.41695 17.83220  1.000 153.86185 ? 290 ARG   A CG     1 
ATOM   4147 C CD     . ARG   A 1 289 ? 30.46600  -66.56970 18.75195  1.000 157.68964 ? 290 ARG   A CD     1 
ATOM   4148 N NE     . ARG   A 1 289 ? 31.71194  -66.30883 19.46556  1.000 168.62918 ? 290 ARG   A NE     1 
ATOM   4149 C CZ     . ARG   A 1 289 ? 31.79596  -65.94138 20.73879  1.000 172.15830 ? 290 ARG   A CZ     1 
ATOM   4150 N NH1    . ARG   A 1 289 ? 30.71744  -65.79506 21.49245  1.000 166.08903 ? 290 ARG   A NH1    1 
ATOM   4151 N NH2    . ARG   A 1 289 ? 32.99472  -65.71914 21.27100  1.000 154.57794 ? 290 ARG   A NH2    1 
ATOM   4152 H H      . ARG   A 1 289 ? 28.20117  -63.32417 17.66183  1.000 155.22116 ? 290 ARG   A H      1 
ATOM   4153 H HA     . ARG   A 1 289 ? 29.02777  -64.51630 15.49701  1.000 159.86379 ? 290 ARG   A HA     1 
ATOM   4154 H HB2    . ARG   A 1 289 ? 28.05570  -65.67117 17.88567  1.000 182.12510 ? 290 ARG   A HB2    1 
ATOM   4155 H HB3    . ARG   A 1 289 ? 28.75672  -66.51843 16.73845  1.000 182.12510 ? 290 ARG   A HB3    1 
ATOM   4156 H HG2    . ARG   A 1 289 ? 30.75447  -65.33453 17.14321  1.000 185.02469 ? 290 ARG   A HG2    1 
ATOM   4157 H HG3    . ARG   A 1 289 ? 30.04028  -64.60436 18.36067  1.000 185.02469 ? 290 ARG   A HG3    1 
ATOM   4158 H HD2    . ARG   A 1 289 ? 29.76447  -66.70441 19.40816  1.000 189.61804 ? 290 ARG   A HD2    1 
ATOM   4159 H HD3    . ARG   A 1 289 ? 30.58377  -67.37380 18.22239  1.000 189.61804 ? 290 ARG   A HD3    1 
ATOM   4160 H HE     . ARG   A 1 289 ? 32.44704  -66.39994 19.02861  1.000 202.74548 ? 290 ARG   A HE     1 
ATOM   4161 H HH11   . ARG   A 1 289 ? 29.93758  -65.93892 21.15969  1.000 199.69730 ? 290 ARG   A HH11   1 
ATOM   4162 H HH12   . ARG   A 1 289 ? 30.79668  -65.55616 22.31479  1.000 199.69730 ? 290 ARG   A HH12   1 
ATOM   4163 H HH21   . ARG   A 1 289 ? 33.70233  -65.81390 20.79152  1.000 185.88400 ? 290 ARG   A HH21   1 
ATOM   4164 H HH22   . ARG   A 1 289 ? 33.06207  -65.48070 22.09453  1.000 185.88400 ? 290 ARG   A HH22   1 
ATOM   4165 N N      . VAL   A 1 290 ? 25.88190  -64.57388 15.86136  1.000 130.25289 ? 291 VAL   A N      1 
ATOM   4166 C CA     . VAL   A 1 290 ? 24.62178  -65.05301 15.30074  1.000 140.28014 ? 291 VAL   A CA     1 
ATOM   4167 C C      . VAL   A 1 290 ? 24.08761  -64.18454 14.17132  1.000 147.02615 ? 291 VAL   A C      1 
ATOM   4168 O O      . VAL   A 1 290 ? 23.11920  -64.58183 13.50452  1.000 129.53853 ? 291 VAL   A O      1 
ATOM   4169 C CB     . VAL   A 1 290 ? 23.53624  -65.14976 16.39317  1.000 143.93851 ? 291 VAL   A CB     1 
ATOM   4170 C CG1    . VAL   A 1 290 ? 23.94523  -66.15599 17.44347  1.000 156.79455 ? 291 VAL   A CG1    1 
ATOM   4171 C CG2    . VAL   A 1 290 ? 23.28515  -63.78572 17.03223  1.000 144.15838 ? 291 VAL   A CG2    1 
ATOM   4172 H H      . VAL   A 1 290 ? 25.79270  -63.98280 16.47963  1.000 156.69393 ? 291 VAL   A H      1 
ATOM   4173 H HA     . VAL   A 1 290 ? 24.79402  -65.93590 14.93777  1.000 168.72663 ? 291 VAL   A HA     1 
ATOM   4174 H HB     . VAL   A 1 290 ? 22.70728  -65.44526 15.98524  1.000 173.11668 ? 291 VAL   A HB     1 
ATOM   4175 H HG11   . VAL   A 1 290 ? 23.24264  -66.22099 18.10909  1.000 188.54393 ? 291 VAL   A HG11   1 
ATOM   4176 H HG12   . VAL   A 1 290 ? 24.07999  -67.01796 17.01949  1.000 188.54393 ? 291 VAL   A HG12   1 
ATOM   4177 H HG13   . VAL   A 1 290 ? 24.76951  -65.85996 17.86040  1.000 188.54393 ? 291 VAL   A HG13   1 
ATOM   4178 H HG21   . VAL   A 1 290 ? 22.52432  -63.85239 17.63022  1.000 173.38053 ? 291 VAL   A HG21   1 
ATOM   4179 H HG22   . VAL   A 1 290 ? 24.07441  -63.51985 17.52949  1.000 173.38053 ? 291 VAL   A HG22   1 
ATOM   4180 H HG23   . VAL   A 1 290 ? 23.10093  -63.13869 16.33343  1.000 173.38053 ? 291 VAL   A HG23   1 
ATOM   4181 N N      . THR   A 1 291 ? 24.67125  -63.01317 13.93910  1.000 147.09501 ? 292 THR   A N      1 
ATOM   4182 C CA     . THR   A 1 291 ? 24.14944  -62.11208 12.92171  1.000 123.19236 ? 292 THR   A CA     1 
ATOM   4183 C C      . THR   A 1 291 ? 24.30044  -62.72652 11.53612  1.000 132.05436 ? 292 THR   A C      1 
ATOM   4184 O O      . THR   A 1 291 ? 25.35550  -63.27135 11.19257  1.000 131.96352 ? 292 THR   A O      1 
ATOM   4185 C CB     . THR   A 1 291 ? 24.86507  -60.76482 12.98589  1.000 129.57728 ? 292 THR   A CB     1 
ATOM   4186 O OG1    . THR   A 1 291 ? 24.55655  -60.11700 14.22653  1.000 141.45102 ? 292 THR   A OG1    1 
ATOM   4187 C CG2    . THR   A 1 291 ? 24.43440  -59.86974 11.83400  1.000 145.01364 ? 292 THR   A CG2    1 
ATOM   4188 H H      . THR   A 1 291 ? 25.36503  -62.71987 14.35413  1.000 176.90448 ? 292 THR   A H      1 
ATOM   4189 H HA     . THR   A 1 291 ? 23.20523  -61.96154 13.08508  1.000 148.22130 ? 292 THR   A HA     1 
ATOM   4190 H HB     . THR   A 1 291 ? 25.82239  -60.90674 12.92032  1.000 155.88321 ? 292 THR   A HB     1 
ATOM   4191 H HG1    . THR   A 1 291 ? 24.79205  -60.60234 14.87041  1.000 170.13169 ? 292 THR   A HG1    1 
ATOM   4192 H HG21   . THR   A 1 291 ? 24.71524  -58.95636 12.00067  1.000 174.40684 ? 292 THR   A HG21   1 
ATOM   4193 H HG22   . THR   A 1 291 ? 24.83705  -60.17690 11.00671  1.000 174.40684 ? 292 THR   A HG22   1 
ATOM   4194 H HG23   . THR   A 1 291 ? 23.46909  -59.89026 11.74090  1.000 174.40684 ? 292 THR   A HG23   1 
ATOM   4195 N N      . SER   A 1 292 ? 23.23738  -62.63369 10.74003  1.000 131.50778 ? 293 SER   A N      1 
ATOM   4196 C CA     . SER   A 1 292 ? 23.24989  -63.20130 9.39808   1.000 131.07118 ? 293 SER   A CA     1 
ATOM   4197 C C      . SER   A 1 292 ? 23.96565  -62.28200 8.41718   1.000 134.30677 ? 293 SER   A C      1 
ATOM   4198 O O      . SER   A 1 292 ? 24.97276  -62.66159 7.81018   1.000 133.90575 ? 293 SER   A O      1 
ATOM   4199 C CB     . SER   A 1 292 ? 21.81775  -63.46004 8.92428   1.000 132.06133 ? 293 SER   A CB     1 
ATOM   4200 O OG     . SER   A 1 292 ? 21.81312  -64.00534 7.61604   1.000 153.60111 ? 293 SER   A OG     1 
ATOM   4201 H H      . SER   A 1 292 ? 22.49912  -62.24783 10.95378  1.000 158.19981 ? 293 SER   A H      1 
ATOM   4202 H HA     . SER   A 1 292 ? 23.72213  -64.04813 9.42586   1.000 157.67589 ? 293 SER   A HA     1 
ATOM   4203 H HB2    . SER   A 1 292 ? 21.39277  -64.08736 9.52989   1.000 158.86406 ? 293 SER   A HB2    1 
ATOM   4204 H HB3    . SER   A 1 292 ? 21.33001  -62.62160 8.91914   1.000 158.86406 ? 293 SER   A HB3    1 
ATOM   4205 H HG     . SER   A 1 292 ? 21.04988  -64.30395 7.43195   1.000 184.71180 ? 293 SER   A HG     1 
ATOM   4206 N N      . SER   A 1 293 ? 23.45083  -61.06750 8.25030   1.000 136.97902 ? 294 SER   A N      1 
ATOM   4207 C CA     . SER   A 1 293 ? 23.92104  -60.13512 7.23765   1.000 134.73222 ? 294 SER   A CA     1 
ATOM   4208 C C      . SER   A 1 293 ? 24.32936  -58.82972 7.89973   1.000 119.54164 ? 294 SER   A C      1 
ATOM   4209 O O      . SER   A 1 293 ? 23.55165  -58.24594 8.66139   1.000 107.86018 ? 294 SER   A O      1 
ATOM   4210 C CB     . SER   A 1 293 ? 22.83313  -59.87613 6.19304   1.000 131.88431 ? 294 SER   A CB     1 
ATOM   4211 O OG     . SER   A 1 293 ? 23.29573  -58.99367 5.18778   1.000 161.26345 ? 294 SER   A OG     1 
ATOM   4212 H H      . SER   A 1 293 ? 22.80824  -60.75366 8.72798   1.000 164.76530 ? 294 SER   A H      1 
ATOM   4213 H HA     . SER   A 1 293 ? 24.69949  -60.50526 6.79277   1.000 162.06913 ? 294 SER   A HA     1 
ATOM   4214 H HB2    . SER   A 1 293 ? 22.58347  -60.71869 5.78235   1.000 158.65164 ? 294 SER   A HB2    1 
ATOM   4215 H HB3    . SER   A 1 293 ? 22.06372  -59.47962 6.63086   1.000 158.65164 ? 294 SER   A HB3    1 
ATOM   4216 H HG     . SER   A 1 293 ? 22.72402  -58.93054 4.57560   1.000 193.90661 ? 294 SER   A HG     1 
ATOM   4217 N N      . PHE   A 1 294 ? 25.54087  -58.37422 7.60113   1.000 119.02335 ? 295 PHE   A N      1 
ATOM   4218 C CA     . PHE   A 1 294 ? 26.05568  -57.11398 8.11281   1.000 120.43383 ? 295 PHE   A CA     1 
ATOM   4219 C C      . PHE   A 1 294 ? 25.94700  -56.04193 7.03759   1.000 112.24994 ? 295 PHE   A C      1 
ATOM   4220 O O      . PHE   A 1 294 ? 26.11268  -56.32382 5.84730   1.000 124.11509 ? 295 PHE   A O      1 
ATOM   4221 C CB     . PHE   A 1 294 ? 27.51133  -57.25899 8.55759   1.000 139.41149 ? 295 PHE   A CB     1 
ATOM   4222 C CG     . PHE   A 1 294 ? 27.70314  -58.19427 9.71707   1.000 129.31946 ? 295 PHE   A CG     1 
ATOM   4223 C CD1    . PHE   A 1 294 ? 27.43268  -57.77811 11.00802  1.000 119.35168 ? 295 PHE   A CD1    1 
ATOM   4224 C CD2    . PHE   A 1 294 ? 28.16733  -59.48425 9.51775   1.000 133.66463 ? 295 PHE   A CD2    1 
ATOM   4225 C CE1    . PHE   A 1 294 ? 27.61303  -58.63201 12.07729  1.000 124.68642 ? 295 PHE   A CE1    1 
ATOM   4226 C CE2    . PHE   A 1 294 ? 28.35013  -60.34205 10.58420  1.000 123.46535 ? 295 PHE   A CE2    1 
ATOM   4227 C CZ     . PHE   A 1 294 ? 28.07425  -59.91479 11.86472  1.000 121.69599 ? 295 PHE   A CZ     1 
ATOM   4228 H H      . PHE   A 1 294 ? 26.09552  -58.78898 7.09129   1.000 143.21849 ? 295 PHE   A H      1 
ATOM   4229 H HA     . PHE   A 1 294 ? 25.53226  -56.83631 8.88082   1.000 144.91107 ? 295 PHE   A HA     1 
ATOM   4230 H HB2    . PHE   A 1 294 ? 28.03167  -57.60029 7.81351   1.000 167.68426 ? 295 PHE   A HB2    1 
ATOM   4231 H HB3    . PHE   A 1 294 ? 27.84407  -56.38734 8.82295   1.000 167.68426 ? 295 PHE   A HB3    1 
ATOM   4232 H HD1    . PHE   A 1 294 ? 27.12577  -56.91300 11.15730  1.000 143.61248 ? 295 PHE   A HD1    1 
ATOM   4233 H HD2    . PHE   A 1 294 ? 28.35805  -59.77589 8.65550   1.000 160.78803 ? 295 PHE   A HD2    1 
ATOM   4234 H HE1    . PHE   A 1 294 ? 27.42375  -58.34280 12.94067  1.000 150.01417 ? 295 PHE   A HE1    1 
ATOM   4235 H HE2    . PHE   A 1 294 ? 28.65906  -61.20703 10.43836  1.000 148.54889 ? 295 PHE   A HE2    1 
ATOM   4236 H HZ     . PHE   A 1 294 ? 28.19874  -60.49022 12.58464  1.000 146.42566 ? 295 PHE   A HZ     1 
ATOM   4237 N N      . VAL   A 1 295 ? 25.66707  -54.81263 7.46378   1.000 103.40250 ? 296 VAL   A N      1 
ATOM   4238 C CA     . VAL   A 1 295 ? 25.53055  -53.66852 6.56838   1.000 93.58234  ? 296 VAL   A CA     1 
ATOM   4239 C C      . VAL   A 1 295 ? 26.44600  -52.56821 7.08404   1.000 91.78465  ? 296 VAL   A C      1 
ATOM   4240 O O      . VAL   A 1 295 ? 26.21087  -52.01887 8.16646   1.000 102.90626 ? 296 VAL   A O      1 
ATOM   4241 C CB     . VAL   A 1 295 ? 24.08311  -53.16907 6.48108   1.000 91.11241  ? 296 VAL   A CB     1 
ATOM   4242 C CG1    . VAL   A 1 295 ? 24.00620  -51.93235 5.60214   1.000 99.86057  ? 296 VAL   A CG1    1 
ATOM   4243 C CG2    . VAL   A 1 295 ? 23.17649  -54.26690 5.95467   1.000 109.52068 ? 296 VAL   A CG2    1 
ATOM   4244 H H      . VAL   A 1 295 ? 25.54857  -54.61185 8.29157   1.000 124.47347 ? 296 VAL   A H      1 
ATOM   4245 H HA     . VAL   A 1 295 ? 25.82600  -53.92263 5.68010   1.000 112.68928 ? 296 VAL   A HA     1 
ATOM   4246 H HB     . VAL   A 1 295 ? 23.77415  -52.92687 7.36809   1.000 109.72536 ? 296 VAL   A HB     1 
ATOM   4247 H HG11   . VAL   A 1 295 ? 23.07754  -51.75805 5.38280   1.000 120.22316 ? 296 VAL   A HG11   1 
ATOM   4248 H HG12   . VAL   A 1 295 ? 24.37924  -51.17818 6.08482   1.000 120.22316 ? 296 VAL   A HG12   1 
ATOM   4249 H HG13   . VAL   A 1 295 ? 24.51386  -52.08955 4.79068   1.000 120.22316 ? 296 VAL   A HG13   1 
ATOM   4250 H HG21   . VAL   A 1 295 ? 22.27713  -53.91584 5.86080   1.000 131.81529 ? 296 VAL   A HG21   1 
ATOM   4251 H HG22   . VAL   A 1 295 ? 23.50748  -54.56347 5.09246   1.000 131.81529 ? 296 VAL   A HG22   1 
ATOM   4252 H HG23   . VAL   A 1 295 ? 23.17903  -55.00656 6.58219   1.000 131.81529 ? 296 VAL   A HG23   1 
ATOM   4253 N N      . GLY   A 1 296 ? 27.47925  -52.24202 6.31528   1.000 91.65836  ? 297 GLY   A N      1 
ATOM   4254 C CA     . GLY   A 1 296 ? 28.42287  -51.19879 6.68188   1.000 97.80713  ? 297 GLY   A CA     1 
ATOM   4255 C C      . GLY   A 1 296 ? 28.08390  -49.88550 5.99810   1.000 105.65750 ? 297 GLY   A C      1 
ATOM   4256 O O      . GLY   A 1 296 ? 27.66177  -49.86433 4.84176   1.000 122.37726 ? 297 GLY   A O      1 
ATOM   4257 H H      . GLY   A 1 296 ? 27.65635  -52.61899 5.56287   1.000 110.38050 ? 297 GLY   A H      1 
ATOM   4258 H HA2    . GLY   A 1 296 ? 28.40184  -51.06308 7.64211   1.000 117.75903 ? 297 GLY   A HA2    1 
ATOM   4259 H HA3    . GLY   A 1 296 ? 29.31868  -51.46285 6.41980   1.000 117.75903 ? 297 GLY   A HA3    1 
ATOM   4260 N N      . LEU   A 1 297 ? 28.27983  -48.79020 6.72700   1.000 102.02447 ? 298 LEU   A N      1 
ATOM   4261 C CA     . LEU   A 1 297 ? 27.97443  -47.46248 6.20694   1.000 104.77174 ? 298 LEU   A CA     1 
ATOM   4262 C C      . LEU   A 1 297 ? 28.85639  -46.44831 6.91213   1.000 113.44982 ? 298 LEU   A C      1 
ATOM   4263 O O      . LEU   A 1 297 ? 28.85129  -46.37289 8.14424   1.000 141.99176 ? 298 LEU   A O      1 
ATOM   4264 C CB     . LEU   A 1 297 ? 26.49831  -47.11712 6.41103   1.000 110.97808 ? 298 LEU   A CB     1 
ATOM   4265 C CG     . LEU   A 1 297 ? 26.05696  -45.74820 5.88758   1.000 125.33803 ? 298 LEU   A CG     1 
ATOM   4266 C CD1    . LEU   A 1 297 ? 26.10066  -45.71761 4.36637   1.000 120.39948 ? 298 LEU   A CD1    1 
ATOM   4267 C CD2    . LEU   A 1 297 ? 24.66758  -45.39854 6.39649   1.000 134.27044 ? 298 LEU   A CD2    1 
ATOM   4268 H H      . LEU   A 1 297 ? 28.59008  -48.79035 7.52909   1.000 122.81983 ? 298 LEU   A H      1 
ATOM   4269 H HA     . LEU   A 1 297 ? 28.17167  -47.43770 5.25752   1.000 126.11655 ? 298 LEU   A HA     1 
ATOM   4270 H HB2    . LEU   A 1 297 ? 25.96436  -47.78607 5.95463   1.000 133.56417 ? 298 LEU   A HB2    1 
ATOM   4271 H HB3    . LEU   A 1 297 ? 26.31114  -47.13589 7.36261   1.000 133.56417 ? 298 LEU   A HB3    1 
ATOM   4272 H HG     . LEU   A 1 297 ? 26.67048  -45.07312 6.21737   1.000 150.79611 ? 298 LEU   A HG     1 
ATOM   4273 H HD11   . LEU   A 1 297 ? 25.76568  -44.86112 4.05798   1.000 144.86985 ? 298 LEU   A HD11   1 
ATOM   4274 H HD12   . LEU   A 1 297 ? 27.01768  -45.83873 4.07429   1.000 144.86985 ? 298 LEU   A HD12   1 
ATOM   4275 H HD13   . LEU   A 1 297 ? 25.54584  -46.43393 4.02003   1.000 144.86985 ? 298 LEU   A HD13   1 
ATOM   4276 H HD21   . LEU   A 1 297 ? 24.42671  -44.51541 6.07562   1.000 161.51500 ? 298 LEU   A HD21   1 
ATOM   4277 H HD22   . LEU   A 1 297 ? 24.03522  -46.05493 6.06456   1.000 161.51500 ? 298 LEU   A HD22   1 
ATOM   4278 H HD23   . LEU   A 1 297 ? 24.67504  -45.40741 7.36643   1.000 161.51500 ? 298 LEU   A HD23   1 
ATOM   4279 N N      . ALA   A 1 298 ? 29.60798  -45.67359 6.14037   1.000 114.21778 ? 299 ALA   A N      1 
ATOM   4280 C CA     . ALA   A 1 298 ? 30.37864  -44.57961 6.70516   1.000 112.31663 ? 299 ALA   A CA     1 
ATOM   4281 C C      . ALA   A 1 298 ? 29.45574  -43.41800 7.05260   1.000 110.97412 ? 299 ALA   A C      1 
ATOM   4282 O O      . ALA   A 1 298 ? 28.55069  -43.07415 6.28707   1.000 101.25791 ? 299 ALA   A O      1 
ATOM   4283 C CB     . ALA   A 1 298 ? 31.45505  -44.12078 5.72427   1.000 130.71599 ? 299 ALA   A CB     1 
ATOM   4284 H H      . ALA   A 1 298 ? 29.68732  -45.76200 5.28861   1.000 137.45181 ? 299 ALA   A H      1 
ATOM   4285 H HA     . ALA   A 1 298 ? 30.82162  -44.87548 7.51580   1.000 135.17043 ? 299 ALA   A HA     1 
ATOM   4286 H HB1    . ALA   A 1 298 ? 31.94907  -43.38518 6.11890   1.000 157.24966 ? 299 ALA   A HB1    1 
ATOM   4287 H HB2    . ALA   A 1 298 ? 32.05395  -44.86202 5.54318   1.000 157.24966 ? 299 ALA   A HB2    1 
ATOM   4288 H HB3    . ALA   A 1 298 ? 31.03004  -43.83045 4.90209   1.000 157.24966 ? 299 ALA   A HB3    1 
ATOM   4289 N N      . THR   A 1 299 ? 29.68094  -42.81976 8.21855   1.000 122.58882 ? 300 THR   A N      1 
ATOM   4290 C CA     . THR   A 1 299 ? 28.92174  -41.63731 8.59897   1.000 115.69917 ? 300 THR   A CA     1 
ATOM   4291 C C      . THR   A 1 299 ? 29.31352  -40.47296 7.70007   1.000 108.29825 ? 300 THR   A C      1 
ATOM   4292 O O      . THR   A 1 299 ? 30.50174  -40.19466 7.51081   1.000 110.02072 ? 300 THR   A O      1 
ATOM   4293 C CB     . THR   A 1 299 ? 29.17268  -41.27595 10.06073  1.000 113.44951 ? 300 THR   A CB     1 
ATOM   4294 O OG1    . THR   A 1 299 ? 29.01115  -42.43841 10.88257  1.000 113.42985 ? 300 THR   A OG1    1 
ATOM   4295 C CG2    . THR   A 1 299 ? 28.19360  -40.19654 10.51163  1.000 111.39194 ? 300 THR   A CG2    1 
ATOM   4296 H H      . THR   A 1 299 ? 30.26099  -43.07655 8.79923   1.000 147.49705 ? 300 THR   A H      1 
ATOM   4297 H HA     . THR   A 1 299 ? 27.97391  -41.81690 8.49763   1.000 139.22947 ? 300 THR   A HA     1 
ATOM   4298 H HB     . THR   A 1 299 ? 30.07608  -40.93746 10.16170  1.000 136.52988 ? 300 THR   A HB     1 
ATOM   4299 H HG1    . THR   A 1 299 ? 29.20492  -42.25614 11.67933  1.000 136.50630 ? 300 THR   A HG1    1 
ATOM   4300 H HG21   . THR   A 1 299 ? 28.35285  -39.97176 11.44169  1.000 134.06080 ? 300 THR   A HG21   1 
ATOM   4301 H HG22   . THR   A 1 299 ? 28.30698  -39.39908 9.97116   1.000 134.06080 ? 300 THR   A HG22   1 
ATOM   4302 H HG23   . THR   A 1 299 ? 27.28219  -40.51454 10.41622  1.000 134.06080 ? 300 THR   A HG23   1 
ATOM   4303 N N      . ARG   A 1 300 ? 28.31335  -39.78831 7.15284   1.000 104.85722 ? 301 ARG   A N      1 
ATOM   4304 C CA     . ARG   A 1 300 ? 28.54334  -38.71662 6.19764   1.000 108.94856 ? 301 ARG   A CA     1 
ATOM   4305 C C      . ARG   A 1 300 ? 27.62223  -37.54966 6.51837   1.000 119.11697 ? 301 ARG   A C      1 
ATOM   4306 O O      . ARG   A 1 300 ? 26.64278  -37.68717 7.25554   1.000 123.95007 ? 301 ARG   A O      1 
ATOM   4307 C CB     . ARG   A 1 300 ? 28.31059  -39.18999 4.75584   1.000 116.05626 ? 301 ARG   A CB     1 
ATOM   4308 C CG     . ARG   A 1 300 ? 29.28460  -40.26013 4.27117   1.000 125.61746 ? 301 ARG   A CG     1 
ATOM   4309 C CD     . ARG   A 1 300 ? 28.85864  -40.82342 2.91332   1.000 120.73315 ? 301 ARG   A CD     1 
ATOM   4310 N NE     . ARG   A 1 300 ? 29.88741  -41.65967 2.30258   1.000 123.69147 ? 301 ARG   A NE     1 
ATOM   4311 C CZ     . ARG   A 1 300 ? 29.85012  -42.98534 2.22528   1.000 137.11493 ? 301 ARG   A CZ     1 
ATOM   4312 N NH1    . ARG   A 1 300 ? 28.83175  -43.68263 2.70427   1.000 130.17074 ? 301 ARG   A NH1    1 
ATOM   4313 N NH2    . ARG   A 1 300 ? 30.86005  -43.62807 1.64583   1.000 141.94417 ? 301 ARG   A NH2    1 
ATOM   4314 H H      . ARG   A 1 300 ? 27.48229  -39.92982 7.32292   1.000 126.21913 ? 301 ARG   A H      1 
ATOM   4315 H HA     . ARG   A 1 300 ? 29.45968  -38.40826 6.27594   1.000 131.12875 ? 301 ARG   A HA     1 
ATOM   4316 H HB2    . ARG   A 1 300 ? 27.41588  -39.55945 4.69343   1.000 139.65799 ? 301 ARG   A HB2    1 
ATOM   4317 H HB3    . ARG   A 1 300 ? 28.39646  -38.42684 4.16327   1.000 139.65799 ? 301 ARG   A HB3    1 
ATOM   4318 H HG2    . ARG   A 1 300 ? 30.16892  -39.87260 4.17786   1.000 151.13142 ? 301 ARG   A HG2    1 
ATOM   4319 H HG3    . ARG   A 1 300 ? 29.30750  -40.98873 4.91110   1.000 151.13142 ? 301 ARG   A HG3    1 
ATOM   4320 H HD2    . ARG   A 1 300 ? 28.06258  -41.36504 3.03098   1.000 145.27025 ? 301 ARG   A HD2    1 
ATOM   4321 H HD3    . ARG   A 1 300 ? 28.67285  -40.08736 2.30951   1.000 145.27025 ? 301 ARG   A HD3    1 
ATOM   4322 H HE     . ARG   A 1 300 ? 30.57203  -41.26263 1.96606   1.000 148.82023 ? 301 ARG   A HE     1 
ATOM   4323 H HH11   . ARG   A 1 300 ? 28.17112  -43.27783 3.07752   1.000 156.59536 ? 301 ARG   A HH11   1 
ATOM   4324 H HH12   . ARG   A 1 300 ? 28.83085  -44.54039 2.64217   1.000 156.59536 ? 301 ARG   A HH12   1 
ATOM   4325 H HH21   . ARG   A 1 300 ? 31.52525  -43.18561 1.32749   1.000 170.72347 ? 301 ARG   A HH21   1 
ATOM   4326 H HH22   . ARG   A 1 300 ? 30.84790  -44.48613 1.58948   1.000 170.72347 ? 301 ARG   A HH22   1 
ATOM   4327 N N      . ILE   A 1 301 ? 27.94906  -36.39371 5.94607   1.000 125.92258 ? 302 ILE   A N      1 
ATOM   4328 C CA     . ILE   A 1 301 ? 27.18409  -35.16898 6.14519   1.000 126.57473 ? 302 ILE   A CA     1 
ATOM   4329 C C      . ILE   A 1 301 ? 27.14011  -34.40650 4.82955   1.000 124.62648 ? 302 ILE   A C      1 
ATOM   4330 O O      . ILE   A 1 301 ? 28.13681  -34.34343 4.10185   1.000 124.34547 ? 302 ILE   A O      1 
ATOM   4331 C CB     . ILE   A 1 301 ? 27.78861  -34.29324 7.26445   1.000 120.87842 ? 302 ILE   A CB     1 
ATOM   4332 C CG1    . ILE   A 1 301 ? 26.97291  -33.00904 7.44029   1.000 117.03403 ? 302 ILE   A CG1    1 
ATOM   4333 C CG2    . ILE   A 1 301 ? 29.24021  -33.94978 6.95386   1.000 117.46783 ? 302 ILE   A CG2    1 
ATOM   4334 C CD1    . ILE   A 1 301 ? 27.27518  -32.25941 8.71856   1.000 135.65766 ? 302 ILE   A CD1    1 
ATOM   4335 H H      . ILE   A 1 301 ? 28.62641  -36.29286 5.42585   1.000 151.49757 ? 302 ILE   A H      1 
ATOM   4336 H HA     . ILE   A 1 301 ? 26.27588  -35.39890 6.39657   1.000 152.28014 ? 302 ILE   A HA     1 
ATOM   4337 H HB     . ILE   A 1 301 ? 27.75733  -34.80039 8.09072   1.000 145.44457 ? 302 ILE   A HB     1 
ATOM   4338 H HG12   . ILE   A 1 301 ? 27.16392  -32.41506 6.69759   1.000 140.83131 ? 302 ILE   A HG12   1 
ATOM   4339 H HG13   . ILE   A 1 301 ? 26.03032  -33.23787 7.44817   1.000 140.83131 ? 302 ILE   A HG13   1 
ATOM   4340 H HG21   . ILE   A 1 301 ? 29.63181  -33.50792 7.72347   1.000 141.35186 ? 302 ILE   A HG21   1 
ATOM   4341 H HG22   . ILE   A 1 301 ? 29.72394  -34.76804 6.76060   1.000 141.35186 ? 302 ILE   A HG22   1 
ATOM   4342 H HG23   . ILE   A 1 301 ? 29.26745  -33.35982 6.18437   1.000 141.35186 ? 302 ILE   A HG23   1 
ATOM   4343 H HD11   . ILE   A 1 301 ? 26.70467  -31.47648 8.76795   1.000 163.17967 ? 302 ILE   A HD11   1 
ATOM   4344 H HD12   . ILE   A 1 301 ? 27.10322  -32.84223 9.47464   1.000 163.17967 ? 302 ILE   A HD12   1 
ATOM   4345 H HD13   . ILE   A 1 301 ? 28.20698  -31.98994 8.71383   1.000 163.17967 ? 302 ILE   A HD13   1 
ATOM   4346 N N      . PHE   A 1 302 ? 25.97553  -33.84390 4.51728   1.000 115.46197 ? 303 PHE   A N      1 
ATOM   4347 C CA     . PHE   A 1 302 ? 25.84049  -32.91721 3.40057   1.000 126.86008 ? 303 PHE   A CA     1 
ATOM   4348 C C      . PHE   A 1 302 ? 25.85524  -31.49879 3.95944   1.000 131.56549 ? 303 PHE   A C      1 
ATOM   4349 O O      . PHE   A 1 302 ? 24.79188  -30.93623 4.24989   1.000 134.99482 ? 303 PHE   A O      1 
ATOM   4350 C CB     . PHE   A 1 302 ? 24.55620  -33.18701 2.61897   1.000 125.82636 ? 303 PHE   A CB     1 
ATOM   4351 C CG     . PHE   A 1 302 ? 24.51517  -32.51771 1.27456   1.000 136.35030 ? 303 PHE   A CG     1 
ATOM   4352 C CD1    . PHE   A 1 302 ? 25.28389  -32.99584 0.22475   1.000 120.32644 ? 303 PHE   A CD1    1 
ATOM   4353 C CD2    . PHE   A 1 302 ? 23.70520  -31.41522 1.05825   1.000 139.39819 ? 303 PHE   A CD2    1 
ATOM   4354 C CE1    . PHE   A 1 302 ? 25.24897  -32.38520 -1.01186  1.000 116.75836 ? 303 PHE   A CE1    1 
ATOM   4355 C CE2    . PHE   A 1 302 ? 23.66532  -30.80068 -0.17873  1.000 141.63634 ? 303 PHE   A CE2    1 
ATOM   4356 C CZ     . PHE   A 1 302 ? 24.43788  -31.28788 -1.21511  1.000 134.61676 ? 303 PHE   A CZ     1 
ATOM   4357 H H      . PHE   A 1 302 ? 25.24141  -33.98513 4.94240   1.000 138.94484 ? 303 PHE   A H      1 
ATOM   4358 H HA     . PHE   A 1 302 ? 26.57663  -33.02387 2.77799   1.000 152.62257 ? 303 PHE   A HA     1 
ATOM   4359 H HB2    . PHE   A 1 302 ? 24.47245  -34.14286 2.47671   1.000 151.38210 ? 303 PHE   A HB2    1 
ATOM   4360 H HB3    . PHE   A 1 302 ? 23.80242  -32.86114 3.13524   1.000 151.38210 ? 303 PHE   A HB3    1 
ATOM   4361 H HD1    . PHE   A 1 302 ? 25.82980  -33.73729 0.35565   1.000 144.78220 ? 303 PHE   A HD1    1 
ATOM   4362 H HD2    . PHE   A 1 302 ? 23.18256  -31.08500 1.75301   1.000 167.66830 ? 303 PHE   A HD2    1 
ATOM   4363 H HE1    . PHE   A 1 302 ? 25.77167  -32.71294 -1.70775  1.000 140.50051 ? 303 PHE   A HE1    1 
ATOM   4364 H HE2    . PHE   A 1 302 ? 23.11913  -30.06011 -0.31336  1.000 170.35408 ? 303 PHE   A HE2    1 
ATOM   4365 H HZ     . PHE   A 1 302 ? 24.41125  -30.87667 -2.04883  1.000 161.93058 ? 303 PHE   A HZ     1 
ATOM   4366 N N      . PRO   A 1 303 ? 27.02879  -30.88797 4.12134   1.000 131.08356 ? 304 PRO   A N      1 
ATOM   4367 C CA     . PRO   A 1 303 ? 27.10488  -29.64444 4.89870   1.000 132.93100 ? 304 PRO   A CA     1 
ATOM   4368 C C      . PRO   A 1 303 ? 26.24697  -28.53743 4.30400   1.000 134.82881 ? 304 PRO   A C      1 
ATOM   4369 O O      . PRO   A 1 303 ? 26.13170  -28.39616 3.08504   1.000 125.27420 ? 304 PRO   A O      1 
ATOM   4370 C CB     . PRO   A 1 303 ? 28.59775  -29.28998 4.85767   1.000 146.83399 ? 304 PRO   A CB     1 
ATOM   4371 C CG     . PRO   A 1 303 ? 29.13458  -30.00565 3.65719   1.000 151.77863 ? 304 PRO   A CG     1 
ATOM   4372 C CD     . PRO   A 1 303 ? 28.33353  -31.26764 3.54828   1.000 123.40399 ? 304 PRO   A CD     1 
ATOM   4373 H HA     . PRO   A 1 303 ? 26.82577  -29.80438 5.81380   1.000 159.90768 ? 304 PRO   A HA     1 
ATOM   4374 H HB2    . PRO   A 1 303 ? 28.70661  -28.33039 4.76694   1.000 176.59125 ? 304 PRO   A HB2    1 
ATOM   4375 H HB3    . PRO   A 1 303 ? 29.03236  -29.59800 5.66831   1.000 176.59125 ? 304 PRO   A HB3    1 
ATOM   4376 H HG2    . PRO   A 1 303 ? 29.01823  -29.45462 2.86743   1.000 182.52482 ? 304 PRO   A HG2    1 
ATOM   4377 H HG3    . PRO   A 1 303 ? 30.07498  -30.20477 3.78720   1.000 182.52482 ? 304 PRO   A HG3    1 
ATOM   4378 H HD2    . PRO   A 1 303 ? 28.23858  -31.53794 2.62155   1.000 148.47526 ? 304 PRO   A HD2    1 
ATOM   4379 H HD3    . PRO   A 1 303 ? 28.74207  -31.98185 4.06199   1.000 148.47526 ? 304 PRO   A HD3    1 
ATOM   4380 N N      . LEU   A 1 304 ? 25.63208  -27.75578 5.19043   1.000 146.11013 ? 305 LEU   A N      1 
ATOM   4381 C CA     . LEU   A 1 304 ? 24.84517  -26.58102 4.82113   1.000 153.70779 ? 305 LEU   A CA     1 
ATOM   4382 C C      . LEU   A 1 304 ? 25.62471  -25.29330 5.05227   1.000 173.11388 ? 305 LEU   A C      1 
ATOM   4383 O O      . LEU   A 1 304 ? 25.05981  -24.27762 5.46845   1.000 180.49009 ? 305 LEU   A O      1 
ATOM   4384 C CB     . LEU   A 1 304 ? 23.53543  -26.55584 5.60147   1.000 141.22629 ? 305 LEU   A CB     1 
ATOM   4385 C CG     . LEU   A 1 304 ? 22.46010  -27.55826 5.18723   1.000 129.87049 ? 305 LEU   A CG     1 
ATOM   4386 C CD1    . LEU   A 1 304 ? 21.34609  -27.58663 6.22036   1.000 155.32959 ? 305 LEU   A CD1    1 
ATOM   4387 C CD2    . LEU   A 1 304 ? 21.90960  -27.21045 3.81620   1.000 143.46738 ? 305 LEU   A CD2    1 
ATOM   4388 H H      . LEU   A 1 304 ? 25.65735  -27.89062 6.03942   1.000 175.72263 ? 305 LEU   A H      1 
ATOM   4389 H HA     . LEU   A 1 304 ? 24.62766  -26.63646 3.87746   1.000 184.83982 ? 305 LEU   A HA     1 
ATOM   4390 H HB2    . LEU   A 1 304 ? 23.74022  -26.73014 6.53345   1.000 169.86201 ? 305 LEU   A HB2    1 
ATOM   4391 H HB3    . LEU   A 1 304 ? 23.14877  -25.67132 5.50656   1.000 169.86201 ? 305 LEU   A HB3    1 
ATOM   4392 H HG     . LEU   A 1 304 ? 22.85041  -28.44479 5.13593   1.000 156.23506 ? 305 LEU   A HG     1 
ATOM   4393 H HD11   . LEU   A 1 304 ? 20.55518  -27.98162 5.82118   1.000 186.78597 ? 305 LEU   A HD11   1 
ATOM   4394 H HD12   . LEU   A 1 304 ? 21.63329  -28.11708 6.97999   1.000 186.78597 ? 305 LEU   A HD12   1 
ATOM   4395 H HD13   . LEU   A 1 304 ? 21.15525  -26.67887 6.50401   1.000 186.78597 ? 305 LEU   A HD13   1 
ATOM   4396 H HD21   . LEU   A 1 304 ? 21.17006  -27.80428 3.61288   1.000 172.55132 ? 305 LEU   A HD21   1 
ATOM   4397 H HD22   . LEU   A 1 304 ? 21.60267  -26.29031 3.82325   1.000 172.55132 ? 305 LEU   A HD22   1 
ATOM   4398 H HD23   . LEU   A 1 304 ? 22.61246  -27.31964 3.15667   1.000 172.55132 ? 305 LEU   A HD23   1 
ATOM   4399 N N      . GLY   A 1 305 ? 26.93007  -25.31179 4.79858   1.000 173.35806 ? 306 GLY   A N      1 
ATOM   4400 C CA     . GLY   A 1 305 ? 27.75136  -24.13466 4.99419   1.000 189.54732 ? 306 GLY   A CA     1 
ATOM   4401 C C      . GLY   A 1 305 ? 27.47768  -23.04705 3.97699   1.000 192.17138 ? 306 GLY   A C      1 
ATOM   4402 O O      . GLY   A 1 305 ? 27.00140  -21.96207 4.32570   1.000 195.16577 ? 306 GLY   A O      1 
ATOM   4403 H H      . GLY   A 1 305 ? 27.36070  -25.99862 4.51148   1.000 208.42014 ? 306 GLY   A H      1 
ATOM   4404 H HA2    . GLY   A 1 305 ? 27.58339  -23.77240 5.87819   1.000 227.84726 ? 306 GLY   A HA2    1 
ATOM   4405 H HA3    . GLY   A 1 305 ? 28.68639  -24.38399 4.92751   1.000 227.84726 ? 306 GLY   A HA3    1 
ATOM   4406 N N      . LYS   A 1 306 ? 27.77164  -23.33148 2.71192   1.000 192.75136 ? 307 LYS   A N      1 
ATOM   4407 C CA     . LYS   A 1 306 ? 27.60035  -22.35131 1.65033   1.000 187.42472 ? 307 LYS   A CA     1 
ATOM   4408 C C      . LYS   A 1 306 ? 26.15920  -22.35268 1.15837   1.000 177.74307 ? 307 LYS   A C      1 
ATOM   4409 O O      . LYS   A 1 306 ? 25.52424  -23.40577 1.05193   1.000 174.12347 ? 307 LYS   A O      1 
ATOM   4410 C CB     . LYS   A 1 306 ? 28.55568  -22.65532 0.49630   1.000 199.43187 ? 307 LYS   A CB     1 
ATOM   4411 C CG     . LYS   A 1 306 ? 28.85084  -21.46667 -0.40048  1.000 186.14962 ? 307 LYS   A CG     1 
ATOM   4412 C CD     . LYS   A 1 306 ? 29.98421  -21.76946 -1.37130  1.000 171.52146 ? 307 LYS   A CD     1 
ATOM   4413 C CE     . LYS   A 1 306 ? 29.65256  -22.94703 -2.27508  1.000 162.40488 ? 307 LYS   A CE     1 
ATOM   4414 N NZ     . LYS   A 1 306 ? 30.59614  -23.04294 -3.42087  1.000 163.52615 ? 307 LYS   A NZ     1 
ATOM   4415 H H      . LYS   A 1 306 ? 28.07369  -24.09028 2.44251   1.000 231.69210 ? 307 LYS   A H      1 
ATOM   4416 H HA     . LYS   A 1 306 ? 27.80349  -21.46378 1.98485   1.000 225.30014 ? 307 LYS   A HA     1 
ATOM   4417 H HB2    . LYS   A 1 306 ? 29.39895  -22.96172 0.86496   1.000 239.70872 ? 307 LYS   A HB2    1 
ATOM   4418 H HB3    . LYS   A 1 306 ? 28.16320  -23.34957 -0.05586  1.000 239.70872 ? 307 LYS   A HB3    1 
ATOM   4419 H HG2    . LYS   A 1 306 ? 28.05843  -21.24776 -0.91533  1.000 223.77001 ? 307 LYS   A HG2    1 
ATOM   4420 H HG3    . LYS   A 1 306 ? 29.11141  -20.70866 0.14581   1.000 223.77001 ? 307 LYS   A HG3    1 
ATOM   4421 H HD2    . LYS   A 1 306 ? 30.14332  -20.99284 -1.93027  1.000 206.21623 ? 307 LYS   A HD2    1 
ATOM   4422 H HD3    . LYS   A 1 306 ? 30.78566  -21.98736 -0.87020  1.000 206.21623 ? 307 LYS   A HD3    1 
ATOM   4423 H HE2    . LYS   A 1 306 ? 29.70996  -23.76943 -1.76393  1.000 195.27632 ? 307 LYS   A HE2    1 
ATOM   4424 H HE3    . LYS   A 1 306 ? 28.75563  -22.83759 -2.62785  1.000 195.27632 ? 307 LYS   A HE3    1 
ATOM   4425 H HZ1    . LYS   A 1 306 ? 30.37016  -23.72584 -3.94497  1.000 196.62185 ? 307 LYS   A HZ1    1 
ATOM   4426 H HZ2    . LYS   A 1 306 ? 30.57248  -22.29224 -3.89835  1.000 196.62185 ? 307 LYS   A HZ2    1 
ATOM   4427 H HZ3    . LYS   A 1 306 ? 31.42510  -23.16963 -3.12275  1.000 196.62185 ? 307 LYS   A HZ3    1 
ATOM   4428 N N      . SER   A 1 307 ? 25.64266  -21.16159 0.86502   1.000 174.66790 ? 308 SER   A N      1 
ATOM   4429 C CA     . SER   A 1 307 ? 24.27309  -21.04198 0.39077   1.000 165.88748 ? 308 SER   A CA     1 
ATOM   4430 C C      . SER   A 1 307 ? 24.11063  -21.74497 -0.95377  1.000 173.80562 ? 308 SER   A C      1 
ATOM   4431 O O      . SER   A 1 307 ? 25.07587  -21.99281 -1.68217  1.000 170.11039 ? 308 SER   A O      1 
ATOM   4432 C CB     . SER   A 1 307 ? 23.87360  -19.57254 0.26759   1.000 164.98116 ? 308 SER   A CB     1 
ATOM   4433 O OG     . SER   A 1 307 ? 23.78545  -18.96486 1.54378   1.000 167.44208 ? 308 SER   A OG     1 
ATOM   4434 H H      . SER   A 1 307 ? 26.06330  -20.41452 0.93237   1.000 209.99195 ? 308 SER   A H      1 
ATOM   4435 H HA     . SER   A 1 307 ? 23.67393  -21.46213 1.02747   1.000 199.45544 ? 308 SER   A HA     1 
ATOM   4436 H HB2    . SER   A 1 307 ? 24.54238  -19.10665 -0.25832  1.000 198.36786 ? 308 SER   A HB2    1 
ATOM   4437 H HB3    . SER   A 1 307 ? 23.00942  -19.51594 -0.16931  1.000 198.36786 ? 308 SER   A HB3    1 
ATOM   4438 H HG     . SER   A 1 307 ? 23.53711  -18.16626 1.46518   1.000 201.32096 ? 308 SER   A HG     1 
ATOM   4439 N N      . TRP   A 1 308 ? 22.86257  -22.06676 -1.27755  1.000 162.13682 ? 309 TRP   A N      1 
ATOM   4440 C CA     . TRP   A 1 308 ? 22.55731  -22.79184 -2.49847  1.000 156.10684 ? 309 TRP   A CA     1 
ATOM   4441 C C      . TRP   A 1 308 ? 22.48107  -21.83425 -3.68649  1.000 158.92897 ? 309 TRP   A C      1 
ATOM   4442 O O      . TRP   A 1 308 ? 22.45401  -20.60937 -3.53792  1.000 162.78278 ? 309 TRP   A O      1 
ATOM   4443 C CB     . TRP   A 1 308 ? 21.25364  -23.57063 -2.33413  1.000 149.56640 ? 309 TRP   A CB     1 
ATOM   4444 C CG     . TRP   A 1 308 ? 21.39868  -24.77872 -1.45139  1.000 139.46858 ? 309 TRP   A CG     1 
ATOM   4445 C CD1    . TRP   A 1 308 ? 22.54972  -25.24396 -0.88142  1.000 135.74659 ? 309 TRP   A CD1    1 
ATOM   4446 C CD2    . TRP   A 1 308 ? 20.35960  -25.67629 -1.04226  1.000 130.18654 ? 309 TRP   A CD2    1 
ATOM   4447 N NE1    . TRP   A 1 308 ? 22.29221  -26.37337 -0.14613  1.000 128.56318 ? 309 TRP   A NE1    1 
ATOM   4448 C CE2    . TRP   A 1 308 ? 20.95542  -26.66030 -0.22806  1.000 121.62247 ? 309 TRP   A CE2    1 
ATOM   4449 C CE3    . TRP   A 1 308 ? 18.98445  -25.74418 -1.28552  1.000 125.79438 ? 309 TRP   A CE3    1 
ATOM   4450 C CZ2    . TRP   A 1 308 ? 20.22526  -27.69760 0.34340   1.000 130.52074 ? 309 TRP   A CZ2    1 
ATOM   4451 C CZ3    . TRP   A 1 308 ? 18.26155  -26.77537 -0.71766  1.000 126.76486 ? 309 TRP   A CZ3    1 
ATOM   4452 C CH2    . TRP   A 1 308 ? 18.88297  -27.73824 0.08763   1.000 144.76549 ? 309 TRP   A CH2    1 
ATOM   4453 H H      . TRP   A 1 308 ? 22.17234  -21.87416 -0.80207  1.000 194.95466 ? 309 TRP   A H      1 
ATOM   4454 H HA     . TRP   A 1 308 ? 23.26429  -23.42978 -2.68317  1.000 187.71868 ? 309 TRP   A HA     1 
ATOM   4455 H HB2    . TRP   A 1 308 ? 20.58690  -22.98842 -1.93740  1.000 179.87015 ? 309 TRP   A HB2    1 
ATOM   4456 H HB3    . TRP   A 1 308 ? 20.95450  -23.87155 -3.20641  1.000 179.87015 ? 309 TRP   A HB3    1 
ATOM   4457 H HD1    . TRP   A 1 308 ? 23.38736  -24.85159 -0.97791  1.000 163.28637 ? 309 TRP   A HD1    1 
ATOM   4458 H HE1    . TRP   A 1 308 ? 22.87506  -26.82710 0.29433   1.000 154.66628 ? 309 TRP   A HE1    1 
ATOM   4459 H HE3    . TRP   A 1 308 ? 18.56496  -25.10810 -1.81875  1.000 151.34373 ? 309 TRP   A HE3    1 
ATOM   4460 H HZ2    . TRP   A 1 308 ? 20.63453  -28.33856 0.87871   1.000 157.01536 ? 309 TRP   A HZ2    1 
ATOM   4461 H HZ3    . TRP   A 1 308 ? 17.34628  -26.83122 -0.87278  1.000 152.50830 ? 309 TRP   A HZ3    1 
ATOM   4462 H HH2    . TRP   A 1 308 ? 18.37063  -28.42095 0.45683   1.000 174.10906 ? 309 TRP   A HH2    1 
ATOM   4463 N N      . LYS   A 1 309 ? 22.45080  -22.41550 -4.88390  1.000 152.37316 ? 310 LYS   A N      1 
ATOM   4464 C CA     . LYS   A 1 309 ? 22.54039  -21.62143 -6.10170  1.000 166.35739 ? 310 LYS   A CA     1 
ATOM   4465 C C      . LYS   A 1 309 ? 21.41474  -20.59724 -6.16798  1.000 159.71719 ? 310 LYS   A C      1 
ATOM   4466 O O      . LYS   A 1 309 ? 20.25940  -20.88877 -5.84663  1.000 154.49082 ? 310 LYS   A O      1 
ATOM   4467 C CB     . LYS   A 1 309 ? 22.51365  -22.53435 -7.32809  1.000 171.65278 ? 310 LYS   A CB     1 
ATOM   4468 C CG     . LYS   A 1 309 ? 23.82124  -23.28944 -7.53461  1.000 172.89512 ? 310 LYS   A CG     1 
ATOM   4469 C CD     . LYS   A 1 309 ? 23.77270  -24.21626 -8.73886  1.000 172.24771 ? 310 LYS   A CD     1 
ATOM   4470 C CE     . LYS   A 1 309 ? 25.12489  -24.87788 -8.97177  1.000 172.23872 ? 310 LYS   A CE     1 
ATOM   4471 N NZ     . LYS   A 1 309 ? 25.07385  -25.92679 -10.02753 1.000 140.37745 ? 310 LYS   A NZ     1 
ATOM   4472 H H      . LYS   A 1 309 ? 22.37944  -23.26229 -5.01603  1.000 183.23826 ? 310 LYS   A H      1 
ATOM   4473 H HA     . LYS   A 1 309 ? 23.37981  -21.13538 -6.10732  1.000 200.01933 ? 310 LYS   A HA     1 
ATOM   4474 H HB2    . LYS   A 1 309 ? 21.80452  -23.18721 -7.21942  1.000 206.37381 ? 310 LYS   A HB2    1 
ATOM   4475 H HB3    . LYS   A 1 309 ? 22.35056  -21.99581 -8.11820  1.000 206.37381 ? 310 LYS   A HB3    1 
ATOM   4476 H HG2    . LYS   A 1 309 ? 24.53793  -22.65106 -7.67503  1.000 207.86462 ? 310 LYS   A HG2    1 
ATOM   4477 H HG3    . LYS   A 1 309 ? 24.00516  -23.82709 -6.74847  1.000 207.86462 ? 310 LYS   A HG3    1 
ATOM   4478 H HD2    . LYS   A 1 309 ? 23.11313  -24.91088 -8.58598  1.000 207.08773 ? 310 LYS   A HD2    1 
ATOM   4479 H HD3    . LYS   A 1 309 ? 23.53993  -23.70614 -9.53037  1.000 207.08773 ? 310 LYS   A HD3    1 
ATOM   4480 H HE2    . LYS   A 1 309 ? 25.76432  -24.20326 -9.24911  1.000 207.07693 ? 310 LYS   A HE2    1 
ATOM   4481 H HE3    . LYS   A 1 309 ? 25.41971  -25.29542 -8.14737  1.000 207.07693 ? 310 LYS   A HE3    1 
ATOM   4482 H HZ1    . LYS   A 1 309 ? 25.75142  -26.49474 -9.92536  1.000 168.84341 ? 310 LYS   A HZ1    1 
ATOM   4483 H HZ2    . LYS   A 1 309 ? 24.30838  -26.37743 -9.97216  1.000 168.84341 ? 310 LYS   A HZ2    1 
ATOM   4484 H HZ3    . LYS   A 1 309 ? 25.13047  -25.55145 -10.83252 1.000 168.84341 ? 310 LYS   A HZ3    1 
ATOM   4485 N N      . SER   A 1 310 ? 21.76939  -19.38368 -6.59334  1.000 165.01489 ? 311 SER   A N      1 
ATOM   4486 C CA     . SER   A 1 310 ? 20.83491  -18.26495 -6.56935  1.000 170.38513 ? 311 SER   A CA     1 
ATOM   4487 C C      . SER   A 1 310 ? 19.81550  -18.35962 -7.69796  1.000 170.64693 ? 311 SER   A C      1 
ATOM   4488 O O      . SER   A 1 310 ? 18.60579  -18.26506 -7.46098  1.000 167.33744 ? 311 SER   A O      1 
ATOM   4489 C CB     . SER   A 1 310 ? 21.60970  -16.94768 -6.65611  1.000 184.94357 ? 311 SER   A CB     1 
ATOM   4490 O OG     . SER   A 1 310 ? 22.46972  -16.93535 -7.78433  1.000 187.26646 ? 311 SER   A OG     1 
ATOM   4491 H H      . SER   A 1 310 ? 22.54722  -19.18353 -6.90078  1.000 198.40834 ? 311 SER   A H      1 
ATOM   4492 H HA     . SER   A 1 310 ? 20.34782  -18.28121 -5.73068  1.000 204.85262 ? 311 SER   A HA     1 
ATOM   4493 H HB2    . SER   A 1 310 ? 20.97823  -16.21546 -6.73351  1.000 222.32276 ? 311 SER   A HB2    1 
ATOM   4494 H HB3    . SER   A 1 310 ? 22.14284  -16.84245 -5.85262  1.000 222.32276 ? 311 SER   A HB3    1 
ATOM   4495 H HG     . SER   A 1 310 ? 22.86231  -16.19470 -7.83823  1.000 225.11022 ? 311 SER   A HG     1 
ATOM   4496 N N      . LYS   A 1 311 ? 20.28429  -18.54175 -8.92864  1.000 177.19611 ? 312 LYS   A N      1 
ATOM   4497 C CA     . LYS   A 1 311 ? 19.42725  -18.58254 -10.10474 1.000 173.31082 ? 312 LYS   A CA     1 
ATOM   4498 C C      . LYS   A 1 311 ? 19.40998  -19.99118 -10.67770 1.000 166.62519 ? 312 LYS   A C      1 
ATOM   4499 O O      . LYS   A 1 311 ? 20.46548  -20.56003 -10.97610 1.000 175.68538 ? 312 LYS   A O      1 
ATOM   4500 C CB     . LYS   A 1 311 ? 19.90354  -17.58410 -11.16135 1.000 175.44213 ? 312 LYS   A CB     1 
ATOM   4501 C CG     . LYS   A 1 311 ? 19.64076  -16.13782 -10.78550 1.000 186.16325 ? 312 LYS   A CG     1 
ATOM   4502 C CD     . LYS   A 1 311 ? 20.07331  -15.18679 -11.88655 1.000 198.44355 ? 312 LYS   A CD     1 
ATOM   4503 C CE     . LYS   A 1 311 ? 19.78124  -13.73793 -11.52303 1.000 207.23385 ? 312 LYS   A CE     1 
ATOM   4504 N NZ     . LYS   A 1 311 ? 20.61710  -13.26185 -10.38462 1.000 210.12749 ? 312 LYS   A NZ     1 
ATOM   4505 H H      . LYS   A 1 311 ? 21.11827  -18.64675 -9.11042  1.000 213.02580 ? 312 LYS   A H      1 
ATOM   4506 H HA     . LYS   A 1 311 ? 18.52030  -18.35022 -9.85101  1.000 208.36345 ? 312 LYS   A HA     1 
ATOM   4507 H HB2    . LYS   A 1 311 ? 20.85978  -17.69065 -11.28441 1.000 210.92103 ? 312 LYS   A HB2    1 
ATOM   4508 H HB3    . LYS   A 1 311 ? 19.43978  -17.76424 -11.99404 1.000 210.92103 ? 312 LYS   A HB3    1 
ATOM   4509 H HG2    . LYS   A 1 311 ? 18.69111  -16.01368 -10.63171 1.000 223.78637 ? 312 LYS   A HG2    1 
ATOM   4510 H HG3    . LYS   A 1 311 ? 20.13830  -15.91960 -9.98193  1.000 223.78637 ? 312 LYS   A HG3    1 
ATOM   4511 H HD2    . LYS   A 1 311 ? 21.02802  -15.27752 -12.03215 1.000 238.52273 ? 312 LYS   A HD2    1 
ATOM   4512 H HD3    . LYS   A 1 311 ? 19.59179  -15.39912 -12.70139 1.000 238.52273 ? 312 LYS   A HD3    1 
ATOM   4513 H HE2    . LYS   A 1 311 ? 19.96653  -13.17385 -12.29010 1.000 249.07109 ? 312 LYS   A HE2    1 
ATOM   4514 H HE3    . LYS   A 1 311 ? 18.84897  -13.65554 -11.26811 1.000 249.07109 ? 312 LYS   A HE3    1 
ATOM   4515 H HZ1    . LYS   A 1 311 ? 20.42179  -12.41400 -10.19727 1.000 252.54346 ? 312 LYS   A HZ1    1 
ATOM   4516 H HZ2    . LYS   A 1 311 ? 20.46181  -13.76012 -9.66371  1.000 252.54346 ? 312 LYS   A HZ2    1 
ATOM   4517 H HZ3    . LYS   A 1 311 ? 21.47986  -13.31973 -10.59536 1.000 252.54346 ? 312 LYS   A HZ3    1 
ATOM   4518 N N      . ARG   A 1 312 ? 18.21223  -20.54078 -10.83901 1.000 161.88719 ? 313 ARG   A N      1 
ATOM   4519 C CA     . ARG   A 1 312 ? 18.01358  -21.89089 -11.33678 1.000 163.64883 ? 313 ARG   A CA     1 
ATOM   4520 C C      . ARG   A 1 312 ? 17.05981  -21.86035 -12.52021 1.000 169.22119 ? 313 ARG   A C      1 
ATOM   4521 O O      . ARG   A 1 312 ? 16.13840  -21.03850 -12.56003 1.000 174.57663 ? 313 ARG   A O      1 
ATOM   4522 C CB     . ARG   A 1 312 ? 17.45910  -22.80060 -10.23129 1.000 173.14780 ? 313 ARG   A CB     1 
ATOM   4523 C CG     . ARG   A 1 312 ? 18.35953  -22.86220 -9.00209  1.000 164.35170 ? 313 ARG   A CG     1 
ATOM   4524 C CD     . ARG   A 1 312 ? 17.66995  -23.50332 -7.81232  1.000 160.56217 ? 313 ARG   A CD     1 
ATOM   4525 N NE     . ARG   A 1 312 ? 18.29601  -23.09915 -6.55890  1.000 144.21050 ? 313 ARG   A NE     1 
ATOM   4526 C CZ     . ARG   A 1 312 ? 17.83509  -23.40806 -5.35526  1.000 148.22674 ? 313 ARG   A CZ     1 
ATOM   4527 N NH1    . ARG   A 1 312 ? 16.74545  -24.14198 -5.19965  1.000 166.90768 ? 313 ARG   A NH1    1 
ATOM   4528 N NH2    . ARG   A 1 312 ? 18.48166  -22.96582 -4.28043  1.000 148.31756 ? 313 ARG   A NH2    1 
ATOM   4529 H H      . ARG   A 1 312 ? 17.47531  -20.13518 -10.66002 1.000 194.65510 ? 313 ARG   A H      1 
ATOM   4530 H HA     . ARG   A 1 312 ? 18.85474  -22.26716 -11.63971 1.000 196.76907 ? 313 ARG   A HA     1 
ATOM   4531 H HB2    . ARG   A 1 312 ? 16.59343  -22.46405 -9.95156  1.000 208.16783 ? 313 ARG   A HB2    1 
ATOM   4532 H HB3    . ARG   A 1 312 ? 17.36790  -23.70081 -10.58086 1.000 208.16783 ? 313 ARG   A HB3    1 
ATOM   4533 H HG2    . ARG   A 1 312 ? 19.14815  -23.38667 -9.21163  1.000 197.61251 ? 313 ARG   A HG2    1 
ATOM   4534 H HG3    . ARG   A 1 312 ? 18.61723  -21.96132 -8.75129  1.000 197.61251 ? 313 ARG   A HG3    1 
ATOM   4535 H HD2    . ARG   A 1 312 ? 16.73982  -23.22879 -7.79259  1.000 193.06507 ? 313 ARG   A HD2    1 
ATOM   4536 H HD3    . ARG   A 1 312 ? 17.72944  -24.46860 -7.88710  1.000 193.06507 ? 313 ARG   A HD3    1 
ATOM   4537 H HE     . ARG   A 1 312 ? 19.01392  -22.62778 -6.60379  1.000 173.44308 ? 313 ARG   A HE     1 
ATOM   4538 H HH11   . ARG   A 1 312 ? 16.31909  -24.43016 -5.88868  1.000 200.67969 ? 313 ARG   A HH11   1 
ATOM   4539 H HH12   . ARG   A 1 312 ? 16.46347  -24.33089 -4.40946  1.000 200.67969 ? 313 ARG   A HH12   1 
ATOM   4540 H HH21   . ARG   A 1 312 ? 19.18941  -22.48583 -4.37158  1.000 178.37155 ? 313 ARG   A HH21   1 
ATOM   4541 H HH22   . ARG   A 1 312 ? 18.19200  -23.15985 -3.49426  1.000 178.37155 ? 313 ARG   A HH22   1 
ATOM   4542 N N      . PRO   A 1 313 ? 17.25943  -22.74323 -13.50336 1.000 166.33363 ? 314 PRO   A N      1 
ATOM   4543 C CA     . PRO   A 1 313 ? 16.45559  -22.64315 -14.73457 1.000 176.03069 ? 314 PRO   A CA     1 
ATOM   4544 C C      . PRO   A 1 313 ? 14.95911  -22.77214 -14.50316 1.000 183.22419 ? 314 PRO   A C      1 
ATOM   4545 O O      . PRO   A 1 313 ? 14.18020  -22.02094 -15.10215 1.000 189.49186 ? 314 PRO   A O      1 
ATOM   4546 C CB     . PRO   A 1 313 ? 17.00451  -23.78592 -15.60538 1.000 172.24741 ? 314 PRO   A CB     1 
ATOM   4547 C CG     . PRO   A 1 313 ? 17.67994  -24.71829 -14.65917 1.000 158.97108 ? 314 PRO   A CG     1 
ATOM   4548 C CD     . PRO   A 1 313 ? 18.20908  -23.86947 -13.54541 1.000 159.75581 ? 314 PRO   A CD     1 
ATOM   4549 H HA     . PRO   A 1 313 ? 16.63408  -21.79373 -15.16762 1.000 211.62730 ? 314 PRO   A HA     1 
ATOM   4550 H HB2    . PRO   A 1 313 ? 16.27368  -24.22898 -16.06417 1.000 207.08736 ? 314 PRO   A HB2    1 
ATOM   4551 H HB3    . PRO   A 1 313 ? 17.63581  -23.43211 -16.25128 1.000 207.08736 ? 314 PRO   A HB3    1 
ATOM   4552 H HG2    . PRO   A 1 313 ? 17.03810  -25.36325 -14.32306 1.000 191.15577 ? 314 PRO   A HG2    1 
ATOM   4553 H HG3    . PRO   A 1 313 ? 18.40373  -25.17667 -15.11404 1.000 191.15577 ? 314 PRO   A HG3    1 
ATOM   4554 H HD2    . PRO   A 1 313 ? 18.20485  -24.35703 -12.70685 1.000 192.09744 ? 314 PRO   A HD2    1 
ATOM   4555 H HD3    . PRO   A 1 313 ? 19.10616  -23.55834 -13.74375 1.000 192.09744 ? 314 PRO   A HD3    1 
ATOM   4556 N N      . LEU   A 1 314 ? 14.52944  -23.69428 -13.65476 1.000 181.04175 ? 315 LEU   A N      1 
ATOM   4557 C CA     . LEU   A 1 314 ? 13.11670  -23.91291 -13.39166 1.000 176.48150 ? 315 LEU   A CA     1 
ATOM   4558 C C      . LEU   A 1 314 ? 12.93224  -24.21422 -11.90921 1.000 173.17782 ? 315 LEU   A C      1 
ATOM   4559 O O      . LEU   A 1 314 ? 13.89745  -24.53917 -11.21512 1.000 176.32405 ? 315 LEU   A O      1 
ATOM   4560 C CB     . LEU   A 1 314 ? 12.56238  -25.06218 -14.24334 1.000 178.99458 ? 315 LEU   A CB     1 
ATOM   4561 C CG     . LEU   A 1 314 ? 12.56070  -24.83096 -15.75757 1.000 174.99934 ? 315 LEU   A CG     1 
ATOM   4562 C CD1    . LEU   A 1 314 ? 12.17580  -26.10692 -16.49411 1.000 175.44752 ? 315 LEU   A CD1    1 
ATOM   4563 C CD2    . LEU   A 1 314 ? 11.62166  -23.69547 -16.13636 1.000 179.27658 ? 315 LEU   A CD2    1 
ATOM   4564 H H      . LEU   A 1 314 ? 15.04892  -24.21624 -13.21058 1.000 217.64058 ? 315 LEU   A H      1 
ATOM   4565 H HA     . LEU   A 1 314 ? 12.61260  -23.11064 -13.59939 1.000 212.16827 ? 315 LEU   A HA     1 
ATOM   4566 H HB2    . LEU   A 1 314 ? 13.09965  -25.85170 -14.07334 1.000 215.18396 ? 315 LEU   A HB2    1 
ATOM   4567 H HB3    . LEU   A 1 314 ? 11.64386  -25.22198 -13.97558 1.000 215.18396 ? 315 LEU   A HB3    1 
ATOM   4568 H HG     . LEU   A 1 314 ? 13.45648  -24.57933 -16.03174 1.000 210.38967 ? 315 LEU   A HG     1 
ATOM   4569 H HD11   . LEU   A 1 314 ? 12.19408  -25.93804 -17.44912 1.000 210.92750 ? 315 LEU   A HD11   1 
ATOM   4570 H HD12   . LEU   A 1 314 ? 12.81070  -26.80501 -16.26943 1.000 210.92750 ? 315 LEU   A HD12   1 
ATOM   4571 H HD13   . LEU   A 1 314 ? 11.28315  -26.37158 -16.22202 1.000 210.92750 ? 315 LEU   A HD13   1 
ATOM   4572 H HD21   . LEU   A 1 314 ? 11.59956  -23.61295 -17.10259 1.000 215.52237 ? 315 LEU   A HD21   1 
ATOM   4573 H HD22   . LEU   A 1 314 ? 10.73360  -23.89490 -15.80100 1.000 215.52237 ? 315 LEU   A HD22   1 
ATOM   4574 H HD23   . LEU   A 1 314 ? 11.94708  -22.87146 -15.74136 1.000 215.52237 ? 315 LEU   A HD23   1 
ATOM   4575 N N      . PRO   A 1 315 ? 11.70359  -24.10299 -11.40664 1.000 177.52062 ? 316 PRO   A N      1 
ATOM   4576 C CA     . PRO   A 1 315 ? 11.47847  -24.32884 -9.96993  1.000 180.42496 ? 316 PRO   A CA     1 
ATOM   4577 C C      . PRO   A 1 315 ? 11.97579  -25.69705 -9.52697  1.000 169.95743 ? 316 PRO   A C      1 
ATOM   4578 O O      . PRO   A 1 315 ? 11.59292  -26.72872 -10.08347 1.000 168.42336 ? 316 PRO   A O      1 
ATOM   4579 C CB     . PRO   A 1 315 ? 9.95567   -24.20629 -9.82942  1.000 191.78660 ? 316 PRO   A CB     1 
ATOM   4580 C CG     . PRO   A 1 315 ? 9.53861   -23.34507 -10.96997 1.000 204.14694 ? 316 PRO   A CG     1 
ATOM   4581 C CD     . PRO   A 1 315 ? 10.47511  -23.67601 -12.09890 1.000 166.87252 ? 316 PRO   A CD     1 
ATOM   4582 H HA     . PRO   A 1 315 ? 11.91891  -23.64150 -9.44602  1.000 216.90042 ? 316 PRO   A HA     1 
ATOM   4583 H HB2    . PRO   A 1 315 ? 9.54596   -25.08359 -9.88760  1.000 230.53439 ? 316 PRO   A HB2    1 
ATOM   4584 H HB3    . PRO   A 1 315 ? 9.73356   -23.79201 -8.98093  1.000 230.53439 ? 316 PRO   A HB3    1 
ATOM   4585 H HG2    . PRO   A 1 315 ? 8.62171   -23.54674 -11.21394 1.000 245.36680 ? 316 PRO   A HG2    1 
ATOM   4586 H HG3    . PRO   A 1 315 ? 9.61778   -22.41102 -10.72060 1.000 245.36680 ? 316 PRO   A HG3    1 
ATOM   4587 H HD2    . PRO   A 1 315 ? 10.11839  -24.39485 -12.64380 1.000 200.63750 ? 316 PRO   A HD2    1 
ATOM   4588 H HD3    . PRO   A 1 315 ? 10.64259  -22.89465 -12.64874 1.000 200.63750 ? 316 PRO   A HD3    1 
ATOM   4589 N N      . ILE   A 1 316 ? 12.83681  -25.69696 -8.50898  1.000 156.19331 ? 317 ILE   A N      1 
ATOM   4590 C CA     . ILE   A 1 316 ? 13.38298  -26.93195 -7.95973  1.000 154.19508 ? 317 ILE   A CA     1 
ATOM   4591 C C      . ILE   A 1 316 ? 13.89185  -26.63984 -6.55751  1.000 168.47497 ? 317 ILE   A C      1 
ATOM   4592 O O      . ILE   A 1 316 ? 14.32805  -25.52463 -6.25986  1.000 162.80008 ? 317 ILE   A O      1 
ATOM   4593 C CB     . ILE   A 1 316 ? 14.50562  -27.50437 -8.86260  1.000 163.34908 ? 317 ILE   A CB     1 
ATOM   4594 C CG1    . ILE   A 1 316 ? 14.97877  -28.85771 -8.32481  1.000 157.57965 ? 317 ILE   A CG1    1 
ATOM   4595 C CG2    . ILE   A 1 316 ? 15.67040  -26.52634 -8.94479  1.000 173.63704 ? 317 ILE   A CG2    1 
ATOM   4596 C CD1    . ILE   A 1 316 ? 16.01023  -29.54611 -9.19753  1.000 157.41605 ? 317 ILE   A CD1    1 
ATOM   4597 H H      . ILE   A 1 316 ? 13.12128  -24.98624 -8.11712  1.000 187.82244 ? 317 ILE   A H      1 
ATOM   4598 H HA     . ILE   A 1 316 ? 12.67230  -27.58943 -7.90006  1.000 185.42456 ? 317 ILE   A HA     1 
ATOM   4599 H HB     . ILE   A 1 316 ? 14.14777  -27.63381 -9.75484  1.000 196.40936 ? 317 ILE   A HB     1 
ATOM   4600 H HG12   . ILE   A 1 316 ? 15.37624  -28.72237 -7.45039  1.000 189.48605 ? 317 ILE   A HG12   1 
ATOM   4601 H HG13   . ILE   A 1 316 ? 14.21257  -29.44822 -8.25316  1.000 189.48605 ? 317 ILE   A HG13   1 
ATOM   4602 H HG21   . ILE   A 1 316 ? 16.29320  -26.83316 -9.62220  1.000 208.75492 ? 317 ILE   A HG21   1 
ATOM   4603 H HG22   . ILE   A 1 316 ? 15.33022  -25.64924 -9.18116  1.000 208.75492 ? 317 ILE   A HG22   1 
ATOM   4604 H HG23   . ILE   A 1 316 ? 16.11228  -26.48828 -8.08212  1.000 208.75492 ? 317 ILE   A HG23   1 
ATOM   4605 H HD11   . ILE   A 1 316 ? 16.22862  -30.40750 -8.80867  1.000 189.28974 ? 317 ILE   A HD11   1 
ATOM   4606 H HD12   . ILE   A 1 316 ? 15.64103  -29.66838 -10.08615 1.000 189.28974 ? 317 ILE   A HD12   1 
ATOM   4607 H HD13   . ILE   A 1 316 ? 16.80546  -28.99254 -9.24302  1.000 189.28974 ? 317 ILE   A HD13   1 
ATOM   4608 N N      . THR   A 1 317 ? 13.83933  -27.65159 -5.69498  1.000 180.98374 ? 318 THR   A N      1 
ATOM   4609 C CA     . THR   A 1 317 ? 14.36808  -27.55067 -4.34038  1.000 156.85442 ? 318 THR   A CA     1 
ATOM   4610 C C      . THR   A 1 317 ? 14.63173  -28.96288 -3.82944  1.000 143.50254 ? 318 THR   A C      1 
ATOM   4611 O O      . THR   A 1 317 ? 14.40743  -29.95065 -4.53465  1.000 154.61158 ? 318 THR   A O      1 
ATOM   4612 C CB     . THR   A 1 317 ? 13.40753  -26.79337 -3.41957  1.000 143.14600 ? 318 THR   A CB     1 
ATOM   4613 O OG1    . THR   A 1 317 ? 14.07553  -26.46527 -2.19496  1.000 140.96139 ? 318 THR   A OG1    1 
ATOM   4614 C CG2    . THR   A 1 317 ? 12.17970  -27.63747 -3.11297  1.000 142.61238 ? 318 THR   A CG2    1 
ATOM   4615 H H      . THR   A 1 317 ? 13.49624  -28.41941 -5.87484  1.000 217.57096 ? 318 THR   A H      1 
ATOM   4616 H HA     . THR   A 1 317 ? 15.20820  -27.06645 -4.36555  1.000 188.61577 ? 318 THR   A HA     1 
ATOM   4617 H HB     . THR   A 1 317 ? 13.11540  -25.97905 -3.85824  1.000 172.16567 ? 318 THR   A HB     1 
ATOM   4618 H HG1    . THR   A 1 317 ? 14.65315  -25.87122 -2.33302  1.000 169.54414 ? 318 THR   A HG1    1 
ATOM   4619 H HG21   . THR   A 1 317 ? 11.45978  -27.07179 -2.79262  1.000 171.52532 ? 318 THR   A HG21   1 
ATOM   4620 H HG22   . THR   A 1 317 ? 11.88531  -28.09817 -3.91422  1.000 171.52532 ? 318 THR   A HG22   1 
ATOM   4621 H HG23   . THR   A 1 317 ? 12.39067  -28.29471 -2.43149  1.000 171.52532 ? 318 THR   A HG23   1 
ATOM   4622 N N      . MET   A 1 318 ? 15.10871  -29.05297 -2.58962  1.000 127.66460 ? 319 MET   A N      1 
ATOM   4623 C CA     . MET   A 1 318 ? 15.44786  -30.33435 -1.98994  1.000 135.23764 ? 319 MET   A CA     1 
ATOM   4624 C C      . MET   A 1 318 ? 14.92207  -30.38295 -0.56393  1.000 139.17100 ? 319 MET   A C      1 
ATOM   4625 O O      . MET   A 1 318 ? 14.80742  -29.35506 0.10897   1.000 135.28138 ? 319 MET   A O      1 
ATOM   4626 C CB     . MET   A 1 318 ? 16.96302  -30.57276 -1.99449  1.000 143.69694 ? 319 MET   A CB     1 
ATOM   4627 C CG     . MET   A 1 318 ? 17.65242  -30.11394 -3.26667  1.000 147.02097 ? 319 MET   A CG     1 
ATOM   4628 S SD     . MET   A 1 318 ? 19.31273  -30.79192 -3.44793  1.000 143.35102 ? 319 MET   A SD     1 
ATOM   4629 C CE     . MET   A 1 318 ? 20.16318  -30.02374 -2.07163  1.000 132.43356 ? 319 MET   A CE     1 
ATOM   4630 H H      . MET   A 1 318 ? 15.24476  -28.37839 -2.07384  1.000 153.58799 ? 319 MET   A H      1 
ATOM   4631 H HA     . MET   A 1 318 ? 15.02886  -31.04455 -2.50078  1.000 162.67563 ? 319 MET   A HA     1 
ATOM   4632 H HB2    . MET   A 1 318 ? 17.35697  -30.08717 -1.25293  1.000 172.82680 ? 319 MET   A HB2    1 
ATOM   4633 H HB3    . MET   A 1 318 ? 17.12909  -31.52317 -1.89432  1.000 172.82680 ? 319 MET   A HB3    1 
ATOM   4634 H HG2    . MET   A 1 318 ? 17.12737  -30.39941 -4.03069  1.000 176.81564 ? 319 MET   A HG2    1 
ATOM   4635 H HG3    . MET   A 1 318 ? 17.72355  -29.14661 -3.25579  1.000 176.81564 ? 319 MET   A HG3    1 
ATOM   4636 H HE1    . MET   A 1 318 ? 20.08901  -29.05999 -2.15276  1.000 159.31074 ? 319 MET   A HE1    1 
ATOM   4637 H HE2    . MET   A 1 318 ? 19.75367  -30.31843 -1.24316  1.000 159.31074 ? 319 MET   A HE2    1 
ATOM   4638 H HE3    . MET   A 1 318 ? 21.09673  -30.28644 -2.09092  1.000 159.31074 ? 319 MET   A HE3    1 
ATOM   4639 N N      . ILE   A 1 319 ? 14.60248  -31.59595 -0.10921  1.000 131.97810 ? 320 ILE   A N      1 
ATOM   4640 C CA     . ILE   A 1 319 ? 14.10535  -31.82259 1.24016   1.000 120.74111 ? 320 ILE   A CA     1 
ATOM   4641 C C      . ILE   A 1 319 ? 14.68444  -33.12920 1.76411   1.000 118.09624 ? 320 ILE   A C      1 
ATOM   4642 O O      . ILE   A 1 319 ? 15.12730  -33.99242 1.00354   1.000 115.49349 ? 320 ILE   A O      1 
ATOM   4643 C CB     . ILE   A 1 319 ? 12.56069  -31.86343 1.30222   1.000 119.79299 ? 320 ILE   A CB     1 
ATOM   4644 C CG1    . ILE   A 1 319 ? 12.01544  -32.98006 0.40888   1.000 122.38495 ? 320 ILE   A CG1    1 
ATOM   4645 C CG2    . ILE   A 1 319 ? 11.97629  -30.51981 0.89289   1.000 120.53734 ? 320 ILE   A CG2    1 
ATOM   4646 C CD1    . ILE   A 1 319 ? 10.51069  -33.14675 0.48734   1.000 112.26158 ? 320 ILE   A CD1    1 
ATOM   4647 H H      . ILE   A 1 319 ? 14.66793  -32.31498 -0.57644  1.000 158.76419 ? 320 ILE   A H      1 
ATOM   4648 H HA     . ILE   A 1 319 ? 14.41119  -31.10209 1.81308   1.000 145.27980 ? 320 ILE   A HA     1 
ATOM   4649 H HB     . ILE   A 1 319 ? 12.29879  -32.04892 2.21759   1.000 144.14206 ? 320 ILE   A HB     1 
ATOM   4650 H HG12   . ILE   A 1 319 ? 12.24341  -32.78125 -0.51275  1.000 147.25241 ? 320 ILE   A HG12   1 
ATOM   4651 H HG13   . ILE   A 1 319 ? 12.42047  -33.81964 0.67713   1.000 147.25241 ? 320 ILE   A HG13   1 
ATOM   4652 H HG21   . ILE   A 1 319 ? 11.02031  -30.52805 1.05701   1.000 145.03527 ? 320 ILE   A HG21   1 
ATOM   4653 H HG22   . ILE   A 1 319 ? 12.39592  -29.81996 1.41732   1.000 145.03527 ? 320 ILE   A HG22   1 
ATOM   4654 H HG23   . ILE   A 1 319 ? 12.14870  -30.37468 -0.05057  1.000 145.03527 ? 320 ILE   A HG23   1 
ATOM   4655 H HD11   . ILE   A 1 319 ? 10.25702  -33.95299 0.01139   1.000 135.10436 ? 320 ILE   A HD11   1 
ATOM   4656 H HD12   . ILE   A 1 319 ? 10.24879  -33.21621 1.41873   1.000 135.10436 ? 320 ILE   A HD12   1 
ATOM   4657 H HD13   . ILE   A 1 319 ? 10.08587  -32.37521 0.08094   1.000 135.10436 ? 320 ILE   A HD13   1 
ATOM   4658 N N      . GLY   A 1 320 ? 14.67596  -33.26261 3.08646   1.000 139.91056 ? 321 GLY   A N      1 
ATOM   4659 C CA     . GLY   A 1 320 ? 15.11877  -34.48647 3.71863   1.000 141.00098 ? 321 GLY   A CA     1 
ATOM   4660 C C      . GLY   A 1 320 ? 16.63049  -34.61989 3.72808   1.000 122.25771 ? 321 GLY   A C      1 
ATOM   4661 O O      . GLY   A 1 320 ? 17.38044  -33.64117 3.64481   1.000 117.23565 ? 321 GLY   A O      1 
ATOM   4662 H H      . GLY   A 1 320 ? 14.41684  -32.65461 3.63672   1.000 168.28314 ? 321 GLY   A H      1 
ATOM   4663 H HA2    . GLY   A 1 320 ? 14.80482  -34.50538 4.63623   1.000 169.59165 ? 321 GLY   A HA2    1 
ATOM   4664 H HA3    . GLY   A 1 320 ? 14.74818  -35.24588 3.24235   1.000 169.59165 ? 321 GLY   A HA3    1 
ATOM   4665 N N      . ASP   A 1 321 ? 17.08003  -35.87262 3.83244   1.000 116.29996 ? 322 ASP   A N      1 
ATOM   4666 C CA     . ASP   A 1 321 ? 18.51373  -36.13306 3.87050   1.000 118.53617 ? 322 ASP   A CA     1 
ATOM   4667 C C      . ASP   A 1 321 ? 19.21369  -35.58510 2.63599   1.000 132.88755 ? 322 ASP   A C      1 
ATOM   4668 O O      . ASP   A 1 321 ? 20.37079  -35.15674 2.71931   1.000 132.72053 ? 322 ASP   A O      1 
ATOM   4669 C CB     . ASP   A 1 321 ? 18.77213  -37.63101 4.00817   1.000 110.29090 ? 322 ASP   A CB     1 
ATOM   4670 C CG     . ASP   A 1 321 ? 18.56050  -38.12429 5.41876   1.000 106.64319 ? 322 ASP   A CG     1 
ATOM   4671 O OD1    . ASP   A 1 321 ? 17.95801  -37.38159 6.22220   1.000 118.17613 ? 322 ASP   A OD1    1 
ATOM   4672 O OD2    . ASP   A 1 321 ? 19.00669  -39.24785 5.72772   1.000 108.53373 ? 322 ASP   A OD2    1 
ATOM   4673 H H      . ASP   A 1 321 ? 16.58405  -36.57346 3.88171   1.000 139.95042 ? 322 ASP   A H      1 
ATOM   4674 H HA     . ASP   A 1 321 ? 18.89038  -35.69292 4.64851   1.000 142.63388 ? 322 ASP   A HA     1 
ATOM   4675 H HB2    . ASP   A 1 321 ? 18.16402  -38.11284 3.42598   1.000 132.73955 ? 322 ASP   A HB2    1 
ATOM   4676 H HB3    . ASP   A 1 321 ? 19.69016  -37.81909 3.75767   1.000 132.73955 ? 322 ASP   A HB3    1 
ATOM   4677 N N      . ALA   A 1 322 ? 18.53334  -35.58362 1.48653   1.000 119.04458 ? 323 ALA   A N      1 
ATOM   4678 C CA     . ALA   A 1 322 ? 19.11812  -34.98649 0.29198   1.000 117.70084 ? 323 ALA   A CA     1 
ATOM   4679 C C      . ALA   A 1 322 ? 19.49342  -33.53043 0.52699   1.000 128.29165 ? 323 ALA   A C      1 
ATOM   4680 O O      . ALA   A 1 322 ? 20.41799  -33.01608 -0.11266  1.000 131.05915 ? 323 ALA   A O      1 
ATOM   4681 C CB     . ALA   A 1 322 ? 18.14649  -35.09610 -0.88201  1.000 129.28303 ? 323 ALA   A CB     1 
ATOM   4682 H H      . ALA   A 1 322 ? 17.74769  -35.91572 1.37665   1.000 143.24396 ? 323 ALA   A H      1 
ATOM   4683 H HA     . ALA   A 1 322 ? 19.92341  -35.47553 0.06123   1.000 141.63148 ? 323 ALA   A HA     1 
ATOM   4684 H HB1    . ALA   A 1 322 ? 18.56516  -34.72452 -1.67418  1.000 155.53011 ? 323 ALA   A HB1    1 
ATOM   4685 H HB2    . ALA   A 1 322 ? 17.93240  -36.03076 -1.02854  1.000 155.53011 ? 323 ALA   A HB2    1 
ATOM   4686 H HB3    . ALA   A 1 322 ? 17.33943  -34.60099 -0.67127  1.000 155.53011 ? 323 ALA   A HB3    1 
ATOM   4687 N N      . ALA   A 1 323 ? 18.79632  -32.85499 1.43976   1.000 120.11892 ? 324 ALA   A N      1 
ATOM   4688 C CA     . ALA   A 1 323 ? 19.07616  -31.45767 1.73430   1.000 112.63650 ? 324 ALA   A CA     1 
ATOM   4689 C C      . ALA   A 1 323 ? 20.09205  -31.28101 2.85187   1.000 116.93696 ? 324 ALA   A C      1 
ATOM   4690 O O      . ALA   A 1 323 ? 20.84153  -30.29781 2.84518   1.000 124.91005 ? 324 ALA   A O      1 
ATOM   4691 C CB     . ALA   A 1 323 ? 17.78242  -30.73228 2.11453   1.000 118.99469 ? 324 ALA   A CB     1 
ATOM   4692 H H      . ALA   A 1 323 ? 18.15302  -33.18822 1.90315   1.000 144.53318 ? 324 ALA   A H      1 
ATOM   4693 H HA     . ALA   A 1 323 ? 19.43500  -31.04010 0.93570   1.000 135.55428 ? 324 ALA   A HA     1 
ATOM   4694 H HB1    . ALA   A 1 323 ? 17.98949  -29.80959 2.33054   1.000 143.18409 ? 324 ALA   A HB1    1 
ATOM   4695 H HB2    . ALA   A 1 323 ? 17.16884  -30.76663 1.36404   1.000 143.18409 ? 324 ALA   A HB2    1 
ATOM   4696 H HB3    . ALA   A 1 323 ? 17.38845  -31.17180 2.88427   1.000 143.18409 ? 324 ALA   A HB3    1 
ATOM   4697 N N      . HIS   A 1 324 ? 20.14362  -32.21051 3.80552   1.000 121.11762 ? 325 HIS   A N      1 
ATOM   4698 C CA     . HIS   A 1 324 ? 20.94581  -32.01186 5.00552   1.000 123.36114 ? 325 HIS   A CA     1 
ATOM   4699 C C      . HIS   A 1 324 ? 21.26565  -33.32587 5.70451   1.000 115.30143 ? 325 HIS   A C      1 
ATOM   4700 O O      . HIS   A 1 324 ? 20.97915  -33.48522 6.89538   1.000 104.56312 ? 325 HIS   A O      1 
ATOM   4701 C CB     . HIS   A 1 324 ? 20.20924  -31.07734 5.96776   1.000 112.53061 ? 325 HIS   A CB     1 
ATOM   4702 C CG     . HIS   A 1 324 ? 18.76542  -31.42831 6.14936   1.000 109.57692 ? 325 HIS   A CG     1 
ATOM   4703 N ND1    . HIS   A 1 324 ? 18.35421  -32.59483 6.75784   1.000 103.78994 ? 325 HIS   A ND1    1 
ATOM   4704 C CD2    . HIS   A 1 324 ? 17.63635  -30.77612 5.78431   1.000 112.15553 ? 325 HIS   A CD2    1 
ATOM   4705 C CE1    . HIS   A 1 324 ? 17.03404  -32.64090 6.76951   1.000 114.33848 ? 325 HIS   A CE1    1 
ATOM   4706 N NE2    . HIS   A 1 324 ? 16.57393  -31.54996 6.18379   1.000 116.24309 ? 325 HIS   A NE2    1 
ATOM   4707 H H      . HIS   A 1 324 ? 19.72404  -32.96075 3.77908   1.000 145.73162 ? 325 HIS   A H      1 
ATOM   4708 H HA     . HIS   A 1 324 ? 21.79040  -31.61050 4.74770   1.000 148.42384 ? 325 HIS   A HA     1 
ATOM   4709 H HB2    . HIS   A 1 324 ? 20.63776  -31.12157 6.83685   1.000 135.42720 ? 325 HIS   A HB2    1 
ATOM   4710 H HB3    . HIS   A 1 324 ? 20.25415  -30.17241 5.62138   1.000 135.42720 ? 325 HIS   A HB3    1 
ATOM   4711 H HD2    . HIS   A 1 324 ? 17.58898  -29.95760 5.34536   1.000 134.97710 ? 325 HIS   A HD2    1 
ATOM   4712 H HE1    . HIS   A 1 324 ? 16.51661  -33.32500 7.12893   1.000 137.59665 ? 325 HIS   A HE1    1 
ATOM   4713 N N      . LEU   A 1 325 ? 21.84979  -34.27555 4.97685   1.000 120.12158 ? 326 LEU   A N      1 
ATOM   4714 C CA     . LEU   A 1 325 ? 22.37288  -35.47537 5.61440   1.000 127.92033 ? 326 LEU   A CA     1 
ATOM   4715 C C      . LEU   A 1 325 ? 23.27622  -35.08256 6.77594   1.000 131.26345 ? 326 LEU   A C      1 
ATOM   4716 O O      . LEU   A 1 325 ? 24.06149  -34.13718 6.67608   1.000 127.20566 ? 326 LEU   A O      1 
ATOM   4717 C CB     . LEU   A 1 325 ? 23.15187  -36.32042 4.60578   1.000 117.29238 ? 326 LEU   A CB     1 
ATOM   4718 C CG     . LEU   A 1 325 ? 23.86891  -37.54762 5.17563   1.000 108.65620 ? 326 LEU   A CG     1 
ATOM   4719 C CD1    . LEU   A 1 325 ? 22.87950  -38.65807 5.48314   1.000 110.98915 ? 326 LEU   A CD1    1 
ATOM   4720 C CD2    . LEU   A 1 325 ? 24.94385  -38.03175 4.21932   1.000 131.59154 ? 326 LEU   A CD2    1 
ATOM   4721 H H      . LEU   A 1 325 ? 21.95343  -34.24776 4.12357   1.000 144.53637 ? 326 LEU   A H      1 
ATOM   4722 H HA     . LEU   A 1 325 ? 21.64015  -36.01606 5.94856   1.000 153.89487 ? 326 LEU   A HA     1 
ATOM   4723 H HB2    . LEU   A 1 325 ? 22.53031  -36.63734 3.93189   1.000 141.14132 ? 326 LEU   A HB2    1 
ATOM   4724 H HB3    . LEU   A 1 325 ? 23.82688  -35.75719 4.19586   1.000 141.14132 ? 326 LEU   A HB3    1 
ATOM   4725 H HG     . LEU   A 1 325 ? 24.30026  -37.29845 6.00795   1.000 130.77791 ? 326 LEU   A HG     1 
ATOM   4726 H HD11   . LEU   A 1 325 ? 23.36190  -39.42213 5.83584   1.000 133.57745 ? 326 LEU   A HD11   1 
ATOM   4727 H HD12   . LEU   A 1 325 ? 22.24035  -38.33882 6.13924   1.000 133.57745 ? 326 LEU   A HD12   1 
ATOM   4728 H HD13   . LEU   A 1 325 ? 22.41905  -38.90596 4.66617   1.000 133.57745 ? 326 LEU   A HD13   1 
ATOM   4729 H HD21   . LEU   A 1 325 ? 25.32425  -38.85539 4.56257   1.000 158.30032 ? 326 LEU   A HD21   1 
ATOM   4730 H HD22   . LEU   A 1 325 ? 24.54494  -38.18903 3.34925   1.000 158.30032 ? 326 LEU   A HD22   1 
ATOM   4731 H HD23   . LEU   A 1 325 ? 25.63325  -37.35297 4.14931   1.000 158.30032 ? 326 LEU   A HD23   1 
ATOM   4732 N N      . MET   A 1 326 ? 23.16113  -35.81036 7.88080   1.000 139.82383 ? 327 MET   A N      1 
ATOM   4733 C CA     . MET   A 1 326 ? 23.94878  -35.52897 9.07207   1.000 132.26273 ? 327 MET   A CA     1 
ATOM   4734 C C      . MET   A 1 326 ? 24.09040  -36.81501 9.86903   1.000 125.18354 ? 327 MET   A C      1 
ATOM   4735 O O      . MET   A 1 326 ? 23.30733  -37.75221 9.68541   1.000 144.76647 ? 327 MET   A O      1 
ATOM   4736 C CB     . MET   A 1 326 ? 23.29531  -34.44004 9.93270   1.000 113.67737 ? 327 MET   A CB     1 
ATOM   4737 C CG     . MET   A 1 326 ? 21.95015  -34.84187 10.51145  1.000 115.88290 ? 327 MET   A CG     1 
ATOM   4738 S SD     . MET   A 1 326 ? 21.14994  -33.52570 11.44982  1.000 125.11618 ? 327 MET   A SD     1 
ATOM   4739 C CE     . MET   A 1 326 ? 20.42912  -32.54967 10.13095  1.000 128.39010 ? 327 MET   A CE     1 
ATOM   4740 H H      . MET   A 1 326 ? 22.62748  -36.47950 7.96487   1.000 168.17907 ? 327 MET   A H      1 
ATOM   4741 H HA     . MET   A 1 326 ? 24.82910  -35.21871 8.80809   1.000 159.10575 ? 327 MET   A HA     1 
ATOM   4742 H HB2    . MET   A 1 326 ? 23.88599  -34.23190 10.67343  1.000 136.80332 ? 327 MET   A HB2    1 
ATOM   4743 H HB3    . MET   A 1 326 ? 23.15836  -33.65079 9.38568   1.000 136.80332 ? 327 MET   A HB3    1 
ATOM   4744 H HG2    . MET   A 1 326 ? 21.35799  -35.09059 9.78455   1.000 139.44995 ? 327 MET   A HG2    1 
ATOM   4745 H HG3    . MET   A 1 326 ? 22.07831  -35.59607 11.10782  1.000 139.44995 ? 327 MET   A HG3    1 
ATOM   4746 H HE1    . MET   A 1 326 ? 20.01059  -31.76248 10.51314  1.000 154.45859 ? 327 MET   A HE1    1 
ATOM   4747 H HE2    . MET   A 1 326 ? 21.12982  -32.28539 9.51445   1.000 154.45859 ? 327 MET   A HE2    1 
ATOM   4748 H HE3    . MET   A 1 326 ? 19.76589  -33.08514 9.66804   1.000 154.45859 ? 327 MET   A HE3    1 
ATOM   4749 N N      . PRO   A 1 327 ? 25.08593  -36.89318 10.75259  1.000 105.92033 ? 328 PRO   A N      1 
ATOM   4750 C CA     . PRO   A 1 327 ? 25.20284  -38.07339 11.60261  1.000 110.58580 ? 328 PRO   A CA     1 
ATOM   4751 C C      . PRO   A 1 327 ? 23.91690  -38.30412 12.37461  1.000 135.56817 ? 328 PRO   A C      1 
ATOM   4752 O O      . PRO   A 1 327 ? 23.21584  -37.34610 12.74324  1.000 138.60956 ? 328 PRO   A O      1 
ATOM   4753 C CB     . PRO   A 1 327 ? 26.36724  -37.71688 12.53864  1.000 122.21312 ? 328 PRO   A CB     1 
ATOM   4754 C CG     . PRO   A 1 327 ? 27.19757  -36.77577 11.75393  1.000 124.24504 ? 328 PRO   A CG     1 
ATOM   4755 C CD     . PRO   A 1 327 ? 26.24377  -35.99266 10.88769  1.000 108.72404 ? 328 PRO   A CD     1 
ATOM   4756 H HA     . PRO   A 1 327 ? 25.42316  -38.86141 11.08167  1.000 133.09343 ? 328 PRO   A HA     1 
ATOM   4757 H HB2    . PRO   A 1 327 ? 26.02898  -37.29570 13.34430  1.000 147.04622 ? 328 PRO   A HB2    1 
ATOM   4758 H HB3    . PRO   A 1 327 ? 26.86685  -38.51637 12.76693  1.000 147.04622 ? 328 PRO   A HB3    1 
ATOM   4759 H HG2    . PRO   A 1 327 ? 27.67687  -36.18494 12.35568  1.000 149.48452 ? 328 PRO   A HG2    1 
ATOM   4760 H HG3    . PRO   A 1 327 ? 27.82574  -37.27359 11.20759  1.000 149.48452 ? 328 PRO   A HG3    1 
ATOM   4761 H HD2    . PRO   A 1 327 ? 25.98682  -35.16340 11.32035  1.000 130.17821 ? 328 PRO   A HD2    1 
ATOM   4762 H HD3    . PRO   A 1 327 ? 26.63852  -35.80646 10.02143  1.000 130.17821 ? 328 PRO   A HD3    1 
ATOM   4763 N N      . PRO   A 1 328 ? 23.57056  -39.56331 12.63422  1.000 140.08689 ? 329 PRO   A N      1 
ATOM   4764 C CA     . PRO   A 1 328 ? 22.31440  -39.86039 13.33254  1.000 116.70669 ? 329 PRO   A CA     1 
ATOM   4765 C C      . PRO   A 1 328 ? 22.44763  -39.96853 14.84075  1.000 142.84727 ? 329 PRO   A C      1 
ATOM   4766 O O      . PRO   A 1 328 ? 21.46115  -40.30804 15.50447  1.000 144.17609 ? 329 PRO   A O      1 
ATOM   4767 C CB     . PRO   A 1 328 ? 21.93634  -41.21584 12.73127  1.000 126.30129 ? 329 PRO   A CB     1 
ATOM   4768 C CG     . PRO   A 1 328 ? 23.26734  -41.89630 12.57440  1.000 127.52877 ? 329 PRO   A CG     1 
ATOM   4769 C CD     . PRO   A 1 328 ? 24.28146  -40.80233 12.26596  1.000 128.26036 ? 329 PRO   A CD     1 
ATOM   4770 H HA     . PRO   A 1 328 ? 21.63080  -39.20739 13.11534  1.000 140.43850 ? 329 PRO   A HA     1 
ATOM   4771 H HB2    . PRO   A 1 328 ? 21.35702  -41.70492 13.33632  1.000 151.95202 ? 329 PRO   A HB2    1 
ATOM   4772 H HB3    . PRO   A 1 328 ? 21.49630  -41.09564 11.87523  1.000 151.95202 ? 329 PRO   A HB3    1 
ATOM   4773 H HG2    . PRO   A 1 328 ? 23.49770  -42.35186 13.39921  1.000 153.42499 ? 329 PRO   A HG2    1 
ATOM   4774 H HG3    . PRO   A 1 328 ? 23.22140  -42.53395 11.84488  1.000 153.42499 ? 329 PRO   A HG3    1 
ATOM   4775 H HD2    . PRO   A 1 328 ? 25.08196  -40.91302 12.80247  1.000 154.30291 ? 329 PRO   A HD2    1 
ATOM   4776 H HD3    . PRO   A 1 328 ? 24.51124  -40.80092 11.32358  1.000 154.30291 ? 329 PRO   A HD3    1 
ATOM   4777 N N      . PHE   A 1 329 ? 23.63207  -39.69479 15.38773  1.000 144.94262 ? 330 PHE   A N      1 
ATOM   4778 C CA     . PHE   A 1 329 ? 23.87453  -39.87297 16.81270  1.000 130.02352 ? 330 PHE   A CA     1 
ATOM   4779 C C      . PHE   A 1 329 ? 23.11416  -38.87562 17.67065  1.000 137.15452 ? 330 PHE   A C      1 
ATOM   4780 O O      . PHE   A 1 329 ? 23.18200  -38.97435 18.90022  1.000 150.02854 ? 330 PHE   A O      1 
ATOM   4781 C CB     . PHE   A 1 329 ? 25.37293  -39.77193 17.10078  1.000 115.44528 ? 330 PHE   A CB     1 
ATOM   4782 C CG     . PHE   A 1 329 ? 26.21531  -40.63709 16.21145  1.000 116.24565 ? 330 PHE   A CG     1 
ATOM   4783 C CD1    . PHE   A 1 329 ? 26.43006  -41.97164 16.51262  1.000 115.79165 ? 330 PHE   A CD1    1 
ATOM   4784 C CD2    . PHE   A 1 329 ? 26.78645  -40.11463 15.06768  1.000 139.44672 ? 330 PHE   A CD2    1 
ATOM   4785 C CE1    . PHE   A 1 329 ? 27.20273  -42.76557 15.68922  1.000 114.03660 ? 330 PHE   A CE1    1 
ATOM   4786 C CE2    . PHE   A 1 329 ? 27.55730  -40.90204 14.24051  1.000 147.05207 ? 330 PHE   A CE2    1 
ATOM   4787 C CZ     . PHE   A 1 329 ? 27.76549  -42.23036 14.55091  1.000 140.62305 ? 330 PHE   A CZ     1 
ATOM   4788 H H      . PHE   A 1 329 ? 24.31282  -39.40336 14.95041  1.000 174.32161 ? 330 PHE   A H      1 
ATOM   4789 H HA     . PHE   A 1 329 ? 23.58174  -40.76164 17.06849  1.000 156.41870 ? 330 PHE   A HA     1 
ATOM   4790 H HB2    . PHE   A 1 329 ? 25.65433  -38.85247 16.97311  1.000 138.92481 ? 330 PHE   A HB2    1 
ATOM   4791 H HB3    . PHE   A 1 329 ? 25.53379  -40.04382 18.01790  1.000 138.92481 ? 330 PHE   A HB3    1 
ATOM   4792 H HD1    . PHE   A 1 329 ? 26.04935  -42.33711 17.27838  1.000 139.34045 ? 330 PHE   A HD1    1 
ATOM   4793 H HD2    . PHE   A 1 329 ? 26.64904  -39.22021 14.85313  1.000 167.72653 ? 330 PHE   A HD2    1 
ATOM   4794 H HE1    . PHE   A 1 329 ? 27.34323  -43.65987 15.90225  1.000 137.23440 ? 330 PHE   A HE1    1 
ATOM   4795 H HE2    . PHE   A 1 329 ? 27.93710  -40.53846 13.47339  1.000 176.85296 ? 330 PHE   A HE2    1 
ATOM   4796 H HZ     . PHE   A 1 329 ? 28.28460  -42.76337 13.99294  1.000 169.13813 ? 330 PHE   A HZ     1 
ATOM   4797 N N      . ALA   A 1 330 ? 22.40047  -37.92834 17.06644  1.000 139.30521 ? 331 ALA   A N      1 
ATOM   4798 C CA     . ALA   A 1 330 ? 21.52737  -37.02237 17.79626  1.000 132.79047 ? 331 ALA   A CA     1 
ATOM   4799 C C      . ALA   A 1 330 ? 20.05246  -37.31859 17.56595  1.000 144.72365 ? 331 ALA   A C      1 
ATOM   4800 O O      . ALA   A 1 330 ? 19.20084  -36.62719 18.13484  1.000 138.06360 ? 331 ALA   A O      1 
ATOM   4801 C CB     . ALA   A 1 330 ? 21.82876  -35.57145 17.40664  1.000 142.43381 ? 331 ALA   A CB     1 
ATOM   4802 H H      . ALA   A 1 330 ? 22.40749  -37.79048 16.21759  1.000 167.55672 ? 331 ALA   A H      1 
ATOM   4803 H HA     . ALA   A 1 330 ? 21.70525  -37.11580 18.74522  1.000 159.73904 ? 331 ALA   A HA     1 
ATOM   4804 H HB1    . ALA   A 1 330 ? 21.19295  -34.98720 17.84857  1.000 171.31104 ? 331 ALA   A HB1    1 
ATOM   4805 H HB2    . ALA   A 1 330 ? 22.73090  -35.35029 17.68613  1.000 171.31104 ? 331 ALA   A HB2    1 
ATOM   4806 H HB3    . ALA   A 1 330 ? 21.74876  -35.47976 16.44430  1.000 171.31104 ? 331 ALA   A HB3    1 
ATOM   4807 N N      . GLY   A 1 331 ? 19.72981  -38.32969 16.75903  1.000 157.95075 ? 332 GLY   A N      1 
ATOM   4808 C CA     . GLY   A 1 331 ? 18.35280  -38.65475 16.44033  1.000 149.29456 ? 332 GLY   A CA     1 
ATOM   4809 C C      . GLY   A 1 331 ? 17.57654  -37.47374 15.89485  1.000 136.52864 ? 332 GLY   A C      1 
ATOM   4810 O O      . GLY   A 1 331 ? 16.46401  -37.19213 16.34968  1.000 147.98037 ? 332 GLY   A O      1 
ATOM   4811 H H      . GLY   A 1 331 ? 20.30318  -38.84700 16.38057  1.000 189.93137 ? 332 GLY   A H      1 
ATOM   4812 H HA2    . GLY   A 1 331 ? 18.33800  -39.36061 15.77517  1.000 179.54394 ? 332 GLY   A HA2    1 
ATOM   4813 H HA3    . GLY   A 1 331 ? 17.90556  -38.96718 17.24237  1.000 179.54394 ? 332 GLY   A HA3    1 
ATOM   4814 N N      . GLN   A 1 332 ? 18.15328  -36.77552 14.91578  1.000 134.81263 ? 333 GLN   A N      1 
ATOM   4815 C CA     . GLN   A 1 332 ? 17.55380  -35.57374 14.35654  1.000 146.52767 ? 333 GLN   A CA     1 
ATOM   4816 C C      . GLN   A 1 332 ? 17.31384  -35.65829 12.85534  1.000 158.89393 ? 333 GLN   A C      1 
ATOM   4817 O O      . GLN   A 1 332 ? 16.75926  -34.71416 12.28032  1.000 161.11142 ? 333 GLN   A O      1 
ATOM   4818 C CB     . GLN   A 1 332 ? 18.44034  -34.35628 14.65753  1.000 147.31047 ? 333 GLN   A CB     1 
ATOM   4819 C CG     . GLN   A 1 332 ? 18.57855  -34.04341 16.13625  1.000 175.32644 ? 333 GLN   A CG     1 
ATOM   4820 C CD     . GLN   A 1 332 ? 17.25954  -33.67001 16.78100  1.000 192.07551 ? 333 GLN   A CD     1 
ATOM   4821 O OE1    . GLN   A 1 332 ? 16.45795  -32.94509 16.19588  1.000 187.83896 ? 333 GLN   A OE1    1 
ATOM   4822 N NE2    . GLN   A 1 332 ? 17.02818  -34.16330 17.99440  1.000 190.08256 ? 333 GLN   A NE2    1 
ATOM   4823 H H      . GLN   A 1 332 ? 18.90544  -36.98505 14.55528  1.000 162.16563 ? 333 GLN   A H      1 
ATOM   4824 H HA     . GLN   A 1 332 ? 16.69314  -35.43553 14.78205  1.000 176.22367 ? 333 GLN   A HA     1 
ATOM   4825 H HB2    . GLN   A 1 332 ? 19.32906  -34.52476 14.30726  1.000 177.16304 ? 333 GLN   A HB2    1 
ATOM   4826 H HB3    . GLN   A 1 332 ? 18.05575  -33.57742 14.22583  1.000 177.16304 ? 333 GLN   A HB3    1 
ATOM   4827 H HG2    . GLN   A 1 332 ? 18.92560  -34.82513 16.59381  1.000 210.78220 ? 333 GLN   A HG2    1 
ATOM   4828 H HG3    . GLN   A 1 332 ? 19.18816  -33.29692 16.24592  1.000 210.78220 ? 333 GLN   A HG3    1 
ATOM   4829 H HE21   . GLN   A 1 332 ? 17.61387  -34.66667 18.37280  1.000 228.48954 ? 333 GLN   A HE21   1 
ATOM   4830 H HE22   . GLN   A 1 332 ? 16.29289  -33.97888 18.40054  1.000 228.48954 ? 333 GLN   A HE22   1 
ATOM   4831 N N      . GLY   A 1 333 ? 17.69757  -36.75441 12.20592  1.000 129.08304 ? 334 GLY   A N      1 
ATOM   4832 C CA     . GLY   A 1 333 ? 17.58585  -36.85110 10.76357  1.000 125.99508 ? 334 GLY   A CA     1 
ATOM   4833 C C      . GLY   A 1 333 ? 16.16822  -36.73889 10.23691  1.000 136.72457 ? 334 GLY   A C      1 
ATOM   4834 O O      . GLY   A 1 333 ? 15.82792  -35.75485 9.57239   1.000 147.37183 ? 334 GLY   A O      1 
ATOM   4835 H H      . GLY   A 1 333 ? 18.02579  -37.45436 12.58266  1.000 155.29012 ? 334 GLY   A H      1 
ATOM   4836 H HA2    . GLY   A 1 333 ? 18.10982  -36.14115 10.36065  1.000 151.58456 ? 334 GLY   A HA2    1 
ATOM   4837 H HA3    . GLY   A 1 333 ? 17.94203  -37.70716 10.47863  1.000 151.58456 ? 334 GLY   A HA3    1 
ATOM   4838 N N      . VAL   A 1 334 ? 15.32860  -37.74153 10.52260  1.000 127.09470 ? 335 VAL   A N      1 
ATOM   4839 C CA     . VAL   A 1 334 ? 13.97240  -37.75405 9.97358   1.000 134.04318 ? 335 VAL   A CA     1 
ATOM   4840 C C      . VAL   A 1 334 ? 13.16262  -36.58478 10.51629  1.000 131.73843 ? 335 VAL   A C      1 
ATOM   4841 O O      . VAL   A 1 334 ? 12.34987  -35.99066 9.79783   1.000 119.78156 ? 335 VAL   A O      1 
ATOM   4842 C CB     . VAL   A 1 334 ? 13.27054  -39.09294 10.27018  1.000 121.82807 ? 335 VAL   A CB     1 
ATOM   4843 C CG1    . VAL   A 1 334 ? 13.11345  -39.28074 11.75645  1.000 122.87536 ? 335 VAL   A CG1    1 
ATOM   4844 C CG2    . VAL   A 1 334 ? 11.89692  -39.13652 9.60398   1.000 106.97921 ? 335 VAL   A CG2    1 
ATOM   4845 H H      . VAL   A 1 334 ? 15.51811  -38.41440 11.02353  1.000 152.90411 ? 335 VAL   A H      1 
ATOM   4846 H HA     . VAL   A 1 334 ? 14.04404  -37.65814 9.01100   1.000 161.24228 ? 335 VAL   A HA     1 
ATOM   4847 H HB     . VAL   A 1 334 ? 13.81426  -39.81312 9.91435   1.000 146.58416 ? 335 VAL   A HB     1 
ATOM   4848 H HG11   . VAL   A 1 334 ? 12.96868  -40.22169 11.94231  1.000 147.84091 ? 335 VAL   A HG11   1 
ATOM   4849 H HG12   . VAL   A 1 334 ? 13.92042  -38.97623 12.20027  1.000 147.84091 ? 335 VAL   A HG12   1 
ATOM   4850 H HG13   . VAL   A 1 334 ? 12.35244  -38.76240 12.06156  1.000 147.84091 ? 335 VAL   A HG13   1 
ATOM   4851 H HG21   . VAL   A 1 334 ? 11.45927  -39.97025 9.83693   1.000 128.76552 ? 335 VAL   A HG21   1 
ATOM   4852 H HG22   . VAL   A 1 334 ? 11.36900  -38.38641 9.91945   1.000 128.76552 ? 335 VAL   A HG22   1 
ATOM   4853 H HG23   . VAL   A 1 334 ? 12.01041  -39.07996 8.64231   1.000 128.76552 ? 335 VAL   A HG23   1 
ATOM   4854 N N      . ASN   A 1 335 ? 13.35015  -36.25014 11.79754  1.000 143.52939 ? 336 ASN   A N      1 
ATOM   4855 C CA     . ASN   A 1 335 ? 12.59115  -35.15135 12.38779  1.000 138.58331 ? 336 ASN   A CA     1 
ATOM   4856 C C      . ASN   A 1 335 ? 12.82536  -33.85809 11.61938  1.000 141.31858 ? 336 ASN   A C      1 
ATOM   4857 O O      . ASN   A 1 335 ? 11.88774  -33.08746 11.37986  1.000 143.22231 ? 336 ASN   A O      1 
ATOM   4858 C CB     . ASN   A 1 335 ? 12.96711  -34.97942 13.86089  1.000 130.36604 ? 336 ASN   A CB     1 
ATOM   4859 C CG     . ASN   A 1 335 ? 12.63921  -36.20204 14.69273  1.000 131.90661 ? 336 ASN   A CG     1 
ATOM   4860 O OD1    . ASN   A 1 335 ? 11.98291  -37.12907 14.22218  1.000 116.59148 ? 336 ASN   A OD1    1 
ATOM   4861 N ND2    . ASN   A 1 335 ? 13.08152  -36.20145 15.94396  1.000 176.35813 ? 336 ASN   A ND2    1 
ATOM   4862 H H      . ASN   A 1 335 ? 13.90016  -36.63702 12.33364  1.000 172.62574 ? 336 ASN   A H      1 
ATOM   4863 H HA     . ASN   A 1 335 ? 11.64548  -35.36338 12.34733  1.000 166.69045 ? 336 ASN   A HA     1 
ATOM   4864 H HB2    . ASN   A 1 335 ? 13.92126  -34.81790 13.92732  1.000 156.82972 ? 336 ASN   A HB2    1 
ATOM   4865 H HB3    . ASN   A 1 335 ? 12.47692  -34.22668 14.22694  1.000 156.82972 ? 336 ASN   A HB3    1 
ATOM   4866 H HD21   . ASN   A 1 335 ? 12.92133  -36.87282 16.45699  1.000 212.02023 ? 336 ASN   A HD21   1 
ATOM   4867 H HD22   . ASN   A 1 335 ? 13.52835  -35.52969 16.24176  1.000 212.02023 ? 336 ASN   A HD22   1 
ATOM   4868 N N      . SER   A 1 336 ? 14.07143  -33.61183 11.21028  1.000 132.29431 ? 337 SER   A N      1 
ATOM   4869 C CA     . SER   A 1 336 ? 14.37077  -32.41603 10.43187  1.000 127.26891 ? 337 SER   A CA     1 
ATOM   4870 C C      . SER   A 1 336 ? 13.79201  -32.51829 9.02758   1.000 134.56242 ? 337 SER   A C      1 
ATOM   4871 O O      . SER   A 1 336 ? 13.19157  -31.56017 8.52625   1.000 123.11166 ? 337 SER   A O      1 
ATOM   4872 C CB     . SER   A 1 336 ? 15.88187  -32.19861 10.37371  1.000 133.24749 ? 337 SER   A CB     1 
ATOM   4873 O OG     . SER   A 1 336 ? 16.44322  -32.18981 11.67380  1.000 171.57081 ? 337 SER   A OG     1 
ATOM   4874 H H      . SER   A 1 336 ? 14.75046  -34.11520 11.36884  1.000 159.14364 ? 337 SER   A H      1 
ATOM   4875 H HA     . SER   A 1 336 ? 13.97164  -31.64700 10.86798  1.000 153.11316 ? 337 SER   A HA     1 
ATOM   4876 H HB2    . SER   A 1 336 ? 16.28427  -32.91735 9.86147   1.000 160.28746 ? 337 SER   A HB2    1 
ATOM   4877 H HB3    . SER   A 1 336 ? 16.06150  -31.34621 9.94702   1.000 160.28746 ? 337 SER   A HB3    1 
ATOM   4878 H HG     . SER   A 1 336 ? 17.28073  -32.14765 11.62485  1.000 206.27544 ? 337 SER   A HG     1 
ATOM   4879 N N      . GLY   A 1 337 ? 13.95529  -33.67432 8.38037   1.000 142.82582 ? 338 GLY   A N      1 
ATOM   4880 C CA     . GLY   A 1 337 ? 13.42452  -33.83635 7.03736   1.000 115.89053 ? 338 GLY   A CA     1 
ATOM   4881 C C      . GLY   A 1 337 ? 11.93436  -33.56994 6.96935   1.000 117.79451 ? 338 GLY   A C      1 
ATOM   4882 O O      . GLY   A 1 337 ? 11.44853  -32.93269 6.03146   1.000 108.93187 ? 338 GLY   A O      1 
ATOM   4883 H H      . GLY   A 1 337 ? 14.36206  -34.36414 8.69386   1.000 171.78145 ? 338 GLY   A H      1 
ATOM   4884 H HA2    . GLY   A 1 337 ? 13.87305  -33.21914 6.43838   1.000 139.45911 ? 338 GLY   A HA2    1 
ATOM   4885 H HA3    . GLY   A 1 337 ? 13.58693  -34.74373 6.73539   1.000 139.45911 ? 338 GLY   A HA3    1 
ATOM   4886 N N      . LEU   A 1 338 ? 11.18901  -34.04600 7.96918   1.000 118.18331 ? 339 LEU   A N      1 
ATOM   4887 C CA     . LEU   A 1 338 ? 9.75441   -33.79411 8.00353   1.000 106.64144 ? 339 LEU   A CA     1 
ATOM   4888 C C      . LEU   A 1 338 ? 9.45612   -32.31186 8.17576   1.000 131.27535 ? 339 LEU   A C      1 
ATOM   4889 O O      . LEU   A 1 338 ? 8.45603   -31.81827 7.64287   1.000 136.91219 ? 339 LEU   A O      1 
ATOM   4890 C CB     . LEU   A 1 338 ? 9.11053   -34.60892 9.12338   1.000 117.87625 ? 339 LEU   A CB     1 
ATOM   4891 C CG     . LEU   A 1 338 ? 9.17344   -36.12308 8.91771   1.000 95.19316  ? 339 LEU   A CG     1 
ATOM   4892 C CD1    . LEU   A 1 338 ? 8.63697   -36.85008 10.13361  1.000 118.38799 ? 339 LEU   A CD1    1 
ATOM   4893 C CD2    . LEU   A 1 338 ? 8.40084   -36.52891 7.67427   1.000 98.98143  ? 339 LEU   A CD2    1 
ATOM   4894 H H      . LEU   A 1 338 ? 11.48753  -34.51039 8.62860   1.000 142.21045 ? 339 LEU   A H      1 
ATOM   4895 H HA     . LEU   A 1 338 ? 9.35996   -34.08081 7.16501   1.000 128.36020 ? 339 LEU   A HA     1 
ATOM   4896 H HB2    . LEU   A 1 338 ? 9.56684   -34.40567 9.95486   1.000 141.84197 ? 339 LEU   A HB2    1 
ATOM   4897 H HB3    . LEU   A 1 338 ? 8.17544   -34.35939 9.18853   1.000 141.84197 ? 339 LEU   A HB3    1 
ATOM   4898 H HG     . LEU   A 1 338 ? 10.10001  -36.38240 8.79476   1.000 114.62227 ? 339 LEU   A HG     1 
ATOM   4899 H HD11   . LEU   A 1 338 ? 8.58682   -37.79876 9.93770   1.000 142.45606 ? 339 LEU   A HD11   1 
ATOM   4900 H HD12   . LEU   A 1 338 ? 9.23517   -36.69802 10.88190  1.000 142.45606 ? 339 LEU   A HD12   1 
ATOM   4901 H HD13   . LEU   A 1 338 ? 7.75341   -36.50813 10.34168  1.000 142.45606 ? 339 LEU   A HD13   1 
ATOM   4902 H HD21   . LEU   A 1 338 ? 8.35729   -37.49699 7.63147   1.000 119.16819 ? 339 LEU   A HD21   1 
ATOM   4903 H HD22   . LEU   A 1 338 ? 7.50538   -36.15940 7.72424   1.000 119.16819 ? 339 LEU   A HD22   1 
ATOM   4904 H HD23   . LEU   A 1 338 ? 8.85804   -36.18344 6.89163   1.000 119.16819 ? 339 LEU   A HD23   1 
ATOM   4905 N N      . MET   A 1 339 ? 10.31006  -31.58603 8.90284   1.000 134.06435 ? 340 MET   A N      1 
ATOM   4906 C CA     . MET   A 1 339 ? 10.12440  -30.14426 9.02229   1.000 130.90987 ? 340 MET   A CA     1 
ATOM   4907 C C      . MET   A 1 339 ? 10.18457  -29.48122 7.65355   1.000 135.94037 ? 340 MET   A C      1 
ATOM   4908 O O      . MET   A 1 339 ? 9.40853   -28.56318 7.36227   1.000 144.23400 ? 340 MET   A O      1 
ATOM   4909 C CB     . MET   A 1 339 ? 11.18257  -29.54880 9.95098   1.000 129.72480 ? 340 MET   A CB     1 
ATOM   4910 C CG     . MET   A 1 339 ? 10.88335  -28.12129 10.38600  1.000 145.83722 ? 340 MET   A CG     1 
ATOM   4911 S SD     . MET   A 1 339 ? 9.72972   -28.04196 11.76990  1.000 138.63686 ? 340 MET   A SD     1 
ATOM   4912 C CE     . MET   A 1 339 ? 10.84410  -28.30380 13.14791  1.000 186.58265 ? 340 MET   A CE     1 
ATOM   4913 H H      . MET   A 1 339 ? 10.98948  -31.89953 9.32675   1.000 161.26769 ? 340 MET   A H      1 
ATOM   4914 H HA     . MET   A 1 339 ? 9.25713   -29.97412 9.42204   1.000 157.48231 ? 340 MET   A HA     1 
ATOM   4915 H HB2    . MET   A 1 339 ? 11.23978  -30.09600 10.74985  1.000 156.06023 ? 340 MET   A HB2    1 
ATOM   4916 H HB3    . MET   A 1 339 ? 12.03581  -29.54509 9.48960   1.000 156.06023 ? 340 MET   A HB3    1 
ATOM   4917 H HG2    . MET   A 1 339 ? 11.71018  -27.69427 10.65970  1.000 175.39513 ? 340 MET   A HG2    1 
ATOM   4918 H HG3    . MET   A 1 339 ? 10.49181  -27.63919 9.64090   1.000 175.39513 ? 340 MET   A HG3    1 
ATOM   4919 H HE1    . MET   A 1 339 ? 10.32318  -28.41501 13.95858  1.000 224.28965 ? 340 MET   A HE1    1 
ATOM   4920 H HE2    . MET   A 1 339 ? 11.37069  -29.10115 12.98111  1.000 224.28965 ? 340 MET   A HE2    1 
ATOM   4921 H HE3    . MET   A 1 339 ? 11.42774  -27.53370 13.23281  1.000 224.28965 ? 340 MET   A HE3    1 
ATOM   4922 N N      . ASP   A 1 340 ? 11.09906  -29.94043 6.79671   1.000 136.83950 ? 341 ASP   A N      1 
ATOM   4923 C CA     . ASP   A 1 340 ? 11.18753  -29.40033 5.44528   1.000 136.40774 ? 341 ASP   A CA     1 
ATOM   4924 C C      . ASP   A 1 340 ? 9.88058   -29.60929 4.69238   1.000 137.50276 ? 341 ASP   A C      1 
ATOM   4925 O O      . ASP   A 1 340 ? 9.32550   -28.66843 4.11318   1.000 144.04402 ? 341 ASP   A O      1 
ATOM   4926 C CB     . ASP   A 1 340 ? 12.35008  -30.05394 4.69664   1.000 132.32908 ? 341 ASP   A CB     1 
ATOM   4927 C CG     . ASP   A 1 340 ? 13.69063  -29.78263 5.34923   1.000 128.12395 ? 341 ASP   A CG     1 
ATOM   4928 O OD1    . ASP   A 1 340 ? 13.81652  -28.75254 6.04391   1.000 134.84974 ? 341 ASP   A OD1    1 
ATOM   4929 O OD2    . ASP   A 1 340 ? 14.61950  -30.59717 5.16457   1.000 117.75393 ? 341 ASP   A OD2    1 
ATOM   4930 H H      . ASP   A 1 340 ? 11.67218  -30.55691 6.97305   1.000 164.59787 ? 341 ASP   A H      1 
ATOM   4931 H HA     . ASP   A 1 340 ? 11.36038  -28.44725 5.49698   1.000 164.07976 ? 341 ASP   A HA     1 
ATOM   4932 H HB2    . ASP   A 1 340 ? 12.21421  -31.01418 4.67739   1.000 159.18536 ? 341 ASP   A HB2    1 
ATOM   4933 H HB3    . ASP   A 1 340 ? 12.38021  -29.70493 3.79210   1.000 159.18536 ? 341 ASP   A HB3    1 
ATOM   4934 N N      . ALA   A 1 341 ? 9.36995   -30.84327 4.69485   1.000 130.99528 ? 342 ALA   A N      1 
ATOM   4935 C CA     . ALA   A 1 341 ? 8.12455   -31.12578 3.98992   1.000 136.21023 ? 342 ALA   A CA     1 
ATOM   4936 C C      . ALA   A 1 341 ? 6.98611   -30.27102 4.52719   1.000 138.26352 ? 342 ALA   A C      1 
ATOM   4937 O O      . ALA   A 1 341 ? 6.12161   -29.82237 3.76560   1.000 144.81960 ? 342 ALA   A O      1 
ATOM   4938 C CB     . ALA   A 1 341 ? 7.77866   -32.60990 4.10705   1.000 139.32789 ? 342 ALA   A CB     1 
ATOM   4939 H H      . ALA   A 1 341 ? 9.72053   -31.52143 5.09083   1.000 157.58481 ? 342 ALA   A H      1 
ATOM   4940 H HA     . ALA   A 1 341 ? 8.24320   -30.91837 3.04982   1.000 163.84275 ? 342 ALA   A HA     1 
ATOM   4941 H HB1    . ALA   A 1 341 ? 6.95188   -32.78014 3.62918   1.000 167.58393 ? 342 ALA   A HB1    1 
ATOM   4942 H HB2    . ALA   A 1 341 ? 8.49800   -33.13329 3.72038   1.000 167.58393 ? 342 ALA   A HB2    1 
ATOM   4943 H HB3    . ALA   A 1 341 ? 7.67169   -32.83624 5.04419   1.000 167.58393 ? 342 ALA   A HB3    1 
ATOM   4944 N N      . LEU   A 1 342 ? 6.97093   -30.03185 5.83827   1.000 134.43244 ? 343 LEU   A N      1 
ATOM   4945 C CA     . LEU   A 1 342 ? 5.91490   -29.21825 6.42898   1.000 146.71648 ? 343 LEU   A CA     1 
ATOM   4946 C C      . LEU   A 1 342 ? 6.01669   -27.77093 5.96526   1.000 147.62790 ? 343 LEU   A C      1 
ATOM   4947 O O      . LEU   A 1 342 ? 5.02412   -27.17464 5.53196   1.000 151.65390 ? 343 LEU   A O      1 
ATOM   4948 C CB     . LEU   A 1 342 ? 5.98779   -29.29939 7.95360   1.000 155.46428 ? 343 LEU   A CB     1 
ATOM   4949 C CG     . LEU   A 1 342 ? 4.83178   -28.64171 8.70814   1.000 150.44866 ? 343 LEU   A CG     1 
ATOM   4950 C CD1    . LEU   A 1 342 ? 3.53271   -29.38458 8.43910   1.000 160.58466 ? 343 LEU   A CD1    1 
ATOM   4951 C CD2    . LEU   A 1 342 ? 5.11836   -28.58341 10.19910  1.000 157.03082 ? 343 LEU   A CD2    1 
ATOM   4952 H H      . LEU   A 1 342 ? 7.55304   -30.32552 6.39907   1.000 161.70939 ? 343 LEU   A H      1 
ATOM   4953 H HA     . LEU   A 1 342 ? 5.05449   -29.56638 6.14719   1.000 176.45024 ? 343 LEU   A HA     1 
ATOM   4954 H HB2    . LEU   A 1 342 ? 6.00270   -30.23545 8.20751   1.000 186.94760 ? 343 LEU   A HB2    1 
ATOM   4955 H HB3    . LEU   A 1 342 ? 6.80534   -28.86432 8.24210   1.000 186.94760 ? 343 LEU   A HB3    1 
ATOM   4956 H HG     . LEU   A 1 342 ? 4.73086   -27.72994 8.39289   1.000 180.92886 ? 343 LEU   A HG     1 
ATOM   4957 H HD11   . LEU   A 1 342 ? 2.87797   -29.12795 9.10720   1.000 193.09206 ? 343 LEU   A HD11   1 
ATOM   4958 H HD12   . LEU   A 1 342 ? 3.21199   -29.14967 7.55431   1.000 193.09206 ? 343 LEU   A HD12   1 
ATOM   4959 H HD13   . LEU   A 1 342 ? 3.69872   -30.33901 8.48815   1.000 193.09206 ? 343 LEU   A HD13   1 
ATOM   4960 H HD21   . LEU   A 1 342 ? 4.35913   -28.18332 10.65120  1.000 188.82745 ? 343 LEU   A HD21   1 
ATOM   4961 H HD22   . LEU   A 1 342 ? 5.26233   -29.48434 10.52847  1.000 188.82745 ? 343 LEU   A HD22   1 
ATOM   4962 H HD23   . LEU   A 1 342 ? 5.91230   -28.04621 10.34731  1.000 188.82745 ? 343 LEU   A HD23   1 
ATOM   4963 N N      . ILE   A 1 343 ? 7.21484   -27.19168 6.04435   1.000 150.57888 ? 344 ILE   A N      1 
ATOM   4964 C CA     . ILE   A 1 343 ? 7.38871   -25.78565 5.69542   1.000 156.53536 ? 344 ILE   A CA     1 
ATOM   4965 C C      . ILE   A 1 343 ? 7.14231   -25.56843 4.20853   1.000 159.81775 ? 344 ILE   A C      1 
ATOM   4966 O O      . ILE   A 1 343 ? 6.38237   -24.67716 3.81224   1.000 165.31450 ? 344 ILE   A O      1 
ATOM   4967 C CB     . ILE   A 1 343 ? 8.79182   -25.30649 6.10633   1.000 144.86350 ? 344 ILE   A CB     1 
ATOM   4968 C CG1    . ILE   A 1 343 ? 8.90339   -25.25616 7.62910   1.000 157.46890 ? 344 ILE   A CG1    1 
ATOM   4969 C CG2    . ILE   A 1 343 ? 9.08598   -23.94493 5.49960   1.000 143.00489 ? 344 ILE   A CG2    1 
ATOM   4970 C CD1    . ILE   A 1 343 ? 10.32580  -25.30561 8.13535   1.000 157.51254 ? 344 ILE   A CD1    1 
ATOM   4971 H H      . ILE   A 1 343 ? 7.93580   -27.58792 6.29499   1.000 181.08513 ? 344 ILE   A H      1 
ATOM   4972 H HA     . ILE   A 1 343 ? 6.73303   -25.26449 6.18469   1.000 188.23291 ? 344 ILE   A HA     1 
ATOM   4973 H HB     . ILE   A 1 343 ? 9.44685   -25.93768 5.76953   1.000 174.22667 ? 344 ILE   A HB     1 
ATOM   4974 H HG12   . ILE   A 1 343 ? 8.50528   -24.42962 7.94411   1.000 189.35315 ? 344 ILE   A HG12   1 
ATOM   4975 H HG13   . ILE   A 1 343 ? 8.42950   -26.01591 8.00209   1.000 189.35315 ? 344 ILE   A HG13   1 
ATOM   4976 H HG21   . ILE   A 1 343 ? 9.82267   -23.53711 5.98113   1.000 171.99634 ? 344 ILE   A HG21   1 
ATOM   4977 H HG22   . ILE   A 1 343 ? 9.32407   -24.05984 4.56633   1.000 171.99634 ? 344 ILE   A HG22   1 
ATOM   4978 H HG23   . ILE   A 1 343 ? 8.29461   -23.38883 5.57304   1.000 171.99634 ? 344 ILE   A HG23   1 
ATOM   4979 H HD11   . ILE   A 1 343 ? 10.32213  -25.19390 9.09889   1.000 189.40552 ? 344 ILE   A HD11   1 
ATOM   4980 H HD12   . ILE   A 1 343 ? 10.71393  -26.16376 7.90332   1.000 189.40552 ? 344 ILE   A HD12   1 
ATOM   4981 H HD13   . ILE   A 1 343 ? 10.83340  -24.59019 7.72134   1.000 189.40552 ? 344 ILE   A HD13   1 
ATOM   4982 N N      . LEU   A 1 344 ? 7.78775   -26.37232 3.36265   1.000 152.16580 ? 345 LEU   A N      1 
ATOM   4983 C CA     . LEU   A 1 344 ? 7.65665   -26.18096 1.92267   1.000 151.59497 ? 345 LEU   A CA     1 
ATOM   4984 C C      . LEU   A 1 344 ? 6.19957   -26.28706 1.48950   1.000 155.18672 ? 345 LEU   A C      1 
ATOM   4985 O O      . LEU   A 1 344 ? 5.67886   -25.40211 0.80153   1.000 164.25087 ? 345 LEU   A O      1 
ATOM   4986 C CB     . LEU   A 1 344 ? 8.52365   -27.19820 1.18101   1.000 149.18296 ? 345 LEU   A CB     1 
ATOM   4987 C CG     . LEU   A 1 344 ? 8.51604   -27.10851 -0.34696  1.000 163.63571 ? 345 LEU   A CG     1 
ATOM   4988 C CD1    . LEU   A 1 344 ? 8.93951   -25.72674 -0.82473  1.000 135.63595 ? 345 LEU   A CD1    1 
ATOM   4989 C CD2    . LEU   A 1 344 ? 9.41911   -28.17902 -0.94235  1.000 150.46492 ? 345 LEU   A CD2    1 
ATOM   4990 H H      . LEU   A 1 344 ? 8.29858   -27.02427 3.59419   1.000 182.98943 ? 345 LEU   A H      1 
ATOM   4991 H HA     . LEU   A 1 344 ? 7.97339   -25.29397 1.69066   1.000 182.30444 ? 345 LEU   A HA     1 
ATOM   4992 H HB2    . LEU   A 1 344 ? 9.44191   -27.07906 1.46997   1.000 179.41002 ? 345 LEU   A HB2    1 
ATOM   4993 H HB3    . LEU   A 1 344 ? 8.21424   -28.08674 1.41693   1.000 179.41002 ? 345 LEU   A HB3    1 
ATOM   4994 H HG     . LEU   A 1 344 ? 7.61039   -27.25849 -0.66033  1.000 196.75332 ? 345 LEU   A HG     1 
ATOM   4995 H HD11   . LEU   A 1 344 ? 9.04651   -25.74494 -1.78864  1.000 163.15361 ? 345 LEU   A HD11   1 
ATOM   4996 H HD12   . LEU   A 1 344 ? 8.25505   -25.08447 -0.57997  1.000 163.15361 ? 345 LEU   A HD12   1 
ATOM   4997 H HD13   . LEU   A 1 344 ? 9.78053   -25.49077 -0.40296  1.000 163.15361 ? 345 LEU   A HD13   1 
ATOM   4998 H HD21   . LEU   A 1 344 ? 9.40149   -28.10501 -1.90936  1.000 180.94837 ? 345 LEU   A HD21   1 
ATOM   4999 H HD22   . LEU   A 1 344 ? 10.32319  -28.04632 -0.61687  1.000 180.94837 ? 345 LEU   A HD22   1 
ATOM   5000 H HD23   . LEU   A 1 344 ? 9.09485   -29.05217 -0.67147  1.000 180.94837 ? 345 LEU   A HD23   1 
ATOM   5001 N N      . SER   A 1 345 ? 5.51685   -27.35814 1.89862   1.000 152.24166 ? 346 SER   A N      1 
ATOM   5002 C CA     . SER   A 1 345 ? 4.12511   -27.53292 1.49633   1.000 166.38537 ? 346 SER   A CA     1 
ATOM   5003 C C      . SER   A 1 345 ? 3.25672   -26.39583 2.01837   1.000 172.80734 ? 346 SER   A C      1 
ATOM   5004 O O      . SER   A 1 345 ? 2.36679   -25.90820 1.31188   1.000 185.45908 ? 346 SER   A O      1 
ATOM   5005 C CB     . SER   A 1 345 ? 3.59853   -28.87834 1.99255   1.000 166.67204 ? 346 SER   A CB     1 
ATOM   5006 O OG     . SER   A 1 345 ? 3.55026   -28.91553 3.40773   1.000 155.87182 ? 346 SER   A OG     1 
ATOM   5007 H H      . SER   A 1 345 ? 5.83049   -27.98368 2.39855   1.000 183.08046 ? 346 SER   A H      1 
ATOM   5008 H HA     . SER   A 1 345 ? 4.07740   -27.53118 0.52751   1.000 200.05291 ? 346 SER   A HA     1 
ATOM   5009 H HB2    . SER   A 1 345 ? 2.70390   -29.01453 1.64328   1.000 200.39692 ? 346 SER   A HB2    1 
ATOM   5010 H HB3    . SER   A 1 345 ? 4.18780   -29.58214 1.67898   1.000 200.39692 ? 346 SER   A HB3    1 
ATOM   5011 H HG     . SER   A 1 345 ? 4.32097   -28.80904 3.72438   1.000 187.43665 ? 346 SER   A HG     1 
ATOM   5012 N N      . ASP   A 1 346 ? 3.49837   -25.96191 3.25593   1.000 163.17862 ? 347 ASP   A N      1 
ATOM   5013 C CA     . ASP   A 1 346 ? 2.75655   -24.83023 3.80022   1.000 175.03944 ? 347 ASP   A CA     1 
ATOM   5014 C C      . ASP   A 1 346 ? 2.96128   -23.58579 2.94441   1.000 183.93387 ? 347 ASP   A C      1 
ATOM   5015 O O      . ASP   A 1 346 ? 1.99718   -22.91126 2.56411   1.000 190.41565 ? 347 ASP   A O      1 
ATOM   5016 C CB     . ASP   A 1 346 ? 3.19434   -24.57157 5.24171   1.000 186.77969 ? 347 ASP   A CB     1 
ATOM   5017 C CG     . ASP   A 1 346 ? 2.15030   -23.82561 6.04209   1.000 199.15948 ? 347 ASP   A CG     1 
ATOM   5018 O OD1    . ASP   A 1 346 ? 1.33928   -23.09764 5.43196   1.000 197.61171 ? 347 ASP   A OD1    1 
ATOM   5019 O OD2    . ASP   A 1 346 ? 2.13977   -23.97103 7.28252   1.000 201.42676 ? 347 ASP   A OD2    1 
ATOM   5020 H H      . ASP   A 1 346 ? 4.07863   -26.30140 3.79224   1.000 196.20481 ? 347 ASP   A H      1 
ATOM   5021 H HA     . ASP   A 1 346 ? 1.81000   -25.04219 3.80415   1.000 210.43780 ? 347 ASP   A HA     1 
ATOM   5022 H HB2    . ASP   A 1 346 ? 3.35851   -25.42119 5.67999   1.000 224.52610 ? 347 ASP   A HB2    1 
ATOM   5023 H HB3    . ASP   A 1 346 ? 4.00522   -24.03927 5.23561   1.000 224.52610 ? 347 ASP   A HB3    1 
ATOM   5024 N N      . ASN   A 1 347 ? 4.21964   -23.27023 2.62678   1.000 177.02230 ? 348 ASN   A N      1 
ATOM   5025 C CA     . ASN   A 1 347 ? 4.51220   -22.08237 1.83126   1.000 180.65430 ? 348 ASN   A CA     1 
ATOM   5026 C C      . ASN   A 1 347 ? 3.82966   -22.13798 0.47093   1.000 189.06293 ? 348 ASN   A C      1 
ATOM   5027 O O      . ASN   A 1 347 ? 3.37870   -21.11051 -0.04908  1.000 201.60398 ? 348 ASN   A O      1 
ATOM   5028 C CB     . ASN   A 1 347 ? 6.02371   -21.93350 1.65549   1.000 186.35162 ? 348 ASN   A CB     1 
ATOM   5029 C CG     . ASN   A 1 347 ? 6.70741   -21.41944 2.90315   1.000 188.07509 ? 348 ASN   A CG     1 
ATOM   5030 O OD1    . ASN   A 1 347 ? 6.07902   -21.26172 3.94898   1.000 190.78384 ? 348 ASN   A OD1    1 
ATOM   5031 N ND2    . ASN   A 1 347 ? 8.00429   -21.15657 2.80050   1.000 195.83751 ? 348 ASN   A ND2    1 
ATOM   5032 H H      . ASN   A 1 347 ? 4.91304   -23.72345 2.85784   1.000 212.81724 ? 348 ASN   A H      1 
ATOM   5033 H HA     . ASN   A 1 347 ? 4.17750   -21.30438 2.30413   1.000 217.17563 ? 348 ASN   A HA     1 
ATOM   5034 H HB2    . ASN   A 1 347 ? 6.40404   -22.79931 1.43958   1.000 224.01242 ? 348 ASN   A HB2    1 
ATOM   5035 H HB3    . ASN   A 1 347 ? 6.19849   -21.30583 0.93689   1.000 224.01242 ? 348 ASN   A HB3    1 
ATOM   5036 H HD21   . ASN   A 1 347 ? 8.43860   -20.86210 3.48186   1.000 235.39548 ? 348 ASN   A HD21   1 
ATOM   5037 H HD22   . ASN   A 1 347 ? 8.41032   -21.28072 2.05261   1.000 235.39548 ? 348 ASN   A HD22   1 
ATOM   5038 N N      . LEU   A 1 348 ? 3.74711   -23.32623 -0.12330  1.000 182.29368 ? 349 LEU   A N      1 
ATOM   5039 C CA     . LEU   A 1 348 ? 3.22795   -23.46013 -1.47629  1.000 195.58795 ? 349 LEU   A CA     1 
ATOM   5040 C C      . LEU   A 1 348 ? 1.70903   -23.38360 -1.55171  1.000 196.97640 ? 349 LEU   A C      1 
ATOM   5041 O O      . LEU   A 1 348 ? 1.17410   -23.21822 -2.65318  1.000 185.01743 ? 349 LEU   A O      1 
ATOM   5042 C CB     . LEU   A 1 348 ? 3.69569   -24.78552 -2.08344  1.000 203.46445 ? 349 LEU   A CB     1 
ATOM   5043 C CG     . LEU   A 1 348 ? 5.20349   -24.94662 -2.28812  1.000 199.50203 ? 349 LEU   A CG     1 
ATOM   5044 C CD1    . LEU   A 1 348 ? 5.52564   -26.37477 -2.70361  1.000 170.23344 ? 349 LEU   A CD1    1 
ATOM   5045 C CD2    . LEU   A 1 348 ? 5.72986   -23.95460 -3.31730  1.000 200.37392 ? 349 LEU   A CD2    1 
ATOM   5046 H H      . LEU   A 1 348 ? 3.98614   -24.06902 0.23828   1.000 219.14289 ? 349 LEU   A H      1 
ATOM   5047 H HA     . LEU   A 1 348 ? 3.58456   -22.73426 -2.01186  1.000 235.09601 ? 349 LEU   A HA     1 
ATOM   5048 H HB2    . LEU   A 1 348 ? 3.40919   -25.50277 -1.49660  1.000 244.54782 ? 349 LEU   A HB2    1 
ATOM   5049 H HB3    . LEU   A 1 348 ? 3.27778   -24.88177 -2.95348  1.000 244.54782 ? 349 LEU   A HB3    1 
ATOM   5050 H HG     . LEU   A 1 348 ? 5.65493   -24.76033 -1.45003  1.000 239.79290 ? 349 LEU   A HG     1 
ATOM   5051 H HD11   . LEU   A 1 348 ? 6.46164   -26.42772 -2.95260  1.000 204.67059 ? 349 LEU   A HD11   1 
ATOM   5052 H HD12   . LEU   A 1 348 ? 5.34774   -26.96850 -1.95746  1.000 204.67059 ? 349 LEU   A HD12   1 
ATOM   5053 H HD13   . LEU   A 1 348 ? 4.96808   -26.61716 -3.45944  1.000 204.67059 ? 349 LEU   A HD13   1 
ATOM   5054 H HD21   . LEU   A 1 348 ? 6.68044   -24.10269 -3.44128  1.000 240.83917 ? 349 LEU   A HD21   1 
ATOM   5055 H HD22   . LEU   A 1 348 ? 5.26169   -24.09117 -4.15579  1.000 240.83917 ? 349 LEU   A HD22   1 
ATOM   5056 H HD23   . LEU   A 1 348 ? 5.57483   -23.05297 -2.99493  1.000 240.83917 ? 349 LEU   A HD23   1 
ATOM   5057 N N      . THR   A 1 349 ? 1.00221   -23.48754 -0.42370  1.000 187.18979 ? 350 THR   A N      1 
ATOM   5058 C CA     . THR   A 1 349 ? -0.44997  -23.56760 -0.44630  1.000 195.53083 ? 350 THR   A CA     1 
ATOM   5059 C C      . THR   A 1 349 ? -1.14575  -22.54364 0.44109   1.000 197.80558 ? 350 THR   A C      1 
ATOM   5060 O O      . THR   A 1 349 ? -2.37956  -22.47467 0.41784   1.000 204.04578 ? 350 THR   A O      1 
ATOM   5061 C CB     . THR   A 1 349 ? -0.91264  -24.97489 -0.03164  1.000 185.50797 ? 350 THR   A CB     1 
ATOM   5062 O OG1    . THR   A 1 349 ? -0.66776  -25.17167 1.36680   1.000 180.86534 ? 350 THR   A OG1    1 
ATOM   5063 C CG2    . THR   A 1 349 ? -0.16677  -26.03810 -0.82737  1.000 191.07568 ? 350 THR   A CG2    1 
ATOM   5064 H H      . THR   A 1 349 ? 1.34539   -23.51329 0.36444   1.000 225.01822 ? 350 THR   A H      1 
ATOM   5065 H HA     . THR   A 1 349 ? -0.74129  -23.40512 -1.35714  1.000 235.02746 ? 350 THR   A HA     1 
ATOM   5066 H HB     . THR   A 1 349 ? -1.86179  -25.06723 -0.20910  1.000 223.00003 ? 350 THR   A HB     1 
ATOM   5067 H HG1    . THR   A 1 349 ? 0.15518   -25.11446 1.52520   1.000 217.42888 ? 350 THR   A HG1    1 
ATOM   5068 H HG21   . THR   A 1 349 ? -0.52201  -26.91686 -0.62123  1.000 229.68129 ? 350 THR   A HG21   1 
ATOM   5069 H HG22   . THR   A 1 349 ? -0.26766  -25.87280 -1.77784  1.000 229.68129 ? 350 THR   A HG22   1 
ATOM   5070 H HG23   . THR   A 1 349 ? 0.77673   -26.01940 -0.60300  1.000 229.68129 ? 350 THR   A HG23   1 
ATOM   5071 N N      . ASN   A 1 350 ? -0.40815  -21.75097 1.21514   1.000 190.30390 ? 351 ASN   A N      1 
ATOM   5072 C CA     . ASN   A 1 350 ? -1.01921  -20.73690 2.06489   1.000 191.21386 ? 351 ASN   A CA     1 
ATOM   5073 C C      . ASN   A 1 350 ? -1.23087  -19.41007 1.34439   1.000 197.73595 ? 351 ASN   A C      1 
ATOM   5074 O O      . ASN   A 1 350 ? -1.75154  -18.46818 1.95145   1.000 187.36664 ? 351 ASN   A O      1 
ATOM   5075 C CB     . ASN   A 1 350 ? -0.17107  -20.51506 3.32419   1.000 191.16203 ? 351 ASN   A CB     1 
ATOM   5076 C CG     . ASN   A 1 350 ? 1.21097   -19.96743 3.01800   1.000 193.87136 ? 351 ASN   A CG     1 
ATOM   5077 O OD1    . ASN   A 1 350 ? 1.48988   -19.52350 1.90401   1.000 191.63225 ? 351 ASN   A OD1    1 
ATOM   5078 N ND2    . ASN   A 1 350 ? 2.08492   -19.99050 4.01719   1.000 194.69693 ? 351 ASN   A ND2    1 
ATOM   5079 H H      . ASN   A 1 350 ? 0.44985   -21.78273 1.26434   1.000 228.75515 ? 351 ASN   A H      1 
ATOM   5080 H HA     . ASN   A 1 350 ? -1.88820  -21.05867 2.35162   1.000 229.84711 ? 351 ASN   A HA     1 
ATOM   5081 H HB2    . ASN   A 1 350 ? -0.62339  -19.87995 3.90120   1.000 229.78491 ? 351 ASN   A HB2    1 
ATOM   5082 H HB3    . ASN   A 1 350 ? -0.06204  -21.36205 3.78422   1.000 229.78491 ? 351 ASN   A HB3    1 
ATOM   5083 H HD21   . ASN   A 1 350 ? 2.88261   -19.69215 3.89773   1.000 234.02678 ? 351 ASN   A HD21   1 
ATOM   5084 H HD22   . ASN   A 1 350 ? 1.85332   -20.30380 4.78388   1.000 234.02678 ? 351 ASN   A HD22   1 
ATOM   5085 N N      . GLY   A 1 351 ? -0.83969  -19.31360 0.07700   1.000 181.34501 ? 352 GLY   A N      1 
ATOM   5086 C CA     . GLY   A 1 351 ? -1.08292  -18.10703 -0.69347  1.000 183.22226 ? 352 GLY   A CA     1 
ATOM   5087 C C      . GLY   A 1 351 ? -0.35981  -16.87740 -0.19422  1.000 188.55667 ? 352 GLY   A C      1 
ATOM   5088 O O      . GLY   A 1 351 ? -0.82077  -15.75947 -0.44367  1.000 183.58232 ? 352 GLY   A O      1 
ATOM   5089 H H      . GLY   A 1 351 ? -0.43189  -19.93391 -0.35718  1.000 218.00448 ? 352 GLY   A H      1 
ATOM   5090 H HA2    . GLY   A 1 351 ? -0.80452  -18.26188 -1.60967  1.000 220.25719 ? 352 GLY   A HA2    1 
ATOM   5091 H HA3    . GLY   A 1 351 ? -2.03388  -17.91626 -0.68033  1.000 220.25719 ? 352 GLY   A HA3    1 
ATOM   5092 N N      . LYS   A 1 352 ? 0.76759   -17.04667 0.49448   1.000 184.74487 ? 353 LYS   A N      1 
ATOM   5093 C CA     . LYS   A 1 352 ? 1.51503   -15.92756 1.05050   1.000 182.33531 ? 353 LYS   A CA     1 
ATOM   5094 C C      . LYS   A 1 352 ? 2.72627   -15.54082 0.21043   1.000 197.38289 ? 353 LYS   A C      1 
ATOM   5095 O O      . LYS   A 1 352 ? 3.52020   -14.69936 0.64353   1.000 199.57629 ? 353 LYS   A O      1 
ATOM   5096 C CB     . LYS   A 1 352 ? 1.97246   -16.25483 2.47274   1.000 181.58439 ? 353 LYS   A CB     1 
ATOM   5097 C CG     . LYS   A 1 352 ? 0.84694   -16.43516 3.46988   1.000 181.77022 ? 353 LYS   A CG     1 
ATOM   5098 C CD     . LYS   A 1 352 ? 1.39511   -16.52123 4.88600   1.000 194.55938 ? 353 LYS   A CD     1 
ATOM   5099 C CE     . LYS   A 1 352 ? 0.28688   -16.45903 5.92317   1.000 202.33452 ? 353 LYS   A CE     1 
ATOM   5100 N NZ     . LYS   A 1 352 ? 0.80178   -16.03107 7.25358   1.000 166.79798 ? 353 LYS   A NZ     1 
ATOM   5101 H H      . LYS   A 1 352 ? 1.12275   -17.81353 0.65382   1.000 222.08432 ? 353 LYS   A H      1 
ATOM   5102 H HA     . LYS   A 1 352 ? 0.92041   -15.16199 1.08558   1.000 219.19284 ? 353 LYS   A HA     1 
ATOM   5103 H HB2    . LYS   A 1 352 ? 2.47985   -17.08127 2.45136   1.000 218.29174 ? 353 LYS   A HB2    1 
ATOM   5104 H HB3    . LYS   A 1 352 ? 2.53255   -15.52982 2.79142   1.000 218.29174 ? 353 LYS   A HB3    1 
ATOM   5105 H HG2    . LYS   A 1 352 ? 0.24295   -15.67791 3.41824   1.000 218.51474 ? 353 LYS   A HG2    1 
ATOM   5106 H HG3    . LYS   A 1 352 ? 0.36792   -17.25557 3.27399   1.000 218.51474 ? 353 LYS   A HG3    1 
ATOM   5107 H HD2    . LYS   A 1 352 ? 1.86754   -17.36121 4.99617   1.000 233.86173 ? 353 LYS   A HD2    1 
ATOM   5108 H HD3    . LYS   A 1 352 ? 1.99887   -15.77814 5.04155   1.000 233.86173 ? 353 LYS   A HD3    1 
ATOM   5109 H HE2    . LYS   A 1 352 ? -0.38447  -15.82011 5.63684   1.000 243.19189 ? 353 LYS   A HE2    1 
ATOM   5110 H HE3    . LYS   A 1 352 ? -0.11153  -17.33816 6.01952   1.000 243.19189 ? 353 LYS   A HE3    1 
ATOM   5111 H HZ1    . LYS   A 1 352 ? 0.13903   -16.02069 7.84751   1.000 200.54804 ? 353 LYS   A HZ1    1 
ATOM   5112 H HZ2    . LYS   A 1 352 ? 1.43077   -16.59559 7.53251   1.000 200.54804 ? 353 LYS   A HZ2    1 
ATOM   5113 H HZ3    . LYS   A 1 352 ? 1.15124   -15.21455 7.19645   1.000 200.54804 ? 353 LYS   A HZ3    1 
ATOM   5114 N N      . PHE   A 1 353 ? 2.89029   -16.12906 -0.97291  1.000 205.69967 ? 354 PHE   A N      1 
ATOM   5115 C CA     . PHE   A 1 353 ? 4.05672   -15.88180 -1.80964  1.000 211.69430 ? 354 PHE   A CA     1 
ATOM   5116 C C      . PHE   A 1 353 ? 3.62258   -15.59649 -3.23838  1.000 206.34884 ? 354 PHE   A C      1 
ATOM   5117 O O      . PHE   A 1 353 ? 2.70902   -16.24040 -3.76267  1.000 205.60860 ? 354 PHE   A O      1 
ATOM   5118 C CB     . PHE   A 1 353 ? 5.01889   -17.07396 -1.77073  1.000 207.04756 ? 354 PHE   A CB     1 
ATOM   5119 C CG     . PHE   A 1 353 ? 5.58690   -17.34116 -0.40589  1.000 209.74648 ? 354 PHE   A CG     1 
ATOM   5120 C CD1    . PHE   A 1 353 ? 6.72012   -16.67436 0.02715   1.000 203.26557 ? 354 PHE   A CD1    1 
ATOM   5121 C CD2    . PHE   A 1 353 ? 4.98134   -18.24755 0.44914   1.000 203.23585 ? 354 PHE   A CD2    1 
ATOM   5122 C CE1    . PHE   A 1 353 ? 7.24321   -16.91053 1.28334   1.000 184.89619 ? 354 PHE   A CE1    1 
ATOM   5123 C CE2    . PHE   A 1 353 ? 5.50119   -18.48840 1.70769   1.000 190.50909 ? 354 PHE   A CE2    1 
ATOM   5124 C CZ     . PHE   A 1 353 ? 6.63361   -17.81877 2.12451   1.000 187.93926 ? 354 PHE   A CZ     1 
ATOM   5125 H H      . PHE   A 1 353 ? 2.32934   -16.68357 -1.31563  1.000 247.23007 ? 354 PHE   A H      1 
ATOM   5126 H HA     . PHE   A 1 353 ? 4.52841   -15.09737 -1.48859  1.000 254.42363 ? 354 PHE   A HA     1 
ATOM   5127 H HB2    . PHE   A 1 353 ? 4.54278   -17.86969 -2.05542  1.000 248.84754 ? 354 PHE   A HB2    1 
ATOM   5128 H HB3    . PHE   A 1 353 ? 5.75972   -16.89783 -2.37161  1.000 248.84754 ? 354 PHE   A HB3    1 
ATOM   5129 H HD1    . PHE   A 1 353 ? 7.13428   -16.05981 -0.53473  1.000 244.30915 ? 354 PHE   A HD1    1 
ATOM   5130 H HD2    . PHE   A 1 353 ? 4.21649   -18.69917 0.17355   1.000 244.27349 ? 354 PHE   A HD2    1 
ATOM   5131 H HE1    . PHE   A 1 353 ? 8.00607   -16.45757 1.56222   1.000 222.26590 ? 354 PHE   A HE1    1 
ATOM   5132 H HE2    . PHE   A 1 353 ? 5.08815   -19.10094 2.27258   1.000 229.00138 ? 354 PHE   A HE2    1 
ATOM   5133 H HZ     . PHE   A 1 353 ? 6.98510   -17.97928 2.97044   1.000 225.91758 ? 354 PHE   A HZ     1 
ATOM   5134 N N      . ASN   A 1 354 ? 4.29214   -14.62548 -3.86474  1.000 203.28252 ? 355 ASN   A N      1 
ATOM   5135 C CA     . ASN   A 1 354 ? 3.89906   -14.18085 -5.19537  1.000 204.44353 ? 355 ASN   A CA     1 
ATOM   5136 C C      . ASN   A 1 354 ? 4.26712   -15.18234 -6.28115  1.000 193.91791 ? 355 ASN   A C      1 
ATOM   5137 O O      . ASN   A 1 354 ? 3.63345   -15.18394 -7.34182  1.000 198.17154 ? 355 ASN   A O      1 
ATOM   5138 C CB     . ASN   A 1 354 ? 4.54449   -12.82823 -5.50734  1.000 205.84168 ? 355 ASN   A CB     1 
ATOM   5139 C CG     . ASN   A 1 354 ? 4.16702   -11.75514 -4.50319  1.000 208.59585 ? 355 ASN   A CG     1 
ATOM   5140 O OD1    . ASN   A 1 354 ? 3.09224   -11.79887 -3.90459  1.000 208.44997 ? 355 ASN   A OD1    1 
ATOM   5141 N ND2    . ASN   A 1 354 ? 5.05231   -10.78302 -4.31485  1.000 210.79485 ? 355 ASN   A ND2    1 
ATOM   5142 H H      . ASN   A 1 354 ? 4.97306   -14.21254 -3.54005  1.000 244.32950 ? 355 ASN   A H      1 
ATOM   5143 H HA     . ASN   A 1 354 ? 2.93544   -14.07046 -5.20744  1.000 245.72270 ? 355 ASN   A HA     1 
ATOM   5144 H HB2    . ASN   A 1 354 ? 5.50933   -12.92708 -5.49290  1.000 247.40049 ? 355 ASN   A HB2    1 
ATOM   5145 H HB3    . ASN   A 1 354 ? 4.25424   -12.53391 -6.38486  1.000 247.40049 ? 355 ASN   A HB3    1 
ATOM   5146 H HD21   . ASN   A 1 354 ? 4.88484   -10.15128 -3.75588  1.000 253.34430 ? 355 ASN   A HD21   1 
ATOM   5147 H HD22   . ASN   A 1 354 ? 5.79298   -10.78534 -4.75189  1.000 253.34430 ? 355 ASN   A HD22   1 
ATOM   5148 N N      . SER   A 1 355 ? 5.26796   -16.02823 -6.04810  1.000 188.56482 ? 356 SER   A N      1 
ATOM   5149 C CA     . SER   A 1 355 ? 5.71358   -16.96689 -7.06580  1.000 194.40108 ? 356 SER   A CA     1 
ATOM   5150 C C      . SER   A 1 355 ? 6.18396   -18.25091 -6.40189  1.000 194.07877 ? 356 SER   A C      1 
ATOM   5151 O O      . SER   A 1 355 ? 6.52072   -18.27656 -5.21502  1.000 193.98030 ? 356 SER   A O      1 
ATOM   5152 C CB     . SER   A 1 355 ? 6.83730   -16.37196 -7.92454  1.000 187.23096 ? 356 SER   A CB     1 
ATOM   5153 O OG     . SER   A 1 355 ? 7.92502   -15.95163 -7.12014  1.000 184.48667 ? 356 SER   A OG     1 
ATOM   5154 H H      . SER   A 1 355 ? 5.70308   -16.07576 -5.30783  1.000 226.66826 ? 356 SER   A H      1 
ATOM   5155 H HA     . SER   A 1 355 ? 4.96439   -17.18474 -7.64213  1.000 233.67177 ? 356 SER   A HA     1 
ATOM   5156 H HB2    . SER   A 1 355 ? 7.14879   -17.04727 -8.54730  1.000 225.06762 ? 356 SER   A HB2    1 
ATOM   5157 H HB3    . SER   A 1 355 ? 6.49099   -15.60714 -8.41036  1.000 225.06762 ? 356 SER   A HB3    1 
ATOM   5158 H HG     . SER   A 1 355 ? 8.51311   -15.58978 -7.59848  1.000 221.77447 ? 356 SER   A HG     1 
ATOM   5159 N N      . ILE   A 1 356 ? 6.19601   -19.32577 -7.19274  1.000 178.03181 ? 357 ILE   A N      1 
ATOM   5160 C CA     . ILE   A 1 356 ? 6.70583   -20.60231 -6.70332  1.000 187.99405 ? 357 ILE   A CA     1 
ATOM   5161 C C      . ILE   A 1 356 ? 8.15779   -20.45896 -6.26881  1.000 184.40962 ? 357 ILE   A C      1 
ATOM   5162 O O      . ILE   A 1 356 ? 8.57873   -21.03076 -5.25561  1.000 178.05083 ? 357 ILE   A O      1 
ATOM   5163 C CB     . ILE   A 1 356 ? 6.54126   -21.68968 -7.78252  1.000 183.57153 ? 357 ILE   A CB     1 
ATOM   5164 C CG1    . ILE   A 1 356 ? 5.05494   -21.97047 -8.02260  1.000 183.32486 ? 357 ILE   A CG1    1 
ATOM   5165 C CG2    . ILE   A 1 356 ? 7.28471   -22.95908 -7.37801  1.000 187.02245 ? 357 ILE   A CG2    1 
ATOM   5166 C CD1    . ILE   A 1 356 ? 4.77770   -22.86542 -9.21382  1.000 176.50342 ? 357 ILE   A CD1    1 
ATOM   5167 H H      . ILE   A 1 356 ? 5.91777   -19.34062 -8.00635  1.000 214.02865 ? 357 ILE   A H      1 
ATOM   5168 H HA     . ILE   A 1 356 ? 6.18623   -20.86808 -5.92854  1.000 225.98333 ? 357 ILE   A HA     1 
ATOM   5169 H HB     . ILE   A 1 356 ? 6.92773   -21.36867 -8.61227  1.000 220.67631 ? 357 ILE   A HB     1 
ATOM   5170 H HG12   . ILE   A 1 356 ? 4.69030   -22.40574 -7.23617  1.000 220.38030 ? 357 ILE   A HG12   1 
ATOM   5171 H HG13   . ILE   A 1 356 ? 4.60056   -21.12727 -8.17579  1.000 220.38030 ? 357 ILE   A HG13   1 
ATOM   5172 H HG21   . ILE   A 1 356 ? 7.00821   -23.68550 -7.95833  1.000 224.81741 ? 357 ILE   A HG21   1 
ATOM   5173 H HG22   . ILE   A 1 356 ? 8.23872   -22.80859 -7.46804  1.000 224.81741 ? 357 ILE   A HG22   1 
ATOM   5174 H HG23   . ILE   A 1 356 ? 7.06884   -23.17141 -6.45648  1.000 224.81741 ? 357 ILE   A HG23   1 
ATOM   5175 H HD11   . ILE   A 1 356 ? 3.82223   -22.88275 -9.38020  1.000 212.19457 ? 357 ILE   A HD11   1 
ATOM   5176 H HD12   . ILE   A 1 356 ? 5.24207   -22.51246 -9.98885  1.000 212.19457 ? 357 ILE   A HD12   1 
ATOM   5177 H HD13   . ILE   A 1 356 ? 5.09548   -23.76052 -9.01706  1.000 212.19457 ? 357 ILE   A HD13   1 
ATOM   5178 N N      . GLU   A 1 357 ? 8.94571   -19.69100 -7.02395  1.000 168.24056 ? 358 GLU   A N      1 
ATOM   5179 C CA     . GLU   A 1 357 ? 10.35034  -19.50887 -6.67566  1.000 166.24361 ? 358 GLU   A CA     1 
ATOM   5180 C C      . GLU   A 1 357 ? 10.49267  -18.82678 -5.32119  1.000 175.85982 ? 358 GLU   A C      1 
ATOM   5181 O O      . GLU   A 1 357 ? 11.30247  -19.24288 -4.48469  1.000 174.45699 ? 358 GLU   A O      1 
ATOM   5182 C CB     . GLU   A 1 357 ? 11.06103  -18.69941 -7.76014  1.000 175.75788 ? 358 GLU   A CB     1 
ATOM   5183 C CG     . GLU   A 1 357 ? 11.21744  -19.42832 -9.08703  1.000 186.14891 ? 358 GLU   A CG     1 
ATOM   5184 C CD     . GLU   A 1 357 ? 9.96490   -19.38024 -9.94278  1.000 182.09683 ? 358 GLU   A CD     1 
ATOM   5185 O OE1    . GLU   A 1 357 ? 8.97190   -18.75219 -9.51904  1.000 205.64635 ? 358 GLU   A OE1    1 
ATOM   5186 O OE2    . GLU   A 1 357 ? 9.97527   -19.97001 -11.04369 1.000 174.60963 ? 358 GLU   A OE2    1 
ATOM   5187 H H      . GLU   A 1 357 ? 8.69386   -19.27186 -7.73141  1.000 202.27914 ? 358 GLU   A H      1 
ATOM   5188 H HA     . GLU   A 1 357 ? 10.77368  -20.38009 -6.62407  1.000 199.88280 ? 358 GLU   A HA     1 
ATOM   5189 H HB2    . GLU   A 1 357 ? 10.55097  -17.89148 -7.92744  1.000 211.29992 ? 358 GLU   A HB2    1 
ATOM   5190 H HB3    . GLU   A 1 357 ? 11.94929  -18.47148 -7.44400  1.000 211.29992 ? 358 GLU   A HB3    1 
ATOM   5191 H HG2    . GLU   A 1 357 ? 11.93825  -19.01708 -9.58924  1.000 223.76916 ? 358 GLU   A HG2    1 
ATOM   5192 H HG3    . GLU   A 1 357 ? 11.42418  -20.35977 -8.91224  1.000 223.76916 ? 358 GLU   A HG3    1 
ATOM   5193 N N      . GLU   A 1 358 ? 9.71330   -17.76781 -5.08887  1.000 180.74622 ? 359 GLU   A N      1 
ATOM   5194 C CA     . GLU   A 1 358 ? 9.77840   -17.07577 -3.80603  1.000 179.11029 ? 359 GLU   A CA     1 
ATOM   5195 C C      . GLU   A 1 358 ? 9.38636   -18.00094 -2.66079  1.000 182.42045 ? 359 GLU   A C      1 
ATOM   5196 O O      . GLU   A 1 358 ? 10.01066  -17.97801 -1.59344  1.000 187.04430 ? 359 GLU   A O      1 
ATOM   5197 C CB     . GLU   A 1 358 ? 8.87831   -15.84116 -3.82915  1.000 189.77423 ? 359 GLU   A CB     1 
ATOM   5198 C CG     . GLU   A 1 358 ? 9.39400   -14.71490 -4.71045  1.000 188.31224 ? 359 GLU   A CG     1 
ATOM   5199 C CD     . GLU   A 1 358 ? 8.45296   -13.52760 -4.74422  1.000 195.30248 ? 359 GLU   A CD     1 
ATOM   5200 O OE1    . GLU   A 1 358 ? 7.37061   -13.61052 -4.12694  1.000 206.83812 ? 359 GLU   A OE1    1 
ATOM   5201 O OE2    . GLU   A 1 358 ? 8.79497   -12.51225 -5.38586  1.000 200.76755 ? 359 GLU   A OE2    1 
ATOM   5202 H H      . GLU   A 1 358 ? 9.14947   -17.43754 -5.64799  1.000 217.28594 ? 359 GLU   A H      1 
ATOM   5203 H HA     . GLU   A 1 358 ? 10.69010  -16.78024 -3.65648  1.000 215.32282 ? 359 GLU   A HA     1 
ATOM   5204 H HB2    . GLU   A 1 358 ? 8.00474   -16.09977 -4.16213  1.000 228.11954 ? 359 GLU   A HB2    1 
ATOM   5205 H HB3    . GLU   A 1 358 ? 8.80034   -15.49660 -2.92576  1.000 228.11954 ? 359 GLU   A HB3    1 
ATOM   5206 H HG2    . GLU   A 1 358 ? 10.24955  -14.41128 -4.36876  1.000 226.36516 ? 359 GLU   A HG2    1 
ATOM   5207 H HG3    . GLU   A 1 358 ? 9.49665   -15.04353 -5.61729  1.000 226.36516 ? 359 GLU   A HG3    1 
ATOM   5208 N N      . ALA   A 1 359 ? 8.35138   -18.82111 -2.86036  1.000 182.60330 ? 360 ALA   A N      1 
ATOM   5209 C CA     . ALA   A 1 359 ? 7.95723   -19.76931 -1.82366  1.000 187.79888 ? 360 ALA   A CA     1 
ATOM   5210 C C      . ALA   A 1 359 ? 9.07684   -20.76242 -1.53890  1.000 182.62656 ? 360 ALA   A C      1 
ATOM   5211 O O      . ALA   A 1 359 ? 9.30693   -21.13702 -0.38269  1.000 173.84177 ? 360 ALA   A O      1 
ATOM   5212 C CB     . ALA   A 1 359 ? 6.68037   -20.50053 -2.23781  1.000 190.70703 ? 360 ALA   A CB     1 
ATOM   5213 H H      . ALA   A 1 359 ? 7.87159   -18.84660 -3.57363  1.000 219.51443 ? 360 ALA   A H      1 
ATOM   5214 H HA     . ALA   A 1 359 ? 7.76934   -19.28242 -1.00602  1.000 225.74913 ? 360 ALA   A HA     1 
ATOM   5215 H HB1    . ALA   A 1 359 ? 6.43256   -21.12450 -1.53771  1.000 229.23891 ? 360 ALA   A HB1    1 
ATOM   5216 H HB2    . ALA   A 1 359 ? 5.97214   -19.85054 -2.36749  1.000 229.23891 ? 360 ALA   A HB2    1 
ATOM   5217 H HB3    . ALA   A 1 359 ? 6.84503   -20.97976 -3.06493  1.000 229.23891 ? 360 ALA   A HB3    1 
ATOM   5218 N N      . ILE   A 1 360 ? 9.78578   -21.19917 -2.58295  1.000 174.12773 ? 361 ILE   A N      1 
ATOM   5219 C CA     . ILE   A 1 360 ? 10.92438  -22.09074 -2.38810  1.000 166.36851 ? 361 ILE   A CA     1 
ATOM   5220 C C      . ILE   A 1 360 ? 12.04644  -21.36911 -1.65370  1.000 166.96411 ? 361 ILE   A C      1 
ATOM   5221 O O      . ILE   A 1 360 ? 12.68755  -21.93512 -0.76023  1.000 165.53639 ? 361 ILE   A O      1 
ATOM   5222 C CB     . ILE   A 1 360 ? 11.40320  -22.64707 -3.74243  1.000 150.64225 ? 361 ILE   A CB     1 
ATOM   5223 C CG1    . ILE   A 1 360 ? 10.39003  -23.65974 -4.28127  1.000 156.96039 ? 361 ILE   A CG1    1 
ATOM   5224 C CG2    . ILE   A 1 360 ? 12.78703  -23.27358 -3.60154  1.000 144.65077 ? 361 ILE   A CG2    1 
ATOM   5225 C CD1    . ILE   A 1 360 ? 10.62861  -24.07381 -5.71915  1.000 159.84245 ? 361 ILE   A CD1    1 
ATOM   5226 H H      . ILE   A 1 360 ? 9.62858   -20.99544 -3.40355  1.000 209.34375 ? 361 ILE   A H      1 
ATOM   5227 H HA     . ILE   A 1 360 ? 10.63916  -22.83796 -1.83927  1.000 200.03268 ? 361 ILE   A HA     1 
ATOM   5228 H HB     . ILE   A 1 360 ? 11.46878  -21.91567 -4.37619  1.000 181.16117 ? 361 ILE   A HB     1 
ATOM   5229 H HG12   . ILE   A 1 360 ? 10.43062  -24.45983 -3.73436  1.000 188.74293 ? 361 ILE   A HG12   1 
ATOM   5230 H HG13   . ILE   A 1 360 ? 9.50393   -23.26829 -4.23125  1.000 188.74293 ? 361 ILE   A HG13   1 
ATOM   5231 H HG21   . ILE   A 1 360 ? 12.97887  -23.79728 -4.39516  1.000 173.97139 ? 361 ILE   A HG21   1 
ATOM   5232 H HG22   . ILE   A 1 360 ? 13.44493  -22.56748 -3.50416  1.000 173.97139 ? 361 ILE   A HG22   1 
ATOM   5233 H HG23   . ILE   A 1 360 ? 12.79666  -23.84505 -2.81781  1.000 173.97139 ? 361 ILE   A HG23   1 
ATOM   5234 H HD11   . ILE   A 1 360 ? 9.89847   -24.64270 -6.00925  1.000 192.20141 ? 361 ILE   A HD11   1 
ATOM   5235 H HD12   . ILE   A 1 360 ? 10.66939  -23.27922 -6.27399  1.000 192.20141 ? 361 ILE   A HD12   1 
ATOM   5236 H HD13   . ILE   A 1 360 ? 11.46713  -24.55843 -5.77324  1.000 192.20141 ? 361 ILE   A HD13   1 
ATOM   5237 N N      . GLU   A 1 361 ? 12.30673  -20.11310 -2.02019  1.000 166.60860 ? 362 GLU   A N      1 
ATOM   5238 C CA     . GLU   A 1 361 ? 13.37250  -19.35765 -1.37052  1.000 165.68942 ? 362 GLU   A CA     1 
ATOM   5239 C C      . GLU   A 1 361 ? 13.10884  -19.21823 0.12390   1.000 172.35937 ? 362 GLU   A C      1 
ATOM   5240 O O      . GLU   A 1 361 ? 14.01161  -19.41209 0.94683   1.000 168.55902 ? 362 GLU   A O      1 
ATOM   5241 C CB     . GLU   A 1 361 ? 13.50816  -17.98371 -2.02784  1.000 168.77710 ? 362 GLU   A CB     1 
ATOM   5242 C CG     . GLU   A 1 361 ? 14.66121  -17.14129 -1.49878  1.000 186.68338 ? 362 GLU   A CG     1 
ATOM   5243 C CD     . GLU   A 1 361 ? 16.02222  -17.70908 -1.86008  1.000 189.24736 ? 362 GLU   A CD     1 
ATOM   5244 O OE1    . GLU   A 1 361 ? 16.07697  -18.80777 -2.45255  1.000 173.46835 ? 362 GLU   A OE1    1 
ATOM   5245 O OE2    . GLU   A 1 361 ? 17.03984  -17.05177 -1.55441  1.000 172.54193 ? 362 GLU   A OE2    1 
ATOM   5246 H H      . GLU   A 1 361 ? 11.88581  -19.68237 -2.63411  1.000 200.32079 ? 362 GLU   A H      1 
ATOM   5247 H HA     . GLU   A 1 361 ? 14.21146  -19.83102 -1.48443  1.000 199.21777 ? 362 GLU   A HA     1 
ATOM   5248 H HB2    . GLU   A 1 361 ? 13.64946  -18.10909 -2.97927  1.000 202.92299 ? 362 GLU   A HB2    1 
ATOM   5249 H HB3    . GLU   A 1 361 ? 12.68893  -17.48679 -1.87675  1.000 202.92299 ? 362 GLU   A HB3    1 
ATOM   5250 H HG2    . GLU   A 1 361 ? 14.59930  -16.24958 -1.87549  1.000 224.41053 ? 362 GLU   A HG2    1 
ATOM   5251 H HG3    . GLU   A 1 361 ? 14.60226  -17.09766 -0.53156  1.000 224.41053 ? 362 GLU   A HG3    1 
ATOM   5252 N N      . ASN   A 1 362 ? 11.87194  -18.88307 0.49588   1.000 164.59313 ? 363 ASN   A N      1 
ATOM   5253 C CA     . ASN   A 1 362 ? 11.54657  -18.72706 1.90941   1.000 160.99674 ? 363 ASN   A CA     1 
ATOM   5254 C C      . ASN   A 1 362 ? 11.78502  -20.02401 2.67178   1.000 161.85585 ? 363 ASN   A C      1 
ATOM   5255 O O      . ASN   A 1 362 ? 12.36736  -20.01811 3.76143   1.000 159.32670 ? 363 ASN   A O      1 
ATOM   5256 C CB     . ASN   A 1 362 ? 10.09824  -18.26878 2.07266   1.000 177.33719 ? 363 ASN   A CB     1 
ATOM   5257 C CG     . ASN   A 1 362 ? 9.69834   -18.10617 3.53059   1.000 182.15483 ? 363 ASN   A CG     1 
ATOM   5258 O OD1    . ASN   A 1 362 ? 9.24914   -19.05572 4.17335   1.000 161.09753 ? 363 ASN   A OD1    1 
ATOM   5259 N ND2    . ASN   A 1 362 ? 9.86073   -16.89771 4.05843   1.000 179.81205 ? 363 ASN   A ND2    1 
ATOM   5260 H H      . ASN   A 1 362 ? 11.21578  -18.74319 -0.04216  1.000 197.90222 ? 363 ASN   A H      1 
ATOM   5261 H HA     . ASN   A 1 362 ? 12.12166  -18.04220 2.28509   1.000 193.58656 ? 363 ASN   A HA     1 
ATOM   5262 H HB2    . ASN   A 1 362 ? 9.98562   -17.41173 1.63255   1.000 213.19510 ? 363 ASN   A HB2    1 
ATOM   5263 H HB3    . ASN   A 1 362 ? 9.51031   -18.92765 1.67125   1.000 213.19510 ? 363 ASN   A HB3    1 
ATOM   5264 H HD21   . ASN   A 1 362 ? 9.64906   -16.75521 4.87970   1.000 216.16493 ? 363 ASN   A HD21   1 
ATOM   5265 H HD22   . ASN   A 1 362 ? 10.17751  -16.25801 3.57881   1.000 216.16493 ? 363 ASN   A HD22   1 
ATOM   5266 N N      . TYR   A 1 363 ? 11.33402  -21.15136 2.11450   1.000 156.35459 ? 364 TYR   A N      1 
ATOM   5267 C CA     . TYR   A 1 363 ? 11.57747  -22.43707 2.75954   1.000 149.59146 ? 364 TYR   A CA     1 
ATOM   5268 C C      . TYR   A 1 363 ? 13.06774  -22.66004 2.98443   1.000 149.63664 ? 364 TYR   A C      1 
ATOM   5269 O O      . TYR   A 1 363 ? 13.49534  -23.02740 4.08478   1.000 136.26088 ? 364 TYR   A O      1 
ATOM   5270 C CB     . TYR   A 1 363 ? 10.99223  -23.57142 1.91834   1.000 143.86560 ? 364 TYR   A CB     1 
ATOM   5271 C CG     . TYR   A 1 363 ? 11.81061  -24.84065 1.99126   1.000 151.76796 ? 364 TYR   A CG     1 
ATOM   5272 C CD1    . TYR   A 1 363 ? 11.83041  -25.61341 3.14538   1.000 153.60256 ? 364 TYR   A CD1    1 
ATOM   5273 C CD2    . TYR   A 1 363 ? 12.57151  -25.26120 0.90876   1.000 157.72649 ? 364 TYR   A CD2    1 
ATOM   5274 C CE1    . TYR   A 1 363 ? 12.58473  -26.76881 3.21707   1.000 150.62528 ? 364 TYR   A CE1    1 
ATOM   5275 C CE2    . TYR   A 1 363 ? 13.32519  -26.41487 0.97088   1.000 144.89170 ? 364 TYR   A CE2    1 
ATOM   5276 C CZ     . TYR   A 1 363 ? 13.32765  -27.16463 2.12427   1.000 139.16982 ? 364 TYR   A CZ     1 
ATOM   5277 O OH     . TYR   A 1 363 ? 14.08412  -28.31051 2.17903   1.000 133.92824 ? 364 TYR   A OH     1 
ATOM   5278 H H      . TYR   A 1 363 ? 10.89311  -21.19561 1.37746   1.000 188.01597 ? 364 TYR   A H      1 
ATOM   5279 H HA     . TYR   A 1 363 ? 11.13195  -22.43988 3.62116   1.000 179.90022 ? 364 TYR   A HA     1 
ATOM   5280 H HB2    . TYR   A 1 363 ? 10.09869  -23.77217 2.23799   1.000 173.02920 ? 364 TYR   A HB2    1 
ATOM   5281 H HB3    . TYR   A 1 363 ? 10.95734  -23.29019 0.99066   1.000 173.02920 ? 364 TYR   A HB3    1 
ATOM   5282 H HD1    . TYR   A 1 363 ? 11.32780  -25.34880 3.88177   1.000 184.71354 ? 364 TYR   A HD1    1 
ATOM   5283 H HD2    . TYR   A 1 363 ? 12.57309  -24.75612 0.12787   1.000 189.66226 ? 364 TYR   A HD2    1 
ATOM   5284 H HE1    . TYR   A 1 363 ? 12.59154  -27.27603 3.99655   1.000 181.14080 ? 364 TYR   A HE1    1 
ATOM   5285 H HE2    . TYR   A 1 363 ? 13.82892  -26.68432 0.23702   1.000 174.26052 ? 364 TYR   A HE2    1 
ATOM   5286 H HH     . TYR   A 1 363 ? 14.33777  -28.44990 2.96759   1.000 161.10436 ? 364 TYR   A HH     1 
ATOM   5287 N N      . GLU   A 1 364 ? 13.87688  -22.44373 1.94568   1.000 156.94561 ? 365 GLU   A N      1 
ATOM   5288 C CA     . GLU   A 1 364 ? 15.31075  -22.68283 2.06950   1.000 162.98920 ? 365 GLU   A CA     1 
ATOM   5289 C C      . GLU   A 1 364 ? 15.93849  -21.74504 3.09267   1.000 158.36574 ? 365 GLU   A C      1 
ATOM   5290 O O      . GLU   A 1 364 ? 16.85526  -22.13765 3.82407   1.000 151.95376 ? 365 GLU   A O      1 
ATOM   5291 C CB     . GLU   A 1 364 ? 15.98084  -22.53353 0.70438   1.000 148.94780 ? 365 GLU   A CB     1 
ATOM   5292 C CG     . GLU   A 1 364 ? 15.49603  -23.55285 -0.31491  1.000 142.29544 ? 365 GLU   A CG     1 
ATOM   5293 C CD     . GLU   A 1 364 ? 16.16883  -23.40508 -1.65930  1.000 144.38701 ? 365 GLU   A CD     1 
ATOM   5294 O OE1    . GLU   A 1 364 ? 16.96853  -22.46120 -1.82622  1.000 160.26316 ? 365 GLU   A OE1    1 
ATOM   5295 O OE2    . GLU   A 1 364 ? 15.89526  -24.23531 -2.55002  1.000 141.70941 ? 365 GLU   A OE2    1 
ATOM   5296 H H      . GLU   A 1 364 ? 13.62403  -22.16365 1.17288   1.000 188.72521 ? 365 GLU   A H      1 
ATOM   5297 H HA     . GLU   A 1 364 ? 15.45699  -23.59186 2.37476   1.000 195.97751 ? 365 GLU   A HA     1 
ATOM   5298 H HB2    . GLU   A 1 364 ? 15.78989  -21.64866 0.35589   1.000 179.12783 ? 365 GLU   A HB2    1 
ATOM   5299 H HB3    . GLU   A 1 364 ? 16.93812  -22.64899 0.81011   1.000 179.12783 ? 365 GLU   A HB3    1 
ATOM   5300 H HG2    . GLU   A 1 364 ? 15.68325  -24.44481 0.01714   1.000 171.14500 ? 365 GLU   A HG2    1 
ATOM   5301 H HG3    . GLU   A 1 364 ? 14.54124  -23.44053 -0.44400  1.000 171.14500 ? 365 GLU   A HG3    1 
ATOM   5302 N N      . GLN   A 1 365 ? 15.45779  -20.50212 3.16315   1.000 159.36987 ? 366 GLN   A N      1 
ATOM   5303 C CA     . GLN   A 1 365 ? 15.92588  -19.58947 4.20134   1.000 161.80191 ? 366 GLN   A CA     1 
ATOM   5304 C C      . GLN   A 1 365 ? 15.66212  -20.16534 5.58676   1.000 161.11730 ? 366 GLN   A C      1 
ATOM   5305 O O      . GLN   A 1 365 ? 16.56215  -20.22138 6.43307   1.000 152.55308 ? 366 GLN   A O      1 
ATOM   5306 C CB     . GLN   A 1 365 ? 15.24765  -18.22834 4.04659   1.000 156.87679 ? 366 GLN   A CB     1 
ATOM   5307 C CG     . GLN   A 1 365 ? 15.83215  -17.36855 2.93982   1.000 189.87520 ? 366 GLN   A CG     1 
ATOM   5308 C CD     . GLN   A 1 365 ? 14.94750  -16.18797 2.59007   1.000 195.60727 ? 366 GLN   A CD     1 
ATOM   5309 O OE1    . GLN   A 1 365 ? 13.94533  -15.92971 3.25643   1.000 189.20201 ? 366 GLN   A OE1    1 
ATOM   5310 N NE2    . GLN   A 1 365 ? 15.31183  -15.46715 1.53549   1.000 186.34566 ? 366 GLN   A NE2    1 
ATOM   5311 H H      . GLN   A 1 365 ? 14.87013  -20.16974 2.63043   1.000 191.63431 ? 366 GLN   A H      1 
ATOM   5312 H HA     . GLN   A 1 365 ? 16.88217  -19.46166 4.10092   1.000 194.55276 ? 366 GLN   A HA     1 
ATOM   5313 H HB2    . GLN   A 1 365 ? 14.30925  -18.36978 3.84586   1.000 188.64262 ? 366 GLN   A HB2    1 
ATOM   5314 H HB3    . GLN   A 1 365 ? 15.33875  -17.73931 4.87933   1.000 188.64262 ? 366 GLN   A HB3    1 
ATOM   5315 H HG2    . GLN   A 1 365 ? 16.69259  -17.02477 3.22682   1.000 228.24071 ? 366 GLN   A HG2    1 
ATOM   5316 H HG3    . GLN   A 1 365 ? 15.94044  -17.90972 2.14213   1.000 228.24071 ? 366 GLN   A HG3    1 
ATOM   5317 H HE21   . GLN   A 1 365 ? 16.01691  -15.68044 1.09167   1.000 224.00527 ? 366 GLN   A HE21   1 
ATOM   5318 H HE22   . GLN   A 1 365 ? 14.84264  -14.78717 1.29654   1.000 224.00527 ? 366 GLN   A HE22   1 
ATOM   5319 N N      . GLN   A 1 366 ? 14.42541  -20.60343 5.83435   1.000 161.48648 ? 367 GLN   A N      1 
ATOM   5320 C CA     . GLN   A 1 366 ? 14.09537  -21.19359 7.12647   1.000 151.04313 ? 367 GLN   A CA     1 
ATOM   5321 C C      . GLN   A 1 366 ? 14.86455  -22.48767 7.35539   1.000 146.61819 ? 367 GLN   A C      1 
ATOM   5322 O O      . GLN   A 1 366 ? 15.35821  -22.73958 8.46117   1.000 140.92438 ? 367 GLN   A O      1 
ATOM   5323 C CB     . GLN   A 1 366 ? 12.59236  -21.45653 7.21564   1.000 151.39849 ? 367 GLN   A CB     1 
ATOM   5324 C CG     . GLN   A 1 366 ? 11.73241  -20.20795 7.23646   1.000 159.20865 ? 367 GLN   A CG     1 
ATOM   5325 C CD     . GLN   A 1 366 ? 10.26347  -20.52142 7.44757   1.000 164.19434 ? 367 GLN   A CD     1 
ATOM   5326 O OE1    . GLN   A 1 366 ? 9.88887   -21.16337 8.42870   1.000 138.49150 ? 367 GLN   A OE1    1 
ATOM   5327 N NE2    . GLN   A 1 366 ? 9.42362   -20.07455 6.52147   1.000 175.65891 ? 367 GLN   A NE2    1 
ATOM   5328 H H      . GLN   A 1 366 ? 13.77042  -20.57011 5.27805   1.000 194.17424 ? 367 GLN   A H      1 
ATOM   5329 H HA     . GLN   A 1 366 ? 14.33875  -20.56476 7.82377   1.000 181.64223 ? 367 GLN   A HA     1 
ATOM   5330 H HB2    . GLN   A 1 366 ? 12.32516  -21.98277 6.44585   1.000 182.06866 ? 367 GLN   A HB2    1 
ATOM   5331 H HB3    . GLN   A 1 366 ? 12.41328  -21.94853 8.03219   1.000 182.06866 ? 367 GLN   A HB3    1 
ATOM   5332 H HG2    . GLN   A 1 366 ? 12.02508  -19.63292 7.96075   1.000 191.44085 ? 367 GLN   A HG2    1 
ATOM   5333 H HG3    . GLN   A 1 366 ? 11.82320  -19.74574 6.38851   1.000 191.44085 ? 367 GLN   A HG3    1 
ATOM   5334 H HE21   . GLN   A 1 366 ? 9.72274   -19.63294 5.84685   1.000 211.18116 ? 367 GLN   A HE21   1 
ATOM   5335 H HE22   . GLN   A 1 366 ? 8.58049   -20.22670 6.59620   1.000 211.18116 ? 367 GLN   A HE22   1 
ATOM   5336 N N      . MET   A 1 367 ? 14.97193  -23.32423 6.32029   1.000 149.20204 ? 368 MET   A N      1 
ATOM   5337 C CA     . MET   A 1 367 ? 15.59444  -24.63375 6.48693   1.000 155.79441 ? 368 MET   A CA     1 
ATOM   5338 C C      . MET   A 1 367 ? 17.06820  -24.50410 6.84791   1.000 146.90944 ? 368 MET   A C      1 
ATOM   5339 O O      . MET   A 1 367 ? 17.58117  -25.26500 7.67786   1.000 122.60069 ? 368 MET   A O      1 
ATOM   5340 C CB     . MET   A 1 367 ? 15.42007  -25.45571 5.20819   1.000 153.81916 ? 368 MET   A CB     1 
ATOM   5341 C CG     . MET   A 1 367 ? 16.10100  -26.81824 5.23649   1.000 153.22869 ? 368 MET   A CG     1 
ATOM   5342 S SD     . MET   A 1 367 ? 17.79328  -26.79808 4.61221   1.000 135.51283 ? 368 MET   A SD     1 
ATOM   5343 C CE     . MET   A 1 367 ? 17.51030  -26.45511 2.87784   1.000 159.33903 ? 368 MET   A CE     1 
ATOM   5344 H H      . MET   A 1 367 ? 14.69576  -23.15859 5.52286   1.000 179.43292 ? 368 MET   A H      1 
ATOM   5345 H HA     . MET   A 1 367 ? 15.14369  -25.10301 7.20632   1.000 187.34377 ? 368 MET   A HA     1 
ATOM   5346 H HB2    . MET   A 1 367 ? 14.47257  -25.60445 5.06316   1.000 184.97347 ? 368 MET   A HB2    1 
ATOM   5347 H HB3    . MET   A 1 367 ? 15.79486  -24.95604 4.46606   1.000 184.97347 ? 368 MET   A HB3    1 
ATOM   5348 H HG2    . MET   A 1 367 ? 16.12764  -27.13497 6.15294   1.000 184.26489 ? 368 MET   A HG2    1 
ATOM   5349 H HG3    . MET   A 1 367 ? 15.59059  -27.43381 4.68744   1.000 184.26489 ? 368 MET   A HG3    1 
ATOM   5350 H HE1    . MET   A 1 367 ? 18.36388  -26.30490 2.44226   1.000 191.59731 ? 368 MET   A HE1    1 
ATOM   5351 H HE2    . MET   A 1 367 ? 17.06239  -27.21516 2.47461   1.000 191.59731 ? 368 MET   A HE2    1 
ATOM   5352 H HE3    . MET   A 1 367 ? 16.95489  -25.66378 2.79894   1.000 191.59731 ? 368 MET   A HE3    1 
ATOM   5353 N N      . PHE   A 1 368 ? 17.76518  -23.54354 6.23912   1.000 148.06509 ? 369 PHE   A N      1 
ATOM   5354 C CA     . PHE   A 1 368 ? 19.18408  -23.36934 6.52708   1.000 154.72443 ? 369 PHE   A CA     1 
ATOM   5355 C C      . PHE   A 1 368 ? 19.42200  -23.08905 8.00409   1.000 134.40659 ? 369 PHE   A C      1 
ATOM   5356 O O      . PHE   A 1 368 ? 20.42378  -23.53590 8.57238   1.000 130.00318 ? 369 PHE   A O      1 
ATOM   5357 C CB     . PHE   A 1 368 ? 19.75944  -22.24050 5.67286   1.000 171.05255 ? 369 PHE   A CB     1 
ATOM   5358 C CG     . PHE   A 1 368 ? 20.56903  -22.71881 4.50192   1.000 144.96598 ? 369 PHE   A CG     1 
ATOM   5359 C CD1    . PHE   A 1 368 ? 19.94860  -23.24959 3.38437   1.000 140.42422 ? 369 PHE   A CD1    1 
ATOM   5360 C CD2    . PHE   A 1 368 ? 21.95147  -22.63381 4.51836   1.000 144.93694 ? 369 PHE   A CD2    1 
ATOM   5361 C CE1    . PHE   A 1 368 ? 20.69213  -23.69026 2.30669   1.000 157.64475 ? 369 PHE   A CE1    1 
ATOM   5362 C CE2    . PHE   A 1 368 ? 22.69965  -23.07196 3.44377   1.000 157.53764 ? 369 PHE   A CE2    1 
ATOM   5363 C CZ     . PHE   A 1 368 ? 22.06955  -23.60060 2.33679   1.000 160.75630 ? 369 PHE   A CZ     1 
ATOM   5364 H H      . PHE   A 1 368 ? 17.44423  -22.98941 5.66507   1.000 178.06858 ? 369 PHE   A H      1 
ATOM   5365 H HA     . PHE   A 1 368 ? 19.64787  -24.18993 6.29810   1.000 186.05979 ? 369 PHE   A HA     1 
ATOM   5366 H HB2    . PHE   A 1 368 ? 19.02697  -21.70640 5.32770   1.000 205.65353 ? 369 PHE   A HB2    1 
ATOM   5367 H HB3    . PHE   A 1 368 ? 20.33664  -21.69288 6.22770   1.000 205.65353 ? 369 PHE   A HB3    1 
ATOM   5368 H HD1    . PHE   A 1 368 ? 19.02093  -23.31025 3.35865   1.000 168.89954 ? 369 PHE   A HD1    1 
ATOM   5369 H HD2    . PHE   A 1 368 ? 22.38095  -22.27728 5.26223   1.000 174.31480 ? 369 PHE   A HD2    1 
ATOM   5370 H HE1    . PHE   A 1 368 ? 20.26519  -24.04705 1.56149   1.000 189.56417 ? 369 PHE   A HE1    1 
ATOM   5371 H HE2    . PHE   A 1 368 ? 23.62735  -23.01065 3.46645   1.000 189.43564 ? 369 PHE   A HE2    1 
ATOM   5372 H HZ     . PHE   A 1 368 ? 22.57155  -23.89617 1.61186   1.000 193.29803 ? 369 PHE   A HZ     1 
ATOM   5373 N N      . ALA   A 1 369 ? 18.50788  -22.35847 8.64649   1.000 138.93410 ? 370 ALA   A N      1 
ATOM   5374 C CA     . ALA   A 1 369 ? 18.71613  -21.96463 10.03609  1.000 151.39320 ? 370 ALA   A CA     1 
ATOM   5375 C C      . ALA   A 1 369 ? 18.65311  -23.17086 10.96586  1.000 146.06389 ? 370 ALA   A C      1 
ATOM   5376 O O      . ALA   A 1 369 ? 19.64979  -23.53427 11.60145  1.000 137.59369 ? 370 ALA   A O      1 
ATOM   5377 C CB     . ALA   A 1 369 ? 17.68148  -20.91224 10.44084  1.000 148.71984 ? 370 ALA   A CB     1 
ATOM   5378 H H      . ALA   A 1 369 ? 17.76915  -22.08263 8.30328   1.000 167.11139 ? 370 ALA   A H      1 
ATOM   5379 H HA     . ALA   A 1 369 ? 19.59788  -21.56905 10.11932  1.000 182.06231 ? 370 ALA   A HA     1 
ATOM   5380 H HB1    . ALA   A 1 369 ? 17.83535  -20.65674 11.36385  1.000 178.85427 ? 370 ALA   A HB1    1 
ATOM   5381 H HB2    . ALA   A 1 369 ? 17.77546  -20.13854 9.86338   1.000 178.85427 ? 370 ALA   A HB2    1 
ATOM   5382 H HB3    . ALA   A 1 369 ? 16.79308  -21.28991 10.34587  1.000 178.85427 ? 370 ALA   A HB3    1 
ATOM   5383 N N      . TYR   A 1 370 ? 17.48388  -23.80968 11.05920  1.000 146.22312 ? 371 TYR   A N      1 
ATOM   5384 C CA     . TYR   A 1 370 ? 17.33307  -24.90880 12.00680  1.000 148.82588 ? 371 TYR   A CA     1 
ATOM   5385 C C      . TYR   A 1 370 ? 18.05182  -26.16622 11.53316  1.000 145.22201 ? 371 TYR   A C      1 
ATOM   5386 O O      . TYR   A 1 370 ? 18.44085  -27.00181 12.35761  1.000 125.68276 ? 371 TYR   A O      1 
ATOM   5387 C CB     . TYR   A 1 370 ? 15.84999  -25.19870 12.25366  1.000 159.20570 ? 371 TYR   A CB     1 
ATOM   5388 C CG     . TYR   A 1 370 ? 15.08084  -25.69211 11.04622  1.000 156.61463 ? 371 TYR   A CG     1 
ATOM   5389 C CD1    . TYR   A 1 370 ? 15.22469  -26.99655 10.59019  1.000 147.92374 ? 371 TYR   A CD1    1 
ATOM   5390 C CD2    . TYR   A 1 370 ? 14.19038  -24.86095 10.37885  1.000 159.06516 ? 371 TYR   A CD2    1 
ATOM   5391 C CE1    . TYR   A 1 370 ? 14.52040  -27.45288 9.49453   1.000 146.71854 ? 371 TYR   A CE1    1 
ATOM   5392 C CE2    . TYR   A 1 370 ? 13.47719  -25.31048 9.28381   1.000 149.92759 ? 371 TYR   A CE2    1 
ATOM   5393 C CZ     . TYR   A 1 370 ? 13.64662  -26.60769 8.84650   1.000 141.39052 ? 371 TYR   A CZ     1 
ATOM   5394 O OH     . TYR   A 1 370 ? 12.94281  -27.06158 7.75543   1.000 137.74174 ? 371 TYR   A OH     1 
ATOM   5395 H H      . TYR   A 1 370 ? 16.78186  -23.62932 10.59635  1.000 175.85821 ? 371 TYR   A H      1 
ATOM   5396 H HA     . TYR   A 1 370 ? 17.72657  -24.64290 12.85258  1.000 178.98152 ? 371 TYR   A HA     1 
ATOM   5397 H HB2    . TYR   A 1 370 ? 15.78121  -25.88073 12.93997  1.000 191.43731 ? 371 TYR   A HB2    1 
ATOM   5398 H HB3    . TYR   A 1 370 ? 15.42391  -24.38095 12.55471  1.000 191.43731 ? 371 TYR   A HB3    1 
ATOM   5399 H HD1    . TYR   A 1 370 ? 15.80624  -27.57282 11.03135  1.000 177.89895 ? 371 TYR   A HD1    1 
ATOM   5400 H HD2    . TYR   A 1 370 ? 14.07207  -23.98698 10.67394  1.000 191.26866 ? 371 TYR   A HD2    1 
ATOM   5401 H HE1    . TYR   A 1 370 ? 14.63504  -28.32597 9.19540   1.000 176.45271 ? 371 TYR   A HE1    1 
ATOM   5402 H HE2    . TYR   A 1 370 ? 12.88671  -24.74196 8.84449   1.000 180.30358 ? 371 TYR   A HE2    1 
ATOM   5403 H HH     . TYR   A 1 370 ? 13.08605  -27.88146 7.64194   1.000 165.68056 ? 371 TYR   A HH     1 
ATOM   5404 N N      . GLY   A 1 371 ? 18.23349  -26.32281 10.22077  1.000 155.72108 ? 372 GLY   A N      1 
ATOM   5405 C CA     . GLY   A 1 371 ? 18.97028  -27.47202 9.72259   1.000 152.01215 ? 372 GLY   A CA     1 
ATOM   5406 C C      . GLY   A 1 371 ? 20.44094  -27.41622 10.08621  1.000 143.61000 ? 372 GLY   A C      1 
ATOM   5407 O O      . GLY   A 1 371 ? 21.02481  -28.41822 10.50872  1.000 135.97836 ? 372 GLY   A O      1 
ATOM   5408 H H      . GLY   A 1 371 ? 17.94476  -25.78694 9.61325   1.000 187.25576 ? 372 GLY   A H      1 
ATOM   5409 H HA2    . GLY   A 1 371 ? 18.59290  -28.28280 10.09826  1.000 182.80505 ? 372 GLY   A HA2    1 
ATOM   5410 H HA3    . GLY   A 1 371 ? 18.89531  -27.50711 8.75613   1.000 182.80505 ? 372 GLY   A HA3    1 
ATOM   5411 N N      . ARG   A 1 372 ? 21.06198  -26.24620 9.92383   1.000 144.08883 ? 373 ARG   A N      1 
ATOM   5412 C CA     . ARG   A 1 372 ? 22.44164  -26.07863 10.36647  1.000 153.03058 ? 373 ARG   A CA     1 
ATOM   5413 C C      . ARG   A 1 372 ? 22.57991  -26.37472 11.85409  1.000 137.90486 ? 373 ARG   A C      1 
ATOM   5414 O O      . ARG   A 1 372 ? 23.55453  -27.00449 12.28232  1.000 127.93964 ? 373 ARG   A O      1 
ATOM   5415 C CB     . ARG   A 1 372 ? 22.92088  -24.66267 10.05133  1.000 144.40458 ? 373 ARG   A CB     1 
ATOM   5416 C CG     . ARG   A 1 372 ? 23.41400  -24.49812 8.62775   1.000 155.57983 ? 373 ARG   A CG     1 
ATOM   5417 C CD     . ARG   A 1 372 ? 23.59105  -23.03811 8.25331   1.000 172.12500 ? 373 ARG   A CD     1 
ATOM   5418 N NE     . ARG   A 1 372 ? 24.62365  -22.38159 9.04557   1.000 184.12893 ? 373 ARG   A NE     1 
ATOM   5419 C CZ     . ARG   A 1 372 ? 25.92536  -22.58491 8.89501   1.000 199.83449 ? 373 ARG   A CZ     1 
ATOM   5420 N NH1    . ARG   A 1 372 ? 26.39110  -23.46588 8.02478   1.000 178.00685 ? 373 ARG   A NH1    1 
ATOM   5421 N NH2    . ARG   A 1 372 ? 26.78107  -21.88963 9.63923   1.000 181.58750 ? 373 ARG   A NH2    1 
ATOM   5422 H H      . ARG   A 1 372 ? 20.71154  -25.54693 9.56632   1.000 173.29707 ? 373 ARG   A H      1 
ATOM   5423 H HA     . ARG   A 1 372 ? 23.00677  -26.70140 9.88306   1.000 184.02717 ? 373 ARG   A HA     1 
ATOM   5424 H HB2    . ARG   A 1 372 ? 22.18437  -24.04566 10.18460  1.000 173.67597 ? 373 ARG   A HB2    1 
ATOM   5425 H HB3    . ARG   A 1 372 ? 23.65265  -24.43955 10.64768  1.000 173.67597 ? 373 ARG   A HB3    1 
ATOM   5426 H HG2    . ARG   A 1 372 ? 24.27178  -24.94110 8.53355   1.000 187.08626 ? 373 ARG   A HG2    1 
ATOM   5427 H HG3    . ARG   A 1 372 ? 22.76913  -24.89089 8.01884   1.000 187.08626 ? 373 ARG   A HG3    1 
ATOM   5428 H HD2    . ARG   A 1 372 ? 23.84496  -22.97851 7.31904   1.000 206.94047 ? 373 ARG   A HD2    1 
ATOM   5429 H HD3    . ARG   A 1 372 ? 22.75488  -22.56898 8.40044   1.000 206.94047 ? 373 ARG   A HD3    1 
ATOM   5430 H HE     . ARG   A 1 372 ? 24.37181  -21.82523 9.65107   1.000 221.34518 ? 373 ARG   A HE     1 
ATOM   5431 H HH11   . ARG   A 1 372 ? 25.84572  -23.92209 7.54101   1.000 213.99869 ? 373 ARG   A HH11   1 
ATOM   5432 H HH12   . ARG   A 1 372 ? 27.23924  -23.58233 7.94286   1.000 213.99869 ? 373 ARG   A HH12   1 
ATOM   5433 H HH21   . ARG   A 1 372 ? 26.48790  -21.31654 10.20951  1.000 218.29547 ? 373 ARG   A HH21   1 
ATOM   5434 H HH22   . ARG   A 1 372 ? 27.62746  -22.01322 9.55009   1.000 218.29547 ? 373 ARG   A HH22   1 
ATOM   5435 N N      . GLU   A 1 373 ? 21.61163  -25.93227 12.65833  1.000 141.56322 ? 374 GLU   A N      1 
ATOM   5436 C CA     . GLU   A 1 373 ? 21.65466  -26.21447 14.08895  1.000 148.13727 ? 374 GLU   A CA     1 
ATOM   5437 C C      . GLU   A 1 373 ? 21.60347  -27.71464 14.34649  1.000 132.86003 ? 374 GLU   A C      1 
ATOM   5438 O O      . GLU   A 1 373 ? 22.38201  -28.24815 15.14556  1.000 126.45154 ? 374 GLU   A O      1 
ATOM   5439 C CB     . GLU   A 1 373 ? 20.49917  -25.50645 14.79712  1.000 156.34698 ? 374 GLU   A CB     1 
ATOM   5440 C CG     . GLU   A 1 373 ? 20.48068  -25.70843 16.30568  1.000 167.34811 ? 374 GLU   A CG     1 
ATOM   5441 C CD     . GLU   A 1 373 ? 19.34109  -24.97097 16.98153  1.000 182.94787 ? 374 GLU   A CD     1 
ATOM   5442 O OE1    . GLU   A 1 373 ? 18.26936  -24.82641 16.35561  1.000 187.27878 ? 374 GLU   A OE1    1 
ATOM   5443 O OE2    . GLU   A 1 373 ? 19.52013  -24.53228 18.13771  1.000 191.37125 ? 374 GLU   A OE2    1 
ATOM   5444 H H      . GLU   A 1 373 ? 20.93019  -25.47386 12.40318  1.000 170.26633 ? 374 GLU   A H      1 
ATOM   5445 H HA     . GLU   A 1 373 ? 22.48553  -25.87112 14.45319  1.000 178.15519 ? 374 GLU   A HA     1 
ATOM   5446 H HB2    . GLU   A 1 373 ? 20.56775  -24.55382 14.62776  1.000 188.00685 ? 374 GLU   A HB2    1 
ATOM   5447 H HB3    . GLU   A 1 373 ? 19.66253  -25.84690 14.44353  1.000 188.00685 ? 374 GLU   A HB3    1 
ATOM   5448 H HG2    . GLU   A 1 373 ? 20.38132  -26.65419 16.49690  1.000 201.20820 ? 374 GLU   A HG2    1 
ATOM   5449 H HG3    . GLU   A 1 373 ? 21.31368  -25.38022 16.67890  1.000 201.20820 ? 374 GLU   A HG3    1 
ATOM   5450 N N      . ALA   A 1 374 ? 20.68443  -28.41284 13.67614  1.000 128.18870 ? 375 ALA   A N      1 
ATOM   5451 C CA     . ALA   A 1 374 ? 20.58868  -29.85782 13.84656  1.000 128.92889 ? 375 ALA   A CA     1 
ATOM   5452 C C      . ALA   A 1 374 ? 21.90777  -30.53841 13.50521  1.000 137.46589 ? 375 ALA   A C      1 
ATOM   5453 O O      . ALA   A 1 374 ? 22.35712  -31.43601 14.22752  1.000 121.95546 ? 375 ALA   A O      1 
ATOM   5454 C CB     . ALA   A 1 374 ? 19.45698  -30.41137 12.98180  1.000 156.56987 ? 375 ALA   A CB     1 
ATOM   5455 H H      . ALA   A 1 374 ? 20.11469  -28.07755 13.12608  1.000 154.21691 ? 375 ALA   A H      1 
ATOM   5456 H HA     . ALA   A 1 374 ? 20.38076  -30.05327 14.77364  1.000 155.10514 ? 375 ALA   A HA     1 
ATOM   5457 H HB1    . ALA   A 1 374 ? 19.42739  -31.37594 13.07992  1.000 188.27431 ? 375 ALA   A HB1    1 
ATOM   5458 H HB2    . ALA   A 1 374 ? 18.61742  -30.02325 13.27405  1.000 188.27431 ? 375 ALA   A HB2    1 
ATOM   5459 H HB3    . ALA   A 1 374 ? 19.62446  -30.17812 12.05528  1.000 188.27431 ? 375 ALA   A HB3    1 
ATOM   5460 N N      . GLN   A 1 375 ? 22.54585  -30.12349 12.40803  1.000 143.87184 ? 376 GLN   A N      1 
ATOM   5461 C CA     . GLN   A 1 375 ? 23.83867  -30.69770 12.05100  1.000 138.05616 ? 376 GLN   A CA     1 
ATOM   5462 C C      . GLN   A 1 375 ? 24.85746  -30.48281 13.16278  1.000 142.07216 ? 376 GLN   A C      1 
ATOM   5463 O O      . GLN   A 1 375 ? 25.62290  -31.39395 13.50103  1.000 128.52502 ? 376 GLN   A O      1 
ATOM   5464 C CB     . GLN   A 1 375 ? 24.34230  -30.08999 10.74053  1.000 136.60584 ? 376 GLN   A CB     1 
ATOM   5465 C CG     . GLN   A 1 375 ? 23.49692  -30.43978 9.52554   1.000 138.35607 ? 376 GLN   A CG     1 
ATOM   5466 C CD     . GLN   A 1 375 ? 24.20854  -30.16112 8.21352   1.000 120.74319 ? 376 GLN   A CD     1 
ATOM   5467 O OE1    . GLN   A 1 375 ? 24.93148  -29.17360 8.08102   1.000 126.13020 ? 376 GLN   A OE1    1 
ATOM   5468 N NE2    . GLN   A 1 375 ? 24.01033  -31.03951 7.23677   1.000 122.65700 ? 376 GLN   A NE2    1 
ATOM   5469 H H      . GLN   A 1 375 ? 22.25596  -29.52256 11.86540  1.000 173.03667 ? 376 GLN   A H      1 
ATOM   5470 H HA     . GLN   A 1 375 ? 23.73065  -31.65225 11.91653  1.000 166.05786 ? 376 GLN   A HA     1 
ATOM   5471 H HB2    . GLN   A 1 375 ? 24.34617  -29.12395 10.82804  1.000 164.31748 ? 376 GLN   A HB2    1 
ATOM   5472 H HB3    . GLN   A 1 375 ? 25.24233  -30.41174 10.57525  1.000 164.31748 ? 376 GLN   A HB3    1 
ATOM   5473 H HG2    . GLN   A 1 375 ? 23.27912  -31.38459 9.55362   1.000 166.41775 ? 376 GLN   A HG2    1 
ATOM   5474 H HG3    . GLN   A 1 375 ? 22.68380  -29.91119 9.54366   1.000 166.41775 ? 376 GLN   A HG3    1 
ATOM   5475 H HE21   . GLN   A 1 375 ? 23.50153  -31.72041 7.36751   1.000 147.57887 ? 376 GLN   A HE21   1 
ATOM   5476 H HE22   . GLN   A 1 375 ? 24.39081  -30.92723 6.47373   1.000 147.57887 ? 376 GLN   A HE22   1 
ATOM   5477 N N      . ALA   A 1 376 ? 24.87898  -29.28155 13.74421  1.000 142.75290 ? 377 ALA   A N      1 
ATOM   5478 C CA     . ALA   A 1 376 ? 25.82459  -28.98839 14.81496  1.000 130.27704 ? 377 ALA   A CA     1 
ATOM   5479 C C      . ALA   A 1 376 ? 25.65961  -29.96422 15.97262  1.000 135.12550 ? 377 ALA   A C      1 
ATOM   5480 O O      . ALA   A 1 376 ? 26.64075  -30.52294 16.47581  1.000 134.55288 ? 377 ALA   A O      1 
ATOM   5481 C CB     . ALA   A 1 376 ? 25.63415  -27.55148 15.29823  1.000 134.61266 ? 377 ALA   A CB     1 
ATOM   5482 H H      . ALA   A 1 376 ? 24.36092  -28.62688 13.53777  1.000 171.69395 ? 377 ALA   A H      1 
ATOM   5483 H HA     . ALA   A 1 376 ? 26.72637  -29.07712 14.46882  1.000 156.72292 ? 377 ALA   A HA     1 
ATOM   5484 H HB1    . ALA   A 1 376 ? 26.44296  -27.25942 15.74703  1.000 161.92566 ? 377 ALA   A HB1    1 
ATOM   5485 H HB2    . ALA   A 1 376 ? 25.45622  -26.98203 14.53340  1.000 161.92566 ? 377 ALA   A HB2    1 
ATOM   5486 H HB3    . ALA   A 1 376 ? 24.88518  -27.52202 15.91392  1.000 161.92566 ? 377 ALA   A HB3    1 
ATOM   5487 N N      . GLU   A 1 377 ? 24.41946  -30.18029 16.41154  1.000 134.25076 ? 378 GLU   A N      1 
ATOM   5488 C CA     . GLU   A 1 377 ? 24.17747  -31.09352 17.52278  1.000 137.47503 ? 378 GLU   A CA     1 
ATOM   5489 C C      . GLU   A 1 377 ? 24.64615  -32.50426 17.18803  1.000 138.24716 ? 378 GLU   A C      1 
ATOM   5490 O O      . GLU   A 1 377 ? 25.30117  -33.16329 18.00240  1.000 132.93781 ? 378 GLU   A O      1 
ATOM   5491 C CB     . GLU   A 1 377 ? 22.69286  -31.09210 17.88336  1.000 149.54348 ? 378 GLU   A CB     1 
ATOM   5492 C CG     . GLU   A 1 377 ? 22.34217  -31.96910 19.07286  1.000 173.46713 ? 378 GLU   A CG     1 
ATOM   5493 C CD     . GLU   A 1 377 ? 20.86640  -31.90998 19.42888  1.000 193.51369 ? 378 GLU   A CD     1 
ATOM   5494 O OE1    . GLU   A 1 377 ? 20.10900  -31.21410 18.71956  1.000 208.68186 ? 378 GLU   A OE1    1 
ATOM   5495 O OE2    . GLU   A 1 377 ? 20.46335  -32.55857 20.41873  1.000 190.69792 ? 378 GLU   A OE2    1 
ATOM   5496 H H      . GLU   A 1 377 ? 23.71165  -29.81522 16.08700  1.000 161.49138 ? 378 GLU   A H      1 
ATOM   5497 H HA     . GLU   A 1 377 ? 24.67810  -30.78586 18.29454  1.000 165.36051 ? 378 GLU   A HA     1 
ATOM   5498 H HB2    . GLU   A 1 377 ? 22.42642  -30.18441 18.09787  1.000 179.84265 ? 378 GLU   A HB2    1 
ATOM   5499 H HB3    . GLU   A 1 377 ? 22.18787  -31.41459 17.12055  1.000 179.84265 ? 378 GLU   A HB3    1 
ATOM   5500 H HG2    . GLU   A 1 377 ? 22.56394  -32.88989 18.86344  1.000 208.55103 ? 378 GLU   A HG2    1 
ATOM   5501 H HG3    . GLU   A 1 377 ? 22.84944  -31.67300 19.84481  1.000 208.55103 ? 378 GLU   A HG3    1 
ATOM   5502 N N      . SER   A 1 378 ? 24.31918  -32.98588 15.98601  1.000 152.65377 ? 379 SER   A N      1 
ATOM   5503 C CA     . SER   A 1 378 ? 24.66501  -34.35685 15.62612  1.000 132.82386 ? 379 SER   A CA     1 
ATOM   5504 C C      . SER   A 1 378 ? 26.17400  -34.54113 15.53452  1.000 129.62748 ? 379 SER   A C      1 
ATOM   5505 O O      . SER   A 1 378 ? 26.70485  -35.57669 15.95340  1.000 126.38873 ? 379 SER   A O      1 
ATOM   5506 C CB     . SER   A 1 378 ? 24.00088  -34.73072 14.30402  1.000 121.42114 ? 379 SER   A CB     1 
ATOM   5507 O OG     . SER   A 1 378 ? 24.64063  -34.08144 13.22118  1.000 153.57613 ? 379 SER   A OG     1 
ATOM   5508 H H      . SER   A 1 378 ? 23.90494  -32.54626 15.37385  1.000 183.57500 ? 379 SER   A H      1 
ATOM   5509 H HA     . SER   A 1 378 ? 24.33067  -34.95416 16.31339  1.000 159.77910 ? 379 SER   A HA     1 
ATOM   5510 H HB2    . SER   A 1 378 ? 24.06355  -35.69058 14.17892  1.000 146.09584 ? 379 SER   A HB2    1 
ATOM   5511 H HB3    . SER   A 1 378 ? 23.06990  -34.45962 14.32995  1.000 146.09584 ? 379 SER   A HB3    1 
ATOM   5512 H HG     . SER   A 1 378 ? 24.79612  -33.27981 13.41818  1.000 184.68183 ? 379 SER   A HG     1 
ATOM   5513 N N      . ILE   A 1 379 ? 26.88118  -33.55453 14.98181  1.000 139.64166 ? 380 ILE   A N      1 
ATOM   5514 C CA     . ILE   A 1 379 ? 28.33567  -33.64202 14.91242  1.000 150.44134 ? 380 ILE   A CA     1 
ATOM   5515 C C      . ILE   A 1 379 ? 28.93811  -33.51179 16.30619  1.000 146.98532 ? 380 ILE   A C      1 
ATOM   5516 O O      . ILE   A 1 379 ? 29.81459  -34.29159 16.69683  1.000 138.81235 ? 380 ILE   A O      1 
ATOM   5517 C CB     . ILE   A 1 379 ? 28.89859  -32.57500 13.95791  1.000 128.30476 ? 380 ILE   A CB     1 
ATOM   5518 C CG1    . ILE   A 1 379 ? 28.44513  -32.83138 12.51963  1.000 163.80675 ? 380 ILE   A CG1    1 
ATOM   5519 C CG2    . ILE   A 1 379 ? 30.40979  -32.58547 14.01031  1.000 127.83801 ? 380 ILE   A CG2    1 
ATOM   5520 C CD1    . ILE   A 1 379 ? 29.14996  -34.00252 11.84848  1.000 173.51020 ? 380 ILE   A CD1    1 
ATOM   5521 H H      . ILE   A 1 379 ? 26.54725  -32.83672 14.64590  1.000 167.96047 ? 380 ILE   A H      1 
ATOM   5522 H HA     . ILE   A 1 379 ? 28.57303  -34.51330 14.55825  1.000 180.92008 ? 380 ILE   A HA     1 
ATOM   5523 H HB     . ILE   A 1 379 ? 28.56074  -31.71172 14.24343  1.000 154.35619 ? 380 ILE   A HB     1 
ATOM   5524 H HG12   . ILE   A 1 379 ? 27.49399  -33.02168 12.52256  1.000 196.95857 ? 380 ILE   A HG12   1 
ATOM   5525 H HG13   . ILE   A 1 379 ? 28.62304  -32.03766 11.99118  1.000 196.95857 ? 380 ILE   A HG13   1 
ATOM   5526 H HG21   . ILE   A 1 379 ? 30.75548  -32.08693 13.25344  1.000 153.79608 ? 380 ILE   A HG21   1 
ATOM   5527 H HG22   . ILE   A 1 379 ? 30.69993  -32.17260 14.83871  1.000 153.79608 ? 380 ILE   A HG22   1 
ATOM   5528 H HG23   . ILE   A 1 379 ? 30.72077  -33.50346 13.97159  1.000 153.79608 ? 380 ILE   A HG23   1 
ATOM   5529 H HD11   . ILE   A 1 379 ? 28.58457  -34.34718 11.13965  1.000 208.60270 ? 380 ILE   A HD11   1 
ATOM   5530 H HD12   . ILE   A 1 379 ? 29.99247  -33.69456 11.47938  1.000 208.60270 ? 380 ILE   A HD12   1 
ATOM   5531 H HD13   . ILE   A 1 379 ? 29.31135  -34.69445 12.50885  1.000 208.60270 ? 380 ILE   A HD13   1 
ATOM   5532 N N      . ILE   A 1 380 ? 28.47932  -32.52502 17.07792  1.000 140.89591 ? 381 ILE   A N      1 
ATOM   5533 C CA     . ILE   A 1 380 ? 29.00430  -32.34318 18.42850  1.000 154.86147 ? 381 ILE   A CA     1 
ATOM   5534 C C      . ILE   A 1 380 ? 28.79173  -33.61077 19.25029  1.000 146.43079 ? 381 ILE   A C      1 
ATOM   5535 O O      . ILE   A 1 380 ? 29.70200  -34.08435 19.93880  1.000 143.07490 ? 381 ILE   A O      1 
ATOM   5536 C CB     . ILE   A 1 380 ? 28.36110  -31.11672 19.09906  1.000 167.33569 ? 381 ILE   A CB     1 
ATOM   5537 C CG1    . ILE   A 1 380 ? 28.77110  -29.82871 18.37703  1.000 144.02634 ? 381 ILE   A CG1    1 
ATOM   5538 C CG2    . ILE   A 1 380 ? 28.76653  -31.04282 20.56628  1.000 146.95212 ? 381 ILE   A CG2    1 
ATOM   5539 C CD1    . ILE   A 1 380 ? 27.93109  -28.61552 18.74842  1.000 144.15280 ? 381 ILE   A CD1    1 
ATOM   5540 H H      . ILE   A 1 380 ? 27.87543  -31.95805 16.84671  1.000 169.46556 ? 381 ILE   A H      1 
ATOM   5541 H HA     . ILE   A 1 380 ? 29.95869  -32.18020 18.36952  1.000 186.22424 ? 381 ILE   A HA     1 
ATOM   5542 H HB     . ILE   A 1 380 ? 27.39756  -31.21186 19.04029  1.000 201.19330 ? 381 ILE   A HB     1 
ATOM   5543 H HG12   . ILE   A 1 380 ? 29.69362  -29.62787 18.59957  1.000 173.22207 ? 381 ILE   A HG12   1 
ATOM   5544 H HG13   . ILE   A 1 380 ? 28.68297  -29.96685 17.42097  1.000 173.22207 ? 381 ILE   A HG13   1 
ATOM   5545 H HG21   . ILE   A 1 380 ? 28.53307  -30.16820 20.91476  1.000 176.73301 ? 381 ILE   A HG21   1 
ATOM   5546 H HG22   . ILE   A 1 380 ? 28.29469  -31.73209 21.05940  1.000 176.73301 ? 381 ILE   A HG22   1 
ATOM   5547 H HG23   . ILE   A 1 380 ? 29.72386  -31.18223 20.63678  1.000 176.73301 ? 381 ILE   A HG23   1 
ATOM   5548 H HD11   . ILE   A 1 380 ? 28.18489  -27.87024 18.18181  1.000 173.37383 ? 381 ILE   A HD11   1 
ATOM   5549 H HD12   . ILE   A 1 380 ? 26.99392  -28.82772 18.61578  1.000 173.37383 ? 381 ILE   A HD12   1 
ATOM   5550 H HD13   . ILE   A 1 380 ? 28.09143  -28.39324 19.67889  1.000 173.37383 ? 381 ILE   A HD13   1 
ATOM   5551 N N      . ASN   A 1 381 ? 27.58309  -34.17951 19.18882  1.000 148.58989 ? 382 ASN   A N      1 
ATOM   5552 C CA     . ASN   A 1 381 ? 27.31955  -35.42498 19.90485  1.000 158.62920 ? 382 ASN   A CA     1 
ATOM   5553 C C      . ASN   A 1 381 ? 28.17151  -36.56215 19.36258  1.000 148.74181 ? 382 ASN   A C      1 
ATOM   5554 O O      . ASN   A 1 381 ? 28.61153  -37.43576 20.11970  1.000 129.51528 ? 382 ASN   A O      1 
ATOM   5555 C CB     . ASN   A 1 381 ? 25.83691  -35.78237 19.81831  1.000 149.85460 ? 382 ASN   A CB     1 
ATOM   5556 C CG     . ASN   A 1 381 ? 24.99785  -35.01638 20.81710  1.000 170.65531 ? 382 ASN   A CG     1 
ATOM   5557 O OD1    . ASN   A 1 381 ? 24.14032  -34.21838 20.44119  1.000 189.42605 ? 382 ASN   A OD1    1 
ATOM   5558 N ND2    . ASN   A 1 381 ? 25.24427  -35.25306 22.10247  1.000 184.90416 ? 382 ASN   A ND2    1 
ATOM   5559 H H      . ASN   A 1 381 ? 26.91321  -33.86908 18.74780  1.000 178.69833 ? 382 ASN   A H      1 
ATOM   5560 H HA     . ASN   A 1 381 ? 27.54292  -35.29731 20.84010  1.000 190.74551 ? 382 ASN   A HA     1 
ATOM   5561 H HB2    . ASN   A 1 381 ? 25.51169  -35.57325 18.92871  1.000 180.21598 ? 382 ASN   A HB2    1 
ATOM   5562 H HB3    . ASN   A 1 381 ? 25.72803  -36.72949 19.99721  1.000 180.21598 ? 382 ASN   A HB3    1 
ATOM   5563 H HD21   . ASN   A 1 381 ? 24.79398  -34.84250 22.70933  1.000 222.27546 ? 382 ASN   A HD21   1 
ATOM   5564 H HD22   . ASN   A 1 381 ? 25.85391  -35.81665 22.32675  1.000 222.27546 ? 382 ASN   A HD22   1 
ATOM   5565 N N      . GLU   A 1 382 ? 28.40770  -36.57557 18.04865  1.000 141.21001 ? 383 GLU   A N      1 
ATOM   5566 C CA     . GLU   A 1 382 ? 29.28850  -37.57731 17.45969  1.000 142.79549 ? 383 GLU   A CA     1 
ATOM   5567 C C      . GLU   A 1 382 ? 30.68301  -37.49100 18.06839  1.000 147.06163 ? 383 GLU   A C      1 
ATOM   5568 O O      . GLU   A 1 382 ? 31.20560  -38.47324 18.60728  1.000 143.92843 ? 383 GLU   A O      1 
ATOM   5569 C CB     . GLU   A 1 382 ? 29.33963  -37.38885 15.94332  1.000 142.80646 ? 383 GLU   A CB     1 
ATOM   5570 C CG     . GLU   A 1 382 ? 30.26340  -38.34264 15.21008  1.000 142.69361 ? 383 GLU   A CG     1 
ATOM   5571 C CD     . GLU   A 1 382 ? 30.35129  -38.01872 13.73261  1.000 146.77802 ? 383 GLU   A CD     1 
ATOM   5572 O OE1    . GLU   A 1 382 ? 30.74124  -36.87929 13.40116  1.000 156.96480 ? 383 GLU   A OE1    1 
ATOM   5573 O OE2    . GLU   A 1 382 ? 30.01880  -38.89349 12.90508  1.000 140.41288 ? 383 GLU   A OE2    1 
ATOM   5574 H H      . GLU   A 1 382 ? 28.07239  -36.02011 17.48418  1.000 169.84248 ? 383 GLU   A H      1 
ATOM   5575 H HA     . GLU   A 1 382 ? 28.93515  -38.46238 17.64050  1.000 171.74506 ? 383 GLU   A HA     1 
ATOM   5576 H HB2    . GLU   A 1 382 ? 28.44647  -37.51780 15.58761  1.000 171.75822 ? 383 GLU   A HB2    1 
ATOM   5577 H HB3    . GLU   A 1 382 ? 29.64432  -36.48718 15.75609  1.000 171.75822 ? 383 GLU   A HB3    1 
ATOM   5578 H HG2    . GLU   A 1 382 ? 31.15425  -38.27893 15.58852  1.000 171.62280 ? 383 GLU   A HG2    1 
ATOM   5579 H HG3    . GLU   A 1 382 ? 29.92737  -39.24780 15.30313  1.000 171.62280 ? 383 GLU   A HG3    1 
ATOM   5580 N N      . THR   A 1 383 ? 31.29807  -36.30554 17.99711  1.000 146.06242 ? 384 THR   A N      1 
ATOM   5581 C CA     . THR   A 1 383 ? 32.61916  -36.10992 18.58593  1.000 147.58388 ? 384 THR   A CA     1 
ATOM   5582 C C      . THR   A 1 383 ? 32.60901  -36.44099 20.07234  1.000 141.10504 ? 384 THR   A C      1 
ATOM   5583 O O      . THR   A 1 383 ? 33.55796  -37.03845 20.59441  1.000 139.40443 ? 384 THR   A O      1 
ATOM   5584 C CB     . THR   A 1 383 ? 33.07526  -34.66557 18.36395  1.000 136.62839 ? 384 THR   A CB     1 
ATOM   5585 O OG1    . THR   A 1 383 ? 33.01754  -34.34865 16.96745  1.000 163.08562 ? 384 THR   A OG1    1 
ATOM   5586 C CG2    . THR   A 1 383 ? 34.49210  -34.46259 18.85799  1.000 144.11345 ? 384 THR   A CG2    1 
ATOM   5587 H H      . THR   A 1 383 ? 30.97278  -35.60644 17.61626  1.000 175.66537 ? 384 THR   A H      1 
ATOM   5588 H HA     . THR   A 1 383 ? 33.25240  -36.70033 18.14852  1.000 177.49113 ? 384 THR   A HA     1 
ATOM   5589 H HB     . THR   A 1 383 ? 32.49072  -34.07062 18.85918  1.000 164.34454 ? 384 THR   A HB     1 
ATOM   5590 H HG1    . THR   A 1 383 ? 32.22060  -34.36279 16.70234  1.000 196.09321 ? 384 THR   A HG1    1 
ATOM   5591 H HG21   . THR   A 1 383 ? 34.79764  -33.57017 18.63186  1.000 173.32661 ? 384 THR   A HG21   1 
ATOM   5592 H HG22   . THR   A 1 383 ? 34.52656  -34.57251 19.82112  1.000 173.32661 ? 384 THR   A HG22   1 
ATOM   5593 H HG23   . THR   A 1 383 ? 35.08339  -35.11166 18.44571  1.000 173.32661 ? 384 THR   A HG23   1 
ATOM   5594 N N      . GLU   A 1 384 ? 31.53289  -36.06933 20.76576  1.000 143.82099 ? 385 GLU   A N      1 
ATOM   5595 C CA     . GLU   A 1 384 ? 31.45392  -36.28890 22.20484  1.000 140.97461 ? 385 GLU   A CA     1 
ATOM   5596 C C      . GLU   A 1 384 ? 31.32968  -37.76987 22.53591  1.000 146.41508 ? 385 GLU   A C      1 
ATOM   5597 O O      . GLU   A 1 384 ? 31.92629  -38.24607 23.50882  1.000 148.75282 ? 385 GLU   A O      1 
ATOM   5598 C CB     . GLU   A 1 384 ? 30.26983  -35.50337 22.76765  1.000 140.82131 ? 385 GLU   A CB     1 
ATOM   5599 C CG     . GLU   A 1 384 ? 29.93077  -35.79097 24.21761  1.000 148.88133 ? 385 GLU   A CG     1 
ATOM   5600 C CD     . GLU   A 1 384 ? 28.86448  -34.85330 24.74215  1.000 151.85106 ? 385 GLU   A CD     1 
ATOM   5601 O OE1    . GLU   A 1 384 ? 28.45737  -33.95021 23.98208  1.000 146.75615 ? 385 GLU   A OE1    1 
ATOM   5602 O OE2    . GLU   A 1 384 ? 28.43395  -35.01654 25.90341  1.000 188.53904 ? 385 GLU   A OE2    1 
ATOM   5603 H H      . GLU   A 1 384 ? 30.83911  -35.69008 20.42746  1.000 172.97566 ? 385 GLU   A H      1 
ATOM   5604 H HA     . GLU   A 1 384 ? 32.26609  -35.96522 22.62497  1.000 169.56001 ? 385 GLU   A HA     1 
ATOM   5605 H HB2    . GLU   A 1 384 ? 30.47088  -34.55687 22.69969  1.000 169.37604 ? 385 GLU   A HB2    1 
ATOM   5606 H HB3    . GLU   A 1 384 ? 29.48416  -35.71441 22.23936  1.000 169.37604 ? 385 GLU   A HB3    1 
ATOM   5607 H HG2    . GLU   A 1 384 ? 29.60093  -36.69991 24.29467  1.000 179.04806 ? 385 GLU   A HG2    1 
ATOM   5608 H HG3    . GLU   A 1 384 ? 30.72702  -35.67985 24.76032  1.000 179.04806 ? 385 GLU   A HG3    1 
ATOM   5609 N N      . MET   A 1 385 ? 30.56827  -38.51685 21.73418  1.000 147.90945 ? 386 MET   A N      1 
ATOM   5610 C CA     . MET   A 1 385 ? 30.31052  -39.91691 22.05646  1.000 158.57808 ? 386 MET   A CA     1 
ATOM   5611 C C      . MET   A 1 385 ? 31.54436  -40.77824 21.82797  1.000 152.44889 ? 386 MET   A C      1 
ATOM   5612 O O      . MET   A 1 385 ? 31.88374  -41.62211 22.66660  1.000 134.40820 ? 386 MET   A O      1 
ATOM   5613 C CB     . MET   A 1 385 ? 29.13147  -40.42936 21.22990  1.000 152.27773 ? 386 MET   A CB     1 
ATOM   5614 C CG     . MET   A 1 385 ? 27.79598  -40.26748 21.93433  1.000 161.44058 ? 386 MET   A CG     1 
ATOM   5615 S SD     . MET   A 1 385 ? 26.39888  -40.20455 20.80220  1.000 135.28621 ? 386 MET   A SD     1 
ATOM   5616 C CE     . MET   A 1 385 ? 26.44521  -41.85646 20.11450  1.000 157.13807 ? 386 MET   A CE     1 
ATOM   5617 H H      . MET   A 1 385 ? 30.19577  -38.24066 21.00991  1.000 177.88182 ? 386 MET   A H      1 
ATOM   5618 H HA     . MET   A 1 385 ? 30.06660  -39.97806 22.99329  1.000 190.68417 ? 386 MET   A HA     1 
ATOM   5619 H HB2    . MET   A 1 385 ? 29.09230  -39.93370 20.39702  1.000 183.12375 ? 386 MET   A HB2    1 
ATOM   5620 H HB3    . MET   A 1 385 ? 29.26137  -41.37333 21.04839  1.000 183.12375 ? 386 MET   A HB3    1 
ATOM   5621 H HG2    . MET   A 1 385 ? 27.66220  -41.02046 22.53101  1.000 194.11916 ? 386 MET   A HG2    1 
ATOM   5622 H HG3    . MET   A 1 385 ? 27.80627  -39.44041 22.44104  1.000 194.11916 ? 386 MET   A HG3    1 
ATOM   5623 H HE1    . MET   A 1 385 ? 25.73767  -41.94471 19.45685  1.000 188.95615 ? 386 MET   A HE1    1 
ATOM   5624 H HE2    . MET   A 1 385 ? 27.30749  -41.99935 19.69384  1.000 188.95615 ? 386 MET   A HE2    1 
ATOM   5625 H HE3    . MET   A 1 385 ? 26.31499  -42.49967 20.82879  1.000 188.95615 ? 386 MET   A HE3    1 
ATOM   5626 N N      . PHE   A 1 386 ? 32.23173  -40.57696 20.70897  1.000 161.75908 ? 387 PHE   A N      1 
ATOM   5627 C CA     . PHE   A 1 386 ? 33.39591  -41.37555 20.35814  1.000 172.69420 ? 387 PHE   A CA     1 
ATOM   5628 C C      . PHE   A 1 386 ? 34.68902  -40.82425 20.94560  1.000 173.85047 ? 387 PHE   A C      1 
ATOM   5629 O O      . PHE   A 1 386 ? 35.77210  -41.28539 20.57061  1.000 176.64405 ? 387 PHE   A O      1 
ATOM   5630 C CB     . PHE   A 1 386 ? 33.50359  -41.48728 18.83667  1.000 148.70885 ? 387 PHE   A CB     1 
ATOM   5631 C CG     . PHE   A 1 386 ? 32.34200  -42.19952 18.20761  1.000 146.00045 ? 387 PHE   A CG     1 
ATOM   5632 C CD1    . PHE   A 1 386 ? 32.30906  -43.58374 18.15207  1.000 144.35031 ? 387 PHE   A CD1    1 
ATOM   5633 C CD2    . PHE   A 1 386 ? 31.27452  -41.48730 17.68822  1.000 143.08835 ? 387 PHE   A CD2    1 
ATOM   5634 C CE1    . PHE   A 1 386 ? 31.23603  -44.24448 17.58062  1.000 135.68547 ? 387 PHE   A CE1    1 
ATOM   5635 C CE2    . PHE   A 1 386 ? 30.19920  -42.14154 17.11439  1.000 153.12125 ? 387 PHE   A CE2    1 
ATOM   5636 C CZ     . PHE   A 1 386 ? 30.17970  -43.52193 17.06149  1.000 132.18531 ? 387 PHE   A CZ     1 
ATOM   5637 H H      . PHE   A 1 386 ? 32.03843  -39.97287 20.12819  1.000 194.50136 ? 387 PHE   A H      1 
ATOM   5638 H HA     . PHE   A 1 386 ? 33.28157  -42.27127 20.71244  1.000 207.62352 ? 387 PHE   A HA     1 
ATOM   5639 H HB2    . PHE   A 1 386 ? 33.54517  -40.59471 18.45920  1.000 178.84109 ? 387 PHE   A HB2    1 
ATOM   5640 H HB3    . PHE   A 1 386 ? 34.30970  -41.97914 18.61496  1.000 178.84109 ? 387 PHE   A HB3    1 
ATOM   5641 H HD1    . PHE   A 1 386 ? 33.01672  -44.07455 18.50311  1.000 173.61084 ? 387 PHE   A HD1    1 
ATOM   5642 H HD2    . PHE   A 1 386 ? 31.28040  -40.55807 17.72553  1.000 172.09650 ? 387 PHE   A HD2    1 
ATOM   5643 H HE1    . PHE   A 1 386 ? 31.22615  -45.17379 17.54616  1.000 163.21304 ? 387 PHE   A HE1    1 
ATOM   5644 H HE2    . PHE   A 1 386 ? 29.48983  -41.65245 16.76442  1.000 184.13597 ? 387 PHE   A HE2    1 
ATOM   5645 H HZ     . PHE   A 1 386 ? 29.45702  -43.96353 16.67726  1.000 159.01285 ? 387 PHE   A HZ     1 
ATOM   5646 N N      . SER   A 1 387 ? 34.60263  -39.85769 21.85521  1.000 155.81705 ? 388 SER   A N      1 
ATOM   5647 C CA     . SER   A 1 387 ? 35.78049  -39.42122 22.58532  1.000 168.40879 ? 388 SER   A CA     1 
ATOM   5648 C C      . SER   A 1 387 ? 36.18168  -40.48497 23.60422  1.000 184.55949 ? 388 SER   A C      1 
ATOM   5649 O O      . SER   A 1 387 ? 35.37948  -41.33001 24.01066  1.000 178.84241 ? 388 SER   A O      1 
ATOM   5650 C CB     . SER   A 1 387 ? 35.51886  -38.08961 23.28583  1.000 181.61099 ? 388 SER   A CB     1 
ATOM   5651 O OG     . SER   A 1 387 ? 36.69039  -37.61595 23.92813  1.000 192.41401 ? 388 SER   A OG     1 
ATOM   5652 H H      . SER   A 1 387 ? 33.87838  -39.44379 22.06438  1.000 187.37093 ? 388 SER   A H      1 
ATOM   5653 H HA     . SER   A 1 387 ? 36.51839  -39.28763 21.97005  1.000 202.48102 ? 388 SER   A HA     1 
ATOM   5654 H HB2    . SER   A 1 387 ? 35.23485  -37.43706 22.62673  1.000 218.32366 ? 388 SER   A HB2    1 
ATOM   5655 H HB3    . SER   A 1 387 ? 34.82336  -38.21423 23.95039  1.000 218.32366 ? 388 SER   A HB3    1 
ATOM   5656 H HG     . SER   A 1 387 ? 37.30432  -37.51045 23.36460  1.000 231.28728 ? 388 SER   A HG     1 
ATOM   5657 N N      . SER   A 1 388 ? 37.44853  -40.43610 24.01947  1.000 196.06421 ? 389 SER   A N      1 
ATOM   5658 C CA     . SER   A 1 388 ? 37.97401  -41.46536 24.90933  1.000 187.72268 ? 389 SER   A CA     1 
ATOM   5659 C C      . SER   A 1 388 ? 37.36814  -41.39903 26.30684  1.000 177.97186 ? 389 SER   A C      1 
ATOM   5660 O O      . SER   A 1 388 ? 37.35338  -42.41333 27.01359  1.000 179.61665 ? 389 SER   A O      1 
ATOM   5661 C CB     . SER   A 1 388 ? 39.49819  -41.34703 24.99987  1.000 193.56981 ? 389 SER   A CB     1 
ATOM   5662 O OG     . SER   A 1 388 ? 40.09976  -41.48202 23.72337  1.000 182.86165 ? 389 SER   A OG     1 
ATOM   5663 H H      . SER   A 1 388 ? 38.01439  -39.82586 23.80264  1.000 235.66752 ? 389 SER   A H      1 
ATOM   5664 H HA     . SER   A 1 388 ? 37.75731  -42.33410 24.53620  1.000 225.65768 ? 389 SER   A HA     1 
ATOM   5665 H HB2    . SER   A 1 388 ? 39.72483  -40.47688 25.36370  1.000 232.67424 ? 389 SER   A HB2    1 
ATOM   5666 H HB3    . SER   A 1 388 ? 39.83383  -42.04731 25.58114  1.000 232.67424 ? 389 SER   A HB3    1 
ATOM   5667 H HG     . SER   A 1 388 ? 40.93642  -41.47555 23.79792  1.000 219.82445 ? 389 SER   A HG     1 
ATOM   5668 N N      . ASP   A 1 389 ? 36.86955  -40.23819 26.72075  1.000 176.56154 ? 390 ASP   A N      1 
ATOM   5669 C CA     . ASP   A 1 389 ? 36.36867  -40.04040 28.07305  1.000 182.60511 ? 390 ASP   A CA     1 
ATOM   5670 C C      . ASP   A 1 389 ? 34.85893  -40.21120 28.18708  1.000 183.24627 ? 390 ASP   A C      1 
ATOM   5671 O O      . ASP   A 1 389 ? 34.31748  -40.07851 29.28883  1.000 178.06845 ? 390 ASP   A O      1 
ATOM   5672 C CB     . ASP   A 1 389 ? 36.76095  -38.64268 28.56949  1.000 192.44838 ? 390 ASP   A CB     1 
ATOM   5673 C CG     . ASP   A 1 389 ? 36.58137  -38.47780 30.06568  1.000 210.16224 ? 390 ASP   A CG     1 
ATOM   5674 O OD1    . ASP   A 1 389 ? 36.42275  -39.49891 30.76575  1.000 230.03577 ? 390 ASP   A OD1    1 
ATOM   5675 O OD2    . ASP   A 1 389 ? 36.59697  -37.32316 30.54125  1.000 207.08536 ? 390 ASP   A OD2    1 
ATOM   5676 H H      . ASP   A 1 389 ? 36.81040  -39.53760 26.22549  1.000 212.26432 ? 390 ASP   A H      1 
ATOM   5677 H HA     . ASP   A 1 389 ? 36.78098  -40.70003 28.65252  1.000 219.51661 ? 390 ASP   A HA     1 
ATOM   5678 H HB2    . ASP   A 1 389 ? 37.69477  -38.48392 28.36053  1.000 231.32853 ? 390 ASP   A HB2    1 
ATOM   5679 H HB3    . ASP   A 1 389 ? 36.20501  -37.98268 28.12650  1.000 231.32853 ? 390 ASP   A HB3    1 
ATOM   5680 N N      . PHE   A 1 390 ? 34.16823  -40.50940 27.08989  1.000 186.20189 ? 391 PHE   A N      1 
ATOM   5681 C CA     . PHE   A 1 390 ? 32.71191  -40.50089 27.10498  1.000 174.58148 ? 391 PHE   A CA     1 
ATOM   5682 C C      . PHE   A 1 390 ? 32.16283  -41.59387 28.01360  1.000 165.30967 ? 391 PHE   A C      1 
ATOM   5683 O O      . PHE   A 1 390 ? 32.68799  -42.70795 28.06723  1.000 159.17323 ? 391 PHE   A O      1 
ATOM   5684 C CB     . PHE   A 1 390 ? 32.16602  -40.67974 25.69061  1.000 173.13613 ? 391 PHE   A CB     1 
ATOM   5685 C CG     . PHE   A 1 390 ? 30.67046  -40.61370 25.61093  1.000 165.78890 ? 391 PHE   A CG     1 
ATOM   5686 C CD1    . PHE   A 1 390 ? 30.01184  -39.40603 25.76589  1.000 168.77427 ? 391 PHE   A CD1    1 
ATOM   5687 C CD2    . PHE   A 1 390 ? 29.92223  -41.75594 25.38051  1.000 163.78595 ? 391 PHE   A CD2    1 
ATOM   5688 C CE1    . PHE   A 1 390 ? 28.63511  -39.33745 25.69437  1.000 161.94105 ? 391 PHE   A CE1    1 
ATOM   5689 C CE2    . PHE   A 1 390 ? 28.54402  -41.69403 25.30681  1.000 160.66440 ? 391 PHE   A CE2    1 
ATOM   5690 C CZ     . PHE   A 1 390 ? 27.89998  -40.48252 25.46320  1.000 163.12154 ? 391 PHE   A CZ     1 
ATOM   5691 H H      . PHE   A 1 390 ? 34.51674  -40.71791 26.33183  1.000 223.83273 ? 391 PHE   A H      1 
ATOM   5692 H HA     . PHE   A 1 390 ? 32.40764  -39.64612 27.44804  1.000 209.88825 ? 391 PHE   A HA     1 
ATOM   5693 H HB2    . PHE   A 1 390 ? 32.52443  -39.97693 25.12625  1.000 208.15383 ? 391 PHE   A HB2    1 
ATOM   5694 H HB3    . PHE   A 1 390 ? 32.44282  -41.54723 25.35632  1.000 208.15383 ? 391 PHE   A HB3    1 
ATOM   5695 H HD1    . PHE   A 1 390 ? 30.50294  -38.63147 25.92006  1.000 202.91959 ? 391 PHE   A HD1    1 
ATOM   5696 H HD2    . PHE   A 1 390 ? 30.35220  -42.57370 25.27422  1.000 196.93362 ? 391 PHE   A HD2    1 
ATOM   5697 H HE1    . PHE   A 1 390 ? 28.20340  -38.52076 25.80181  1.000 194.71973 ? 391 PHE   A HE1    1 
ATOM   5698 H HE2    . PHE   A 1 390 ? 28.05074  -42.46710 25.15209  1.000 193.18775 ? 391 PHE   A HE2    1 
ATOM   5699 H HZ     . PHE   A 1 390 ? 26.97240  -40.43824 25.41285  1.000 196.13631 ? 391 PHE   A HZ     1 
ATOM   5700 N N      . SER   A 1 391 ? 31.07922  -41.26498 28.72804  1.000 166.67735 ? 392 SER   A N      1 
ATOM   5701 C CA     . SER   A 1 391 ? 30.46150  -42.20283 29.66116  1.000 171.32587 ? 392 SER   A CA     1 
ATOM   5702 C C      . SER   A 1 391 ? 28.96614  -41.92466 29.79286  1.000 176.01992 ? 392 SER   A C      1 
ATOM   5703 O O      . SER   A 1 391 ? 28.39474  -42.09584 30.87829  1.000 185.25669 ? 392 SER   A O      1 
ATOM   5704 C CB     . SER   A 1 391 ? 31.14067  -42.14125 31.03327  1.000 169.30473 ? 392 SER   A CB     1 
ATOM   5705 O OG     . SER   A 1 391 ? 30.56610  -43.07994 31.92684  1.000 178.18268 ? 392 SER   A OG     1 
ATOM   5706 H H      . SER   A 1 391 ? 30.68446  -40.50200 28.68777  1.000 200.40329 ? 392 SER   A H      1 
ATOM   5707 H HA     . SER   A 1 391 ? 30.57223  -43.10744 29.32899  1.000 205.98151 ? 392 SER   A HA     1 
ATOM   5708 H HB2    . SER   A 1 391 ? 32.08355  -42.34300 30.92757  1.000 203.55615 ? 392 SER   A HB2    1 
ATOM   5709 H HB3    . SER   A 1 391 ? 31.03118  -41.24970 31.39941  1.000 203.55615 ? 392 SER   A HB3    1 
ATOM   5710 H HG     . SER   A 1 391 ? 29.74424  -42.92901 32.01273  1.000 214.20969 ? 392 SER   A HG     1 
ATOM   5711 N N      . PHE   A 1 392 ? 28.32810  -41.50478 28.70951  1.000 165.50431 ? 393 PHE   A N      1 
ATOM   5712 C CA     . PHE   A 1 392 ? 26.89708  -41.21202 28.71365  1.000 154.40370 ? 393 PHE   A CA     1 
ATOM   5713 C C      . PHE   A 1 392 ? 26.49042  -40.36830 29.92214  1.000 163.78074 ? 393 PHE   A C      1 
ATOM   5714 O O      . PHE   A 1 392 ? 25.49764  -39.63941 29.88123  1.000 157.06025 ? 393 PHE   A O      1 
ATOM   5715 C CB     . PHE   A 1 392 ? 26.08558  -42.51236 28.69053  1.000 140.25452 ? 393 PHE   A CB     1 
ATOM   5716 C CG     . PHE   A 1 392 ? 26.03943  -43.17772 27.34251  1.000 160.10661 ? 393 PHE   A CG     1 
ATOM   5717 C CD1    . PHE   A 1 392 ? 25.35425  -42.59073 26.29124  1.000 180.42300 ? 393 PHE   A CD1    1 
ATOM   5718 C CD2    . PHE   A 1 392 ? 26.66739  -44.39461 27.12780  1.000 178.73408 ? 393 PHE   A CD2    1 
ATOM   5719 C CE1    . PHE   A 1 392 ? 25.30287  -43.19881 25.04779  1.000 158.01198 ? 393 PHE   A CE1    1 
ATOM   5720 C CE2    . PHE   A 1 392 ? 26.61908  -45.00944 25.88357  1.000 171.95118 ? 393 PHE   A CE2    1 
ATOM   5721 C CZ     . PHE   A 1 392 ? 25.93477  -44.40972 24.84442  1.000 139.28923 ? 393 PHE   A CZ     1 
ATOM   5722 H H      . PHE   A 1 392 ? 28.70456  -41.37868 27.94664  1.000 198.99564 ? 393 PHE   A H      1 
ATOM   5723 H HA     . PHE   A 1 392 ? 26.68745  -40.70123 27.91612  1.000 185.67491 ? 393 PHE   A HA     1 
ATOM   5724 H HB2    . PHE   A 1 392 ? 26.48304  -43.13857 29.31566  1.000 168.69589 ? 393 PHE   A HB2    1 
ATOM   5725 H HB3    . PHE   A 1 392 ? 25.17318  -42.31470 28.95386  1.000 168.69589 ? 393 PHE   A HB3    1 
ATOM   5726 H HD1    . PHE   A 1 392 ? 24.92288  -41.77730 26.42218  1.000 216.89807 ? 393 PHE   A HD1    1 
ATOM   5727 H HD2    . PHE   A 1 392 ? 27.12648  -44.80416 27.82522  1.000 214.87137 ? 393 PHE   A HD2    1 
ATOM   5728 H HE1    . PHE   A 1 392 ? 24.84274  -42.79150 24.34973  1.000 190.00485 ? 393 PHE   A HE1    1 
ATOM   5729 H HE2    . PHE   A 1 392 ? 27.04710  -45.82423 25.75012  1.000 206.73189 ? 393 PHE   A HE2    1 
ATOM   5730 H HZ     . PHE   A 1 392 ? 25.89968  -44.82005 24.01058  1.000 167.53755 ? 393 PHE   A HZ     1 
HETATM 5731 C C1     . A1BDP B 2 .   ? 20.13327  -47.09073 17.31886  1.000 166.57896 ? 401 A1BDP A C1     1 
HETATM 5732 C C2     . A1BDP B 2 .   ? 21.02281  -47.94732 16.54848  1.000 166.01631 ? 401 A1BDP A C2     1 
HETATM 5733 C C3     . A1BDP B 2 .   ? 22.13186  -47.36843 15.99874  1.000 160.09628 ? 401 A1BDP A C3     1 
HETATM 5734 C C4     . A1BDP B 2 .   ? 22.56285  -45.94137 16.30792  1.000 157.75524 ? 401 A1BDP A C4     1 
HETATM 5735 C C5     . A1BDP B 2 .   ? 21.69701  -44.58703 18.24779  1.000 154.63375 ? 401 A1BDP A C5     1 
HETATM 5736 C C6     . A1BDP B 2 .   ? 21.23979  -42.36054 19.32643  1.000 161.30314 ? 401 A1BDP A C6     1 
HETATM 5737 O O1     . A1BDP B 2 .   ? 19.51994  -47.42066 18.31213  1.000 152.62292 ? 401 A1BDP A O1     1 
HETATM 5738 C C10    . A1BDP B 2 .   ? 18.02102  -40.42412 19.57620  1.000 176.03436 ? 401 A1BDP A C10    1 
HETATM 5739 C C11    . A1BDP B 2 .   ? 18.55911  -42.61105 18.54342  1.000 170.84745 ? 401 A1BDP A C11    1 
HETATM 5740 C C12    . A1BDP B 2 .   ? 18.98053  -44.78345 17.49699  1.000 164.55105 ? 401 A1BDP A C12    1 
HETATM 5741 C C13    . A1BDP B 2 .   ? 15.59051  -40.06358 19.93317  1.000 194.34131 ? 401 A1BDP A C13    1 
HETATM 5742 C C15    . A1BDP B 2 .   ? 14.94990  -38.57508 19.87160  1.000 197.54434 ? 401 A1BDP A C15    1 
HETATM 5743 C C17    . A1BDP B 2 .   ? 14.65584  -36.52930 18.74441  1.000 169.11298 ? 401 A1BDP A C17    1 
HETATM 5744 C C18    . A1BDP B 2 .   ? 13.83607  -36.02040 19.76067  1.000 193.05815 ? 401 A1BDP A C18    1 
HETATM 5745 C C19    . A1BDP B 2 .   ? 13.61388  -36.89074 20.84134  1.000 195.37323 ? 401 A1BDP A C19    1 
HETATM 5746 C C1A    . A1BDP B 2 .   ? 18.95714  -41.44879 19.25687  1.000 167.82719 ? 401 A1BDP A C1A    1 
HETATM 5747 C C1B    . A1BDP B 2 .   ? 19.45843  -43.60731 18.23205  1.000 171.67229 ? 401 A1BDP A C1B    1 
HETATM 5748 C C1C    . A1BDP B 2 .   ? 20.01179  -45.67242 16.79427  1.000 167.26430 ? 401 A1BDP A C1C    1 
HETATM 5749 C C21    . A1BDP B 2 .   ? 20.74526  -49.38567 16.37786  1.000 151.14790 ? 401 A1BDP A C21    1 
HETATM 5750 C C41    . A1BDP B 2 .   ? 21.40693  -45.04107 16.81458  1.000 162.39923 ? 401 A1BDP A C41    1 
HETATM 5751 C C42    . A1BDP B 2 .   ? 23.06202  -45.84838 13.84260  1.000 132.69409 ? 401 A1BDP A C42    1 
HETATM 5752 C C43    . A1BDP B 2 .   ? 24.66389  -44.78674 15.37010  1.000 132.76102 ? 401 A1BDP A C43    1 
HETATM 5753 C C51    . A1BDP B 2 .   ? 20.80490  -43.47826 18.63726  1.000 171.78216 ? 401 A1BDP A C51    1 
HETATM 5754 C C61    . A1BDP B 2 .   ? 20.29923  -41.31597 19.65254  1.000 160.49609 ? 401 A1BDP A C61    1 
HETATM 5755 C C62    . A1BDP B 2 .   ? 22.67361  -42.20546 19.75638  1.000 146.39297 ? 401 A1BDP A C62    1 
HETATM 5756 C C7     . A1BDP B 2 .   ? 20.66463  -40.14458 20.36083  1.000 153.59612 ? 401 A1BDP A C7     1 
HETATM 5757 C C8     . A1BDP B 2 .   ? 19.74634  -39.17360 20.65455  1.000 164.14658 ? 401 A1BDP A C8     1 
HETATM 5758 C C9     . A1BDP B 2 .   ? 18.41235  -39.30375 20.26302  1.000 171.87992 ? 401 A1BDP A C9     1 
HETATM 5759 N N16    . A1BDP B 2 .   ? 15.20932  -37.78207 18.78392  1.000 182.06068 ? 401 A1BDP A N16    1 
HETATM 5760 N N20    . A1BDP B 2 .   ? 14.14658  -38.14975 20.92127  1.000 201.54233 ? 401 A1BDP A N20    1 
HETATM 5761 N N21    . A1BDP B 2 .   ? 20.05346  -50.00579 17.38208  1.000 130.65910 ? 401 A1BDP A N21    1 
HETATM 5762 N N4     . A1BDP B 2 .   ? 23.27538  -45.26838 15.18990  1.000 131.10932 ? 401 A1BDP A N4     1 
HETATM 5763 O O10    . A1BDP B 2 .   ? 16.70719  -40.49372 19.21960  1.000 183.68511 ? 401 A1BDP A O10    1 
HETATM 5764 O O11    . A1BDP B 2 .   ? 17.25741  -42.67149 18.20178  1.000 165.37497 ? 401 A1BDP A O11    1 
HETATM 5765 O O12    . A1BDP B 2 .   ? 17.80034  -45.08414 17.41714  1.000 167.44793 ? 401 A1BDP A O12    1 
HETATM 5766 O O14    . A1BDP B 2 .   ? 15.09160  -40.92154 20.62972  1.000 192.34717 ? 401 A1BDP A O14    1 
HETATM 5767 O O1C    . A1BDP B 2 .   ? 19.55430  -45.79230 15.49380  1.000 155.69685 ? 401 A1BDP A O1C    1 
HETATM 5768 O O21    . A1BDP B 2 .   ? 21.12020  -50.01472 15.37621  1.000 150.12141 ? 401 A1BDP A O21    1 
HETATM 5769 O O3     . A1BDP B 2 .   ? 23.19979  -48.15147 15.85681  1.000 147.46989 ? 401 A1BDP A O3     1 
HETATM 5770 H H4     . A1BDP B 2 .   ? 23.29688  -46.07625 17.16304  1.000 189.69675 ? 401 A1BDP A H4     1 
HETATM 5771 H H5C1   . A1BDP B 2 .   ? 21.58737  -45.43441 18.96258  1.000 185.95098 ? 401 A1BDP A H5C1   1 
HETATM 5772 H H5C2   . A1BDP B 2 .   ? 22.76143  -44.27758 18.35848  1.000 185.95098 ? 401 A1BDP A H5C2   1 
HETATM 5773 H H191   . A1BDP B 2 .   ? 14.90535  -35.92310 17.82767  1.000 203.32605 ? 401 A1BDP A H191   1 
HETATM 5774 H H181   . A1BDP B 2 .   ? 13.39271  -35.00685 19.72063  1.000 232.06025 ? 401 A1BDP A H181   1 
HETATM 5775 H H171   . A1BDP B 2 .   ? 12.97087  -36.58135 21.71108  1.000 234.83835 ? 401 A1BDP A H171   1 
HETATM 5776 H H41    . A1BDP B 2 .   ? 21.37615  -44.13755 16.16194  1.000 195.26954 ? 401 A1BDP A H41    1 
HETATM 5777 H H431   . A1BDP B 2 .   ? 22.00138  -46.08996 13.62176  1.000 159.62338 ? 401 A1BDP A H431   1 
HETATM 5778 H H432   . A1BDP B 2 .   ? 23.61096  -46.79786 13.67160  1.000 159.62338 ? 401 A1BDP A H432   1 
HETATM 5779 H H433   . A1BDP B 2 .   ? 23.38029  -45.18311 13.01301  1.000 159.62338 ? 401 A1BDP A H433   1 
HETATM 5780 H H422   . A1BDP B 2 .   ? 24.95398  -44.65960 16.43082  1.000 159.70369 ? 401 A1BDP A H422   1 
HETATM 5781 H H423   . A1BDP B 2 .   ? 24.85584  -43.80356 14.89897  1.000 159.70369 ? 401 A1BDP A H423   1 
HETATM 5782 H H421   . A1BDP B 2 .   ? 25.42666  -45.46528 14.94205  1.000 159.70369 ? 401 A1BDP A H421   1 
HETATM 5783 H H622   . A1BDP B 2 .   ? 22.85659  -41.57905 20.66292  1.000 176.06203 ? 401 A1BDP A H622   1 
HETATM 5784 H H623   . A1BDP B 2 .   ? 23.36775  -41.73897 19.01594  1.000 176.06203 ? 401 A1BDP A H623   1 
HETATM 5785 H H621   . A1BDP B 2 .   ? 23.21958  -43.14444 20.01699  1.000 176.06203 ? 401 A1BDP A H621   1 
HETATM 5786 H H7     . A1BDP B 2 .   ? 21.75038  -40.02270 20.68625  1.000 184.70581 ? 401 A1BDP A H7     1 
HETATM 5787 H H8     . A1BDP B 2 .   ? 20.05558  -38.22622 21.23242  1.000 197.36636 ? 401 A1BDP A H8     1 
HETATM 5788 H H9     . A1BDP B 2 .   ? 17.69112  -38.46777 20.53036  1.000 206.64637 ? 401 A1BDP A H9     1 
HETATM 5789 H H211   . A1BDP B 2 .   ? 19.71225  -49.57533 18.22843  1.000 157.18139 ? 401 A1BDP A H211   1 
HETATM 5790 H H212   . A1BDP B 2 .   ? 19.79664  -50.99305 17.38696  1.000 157.18139 ? 401 A1BDP A H212   1 
HETATM 5791 H H11    . A1BDP B 2 .   ? 16.63676  -43.14265 18.81564  1.000 198.84044 ? 401 A1BDP A H11    1 
HETATM 5792 H H1C    . A1BDP B 2 .   ? 20.03617  -45.21113 14.90556  1.000 187.22669 ? 401 A1BDP A H1C    1 
HETATM 5793 H H3     . A1BDP B 2 .   ? 23.35191  -48.89992 16.50068  1.000 177.35434 ? 401 A1BDP A H3     1 
HETATM 5794 P PA     . FAD   C 3 .   ? 15.83809  -41.70469 2.73474   1.000 96.24200  ? 402 FAD   A PA     1 
HETATM 5795 O O1A    . FAD   C 3 .   ? 15.23442  -42.20711 4.00385   1.000 118.83228 ? 402 FAD   A O1A    1 
HETATM 5796 O O2A    . FAD   C 3 .   ? 17.25075  -42.05079 2.32910   1.000 91.48179  ? 402 FAD   A O2A    1 
HETATM 5797 O O5B    . FAD   C 3 .   ? 14.92074  -42.17601 1.47298   1.000 102.11204 ? 402 FAD   A O5B    1 
HETATM 5798 C C5B    . FAD   C 3 .   ? 15.22143  -41.68888 0.18623   1.000 119.12069 ? 402 FAD   A C5B    1 
HETATM 5799 C C4B    . FAD   C 3 .   ? 14.23369  -42.29576 -0.80636  1.000 128.59824 ? 402 FAD   A C4B    1 
HETATM 5800 O O4B    . FAD   C 3 .   ? 14.69969  -42.05283 -2.13793  1.000 128.11191 ? 402 FAD   A O4B    1 
HETATM 5801 C C3B    . FAD   C 3 .   ? 14.04931  -43.80735 -0.68094  1.000 132.57109 ? 402 FAD   A C3B    1 
HETATM 5802 O O3B    . FAD   C 3 .   ? 12.68472  -44.09995 -0.88380  1.000 133.03521 ? 402 FAD   A O3B    1 
HETATM 5803 C C2B    . FAD   C 3 .   ? 14.88373  -44.34567 -1.83779  1.000 130.01904 ? 402 FAD   A C2B    1 
HETATM 5804 O O2B    . FAD   C 3 .   ? 14.44695  -45.60802 -2.23187  1.000 135.80980 ? 402 FAD   A O2B    1 
HETATM 5805 C C1B    . FAD   C 3 .   ? 14.64801  -43.24111 -2.87312  1.000 122.44822 ? 402 FAD   A C1B    1 
HETATM 5806 N N9A    . FAD   C 3 .   ? 15.59094  -43.21028 -3.95816  1.000 122.84372 ? 402 FAD   A N9A    1 
HETATM 5807 C C8A    . FAD   C 3 .   ? 16.89724  -43.62172 -3.95987  1.000 126.38406 ? 402 FAD   A C8A    1 
HETATM 5808 N N7A    . FAD   C 3 .   ? 17.48116  -43.46659 -5.11045  1.000 132.14733 ? 402 FAD   A N7A    1 
HETATM 5809 C C5A    . FAD   C 3 .   ? 16.51153  -42.92355 -5.91671  1.000 139.12111 ? 402 FAD   A C5A    1 
HETATM 5810 C C6A    . FAD   C 3 .   ? 16.49544  -42.51947 -7.26324  1.000 116.61279 ? 402 FAD   A C6A    1 
HETATM 5811 N N6A    . FAD   C 3 .   ? 17.55865  -42.61953 -8.05841  1.000 117.45412 ? 402 FAD   A N6A    1 
HETATM 5812 N N1A    . FAD   C 3 .   ? 15.35847  -42.01723 -7.75613  1.000 116.68331 ? 402 FAD   A N1A    1 
HETATM 5813 C C2A    . FAD   C 3 .   ? 14.29614  -41.91869 -6.96509  1.000 117.65881 ? 402 FAD   A C2A    1 
HETATM 5814 N N3A    . FAD   C 3 .   ? 14.18753  -42.26011 -5.69483  1.000 137.90381 ? 402 FAD   A N3A    1 
HETATM 5815 C C4A    . FAD   C 3 .   ? 15.32698  -42.75962 -5.21965  1.000 132.88163 ? 402 FAD   A C4A    1 
HETATM 5816 N N1     . FAD   C 3 .   ? 16.30699  -40.49459 12.53346  1.000 126.76848 ? 402 FAD   A N1     1 
HETATM 5817 C C2     . FAD   C 3 .   ? 15.62411  -40.47415 13.71497  1.000 132.37796 ? 402 FAD   A C2     1 
HETATM 5818 O O2     . FAD   C 3 .   ? 14.74755  -39.68335 13.98197  1.000 138.34321 ? 402 FAD   A O2     1 
HETATM 5819 N N3     . FAD   C 3 .   ? 15.92948  -41.40399 14.70566  1.000 140.98326 ? 402 FAD   A N3     1 
HETATM 5820 C C4     . FAD   C 3 .   ? 16.87241  -42.37209 14.62769  1.000 145.76138 ? 402 FAD   A C4     1 
HETATM 5821 O O4     . FAD   C 3 .   ? 17.10557  -43.16131 15.51642  1.000 157.73984 ? 402 FAD   A O4     1 
HETATM 5822 C C4X    . FAD   C 3 .   ? 17.59386  -42.36780 13.33805  1.000 133.45583 ? 402 FAD   A C4X    1 
HETATM 5823 N N5     . FAD   C 3 .   ? 18.50025  -43.25897 13.19783  1.000 150.20996 ? 402 FAD   A N5     1 
HETATM 5824 C C5X    . FAD   C 3 .   ? 19.18449  -43.29701 12.04465  1.000 132.80596 ? 402 FAD   A C5X    1 
HETATM 5825 C C6     . FAD   C 3 .   ? 20.16932  -44.28630 11.92705  1.000 132.29374 ? 402 FAD   A C6     1 
HETATM 5826 C C7     . FAD   C 3 .   ? 20.92829  -44.41915 10.80114  1.000 119.02128 ? 402 FAD   A C7     1 
HETATM 5827 C C7M    . FAD   C 3 .   ? 21.97156  -45.49288 10.71223  1.000 109.52193 ? 402 FAD   A C7M    1 
HETATM 5828 C C8     . FAD   C 3 .   ? 20.68636  -43.51314 9.73293   1.000 131.35916 ? 402 FAD   A C8     1 
HETATM 5829 C C8M    . FAD   C 3 .   ? 21.48596  -43.60816 8.47079   1.000 150.69350 ? 402 FAD   A C8M    1 
HETATM 5830 C C9     . FAD   C 3 .   ? 19.71842  -42.53269 9.83507   1.000 136.28865 ? 402 FAD   A C9     1 
HETATM 5831 C C9A    . FAD   C 3 .   ? 18.93805  -42.39215 10.99061  1.000 132.28712 ? 402 FAD   A C9A    1 
HETATM 5832 N N10    . FAD   C 3 .   ? 17.94915  -41.43828 11.16048  1.000 140.58736 ? 402 FAD   A N10    1 
HETATM 5833 C C10    . FAD   C 3 .   ? 17.24500  -41.38591 12.33863  1.000 131.68369 ? 402 FAD   A C10    1 
HETATM 5834 C "C1'"  . FAD   C 3 .   ? 17.64827  -40.46422 10.09481  1.000 139.82502 ? 402 FAD   A "C1'"  1 
HETATM 5835 C "C2'"  . FAD   C 3 .   ? 16.66483  -40.97826 9.03354   1.000 129.21444 ? 402 FAD   A "C2'"  1 
HETATM 5836 O "O2'"  . FAD   C 3 .   ? 17.03861  -42.27870 8.66014   1.000 129.33605 ? 402 FAD   A "O2'"  1 
HETATM 5837 C "C3'"  . FAD   C 3 .   ? 16.63557  -40.02773 7.81658   1.000 126.38930 ? 402 FAD   A "C3'"  1 
HETATM 5838 O "O3'"  . FAD   C 3 .   ? 16.72482  -38.70888 8.31259   1.000 139.80577 ? 402 FAD   A "O3'"  1 
HETATM 5839 C "C4'"  . FAD   C 3 .   ? 15.35705  -40.15114 6.96147   1.000 120.50285 ? 402 FAD   A "C4'"  1 
HETATM 5840 O "O4'"  . FAD   C 3 .   ? 15.16009  -41.51370 6.66920   1.000 121.69233 ? 402 FAD   A "O4'"  1 
HETATM 5841 C "C5'"  . FAD   C 3 .   ? 15.45870  -39.31420 5.68596   1.000 118.90862 ? 402 FAD   A "C5'"  1 
HETATM 5842 O "O5'"  . FAD   C 3 .   ? 14.31525  -39.52058 4.88108   1.000 114.69063 ? 402 FAD   A "O5'"  1 
HETATM 5843 P P      . FAD   C 3 .   ? 14.34181  -39.18142 3.27681   1.000 108.28349 ? 402 FAD   A P      1 
HETATM 5844 O O1P    . FAD   C 3 .   ? 14.67065  -37.73038 3.16737   1.000 111.22101 ? 402 FAD   A O1P    1 
HETATM 5845 O O2P    . FAD   C 3 .   ? 13.16663  -39.79668 2.58845   1.000 111.79902 ? 402 FAD   A O2P    1 
HETATM 5846 O O3P    . FAD   C 3 .   ? 15.62813  -40.08785 2.75330   1.000 107.49883 ? 402 FAD   A O3P    1 
HETATM 5847 H H51A   . FAD   C 3 .   ? 16.13078  -41.92245 -0.05756  1.000 143.33530 ? 402 FAD   A H51A   1 
HETATM 5848 H H52A   . FAD   C 3 .   ? 15.16265  -40.72078 0.17113   1.000 143.33530 ? 402 FAD   A H52A   1 
HETATM 5849 H H4B    . FAD   C 3 .   ? 13.37938  -41.84852 -0.70129  1.000 154.70836 ? 402 FAD   A H4B    1 
HETATM 5850 H H3B    . FAD   C 3 .   ? 14.38173  -44.12624 0.17270   1.000 159.47578 ? 402 FAD   A H3B    1 
HETATM 5851 H HO3A   . FAD   C 3 .   ? 12.42366  -43.69201 -1.58232  1.000 160.03273 ? 402 FAD   A HO3A   1 
HETATM 5852 H H2B    . FAD   C 3 .   ? 15.81918  -44.35810 -1.58154  1.000 156.41332 ? 402 FAD   A H2B    1 
HETATM 5853 H HO2A   . FAD   C 3 .   ? 14.94792  -45.89717 -2.85470  1.000 163.36223 ? 402 FAD   A HO2A   1 
HETATM 5854 H H1B    . FAD   C 3 .   ? 13.78930  -43.36059 -3.30813  1.000 147.32833 ? 402 FAD   A H1B    1 
HETATM 5855 H H8A    . FAD   C 3 .   ? 17.29971  -43.97309 -3.19865  1.000 152.05134 ? 402 FAD   A H8A    1 
HETATM 5856 H H61A   . FAD   C 3 .   ? 18.27743  -42.99783 -7.77708  1.000 141.33542 ? 402 FAD   A H61A   1 
HETATM 5857 H H62A   . FAD   C 3 .   ? 17.54163  -42.31434 -8.86182  1.000 141.33542 ? 402 FAD   A H62A   1 
HETATM 5858 H H2A    . FAD   C 3 .   ? 13.53356  -41.56307 -7.36119  1.000 141.58105 ? 402 FAD   A H2A    1 
HETATM 5859 H HN3    . FAD   C 3 .   ? 15.47329  -41.35396 15.43298  1.000 169.57039 ? 402 FAD   A HN3    1 
HETATM 5860 H H6     . FAD   C 3 .   ? 20.28946  -44.85648 12.65187  1.000 159.14296 ? 402 FAD   A H6     1 
HETATM 5861 H HM71   . FAD   C 3 .   ? 21.97326  -45.91274 9.83780   1.000 131.81678 ? 402 FAD   A HM71   1 
HETATM 5862 H HM72   . FAD   C 3 .   ? 21.81908  -46.18940 11.36988  1.000 131.81678 ? 402 FAD   A HM72   1 
HETATM 5863 H HM73   . FAD   C 3 .   ? 22.86030  -45.13600 10.86611  1.000 131.81678 ? 402 FAD   A HM73   1 
HETATM 5864 H HM81   . FAD   C 3 .   ? 21.06138  -43.13013 7.74133   1.000 181.22267 ? 402 FAD   A HM81   1 
HETATM 5865 H HM82   . FAD   C 3 .   ? 21.59583  -44.52863 8.18520   1.000 181.22267 ? 402 FAD   A HM82   1 
HETATM 5866 H HM83   . FAD   C 3 .   ? 22.37405  -43.23387 8.58074   1.000 181.22267 ? 402 FAD   A HM83   1 
HETATM 5867 H H9     . FAD   C 3 .   ? 19.59927  -41.96443 9.10858   1.000 163.93685 ? 402 FAD   A H9     1 
HETATM 5868 H "H1'1" . FAD   C 3 .   ? 18.49248  -40.22216 9.68296   1.000 168.18050 ? 402 FAD   A "H1'1" 1 
HETATM 5869 H "H1'2" . FAD   C 3 .   ? 17.29470  -39.67028 10.52558  1.000 168.18050 ? 402 FAD   A "H1'2" 1 
HETATM 5870 H "H2'"  . FAD   C 3 .   ? 15.78791  -40.96039 9.44778   1.000 155.44779 ? 402 FAD   A "H2'"  1 
HETATM 5871 H "HO2'" . FAD   C 3 .   ? 16.74465  -42.38946 7.87032   1.000 155.59373 ? 402 FAD   A "HO2'" 1 
HETATM 5872 H "H3'"  . FAD   C 3 .   ? 17.39507  -40.26907 7.26357   1.000 152.05763 ? 402 FAD   A "H3'"  1 
HETATM 5873 H "HO3'" . FAD   C 3 .   ? 17.52448  -38.43228 8.23173   1.000 168.15739 ? 402 FAD   A "HO3'" 1 
HETATM 5874 H "H4'"  . FAD   C 3 .   ? 14.62884  -39.80254 7.49914   1.000 144.99389 ? 402 FAD   A "H4'"  1 
HETATM 5875 H "HO4'" . FAD   C 3 .   ? 14.43065  -41.66813 6.26108   1.000 146.42127 ? 402 FAD   A "HO4'" 1 
HETATM 5876 H "H5'1" . FAD   C 3 .   ? 16.25280  -39.55754 5.18487   1.000 143.08081 ? 402 FAD   A "H5'1" 1 
HETATM 5877 H "H5'2" . FAD   C 3 .   ? 15.53180  -38.37214 5.90522   1.000 143.08081 ? 402 FAD   A "H5'2" 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   . THR A 22  ? 2.18193 2.17720 2.23698 0.22046  0.10485  0.19402  23  THR A N   
2    C CA  . THR A 22  ? 2.28048 2.24089 2.27815 0.25224  0.10785  0.20017  23  THR A CA  
3    C C   . THR A 22  ? 2.37408 2.28980 2.31135 0.24387  0.11732  0.19723  23  THR A C   
4    O O   . THR A 22  ? 2.70581 2.61111 2.61062 0.25991  0.09875  0.19316  23  THR A O   
5    C CB  . THR A 22  ? 2.38711 2.32489 2.36747 0.26927  0.13766  0.21361  23  THR A CB  
6    O OG1 . THR A 22  ? 2.36642 2.34844 2.40446 0.27777  0.12932  0.21530  23  THR A OG1 
7    C CG2 . THR A 22  ? 2.27064 2.16971 2.18951 0.30300  0.13922  0.22084  23  THR A CG2 
14   N N   . LEU A 23  ? 2.32765 2.21889 2.25027 0.21789  0.14662  0.19880  24  LEU A N   
15   C CA  . LEU A 23  ? 2.44655 2.29660 2.31203 0.20794  0.15915  0.19553  24  LEU A CA  
16   C C   . LEU A 23  ? 2.48774 2.35261 2.35681 0.20218  0.12804  0.18187  24  LEU A C   
17   O O   . LEU A 23  ? 2.48895 2.32515 2.30661 0.20927  0.12626  0.17812  24  LEU A O   
18   C CB  . LEU A 23  ? 2.69045 2.52447 2.55362 0.17639  0.19130  0.19730  24  LEU A CB  
19   C CG  . LEU A 23  ? 2.71918 2.51048 2.52269 0.16362  0.21092  0.19451  24  LEU A CG  
20   C CD1 . LEU A 23  ? 2.67894 2.42453 2.41521 0.18824  0.22702  0.20221  24  LEU A CD1 
21   C CD2 . LEU A 23  ? 2.86423 2.64794 2.67435 0.13179  0.24134  0.19655  24  LEU A CD2 
33   N N   . LEU A 24  ? 2.49696 2.40595 2.42565 0.18884  0.10353  0.17379  25  LEU A N   
34   C CA  . LEU A 24  ? 2.44426 2.36891 2.38243 0.18080  0.07413  0.15978  25  LEU A CA  
35   C C   . LEU A 24  ? 2.49573 2.45470 2.46040 0.20213  0.03780  0.15479  25  LEU A C   
36   O O   . LEU A 24  ? 2.47197 2.45673 2.46541 0.19219  0.01059  0.14272  25  LEU A O   
37   C CB  . LEU A 24  ? 2.33247 2.27824 2.31536 0.14693  0.07224  0.15307  25  LEU A CB  
38   C CG  . LEU A 24  ? 2.55883 2.47619 2.51877 0.12138  0.10261  0.15474  25  LEU A CG  
39   C CD1 . LEU A 24  ? 2.48867 2.43214 2.49895 0.09041  0.09502  0.14877  25  LEU A CD1 
40   C CD2 . LEU A 24  ? 2.49582 2.37751 2.39577 0.12397  0.10750  0.14868  25  LEU A CD2 
52   N N   . LYS A 25  ? 2.60984 2.56982 2.56530 0.23135  0.03655  0.16356  26  LYS A N   
53   C CA  . LYS A 25  ? 2.58546 2.58317 2.57005 0.25140  0.00229  0.15924  26  LYS A CA  
54   C C   . LYS A 25  ? 2.55513 2.54817 2.51214 0.25741  -0.02284 0.14790  26  LYS A C   
55   O O   . LYS A 25  ? 2.62146 2.57534 2.51849 0.26653  -0.01311 0.14923  26  LYS A O   
56   C CB  . LYS A 25  ? 2.56925 2.56495 2.54216 0.28440  0.00671  0.17144  26  LYS A CB  
57   C CG  . LYS A 25  ? 2.56720 2.60662 2.57269 0.30572  -0.02894 0.16717  26  LYS A CG  
58   C CD  . LYS A 25  ? 2.73285 2.77449 2.73259 0.33925  -0.02535 0.17947  26  LYS A CD  
59   C CE  . LYS A 25  ? 2.50996 2.59829 2.54153 0.35995  -0.06237 0.17425  26  LYS A CE  
60   N NZ  . LYS A 25  ? 2.46940 2.56286 2.49699 0.39505  -0.06130 0.18600  26  LYS A NZ  
74   N N   . ASN A 26  ? 2.47958 2.51285 2.48019 0.25127  -0.05485 0.13614  27  ASN A N   
75   C CA  . ASN A 26  ? 2.49366 2.52944 2.47605 0.25656  -0.08199 0.12357  27  ASN A CA  
76   C C   . ASN A 26  ? 2.51934 2.51818 2.45898 0.24008  -0.06989 0.11657  27  ASN A C   
77   O O   . ASN A 26  ? 2.64682 2.63177 2.54836 0.24935  -0.08220 0.10909  27  ASN A O   
78   C CB  . ASN A 26  ? 2.58163 2.61378 2.53047 0.29131  -0.09474 0.12834  27  ASN A CB  
79   C CG  . ASN A 26  ? 2.48035 2.55411 2.47310 0.30965  -0.11027 0.13357  27  ASN A CG  
80   O OD1 . ASN A 26  ? 2.33561 2.44642 2.38728 0.29488  -0.11683 0.13054  27  ASN A OD1 
81   N ND2 . ASN A 26  ? 2.51704 2.58563 2.48089 0.34188  -0.11658 0.14131  27  ASN A ND2 
88   N N   . LYS A 27  ? 2.39935 2.38383 2.34504 0.21524  -0.04586 0.11840  28  LYS A N   
89   C CA  . LYS A 27  ? 2.32354 2.27797 2.23507 0.19719  -0.03370 0.11098  28  LYS A CA  
90   C C   . LYS A 27  ? 2.28324 2.26216 2.24141 0.17059  -0.04963 0.09844  28  LYS A C   
91   O O   . LYS A 27  ? 2.39798 2.39548 2.40147 0.15305  -0.04408 0.10206  28  LYS A O   
92   C CB  . LYS A 27  ? 2.50374 2.42206 2.38314 0.18833  0.00606  0.12207  28  LYS A CB  
93   C CG  . LYS A 27  ? 2.53190 2.41756 2.35748 0.21341  0.02448  0.13437  28  LYS A CG  
94   C CD  . LYS A 27  ? 2.25284 2.11512 2.02229 0.22850  0.01449  0.12801  28  LYS A CD  
95   C CE  . LYS A 27  ? 2.27280 2.10232 1.98925 0.25480  0.03004  0.14136  28  LYS A CE  
96   N NZ  . LYS A 27  ? 2.36398 2.15595 2.04859 0.24573  0.07012  0.15202  28  LYS A NZ  
110  N N   . LYS A 28  ? 2.18842 2.16639 2.13462 0.16755  -0.06925 0.08366  29  LYS A N   
111  C CA  . LYS A 28  ? 2.20029 2.19804 2.18711 0.14446  -0.08679 0.07057  29  LYS A CA  
112  C C   . LYS A 28  ? 2.19026 2.16311 2.16258 0.12115  -0.06307 0.06953  29  LYS A C   
113  O O   . LYS A 28  ? 2.13938 2.08466 2.06503 0.12165  -0.05414 0.06360  29  LYS A O   
114  C CB  . LYS A 28  ? 2.16686 2.17389 2.14684 0.15204  -0.11756 0.05427  29  LYS A CB  
115  C CG  . LYS A 28  ? 2.05163 2.07610 2.07137 0.12987  -0.13717 0.03963  29  LYS A CG  
116  C CD  . LYS A 28  ? 2.20353 2.23847 2.21753 0.13852  -0.16788 0.02285  29  LYS A CD  
117  C CE  . LYS A 28  ? 2.13022 2.13371 2.08969 0.14048  -0.16031 0.01350  29  LYS A CE  
118  N NZ  . LYS A 28  ? 1.84795 1.86267 1.81177 0.14011  -0.18945 -0.00628 29  LYS A NZ  
132  N N   . ILE A 29  ? 2.06574 2.04984 2.07786 0.10015  -0.05306 0.07494  30  ILE A N   
133  C CA  . ILE A 29  ? 1.90624 1.87099 1.90998 0.07684  -0.03036 0.07552  30  ILE A CA  
134  C C   . ILE A 29  ? 1.80524 1.78324 1.84016 0.05779  -0.05157 0.06143  30  ILE A C   
135  O O   . ILE A 29  ? 1.87476 1.88200 1.95780 0.05285  -0.07594 0.05718  30  ILE A O   
136  C CB  . ILE A 29  ? 2.11635 2.08434 2.14296 0.06408  -0.00564 0.09036  30  ILE A CB  
137  C CG1 . ILE A 29  ? 2.31550 2.28059 2.32802 0.08615  0.00697  0.10349  30  ILE A CG1 
138  C CG2 . ILE A 29  ? 2.11065 2.05196 2.11128 0.04500  0.02410  0.09318  30  ILE A CG2 
139  C CD1 . ILE A 29  ? 2.18668 2.11545 2.13262 0.10499  0.02413  0.10670  30  ILE A CD1 
151  N N   . THR A 30  ? 1.73515 1.69159 1.74255 0.04698  -0.04225 0.05380  31  THR A N   
152  C CA  . THR A 30  ? 1.72199 1.68616 1.75464 0.02958  -0.05985 0.04038  31  THR A CA  
153  C C   . THR A 30  ? 1.88086 1.83180 1.91299 0.00653  -0.03632 0.04455  31  THR A C   
154  O O   . THR A 30  ? 1.93217 1.85838 1.92019 0.00658  -0.01047 0.04745  31  THR A O   
155  C CB  . THR A 30  ? 2.00335 1.95770 2.00480 0.03981  -0.07589 0.02334  31  THR A CB  
156  O OG1 . THR A 30  ? 2.27808 2.20268 2.22094 0.04598  -0.05117 0.02447  31  THR A OG1 
157  C CG2 . THR A 30  ? 2.01814 1.98932 2.02427 0.06048  -0.10264 0.01800  31  THR A CG2 
165  N N   . ILE A 31  ? 1.76979 1.73732 1.84978 -0.01373 -0.04542 0.04484  32  ILE A N   
166  C CA  . ILE A 31  ? 1.57348 1.53226 1.65879 -0.03711 -0.02785 0.04809  32  ILE A CA  
167  C C   . ILE A 31  ? 1.57280 1.53001 1.66498 -0.04535 -0.04726 0.03193  32  ILE A C   
168  O O   . ILE A 31  ? 1.59195 1.56503 1.71659 -0.04512 -0.07688 0.02271  32  ILE A O   
169  C CB  . ILE A 31  ? 1.64880 1.62564 1.78132 -0.05530 -0.02366 0.06056  32  ILE A CB  
170  C CG1 . ILE A 31  ? 1.60599 1.58493 1.73218 -0.04577 -0.00360 0.07544  32  ILE A CG1 
171  C CG2 . ILE A 31  ? 1.81910 1.78774 1.95693 -0.08022 -0.00733 0.06394  32  ILE A CG2 
172  C CD1 . ILE A 31  ? 1.96949 1.97140 2.14502 -0.06113 -0.00251 0.08615  32  ILE A CD1 
184  N N   . ILE A 32  ? 1.56697 1.50551 1.62876 -0.05255 -0.03057 0.02782  33  ILE A N   
185  C CA  . ILE A 32  ? 1.53044 1.46602 1.59532 -0.05904 -0.04620 0.01186  33  ILE A CA  
186  C C   . ILE A 32  ? 1.67893 1.61951 1.77830 -0.08364 -0.04305 0.01718  33  ILE A C   
187  O O   . ILE A 32  ? 1.76766 1.69847 1.85108 -0.09563 -0.01698 0.02478  33  ILE A O   
188  C CB  . ILE A 32  ? 1.52761 1.44248 1.53844 -0.05164 -0.03111 0.00236  33  ILE A CB  
189  C CG1 . ILE A 32  ? 1.69220 1.59831 1.66227 -0.02890 -0.02725 0.00208  33  ILE A CG1 
190  C CG2 . ILE A 32  ? 1.52507 1.44006 1.54074 -0.05355 -0.05186 -0.01711 33  ILE A CG2 
191  C CD1 . ILE A 32  ? 2.03128 1.95118 2.01687 -0.01315 -0.05921 -0.00725 33  ILE A CD1 
203  N N   . GLY A 33  ? 1.65698 1.61229 1.80229 -0.09190 -0.06964 0.01319  34  GLY A N   
204  C CA  . GLY A 33  ? 1.52230 1.48114 1.70087 -0.11511 -0.07061 0.01789  34  GLY A CA  
205  C C   . GLY A 33  ? 1.44546 1.42175 1.66790 -0.12771 -0.07509 0.03116  34  GLY A C   
206  O O   . GLY A 33  ? 1.39663 1.37695 1.61550 -0.12832 -0.05475 0.04509  34  GLY A O   
210  N N   . ALA A 34  ? 1.49549 1.48182 1.75910 -0.13826 -0.10135 0.02643  35  ALA A N   
211  C CA  . ALA A 34  ? 1.40466 1.40881 1.71215 -0.15304 -0.10802 0.03731  35  ALA A CA  
212  C C   . ALA A 34  ? 1.36888 1.37067 1.69648 -0.17920 -0.09779 0.04774  35  ALA A C   
213  O O   . ALA A 34  ? 1.30193 1.31443 1.66963 -0.19566 -0.11284 0.05137  35  ALA A O   
214  C CB  . ALA A 34  ? 1.41131 1.42813 1.75152 -0.15084 -0.14288 0.02639  35  ALA A CB  
220  N N   . GLY A 35  ? 1.40485 1.39301 1.70425 -0.18424 -0.07260 0.05247  36  GLY A N   
221  C CA  . GLY A 35  ? 1.33058 1.31839 1.64561 -0.20867 -0.05949 0.06433  36  GLY A CA  
222  C C   . GLY A 35  ? 1.42668 1.42857 1.76011 -0.22002 -0.04332 0.08089  36  GLY A C   
223  O O   . GLY A 35  ? 1.21437 1.22659 1.54890 -0.20729 -0.04245 0.08289  36  GLY A O   
227  N N   . PRO A 36  ? 1.39697 1.40043 1.74541 -0.24413 -0.03040 0.09276  37  PRO A N   
228  C CA  . PRO A 36  ? 1.09107 1.10899 1.45780 -0.25700 -0.01340 0.10800  37  PRO A CA  
229  C C   . PRO A 36  ? 1.14463 1.16054 1.48003 -0.24212 0.01397  0.11312  37  PRO A C   
230  O O   . PRO A 36  ? 1.09779 1.12820 1.44845 -0.23953 0.01853  0.11979  37  PRO A O   
231  C CB  . PRO A 36  ? 1.10829 1.12371 1.48484 -0.28455 -0.00074 0.11850  37  PRO A CB  
232  C CG  . PRO A 36  ? 1.14141 1.13943 1.49308 -0.28136 -0.00255 0.10976  37  PRO A CG  
233  C CD  . PRO A 36  ? 1.16740 1.16056 1.51584 -0.26033 -0.02988 0.09289  37  PRO A CD  
241  N N   . VAL A 37  ? 1.24462 1.24261 1.53597 -0.23202 0.03231  0.10971  38  VAL A N   
242  C CA  . VAL A 37  ? 1.21485 1.20619 1.47210 -0.21809 0.05924  0.11477  38  VAL A CA  
243  C C   . VAL A 37  ? 1.40485 1.39926 1.65542 -0.19120 0.04421  0.10751  38  VAL A C   
244  O O   . VAL A 37  ? 1.45863 1.46215 1.71453 -0.18303 0.05205  0.11460  38  VAL A O   
245  C CB  . VAL A 37  ? 1.12298 1.09355 1.33289 -0.21654 0.08273  0.11228  38  VAL A CB  
246  C CG1 . VAL A 37  ? 1.30570 1.26522 1.47691 -0.20159 0.10991  0.11707  38  VAL A CG1 
247  C CG2 . VAL A 37  ? 1.40764 1.37828 1.62455 -0.24341 0.09859  0.12037  38  VAL A CG2 
257  N N   . GLY A 38  ? 1.38005 1.36781 1.61899 -0.17678 0.02226  0.09297  39  GLY A N   
258  C CA  . GLY A 38  ? 1.35582 1.34655 1.58523 -0.15134 0.00745  0.08562  39  GLY A CA  
259  C C   . GLY A 38  ? 1.44017 1.45529 1.71244 -0.15083 -0.01089 0.08889  39  GLY A C   
260  O O   . GLY A 38  ? 1.18170 1.20388 1.44845 -0.13344 -0.00869 0.09171  39  GLY A O   
264  N N   . LEU A 39  ? 1.42702 1.45551 1.74210 -0.17002 -0.02929 0.08851  40  LEU A N   
265  C CA  . LEU A 39  ? 1.28812 1.34199 1.64574 -0.17283 -0.04682 0.09072  40  LEU A CA  
266  C C   . LEU A 39  ? 1.52423 1.59009 1.88987 -0.17641 -0.02311 0.10518  40  LEU A C   
267  O O   . LEU A 39  ? 1.44518 1.52793 1.82181 -0.16237 -0.02826 0.10619  40  LEU A O   
268  C CB  . LEU A 39  ? 1.13372 1.19558 1.53197 -0.19651 -0.06758 0.08872  40  LEU A CB  
269  C CG  . LEU A 39  ? 1.18520 1.23950 1.58556 -0.19164 -0.09719 0.07279  40  LEU A CG  
270  C CD1 . LEU A 39  ? 1.33666 1.39241 1.77243 -0.21701 -0.11304 0.07316  40  LEU A CD1 
271  C CD2 . LEU A 39  ? 1.73980 1.80840 2.14781 -0.17206 -0.12070 0.06260  40  LEU A CD2 
283  N N   . THR A 40  ? 1.48831 1.54669 1.84888 -0.19501 0.00316  0.11606  41  THR A N   
284  C CA  . THR A 40  ? 1.23157 1.29937 1.59718 -0.19893 0.02855  0.12907  41  THR A CA  
285  C C   . THR A 40  ? 1.55854 1.61830 1.88945 -0.17087 0.04252  0.12977  41  THR A C   
286  O O   . THR A 40  ? 1.41813 1.49406 1.76334 -0.16193 0.04646  0.13502  41  THR A O   
287  C CB  . THR A 40  ? 1.12955 1.18667 1.48635 -0.22226 0.05650  0.13920  41  THR A CB  
288  O OG1 . THR A 40  ? 1.29053 1.35421 1.67902 -0.24794 0.04207  0.13955  41  THR A OG1 
289  C CG2 . THR A 40  ? 1.56779 1.63493 1.93119 -0.22757 0.08336  0.15175  41  THR A CG2 
297  N N   . MET A 41  ? 1.61958 1.65426 1.90408 -0.15670 0.05021  0.12443  42  MET A N   
298  C CA  . MET A 41  ? 1.61118 1.63455 1.85867 -0.12918 0.06068  0.12461  42  MET A CA  
299  C C   . MET A 41  ? 1.61498 1.65743 1.88112 -0.10853 0.03323  0.11851  42  MET A C   
300  O O   . MET A 41  ? 1.77109 1.81991 2.03336 -0.09118 0.04025  0.12397  42  MET A O   
301  C CB  . MET A 41  ? 1.62534 1.62006 1.82145 -0.11950 0.06813  0.11732  42  MET A CB  
302  C CG  . MET A 41  ? 1.79979 1.77700 1.95022 -0.09342 0.08273  0.11890  42  MET A CG  
303  S SD  . MET A 41  ? 1.95277 1.91564 2.07998 -0.09822 0.12668  0.13477  42  MET A SD  
304  C CE  . MET A 41  ? 2.01465 1.96642 2.10792 -0.06261 0.12951  0.13680  42  MET A CE  
314  N N   . ALA A 42  ? 1.44782 1.49992 1.73441 -0.10994 0.00171  0.10693  43  ALA A N   
315  C CA  . ALA A 42  ? 1.61690 1.68900 1.92121 -0.09184 -0.02573 0.09981  43  ALA A CA  
316  C C   . ALA A 42  ? 1.59130 1.69372 1.93834 -0.09623 -0.02755 0.10743  43  ALA A C   
317  O O   . ALA A 42  ? 1.56696 1.68366 1.91605 -0.07518 -0.03388 0.10773  43  ALA A O   
318  C CB  . ALA A 42  ? 1.71498 1.79184 2.03695 -0.09743 -0.05791 0.08568  43  ALA A CB  
324  N N   . ARG A 43  ? 1.49443 1.60816 1.87582 -0.12353 -0.02221 0.11348  44  ARG A N   
325  C CA  . ARG A 43  ? 1.60969 1.75446 2.03344 -0.13061 -0.02323 0.11969  44  ARG A CA  
326  C C   . ARG A 43  ? 1.71731 1.86096 2.12507 -0.11738 0.00523  0.13054  44  ARG A C   
327  O O   . ARG A 43  ? 1.77365 1.93975 2.19804 -0.10184 -0.00034 0.13155  44  ARG A O   
328  C CB  . ARG A 43  ? 1.60669 1.76075 2.06643 -0.16499 -0.02234 0.12400  44  ARG A CB  
329  C CG  . ARG A 43  ? 1.62385 1.80644 2.12163 -0.17754 -0.01296 0.13265  44  ARG A CG  
330  C CD  . ARG A 43  ? 1.75145 1.96726 2.28063 -0.16434 -0.03604 0.12677  44  ARG A CD  
331  N NE  . ARG A 43  ? 1.74935 1.99392 2.31359 -0.17539 -0.02481 0.13423  44  ARG A NE  
332  C CZ  . ARG A 43  ? 1.68475 1.96519 2.28542 -0.17112 -0.04188 0.13017  44  ARG A CZ  
333  N NH1 . ARG A 43  ? 1.47521 1.76799 2.08317 -0.15688 -0.07175 0.11905  44  ARG A NH1 
334  N NH2 . ARG A 43  ? 1.62609 1.93227 2.25686 -0.18203 -0.02835 0.13669  44  ARG A NH2 
348  N N   . LEU A 44  ? 1.70075 1.81858 2.07609 -0.12310 0.03605  0.13835  45  LEU A N   
349  C CA  . LEU A 44  ? 1.76957 1.88212 2.12735 -0.11152 0.06514  0.14854  45  LEU A CA  
350  C C   . LEU A 44  ? 1.89444 2.00211 2.22542 -0.07605 0.05936  0.14604  45  LEU A C   
351  O O   . LEU A 44  ? 1.96064 2.07948 2.29756 -0.06135 0.06887  0.15213  45  LEU A O   
352  C CB  . LEU A 44  ? 1.83568 1.91747 2.15626 -0.12314 0.09818  0.15542  45  LEU A CB  
353  C CG  . LEU A 44  ? 1.99975 2.08667 2.34427 -0.15821 0.10949  0.16079  45  LEU A CG  
354  C CD1 . LEU A 44  ? 1.92446 1.98130 2.22737 -0.16735 0.14132  0.16623  45  LEU A CD1 
355  C CD2 . LEU A 44  ? 1.83964 1.95513 2.22657 -0.17069 0.11696  0.16830  45  LEU A CD2 
367  N N   . LEU A 45  ? 1.81485 1.90618 2.11608 -0.06165 0.04354  0.13698  46  LEU A N   
368  C CA  . LEU A 45  ? 1.76045 1.84759 2.03538 -0.02858 0.03511  0.13447  46  LEU A CA  
369  C C   . LEU A 45  ? 1.76092 1.88542 2.07722 -0.01811 0.00512  0.12925  46  LEU A C   
370  O O   . LEU A 45  ? 1.84699 1.98395 2.16550 0.00339  0.00630  0.13359  46  LEU A O   
371  C CB  . LEU A 45  ? 1.79456 1.85483 2.02549 -0.01856 0.02697  0.12538  46  LEU A CB  
372  C CG  . LEU A 45  ? 2.11686 2.13853 2.29477 -0.02040 0.05724  0.12950  46  LEU A CG  
373  C CD1 . LEU A 45  ? 2.49193 2.49383 2.63367 -0.01277 0.04452  0.11776  46  LEU A CD1 
374  C CD2 . LEU A 45  ? 2.39140 2.39677 2.53695 -0.00065 0.08259  0.14010  46  LEU A CD2 
386  N N   . GLN A 46  ? 1.70255 1.84541 2.05184 -0.03306 -0.02208 0.11963  47  GLN A N   
387  C CA  . GLN A 46  ? 1.80081 1.97916 2.18672 -0.02423 -0.05237 0.11260  47  GLN A CA  
388  C C   . GLN A 46  ? 1.89642 2.10714 2.32300 -0.02762 -0.04596 0.12002  47  GLN A C   
389  O O   . GLN A 46  ? 1.87877 2.11543 2.32061 -0.00793 -0.05975 0.11830  47  GLN A O   
390  C CB  . GLN A 46  ? 1.73250 1.92092 2.14585 -0.04386 -0.07984 0.10107  47  GLN A CB  
391  C CG  . GLN A 46  ? 1.64106 1.86448 2.08840 -0.03602 -0.11272 0.09160  47  GLN A CG  
392  C CD  . GLN A 46  ? 1.63307 1.85066 2.07729 -0.03888 -0.14033 0.07712  47  GLN A CD  
393  O OE1 . GLN A 46  ? 1.92937 2.15292 2.36144 -0.01803 -0.15988 0.06854  47  GLN A OE1 
394  N NE2 . GLN A 46  ? 1.55106 1.75663 2.00578 -0.06455 -0.14213 0.07421  47  GLN A NE2 
403  N N   . GLN A 47  ? 1.87947 2.09085 2.32422 -0.05248 -0.02508 0.12791  48  GLN A N   
404  C CA  . GLN A 47  ? 1.85080 2.09294 2.33335 -0.05712 -0.01616 0.13442  48  GLN A CA  
405  C C   . GLN A 47  ? 1.86887 2.10355 2.32718 -0.03091 0.00647  0.14310  48  GLN A C   
406  O O   . GLN A 47  ? 1.92162 2.18354 2.41010 -0.02890 0.01313  0.14743  48  GLN A O   
407  C CB  . GLN A 47  ? 1.82480 2.06851 2.33099 -0.09240 0.00081  0.14044  48  GLN A CB  
408  C CG  . GLN A 47  ? 1.87801 2.08845 2.34855 -0.09853 0.03700  0.15052  48  GLN A CG  
409  C CD  . GLN A 47  ? 1.84425 2.05804 2.33853 -0.13507 0.05093  0.15596  48  GLN A CD  
410  O OE1 . GLN A 47  ? 1.65319 1.88713 2.18489 -0.15696 0.03168  0.15180  48  GLN A OE1 
411  N NE2 . GLN A 47  ? 1.83052 2.02388 2.30188 -0.14250 0.08460  0.16540  48  GLN A NE2 
420  N N   . ASN A 48  ? 1.91849 2.11662 2.32299 -0.01122 0.01868  0.14541  49  ASN A N   
421  C CA  . ASN A 48  ? 2.02170 2.20762 2.39738 0.01713  0.03716  0.15324  49  ASN A CA  
422  C C   . ASN A 48  ? 1.86428 2.05406 2.22239 0.05056  0.01415  0.14811  49  ASN A C   
423  O O   . ASN A 48  ? 1.87102 2.03742 2.18856 0.07640  0.02725  0.15393  49  ASN A O   
424  C CB  . ASN A 48  ? 2.03626 2.17618 2.35993 0.01522  0.07018  0.16069  49  ASN A CB  
425  C CG  . ASN A 48  ? 2.13860 2.27653 2.47763 -0.01410 0.09769  0.16790  49  ASN A CG  
426  O OD1 . ASN A 48  ? 2.08526 2.23980 2.44752 -0.01491 0.11279  0.17437  49  ASN A OD1 
427  N ND2 . ASN A 48  ? 2.22989 2.34835 2.55579 -0.03813 0.10447  0.16652  49  ASN A ND2 
434  N N   . ARG A 49  ? 1.82801 2.04583 2.21445 0.04984  -0.01983 0.13739  50  ARG A N   
435  C CA  . ARG A 49  ? 1.86182 2.08980 2.23705 0.07936  -0.04479 0.13153  50  ARG A CA  
436  C C   . ARG A 49  ? 1.92678 2.11478 2.24363 0.09321  -0.04487 0.12881  50  ARG A C   
437  O O   . ARG A 49  ? 2.13060 2.31295 2.41926 0.12258  -0.05267 0.12916  50  ARG A O   
438  C CB  . ARG A 49  ? 1.89386 2.13849 2.27372 0.10732  -0.03893 0.13898  50  ARG A CB  
439  C CG  . ARG A 49  ? 1.89702 2.18439 2.33451 0.09580  -0.03779 0.14074  50  ARG A CG  
440  C CD  . ARG A 49  ? 2.01374 2.32183 2.45769 0.12752  -0.03721 0.14585  50  ARG A CD  
441  N NE  . ARG A 49  ? 2.23730 2.59616 2.74181 0.11811  -0.04429 0.14356  50  ARG A NE  
442  C CZ  . ARG A 49  ? 2.24292 2.64695 2.78328 0.12722  -0.07371 0.13536  50  ARG A CZ  
443  N NH1 . ARG A 49  ? 2.28162 2.68766 2.80444 0.14709  -0.09987 0.12890  50  ARG A NH1 
444  N NH2 . ARG A 49  ? 2.11619 2.56591 2.71104 0.11523  -0.07661 0.13306  50  ARG A NH2 
458  N N   . VAL A 50  ? 1.84120 2.00230 2.13920 0.07233  -0.03663 0.12588  51  VAL A N   
459  C CA  . VAL A 50  ? 1.88319 2.00646 2.12550 0.08198  -0.03371 0.12235  51  VAL A CA  
460  C C   . VAL A 50  ? 1.97573 2.10858 2.22633 0.07731  -0.06583 0.10743  51  VAL A C   
461  O O   . VAL A 50  ? 1.84560 1.99799 2.13658 0.05420  -0.08007 0.10094  51  VAL A O   
462  C CB  . VAL A 50  ? 1.80213 1.88969 2.01503 0.06320  -0.00234 0.12775  51  VAL A CB  
463  C CG1 . VAL A 50  ? 1.91189 1.96372 2.06903 0.07098  -0.00048 0.12204  51  VAL A CG1 
464  C CG2 . VAL A 50  ? 2.08384 2.15952 2.28516 0.06824  0.03063  0.14183  51  VAL A CG2 
474  N N   . ASP A 51  ? 1.87302 1.99097 2.08424 0.09892  -0.07713 0.10185  52  ASP A N   
475  C CA  . ASP A 51  ? 1.83408 1.95458 2.04377 0.09543  -0.10434 0.08664  52  ASP A CA  
476  C C   . ASP A 51  ? 1.86517 1.95376 2.04908 0.07651  -0.09051 0.08268  52  ASP A C   
477  O O   . ASP A 51  ? 1.82404 1.87905 1.95662 0.08491  -0.07111 0.08564  52  ASP A O   
478  C CB  . ASP A 51  ? 2.00765 2.12428 2.18262 0.12482  -0.11999 0.08219  52  ASP A CB  
479  C CG  . ASP A 51  ? 2.10388 2.22982 2.28356 0.12187  -0.15092 0.06510  52  ASP A CG  
480  O OD1 . ASP A 51  ? 1.95723 2.08167 2.15530 0.09819  -0.15613 0.05674  52  ASP A OD1 
481  O OD2 . ASP A 51  ? 1.89489 2.02920 2.05932 0.14346  -0.17011 0.05997  52  ASP A OD2 
486  N N   . VAL A 52  ? 1.77058 1.86955 1.98927 0.05093  -0.10042 0.07594  53  VAL A N   
487  C CA  . VAL A 52  ? 1.73819 1.81158 1.93999 0.03143  -0.08833 0.07241  53  VAL A CA  
488  C C   . VAL A 52  ? 1.72291 1.80562 1.94605 0.02028  -0.11746 0.05660  53  VAL A C   
489  O O   . VAL A 52  ? 1.75416 1.86585 2.02236 0.01334  -0.14031 0.05213  53  VAL A O   
490  C CB  . VAL A 52  ? 1.75993 1.83181 1.98251 0.00771  -0.06391 0.08362  53  VAL A CB  
491  C CG1 . VAL A 52  ? 1.85135 1.95671 2.13502 -0.01076 -0.08093 0.08295  53  VAL A CG1 
492  C CG2 . VAL A 52  ? 1.73908 1.78317 1.93712 -0.00940 -0.04833 0.08126  53  VAL A CG2 
502  N N   . THR A 53  ? 1.71011 1.76816 1.90025 0.01850  -0.11629 0.04745  54  THR A N   
503  C CA  . THR A 53  ? 1.65923 1.72044 1.86498 0.00793  -0.14092 0.03164  54  THR A CA  
504  C C   . THR A 53  ? 1.68133 1.72098 1.87853 -0.01221 -0.12590 0.03048  54  THR A C   
505  O O   . THR A 53  ? 1.75913 1.77492 1.91688 -0.01034 -0.09985 0.03573  54  THR A O   
506  C CB  . THR A 53  ? 1.82575 1.88122 1.99988 0.02796  -0.15881 0.01787  54  THR A CB  
507  O OG1 . THR A 53  ? 2.11734 2.19950 2.31015 0.04314  -0.18053 0.01625  54  THR A OG1 
508  C CG2 . THR A 53  ? 1.81149 1.86120 1.99137 0.01646  -0.17700 0.00080  54  THR A CG2 
516  N N   . VAL A 54  ? 1.60795 1.65593 1.84148 -0.03153 -0.14257 0.02352  55  VAL A N   
517  C CA  . VAL A 54  ? 1.61961 1.65018 1.85036 -0.05057 -0.13302 0.02149  55  VAL A CA  
518  C C   . VAL A 54  ? 1.56973 1.59455 1.79770 -0.04928 -0.15708 0.00247  55  VAL A C   
519  O O   . VAL A 54  ? 1.56484 1.60595 1.82183 -0.04896 -0.18518 -0.00687 55  VAL A O   
520  C CB  . VAL A 54  ? 1.66713 1.70921 1.94253 -0.07601 -0.13041 0.03101  55  VAL A CB  
521  C CG1 . VAL A 54  ? 1.72857 1.75256 1.99899 -0.09452 -0.12047 0.02992  55  VAL A CG1 
522  C CG2 . VAL A 54  ? 1.59133 1.64206 1.87231 -0.07711 -0.10738 0.04841  55  VAL A CG2 
532  N N   . TYR A 55  ? 1.55174 1.55425 1.74497 -0.04894 -0.14561 -0.00403 56  TYR A N   
533  C CA  . TYR A 55  ? 1.55864 1.55385 1.74687 -0.04797 -0.16512 -0.02300 56  TYR A CA  
534  C C   . TYR A 55  ? 1.49213 1.47775 1.69527 -0.06878 -0.16048 -0.02367 56  TYR A C   
535  O O   . TYR A 55  ? 1.51788 1.49045 1.69951 -0.07546 -0.13449 -0.01596 56  TYR A O   
536  C CB  . TYR A 55  ? 1.79552 1.77476 1.93054 -0.02963 -0.15752 -0.03250 56  TYR A CB  
537  C CG  . TYR A 55  ? 1.97047 1.95755 2.08760 -0.00778 -0.16497 -0.03271 56  TYR A CG  
538  C CD1 . TYR A 55  ? 1.94328 1.94689 2.07996 0.00016  -0.19561 -0.04451 56  TYR A CD1 
539  C CD2 . TYR A 55  ? 1.99248 1.96975 2.07198 0.00491  -0.14152 -0.02112 56  TYR A CD2 
540  C CE1 . TYR A 55  ? 1.96749 1.98016 2.08768 0.02042  -0.20335 -0.04436 56  TYR A CE1 
541  C CE2 . TYR A 55  ? 2.10626 2.08977 2.16837 0.02606  -0.14921 -0.02037 56  TYR A CE2 
542  C CZ  . TYR A 55  ? 2.12474 2.12719 2.20773 0.03389  -0.18050 -0.03185 56  TYR A CZ  
543  O OH  . TYR A 55  ? 1.92086 1.93149 1.98667 0.05514  -0.18914 -0.03083 56  TYR A OH  
553  N N   . GLU A 56  ? 1.52118 1.51282 1.76002 -0.07892 -0.18579 -0.03295 57  GLU A N   
554  C CA  . GLU A 56  ? 1.42980 1.41340 1.68880 -0.09864 -0.18601 -0.03277 57  GLU A CA  
555  C C   . GLU A 56  ? 1.49534 1.47123 1.75660 -0.09573 -0.20951 -0.05335 57  GLU A C   
556  O O   . GLU A 56  ? 1.70728 1.69147 1.98204 -0.08840 -0.23464 -0.06506 57  GLU A O   
557  C CB  . GLU A 56  ? 1.51187 1.50906 1.81839 -0.11789 -0.19307 -0.02068 57  GLU A CB  
558  C CG  . GLU A 56  ? 1.63134 1.62056 1.96406 -0.13841 -0.20100 -0.02135 57  GLU A CG  
559  C CD  . GLU A 56  ? 1.62952 1.60476 1.94161 -0.14703 -0.17543 -0.01394 57  GLU A CD  
560  O OE1 . GLU A 56  ? 1.60460 1.57695 1.88455 -0.13997 -0.14943 -0.00657 57  GLU A OE1 
561  O OE2 . GLU A 56  ? 1.62425 1.59119 1.95174 -0.16098 -0.18138 -0.01543 57  GLU A OE2 
568  N N   . ARG A 57  ? 1.35911 1.32015 1.60788 -0.10165 -0.20128 -0.05829 58  ARG A N   
569  C CA  . ARG A 57  ? 1.45896 1.41167 1.70724 -0.09711 -0.22152 -0.07909 58  ARG A CA  
570  C C   . ARG A 57  ? 1.46710 1.42085 1.76085 -0.11121 -0.24678 -0.08243 58  ARG A C   
571  O O   . ARG A 57  ? 1.40164 1.35199 1.70298 -0.10572 -0.27043 -0.10045 58  ARG A O   
572  C CB  . ARG A 57  ? 1.57562 1.51417 1.79427 -0.09703 -0.20398 -0.08453 58  ARG A CB  
573  C CG  . ARG A 57  ? 1.65534 1.58821 1.89546 -0.11599 -0.19839 -0.07639 58  ARG A CG  
574  C CD  . ARG A 57  ? 1.85507 1.77783 2.06353 -0.11416 -0.18043 -0.08298 58  ARG A CD  
575  N NE  . ARG A 57  ? 1.84935 1.77009 2.06733 -0.13188 -0.16343 -0.06823 58  ARG A NE  
576  C CZ  . ARG A 57  ? 1.88047 1.79575 2.07554 -0.13432 -0.14549 -0.07058 58  ARG A CZ  
577  N NH1 . ARG A 57  ? 1.93402 1.84501 2.09521 -0.12074 -0.14142 -0.08760 58  ARG A NH1 
578  N NH2 . ARG A 57  ? 1.91158 1.82724 2.11773 -0.15160 -0.13115 -0.05592 58  ARG A NH2 
592  N N   . ASP A 58  ? 1.68903 1.64622 2.01197 -0.12997 -0.24206 -0.06581 59  ASP A N   
593  C CA  . ASP A 58  ? 1.70547 1.66185 2.07025 -0.14499 -0.26578 -0.06746 59  ASP A CA  
594  C C   . ASP A 58  ? 1.55561 1.52268 1.93747 -0.13805 -0.29220 -0.07876 59  ASP A C   
595  O O   . ASP A 58  ? 1.53517 1.51799 1.91255 -0.12950 -0.28987 -0.07474 59  ASP A O   
596  C CB  . ASP A 58  ? 1.67648 1.63873 2.06806 -0.16642 -0.25551 -0.04621 59  ASP A CB  
597  C CG  . ASP A 58  ? 1.60148 1.55308 1.98169 -0.17694 -0.23333 -0.03599 59  ASP A CG  
598  O OD1 . ASP A 58  ? 1.67410 1.61280 2.03512 -0.17048 -0.23228 -0.04708 59  ASP A OD1 
599  O OD2 . ASP A 58  ? 1.67244 1.63019 2.06332 -0.19201 -0.21687 -0.01747 59  ASP A OD2 
604  N N   . LYS A 59  ? 1.60778 1.56626 2.00939 -0.14173 -0.31758 -0.09315 60  LYS A N   
605  C CA  . LYS A 59  ? 1.66968 1.63660 2.08105 -0.13336 -0.34279 -0.10840 60  LYS A CA  
606  C C   . LYS A 59  ? 1.65337 1.64007 2.09570 -0.14356 -0.35129 -0.09803 60  LYS A C   
607  O O   . LYS A 59  ? 1.86469 1.86803 2.30539 -0.13265 -0.36099 -0.10403 60  LYS A O   
608  C CB  . LYS A 59  ? 1.78161 1.73223 2.20671 -0.13601 -0.36680 -0.12670 60  LYS A CB  
609  C CG  . LYS A 59  ? 2.10668 2.06376 2.53242 -0.12446 -0.39064 -0.14681 60  LYS A CG  
610  C CD  . LYS A 59  ? 2.13281 2.07070 2.55976 -0.12147 -0.40880 -0.16820 60  LYS A CD  
611  C CE  . LYS A 59  ? 1.90447 1.84979 2.33041 -0.11072 -0.43134 -0.18894 60  LYS A CE  
612  N NZ  . LYS A 59  ? 2.18269 2.10903 2.60836 -0.10660 -0.44809 -0.21162 60  LYS A NZ  
626  N N   . ASP A 60  ? 1.41568 1.40259 1.88618 -0.16469 -0.34796 -0.08280 61  ASP A N   
627  C CA  . ASP A 60  ? 1.46199 1.46997 1.96252 -0.17619 -0.35406 -0.07294 61  ASP A CA  
628  C C   . ASP A 60  ? 1.62340 1.63341 2.13711 -0.19489 -0.33413 -0.05105 61  ASP A C   
629  O O   . ASP A 60  ? 1.72909 1.72247 2.23356 -0.20173 -0.32033 -0.04442 61  ASP A O   
630  C CB  . ASP A 60  ? 1.39905 1.40673 1.93194 -0.18758 -0.38450 -0.08438 61  ASP A CB  
631  C CG  . ASP A 60  ? 1.40029 1.38221 1.94698 -0.20315 -0.39333 -0.08618 61  ASP A CG  
632  O OD1 . ASP A 60  ? 1.73691 1.71215 2.29101 -0.21852 -0.37913 -0.06990 61  ASP A OD1 
633  O OD2 . ASP A 60  ? 1.35016 1.31826 1.90023 -0.19999 -0.41477 -0.10389 61  ASP A OD2 
638  N N   . ARG A 61  ? 1.62968 1.66235 2.16577 -0.20351 -0.33286 -0.04039 62  ARG A N   
639  C CA  . ARG A 61  ? 1.47425 1.51255 2.02376 -0.22176 -0.31325 -0.02001 62  ARG A CA  
640  C C   . ARG A 61  ? 1.31402 1.33667 1.88763 -0.24684 -0.32111 -0.01499 62  ARG A C   
641  O O   . ARG A 61  ? 1.71929 1.74011 2.29728 -0.26237 -0.30294 0.00129  62  ARG A O   
642  C CB  . ARG A 61  ? 1.52427 1.59270 2.09555 -0.22531 -0.31274 -0.01231 62  ARG A CB  
643  C CG  . ARG A 61  ? 1.64837 1.72905 2.25491 -0.23756 -0.34075 -0.02051 62  ARG A CG  
644  C CD  . ARG A 61  ? 1.75802 1.87298 2.37897 -0.23207 -0.34214 -0.01829 62  ARG A CD  
645  N NE  . ARG A 61  ? 1.91697 2.04805 2.55610 -0.24795 -0.32387 -0.00035 62  ARG A NE  
646  C CZ  . ARG A 61  ? 1.87463 2.03263 2.51655 -0.23919 -0.31203 0.00669  62  ARG A CZ  
647  N NH1 . ARG A 61  ? 1.83812 2.00930 2.46370 -0.21369 -0.31578 -0.00097 62  ARG A NH1 
648  N NH2 . ARG A 61  ? 1.78556 1.95758 2.44677 -0.25617 -0.29602 0.02174  62  ARG A NH2 
662  N N   . ASP A 62  ? 1.29932 1.30965 1.88752 -0.25139 -0.34750 -0.02837 63  ASP A N   
663  C CA  . ASP A 62  ? 1.28250 1.27381 1.89131 -0.27399 -0.35671 -0.02376 63  ASP A CA  
664  C C   . ASP A 62  ? 1.24345 1.20976 1.83141 -0.27104 -0.34658 -0.02282 63  ASP A C   
665  O O   . ASP A 62  ? 1.35242 1.30141 1.95456 -0.28851 -0.35244 -0.01714 63  ASP A O   
666  C CB  . ASP A 62  ? 1.37003 1.35366 1.99990 -0.27926 -0.38842 -0.03910 63  ASP A CB  
667  C CG  . ASP A 62  ? 1.50281 1.51383 2.15355 -0.28236 -0.40000 -0.04212 63  ASP A CG  
668  O OD1 . ASP A 62  ? 1.43082 1.46477 2.09174 -0.29019 -0.38561 -0.02809 63  ASP A OD1 
669  O OD2 . ASP A 62  ? 1.67940 1.69037 2.33658 -0.27693 -0.42320 -0.05914 63  ASP A OD2 
674  N N   . ALA A 63  ? 1.21992 1.18427 1.77432 -0.24982 -0.33203 -0.02836 64  ALA A N   
675  C CA  . ALA A 63  ? 1.60463 1.54937 2.13847 -0.24678 -0.32077 -0.02826 64  ALA A CA  
676  C C   . ALA A 63  ? 1.60371 1.54820 2.14376 -0.26672 -0.30049 -0.00692 64  ALA A C   
677  O O   . ALA A 63  ? 1.43089 1.39183 1.96661 -0.27000 -0.27915 0.00653  64  ALA A O   
678  C CB  . ALA A 63  ? 1.78882 1.73560 2.28379 -0.22245 -0.30530 -0.03677 64  ALA A CB  
684  N N   . ARG A 64  ? 1.45261 1.37828 2.00257 -0.27988 -0.30725 -0.00388 65  ARG A N   
685  C CA  . ARG A 64  ? 1.40193 1.32668 1.95765 -0.30024 -0.28974 0.01615  65  ARG A CA  
686  C C   . ARG A 64  ? 1.36620 1.29178 1.88926 -0.29083 -0.26156 0.02046  65  ARG A C   
687  O O   . ARG A 64  ? 1.31184 1.22815 1.81143 -0.27298 -0.26154 0.00696  65  ARG A O   
688  C CB  . ARG A 64  ? 1.50130 1.40444 2.07634 -0.31639 -0.30740 0.01833  65  ARG A CB  
689  C CG  . ARG A 64  ? 1.64679 1.54665 2.25452 -0.33182 -0.33290 0.01726  65  ARG A CG  
690  C CD  . ARG A 64  ? 2.00401 1.87823 2.62713 -0.34771 -0.34901 0.02105  65  ARG A CD  
691  N NE  . ARG A 64  ? 2.26456 2.13137 2.91571 -0.36220 -0.37457 0.01792  65  ARG A NE  
692  C CZ  . ARG A 64  ? 2.44645 2.28811 3.11304 -0.37687 -0.39293 0.02020  65  ARG A CZ  
693  N NH1 . ARG A 64  ? 2.37074 2.19327 3.02941 -0.37817 -0.38993 0.02602  65  ARG A NH1 
694  N NH2 . ARG A 64  ? 2.45366 2.28905 3.14356 -0.39064 -0.41497 0.01655  65  ARG A NH2 
708  N N   . ILE A 65  ? 1.41310 1.35037 1.93449 -0.30393 -0.23701 0.03863  66  ILE A N   
709  C CA  . ILE A 65  ? 1.18289 1.12142 1.67411 -0.29949 -0.20774 0.04481  66  ILE A CA  
710  C C   . ILE A 65  ? 1.16723 1.09490 1.66419 -0.31734 -0.20391 0.05512  66  ILE A C   
711  O O   . ILE A 65  ? 1.40257 1.33376 1.92124 -0.34063 -0.20168 0.07104  66  ILE A O   
712  C CB  . ILE A 65  ? 1.11915 1.07617 1.60321 -0.30272 -0.18157 0.05801  66  ILE A CB  
713  C CG1 . ILE A 65  ? 1.26444 1.23360 1.74728 -0.28561 -0.18854 0.04930  66  ILE A CG1 
714  C CG2 . ILE A 65  ? 1.36588 1.32184 1.81463 -0.29703 -0.15095 0.06225  66  ILE A CG2 
715  C CD1 . ILE A 65  ? 1.21085 1.19775 1.68817 -0.28627 -0.16439 0.06161  66  ILE A CD1 
727  N N   . PHE A 66  ? 1.32544 1.16874 1.30049 -0.37919 -0.08997 -0.17057 67  PHE A N   
728  C CA  . PHE A 66  ? 1.31547 1.17539 1.27582 -0.39342 -0.07287 -0.15904 67  PHE A CA  
729  C C   . PHE A 66  ? 1.42052 1.30118 1.35813 -0.41203 -0.03414 -0.15171 67  PHE A C   
730  O O   . PHE A 66  ? 1.29902 1.17933 1.21544 -0.40902 -0.01989 -0.15816 67  PHE A O   
731  C CB  . PHE A 66  ? 1.32733 1.18543 1.24562 -0.37494 -0.08625 -0.16642 67  PHE A CB  
732  C CG  . PHE A 66  ? 1.58656 1.46753 1.48666 -0.38795 -0.06836 -0.15380 67  PHE A CG  
733  C CD1 . PHE A 66  ? 1.60611 1.48911 1.53384 -0.39502 -0.07514 -0.14183 67  PHE A CD1 
734  C CD2 . PHE A 66  ? 1.48905 1.39106 1.34896 -0.39252 -0.04540 -0.15262 67  PHE A CD2 
735  C CE1 . PHE A 66  ? 1.47693 1.38477 1.38560 -0.40396 -0.05952 -0.12894 67  PHE A CE1 
736  C CE2 . PHE A 66  ? 1.36999 1.29694 1.21509 -0.40410 -0.03312 -0.14222 67  PHE A CE2 
737  C CZ  . PHE A 66  ? 1.44815 1.37916 1.31417 -0.40859 -0.04030 -0.13040 67  PHE A CZ  
747  N N   . GLY A 67  ? 1.60206 1.49968 1.54440 -0.42968 -0.01752 -0.13845 68  GLY A N   
748  C CA  . GLY A 67  ? 1.73363 1.64951 1.65059 -0.44664 0.01461  -0.13555 68  GLY A CA  
749  C C   . GLY A 67  ? 1.56544 1.48988 1.50833 -0.46102 0.03264  -0.11988 68  GLY A C   
750  O O   . GLY A 67  ? 1.59474 1.51246 1.58445 -0.45931 0.02337  -0.10734 68  GLY A O   
754  N N   . GLY A 68  ? 1.46878 1.40852 1.38141 -0.47390 0.05883  -0.12038 69  GLY A N   
755  C CA  . GLY A 68  ? 1.56771 1.51699 1.49047 -0.48261 0.08096  -0.10597 69  GLY A CA  
756  C C   . GLY A 68  ? 1.53587 1.47060 1.48563 -0.48313 0.09598  -0.10284 69  GLY A C   
757  O O   . GLY A 68  ? 1.48626 1.40438 1.45552 -0.47657 0.08505  -0.10988 69  GLY A O   
761  N N   . THR A 69  ? 1.64173 1.58451 1.59012 -0.48795 0.12231  -0.09075 70  THR A N   
762  C CA  . THR A 69  ? 1.44256 1.37430 1.41491 -0.48689 0.14279  -0.08366 70  THR A CA  
763  C C   . THR A 69  ? 1.35366 1.27527 1.28356 -0.49223 0.16267  -0.10443 70  THR A C   
764  O O   . THR A 69  ? 1.61282 1.53961 1.49688 -0.49942 0.16393  -0.12204 70  THR A O   
765  C CB  . THR A 69  ? 1.49121 1.43558 1.48054 -0.48450 0.16597  -0.05753 70  THR A CB  
766  O OG1 . THR A 69  ? 1.88890 1.84878 1.82105 -0.48729 0.18151  -0.06284 70  THR A OG1 
767  C CG2 . THR A 69  ? 1.42018 1.37164 1.46744 -0.47971 0.14868  -0.03285 70  THR A CG2 
775  N N   . LEU A 70  ? 1.37501 1.28217 1.32646 -0.48882 0.17815  -0.10113 71  LEU A N   
776  C CA  . LEU A 70  ? 1.58446 1.47619 1.50541 -0.49218 0.19894  -0.11874 71  LEU A CA  
777  C C   . LEU A 70  ? 1.73221 1.61876 1.64904 -0.49022 0.23322  -0.10947 71  LEU A C   
778  O O   . LEU A 70  ? 1.63407 1.52343 1.59473 -0.48222 0.24070  -0.08552 71  LEU A O   
779  C CB  . LEU A 70  ? 1.56458 1.44156 1.50946 -0.48482 0.18847  -0.12352 71  LEU A CB  
780  C CG  . LEU A 70  ? 1.47879 1.35667 1.41278 -0.48115 0.16065  -0.13611 71  LEU A CG  
781  C CD1 . LEU A 70  ? 1.61655 1.48254 1.57521 -0.46681 0.14965  -0.13627 71  LEU A CD1 
782  C CD2 . LEU A 70  ? 1.76876 1.64733 1.65632 -0.49066 0.16986  -0.15442 71  LEU A CD2 
794  N N   . ASP A 71  ? 1.82473 1.70331 1.69113 -0.49644 0.25349  -0.12844 72  ASP A N   
795  C CA  . ASP A 71  ? 1.60625 1.47507 1.45333 -0.49125 0.28750  -0.12549 72  ASP A CA  
796  C C   . ASP A 71  ? 1.62842 1.46934 1.47148 -0.49131 0.30656  -0.13941 72  ASP A C   
797  O O   . ASP A 71  ? 1.81936 1.64890 1.64354 -0.50074 0.30024  -0.16238 72  ASP A O   
798  C CB  . ASP A 71  ? 2.05918 1.93602 1.84671 -0.49557 0.29439  -0.14102 72  ASP A CB  
799  C CG  . ASP A 71  ? 2.37286 2.27793 2.16333 -0.48899 0.28717  -0.11914 72  ASP A CG  
800  O OD1 . ASP A 71  ? 2.34530 2.25601 2.16038 -0.47530 0.30562  -0.09066 72  ASP A OD1 
801  O OD2 . ASP A 71  ? 2.52056 2.44344 2.29308 -0.49620 0.26492  -0.12714 72  ASP A OD2 
806  N N   . LEU A 72  ? 1.49715 1.32805 1.36194 -0.47964 0.33210  -0.12246 73  LEU A N   
807  C CA  . LEU A 72  ? 1.91912 1.72303 1.78455 -0.47629 0.35427  -0.13071 73  LEU A CA  
808  C C   . LEU A 72  ? 1.99199 1.77519 1.80547 -0.47411 0.38668  -0.14658 73  LEU A C   
809  O O   . LEU A 72  ? 2.03501 1.82424 1.83743 -0.46223 0.40594  -0.13157 73  LEU A O   
810  C CB  . LEU A 72  ? 1.96167 1.76808 1.88684 -0.46282 0.36135  -0.10163 73  LEU A CB  
811  C CG  . LEU A 72  ? 1.56568 1.38713 1.54338 -0.46189 0.32652  -0.09057 73  LEU A CG  
812  C CD1 . LEU A 72  ? 1.65154 1.47417 1.68713 -0.44888 0.33447  -0.06617 73  LEU A CD1 
813  C CD2 . LEU A 72  ? 1.60268 1.41565 1.56105 -0.46784 0.30756  -0.11370 73  LEU A CD2 
825  N N   . HIS A 73  ? 1.95840 1.71629 1.74114 -0.48372 0.39286  -0.17647 74  HIS A N   
826  C CA  . HIS A 73  ? 1.98504 1.71486 1.71843 -0.48180 0.42069  -0.19858 74  HIS A CA  
827  C C   . HIS A 73  ? 2.14826 1.85492 1.89884 -0.46475 0.45604  -0.18329 74  HIS A C   
828  O O   . HIS A 73  ? 2.20426 1.91046 2.00303 -0.46010 0.45719  -0.16549 74  HIS A O   
829  C CB  . HIS A 73  ? 1.96707 1.67599 1.67515 -0.50036 0.41289  -0.23548 74  HIS A CB  
830  C CG  . HIS A 73  ? 2.63331 2.30668 2.29325 -0.50026 0.43669  -0.26513 74  HIS A CG  
831  N ND1 . HIS A 73  ? 2.82739 2.50257 2.43295 -0.49416 0.44073  -0.27866 74  HIS A ND1 
832  C CD2 . HIS A 73  ? 2.53192 2.16473 2.18849 -0.50355 0.45707  -0.28521 74  HIS A CD2 
833  C CE1 . HIS A 73  ? 2.61885 2.25423 2.18616 -0.49356 0.46001  -0.30940 74  HIS A CE1 
834  N NE2 . HIS A 73  ? 2.58126 2.18891 2.18175 -0.50064 0.47075  -0.31379 74  HIS A NE2 
841  N N   . ARG A 74  ? 2.15282 1.84099 1.86055 -0.45247 0.48503  -0.19024 75  ARG A N   
842  C CA  . ARG A 74  ? 2.08577 1.75694 1.80920 -0.43123 0.52225  -0.16885 75  ARG A CA  
843  C C   . ARG A 74  ? 2.08386 1.71870 1.81826 -0.43342 0.53893  -0.18224 75  ARG A C   
844  O O   . ARG A 74  ? 1.87512 1.50795 1.65281 -0.42006 0.55697  -0.15590 75  ARG A O   
845  C CB  . ARG A 74  ? 2.36764 2.02679 2.03311 -0.41255 0.55071  -0.17349 75  ARG A CB  
846  C CG  . ARG A 74  ? 2.56192 2.25960 2.22149 -0.40327 0.54252  -0.15006 75  ARG A CG  
847  C CD  . ARG A 74  ? 2.32532 2.01175 1.91845 -0.37833 0.57320  -0.15371 75  ARG A CD  
848  N NE  . ARG A 74  ? 2.37271 2.03863 1.97572 -0.35299 0.61661  -0.13185 75  ARG A NE  
849  C CZ  . ARG A 74  ? 2.59683 2.28729 2.24584 -0.33159 0.63877  -0.08202 75  ARG A CZ  
850  N NH1 . ARG A 74  ? 2.52309 2.25691 2.21585 -0.33304 0.62172  -0.04889 75  ARG A NH1 
851  N NH2 . ARG A 74  ? 2.74627 2.41704 2.40269 -0.30789 0.67995  -0.06339 75  ARG A NH2 
865  N N   . ASP A 75  ? 2.27227 1.87953 1.97334 -0.44966 0.53360  -0.22092 76  ASP A N   
866  C CA  . ASP A 75  ? 2.39660 1.96583 2.10971 -0.45133 0.55314  -0.23296 76  ASP A CA  
867  C C   . ASP A 75  ? 2.39420 1.97752 2.15993 -0.45976 0.53461  -0.22031 76  ASP A C   
868  O O   . ASP A 75  ? 2.53443 2.09078 2.31766 -0.45783 0.55259  -0.22280 76  ASP A O   
869  C CB  . ASP A 75  ? 2.47165 2.00247 2.13582 -0.46584 0.55563  -0.27972 76  ASP A CB  
870  C CG  . ASP A 75  ? 2.59394 2.09946 2.19700 -0.45083 0.57875  -0.29744 76  ASP A CG  
871  O OD1 . ASP A 75  ? 2.60812 2.10482 2.21259 -0.42588 0.61131  -0.27394 76  ASP A OD1 
872  O OD2 . ASP A 75  ? 2.68023 2.17592 2.23309 -0.46184 0.56391  -0.33453 76  ASP A OD2 
877  N N   . SER A 76  ? 2.30613 1.92937 2.09507 -0.46595 0.50063  -0.20637 77  SER A N   
878  C CA  . SER A 76  ? 2.11807 1.75494 1.94660 -0.46943 0.48066  -0.19680 77  SER A CA  
879  C C   . SER A 76  ? 2.02407 1.69786 1.89461 -0.45852 0.45945  -0.16486 77  SER A C   
880  O O   . SER A 76  ? 2.11396 1.78988 2.02228 -0.44297 0.46924  -0.14182 77  SER A O   
881  C CB  . SER A 76  ? 2.03083 1.67428 1.84288 -0.49006 0.45426  -0.22058 77  SER A CB  
882  O OG  . SER A 76  ? 2.01053 1.68088 1.80082 -0.49771 0.43033  -0.22452 77  SER A OG  
888  N N   . GLY A 77  ? 1.81748 1.52019 1.68464 -0.46641 0.42901  -0.16385 78  GLY A N   
889  C CA  . GLY A 77  ? 1.80149 1.53535 1.71273 -0.45841 0.40381  -0.13788 78  GLY A CA  
890  C C   . GLY A 77  ? 1.92541 1.66523 1.87262 -0.44268 0.42185  -0.10906 78  GLY A C   
891  O O   . GLY A 77  ? 1.94651 1.69753 1.94204 -0.43182 0.41316  -0.08908 78  GLY A O   
895  N N   . GLN A 78  ? 1.86037 1.59478 1.78507 -0.43903 0.44703  -0.10544 79  GLN A N   
896  C CA  . GLN A 78  ? 1.99321 1.73619 1.95612 -0.42203 0.46882  -0.07276 79  GLN A CA  
897  C C   . GLN A 78  ? 1.96970 1.69359 1.95423 -0.40919 0.49451  -0.06436 79  GLN A C   
898  O O   . GLN A 78  ? 1.83340 1.57416 1.87515 -0.39655 0.49662  -0.03393 79  GLN A O   
899  C CB  . GLN A 78  ? 2.01216 1.75056 1.93568 -0.41497 0.49667  -0.07036 79  GLN A CB  
900  C CG  . GLN A 78  ? 1.89532 1.65969 1.80662 -0.42180 0.47504  -0.06789 79  GLN A CG  
901  C CD  . GLN A 78  ? 2.19282 1.95966 2.07312 -0.40616 0.50556  -0.05453 79  GLN A CD  
902  O OE1 . GLN A 78  ? 2.12644 1.87870 2.00430 -0.38798 0.54280  -0.04116 79  GLN A OE1 
903  N NE2 . GLN A 78  ? 2.29111 2.07739 2.14548 -0.40966 0.49168  -0.05601 79  GLN A NE2 
912  N N   . GLU A 79  ? 1.92881 1.61816 1.87332 -0.41220 0.51390  -0.08997 80  GLU A N   
913  C CA  . GLU A 79  ? 1.93960 1.60863 1.90385 -0.39852 0.54117  -0.08095 80  GLU A CA  
914  C C   . GLU A 79  ? 1.93778 1.62769 1.95281 -0.39384 0.51547  -0.06592 80  GLU A C   
915  O O   . GLU A 79  ? 2.06115 1.75623 2.11719 -0.37712 0.52846  -0.04181 80  GLU A O   
916  C CB  . GLU A 79  ? 2.09626 1.72113 2.01229 -0.40480 0.56469  -0.11307 80  GLU A CB  
917  C CG  . GLU A 79  ? 2.20703 1.80559 2.14072 -0.38915 0.59869  -0.10338 80  GLU A CG  
918  C CD  . GLU A 79  ? 2.32957 1.92672 2.27811 -0.36756 0.63264  -0.07654 80  GLU A CD  
919  O OE1 . GLU A 79  ? 2.08934 1.68550 2.00867 -0.36460 0.64431  -0.07772 80  GLU A OE1 
920  O OE2 . GLU A 79  ? 2.42758 2.02717 2.41734 -0.35093 0.64863  -0.05173 80  GLU A OE2 
927  N N   . ALA A 80  ? 1.94129 1.64472 1.95218 -0.40561 0.47843  -0.07950 81  ALA A N   
928  C CA  . ALA A 80  ? 1.87107 1.59452 1.92076 -0.39655 0.45040  -0.06787 81  ALA A CA  
929  C C   . ALA A 80  ? 1.90799 1.66455 2.01451 -0.38818 0.42823  -0.04072 81  ALA A C   
930  O O   . ALA A 80  ? 1.89051 1.65983 2.04002 -0.37267 0.42150  -0.02275 81  ALA A O   
931  C CB  . ALA A 80  ? 1.69160 1.42108 1.71858 -0.40763 0.41766  -0.08805 81  ALA A CB  
937  N N   . MET A 81  ? 1.81566 1.58773 1.92738 -0.39777 0.41585  -0.03640 82  MET A N   
938  C CA  . MET A 81  ? 1.75607 1.55816 1.93317 -0.39216 0.39685  -0.00836 82  MET A CA  
939  C C   . MET A 81  ? 1.82015 1.62372 2.03538 -0.37711 0.43172  0.02037  82  MET A C   
940  O O   . MET A 81  ? 1.88407 1.71120 2.16610 -0.36753 0.41670  0.04445  82  MET A O   
941  C CB  . MET A 81  ? 1.71784 1.53363 1.89327 -0.40417 0.38451  -0.00585 82  MET A CB  
942  C CG  . MET A 81  ? 1.63800 1.45671 1.78300 -0.41751 0.34835  -0.02994 82  MET A CG  
943  S SD  . MET A 81  ? 1.46837 1.30551 1.65911 -0.41255 0.29339  -0.03070 82  MET A SD  
944  C CE  . MET A 81  ? 1.66526 1.48295 1.81247 -0.40383 0.29854  -0.05181 82  MET A CE  
954  N N   . LYS A 82  ? 1.76022 1.53886 1.93452 -0.37362 0.47735  0.01765  83  LYS A N   
955  C CA  . LYS A 82  ? 1.84292 1.61950 2.04684 -0.35563 0.51627  0.04551  83  LYS A CA  
956  C C   . LYS A 82  ? 1.90281 1.68094 2.14046 -0.34236 0.51536  0.05449  83  LYS A C   
957  O O   . LYS A 82  ? 1.87365 1.67710 2.17821 -0.32979 0.51345  0.08584  83  LYS A O   
958  C CB  . LYS A 82  ? 1.93057 1.67090 2.06940 -0.35141 0.56399  0.03217  83  LYS A CB  
959  C CG  . LYS A 82  ? 2.18430 1.91697 2.34398 -0.32890 0.61029  0.06013  83  LYS A CG  
960  C CD  . LYS A 82  ? 2.57891 2.26658 2.66380 -0.32244 0.65492  0.03855  83  LYS A CD  
961  C CE  . LYS A 82  ? 2.47875 2.16387 2.51093 -0.32916 0.65524  0.02392  83  LYS A CE  
962  N NZ  . LYS A 82  ? 2.39117 2.03515 2.35415 -0.31561 0.69964  0.00710  83  LYS A NZ  
976  N N   . ARG A 83  ? 1.92081 1.67445 2.11666 -0.34378 0.51703  0.02950  84  ARG A N   
977  C CA  . ARG A 83  ? 1.74166 1.49701 1.96371 -0.32709 0.51956  0.03992  84  ARG A CA  
978  C C   . ARG A 83  ? 1.82502 1.61925 2.10213 -0.32222 0.46964  0.05174  84  ARG A C   
979  O O   . ARG A 83  ? 1.96595 1.77648 2.28629 -0.30400 0.46760  0.07190  84  ARG A O   
980  C CB  . ARG A 83  ? 1.86369 1.58602 2.03338 -0.32936 0.53176  0.01338  84  ARG A CB  
981  C CG  . ARG A 83  ? 2.16033 1.87287 2.34611 -0.30774 0.55713  0.02781  84  ARG A CG  
982  C CD  . ARG A 83  ? 2.27889 1.94643 2.41576 -0.31102 0.59040  0.00583  84  ARG A CD  
983  N NE  . ARG A 83  ? 2.17830 1.81161 2.27448 -0.32324 0.62170  -0.01166 84  ARG A NE  
984  C CZ  . ARG A 83  ? 2.37340 1.96351 2.42634 -0.33237 0.64618  -0.03809 84  ARG A CZ  
985  N NH1 . ARG A 83  ? 2.27052 1.84623 2.32079 -0.33168 0.64813  -0.04588 84  ARG A NH1 
986  N NH2 . ARG A 83  ? 2.23120 1.79202 2.24428 -0.34094 0.66884  -0.05680 84  ARG A NH2 
1000 N N   . ALA A 84  ? 1.79575 1.60469 2.07159 -0.33672 0.42786  0.03849  85  ALA A N   
1001 C CA  . ALA A 84  ? 1.87804 1.71992 2.20594 -0.33257 0.37618  0.04541  85  ALA A CA  
1002 C C   . ALA A 84  ? 1.93017 1.80092 2.33432 -0.33338 0.36727  0.07480  85  ALA A C   
1003 O O   . ALA A 84  ? 2.04058 1.93860 2.50080 -0.33075 0.32215  0.08106  85  ALA A O   
1004 C CB  . ALA A 84  ? 1.81650 1.65852 2.11262 -0.34599 0.33604  0.01900  85  ALA A CB  
1010 N N   . GLY A 85  ? 1.81850 1.68370 2.22789 -0.33530 0.40875  0.09324  86  GLY A N   
1011 C CA  . GLY A 85  ? 1.77502 1.66942 2.26293 -0.33466 0.40668  0.12745  86  GLY A CA  
1012 C C   . GLY A 85  ? 1.87261 1.78138 2.38282 -0.35164 0.37439  0.12600  86  GLY A C   
1013 O O   . GLY A 85  ? 2.11189 2.04910 2.70505 -0.35273 0.36002  0.15455  86  GLY A O   
1017 N N   . LEU A 86  ? 1.70000 1.59068 2.14386 -0.36483 0.36338  0.09555  87  LEU A N   
1018 C CA  . LEU A 86  ? 1.75979 1.66218 2.21959 -0.37967 0.33160  0.09246  87  LEU A CA  
1019 C C   . LEU A 86  ? 1.73876 1.63083 2.15268 -0.38667 0.36455  0.09404  87  LEU A C   
1020 O O   . LEU A 86  ? 1.73123 1.63139 2.14859 -0.39784 0.34353  0.09179  87  LEU A O   
1021 C CB  . LEU A 86  ? 1.77987 1.67537 2.20399 -0.38631 0.28605  0.05808  87  LEU A CB  
1022 C CG  . LEU A 86  ? 1.77860 1.68553 2.23847 -0.37512 0.24539  0.05251  87  LEU A CG  
1023 C CD1 . LEU A 86  ? 1.82211 1.71855 2.23061 -0.37645 0.20833  0.01880  87  LEU A CD1 
1024 C CD2 . LEU A 86  ? 1.74191 1.67780 2.30273 -0.37560 0.21265  0.07611  87  LEU A CD2 
1036 N N   . LEU A 87  ? 1.75164 1.62539 2.12078 -0.37799 0.41509  0.09735  88  LEU A N   
1037 C CA  . LEU A 87  ? 1.84002 1.70172 2.14970 -0.38100 0.44350  0.09196  88  LEU A CA  
1038 C C   . LEU A 87  ? 1.72042 1.60880 2.08339 -0.38010 0.44496  0.12619  88  LEU A C   
1039 O O   . LEU A 87  ? 1.49942 1.39124 1.83527 -0.38874 0.43484  0.11900  88  LEU A O   
1040 C CB  . LEU A 87  ? 1.84585 1.68109 2.10402 -0.36738 0.49666  0.09013  88  LEU A CB  
1041 C CG  . LEU A 87  ? 2.02266 1.84043 2.20289 -0.36719 0.52393  0.07558  88  LEU A CG  
1042 C CD1 . LEU A 87  ? 1.85522 1.65955 1.97242 -0.38603 0.49611  0.03343  88  LEU A CD1 
1043 C CD2 . LEU A 87  ? 2.05380 1.84148 2.18729 -0.35010 0.57520  0.07293  88  LEU A CD2 
1055 N N   . GLN A 88  ? 1.80833 1.71799 2.25263 -0.36866 0.45888  0.16698  89  GLN A N   
1056 C CA  . GLN A 88  ? 1.79140 1.72812 2.29914 -0.36644 0.46456  0.20630  89  GLN A CA  
1057 C C   . GLN A 88  ? 1.69017 1.64327 2.24846 -0.38417 0.41066  0.20184  89  GLN A C   
1058 O O   . GLN A 88  ? 1.46625 1.43167 2.04048 -0.38718 0.41163  0.21899  89  GLN A O   
1059 C CB  . GLN A 88  ? 1.76841 1.72773 2.36669 -0.35121 0.48882  0.25389  89  GLN A CB  
1060 C CG  . GLN A 88  ? 1.66892 1.65544 2.33171 -0.34379 0.51012  0.30270  89  GLN A CG  
1061 C CD  . GLN A 88  ? 1.78989 1.76314 2.36574 -0.32941 0.55682  0.30485  89  GLN A CD  
1062 O OE1 . GLN A 88  ? 1.88600 1.84066 2.40216 -0.31041 0.60207  0.30386  89  GLN A OE1 
1063 N NE2 . GLN A 88  ? 1.66340 1.64503 2.22872 -0.33638 0.54500  0.30636  89  GLN A NE2 
1072 N N   . THR A 89  ? 1.67722 1.62956 2.25906 -0.39310 0.36425  0.17942  90  THR A N   
1073 C CA  . THR A 89  ? 1.58462 1.54508 2.20203 -0.40774 0.31072  0.16769  90  THR A CA  
1074 C C   . THR A 89  ? 1.54296 1.48798 2.07602 -0.41671 0.30625  0.13953  90  THR A C   
1075 O O   . THR A 89  ? 1.42078 1.37491 1.97951 -0.42494 0.28611  0.14608  90  THR A O   
1076 C CB  . THR A 89  ? 1.52367 1.48264 2.16253 -0.40935 0.26336  0.14386  90  THR A CB  
1077 O OG1 . THR A 89  ? 1.54636 1.52201 2.25703 -0.39912 0.26953  0.16924  90  THR A OG1 
1078 C CG2 . THR A 89  ? 1.66951 1.63545 2.35632 -0.42099 0.20621  0.13371  90  THR A CG2 
1086 N N   . TYR A 90  ? 1.63313 1.55527 2.07017 -0.41531 0.32493  0.10923  91  TYR A N   
1087 C CA  . TYR A 90  ? 1.56290 1.47377 1.92127 -0.42385 0.32205  0.08318  91  TYR A CA  
1088 C C   . TYR A 90  ? 1.54556 1.46766 1.89734 -0.42022 0.35074  0.10763  91  TYR A C   
1089 O O   . TYR A 90  ? 1.47621 1.40663 1.82467 -0.42741 0.33245  0.10692  91  TYR A O   
1090 C CB  . TYR A 90  ? 1.45983 1.34499 1.72985 -0.42329 0.34086  0.05006  91  TYR A CB  
1091 C CG  . TYR A 90  ? 1.46330 1.33911 1.65246 -0.43083 0.34772  0.02665  91  TYR A CG  
1092 C CD1 . TYR A 90  ? 1.53421 1.41371 1.70487 -0.44232 0.31194  0.00720  91  TYR A CD1 
1093 C CD2 . TYR A 90  ? 1.51843 1.38173 1.64853 -0.42471 0.38858  0.02273  91  TYR A CD2 
1094 C CE1 . TYR A 90  ? 1.48942 1.36511 1.59108 -0.44916 0.31651  -0.01268 91  TYR A CE1 
1095 C CE2 . TYR A 90  ? 1.50698 1.36439 1.56480 -0.43146 0.39009  -0.00110 91  TYR A CE2 
1096 C CZ  . TYR A 90  ? 1.43620 1.30209 1.48300 -0.44454 0.35383  -0.01748 91  TYR A CZ  
1097 O OH  . TYR A 90  ? 1.65496 1.51967 1.63485 -0.45122 0.35372  -0.03952 91  TYR A OH  
1107 N N   . TYR A 91  ? 1.65242 1.57525 2.00010 -0.40551 0.39774  0.13137  92  TYR A N   
1108 C CA  . TYR A 91  ? 1.59117 1.52718 1.93069 -0.39506 0.42899  0.15951  92  TYR A CA  
1109 C C   . TYR A 91  ? 1.57166 1.53526 2.01018 -0.39760 0.41162  0.19816  92  TYR A C   
1110 O O   . TYR A 91  ? 1.60283 1.57800 2.03348 -0.39644 0.41465  0.21120  92  TYR A O   
1111 C CB  . TYR A 91  ? 1.70925 1.64069 2.03232 -0.37320 0.48364  0.18162  92  TYR A CB  
1112 C CG  . TYR A 91  ? 1.69923 1.59913 1.91616 -0.36850 0.50734  0.14387  92  TYR A CG  
1113 C CD1 . TYR A 91  ? 1.68440 1.57136 1.81610 -0.37830 0.49490  0.10549  92  TYR A CD1 
1114 C CD2 . TYR A 91  ? 1.68340 1.56606 1.89060 -0.35437 0.54155  0.14692  92  TYR A CD2 
1115 C CE1 . TYR A 91  ? 1.62588 1.48269 1.67030 -0.37638 0.51313  0.06923  92  TYR A CE1 
1116 C CE2 . TYR A 91  ? 1.62250 1.47132 1.73849 -0.35089 0.56224  0.11063  92  TYR A CE2 
1117 C CZ  . TYR A 91  ? 1.59963 1.43516 1.63672 -0.36304 0.54659  0.07088  92  TYR A CZ  
1118 O OH  . TYR A 91  ? 1.66714 1.46773 1.62233 -0.36191 0.56383  0.03292  92  TYR A OH  
1128 N N   . ASP A 92  ? 1.51423 1.48907 2.05048 -0.40079 0.39220  0.21718  93  ASP A N   
1129 C CA  . ASP A 92  ? 1.44051 1.43950 2.08567 -0.40531 0.37361  0.25391  93  ASP A CA  
1130 C C   . ASP A 92  ? 1.40609 1.40170 2.04565 -0.42097 0.32963  0.23222  93  ASP A C   
1131 O O   . ASP A 92  ? 1.56488 1.57528 2.25370 -0.42173 0.32932  0.26067  93  ASP A O   
1132 C CB  . ASP A 92  ? 1.42912 1.43961 2.17906 -0.40837 0.35118  0.26935  93  ASP A CB  
1133 C CG  . ASP A 92  ? 1.50906 1.53049 2.28867 -0.39042 0.39876  0.30504  93  ASP A CG  
1134 O OD1 . ASP A 92  ? 1.61260 1.64064 2.37056 -0.37404 0.44869  0.33526  93  ASP A OD1 
1135 O OD2 . ASP A 92  ? 1.65651 1.68074 2.47826 -0.38966 0.38708  0.30385  93  ASP A OD2 
1140 N N   . LEU A 93  ? 1.39617 1.37234 1.97697 -0.43123 0.29517  0.18469  94  LEU A N   
1141 C CA  . LEU A 93  ? 1.51461 1.48558 2.08740 -0.44339 0.25257  0.16248  94  LEU A CA  
1142 C C   . LEU A 93  ? 1.56152 1.52604 2.03355 -0.44364 0.26601  0.14280  94  LEU A C   
1143 O O   . LEU A 93  ? 1.48678 1.45563 1.96287 -0.44886 0.24725  0.14360  94  LEU A O   
1144 C CB  . LEU A 93  ? 1.73148 1.68773 2.30136 -0.45022 0.20508  0.12481  94  LEU A CB  
1145 C CG  . LEU A 93  ? 1.75062 1.71463 2.42572 -0.45202 0.17043  0.13583  94  LEU A CG  
1146 C CD1 . LEU A 93  ? 1.57540 1.52422 2.22127 -0.45171 0.12759  0.09486  94  LEU A CD1 
1147 C CD2 . LEU A 93  ? 1.86930 1.84333 2.63645 -0.45994 0.14490  0.15839  94  LEU A CD2 
1159 N N   . ALA A 94  ? 1.63799 1.59216 2.02335 -0.43804 0.29659  0.12492  95  ALA A N   
1160 C CA  . ALA A 94  ? 1.56372 1.51318 1.85538 -0.43984 0.30349  0.10155  95  ALA A CA  
1161 C C   . ALA A 94  ? 1.50068 1.46876 1.78720 -0.42898 0.33305  0.13352  95  ALA A C   
1162 O O   . ALA A 94  ? 1.58224 1.56345 1.91998 -0.41618 0.36271  0.17388  95  ALA A O   
1163 C CB  . ALA A 94  ? 1.62992 1.56044 1.83878 -0.43798 0.32531  0.07140  95  ALA A CB  
1169 N N   . LEU A 95  ? 1.60237 1.57416 1.82640 -0.43166 0.32617  0.11769  96  LEU A N   
1170 C CA  . LEU A 95  ? 1.65193 1.64446 1.86450 -0.41886 0.34941  0.14702  96  LEU A CA  
1171 C C   . LEU A 95  ? 1.83715 1.82772 1.93848 -0.41219 0.36874  0.12153  96  LEU A C   
1172 O O   . LEU A 95  ? 1.93190 1.91583 1.97794 -0.42492 0.34394  0.08410  96  LEU A O   
1173 C CB  . LEU A 95  ? 1.54086 1.54462 1.79384 -0.42625 0.31858  0.15685  96  LEU A CB  
1174 C CG  . LEU A 95  ? 2.02459 2.02593 2.38838 -0.43527 0.28917  0.17381  96  LEU A CG  
1175 C CD1 . LEU A 95  ? 2.17886 2.18041 2.55917 -0.44395 0.25271  0.16717  96  LEU A CD1 
1176 C CD2 . LEU A 95  ? 1.75172 1.76961 2.20436 -0.42364 0.31821  0.22745  96  LEU A CD2 
1188 N N   . PRO A 96  ? 2.00088 1.99721 2.06681 -0.39121 0.41119  0.13961  97  PRO A N   
1189 C CA  . PRO A 96  ? 2.01879 2.01313 1.97662 -0.38326 0.42435  0.11172  97  PRO A CA  
1190 C C   . PRO A 96  ? 1.95068 1.96877 1.88079 -0.38147 0.41022  0.11585  97  PRO A C   
1191 O O   . PRO A 96  ? 1.87864 1.91815 1.86420 -0.37266 0.41421  0.15704  97  PRO A O   
1192 C CB  . PRO A 96  ? 2.08289 2.07851 2.01894 -0.35458 0.47407  0.13740  97  PRO A CB  
1193 C CG  . PRO A 96  ? 1.98958 1.98297 2.02165 -0.35281 0.48633  0.17135  97  PRO A CG  
1194 C CD  . PRO A 96  ? 2.07576 2.07958 2.19726 -0.37193 0.44883  0.18453  97  PRO A CD  
1202 N N   . MET A 97  ? 1.88463 1.89974 1.73338 -0.38977 0.39396  0.07443  98  MET A N   
1203 C CA  . MET A 97  ? 2.01427 2.05329 1.83521 -0.39056 0.37489  0.07346  98  MET A CA  
1204 C C   . MET A 97  ? 1.83847 1.88307 1.55560 -0.38218 0.38104  0.04313  98  MET A C   
1205 O O   . MET A 97  ? 1.74406 1.76607 1.41337 -0.39201 0.37809  0.00221  98  MET A O   
1206 C CB  . MET A 97  ? 2.06945 2.10331 1.91764 -0.41613 0.33139  0.05102  98  MET A CB  
1207 C CG  . MET A 97  ? 1.73215 1.76244 1.67896 -0.42258 0.31626  0.07751  98  MET A CG  
1208 S SD  . MET A 97  ? 2.02313 2.08062 2.01446 -0.41445 0.30793  0.11678  98  MET A SD  
1209 C CE  . MET A 97  ? 1.46870 1.53343 1.39542 -0.42749 0.27334  0.07875  98  MET A CE  
1219 N N   . GLY A 98  ? 1.82428 1.89910 1.50936 -0.36301 0.38877  0.06355  99  GLY A N   
1220 C CA  . GLY A 98  ? 1.99255 2.07895 1.58025 -0.35482 0.38531  0.03319  99  GLY A CA  
1221 C C   . GLY A 98  ? 1.83694 1.93240 1.40795 -0.37933 0.34368  0.00057  99  GLY A C   
1222 O O   . GLY A 98  ? 2.04724 2.13732 1.67525 -0.40037 0.31941  0.00046  99  GLY A O   
1226 N N   . VAL A 99  ? 1.92881 2.03932 1.41905 -0.37433 0.33472  -0.02778 100 VAL A N   
1227 C CA  . VAL A 99  ? 1.91966 2.04442 1.39084 -0.39580 0.29669  -0.05808 100 VAL A CA  
1228 C C   . VAL A 99  ? 1.97858 2.14359 1.38787 -0.37538 0.29300  -0.05320 100 VAL A C   
1229 O O   . VAL A 99  ? 2.21645 2.38678 1.56054 -0.35059 0.31210  -0.05764 100 VAL A O   
1230 C CB  . VAL A 99  ? 2.02205 2.11912 1.46396 -0.42028 0.28028  -0.11214 100 VAL A CB  
1231 C CG1 . VAL A 99  ? 1.99825 2.11527 1.42893 -0.44140 0.24280  -0.13800 100 VAL A CG1 
1232 C CG2 . VAL A 99  ? 2.06810 2.12791 1.56880 -0.43606 0.28620  -0.11352 100 VAL A CG2 
1242 N N   . ASN A 100 ? 1.92535 2.11908 1.35240 -0.38251 0.26881  -0.04332 101 ASN A N   
1243 C CA  . ASN A 100 ? 2.02557 2.26227 1.39637 -0.36609 0.25857  -0.04140 101 ASN A CA  
1244 C C   . ASN A 100 ? 1.89898 2.14704 1.25387 -0.39306 0.21857  -0.08128 101 ASN A C   
1245 O O   . ASN A 100 ? 2.01515 2.25239 1.42359 -0.41725 0.20038  -0.08479 101 ASN A O   
1246 C CB  . ASN A 100 ? 2.12051 2.38744 1.53041 -0.34613 0.26885  0.01362  101 ASN A CB  
1247 C CG  . ASN A 100 ? 2.21810 2.48677 1.63458 -0.31241 0.31137  0.05845  101 ASN A CG  
1248 O OD1 . ASN A 100 ? 2.27270 2.51879 1.66510 -0.30303 0.33423  0.04951  101 ASN A OD1 
1249 N ND2 . ASN A 100 ? 2.19100 2.48626 1.64397 -0.29250 0.32451  0.10978  101 ASN A ND2 
1256 N N   . ILE A 101 ? 1.88625 2.15674 1.16851 -0.38719 0.20446  -0.11114 102 ILE A N   
1257 C CA  . ILE A 101 ? 1.80044 2.09101 1.07070 -0.41077 0.16579  -0.14524 102 ILE A CA  
1258 C C   . ILE A 101 ? 1.81117 2.15612 1.06299 -0.39224 0.15441  -0.11939 102 ILE A C   
1259 O O   . ILE A 101 ? 2.27283 2.64400 1.46702 -0.36090 0.16568  -0.10828 102 ILE A O   
1260 C CB  . ILE A 101 ? 1.88652 2.16523 1.09676 -0.42048 0.15138  -0.20073 102 ILE A CB  
1261 C CG1 . ILE A 101 ? 1.92376 2.14630 1.15127 -0.43465 0.16829  -0.22242 102 ILE A CG1 
1262 C CG2 . ILE A 101 ? 1.84664 2.14931 1.06119 -0.44772 0.11038  -0.23205 102 ILE A CG2 
1263 C CD1 . ILE A 101 ? 2.08798 2.28727 1.38179 -0.46899 0.15474  -0.23300 102 ILE A CD1 
1275 N N   . ALA A 102 ? 1.76498 2.12737 1.06279 -0.40784 0.13390  -0.10805 103 ALA A N   
1276 C CA  . ALA A 102 ? 1.81921 2.23190 1.11006 -0.39064 0.12460  -0.07866 103 ALA A CA  
1277 C C   . ALA A 102 ? 1.93693 2.38084 1.21836 -0.41123 0.08589  -0.10795 103 ALA A C   
1278 O O   . ALA A 102 ? 2.06274 2.48658 1.35752 -0.44088 0.06786  -0.14568 103 ALA A O   
1279 C CB  . ALA A 102 ? 2.10166 2.50875 1.46186 -0.38526 0.13782  -0.03069 103 ALA A CB  
1285 N N   . ASP A 103 ? 2.00712 2.50299 1.26953 -0.39381 0.07478  -0.08689 104 ASP A N   
1286 C CA  . ASP A 103 ? 2.13075 2.66647 1.39342 -0.40939 0.03894  -0.10390 104 ASP A CA  
1287 C C   . ASP A 103 ? 1.91995 2.46912 1.23972 -0.40885 0.03794  -0.06516 104 ASP A C   
1288 O O   . ASP A 103 ? 1.90455 2.42978 1.26230 -0.39771 0.06190  -0.02963 104 ASP A O   
1289 C CB  . ASP A 103 ? 2.50141 3.09082 1.69299 -0.38807 0.02268  -0.11347 104 ASP A CB  
1290 C CG  . ASP A 103 ? 2.17065 2.79477 1.34216 -0.34696 0.04416  -0.06197 104 ASP A CG  
1291 O OD1 . ASP A 103 ? 2.06335 2.66809 1.28294 -0.33763 0.07124  -0.01892 104 ASP A OD1 
1292 O OD2 . ASP A 103 ? 2.18390 2.85526 1.29293 -0.32284 0.03315  -0.06447 104 ASP A OD2 
1297 N N   . GLU A 104 ? 1.93503 2.52235 1.26370 -0.42058 0.00903  -0.07261 105 GLU A N   
1298 C CA  . GLU A 104 ? 2.05669 2.65571 1.43491 -0.41803 0.00745  -0.03837 105 GLU A CA  
1299 C C   . GLU A 104 ? 1.98457 2.61377 1.35387 -0.38322 0.02397  0.00995  105 GLU A C   
1300 O O   . GLU A 104 ? 1.98719 2.60929 1.40171 -0.37632 0.03214  0.04347  105 GLU A O   
1301 C CB  . GLU A 104 ? 2.15019 2.78710 1.54157 -0.43646 -0.02502 -0.05459 105 GLU A CB  
1302 C CG  . GLU A 104 ? 2.14523 2.85051 1.49358 -0.42340 -0.04688 -0.05506 105 GLU A CG  
1303 C CD  . GLU A 104 ? 2.28692 3.00022 1.57916 -0.42909 -0.06189 -0.09874 105 GLU A CD  
1304 O OE1 . GLU A 104 ? 2.09642 2.75980 1.38366 -0.44272 -0.05167 -0.12661 105 GLU A OE1 
1305 O OE2 . GLU A 104 ? 2.37550 3.14447 1.62751 -0.41847 -0.08504 -0.10629 105 GLU A OE2 
1312 N N   . LYS A 105 ? 1.96191 2.62293 1.27345 -0.35883 0.02979  0.01461  106 LYS A N   
1313 C CA  . LYS A 105 ? 2.02809 2.72279 1.32871 -0.32174 0.04850  0.06425  106 LYS A CA  
1314 C C   . LYS A 105 ? 2.06313 2.71999 1.38397 -0.30277 0.08815  0.09826  106 LYS A C   
1315 O O   . LYS A 105 ? 2.09053 2.77045 1.41205 -0.27067 0.10971  0.14525  106 LYS A O   
1316 C CB  . LYS A 105 ? 2.20494 2.95790 1.42942 -0.29864 0.03576  0.05600  106 LYS A CB  
1317 C CG  . LYS A 105 ? 2.19805 2.99863 1.41146 -0.31561 -0.00644 0.02794  106 LYS A CG  
1318 C CD  . LYS A 105 ? 2.52346 3.37187 1.65694 -0.29876 -0.02699 0.00245  106 LYS A CD  
1319 C CE  . LYS A 105 ? 2.59077 3.48941 1.72531 -0.31873 -0.07290 -0.02564 106 LYS A CE  
1320 N NZ  . LYS A 105 ? 3.00876 3.96041 2.06505 -0.29864 -0.09867 -0.04972 106 LYS A NZ  
1334 N N   . GLY A 106 ? 2.07419 2.67573 1.41726 -0.32109 0.09914  0.07882  107 GLY A N   
1335 C CA  . GLY A 106 ? 2.16258 2.72922 1.53609 -0.30620 0.13494  0.11102  107 GLY A CA  
1336 C C   . GLY A 106 ? 2.04195 2.61019 1.36043 -0.28340 0.15831  0.11024  107 GLY A C   
1337 O O   . GLY A 106 ? 2.05180 2.59605 1.39885 -0.26804 0.19168  0.14250  107 GLY A O   
1341 N N   . ASN A 107 ? 2.12937 2.72473 1.37168 -0.27922 0.14153  0.07467  108 ASN A N   
1342 C CA  . ASN A 107 ? 2.21276 2.80639 1.39107 -0.25369 0.16256  0.06848  108 ASN A CA  
1343 C C   . ASN A 107 ? 2.16211 2.69876 1.34937 -0.27705 0.16900  0.03301  108 ASN A C   
1344 O O   . ASN A 107 ? 2.29244 2.80505 1.50143 -0.31411 0.14399  -0.00725 108 ASN A O   
1345 C CB  . ASN A 107 ? 2.25906 2.90002 1.34805 -0.23917 0.13695  0.03731  108 ASN A CB  
1346 C CG  . ASN A 107 ? 2.29225 2.99571 1.36642 -0.21179 0.13081  0.07388  108 ASN A CG  
1347 O OD1 . ASN A 107 ? 2.29592 3.01112 1.39409 -0.18219 0.16247  0.13149  108 ASN A OD1 
1348 N ND2 . ASN A 107 ? 2.30195 3.04706 1.34225 -0.22155 0.09017  0.04244  108 ASN A ND2 
1354 N N   . ILE A 108 ? 2.08509 2.60176 1.25760 -0.25289 0.20524  0.05160  109 ILE A N   
1355 C CA  . ILE A 108 ? 2.08487 2.55050 1.25737 -0.26815 0.21597  0.02113  109 ILE A CA  
1356 C C   . ILE A 108 ? 2.13957 2.61151 1.21744 -0.26046 0.20169  -0.02912 109 ILE A C   
1357 O O   . ILE A 108 ? 2.35210 2.84903 1.36024 -0.22030 0.21750  -0.01781 109 ILE A O   
1358 C CB  . ILE A 108 ? 2.20601 2.64809 1.41304 -0.24509 0.26245  0.06666  109 ILE A CB  
1359 C CG1 . ILE A 108 ? 2.20394 2.62937 1.51540 -0.26123 0.26833  0.10480  109 ILE A CG1 
1360 C CG2 . ILE A 108 ? 2.13789 2.53461 1.32528 -0.25207 0.27618  0.03477  109 ILE A CG2 
1361 C CD1 . ILE A 108 ? 2.25850 2.66712 1.62293 -0.24023 0.31130  0.15626  109 ILE A CD1 
1373 N N   . LEU A 109 ? 2.09635 2.54453 1.17213 -0.29711 0.17169  -0.08478 110 LEU A N   
1374 C CA  . LEU A 109 ? 2.21526 2.66383 1.20892 -0.29474 0.15215  -0.13936 110 LEU A CA  
1375 C C   . LEU A 109 ? 2.31166 2.71739 1.26733 -0.27693 0.18396  -0.15040 110 LEU A C   
1376 O O   . LEU A 109 ? 2.50716 2.92205 1.37548 -0.24637 0.18652  -0.16996 110 LEU A O   
1377 C CB  . LEU A 109 ? 2.18365 2.62045 1.20017 -0.34113 0.11095  -0.19180 110 LEU A CB  
1378 C CG  . LEU A 109 ? 2.15673 2.63415 1.21687 -0.36037 0.08028  -0.18128 110 LEU A CG  
1379 C CD1 . LEU A 109 ? 2.13432 2.60372 1.21278 -0.40217 0.04200  -0.23308 110 LEU A CD1 
1380 C CD2 . LEU A 109 ? 2.18917 2.72983 1.19944 -0.32800 0.07017  -0.16038 110 LEU A CD2 
1392 N N   . THR A 110 ? 2.19344 2.55306 1.21079 -0.29276 0.20795  -0.13830 111 THR A N   
1393 C CA  . THR A 110 ? 2.32004 2.63883 1.31116 -0.27563 0.24172  -0.14314 111 THR A CA  
1394 C C   . THR A 110 ? 2.24946 2.54622 1.32218 -0.27433 0.27792  -0.09197 111 THR A C   
1395 O O   . THR A 110 ? 2.14910 2.44230 1.30211 -0.30124 0.26774  -0.07534 111 THR A O   
1396 C CB  . THR A 110 ? 2.42595 2.69935 1.40086 -0.30555 0.22429  -0.20617 111 THR A CB  
1397 O OG1 . THR A 110 ? 2.15623 2.41144 1.21196 -0.35020 0.20556  -0.21479 111 THR A OG1 
1398 C CG2 . THR A 110 ? 2.46346 2.75472 1.35627 -0.30419 0.18816  -0.26063 111 THR A CG2 
1406 N N   . THR A 111 ? 2.48332 2.76589 1.53494 -0.24092 0.31946  -0.06735 112 THR A N   
1407 C CA  . THR A 111 ? 2.40526 2.66650 1.53603 -0.23780 0.35536  -0.01984 112 THR A CA  
1408 C C   . THR A 111 ? 2.42638 2.63745 1.54873 -0.24378 0.37281  -0.04732 112 THR A C   
1409 O O   . THR A 111 ? 2.50678 2.70860 1.55391 -0.21311 0.39393  -0.05987 112 THR A O   
1410 C CB  . THR A 111 ? 2.47520 2.76706 1.60412 -0.19077 0.39534  0.04418  112 THR A CB  
1411 O OG1 . THR A 111 ? 2.45077 2.78631 1.60060 -0.18717 0.38078  0.07398  112 THR A OG1 
1412 C CG2 . THR A 111 ? 2.47293 2.74172 1.68930 -0.18805 0.43269  0.09149  112 THR A CG2 
1420 N N   . LYS A 112 ? 2.40932 2.58780 1.60539 -0.28009 0.36451  -0.05643 113 LYS A N   
1421 C CA  . LYS A 112 ? 2.48836 2.61912 1.68866 -0.28826 0.38102  -0.07898 113 LYS A CA  
1422 C C   . LYS A 112 ? 2.44178 2.56036 1.71575 -0.27650 0.41875  -0.02730 113 LYS A C   
1423 O O   . LYS A 112 ? 2.57918 2.66322 1.90080 -0.29646 0.42285  -0.03601 113 LYS A O   
1424 C CB  . LYS A 112 ? 2.43403 2.53762 1.66404 -0.33384 0.34736  -0.12469 113 LYS A CB  
1425 C CG  . LYS A 112 ? 2.42349 2.53997 1.59752 -0.35042 0.30796  -0.17501 113 LYS A CG  
1426 C CD  . LYS A 112 ? 2.72114 2.81351 1.93882 -0.39387 0.27979  -0.21026 113 LYS A CD  
1427 C CE  . LYS A 112 ? 2.85056 2.95350 2.02052 -0.41160 0.24258  -0.26128 113 LYS A CE  
1428 N NZ  . LYS A 112 ? 2.59214 2.66832 1.80649 -0.45093 0.22205  -0.29333 113 LYS A NZ  
1442 N N   . ASN A 113 ? 2.37922 2.52793 1.66748 -0.24357 0.44641  0.02842  114 ASN A N   
1443 C CA  . ASN A 113 ? 2.33960 2.48391 1.71253 -0.23270 0.48078  0.08417  114 ASN A CA  
1444 C C   . ASN A 113 ? 2.43435 2.53894 1.80879 -0.23063 0.50595  0.07242  114 ASN A C   
1445 O O   . ASN A 113 ? 2.54555 2.63946 1.84140 -0.20174 0.53041  0.05895  114 ASN A O   
1446 C CB  . ASN A 113 ? 2.40999 2.59105 1.77266 -0.18702 0.51664  0.14235  114 ASN A CB  
1447 C CG  . ASN A 113 ? 2.37834 2.56749 1.85722 -0.18410 0.54032  0.20774  114 ASN A CG  
1448 O OD1 . ASN A 113 ? 2.40571 2.57433 1.97046 -0.21683 0.52456  0.20647  114 ASN A OD1 
1449 N ND2 . ASN A 113 ? 2.53974 2.75989 2.02423 -0.14355 0.57742  0.26593  114 ASN A ND2 
1456 N N   . VAL A 114 ? 2.51930 2.60177 1.98083 -0.25906 0.49912  0.07686  115 VAL A N   
1457 C CA  . VAL A 114 ? 2.54416 2.58952 2.01908 -0.26134 0.51949  0.06627  115 VAL A CA  
1458 C C   . VAL A 114 ? 2.61165 2.65783 2.05158 -0.21624 0.57077  0.09776  115 VAL A C   
1459 O O   . VAL A 114 ? 2.87836 2.95220 2.36092 -0.19017 0.59914  0.15691  115 VAL A O   
1460 C CB  . VAL A 114 ? 2.46604 2.50205 2.05629 -0.28615 0.51205  0.08974  115 VAL A CB  
1461 C CG1 . VAL A 114 ? 2.50286 2.51071 2.11652 -0.27813 0.54309  0.09683  115 VAL A CG1 
1462 C CG2 . VAL A 114 ? 2.53158 2.55602 2.14037 -0.32668 0.46517  0.04948  115 VAL A CG2 
1472 N N   . LYS A 115 ? 2.73728 2.75190 2.10184 -0.20504 0.58467  0.06005  116 LYS A N   
1473 C CA  . LYS A 115 ? 2.72733 2.73516 2.06323 -0.16117 0.63658  0.08929  116 LYS A CA  
1474 C C   . LYS A 115 ? 2.67698 2.67727 2.12062 -0.16551 0.66161  0.13364  116 LYS A C   
1475 O O   . LYS A 115 ? 2.60956 2.59104 2.11580 -0.20256 0.63769  0.11643  116 LYS A O   
1476 C CB  . LYS A 115 ? 2.71346 2.68125 1.94621 -0.14990 0.64308  0.03319  116 LYS A CB  
1477 C CG  . LYS A 115 ? 2.77486 2.74556 1.90172 -0.14861 0.61250  -0.02034 116 LYS A CG  
1478 C CD  . LYS A 115 ? 2.84143 2.76339 1.88321 -0.14244 0.61652  -0.07899 116 LYS A CD  
1479 C CE  . LYS A 115 ? 2.93660 2.86074 1.87183 -0.13788 0.58490  -0.13474 116 LYS A CE  
1480 N NZ  . LYS A 115 ? 3.04654 2.92021 1.89343 -0.12233 0.59424  -0.18865 116 LYS A NZ  
1494 N N   . PRO A 116 ? 2.65416 2.67130 2.12310 -0.12614 0.70990  0.19282  117 PRO A N   
1495 C CA  . PRO A 116 ? 2.59736 2.60756 2.16879 -0.12887 0.73454  0.23311  117 PRO A CA  
1496 C C   . PRO A 116 ? 2.51586 2.48064 2.06538 -0.14022 0.73774  0.19195  117 PRO A C   
1497 O O   . PRO A 116 ? 2.41590 2.37089 2.05330 -0.16556 0.72909  0.19951  117 PRO A O   
1498 C CB  . PRO A 116 ? 2.52610 2.56198 2.10317 -0.07601 0.79226  0.30003  117 PRO A CB  
1499 C CG  . PRO A 116 ? 2.65471 2.69903 2.10254 -0.04009 0.80141  0.28159  117 PRO A CG  
1500 C CD  . PRO A 116 ? 2.57641 2.62352 1.98856 -0.07581 0.74475  0.23015  117 PRO A CD  
1508 N N   . GLU A 117 ? 2.70079 2.63657 2.13420 -0.12107 0.74841  0.14693  118 GLU A N   
1509 C CA  . GLU A 117 ? 2.59638 2.48454 2.00456 -0.12742 0.75690  0.10877  118 GLU A CA  
1510 C C   . GLU A 117 ? 2.47249 2.33696 1.90077 -0.17887 0.70842  0.05581  118 GLU A C   
1511 O O   . GLU A 117 ? 2.45787 2.28923 1.90807 -0.19101 0.71415  0.03933  118 GLU A O   
1512 C CB  . GLU A 117 ? 2.92764 2.78760 2.20333 -0.09054 0.77994  0.07234  118 GLU A CB  
1513 C CG  . GLU A 117 ? 3.05170 2.91740 2.23187 -0.09440 0.74446  0.02378  118 GLU A CG  
1514 C CD  . GLU A 117 ? 2.98068 2.82149 2.02876 -0.05106 0.76654  -0.00932 118 GLU A CD  
1515 O OE1 . GLU A 117 ? 3.08109 2.90164 2.10916 -0.01307 0.81477  0.01157  118 GLU A OE1 
1516 O OE2 . GLU A 117 ? 3.03987 2.88171 2.00372 -0.05341 0.73460  -0.05676 118 GLU A OE2 
1523 N N   . ASN A 118 ? 2.44125 2.32289 1.86281 -0.20640 0.66371  0.03177  119 ASN A N   
1524 C CA  . ASN A 118 ? 2.66511 2.53037 2.11296 -0.25242 0.61947  -0.01055 119 ASN A CA  
1525 C C   . ASN A 118 ? 2.51516 2.40768 2.06908 -0.27845 0.59379  0.02109  119 ASN A C   
1526 O O   . ASN A 118 ? 2.18576 2.07233 1.76053 -0.31283 0.55506  -0.00848 119 ASN A O   
1527 C CB  . ASN A 118 ? 2.62947 2.49193 1.99443 -0.26595 0.58504  -0.06496 119 ASN A CB  
1528 C CG  . ASN A 118 ? 2.78687 2.61433 2.04760 -0.24535 0.60098  -0.10885 119 ASN A CG  
1529 O OD1 . ASN A 118 ? 2.96858 2.80856 2.14981 -0.21699 0.60736  -0.11490 119 ASN A OD1 
1530 N ND2 . ASN A 118 ? 2.55972 2.34179 1.81896 -0.25744 0.60708  -0.14042 119 ASN A ND2 
1531 N N   . ARG A 119 ? 2.53002 2.45107 2.15324 -0.26113 0.61505  0.08093  120 ARG A N   
1532 C CA  . ARG A 119 ? 2.35225 2.29805 2.07616 -0.28344 0.58813  0.10996  120 ARG A CA  
1533 C C   . ARG A 119 ? 2.23779 2.16338 2.02649 -0.31208 0.56681  0.09548  120 ARG A C   
1534 O O   . ARG A 119 ? 1.99761 1.93133 1.83475 -0.33849 0.52788  0.08892  120 ARG A O   
1535 C CB  . ARG A 119 ? 2.25912 2.23588 2.05141 -0.25723 0.62003  0.17862  120 ARG A CB  
1536 C CG  . ARG A 119 ? 2.15944 2.15601 2.07340 -0.27762 0.59701  0.21302  120 ARG A CG  
1537 C CD  . ARG A 119 ? 2.16136 2.18652 2.15230 -0.25091 0.63402  0.28374  120 ARG A CD  
1538 N NE  . ARG A 119 ? 2.50079 2.53778 2.62249 -0.27160 0.61267  0.31413  120 ARG A NE  
1539 C CZ  . ARG A 119 ? 2.56132 2.61678 2.74349 -0.28668 0.58343  0.32950  120 ARG A CZ  
1540 N NH1 . ARG A 119 ? 2.60427 2.67265 2.73209 -0.28265 0.57473  0.32304  120 ARG A NH1 
1541 N NH2 . ARG A 119 ? 2.40742 2.46789 2.70787 -0.30540 0.56085  0.35068  120 ARG A NH2 
1555 N N   . PHE A 120 ? 2.12694 2.02600 1.91357 -0.30431 0.59206  0.09038  121 PHE A N   
1556 C CA  . PHE A 120 ? 1.90394 1.78630 1.74972 -0.32620 0.57520  0.08024  121 PHE A CA  
1557 C C   . PHE A 120 ? 1.96516 1.80952 1.74337 -0.33962 0.56749  0.02431  121 PHE A C   
1558 O O   . PHE A 120 ? 2.06392 1.88271 1.85174 -0.33727 0.58475  0.01826  121 PHE A O   
1559 C CB  . PHE A 120 ? 1.90957 1.79491 1.82482 -0.30810 0.60895  0.12427  121 PHE A CB  
1560 C CG  . PHE A 120 ? 1.99494 1.91810 1.99579 -0.29799 0.61546  0.18242  121 PHE A CG  
1561 C CD1 . PHE A 120 ? 2.09528 2.03567 2.19642 -0.31915 0.58136  0.19961  121 PHE A CD1 
1562 C CD2 . PHE A 120 ? 2.00461 1.94544 1.98631 -0.26571 0.65513  0.21984  121 PHE A CD2 
1563 C CE1 . PHE A 120 ? 1.99584 1.96837 2.18559 -0.31226 0.58558  0.25229  121 PHE A CE1 
1564 C CE2 . PHE A 120 ? 1.97628 1.95241 2.04648 -0.25647 0.66385  0.27778  121 PHE A CE2 
1565 C CZ  . PHE A 120 ? 1.90649 1.89750 2.08502 -0.28185 0.62829  0.29345  121 PHE A CZ  
1575 N N   . ASP A 121 ? 2.11221 1.95394 1.82741 -0.35356 0.54204  -0.01463 122 ASP A N   
1576 C CA  . ASP A 121 ? 2.29227 2.10140 1.95661 -0.37185 0.52800  -0.06770 122 ASP A CA  
1577 C C   . ASP A 121 ? 2.21266 2.02800 1.91261 -0.40257 0.48480  -0.08492 122 ASP A C   
1578 O O   . ASP A 121 ? 2.25899 2.05100 1.97265 -0.41626 0.47847  -0.10511 122 ASP A O   
1579 C CB  . ASP A 121 ? 2.39507 2.19642 1.96187 -0.36462 0.52959  -0.10254 122 ASP A CB  
1580 C CG  . ASP A 121 ? 2.50773 2.29321 2.02092 -0.32983 0.57355  -0.09525 122 ASP A CG  
1581 O OD1 . ASP A 121 ? 2.35349 2.13127 1.90689 -0.31316 0.60576  -0.06387 122 ASP A OD1 
1582 O OD2 . ASP A 121 ? 2.59283 2.37458 2.02236 -0.31693 0.57537  -0.12080 122 ASP A OD2 
1587 N N   . ASN A 122 ? 2.23799 2.08430 1.95262 -0.41055 0.45721  -0.07495 123 ASN A N   
1588 C CA  . ASN A 122 ? 2.08014 1.93333 1.82052 -0.43510 0.41705  -0.09056 123 ASN A CA  
1589 C C   . ASN A 122 ? 1.95112 1.83685 1.74615 -0.43528 0.39674  -0.05768 123 ASN A C   
1590 O O   . ASN A 122 ? 1.78780 1.69214 1.56361 -0.44283 0.37346  -0.06494 123 ASN A O   
1591 C CB  . ASN A 122 ? 2.12571 1.97449 1.80022 -0.44945 0.39866  -0.13282 123 ASN A CB  
1592 C CG  . ASN A 122 ? 2.40807 2.21945 2.03985 -0.45367 0.41375  -0.16931 123 ASN A CG  
1593 O OD1 . ASN A 122 ? 2.49803 2.28688 2.16038 -0.46028 0.41826  -0.17419 123 ASN A OD1 
1594 N ND2 . ASN A 122 ? 2.77294 2.57654 2.33399 -0.44799 0.42146  -0.19526 123 ASN A ND2 
1600 N N   . PRO A 123 ? 1.84844 1.74152 1.71601 -0.42723 0.40408  -0.02121 124 PRO A N   
1601 C CA  . PRO A 123 ? 1.70067 1.61947 1.63101 -0.42936 0.38195  0.00811  124 PRO A CA  
1602 C C   . PRO A 123 ? 1.75199 1.66812 1.70375 -0.44846 0.33965  -0.01250 124 PRO A C   
1603 O O   . PRO A 123 ? 1.92567 1.82295 1.85388 -0.45835 0.33055  -0.04272 124 PRO A O   
1604 C CB  . PRO A 123 ? 1.73244 1.65595 1.74036 -0.41715 0.40121  0.04861  124 PRO A CB  
1605 C CG  . PRO A 123 ? 1.61511 1.51310 1.61189 -0.41530 0.41911  0.03337  124 PRO A CG  
1606 C CD  . PRO A 123 ? 1.65410 1.53198 1.55545 -0.41624 0.43171  -0.00522 124 PRO A CD  
1614 N N   . GLU A 124 ? 1.74775 1.68197 1.74594 -0.45111 0.31533  0.00603  125 GLU A N   
1615 C CA  . GLU A 124 ? 1.73340 1.66667 1.74058 -0.46420 0.27495  -0.01287 125 GLU A CA  
1616 C C   . GLU A 124 ? 1.74484 1.67802 1.83660 -0.46420 0.25210  0.00532  125 GLU A C   
1617 O O   . GLU A 124 ? 1.59278 1.53967 1.74208 -0.45922 0.25263  0.03733  125 GLU A O   
1618 C CB  . GLU A 124 ? 1.92866 1.88061 1.90562 -0.46646 0.26157  -0.01378 125 GLU A CB  
1619 C CG  . GLU A 124 ? 2.19443 2.14889 2.08746 -0.46826 0.27419  -0.03830 125 GLU A CG  
1620 C CD  . GLU A 124 ? 2.47092 2.45086 2.33671 -0.46547 0.26656  -0.03113 125 GLU A CD  
1621 O OE1 . GLU A 124 ? 2.54706 2.53851 2.45680 -0.46511 0.24760  -0.01207 125 GLU A OE1 
1622 O OE2 . GLU A 124 ? 2.54814 2.53596 2.34864 -0.46253 0.27851  -0.04543 125 GLU A OE2 
1629 N N   . ILE A 125 ? 1.72544 1.64361 1.82656 -0.46856 0.23127  -0.01480 126 ILE A N   
1630 C CA  . ILE A 125 ? 1.47961 1.39585 1.65368 -0.46712 0.20278  -0.00570 126 ILE A CA  
1631 C C   . ILE A 125 ? 1.31696 1.22859 1.47879 -0.47086 0.16231  -0.02804 126 ILE A C   
1632 O O   . ILE A 125 ? 1.43119 1.33420 1.53811 -0.47281 0.15789  -0.05453 126 ILE A O   
1633 C CB  . ILE A 125 ? 1.36708 1.27190 1.56108 -0.46226 0.21130  -0.00815 126 ILE A CB  
1634 C CG1 . ILE A 125 ? 1.46084 1.36840 1.73628 -0.45932 0.17857  0.00268  126 ILE A CG1 
1635 C CG2 . ILE A 125 ? 1.42981 1.31840 1.56252 -0.46396 0.21007  -0.04080 126 ILE A CG2 
1636 C CD1 . ILE A 125 ? 1.55925 1.46394 1.86986 -0.45204 0.18950  0.01067  126 ILE A CD1 
1648 N N   . ASN A 126 ? 1.43921 1.35563 1.65448 -0.47056 0.13441  -0.01596 127 ASN A N   
1649 C CA  . ASN A 126 ? 1.38479 1.29327 1.59234 -0.46961 0.09448  -0.03631 127 ASN A CA  
1650 C C   . ASN A 126 ? 1.44154 1.33562 1.63697 -0.46288 0.07624  -0.05964 127 ASN A C   
1651 O O   . ASN A 126 ? 1.45971 1.35092 1.69028 -0.45894 0.07988  -0.05394 127 ASN A O   
1652 C CB  . ASN A 126 ? 1.54278 1.45223 1.82479 -0.46921 0.06691  -0.01948 127 ASN A CB  
1653 C CG  . ASN A 126 ? 1.60055 1.49460 1.88435 -0.46352 0.02102  -0.04317 127 ASN A CG  
1654 O OD1 . ASN A 126 ? 1.60043 1.48335 1.90245 -0.45664 -0.00262 -0.05736 127 ASN A OD1 
1655 N ND2 . ASN A 126 ? 1.70734 1.60100 1.97005 -0.46323 0.00812  -0.04708 127 ASN A ND2 
1662 N N   . ARG A 127 ? 1.48800 1.37545 1.63389 -0.45879 0.05817  -0.08307 128 ARG A N   
1663 C CA  . ARG A 127 ? 1.53336 1.40939 1.65667 -0.44777 0.04707  -0.10249 128 ARG A CA  
1664 C C   . ARG A 127 ? 1.46510 1.33399 1.64423 -0.43647 0.01415  -0.10286 128 ARG A C   
1665 O O   . ARG A 127 ? 1.40326 1.26862 1.58685 -0.42758 0.01647  -0.10645 128 ARG A O   
1666 C CB  . ARG A 127 ? 1.53616 1.40909 1.60357 -0.44160 0.03334  -0.12183 128 ARG A CB  
1667 C CG  . ARG A 127 ? 1.66168 1.54368 1.67549 -0.45308 0.06224  -0.12537 128 ARG A CG  
1668 C CD  . ARG A 127 ? 1.52636 1.40923 1.49611 -0.44595 0.04851  -0.13993 128 ARG A CD  
1669 N NE  . ARG A 127 ? 1.65183 1.54645 1.57958 -0.45901 0.07197  -0.14390 128 ARG A NE  
1670 C CZ  . ARG A 127 ? 1.64522 1.53708 1.54568 -0.46237 0.09230  -0.15320 128 ARG A CZ  
1671 N NH1 . ARG A 127 ? 1.74112 1.61964 1.64745 -0.45154 0.09672  -0.15656 128 ARG A NH1 
1672 N NH2 . ARG A 127 ? 1.71649 1.61976 1.58619 -0.47646 0.10771  -0.15889 128 ARG A NH2 
1686 N N   . ASN A 128 ? 1.59454 1.46101 1.81885 -0.43603 -0.01826 -0.09980 129 ASN A N   
1687 C CA  . ASN A 128 ? 1.40989 1.26906 1.69300 -0.42660 -0.05633 -0.10400 129 ASN A CA  
1688 C C   . ASN A 128 ? 1.40950 1.27942 1.75842 -0.43311 -0.04027 -0.08130 129 ASN A C   
1689 O O   . ASN A 128 ? 1.40458 1.27376 1.78308 -0.42327 -0.05880 -0.08612 129 ASN A O   
1690 C CB  . ASN A 128 ? 1.35381 1.20403 1.67747 -0.42709 -0.09441 -0.10674 129 ASN A CB  
1691 C CG  . ASN A 128 ? 1.32059 1.15525 1.58726 -0.41094 -0.12348 -0.13414 129 ASN A CG  
1692 O OD1 . ASN A 128 ? 1.31910 1.15356 1.55156 -0.41383 -0.11709 -0.13422 129 ASN A OD1 
1693 N ND2 . ASN A 128 ? 1.52233 1.34552 1.77705 -0.39063 -0.15508 -0.15605 129 ASN A ND2 
1700 N N   . ASP A 129 ? 1.46424 1.34634 1.83598 -0.44663 -0.00528 -0.05465 130 ASP A N   
1701 C CA  . ASP A 129 ? 1.41439 1.30838 1.84485 -0.44974 0.01750  -0.02868 130 ASP A CA  
1702 C C   . ASP A 129 ? 1.35713 1.24947 1.74969 -0.44162 0.03958  -0.03622 130 ASP A C   
1703 O O   . ASP A 129 ? 1.31272 1.21056 1.75480 -0.43576 0.03431  -0.02743 130 ASP A O   
1704 C CB  . ASP A 129 ? 1.45091 1.35784 1.89208 -0.45930 0.05856  0.00143  130 ASP A CB  
1705 C CG  . ASP A 129 ? 1.54658 1.45826 2.05004 -0.46565 0.04123  0.01981  130 ASP A CG  
1706 O OD1 . ASP A 129 ? 1.50526 1.40762 2.05544 -0.46500 -0.00455 0.00852  130 ASP A OD1 
1707 O OD2 . ASP A 129 ? 1.54110 1.46470 2.04622 -0.46939 0.07346  0.04547  130 ASP A OD2 
1712 N N   . LEU A 130 ? 1.36865 1.25401 1.67852 -0.44116 0.06410  -0.05143 131 LEU A N   
1713 C CA  . LEU A 130 ? 1.37350 1.25350 1.64894 -0.43355 0.08785  -0.05806 131 LEU A CA  
1714 C C   . LEU A 130 ? 1.44179 1.31720 1.72365 -0.41677 0.05394  -0.07340 131 LEU A C   
1715 O O   . LEU A 130 ? 1.45623 1.33428 1.75766 -0.40748 0.06285  -0.06677 131 LEU A O   
1716 C CB  . LEU A 130 ? 1.43509 1.30688 1.62917 -0.43836 0.11525  -0.07336 131 LEU A CB  
1717 C CG  . LEU A 130 ? 1.59192 1.45371 1.75087 -0.43267 0.14529  -0.07986 131 LEU A CG  
1718 C CD1 . LEU A 130 ? 1.47061 1.33434 1.66033 -0.43328 0.18000  -0.05874 131 LEU A CD1 
1719 C CD2 . LEU A 130 ? 1.54893 1.40237 1.63860 -0.44072 0.16537  -0.09706 131 LEU A CD2 
1731 N N   . ARG A 131 ? 1.55622 1.42515 1.81794 -0.40928 0.01564  -0.09343 132 ARG A N   
1732 C CA  . ARG A 131 ? 1.55485 1.41982 1.81794 -0.38774 -0.02099 -0.10916 132 ARG A CA  
1733 C C   . ARG A 131 ? 1.49372 1.36822 1.84013 -0.38498 -0.04731 -0.09823 132 ARG A C   
1734 O O   . ARG A 131 ? 1.58529 1.46385 1.94035 -0.36790 -0.05897 -0.10146 132 ARG A O   
1735 C CB  . ARG A 131 ? 1.54445 1.39906 1.77415 -0.37777 -0.05891 -0.13155 132 ARG A CB  
1736 C CG  . ARG A 131 ? 1.39814 1.24770 1.64119 -0.35344 -0.10910 -0.14915 132 ARG A CG  
1737 C CD  . ARG A 131 ? 1.54837 1.38393 1.73870 -0.33684 -0.13895 -0.17270 132 ARG A CD  
1738 N NE  . ARG A 131 ? 1.69029 1.52407 1.80403 -0.31908 -0.11671 -0.17932 132 ARG A NE  
1739 C CZ  . ARG A 131 ? 1.85538 1.67985 1.91410 -0.29724 -0.13440 -0.19584 132 ARG A CZ  
1740 N NH1 . ARG A 131 ? 1.73744 1.54976 1.80107 -0.28984 -0.17556 -0.21134 132 ARG A NH1 
1741 N NH2 . ARG A 131 ? 1.83473 1.66106 1.83484 -0.28093 -0.10859 -0.19523 132 ARG A NH2 
1755 N N   . THR A 132 ? 1.45163 1.33212 1.86482 -0.40088 -0.05648 -0.08283 133 THR A N   
1756 C CA  . THR A 132 ? 1.44368 1.33502 1.95047 -0.40077 -0.08641 -0.07152 133 THR A CA  
1757 C C   . THR A 132 ? 1.45268 1.36005 1.99378 -0.40024 -0.05225 -0.04659 133 THR A C   
1758 O O   . THR A 132 ? 1.55017 1.46750 2.13400 -0.38859 -0.07581 -0.04624 133 THR A O   
1759 C CB  . THR A 132 ? 1.56858 1.46227 2.14669 -0.41850 -0.09960 -0.05617 133 THR A CB  
1760 O OG1 . THR A 132 ? 1.54453 1.42068 2.09655 -0.41569 -0.13699 -0.08106 133 THR A OG1 
1761 C CG2 . THR A 132 ? 1.69993 1.60776 2.39088 -0.42194 -0.12724 -0.03967 133 THR A CG2 
1769 N N   . ILE A 133 ? 1.31315 1.22334 1.83440 -0.41045 0.00261  -0.02606 134 ILE A N   
1770 C CA  . ILE A 133 ? 1.33108 1.25352 1.88257 -0.40733 0.03875  -0.00122 134 ILE A CA  
1771 C C   . ILE A 133 ? 1.54781 1.46492 2.04945 -0.38917 0.04527  -0.01547 134 ILE A C   
1772 O O   . ILE A 133 ? 1.81721 1.74691 2.36008 -0.37899 0.04916  -0.00126 134 ILE A O   
1773 C CB  . ILE A 133 ? 1.60230 1.52466 2.13327 -0.41793 0.09594  0.02061  134 ILE A CB  
1774 C CG1 . ILE A 133 ? 1.71930 1.62311 2.14658 -0.41870 0.12301  -0.00136 134 ILE A CG1 
1775 C CG2 . ILE A 133 ? 1.67040 1.60111 2.25195 -0.43138 0.09148  0.03965  134 ILE A CG2 
1776 C CD1 . ILE A 133 ? 1.78131 1.68246 2.17837 -0.42468 0.17794  0.01409  134 ILE A CD1 
1788 N N   . LEU A 134 ? 1.50925 1.40973 1.92618 -0.38346 0.04815  -0.04038 135 LEU A N   
1789 C CA  . LEU A 134 ? 1.52041 1.41575 1.89238 -0.36376 0.05637  -0.05059 135 LEU A CA  
1790 C C   . LEU A 134 ? 1.53422 1.43958 1.93688 -0.34287 0.00568  -0.06010 135 LEU A C   
1791 O O   . LEU A 134 ? 1.51043 1.42574 1.92913 -0.32649 0.01068  -0.05121 135 LEU A O   
1792 C CB  . LEU A 134 ? 1.46419 1.34198 1.74934 -0.36246 0.06961  -0.07152 135 LEU A CB  
1793 C CG  . LEU A 134 ? 1.41809 1.28544 1.66459 -0.38038 0.11936  -0.06701 135 LEU A CG  
1794 C CD1 . LEU A 134 ? 1.35419 1.20964 1.53205 -0.38361 0.11988  -0.08794 135 LEU A CD1 
1795 C CD2 . LEU A 134 ? 1.53666 1.39828 1.77644 -0.37498 0.16436  -0.05512 135 LEU A CD2 
1807 N N   . LEU A 135 ? 1.57392 1.47637 1.98404 -0.34125 -0.04477 -0.07907 136 LEU A N   
1808 C CA  . LEU A 135 ? 1.50999 1.42024 1.94871 -0.32013 -0.10011 -0.09306 136 LEU A CA  
1809 C C   . LEU A 135 ? 1.48434 1.41716 2.01915 -0.32371 -0.11089 -0.07134 136 LEU A C   
1810 O O   . LEU A 135 ? 1.60764 1.55399 2.15742 -0.30227 -0.13107 -0.07271 136 LEU A O   
1811 C CB  . LEU A 135 ? 1.48425 1.38273 1.92321 -0.32067 -0.15231 -0.11766 136 LEU A CB  
1812 C CG  . LEU A 135 ? 1.63011 1.50971 1.97608 -0.30709 -0.15503 -0.14168 136 LEU A CG  
1813 C CD1 . LEU A 135 ? 1.48394 1.34981 1.83899 -0.30900 -0.20352 -0.16290 136 LEU A CD1 
1814 C CD2 . LEU A 135 ? 1.85245 1.73293 2.14163 -0.27134 -0.16260 -0.15404 136 LEU A CD2 
1826 N N   . ASN A 136 ? 1.47074 1.41088 2.07369 -0.34857 -0.09636 -0.04816 137 ASN A N   
1827 C CA  . ASN A 136 ? 1.64716 1.61209 2.35416 -0.35291 -0.10593 -0.02261 137 ASN A CA  
1828 C C   . ASN A 136 ? 1.63588 1.61445 2.34014 -0.34050 -0.06429 -0.00088 137 ASN A C   
1829 O O   . ASN A 136 ? 1.43773 1.44045 2.21547 -0.33331 -0.08137 0.01470  137 ASN A O   
1830 C CB  . ASN A 136 ? 1.47819 1.44874 2.25563 -0.37903 -0.08856 0.00445  137 ASN A CB  
1831 C CG  . ASN A 136 ? 1.39460 1.35603 2.20954 -0.39043 -0.13856 -0.01151 137 ASN A CG  
1832 O OD1 . ASN A 136 ? 1.56171 1.51611 2.37399 -0.37878 -0.19574 -0.04207 137 ASN A OD1 
1833 N ND2 . ASN A 136 ? 1.48129 1.44161 2.32980 -0.41054 -0.11673 0.00932  137 ASN A ND2 
1840 N N   . SER A 137 ? 1.50500 1.46832 2.12982 -0.33781 -0.01072 0.00050  138 SER A N   
1841 C CA  . SER A 137 ? 1.58843 1.55823 2.20464 -0.32441 0.03183  0.01927  138 SER A CA  
1842 C C   . SER A 137 ? 1.69855 1.67218 2.27980 -0.29500 0.00985  0.00419  138 SER A C   
1843 O O   . SER A 137 ? 1.56458 1.54751 2.15113 -0.27997 0.03812  0.02184  138 SER A O   
1844 C CB  . SER A 137 ? 1.76236 1.70981 2.30918 -0.33270 0.09536  0.02319  138 SER A CB  
1845 O OG  . SER A 137 ? 1.69012 1.61624 2.14914 -0.32667 0.09494  -0.00454 138 SER A OG  
1851 N N   . LEU A 138 ? 1.65219 1.61889 2.19587 -0.28314 -0.03753 -0.02607 139 LEU A N   
1852 C CA  . LEU A 138 ? 1.66110 1.63299 2.16511 -0.24918 -0.06081 -0.04004 139 LEU A CA  
1853 C C   . LEU A 138 ? 1.70100 1.69833 2.27454 -0.23584 -0.12413 -0.04495 139 LEU A C   
1854 O O   . LEU A 138 ? 1.70209 1.70575 2.34571 -0.25438 -0.16198 -0.04773 139 LEU A O   
1855 C CB  . LEU A 138 ? 1.64870 1.59890 2.06483 -0.23728 -0.07479 -0.06951 139 LEU A CB  
1856 C CG  . LEU A 138 ? 1.65407 1.58062 2.00348 -0.25130 -0.02126 -0.06917 139 LEU A CG  
1857 C CD1 . LEU A 138 ? 1.64030 1.55153 1.91571 -0.23703 -0.04101 -0.09501 139 LEU A CD1 
1858 C CD2 . LEU A 138 ? 1.76228 1.68622 2.08923 -0.24299 0.03623  -0.04973 139 LEU A CD2 
1870 N N   . GLN A 139 ? 1.72676 1.73928 2.28314 -0.20247 -0.13612 -0.04558 140 GLN A N   
1871 C CA  . GLN A 139 ? 1.74135 1.77884 2.35068 -0.18414 -0.20357 -0.05680 140 GLN A CA  
1872 C C   . GLN A 139 ? 1.77014 1.79178 2.34245 -0.17413 -0.26559 -0.09740 140 GLN A C   
1873 O O   . GLN A 139 ? 1.73590 1.73218 2.22230 -0.16708 -0.25261 -0.11447 140 GLN A O   
1874 C CB  . GLN A 139 ? 1.71973 1.77876 2.30755 -0.14554 -0.19858 -0.04691 140 GLN A CB  
1875 C CG  . GLN A 139 ? 1.74691 1.82380 2.38337 -0.15149 -0.14410 -0.00622 140 GLN A CG  
1876 C CD  . GLN A 139 ? 1.79196 1.88935 2.40351 -0.11082 -0.13533 0.00584  140 GLN A CD  
1877 O OE1 . GLN A 139 ? 1.83497 1.92598 2.36860 -0.07774 -0.14731 -0.01180 140 GLN A OE1 
1878 N NE2 . GLN A 139 ? 1.81527 1.93899 2.49365 -0.11012 -0.11208 0.03920  140 GLN A NE2 
1887 N N   . ASN A 140 ? 1.87146 1.90778 2.51286 -0.17298 -0.33421 -0.11293 141 ASN A N   
1888 C CA  . ASN A 140 ? 1.81877 1.83574 2.43323 -0.16410 -0.39765 -0.15426 141 ASN A CA  
1889 C C   . ASN A 140 ? 1.74571 1.75130 2.24307 -0.11898 -0.40453 -0.17774 141 ASN A C   
1890 O O   . ASN A 140 ? 1.81789 1.84253 2.28381 -0.08557 -0.39438 -0.16844 141 ASN A O   
1891 C CB  . ASN A 140 ? 1.74245 1.77829 2.45209 -0.16452 -0.47495 -0.16977 141 ASN A CB  
1892 C CG  . ASN A 140 ? 1.75389 1.79508 2.58385 -0.21009 -0.47569 -0.14967 141 ASN A CG  
1893 O OD1 . ASN A 140 ? 1.82823 1.84488 2.67221 -0.23248 -0.49091 -0.16337 141 ASN A OD1 
1894 N ND2 . ASN A 140 ? 1.66027 1.73469 2.57974 -0.22166 -0.45656 -0.11361 141 ASN A ND2 
1901 N N   . ASP A 141 ? 1.76468 1.74014 2.19840 -0.11578 -0.41872 -0.20483 142 ASP A N   
1902 C CA  . ASP A 141 ? 1.83805 1.80068 2.16124 -0.07085 -0.42775 -0.22713 142 ASP A CA  
1903 C C   . ASP A 141 ? 1.75675 1.72014 2.00903 -0.05713 -0.35455 -0.20113 142 ASP A C   
1904 O O   . ASP A 141 ? 1.82687 1.79088 1.99951 -0.01228 -0.35402 -0.20762 142 ASP A O   
1905 C CB  . ASP A 141 ? 1.87490 1.85444 2.19063 -0.02610 -0.49410 -0.25113 142 ASP A CB  
1906 C CG  . ASP A 141 ? 1.83355 1.80696 2.21687 -0.03749 -0.57455 -0.28425 142 ASP A CG  
1907 O OD1 . ASP A 141 ? 1.73553 1.67841 2.11109 -0.05481 -0.59059 -0.30482 142 ASP A OD1 
1908 O OD2 . ASP A 141 ? 2.08449 2.08370 2.53358 -0.02970 -0.62213 -0.28914 142 ASP A OD2 
1913 N N   . THR A 142 ? 1.76635 1.72871 2.04670 -0.09301 -0.29211 -0.17135 143 THR A N   
1914 C CA  . THR A 142 ? 1.77112 1.72719 1.98845 -0.08516 -0.22377 -0.15071 143 THR A CA  
1915 C C   . THR A 142 ? 1.65110 1.58194 1.78959 -0.08055 -0.21220 -0.16571 143 THR A C   
1916 O O   . THR A 142 ? 1.65224 1.57926 1.72534 -0.05667 -0.17488 -0.15652 143 THR A O   
1917 C CB  . THR A 142 ? 1.81501 1.77205 2.08035 -0.12437 -0.16454 -0.12050 143 THR A CB  
1918 O OG1 . THR A 142 ? 1.84949 1.83258 2.18853 -0.12445 -0.17061 -0.10181 143 THR A OG1 
1919 C CG2 . THR A 142 ? 1.87603 1.82160 2.08132 -0.11879 -0.09692 -0.10330 143 THR A CG2 
1927 N N   . VAL A 143 ? 1.59986 1.51456 1.74873 -0.10237 -0.24190 -0.18574 144 VAL A N   
1928 C CA  . VAL A 143 ? 1.71154 1.60445 1.79264 -0.09897 -0.23464 -0.19936 144 VAL A CA  
1929 C C   . VAL A 143 ? 1.70477 1.58953 1.74708 -0.06147 -0.29831 -0.23219 144 VAL A C   
1930 O O   . VAL A 143 ? 1.61664 1.50071 1.70867 -0.06603 -0.35559 -0.25235 144 VAL A O   
1931 C CB  . VAL A 143 ? 1.97203 1.85169 2.08583 -0.14679 -0.21930 -0.19716 144 VAL A CB  
1932 C CG1 . VAL A 143 ? 1.84122 1.70153 1.89019 -0.14106 -0.22001 -0.21236 144 VAL A CG1 
1933 C CG2 . VAL A 143 ? 1.81523 1.69986 1.95228 -0.17830 -0.15532 -0.16810 144 VAL A CG2 
1943 N N   . ILE A 144 ? 1.72505 1.60260 1.68090 -0.02324 -0.28835 -0.23737 145 ILE A N   
1944 C CA  . ILE A 144 ? 1.73069 1.59704 1.63144 0.02034  -0.34296 -0.26876 145 ILE A CA  
1945 C C   . ILE A 144 ? 1.72470 1.56699 1.58882 0.00916  -0.33853 -0.27993 145 ILE A C   
1946 O O   . ILE A 144 ? 1.75577 1.59577 1.56807 0.01507  -0.29113 -0.26387 145 ILE A O   
1947 C CB  . ILE A 144 ? 1.92396 1.80193 1.74908 0.08088  -0.33443 -0.26310 145 ILE A CB  
1948 C CG1 . ILE A 144 ? 1.85002 1.75518 1.71235 0.08893  -0.32294 -0.24271 145 ILE A CG1 
1949 C CG2 . ILE A 144 ? 2.04701 1.91383 1.81533 0.13124  -0.39888 -0.29932 145 ILE A CG2 
1950 C CD1 . ILE A 144 ? 1.84411 1.76065 1.78331 0.07607  -0.38110 -0.25917 145 ILE A CD1 
1962 N N   . TRP A 145 ? 1.75145 1.57638 1.64686 -0.00618 -0.38820 -0.30625 146 TRP A N   
1963 C CA  . TRP A 145 ? 1.88853 1.69110 1.75826 -0.01916 -0.38514 -0.31534 146 TRP A CA  
1964 C C   . TRP A 145 ? 1.89457 1.68150 1.67226 0.03604  -0.40943 -0.33733 146 TRP A C   
1965 O O   . TRP A 145 ? 1.81257 1.60304 1.55043 0.08453  -0.44104 -0.35212 146 TRP A O   
1966 C CB  . TRP A 145 ? 1.92454 1.71302 1.87051 -0.05725 -0.42426 -0.33085 146 TRP A CB  
1967 C CG  . TRP A 145 ? 1.84038 1.64543 1.87544 -0.10692 -0.39725 -0.30535 146 TRP A CG  
1968 C CD1 . TRP A 145 ? 1.92425 1.74599 2.03270 -0.11684 -0.41691 -0.30051 146 TRP A CD1 
1969 C CD2 . TRP A 145 ? 1.81508 1.62324 1.87285 -0.14979 -0.34485 -0.28000 146 TRP A CD2 
1970 N NE1 . TRP A 145 ? 1.59739 1.43113 1.77163 -0.16158 -0.37658 -0.27162 146 TRP A NE1 
1971 C CE2 . TRP A 145 ? 1.67951 1.50422 1.82035 -0.18150 -0.33297 -0.26029 146 TRP A CE2 
1972 C CE3 . TRP A 145 ? 1.82031 1.62073 1.83592 -0.16248 -0.30795 -0.27187 146 TRP A CE3 
1973 C CZ2 . TRP A 145 ? 1.88334 1.71431 2.05798 -0.22189 -0.28497 -0.23442 146 TRP A CZ2 
1974 C CZ3 . TRP A 145 ? 1.86864 1.67699 1.92049 -0.20493 -0.26426 -0.24831 146 TRP A CZ3 
1975 C CH2 . TRP A 145 ? 1.88637 1.70851 2.01296 -0.23258 -0.25267 -0.23057 146 TRP A CH2 
1986 N N   . ASP A 146 ? 1.93743 1.70856 1.67871 0.03128  -0.39290 -0.33781 147 ASP A N   
1987 C CA  . ASP A 146 ? 1.89991 1.65438 1.55318 0.08338  -0.41003 -0.35535 147 ASP A CA  
1988 C C   . ASP A 146 ? 1.92138 1.69334 1.50409 0.13378  -0.37830 -0.33723 147 ASP A C   
1989 O O   . ASP A 146 ? 2.04807 1.81369 1.56466 0.19281  -0.40916 -0.35531 147 ASP A O   
1990 C CB  . ASP A 146 ? 2.18197 1.91152 1.83150 0.10960  -0.48750 -0.39927 147 ASP A CB  
1991 C CG  . ASP A 146 ? 2.39594 2.10170 1.95244 0.16268  -0.50569 -0.42014 147 ASP A CG  
1992 O OD1 . ASP A 146 ? 2.18292 1.89343 1.68892 0.17272  -0.45663 -0.39701 147 ASP A OD1 
1993 O OD2 . ASP A 146 ? 2.32945 2.01157 1.86459 0.19560  -0.56962 -0.45988 147 ASP A OD2 
1998 N N   . ARG A 147 ? 1.88619 1.67924 1.48278 0.11255  -0.31552 -0.30084 148 ARG A N   
1999 C CA  . ARG A 147 ? 2.02945 1.84026 1.57372 0.15493  -0.27576 -0.27583 148 ARG A CA  
2000 C C   . ARG A 147 ? 2.00658 1.82387 1.54173 0.13466  -0.21055 -0.24438 148 ARG A C   
2001 O O   . ARG A 147 ? 2.07356 1.90115 1.65848 0.08989  -0.16923 -0.22291 148 ARG A O   
2002 C CB  . ARG A 147 ? 2.03463 1.86584 1.61811 0.15197  -0.26692 -0.26212 148 ARG A CB  
2003 C CG  . ARG A 147 ? 2.15004 1.98190 1.73951 0.18046  -0.33249 -0.29083 148 ARG A CG  
2004 C CD  . ARG A 147 ? 2.36734 2.19500 1.86457 0.25621  -0.36200 -0.30716 148 ARG A CD  
2005 N NE  . ARG A 147 ? 2.14489 1.97646 1.64499 0.28668  -0.42669 -0.33599 148 ARG A NE  
2006 C CZ  . ARG A 147 ? 2.17072 1.98227 1.69173 0.28125  -0.49671 -0.37795 148 ARG A CZ  
2007 N NH1 . ARG A 147 ? 2.19892 1.98380 1.73915 0.24783  -0.50953 -0.39451 148 ARG A NH1 
2008 N NH2 . ARG A 147 ? 2.29062 2.10939 1.81715 0.31020  -0.55629 -0.40372 148 ARG A NH2 
2022 N N   . LYS A 148 ? 1.99526 1.80654 1.46777 0.16919  -0.20244 -0.24215 149 LYS A N   
2023 C CA  . LYS A 148 ? 1.94380 1.76400 1.40913 0.15470  -0.14528 -0.21234 149 LYS A CA  
2024 C C   . LYS A 148 ? 2.04138 1.87926 1.46838 0.20038  -0.10205 -0.18074 149 LYS A C   
2025 O O   . LYS A 148 ? 2.46085 2.29836 1.82013 0.26390  -0.11196 -0.18091 149 LYS A O   
2026 C CB  . LYS A 148 ? 1.90350 1.70991 1.33166 0.16509  -0.15875 -0.22332 149 LYS A CB  
2027 C CG  . LYS A 148 ? 1.90910 1.72902 1.33048 0.15518  -0.10394 -0.19173 149 LYS A CG  
2028 C CD  . LYS A 148 ? 1.79301 1.60207 1.16691 0.18110  -0.11754 -0.19940 149 LYS A CD  
2029 C CE  . LYS A 148 ? 2.22614 2.01481 1.62766 0.14445  -0.15884 -0.22906 149 LYS A CE  
2030 N NZ  . LYS A 148 ? 2.41643 2.19183 1.76994 0.17329  -0.17169 -0.23648 149 LYS A NZ  
2044 N N   . LEU A 149 ? 2.00679 1.85867 1.47651 0.17057  -0.05274 -0.15277 150 LEU A N   
2045 C CA  . LEU A 149 ? 2.00644 1.87441 1.45290 0.20917  -0.00497 -0.11752 150 LEU A CA  
2046 C C   . LEU A 149 ? 2.11079 1.98399 1.52308 0.23044  0.02753  -0.09562 150 LEU A C   
2047 O O   . LEU A 149 ? 2.27015 2.14227 1.71105 0.18656  0.04378  -0.09255 150 LEU A O   
2048 C CB  . LEU A 149 ? 1.99743 1.87322 1.50524 0.16629  0.04064  -0.09498 150 LEU A CB  
2049 C CG  . LEU A 149 ? 1.78738 1.67758 1.28656 0.20111  0.09354  -0.05582 150 LEU A CG  
2050 C CD1 . LEU A 149 ? 2.06387 1.96212 1.52620 0.26013  0.07200  -0.05610 150 LEU A CD1 
2051 C CD2 . LEU A 149 ? 2.05901 1.94914 1.62357 0.14925  0.14051  -0.03732 150 LEU A CD2 
2063 N N   . VAL A 150 ? 2.25882 2.14040 1.61061 0.30025  0.03762  -0.07828 151 VAL A N   
2064 C CA  . VAL A 150 ? 2.28562 2.17523 1.60198 0.33211  0.06911  -0.05271 151 VAL A CA  
2065 C C   . VAL A 150 ? 2.10391 2.01403 1.43943 0.34674  0.13625  -0.00279 151 VAL A C   
2066 O O   . VAL A 150 ? 1.89656 1.81600 1.26340 0.32310  0.17758  0.02328  151 VAL A O   
2067 C CB  . VAL A 150 ? 2.48846 2.37066 1.71616 0.40768  0.03269  -0.06796 151 VAL A CB  
2068 C CG1 . VAL A 150 ? 2.64236 2.53463 1.83461 0.44371  0.06927  -0.03708 151 VAL A CG1 
2069 C CG2 . VAL A 150 ? 2.54874 2.40579 1.76645 0.39031  -0.03495 -0.11901 151 VAL A CG2 
2079 N N   . THR A 151 ? 2.28648 2.20477 1.60829 0.38602  0.14738  0.01218  152 THR A N   
2080 C CA  . THR A 151 ? 2.10807 2.04377 1.45346 0.40279  0.21241  0.06191  152 THR A CA  
2081 C C   . THR A 151 ? 2.09829 2.03522 1.47488 0.39415  0.21877  0.06485  152 THR A C   
2082 O O   . THR A 151 ? 2.17343 2.10515 1.52944 0.40532  0.17127  0.03483  152 THR A O   
2083 C CB  . THR A 151 ? 2.53598 2.48709 1.81324 0.49022  0.23451  0.09482  152 THR A CB  
2084 O OG1 . THR A 151 ? 2.58004 2.52929 1.78698 0.55150  0.19032  0.07330  152 THR A OG1 
2085 C CG2 . THR A 151 ? 2.55297 2.50445 1.80061 0.50293  0.23430  0.09742  152 THR A CG2 
2093 N N   . LEU A 152 ? 2.10218 2.04598 1.53280 0.37469  0.27787  0.10207  153 LEU A N   
2094 C CA  . LEU A 152 ? 2.27943 2.22377 1.74538 0.36696  0.29590  0.11248  153 LEU A CA  
2095 C C   . LEU A 152 ? 2.28664 2.24651 1.75616 0.41373  0.35920  0.16759  153 LEU A C   
2096 O O   . LEU A 152 ? 2.25948 2.22060 1.77506 0.39041  0.40888  0.19743  153 LEU A O   
2097 C CB  . LEU A 152 ? 2.16965 2.09854 1.71198 0.28271  0.30556  0.09808  153 LEU A CB  
2098 C CG  . LEU A 152 ? 2.26153 2.18666 1.84574 0.26748  0.32521  0.10630  153 LEU A CG  
2099 C CD1 . LEU A 152 ? 2.40039 2.33064 1.95228 0.29753  0.27556  0.08347  153 LEU A CD1 
2100 C CD2 . LEU A 152 ? 2.49792 2.40482 2.14877 0.18699  0.33639  0.09061  153 LEU A CD2 
2112 N N   . GLU A 153 ? 2.33834 2.31142 1.76290 0.48053  0.35700  0.18232  154 GLU A N   
2113 C CA  . GLU A 153 ? 2.33591 2.32656 1.75580 0.53742  0.41703  0.23906  154 GLU A CA  
2114 C C   . GLU A 153 ? 2.36664 2.36248 1.80536 0.55279  0.43370  0.25518  154 GLU A C   
2115 O O   . GLU A 153 ? 2.33379 2.33210 1.74139 0.56791  0.38507  0.22583  154 GLU A O   
2116 C CB  . GLU A 153 ? 2.44897 2.45681 1.77796 0.62621  0.40624  0.25221  154 GLU A CB  
2117 C CG  . GLU A 153 ? 2.68766 2.69154 1.99423 0.61983  0.39444  0.24161  154 GLU A CG  
2118 C CD  . GLU A 153 ? 2.66964 2.67445 2.05224 0.57259  0.45173  0.27535  154 GLU A CD  
2119 O OE1 . GLU A 153 ? 2.50196 2.51565 1.93306 0.57937  0.51230  0.32297  154 GLU A OE1 
2120 O OE2 . GLU A 153 ? 2.61765 2.61451 2.01542 0.52826  0.43510  0.25419  154 GLU A OE2 
2127 N N   . PRO A 154 ? 2.35704 2.35504 1.85062 0.55013  0.50140  0.30250  155 PRO A N   
2128 C CA  . PRO A 154 ? 2.36425 2.36421 1.88475 0.55840  0.52214  0.31928  155 PRO A CA  
2129 C C   . PRO A 154 ? 2.55098 2.57810 2.00890 0.65408  0.53205  0.35338  155 PRO A C   
2130 O O   . PRO A 154 ? 2.76297 2.80683 2.16710 0.71755  0.54485  0.37917  155 PRO A O   
2131 C CB  . PRO A 154 ? 2.30483 2.29051 1.91400 0.51348  0.59227  0.35488  155 PRO A CB  
2132 C CG  . PRO A 154 ? 2.31688 2.31052 1.92551 0.52910  0.62264  0.38328  155 PRO A CG  
2133 C CD  . PRO A 154 ? 2.33897 2.33521 1.88574 0.53052  0.56166  0.34119  155 PRO A CD  
2141 N N   . ASP A 155 ? 2.75156 2.78453 2.21628 0.66619  0.52684  0.35468  156 ASP A N   
2142 C CA  . ASP A 155 ? 2.76780 2.82867 2.18266 0.75382  0.54012  0.38990  156 ASP A CA  
2143 C C   . ASP A 155 ? 2.71123 2.76992 2.19581 0.74656  0.60852  0.43729  156 ASP A C   
2144 O O   . ASP A 155 ? 2.78206 2.81522 2.34785 0.67732  0.64494  0.44126  156 ASP A O   
2145 C CB  . ASP A 155 ? 2.71803 2.79203 2.07473 0.78121  0.46359  0.34646  156 ASP A CB  
2146 C CG  . ASP A 155 ? 2.74521 2.85205 2.02034 0.88547  0.46015  0.37294  156 ASP A CG  
2147 O OD1 . ASP A 155 ? 3.14480 3.26149 2.35205 0.94363  0.46167  0.38472  156 ASP A OD1 
2148 O OD2 . ASP A 155 ? 2.79270 2.91679 2.06966 0.91205  0.45670  0.38317  156 ASP A OD2 
2153 N N   . LYS A 156 ? 2.64788 2.73255 2.09896 0.82079  0.62551  0.47276  157 LYS A N   
2154 C CA  . LYS A 156 ? 2.69506 2.77701 2.21106 0.81806  0.68842  0.51759  157 LYS A CA  
2155 C C   . LYS A 156 ? 2.64642 2.71050 2.21557 0.75293  0.66563  0.48372  157 LYS A C   
2156 O O   . LYS A 156 ? 2.60580 2.65328 2.24577 0.72454  0.71949  0.51101  157 LYS A O   
2157 C CB  . LYS A 156 ? 2.77036 2.88848 2.23321 0.91864  0.71048  0.56547  157 LYS A CB  
2158 C CG  . LYS A 156 ? 2.77372 2.90426 2.23377 0.97717  0.78341  0.63351  157 LYS A CG  
2159 C CD  . LYS A 156 ? 2.80203 2.90621 2.37197 0.92588  0.86315  0.67483  157 LYS A CD  
2160 C CE  . LYS A 156 ? 2.84681 2.96869 2.42612 0.99337  0.94158  0.75354  157 LYS A CE  
2161 N NZ  . LYS A 156 ? 2.82854 2.92116 2.52498 0.94003  1.01662  0.79157  157 LYS A NZ  
2175 N N   . GLU A 157 ? 2.58208 2.64791 2.12211 0.72986  0.58907  0.42662  158 GLU A N   
2176 C CA  . GLU A 157 ? 2.71624 2.76970 2.30729 0.67358  0.56769  0.39854  158 GLU A CA  
2177 C C   . GLU A 157 ? 2.85055 2.88849 2.44561 0.60949  0.50151  0.33578  158 GLU A C   
2178 O O   . GLU A 157 ? 2.75389 2.77347 2.40658 0.54765  0.49911  0.31685  158 GLU A O   
2179 C CB  . GLU A 157 ? 2.62454 2.71018 2.18931 0.73032  0.54649  0.40900  158 GLU A CB  
2180 C CG  . GLU A 157 ? 2.71856 2.79428 2.35496 0.69451  0.57590  0.42118  158 GLU A CG  
2181 C CD  . GLU A 157 ? 2.90026 3.01327 2.51391 0.75404  0.55670  0.43636  158 GLU A CD  
2182 O OE1 . GLU A 157 ? 3.10853 3.25313 2.65208 0.80874  0.49881  0.41904  158 GLU A OE1 
2183 O OE2 . GLU A 157 ? 2.89362 3.00404 2.55911 0.74744  0.59843  0.46475  158 GLU A OE2 
2190 N N   . LYS A 158 ? 2.62589 2.66915 2.16343 0.62311  0.45027  0.30450  159 LYS A N   
2191 C CA  . LYS A 158 ? 2.47695 2.50525 2.02166 0.56477  0.38877  0.24789  159 LYS A CA  
2192 C C   . LYS A 158 ? 2.48687 2.50259 2.00409 0.55259  0.38165  0.23364  159 LYS A C   
2193 O O   . LYS A 158 ? 2.47946 2.50521 1.95389 0.60459  0.40758  0.26205  159 LYS A O   
2194 C CB  . LYS A 158 ? 2.41970 2.46909 1.92366 0.59412  0.31041  0.21184  159 LYS A CB  
2195 C CG  . LYS A 158 ? 2.33698 2.39389 1.89279 0.57113  0.29906  0.20779  159 LYS A CG  
2196 C CD  . LYS A 158 ? 2.35728 2.43703 1.88351 0.59639  0.21641  0.17069  159 LYS A CD  
2197 C CE  . LYS A 158 ? 2.37569 2.47585 1.94670 0.59853  0.21400  0.18269  159 LYS A CE  
2198 N NZ  . LYS A 158 ? 2.44994 2.57802 1.99661 0.62946  0.13159  0.14969  159 LYS A NZ  
2212 N N   . TRP A 159 ? 2.57686 2.57226 2.12076 0.48517  0.34821  0.19224  160 TRP A N   
2213 C CA  . TRP A 159 ? 2.55507 2.53997 2.07344 0.47038  0.33165  0.17301  160 TRP A CA  
2214 C C   . TRP A 159 ? 2.59204 2.58826 2.03583 0.51661  0.26206  0.13996  160 TRP A C   
2215 O O   . TRP A 159 ? 2.49315 2.50016 1.92285 0.53431  0.21260  0.11716  160 TRP A O   
2216 C CB  . TRP A 159 ? 2.30531 2.26519 1.88017 0.38275  0.32381  0.14307  160 TRP A CB  
2217 C CG  . TRP A 159 ? 2.31511 2.25808 1.95486 0.33628  0.38897  0.16883  160 TRP A CG  
2218 C CD1 . TRP A 159 ? 2.28363 2.21403 1.98108 0.29768  0.41498  0.17367  160 TRP A CD1 
2219 C CD2 . TRP A 159 ? 2.20515 2.14054 1.86122 0.32400  0.43463  0.19176  160 TRP A CD2 
2220 N NE1 . TRP A 159 ? 2.15964 2.07120 1.90483 0.26206  0.47179  0.19420  160 TRP A NE1 
2221 C CE2 . TRP A 159 ? 2.15539 2.07136 1.88067 0.27568  0.48360  0.20592  160 TRP A CE2 
2222 C CE3 . TRP A 159 ? 2.23247 2.17589 1.85397 0.35000  0.43855  0.20210  160 TRP A CE3 
2223 C CZ2 . TRP A 159 ? 2.17771 2.08236 1.94321 0.25015  0.53206  0.22757  160 TRP A CZ2 
2224 C CZ3 . TRP A 159 ? 2.20531 2.14166 1.86981 0.32495  0.48953  0.22815  160 TRP A CZ3 
2225 C CH2 . TRP A 159 ? 2.19949 2.11674 1.93761 0.27414  0.53373  0.23946  160 TRP A CH2 
2236 N N   . THR A 160 ? 2.46418 2.45752 1.86212 0.53746  0.25793  0.13740  161 THR A N   
2237 C CA  . THR A 160 ? 2.35151 2.34645 1.67748 0.57567  0.19185  0.10041  161 THR A CA  
2238 C C   . THR A 160 ? 2.29834 2.27130 1.63985 0.51833  0.16819  0.06777  161 THR A C   
2239 O O   . THR A 160 ? 2.25445 2.22229 1.60333 0.50498  0.20748  0.08758  161 THR A O   
2240 C CB  . THR A 160 ? 2.54169 2.55331 1.78529 0.66599  0.20751  0.12807  161 THR A CB  
2241 O OG1 . THR A 160 ? 2.85359 2.88854 2.07923 0.72378  0.22638  0.15860  161 THR A OG1 
2242 C CG2 . THR A 160 ? 2.72788 2.73427 1.89224 0.70508  0.13793  0.08462  161 THR A CG2 
2250 N N   . LEU A 161 ? 2.34547 2.30756 1.69670 0.48560  0.10458  0.02035  162 LEU A N   
2251 C CA  . LEU A 161 ? 2.38991 2.33142 1.76407 0.42721  0.08007  -0.01088 162 LEU A CA  
2252 C C   . LEU A 161 ? 2.32788 2.26189 1.63198 0.46760  0.02260  -0.04441 162 LEU A C   
2253 O O   . LEU A 161 ? 2.36893 2.30333 1.64708 0.49396  -0.03689 -0.07601 162 LEU A O   
2254 C CB  . LEU A 161 ? 2.42607 2.35857 1.86934 0.35975  0.05349  -0.03694 162 LEU A CB  
2255 C CG  . LEU A 161 ? 2.43437 2.36432 1.95104 0.30381  0.10718  -0.01333 162 LEU A CG  
2256 C CD1 . LEU A 161 ? 2.44481 2.39049 1.96568 0.34031  0.14897  0.02367  162 LEU A CD1 
2257 C CD2 . LEU A 161 ? 2.50670 2.42748 2.08158 0.24343  0.07502  -0.04167 162 LEU A CD2 
2269 N N   . THR A 162 ? 2.24377 2.16999 1.52145 0.47080  0.03848  -0.03903 163 THR A N   
2270 C CA  . THR A 162 ? 2.20702 2.12187 1.41415 0.51190  -0.00871 -0.06824 163 THR A CA  
2271 C C   . THR A 162 ? 2.29923 2.19184 1.54061 0.44949  -0.04426 -0.10458 163 THR A C   
2272 O O   . THR A 162 ? 2.39969 2.28959 1.68965 0.39407  -0.00942 -0.09123 163 THR A O   
2273 C CB  . THR A 162 ? 2.27417 2.19717 1.42538 0.56583  0.03473  -0.03368 163 THR A CB  
2274 O OG1 . THR A 162 ? 2.38276 2.32793 1.50342 0.62830  0.07124  0.00492  163 THR A OG1 
2275 C CG2 . THR A 162 ? 2.25213 2.15987 1.32395 0.61280  -0.01286 -0.06486 163 THR A CG2 
2283 N N   . PHE A 163 ? 2.27589 2.15278 1.49329 0.46008  -0.11421 -0.15018 164 PHE A N   
2284 C CA  . PHE A 163 ? 2.34521 2.19948 1.59413 0.40795  -0.15188 -0.18461 164 PHE A CA  
2285 C C   . PHE A 163 ? 2.52414 2.35939 1.69834 0.45494  -0.18771 -0.20927 164 PHE A C   
2286 O O   . PHE A 163 ? 2.91206 2.74660 2.01120 0.52728  -0.21341 -0.21966 164 PHE A O   
2287 C CB  . PHE A 163 ? 2.33861 2.18650 1.64261 0.37090  -0.20444 -0.21754 164 PHE A CB  
2288 C CG  . PHE A 163 ? 2.32890 2.19307 1.70685 0.32437  -0.16965 -0.19437 164 PHE A CG  
2289 C CD1 . PHE A 163 ? 2.40128 2.26130 1.84774 0.25204  -0.14222 -0.18664 164 PHE A CD1 
2290 C CD2 . PHE A 163 ? 2.36919 2.25265 1.74440 0.35644  -0.16368 -0.18000 164 PHE A CD2 
2291 C CE1 . PHE A 163 ? 1.98989 1.86106 1.49818 0.21316  -0.10940 -0.16704 164 PHE A CE1 
2292 C CE2 . PHE A 163 ? 2.31998 2.21575 1.76193 0.31609  -0.12953 -0.15810 164 PHE A CE2 
2293 C CZ  . PHE A 163 ? 2.11841 2.00619 1.62563 0.24468  -0.10220 -0.15257 164 PHE A CZ  
2303 N N   . GLU A 164 ? 2.44365 2.26314 1.63576 0.41610  -0.18893 -0.21860 165 GLU A N   
2304 C CA  . GLU A 164 ? 2.56169 2.36094 1.68593 0.45777  -0.21463 -0.23795 165 GLU A CA  
2305 C C   . GLU A 164 ? 2.66050 2.43436 1.75392 0.48574  -0.29413 -0.29053 165 GLU A C   
2306 O O   . GLU A 164 ? 2.71811 2.47713 1.87146 0.43538  -0.33560 -0.32048 165 GLU A O   
2307 C CB  . GLU A 164 ? 2.52716 2.31691 1.68802 0.40428  -0.19994 -0.23591 165 GLU A CB  
2308 C CG  . GLU A 164 ? 2.61191 2.38358 1.70383 0.44851  -0.21230 -0.24598 165 GLU A CG  
2309 C CD  . GLU A 164 ? 2.43008 2.20008 1.55968 0.39831  -0.18937 -0.23541 165 GLU A CD  
2310 O OE1 . GLU A 164 ? 2.31895 2.07663 1.50764 0.33876  -0.21414 -0.25656 165 GLU A OE1 
2311 O OE2 . GLU A 164 ? 2.59426 2.37804 1.69704 0.41995  -0.14551 -0.20324 165 GLU A OE2 
2318 N N   . ASP A 165 ? 2.53982 2.30865 1.54140 0.56769  -0.31571 -0.30140 166 ASP A N   
2319 C CA  . ASP A 165 ? 2.56437 2.30604 1.52551 0.60327  -0.39589 -0.35612 166 ASP A CA  
2320 C C   . ASP A 165 ? 2.57998 2.32809 1.60703 0.56983  -0.43858 -0.37818 166 ASP A C   
2321 O O   . ASP A 165 ? 2.79065 2.51410 1.84178 0.55439  -0.50629 -0.42486 166 ASP A O   
2322 C CB  . ASP A 165 ? 2.64062 2.34424 1.60104 0.58389  -0.43281 -0.39118 166 ASP A CB  
2323 C CG  . ASP A 165 ? 2.65282 2.35252 1.55531 0.61408  -0.38936 -0.36678 166 ASP A CG  
2324 O OD1 . ASP A 165 ? 2.70232 2.41923 1.53303 0.67927  -0.35344 -0.33789 166 ASP A OD1 
2325 O OD2 . ASP A 165 ? 2.63416 2.31591 1.56577 0.57425  -0.38927 -0.37324 166 ASP A OD2 
2330 N N   . LYS A 166 ? 2.45938 2.24056 1.52166 0.55831  -0.39840 -0.34312 167 LYS A N   
2331 C CA  . LYS A 166 ? 2.43534 2.22913 1.56141 0.53089  -0.43048 -0.35566 167 LYS A CA  
2332 C C   . LYS A 166 ? 2.44133 2.26941 1.54258 0.57304  -0.39305 -0.31991 167 LYS A C   
2333 O O   . LYS A 166 ? 2.42230 2.26542 1.49379 0.59382  -0.32640 -0.27608 167 LYS A O   
2334 C CB  . LYS A 166 ? 2.51695 2.31250 1.75479 0.43839  -0.41276 -0.34646 167 LYS A CB  
2335 C CG  . LYS A 166 ? 2.55498 2.31901 1.83320 0.39451  -0.45829 -0.38291 167 LYS A CG  
2336 C CD  . LYS A 166 ? 2.52111 2.26997 1.81597 0.40538  -0.54301 -0.43189 167 LYS A CD  
2337 C CE  . LYS A 166 ? 2.61262 2.32891 1.96218 0.35809  -0.58476 -0.46402 167 LYS A CE  
2338 N NZ  . LYS A 166 ? 2.55374 2.23854 1.83276 0.38765  -0.59061 -0.48028 167 LYS A NZ  
2352 N N   . PRO A 167 ? 2.52618 2.36858 1.64375 0.58707  -0.43355 -0.33518 168 PRO A N   
2353 C CA  . PRO A 167 ? 2.62746 2.50350 1.71588 0.63509  -0.39953 -0.30024 168 PRO A CA  
2354 C C   . PRO A 167 ? 2.49089 2.38683 1.64301 0.58805  -0.31840 -0.24723 168 PRO A C   
2355 O O   . PRO A 167 ? 2.44419 2.33523 1.68303 0.51184  -0.30686 -0.24553 168 PRO A O   
2356 C CB  . PRO A 167 ? 2.70664 2.59387 1.82195 0.64285  -0.46739 -0.33198 168 PRO A CB  
2357 C CG  . PRO A 167 ? 2.57278 2.43769 1.77297 0.57074  -0.51461 -0.36800 168 PRO A CG  
2358 C CD  . PRO A 167 ? 2.55622 2.38704 1.72677 0.55966  -0.51190 -0.38242 168 PRO A CD  
2366 N N   . SER A 168 ? 2.45160 2.36890 1.55948 0.63685  -0.26158 -0.20347 169 SER A N   
2367 C CA  . SER A 168 ? 2.49620 2.42912 1.66092 0.59928  -0.18349 -0.15325 169 SER A CA  
2368 C C   . SER A 168 ? 2.46221 2.41544 1.68723 0.57983  -0.18537 -0.14473 169 SER A C   
2369 O O   . SER A 168 ? 2.50937 2.47325 1.72047 0.61128  -0.24086 -0.16900 169 SER A O   
2370 C CB  . SER A 168 ? 2.51695 2.46456 1.62174 0.65955  -0.12003 -0.10597 169 SER A CB  
2371 O OG  . SER A 168 ? 2.48834 2.41994 1.53926 0.68051  -0.11656 -0.11055 169 SER A OG  
2377 N N   . GLU A 169 ? 2.49880 2.45714 1.79263 0.52779  -0.12485 -0.11056 170 GLU A N   
2378 C CA  . GLU A 169 ? 2.34033 2.31496 1.69931 0.50212  -0.11701 -0.09839 170 GLU A CA  
2379 C C   . GLU A 169 ? 2.31099 2.29669 1.68878 0.50305  -0.03318 -0.04467 170 GLU A C   
2380 O O   . GLU A 169 ? 2.26976 2.24978 1.62466 0.51173  0.01660  -0.01876 170 GLU A O   
2381 C CB  . GLU A 169 ? 2.40580 2.36689 1.85057 0.42027  -0.13925 -0.12181 170 GLU A CB  
2382 C CG  . GLU A 169 ? 2.29316 2.24086 1.73646 0.41288  -0.22091 -0.17302 170 GLU A CG  
2383 C CD  . GLU A 169 ? 2.28902 2.25496 1.72230 0.45507  -0.28318 -0.19480 170 GLU A CD  
2384 O OE1 . GLU A 169 ? 2.36221 2.35419 1.78528 0.49258  -0.26133 -0.16796 170 GLU A OE1 
2385 O OE2 . GLU A 169 ? 2.26065 2.21510 1.69963 0.45073  -0.35508 -0.23877 170 GLU A OE2 
2392 N N   . THR A 170 ? 2.27133 2.27272 1.69651 0.49406  -0.01759 -0.02694 171 THR A N   
2393 C CA  . THR A 170 ? 2.26295 2.27166 1.71424 0.49446  0.06005  0.02275  171 THR A CA  
2394 C C   . THR A 170 ? 2.22978 2.22788 1.77031 0.41896  0.08473  0.02603  171 THR A C   
2395 O O   . THR A 170 ? 2.42419 2.41415 2.00545 0.37133  0.04302  -0.00592 171 THR A O   
2396 C CB  . THR A 170 ? 2.35026 2.38834 1.76738 0.56654  0.06681  0.04921  171 THR A CB  
2397 O OG1 . THR A 170 ? 2.40166 2.45509 1.84911 0.56131  0.01466  0.02711  171 THR A OG1 
2398 C CG2 . THR A 170 ? 2.39539 2.44397 1.71484 0.64844  0.04657  0.04809  171 THR A CG2 
2406 N N   . ALA A 171 ? 2.26428 2.26103 1.83558 0.41066  0.15534  0.06650  172 ALA A N   
2407 C CA  . ALA A 171 ? 2.37662 2.36036 2.02456 0.34690  0.18671  0.07250  172 ALA A CA  
2408 C C   . ALA A 171 ? 2.38352 2.36419 2.05346 0.35488  0.26462  0.11879  172 ALA A C   
2409 O O   . ALA A 171 ? 2.43216 2.41444 2.06966 0.39091  0.30189  0.14598  172 ALA A O   
2410 C CB  . ALA A 171 ? 2.31442 2.27243 1.99143 0.27800  0.18286  0.04764  172 ALA A CB  
2416 N N   . ASP A 172 ? 2.35566 2.33066 2.08406 0.32234  0.29149  0.12963  173 ASP A N   
2417 C CA  . ASP A 172 ? 2.41647 2.38045 2.17520 0.32183  0.36647  0.17006  173 ASP A CA  
2418 C C   . ASP A 172 ? 2.30335 2.23355 2.10037 0.25832  0.40578  0.16597  173 ASP A C   
2419 O O   . ASP A 172 ? 2.27957 2.19719 2.08920 0.26192  0.46359  0.19568  173 ASP A O   
2420 C CB  . ASP A 172 ? 2.45976 2.43219 2.25977 0.32361  0.37921  0.18520  173 ASP A CB  
2421 C CG  . ASP A 172 ? 2.42105 2.43136 2.18777 0.38736  0.33900  0.19033  173 ASP A CG  
2422 O OD1 . ASP A 172 ? 2.35352 2.38143 2.06672 0.45031  0.34457  0.21032  173 ASP A OD1 
2423 O OD2 . ASP A 172 ? 2.40175 2.42610 2.19666 0.37619  0.30082  0.17495  173 ASP A OD2 
2428 N N   . LEU A 173 ? 2.26518 2.18146 2.08315 0.20169  0.37471  0.13040  174 LEU A N   
2429 C CA  . LEU A 173 ? 2.14648 2.03313 1.99538 0.14141  0.40334  0.12074  174 LEU A CA  
2430 C C   . LEU A 173 ? 2.03607 1.92088 1.86824 0.11070  0.35355  0.08364  174 LEU A C   
2431 O O   . LEU A 173 ? 1.91938 1.81266 1.75453 0.10110  0.30412  0.05911  174 LEU A O   
2432 C CB  . LEU A 173 ? 2.25971 2.12644 2.16233 0.09873  0.43148  0.12080  174 LEU A CB  
2433 C CG  . LEU A 173 ? 2.24318 2.08026 2.17282 0.03318  0.44484  0.09917  174 LEU A CG  
2434 C CD1 . LEU A 173 ? 2.28045 2.10104 2.21021 0.02349  0.48415  0.11014  174 LEU A CD1 
2435 C CD2 . LEU A 173 ? 2.13273 1.95012 2.10603 0.00278  0.47316  0.10062  174 LEU A CD2 
2447 N N   . VAL A 174 ? 1.97482 1.84954 1.79545 0.09542  0.36755  0.08186  175 VAL A N   
2448 C CA  . VAL A 174 ? 1.97796 1.85021 1.78266 0.06728  0.32722  0.05077  175 VAL A CA  
2449 C C   . VAL A 174 ? 1.89051 1.73970 1.73365 0.00248  0.35009  0.03881  175 VAL A C   
2450 O O   . VAL A 174 ? 1.89071 1.72533 1.75776 -0.01230 0.39970  0.05612  175 VAL A O   
2451 C CB  . VAL A 174 ? 2.07712 1.95985 1.83460 0.10408  0.32160  0.05790  175 VAL A CB  
2452 C CG1 . VAL A 174 ? 2.16836 2.04647 1.91320 0.07268  0.28487  0.02774  175 VAL A CG1 
2453 C CG2 . VAL A 174 ? 1.94793 1.85253 1.65650 0.17354  0.29458  0.06555  175 VAL A CG2 
2463 N N   . ILE A 175 ? 1.92697 1.77261 1.77715 -0.03460 0.31310  0.00914  176 ILE A N   
2464 C CA  . ILE A 175 ? 1.83699 1.66399 1.71391 -0.09243 0.32696  -0.00595 176 ILE A CA  
2465 C C   . ILE A 175 ? 1.74308 1.57544 1.59686 -0.10638 0.29211  -0.02646 176 ILE A C   
2466 O O   . ILE A 175 ? 1.76098 1.60144 1.60442 -0.10438 0.24522  -0.04505 176 ILE A O   
2467 C CB  . ILE A 175 ? 1.63286 1.45162 1.54283 -0.12284 0.32214  -0.01709 176 ILE A CB  
2468 C CG1 . ILE A 175 ? 1.64270 1.45549 1.57568 -0.10653 0.36043  0.00568  176 ILE A CG1 
2469 C CG2 . ILE A 175 ? 1.71958 1.52033 1.64597 -0.17676 0.33368  -0.03435 176 ILE A CG2 
2470 C CD1 . ILE A 175 ? 2.06180 1.86937 2.02802 -0.12836 0.35934  0.00047  176 ILE A CD1 
2482 N N   . ILE A 176 ? 1.81576 1.64375 1.66685 -0.12084 0.31473  -0.02219 177 ILE A N   
2483 C CA  . ILE A 176 ? 1.73253 1.56814 1.56090 -0.12922 0.28689  -0.03646 177 ILE A CA  
2484 C C   . ILE A 176 ? 1.71093 1.53805 1.55787 -0.18163 0.27225  -0.06074 177 ILE A C   
2485 O O   . ILE A 176 ? 1.90400 1.71779 1.77651 -0.21820 0.30133  -0.06289 177 ILE A O   
2486 C CB  . ILE A 176 ? 2.01794 1.85749 1.84305 -0.12256 0.31788  -0.01800 177 ILE A CB  
2487 C CG1 . ILE A 176 ? 2.15098 2.00027 1.95877 -0.06553 0.33934  0.01250  177 ILE A CG1 
2488 C CG2 . ILE A 176 ? 1.93662 1.78659 1.73831 -0.12830 0.28973  -0.03032 177 ILE A CG2 
2489 C CD1 . ILE A 176 ? 2.05503 1.91873 1.81377 -0.01362 0.29856  0.00846  177 ILE A CD1 
2501 N N   . ALA A 177 ? 1.68245 1.51619 1.51603 -0.18318 0.22697  -0.07916 178 ALA A N   
2502 C CA  . ALA A 177 ? 1.66891 1.49808 1.51854 -0.22693 0.21222  -0.09814 178 ALA A CA  
2503 C C   . ALA A 177 ? 1.63834 1.47613 1.46601 -0.22457 0.17216  -0.11191 178 ALA A C   
2504 O O   . ALA A 177 ? 1.71216 1.54915 1.55242 -0.24631 0.14648  -0.12608 178 ALA A O   
2505 C CB  . ALA A 177 ? 1.64973 1.47432 1.52726 -0.23803 0.20297  -0.10306 178 ALA A CB  
2511 N N   . ASN A 178 ? 1.71741 1.56304 1.51403 -0.19618 0.16879  -0.10545 179 ASN A N   
2512 C CA  . ASN A 178 ? 1.71746 1.56847 1.48794 -0.18493 0.13089  -0.11765 179 ASN A CA  
2513 C C   . ASN A 178 ? 1.69594 1.55224 1.46713 -0.21583 0.13796  -0.12050 179 ASN A C   
2514 O O   . ASN A 178 ? 1.67497 1.53787 1.41987 -0.19922 0.12006  -0.12224 179 ASN A O   
2515 C CB  . ASN A 178 ? 1.78985 1.64652 1.51886 -0.12916 0.12087  -0.10920 179 ASN A CB  
2516 C CG  . ASN A 178 ? 1.83876 1.70342 1.55912 -0.11425 0.16299  -0.08440 179 ASN A CG  
2517 O OD1 . ASN A 178 ? 1.83079 1.69314 1.58053 -0.13380 0.20219  -0.07090 179 ASN A OD1 
2518 N ND2 . ASN A 178 ? 1.85308 1.72607 1.53616 -0.07833 0.15618  -0.07713 179 ASN A ND2 
2525 N N   . GLY A 179 ? 1.60876 1.46261 1.40712 -0.25795 0.16263  -0.12167 180 GLY A N   
2526 C CA  . GLY A 179 ? 1.70001 1.56145 1.50101 -0.29033 0.16176  -0.12845 180 GLY A CA  
2527 C C   . GLY A 179 ? 1.59457 1.46417 1.40158 -0.29924 0.19370  -0.11631 180 GLY A C   
2528 O O   . GLY A 179 ? 1.49040 1.35875 1.30187 -0.27936 0.22002  -0.09966 180 GLY A O   
2532 N N   . GLY A 180 ? 1.47183 1.35196 1.28335 -0.32946 0.19055  -0.12332 181 GLY A N   
2533 C CA  . GLY A 180 ? 1.52513 1.41591 1.35305 -0.34564 0.21577  -0.11460 181 GLY A CA  
2534 C C   . GLY A 180 ? 1.51320 1.42121 1.33041 -0.31476 0.21892  -0.09480 181 GLY A C   
2535 O O   . GLY A 180 ? 1.39841 1.31597 1.23972 -0.32133 0.24500  -0.08027 181 GLY A O   
2539 N N   . MET A 181 ? 1.71101 1.62240 1.49500 -0.28016 0.19313  -0.09354 182 MET A N   
2540 C CA  . MET A 181 ? 1.79456 1.72035 1.55909 -0.24141 0.19685  -0.07351 182 MET A CA  
2541 C C   . MET A 181 ? 1.65415 1.57154 1.39650 -0.19107 0.20442  -0.05978 182 MET A C   
2542 O O   . MET A 181 ? 1.59209 1.51668 1.30111 -0.14666 0.19807  -0.04782 182 MET A O   
2543 C CB  . MET A 181 ? 1.59266 1.52592 1.32812 -0.23131 0.16348  -0.08213 182 MET A CB  
2544 C CG  . MET A 181 ? 1.56206 1.50924 1.31536 -0.27475 0.15604  -0.09151 182 MET A CG  
2545 S SD  . MET A 181 ? 2.96546 2.94103 2.75416 -0.29605 0.18660  -0.07165 182 MET A SD  
2546 C CE  . MET A 181 ? 2.16994 2.16274 1.93175 -0.24266 0.18830  -0.04503 182 MET A CE  
2556 N N   . SER A 182 ? 1.57531 1.47830 1.33244 -0.19395 0.21851  -0.06055 183 SER A N   
2557 C CA  . SER A 182 ? 1.62259 1.52049 1.35816 -0.14473 0.22513  -0.04687 183 SER A CA  
2558 C C   . SER A 182 ? 1.70881 1.62195 1.43942 -0.10823 0.25642  -0.01395 183 SER A C   
2559 O O   . SER A 182 ? 1.85186 1.77587 1.61891 -0.13112 0.28587  0.00202  183 SER A O   
2560 C CB  . SER A 182 ? 1.64717 1.53056 1.40945 -0.15834 0.24429  -0.04733 183 SER A CB  
2561 O OG  . SER A 182 ? 1.54986 1.43216 1.29201 -0.10875 0.25198  -0.03147 183 SER A OG  
2567 N N   . LYS A 183 ? 1.69131 1.60619 1.37790 -0.04900 0.24911  -0.00321 184 LYS A N   
2568 C CA  . LYS A 183 ? 1.62819 1.55871 1.30321 -0.00256 0.28096  0.03297  184 LYS A CA  
2569 C C   . LYS A 183 ? 1.67912 1.60702 1.35227 0.03544  0.30908  0.05584  184 LYS A C   
2570 O O   . LYS A 183 ? 1.95524 1.89685 1.61612 0.08257  0.33862  0.09057  184 LYS A O   
2571 C CB  . LYS A 183 ? 1.62195 1.55872 1.23664 0.04683  0.25408  0.03148  184 LYS A CB  
2572 C CG  . LYS A 183 ? 1.60536 1.54732 1.22092 0.01712  0.23118  0.01580  184 LYS A CG  
2573 C CD  . LYS A 183 ? 1.59247 1.53705 1.14663 0.07198  0.20983  0.01699  184 LYS A CD  
2574 C CE  . LYS A 183 ? 1.57233 1.51591 1.12259 0.04411  0.17870  -0.00483 184 LYS A CE  
2575 N NZ  . LYS A 183 ? 1.61119 1.53835 1.09743 0.08948  0.13743  -0.02568 184 LYS A NZ  
2589 N N   . VAL A 184 ? 1.58693 1.49961 1.27310 0.01899  0.30313  0.04082  185 VAL A N   
2590 C CA  . VAL A 184 ? 1.59317 1.50440 1.27659 0.05660  0.32768  0.06230  185 VAL A CA  
2591 C C   . VAL A 184 ? 1.62872 1.53000 1.37567 0.01393  0.36817  0.07269  185 VAL A C   
2592 O O   . VAL A 184 ? 1.57436 1.46441 1.33100 0.01346  0.37270  0.06955  185 VAL A O   
2593 C CB  . VAL A 184 ? 1.60886 1.51219 1.25344 0.08225  0.28569  0.03846  185 VAL A CB  
2594 C CG1 . VAL A 184 ? 1.64431 1.55321 1.22237 0.13354  0.24689  0.02815  185 VAL A CG1 
2595 C CG2 . VAL A 184 ? 1.99797 1.88667 1.67044 0.02527  0.25660  0.00357  185 VAL A CG2 
2605 N N   . ARG A 185 ? 1.63686 1.54169 1.42917 -0.02129 0.39677  0.08449  186 ARG A N   
2606 C CA  . ARG A 185 ? 1.73352 1.62431 1.58810 -0.06403 0.43336  0.09016  186 ARG A CA  
2607 C C   . ARG A 185 ? 1.75508 1.65216 1.64600 -0.03843 0.48720  0.13520  186 ARG A C   
2608 O O   . ARG A 185 ? 1.64295 1.52358 1.58678 -0.06625 0.52046  0.14219  186 ARG A O   
2609 C CB  . ARG A 185 ? 1.81967 1.70787 1.70925 -0.12715 0.42553  0.06800  186 ARG A CB  
2610 C CG  . ARG A 185 ? 1.86280 1.74406 1.72804 -0.15877 0.37991  0.02730  186 ARG A CG  
2611 C CD  . ARG A 185 ? 1.69178 1.58535 1.56723 -0.19458 0.36497  0.01474  186 ARG A CD  
2612 N NE  . ARG A 185 ? 1.55204 1.43341 1.43661 -0.24585 0.34485  -0.01898 186 ARG A NE  
2613 C CZ  . ARG A 185 ? 1.63255 1.52457 1.51054 -0.27309 0.31907  -0.03700 186 ARG A CZ  
2614 N NH1 . ARG A 185 ? 1.49770 1.41166 1.36036 -0.25582 0.30785  -0.02653 186 ARG A NH1 
2615 N NH2 . ARG A 185 ? 1.66575 1.54701 1.55088 -0.31536 0.30602  -0.06411 186 ARG A NH2 
2629 N N   . LYS A 186 ? 1.77145 1.69041 1.63662 0.01557  0.49820  0.16703  187 LYS A N   
2630 C CA  . LYS A 186 ? 1.77819 1.70806 1.69001 0.03540  0.55250  0.21537  187 LYS A CA  
2631 C C   . LYS A 186 ? 1.78102 1.69556 1.72419 0.04698  0.59209  0.23721  187 LYS A C   
2632 O O   . LYS A 186 ? 1.79474 1.70317 1.80834 0.02670  0.63654  0.26246  187 LYS A O   
2633 C CB  . LYS A 186 ? 1.85753 1.81415 1.72337 0.10440  0.55831  0.24871  187 LYS A CB  
2634 C CG  . LYS A 186 ? 2.00703 1.98054 1.85716 0.09464  0.53312  0.23882  187 LYS A CG  
2635 C CD  . LYS A 186 ? 2.02798 2.00939 1.96002 0.04113  0.55743  0.25026  187 LYS A CD  
2636 C CE  . LYS A 186 ? 2.02131 2.02252 1.93897 0.03026  0.53070  0.24045  187 LYS A CE  
2637 N NZ  . LYS A 186 ? 2.02182 2.03120 2.02038 -0.03143 0.54277  0.24105  187 LYS A NZ  
2651 N N   . PHE A 187 ? 1.76157 1.66981 1.65816 0.07946  0.57633  0.22852  188 PHE A N   
2652 C CA  . PHE A 187 ? 1.72469 1.62123 1.64792 0.09693  0.61535  0.25317  188 PHE A CA  
2653 C C   . PHE A 187 ? 1.91683 1.78297 1.90266 0.03174  0.63056  0.23362  188 PHE A C   
2654 O O   . PHE A 187 ? 1.77452 1.62685 1.80201 0.03758  0.67413  0.25895  188 PHE A O   
2655 C CB  . PHE A 187 ? 1.81616 1.71711 1.67547 0.14623  0.58929  0.24619  188 PHE A CB  
2656 C CG  . PHE A 187 ? 1.98779 1.91492 1.78949 0.22666  0.59243  0.27783  188 PHE A CG  
2657 C CD1 . PHE A 187 ? 1.93827 1.87653 1.75932 0.27417  0.64809  0.33250  188 PHE A CD1 
2658 C CD2 . PHE A 187 ? 2.13591 2.07502 1.86373 0.25743  0.54101  0.25366  188 PHE A CD2 
2659 C CE1 . PHE A 187 ? 2.00032 1.96390 1.76175 0.35427  0.65345  0.36373  188 PHE A CE1 
2660 C CE2 . PHE A 187 ? 2.17915 2.13970 1.84552 0.33616  0.54301  0.27997  188 PHE A CE2 
2661 C CZ  . PHE A 187 ? 2.12318 2.09739 1.80317 0.38635  0.59983  0.33572  188 PHE A CZ  
2671 N N   . VAL A 188 ? 2.06361 1.91798 2.05486 -0.02662 0.59737  0.19028  189 VAL A N   
2672 C CA  . VAL A 188 ? 1.81752 1.64148 1.85945 -0.08691 0.60905  0.16731  189 VAL A CA  
2673 C C   . VAL A 188 ? 1.82631 1.64693 1.92865 -0.13142 0.62712  0.16874  189 VAL A C   
2674 O O   . VAL A 188 ? 1.90123 1.69832 2.06452 -0.15900 0.66207  0.17489  189 VAL A O   
2675 C CB  . VAL A 188 ? 1.83305 1.64627 1.84193 -0.12016 0.56248  0.11944  189 VAL A CB  
2676 C CG1 . VAL A 188 ? 1.97659 1.76041 2.02950 -0.18281 0.57161  0.09252  189 VAL A CG1 
2677 C CG2 . VAL A 188 ? 1.88112 1.69343 1.85378 -0.08465 0.55062  0.11932  189 VAL A CG2 
2687 N N   . THR A 189 ? 1.78691 1.63043 1.87606 -0.13920 0.60206  0.16208  190 THR A N   
2688 C CA  . THR A 189 ? 1.80908 1.65570 1.95745 -0.18253 0.61230  0.16179  190 THR A CA  
2689 C C   . THR A 189 ? 1.82528 1.70830 1.95684 -0.15938 0.59983  0.17994  190 THR A C   
2690 O O   . THR A 189 ? 1.89277 1.79104 1.95697 -0.12886 0.56704  0.17145  190 THR A O   
2691 C CB  . THR A 189 ? 1.83916 1.66680 1.99525 -0.24746 0.58310  0.11165  190 THR A CB  
2692 O OG1 . THR A 189 ? 1.89050 1.72482 2.10491 -0.28761 0.58885  0.11032  190 THR A OG1 
2693 C CG2 . THR A 189 ? 1.85376 1.69374 1.94227 -0.24781 0.53176  0.08038  190 THR A CG2 
2701 N N   . ASP A 190 ? 1.84846 1.74429 2.04602 -0.17412 0.62622  0.20517  191 ASP A N   
2702 C CA  . ASP A 190 ? 1.91447 1.84615 2.10959 -0.16060 0.61722  0.22309  191 ASP A CA  
2703 C C   . ASP A 190 ? 1.95471 1.89295 2.15533 -0.21607 0.57808  0.18378  191 ASP A C   
2704 O O   . ASP A 190 ? 1.89881 1.86792 2.10204 -0.21076 0.56857  0.19640  191 ASP A O   
2705 C CB  . ASP A 190 ? 1.72627 1.67470 1.99975 -0.14653 0.66715  0.27656  191 ASP A CB  
2706 C CG  . ASP A 190 ? 2.02472 1.97643 2.28434 -0.07835 0.70814  0.32514  191 ASP A CG  
2707 O OD1 . ASP A 190 ? 2.09476 2.04904 2.26996 -0.03000 0.69010  0.32103  191 ASP A OD1 
2708 O OD2 . ASP A 190 ? 2.13653 2.08880 2.47164 -0.07201 0.75765  0.36782  191 ASP A OD2 
2713 N N   . THR A 191 ? 1.84565 1.75715 2.04631 -0.26546 0.55695  0.13886  192 THR A N   
2714 C CA  . THR A 191 ? 1.74795 1.66636 1.95254 -0.31647 0.52148  0.10211  192 THR A CA  
2715 C C   . THR A 191 ? 1.76583 1.70949 1.90488 -0.29515 0.48391  0.09444  192 THR A C   
2716 O O   . THR A 191 ? 1.78767 1.72769 1.86329 -0.25591 0.47025  0.09312  192 THR A O   
2717 C CB  . THR A 191 ? 1.57405 1.45784 1.77089 -0.36009 0.50600  0.05642  192 THR A CB  
2718 O OG1 . THR A 191 ? 1.52762 1.38353 1.78762 -0.38104 0.54102  0.06114  192 THR A OG1 
2719 C CG2 . THR A 191 ? 1.59493 1.48826 1.78691 -0.40705 0.46876  0.01916  192 THR A CG2 
2727 N N   . GLU A 192 ? 1.61294 1.58206 1.77077 -0.32090 0.46610  0.08905  193 GLU A N   
2728 C CA  . GLU A 192 ? 1.69836 1.69150 1.80283 -0.30370 0.43293  0.08365  193 GLU A CA  
2729 C C   . GLU A 192 ? 1.67365 1.66384 1.76106 -0.35106 0.39399  0.03926  193 GLU A C   
2730 O O   . GLU A 192 ? 1.72536 1.70951 1.85556 -0.39966 0.39315  0.01917  193 GLU A O   
2731 C CB  . GLU A 192 ? 1.95838 1.98998 2.09581 -0.28716 0.44595  0.12056  193 GLU A CB  
2732 C CG  . GLU A 192 ? 2.23636 2.27655 2.39013 -0.23359 0.48846  0.17176  193 GLU A CG  
2733 C CD  . GLU A 192 ? 2.24334 2.28529 2.31412 -0.16805 0.48002  0.18297  193 GLU A CD  
2734 O OE1 . GLU A 192 ? 2.01862 2.06315 2.03138 -0.16451 0.44123  0.15758  193 GLU A OE1 
2735 O OE2 . GLU A 192 ? 2.30622 2.34620 2.36990 -0.11846 0.51166  0.21686  193 GLU A OE2 
2742 N N   . VAL A 193 ? 1.60544 1.59900 1.62947 -0.33421 0.36143  0.02407  194 VAL A N   
2743 C CA  . VAL A 193 ? 1.50244 1.49983 1.50852 -0.37137 0.32625  -0.01010 194 VAL A CA  
2744 C C   . VAL A 193 ? 1.52898 1.56159 1.57055 -0.39338 0.32044  -0.00219 194 VAL A C   
2745 O O   . VAL A 193 ? 1.44038 1.49883 1.49795 -0.36640 0.33380  0.03112  194 VAL A O   
2746 C CB  . VAL A 193 ? 1.41216 1.40511 1.35162 -0.34474 0.29507  -0.02256 194 VAL A CB  
2747 C CG1 . VAL A 193 ? 1.49911 1.50435 1.42460 -0.37605 0.26266  -0.04709 194 VAL A CG1 
2748 C CG2 . VAL A 193 ? 1.45392 1.41462 1.36820 -0.33448 0.29421  -0.03657 194 VAL A CG2 
2758 N N   . GLU A 194 ? 1.57320 1.60915 1.62671 -0.44027 0.30055  -0.03167 195 GLU A N   
2759 C CA  . GLU A 194 ? 1.55380 1.62620 1.64183 -0.46531 0.28914  -0.02875 195 GLU A CA  
2760 C C   . GLU A 194 ? 1.36048 1.43972 1.41140 -0.49005 0.25303  -0.06060 195 GLU A C   
2761 O O   . GLU A 194 ? 1.37238 1.42480 1.39262 -0.50361 0.24287  -0.08884 195 GLU A O   
2762 C CB  . GLU A 194 ? 1.59152 1.66571 1.75543 -0.50313 0.30622  -0.02977 195 GLU A CB  
2763 C CG  . GLU A 194 ? 1.88039 1.92949 2.08224 -0.48929 0.34525  -0.00931 195 GLU A CG  
2764 C CD  . GLU A 194 ? 2.08972 2.15945 2.30753 -0.44213 0.37257  0.04060  195 GLU A CD  
2765 O OE1 . GLU A 194 ? 1.83559 1.93743 2.03364 -0.42004 0.36084  0.05782  195 GLU A OE1 
2766 O OE2 . GLU A 194 ? 1.96166 2.01529 2.21025 -0.42406 0.40783  0.06439  195 GLU A OE2 
2773 N N   . GLU A 195 ? 1.35169 1.46910 1.40778 -0.49353 0.23617  -0.05235 196 GLU A N   
2774 C CA  . GLU A 195 ? 1.37790 1.50844 1.40184 -0.51336 0.20393  -0.07637 196 GLU A CA  
2775 C C   . GLU A 195 ? 1.46681 1.60675 1.52522 -0.56192 0.19398  -0.10187 196 GLU A C   
2776 O O   . GLU A 195 ? 1.50400 1.65996 1.62344 -0.58027 0.20431  -0.09323 196 GLU A O   
2777 C CB  . GLU A 195 ? 1.47380 1.64163 1.48591 -0.49187 0.19072  -0.05469 196 GLU A CB  
2778 C CG  . GLU A 195 ? 1.55398 1.70932 1.52260 -0.44085 0.19492  -0.03530 196 GLU A CG  
2779 C CD  . GLU A 195 ? 1.91223 2.10022 1.86701 -0.41761 0.18339  -0.01493 196 GLU A CD  
2780 O OE1 . GLU A 195 ? 2.04775 2.26851 2.01938 -0.44274 0.16786  -0.01842 196 GLU A OE1 
2781 O OE2 . GLU A 195 ? 2.21146 2.39219 2.13615 -0.37184 0.18947  0.00414  196 GLU A OE2 
2788 N N   . THR A 196 ? 1.64273 1.77278 1.66320 -0.58105 0.17327  -0.13311 197 THR A N   
2789 C CA  . THR A 196 ? 1.52444 1.65726 1.56227 -0.62250 0.16111  -0.16395 197 THR A CA  
2790 C C   . THR A 196 ? 1.42141 1.60096 1.46146 -0.63872 0.13303  -0.16824 197 THR A C   
2791 O O   . THR A 196 ? 1.48369 1.67203 1.54062 -0.67184 0.11851  -0.19434 197 THR A O   
2792 C CB  . THR A 196 ? 1.52688 1.62275 1.51920 -0.63078 0.15796  -0.19472 197 THR A CB  
2793 O OG1 . THR A 196 ? 1.73670 1.83891 1.67651 -0.61298 0.14205  -0.19298 197 THR A OG1 
2794 C CG2 . THR A 196 ? 1.59937 1.65080 1.59574 -0.61822 0.18572  -0.19196 197 THR A CG2 
2802 N N   . GLY A 197 ? 1.45268 1.66141 1.47414 -0.61482 0.12380  -0.14489 198 GLY A N   
2803 C CA  . GLY A 197 ? 1.44896 1.70702 1.47789 -0.62600 0.09998  -0.14210 198 GLY A CA  
2804 C C   . GLY A 197 ? 1.45506 1.72146 1.42611 -0.61976 0.07853  -0.15216 198 GLY A C   
2805 O O   . GLY A 197 ? 1.59213 1.90183 1.56518 -0.62579 0.05881  -0.14785 198 GLY A O   
2809 N N   . THR A 198 ? 1.69232 1.92129 1.61717 -0.60737 0.08246  -0.16266 199 THR A N   
2810 C CA  . THR A 198 ? 1.62910 1.86333 1.50622 -0.59875 0.06640  -0.16677 199 THR A CA  
2811 C C   . THR A 198 ? 1.52589 1.73770 1.37854 -0.56390 0.07249  -0.14815 199 THR A C   
2812 O O   . THR A 198 ? 1.44909 1.63379 1.30990 -0.54732 0.08870  -0.13986 199 THR A O   
2813 C CB  . THR A 198 ? 1.37706 1.58864 1.22493 -0.61669 0.06333  -0.19701 199 THR A CB  
2814 O OG1 . THR A 198 ? 1.40979 1.57381 1.25475 -0.61135 0.08317  -0.20369 199 THR A OG1 
2815 C CG2 . THR A 198 ? 1.43609 1.66641 1.30191 -0.64915 0.05241  -0.22159 199 THR A CG2 
2823 N N   . PHE A 199 ? 1.59672 1.81983 1.42000 -0.55169 0.05819  -0.14208 200 PHE A N   
2824 C CA  . PHE A 199 ? 1.54352 1.74585 1.34630 -0.51979 0.05753  -0.12756 200 PHE A CA  
2825 C C   . PHE A 199 ? 1.52552 1.71348 1.30039 -0.52000 0.04888  -0.13609 200 PHE A C   
2826 O O   . PHE A 199 ? 1.58481 1.79576 1.34933 -0.53555 0.04042  -0.14255 200 PHE A O   
2827 C CB  . PHE A 199 ? 1.60840 1.84008 1.41391 -0.49810 0.05048  -0.10316 200 PHE A CB  
2828 C CG  . PHE A 199 ? 1.62399 1.82821 1.41077 -0.46162 0.05028  -0.09112 200 PHE A CG  
2829 C CD1 . PHE A 199 ? 1.45451 1.64222 1.24720 -0.43887 0.06326  -0.08157 200 PHE A CD1 
2830 C CD2 . PHE A 199 ? 1.57948 1.77350 1.34338 -0.44820 0.03659  -0.08960 200 PHE A CD2 
2831 C CE1 . PHE A 199 ? 1.56716 1.72829 1.33601 -0.40220 0.05912  -0.07497 200 PHE A CE1 
2832 C CE2 . PHE A 199 ? 1.49198 1.65684 1.24027 -0.41525 0.03182  -0.08359 200 PHE A CE2 
2833 C CZ  . PHE A 199 ? 1.57373 1.72189 1.32082 -0.39155 0.04133  -0.07842 200 PHE A CZ  
2843 N N   . ASN A 200 ? 1.55916 1.71103 1.32432 -0.50106 0.05076  -0.13463 201 ASN A N   
2844 C CA  . ASN A 200 ? 1.46806 1.60331 1.21920 -0.50021 0.04544  -0.13850 201 ASN A CA  
2845 C C   . ASN A 200 ? 1.37519 1.49804 1.12197 -0.47283 0.03342  -0.12468 201 ASN A C   
2846 O O   . ASN A 200 ? 1.59520 1.69912 1.34306 -0.45116 0.03228  -0.12096 201 ASN A O   
2847 C CB  . ASN A 200 ? 1.51109 1.61122 1.26496 -0.50716 0.05758  -0.15242 201 ASN A CB  
2848 C CG  . ASN A 200 ? 1.60412 1.70588 1.36463 -0.53022 0.07114  -0.16807 201 ASN A CG  
2849 O OD1 . ASN A 200 ? 1.65956 1.77580 1.41079 -0.55007 0.07101  -0.18000 201 ASN A OD1 
2850 N ND2 . ASN A 200 ? 1.66172 1.74722 1.43778 -0.52566 0.08285  -0.16841 201 ASN A ND2 
2857 N N   . ILE A 201 ? 1.28982 1.42195 1.03106 -0.47173 0.02460  -0.11729 202 ILE A N   
2858 C CA  . ILE A 201 ? 1.28944 1.40437 1.03246 -0.44861 0.01201  -0.10633 202 ILE A CA  
2859 C C   . ILE A 201 ? 1.29120 1.38533 1.04472 -0.45381 0.01224  -0.10757 202 ILE A C   
2860 O O   . ILE A 201 ? 1.46429 1.57740 1.21452 -0.46749 0.01835  -0.10379 202 ILE A O   
2861 C CB  . ILE A 201 ? 1.29214 1.43791 1.02893 -0.43951 0.00364  -0.08961 202 ILE A CB  
2862 C CG1 . ILE A 201 ? 1.29073 1.46081 1.02416 -0.43318 0.00556  -0.08411 202 ILE A CG1 
2863 C CG2 . ILE A 201 ? 1.40691 1.52777 1.14846 -0.41589 -0.00926 -0.08038 202 ILE A CG2 
2864 C CD1 . ILE A 201 ? 1.50662 1.71583 1.23650 -0.42701 -0.00043 -0.06609 202 ILE A CD1 
2876 N N   . GLN A 202 ? 1.29497 1.35234 1.06226 -0.44095 0.00542  -0.11160 203 GLN A N   
2877 C CA  . GLN A 202 ? 1.32424 1.36120 1.11365 -0.44584 0.00622  -0.11061 203 GLN A CA  
2878 C C   . GLN A 202 ? 1.29735 1.31454 1.10810 -0.42843 -0.01230 -0.10160 203 GLN A C   
2879 O O   . GLN A 202 ? 1.36178 1.37121 1.16404 -0.40917 -0.02684 -0.10198 203 GLN A O   
2880 C CB  . GLN A 202 ? 1.39868 1.40956 1.19704 -0.44852 0.01224  -0.12397 203 GLN A CB  
2881 C CG  . GLN A 202 ? 1.57904 1.60085 1.36022 -0.46260 0.02979  -0.13476 203 GLN A CG  
2882 C CD  . GLN A 202 ? 1.70515 1.75335 1.47414 -0.48377 0.04306  -0.13505 203 GLN A CD  
2883 O OE1 . GLN A 202 ? 1.74423 1.82098 1.49773 -0.49037 0.04261  -0.13509 203 GLN A OE1 
2884 N NE2 . GLN A 202 ? 1.82973 1.86984 1.60543 -0.49245 0.05427  -0.13502 203 GLN A NE2 
2893 N N   . ALA A 203 ? 1.41286 1.42049 1.25408 -0.43403 -0.01085 -0.09274 204 ALA A N   
2894 C CA  . ALA A 203 ? 1.45933 1.44430 1.33403 -0.42083 -0.02914 -0.08446 204 ALA A CA  
2895 C C   . ALA A 203 ? 1.36944 1.34642 1.28862 -0.43072 -0.02188 -0.07222 204 ALA A C   
2896 O O   . ALA A 203 ? 1.30630 1.30120 1.22081 -0.44460 0.00035  -0.06587 204 ALA A O   
2897 C CB  . ALA A 203 ? 1.74726 1.74924 1.61369 -0.41152 -0.03350 -0.06923 204 ALA A CB  
2903 N N   . ASP A 204 ? 1.46998 1.41892 1.43439 -0.42189 -0.04127 -0.06893 205 ASP A N   
2904 C CA  . ASP A 204 ? 1.32191 1.26321 1.34503 -0.42919 -0.03649 -0.05143 205 ASP A CA  
2905 C C   . ASP A 204 ? 1.33183 1.26952 1.39007 -0.42181 -0.04414 -0.03084 205 ASP A C   
2906 O O   . ASP A 204 ? 1.34331 1.26290 1.39666 -0.40785 -0.06653 -0.03982 205 ASP A O   
2907 C CB  . ASP A 204 ? 1.46093 1.37037 1.52515 -0.42781 -0.05562 -0.06547 205 ASP A CB  
2908 C CG  . ASP A 204 ? 1.36605 1.27981 1.40852 -0.43554 -0.04159 -0.07805 205 ASP A CG  
2909 O OD1 . ASP A 204 ? 1.30301 1.23815 1.33606 -0.44779 -0.01254 -0.06641 205 ASP A OD1 
2910 O OD2 . ASP A 204 ? 1.51832 1.41306 1.55085 -0.42674 -0.05904 -0.09946 205 ASP A OD2 
2915 N N   . ILE A 205 ? 1.40683 1.36075 1.49985 -0.42838 -0.02335 -0.00159 206 ILE A N   
2916 C CA  . ILE A 205 ? 1.47340 1.42255 1.61526 -0.42168 -0.02587 0.02451  206 ILE A CA  
2917 C C   . ILE A 205 ? 1.42565 1.36058 1.64947 -0.42849 -0.02258 0.04311  206 ILE A C   
2918 O O   . ILE A 205 ? 1.41772 1.37298 1.64868 -0.43596 0.00472  0.06008  206 ILE A O   
2919 C CB  . ILE A 205 ? 1.41735 1.40627 1.52856 -0.41835 -0.00001 0.05135  206 ILE A CB  
2920 C CG1 . ILE A 205 ? 1.53295 1.53484 1.58171 -0.41009 -0.00928 0.03693  206 ILE A CG1 
2921 C CG2 . ILE A 205 ? 1.44356 1.42949 1.61897 -0.41164 0.00667  0.08749  206 ILE A CG2 
2922 C CD1 . ILE A 205 ? 1.73168 1.78056 1.73858 -0.40820 0.01314  0.05691  206 ILE A CD1 
2934 N N   . HIS A 206 ? 1.42474 1.32442 1.71212 -0.42490 -0.05080 0.03969  207 HIS A N   
2935 C CA  . HIS A 206 ? 1.58718 1.47311 1.96905 -0.43252 -0.05227 0.05895  207 HIS A CA  
2936 C C   . HIS A 206 ? 1.63570 1.53444 2.07158 -0.42973 -0.03038 0.10354  207 HIS A C   
2937 O O   . HIS A 206 ? 1.55610 1.45423 1.97741 -0.41966 -0.03268 0.11096  207 HIS A O   
2938 C CB  . HIS A 206 ? 1.63892 1.47983 2.07016 -0.43071 -0.09794 0.03113  207 HIS A CB  
2939 C CG  . HIS A 206 ? 1.54159 1.37182 1.93263 -0.43052 -0.11711 -0.00627 207 HIS A CG  
2940 N ND1 . HIS A 206 ? 1.75953 1.57006 2.20874 -0.43586 -0.14050 -0.01842 207 HIS A ND1 
2941 C CD2 . HIS A 206 ? 1.41893 1.25785 1.72151 -0.42448 -0.11495 -0.03115 207 HIS A CD2 
2942 C CE1 . HIS A 206 ? 1.95395 1.76130 2.34656 -0.43088 -0.15117 -0.04910 207 HIS A CE1 
2943 N NE2 . HIS A 206 ? 1.59017 1.41350 1.89552 -0.42415 -0.13463 -0.05634 207 HIS A NE2 
2950 N N   . GLN A 207 ? 1.55244 1.46396 2.05258 -0.43620 -0.00662 0.13651  208 GLN A N   
2951 C CA  . GLN A 207 ? 1.54817 1.47711 2.10150 -0.43035 0.02203  0.18649  208 GLN A CA  
2952 C C   . GLN A 207 ? 1.61911 1.58511 2.08664 -0.41870 0.04965  0.19942  208 GLN A C   
2953 O O   . GLN A 207 ? 1.77472 1.74346 2.24984 -0.40812 0.05224  0.21887  208 GLN A O   
2954 C CB  . GLN A 207 ? 1.47951 1.37282 2.11776 -0.42864 -0.00481 0.19318  208 GLN A CB  
2955 C CG  . GLN A 207 ? 1.62794 1.48601 2.36067 -0.44082 -0.03730 0.17964  208 GLN A CG  
2956 C CD  . GLN A 207 ? 2.20246 2.01262 2.98096 -0.43861 -0.08247 0.15634  208 GLN A CD  
2957 O OE1 . GLN A 207 ? 2.19339 1.97623 2.92421 -0.43533 -0.12026 0.10831  208 GLN A OE1 
2958 N NE2 . GLN A 207 ? 2.18333 1.98148 3.05432 -0.43794 -0.07780 0.19085  208 GLN A NE2 
2967 N N   . PRO A 208 ? 1.46898 1.46373 1.85605 -0.41988 0.06913  0.18840  209 PRO A N   
2968 C CA  . PRO A 208 ? 1.50963 1.54135 1.81351 -0.40971 0.08849  0.19482  209 PRO A CA  
2969 C C   . PRO A 208 ? 1.55399 1.61526 1.88259 -0.39494 0.12255  0.24688  209 PRO A C   
2970 O O   . PRO A 208 ? 1.42381 1.50895 1.70903 -0.38282 0.12900  0.25782  209 PRO A O   
2971 C CB  . PRO A 208 ? 1.52329 1.57337 1.75478 -0.41651 0.10104  0.17154  209 PRO A CB  
2972 C CG  . PRO A 208 ? 1.46136 1.49506 1.75069 -0.42467 0.10702  0.17606  209 PRO A CG  
2973 C CD  . PRO A 208 ? 1.45869 1.45373 1.83164 -0.42993 0.07470  0.17089  209 PRO A CD  
2981 N N   . GLU A 209 ? 1.69978 1.76296 2.09891 -0.39329 0.14623  0.28258  210 GLU A N   
2982 C CA  . GLU A 209 ? 1.58724 1.67885 2.01699 -0.37481 0.18281  0.33885  210 GLU A CA  
2983 C C   . GLU A 209 ? 1.54728 1.62841 2.01753 -0.36656 0.17203  0.35753  210 GLU A C   
2984 O O   . GLU A 209 ? 1.60270 1.71442 2.06490 -0.34708 0.19977  0.39805  210 GLU A O   
2985 C CB  . GLU A 209 ? 1.55163 1.64055 2.07365 -0.37461 0.20727  0.37729  210 GLU A CB  
2986 C CG  . GLU A 209 ? 1.54544 1.59206 2.18753 -0.38922 0.17976  0.37840  210 GLU A CG  
2987 C CD  . GLU A 209 ? 1.59149 1.60607 2.22842 -0.40943 0.14092  0.32497  210 GLU A CD  
2988 O OE1 . GLU A 209 ? 1.86030 1.88502 2.40617 -0.41267 0.14018  0.29118  210 GLU A OE1 
2989 O OE2 . GLU A 209 ? 1.57813 1.55731 2.30368 -0.42102 0.11036  0.31679  210 GLU A OE2 
2996 N N   . VAL A 210 ? 1.54995 1.58754 2.06052 -0.37816 0.13244  0.32855  211 VAL A N   
2997 C CA  . VAL A 210 ? 1.59355 1.61235 2.14352 -0.36981 0.11963  0.34141  211 VAL A CA  
2998 C C   . VAL A 210 ? 1.67362 1.69920 2.13094 -0.36352 0.10196  0.31084  211 VAL A C   
2999 O O   . VAL A 210 ? 1.78315 1.82763 2.22476 -0.34734 0.11428  0.33584  211 VAL A O   
3000 C CB  . VAL A 210 ? 1.57110 1.53427 2.22242 -0.38280 0.08459  0.32684  211 VAL A CB  
3001 C CG1 . VAL A 210 ? 1.64229 1.57469 2.31020 -0.37464 0.06102  0.32045  211 VAL A CG1 
3002 C CG2 . VAL A 210 ? 1.55208 1.51383 2.31974 -0.38621 0.10608  0.37259  211 VAL A CG2 
3012 N N   . ASN A 211 ? 1.66469 1.67714 2.06318 -0.37447 0.07468  0.25984  212 ASN A N   
3013 C CA  . ASN A 211 ? 1.72015 1.73372 2.04622 -0.36832 0.05505  0.23152  212 ASN A CA  
3014 C C   . ASN A 211 ? 1.72600 1.79464 1.96314 -0.36112 0.07746  0.23851  212 ASN A C   
3015 O O   . ASN A 211 ? 1.86733 1.95375 2.06789 -0.34871 0.07611  0.24434  212 ASN A O   
3016 C CB  . ASN A 211 ? 1.72178 1.70194 2.02276 -0.37912 0.01997  0.17892  212 ASN A CB  
3017 C CG  . ASN A 211 ? 1.66802 1.59202 2.04614 -0.38154 -0.01206 0.16484  212 ASN A CG  
3018 O OD1 . ASN A 211 ? 1.71627 1.61801 2.14038 -0.37199 -0.01970 0.17964  212 ASN A OD1 
3019 N ND2 . ASN A 211 ? 1.73216 1.63239 2.12614 -0.39348 -0.03214 0.13551  212 ASN A ND2 
3026 N N   . CYS A 212 ? 1.50685 1.60279 1.70946 -0.36764 0.09682  0.23738  213 CYS A N   
3027 C CA  . CYS A 212 ? 1.58095 1.72783 1.69957 -0.36163 0.11418  0.23896  213 CYS A CA  
3028 C C   . CYS A 212 ? 1.81296 1.98982 1.93629 -0.35285 0.15088  0.27456  213 CYS A C   
3029 O O   . CYS A 212 ? 1.83583 2.02847 1.91309 -0.35825 0.16182  0.25988  213 CYS A O   
3030 C CB  . CYS A 212 ? 1.55051 1.69833 1.60337 -0.37656 0.09769  0.19145  213 CYS A CB  
3031 S SG  . CYS A 212 ? 1.64609 1.76274 1.72405 -0.39444 0.09637  0.16793  213 CYS A SG  
3037 N N   . PRO A 213 ? 1.78499 1.96943 1.96346 -0.33638 0.17269  0.32363  214 PRO A N   
3038 C CA  . PRO A 213 ? 1.57346 1.78586 1.76083 -0.32258 0.21193  0.36353  214 PRO A CA  
3039 C C   . PRO A 213 ? 1.59830 1.86154 1.68569 -0.30958 0.22855  0.36086  214 PRO A C   
3040 O O   . PRO A 213 ? 1.56586 1.84240 1.62663 -0.30577 0.25008  0.36323  214 PRO A O   
3041 C CB  . PRO A 213 ? 1.61777 1.83016 1.88352 -0.30461 0.23061  0.41895  214 PRO A CB  
3042 C CG  . PRO A 213 ? 1.62119 1.82330 1.87970 -0.30341 0.20501  0.40692  214 PRO A CG  
3043 C CD  . PRO A 213 ? 1.73969 1.90902 1.97110 -0.32616 0.16571  0.34735  214 PRO A CD  
3051 N N   . GLY A 214 ? 1.66478 1.95684 1.69622 -0.30137 0.21784  0.35514  215 GLY A N   
3052 C CA  . GLY A 214 ? 1.69063 2.03287 1.62863 -0.28944 0.22717  0.34876  215 GLY A CA  
3053 C C   . GLY A 214 ? 1.75062 2.08702 1.63283 -0.30843 0.21647  0.30020  215 GLY A C   
3054 O O   . GLY A 214 ? 1.76741 2.12349 1.60631 -0.29881 0.23712  0.30226  215 GLY A O   
3058 N N   . PHE A 215 ? 1.62587 1.93353 1.50756 -0.33303 0.18555  0.25671  216 PHE A N   
3059 C CA  . PHE A 215 ? 1.59796 1.89681 1.43421 -0.35165 0.17652  0.21204  216 PHE A CA  
3060 C C   . PHE A 215 ? 1.66497 1.93357 1.53951 -0.35696 0.19362  0.21512  216 PHE A C   
3061 O O   . PHE A 215 ? 1.72211 1.99346 1.55244 -0.36122 0.20247  0.19408  216 PHE A O   
3062 C CB  . PHE A 215 ? 1.49002 1.76707 1.32177 -0.37256 0.14322  0.17154  216 PHE A CB  
3063 C CG  . PHE A 215 ? 1.52847 1.79402 1.32236 -0.39185 0.13529  0.12829  216 PHE A CG  
3064 C CD1 . PHE A 215 ? 1.55803 1.85514 1.28349 -0.39639 0.12922  0.10354  216 PHE A CD1 
3065 C CD2 . PHE A 215 ? 1.61893 1.84237 1.44968 -0.40517 0.13310  0.11276  216 PHE A CD2 
3066 C CE1 . PHE A 215 ? 1.60699 1.88989 1.30447 -0.41469 0.12319  0.06457  216 PHE A CE1 
3067 C CE2 . PHE A 215 ? 1.52974 1.74171 1.32808 -0.42110 0.12883  0.07603  216 PHE A CE2 
3068 C CZ  . PHE A 215 ? 1.49902 1.73875 1.23218 -0.42625 0.12497  0.05222  216 PHE A CZ  
3078 N N   . PHE A 216 ? 1.65957 1.89866 1.61909 -0.35680 0.19744  0.24046  217 PHE A N   
3079 C CA  . PHE A 216 ? 1.70499 1.91981 1.71189 -0.36135 0.21342  0.24822  217 PHE A CA  
3080 C C   . PHE A 216 ? 1.65972 1.90418 1.63880 -0.34013 0.25262  0.27843  217 PHE A C   
3081 O O   . PHE A 216 ? 1.65582 1.89469 1.60871 -0.34303 0.26531  0.26336  217 PHE A O   
3082 C CB  . PHE A 216 ? 1.67106 1.85445 1.78357 -0.36383 0.20822  0.27417  217 PHE A CB  
3083 C CG  . PHE A 216 ? 1.52335 1.68511 1.69872 -0.36950 0.22180  0.28538  217 PHE A CG  
3084 C CD1 . PHE A 216 ? 1.67321 1.80643 1.84963 -0.38890 0.20303  0.24669  217 PHE A CD1 
3085 C CD2 . PHE A 216 ? 1.53067 1.70320 1.76818 -0.35360 0.25498  0.33826  217 PHE A CD2 
3086 C CE1 . PHE A 216 ? 1.66410 1.78110 1.90129 -0.39324 0.21494  0.25879  217 PHE A CE1 
3087 C CE2 . PHE A 216 ? 1.68306 1.83946 1.98578 -0.35850 0.26814  0.35199  217 PHE A CE2 
3088 C CZ  . PHE A 216 ? 1.45211 1.58124 1.75418 -0.37882 0.24693  0.31130  217 PHE A CZ  
3098 N N   . GLN A 217 ? 1.71855 1.99455 1.69999 -0.31509 0.27402  0.32264  218 GLN A N   
3099 C CA  . GLN A 217 ? 1.89396 2.20124 1.84108 -0.28741 0.31356  0.35494  218 GLN A CA  
3100 C C   . GLN A 217 ? 1.74928 2.07929 1.58412 -0.28433 0.31050  0.31630  218 GLN A C   
3101 O O   . GLN A 217 ? 1.83273 2.17162 1.62948 -0.26812 0.33748  0.32208  218 GLN A O   
3102 C CB  . GLN A 217 ? 2.06417 2.40400 2.03113 -0.25780 0.33618  0.41102  218 GLN A CB  
3103 C CG  . GLN A 217 ? 2.12893 2.44688 2.21708 -0.25594 0.35022  0.45918  218 GLN A CG  
3104 C CD  . GLN A 217 ? 2.10110 2.44019 2.21854 -0.23573 0.35898  0.50348  218 GLN A CD  
3105 O OE1 . GLN A 217 ? 1.92180 2.30327 1.99979 -0.20278 0.38946  0.54152  218 GLN A OE1 
3106 N NE2 . GLN A 217 ? 1.99791 2.30666 2.18170 -0.25261 0.33240  0.49849  218 GLN A NE2 
3115 N N   . LEU A 218 ? 1.68667 2.02534 1.47013 -0.29882 0.27779  0.27667  219 LEU A N   
3116 C CA  . LEU A 218 ? 1.71628 2.07512 1.40238 -0.29952 0.26974  0.23649  219 LEU A CA  
3117 C C   . LEU A 218 ? 1.76119 2.08657 1.43640 -0.31690 0.27107  0.20074  219 LEU A C   
3118 O O   . LEU A 218 ? 1.82000 2.15474 1.42971 -0.30568 0.28493  0.18583  219 LEU A O   
3119 C CB  . LEU A 218 ? 1.66896 2.04301 1.32161 -0.31530 0.23311  0.20392  219 LEU A CB  
3120 C CG  . LEU A 218 ? 1.75734 2.15864 1.31774 -0.31717 0.21907  0.16347  219 LEU A CG  
3121 C CD1 . LEU A 218 ? 2.12629 2.57413 1.62566 -0.28166 0.23851  0.18820  219 LEU A CD1 
3122 C CD2 . LEU A 218 ? 1.93989 2.35280 1.49035 -0.33752 0.18244  0.13434  219 LEU A CD2 
3134 N N   . CYS A 219 ? 1.85855 2.14383 1.59507 -0.34182 0.25658  0.18615  220 CYS A N   
3135 C CA  . CYS A 219 ? 1.86203 2.11536 1.59875 -0.35546 0.26183  0.15982  220 CYS A CA  
3136 C C   . CYS A 219 ? 1.72715 1.98122 1.47667 -0.33274 0.30222  0.19459  220 CYS A C   
3137 O O   . CYS A 219 ? 1.72804 1.97380 1.43224 -0.32944 0.31676  0.17512  220 CYS A O   
3138 C CB  . CYS A 219 ? 1.65778 1.87225 1.46446 -0.38002 0.24010  0.14636  220 CYS A CB  
3139 S SG  . CYS A 219 ? 1.58570 1.79568 1.37434 -0.40254 0.19693  0.10575  220 CYS A SG  
3145 N N   . ASN A 220 ? 1.52697 1.94904 1.43010 -0.37642 0.08331  0.10324  221 ASN A N   
3146 C CA  . ASN A 220 ? 1.56102 1.98590 1.48487 -0.36050 0.09941  0.12166  221 ASN A CA  
3147 C C   . ASN A 220 ? 1.67443 2.01745 1.55725 -0.35188 0.11700  0.09439  221 ASN A C   
3148 O O   . ASN A 220 ? 1.81183 2.14427 1.64367 -0.35765 0.14105  0.08938  221 ASN A O   
3149 C CB  . ASN A 220 ? 1.63156 2.11754 1.51882 -0.38086 0.11476  0.13702  221 ASN A CB  
3150 C CG  . ASN A 220 ? 1.50428 2.00802 1.42687 -0.35959 0.13048  0.16551  221 ASN A CG  
3151 O OD1 . ASN A 220 ? 1.51021 1.98790 1.49530 -0.33038 0.12760  0.17817  221 ASN A OD1 
3152 N ND2 . ASN A 220 ? 1.68572 2.23400 1.56935 -0.37343 0.14647  0.17771  221 ASN A ND2 
3159 N N   . GLY A 221 ? 1.67099 1.95303 1.57376 -0.33637 0.10471  0.07656  222 GLY A N   
3160 C CA  . GLY A 221 ? 1.65280 1.85527 1.52875 -0.32481 0.11805  0.05245  222 GLY A CA  
3161 C C   . GLY A 221 ? 1.81019 1.95866 1.58897 -0.34907 0.12971  0.00829  222 GLY A C   
3162 O O   . GLY A 221 ? 2.20588 2.28094 1.96862 -0.33901 0.13244  -0.01700 222 GLY A O   
3166 N N   . ASN A 222 ? 1.77456 1.95644 1.48927 -0.38132 0.13502  -0.00077 223 ASN A N   
3167 C CA  . ASN A 222 ? 1.99380 2.12847 1.61566 -0.40797 0.14336  -0.04024 223 ASN A CA  
3168 C C   . ASN A 222 ? 1.93033 2.06740 1.55370 -0.42009 0.12349  -0.05230 223 ASN A C   
3169 O O   . ASN A 222 ? 1.60319 1.78447 1.29102 -0.40983 0.10456  -0.02964 223 ASN A O   
3170 C CB  . ASN A 222 ? 2.03895 2.20167 1.58425 -0.43702 0.15904  -0.04279 223 ASN A CB  
3171 C CG  . ASN A 222 ? 2.15564 2.29781 1.67765 -0.42340 0.18347  -0.03834 223 ASN A CG  
3172 O OD1 . ASN A 222 ? 2.06343 2.17997 1.63670 -0.39271 0.18879  -0.02845 223 ASN A OD1 
3173 N ND2 . ASN A 222 ? 2.38912 2.54118 1.83308 -0.44502 0.19784  -0.04404 223 ASN A ND2 
3180 N N   . ARG A 223 ? 1.92075 2.00861 1.47080 -0.44099 0.12844  -0.08743 224 ARG A N   
3181 C CA  . ARG A 223 ? 1.85483 1.93506 1.39919 -0.45096 0.11336  -0.10120 224 ARG A CA  
3182 C C   . ARG A 223 ? 1.85775 1.99532 1.36090 -0.48815 0.10977  -0.09643 224 ARG A C   
3183 O O   . ARG A 223 ? 2.14328 2.27014 1.57076 -0.51639 0.12103  -0.11230 224 ARG A O   
3184 C CB  . ARG A 223 ? 1.88605 1.87929 1.37927 -0.45176 0.11996  -0.14031 224 ARG A CB  
3185 C CG  . ARG A 223 ? 2.03945 1.97249 1.57733 -0.41503 0.11927  -0.14555 224 ARG A CG  
3186 C CD  . ARG A 223 ? 2.32910 2.18181 1.82129 -0.41634 0.12162  -0.18345 224 ARG A CD  
3187 N NE  . ARG A 223 ? 2.22563 2.05099 1.62641 -0.44660 0.13908  -0.20999 224 ARG A NE  
3188 C CZ  . ARG A 223 ? 2.32105 2.13189 1.66109 -0.47487 0.13793  -0.23277 224 ARG A CZ  
3189 N NH1 . ARG A 223 ? 2.40837 2.21859 1.76608 -0.47349 0.12385  -0.23635 224 ARG A NH1 
3190 N NH2 . ARG A 223 ? 2.51426 2.30911 1.77263 -0.50423 0.15074  -0.25122 224 ARG A NH2 
3204 N N   . LEU A 224 ? 1.71580 1.91147 1.26740 -0.48766 0.09285  -0.07404 225 LEU A N   
3205 C CA  . LEU A 224 ? 1.73776 1.99966 1.26600 -0.52083 0.08712  -0.06146 225 LEU A CA  
3206 C C   . LEU A 224 ? 1.72394 1.96262 1.20381 -0.54474 0.08271  -0.08374 225 LEU A C   
3207 O O   . LEU A 224 ? 1.74801 1.96582 1.25592 -0.52800 0.07419  -0.08841 225 LEU A O   
3208 C CB  . LEU A 224 ? 1.75769 2.09606 1.36388 -0.50745 0.07192  -0.02404 225 LEU A CB  
3209 C CG  . LEU A 224 ? 1.84240 2.26078 1.43776 -0.53879 0.06555  -0.00351 225 LEU A CG  
3210 C CD1 . LEU A 224 ? 1.88161 2.37195 1.55059 -0.52207 0.05718  0.03490  225 LEU A CD1 
3211 C CD2 . LEU A 224 ? 1.87516 2.30610 1.45991 -0.55515 0.05475  -0.00734 225 LEU A CD2 
3223 N N   . MET A 225 ? 1.84763 2.08823 1.25392 -0.58301 0.08761  -0.09627 226 MET A N   
3224 C CA  . MET A 225 ? 1.89128 2.12150 1.25183 -0.61225 0.08174  -0.11176 226 MET A CA  
3225 C C   . MET A 225 ? 1.78147 2.08892 1.13218 -0.64655 0.07181  -0.08887 226 MET A C   
3226 O O   . MET A 225 ? 2.13757 2.46430 1.45116 -0.66639 0.07538  -0.08460 226 MET A O   
3227 C CB  . MET A 225 ? 1.89164 2.04453 1.16829 -0.62998 0.09291  -0.14918 226 MET A CB  
3228 C CG  . MET A 225 ? 1.97894 2.05251 1.26211 -0.59866 0.10218  -0.17347 226 MET A CG  
3229 S SD  . MET A 225 ? 2.06489 2.04826 1.24685 -0.62009 0.11539  -0.21745 226 MET A SD  
3230 C CE  . MET A 225 ? 2.37123 2.27619 1.58483 -0.57980 0.12095  -0.23898 226 MET A CE  
3240 N N   . ALA A 226 ? 1.71156 2.06222 1.09446 -0.65212 0.05943  -0.07299 227 ALA A N   
3241 C CA  . ALA A 226 ? 1.71223 2.14215 1.09750 -0.68270 0.04829  -0.04670 227 ALA A CA  
3242 C C   . ALA A 226 ? 1.75043 2.18595 1.11847 -0.70589 0.04000  -0.04893 227 ALA A C   
3243 O O   . ALA A 226 ? 2.13475 2.53943 1.52372 -0.68475 0.04073  -0.05716 227 ALA A O   
3244 C CB  . ALA A 226 ? 1.75550 2.25886 1.22173 -0.65978 0.04099  -0.01013 227 ALA A CB  
3250 N N   . ALA A 227 ? 1.86000 2.33473 1.19041 -0.74877 0.03136  -0.03979 228 ALA A N   
3251 C CA  . ALA A 227 ? 1.97328 2.45974 1.28728 -0.77620 0.02238  -0.03729 228 ALA A CA  
3252 C C   . ALA A 227 ? 1.99093 2.56623 1.32122 -0.80653 0.00819  -0.00263 228 ALA A C   
3253 O O   . ALA A 227 ? 2.42410 3.02046 1.72191 -0.83179 0.00357  0.00212  228 ALA A O   
3254 C CB  . ALA A 227 ? 1.97940 2.39637 1.20932 -0.80664 0.02419  -0.07071 228 ALA A CB  
3260 N N   . HIS A 228 ? 2.05179 2.67764 1.43042 -0.80282 0.00151  0.02226  229 HIS A N   
3261 C CA  . HIS A 228 ? 2.10456 2.81765 1.50353 -0.83191 -0.01230 0.05796  229 HIS A CA  
3262 C C   . HIS A 228 ? 2.13969 2.88054 1.56789 -0.83319 -0.01638 0.07537  229 HIS A C   
3263 O O   . HIS A 228 ? 2.04675 2.78829 1.52479 -0.79294 -0.01007 0.08226  229 HIS A O   
3264 C CB  . HIS A 228 ? 2.12164 2.90036 1.57978 -0.81065 -0.01384 0.08654  229 HIS A CB  
3265 C CG  . HIS A 228 ? 2.17379 3.04296 1.65352 -0.83993 -0.02782 0.12356  229 HIS A CG  
3266 N ND1 . HIS A 228 ? 2.24444 3.12941 1.67232 -0.88922 -0.03958 0.12590  229 HIS A ND1 
3267 C CD2 . HIS A 228 ? 2.12861 3.07549 1.67523 -0.82653 -0.03307 0.16027  229 HIS A CD2 
3268 C CE1 . HIS A 228 ? 2.32300 3.29337 1.78778 -0.90605 -0.05163 0.16311  229 HIS A CE1 
3269 N NE2 . HIS A 228 ? 2.19499 3.20573 1.73228 -0.86831 -0.04679 0.18464  229 HIS A NE2 
3276 N N   . GLN A 229 ? 2.30775 3.06994 1.70440 -0.87816 -0.02763 0.08397  230 GLN A N   
3277 C CA  . GLN A 229 ? 2.18458 2.98182 1.60912 -0.88400 -0.03142 0.10632  230 GLN A CA  
3278 C C   . GLN A 229 ? 2.29459 3.02127 1.70815 -0.85967 -0.01955 0.08097  230 GLN A C   
3279 O O   . GLN A 229 ? 2.52126 3.26596 1.97893 -0.83128 -0.01419 0.09702  230 GLN A O   
3280 C CB  . GLN A 229 ? 2.17654 3.05758 1.67824 -0.85924 -0.03261 0.14739  230 GLN A CB  
3281 C CG  . GLN A 229 ? 2.34729 3.30633 1.86498 -0.88479 -0.04517 0.17676  230 GLN A CG  
3282 C CD  . GLN A 229 ? 2.35253 3.38954 1.94668 -0.85581 -0.04509 0.21540  230 GLN A CD  
3283 O OE1 . GLN A 229 ? 2.29826 3.32053 1.93021 -0.80780 -0.03569 0.21241  230 GLN A OE1 
3284 N NE2 . GLN A 229 ? 2.45990 3.57858 2.07671 -0.88479 -0.05706 0.25272  230 GLN A NE2 
3293 N N   . GLY A 230 ? 2.39918 3.04353 1.75103 -0.86934 -0.01511 0.04147  231 GLY A N   
3294 C CA  . GLY A 230 ? 2.44570 3.01793 1.78148 -0.84862 -0.00419 0.01458  231 GLY A CA  
3295 C C   . GLY A 230 ? 2.15945 2.69925 1.53540 -0.79070 0.00880  0.00496  231 GLY A C   
3296 O O   . GLY A 230 ? 1.94746 2.42727 1.31353 -0.76932 0.01751  -0.01602 231 GLY A O   
3300 N N   . ASN A 231 ? 2.11530 2.69122 1.53620 -0.76484 0.00872  0.02036  232 ASN A N   
3301 C CA  . ASN A 231 ? 1.94442 2.48601 1.40349 -0.71100 0.01678  0.01192  232 ASN A CA  
3302 C C   . ASN A 231 ? 1.84991 2.34295 1.28533 -0.70516 0.02168  -0.01371 232 ASN A C   
3303 O O   . ASN A 231 ? 1.86260 2.39609 1.30452 -0.71654 0.01787  -0.00108 232 ASN A O   
3304 C CB  . ASN A 231 ? 1.91389 2.52765 1.44349 -0.68334 0.01184  0.04918  232 ASN A CB  
3305 C CG  . ASN A 231 ? 1.98745 2.65003 1.54348 -0.68234 0.00960  0.07758  232 ASN A CG  
3306 O OD1 . ASN A 231 ? 1.90517 2.53307 1.43825 -0.68475 0.01445  0.06689  232 ASN A OD1 
3307 N ND2 . ASN A 231 ? 2.04478 2.78957 1.65020 -0.67758 0.00312  0.11567  232 ASN A ND2 
3314 N N   . LEU A 232 ? 1.89782 2.30555 1.30698 -0.68610 0.03082  -0.04790 233 LEU A N   
3315 C CA  . LEU A 232 ? 1.85974 2.21653 1.24759 -0.67694 0.03775  -0.07161 233 LEU A CA  
3316 C C   . LEU A 232 ? 1.80336 2.13907 1.24682 -0.62508 0.04005  -0.06992 233 LEU A C   
3317 O O   . LEU A 232 ? 1.99120 2.30232 1.46043 -0.59448 0.03958  -0.07143 233 LEU A O   
3318 C CB  . LEU A 232 ? 2.04839 2.32086 1.36700 -0.69217 0.04584  -0.11112 233 LEU A CB  
3319 C CG  . LEU A 232 ? 2.06170 2.33169 1.30986 -0.74250 0.04307  -0.12160 233 LEU A CG  
3320 C CD1 . LEU A 232 ? 1.96579 2.29436 1.21090 -0.77887 0.03089  -0.09877 233 LEU A CD1 
3321 C CD2 . LEU A 232 ? 1.84735 2.02453 1.02932 -0.74920 0.05193  -0.16283 233 LEU A CD2 
3333 N N   . LEU A 233 ? 1.76605 2.11001 1.22703 -0.61478 0.04150  -0.06546 234 LEU A N   
3334 C CA  . LEU A 233 ? 1.83211 2.15344 1.34619 -0.56877 0.04114  -0.06273 234 LEU A CA  
3335 C C   . LEU A 233 ? 1.83009 2.08504 1.31561 -0.56233 0.05178  -0.08927 234 LEU A C   
3336 O O   . LEU A 233 ? 2.06933 2.32427 1.50799 -0.59048 0.05866  -0.09760 234 LEU A O   
3337 C CB  . LEU A 233 ? 1.61422 2.01260 1.18962 -0.55726 0.03244  -0.02630 234 LEU A CB  
3338 C CG  . LEU A 233 ? 1.67042 2.04892 1.30610 -0.51079 0.02796  -0.01917 234 LEU A CG  
3339 C CD1 . LEU A 233 ? 1.48032 1.93163 1.18123 -0.49359 0.01493  0.01808  234 LEU A CD1 
3340 C CD2 . LEU A 233 ? 1.85172 2.20993 1.48420 -0.50823 0.03556  -0.02562 234 LEU A CD2 
3352 N N   . PHE A 234 ? 1.60694 1.80359 1.11930 -0.52404 0.05252  -0.10147 235 PHE A N   
3353 C CA  . PHE A 234 ? 1.65419 1.78728 1.14990 -0.51216 0.06261  -0.12328 235 PHE A CA  
3354 C C   . PHE A 234 ? 1.60287 1.72249 1.16877 -0.46704 0.05488  -0.11066 235 PHE A C   
3355 O O   . PHE A 234 ? 1.77195 1.89805 1.38065 -0.44209 0.04241  -0.09888 235 PHE A O   
3356 C CB  . PHE A 234 ? 1.79728 1.84795 1.23463 -0.51847 0.07155  -0.16123 235 PHE A CB  
3357 C CG  . PHE A 234 ? 1.99081 2.05236 1.37215 -0.55731 0.07242  -0.17037 235 PHE A CG  
3358 C CD1 . PHE A 234 ? 2.06659 2.14629 1.46253 -0.55526 0.06485  -0.16215 235 PHE A CD1 
3359 C CD2 . PHE A 234 ? 2.09186 2.14344 1.40520 -0.59473 0.08001  -0.18570 235 PHE A CD2 
3360 C CE1 . PHE A 234 ? 2.17609 2.26851 1.52645 -0.59156 0.06478  -0.16672 235 PHE A CE1 
3361 C CE2 . PHE A 234 ? 2.07699 2.13642 1.34106 -0.63204 0.07717  -0.19237 235 PHE A CE2 
3362 C CZ  . PHE A 234 ? 2.19572 2.27728 1.48136 -0.63124 0.06958  -0.18197 235 PHE A CZ  
3372 N N   . ALA A 235 ? 1.69228 1.79229 1.26964 -0.45560 0.06144  -0.11132 236 ALA A N   
3373 C CA  . ALA A 235 ? 1.70831 1.80216 1.35846 -0.41570 0.05102  -0.09396 236 ALA A CA  
3374 C C   . ALA A 235 ? 1.68273 1.72684 1.33211 -0.40297 0.06185  -0.10449 236 ALA A C   
3375 O O   . ALA A 235 ? 1.80161 1.85361 1.41148 -0.42378 0.07745  -0.10880 236 ALA A O   
3376 C CB  . ALA A 235 ? 1.57936 1.75981 1.28590 -0.41296 0.04052  -0.05483 236 ALA A CB  
3382 N N   . ASN A 236 ? 1.57528 1.56698 1.26765 -0.36745 0.05275  -0.10718 237 ASN A N   
3383 C CA  . ASN A 236 ? 1.53877 1.49060 1.25290 -0.34845 0.05908  -0.10772 237 ASN A CA  
3384 C C   . ASN A 236 ? 1.49400 1.47499 1.29746 -0.31732 0.04021  -0.07340 237 ASN A C   
3385 O O   . ASN A 236 ? 1.61291 1.56255 1.45566 -0.28975 0.02023  -0.07174 237 ASN A O   
3386 C CB  . ASN A 236 ? 1.55814 1.41527 1.24628 -0.33469 0.06233  -0.14076 237 ASN A CB  
3387 C CG  . ASN A 236 ? 1.58008 1.39574 1.29354 -0.31468 0.06906  -0.13933 237 ASN A CG  
3388 O OD1 . ASN A 236 ? 1.64953 1.50368 1.41940 -0.30175 0.06548  -0.10900 237 ASN A OD1 
3389 N ND2 . ASN A 236 ? 1.68964 1.42745 1.36365 -0.31162 0.07896  -0.17047 237 ASN A ND2 
3396 N N   . PRO A 237 ? 1.58662 1.62404 1.42358 -0.31914 0.04428  -0.04494 238 PRO A N   
3397 C CA  . PRO A 237 ? 1.61166 1.68292 1.53663 -0.29167 0.02366  -0.00932 238 PRO A CA  
3398 C C   . PRO A 237 ? 1.65303 1.66088 1.62854 -0.25748 0.01186  -0.00771 238 PRO A C   
3399 O O   . PRO A 237 ? 1.59336 1.61086 1.63932 -0.23182 -0.01266 0.01685  238 PRO A O   
3400 C CB  . PRO A 237 ? 1.43590 1.57994 1.37379 -0.30550 0.03581  0.01811  238 PRO A CB  
3401 C CG  . PRO A 237 ? 1.69127 1.80806 1.55682 -0.32656 0.06344  -0.00529 238 PRO A CG  
3402 C CD  . PRO A 237 ? 1.79652 1.86643 1.59131 -0.34446 0.06710  -0.04312 238 PRO A CD  
3410 N N   . ASN A 238 ? 1.60884 1.55083 1.55123 -0.25621 0.02673  -0.03204 239 ASN A N   
3411 C CA  . ASN A 238 ? 1.70364 1.58684 1.69584 -0.22577 0.01659  -0.02793 239 ASN A CA  
3412 C C   . ASN A 238 ? 1.73964 1.53255 1.68343 -0.22204 0.02000  -0.06783 239 ASN A C   
3413 O O   . ASN A 238 ? 1.58584 1.34013 1.48641 -0.23062 0.04191  -0.08795 239 ASN A O   
3414 C CB  . ASN A 238 ? 1.76144 1.66414 1.77587 -0.22432 0.03421  -0.00783 239 ASN A CB  
3415 C CG  . ASN A 238 ? 1.71902 1.56583 1.79139 -0.19412 0.02343  0.00121  239 ASN A CG  
3416 O OD1 . ASN A 238 ? 1.42678 1.23076 1.53894 -0.17169 -0.00423 0.00070  239 ASN A OD1 
3417 N ND2 . ASN A 238 ? 1.64186 1.48737 1.71832 -0.19235 0.04467  0.01094  239 ASN A ND2 
3424 N N   . ASN A 239 ? 1.74303 1.50125 1.69222 -0.20752 -0.00146 -0.07876 240 ASN A N   
3425 C CA  . ASN A 239 ? 1.64876 1.31690 1.56446 -0.19678 -0.00382 -0.11299 240 ASN A CA  
3426 C C   . ASN A 239 ? 1.72732 1.34681 1.71294 -0.15879 -0.03382 -0.09937 240 ASN A C   
3427 O O   . ASN A 239 ? 1.65029 1.25119 1.65404 -0.13912 -0.05888 -0.09791 240 ASN A O   
3428 C CB  . ASN A 239 ? 1.59953 1.26048 1.46054 -0.20817 -0.00426 -0.13642 240 ASN A CB  
3429 C CG  . ASN A 239 ? 1.72326 1.29158 1.54561 -0.19746 -0.00474 -0.17233 240 ASN A CG  
3430 O OD1 . ASN A 239 ? 1.69195 1.20175 1.51676 -0.18766 -0.00042 -0.18419 240 ASN A OD1 
3431 N ND2 . ASN A 239 ? 1.87496 1.43065 1.66203 -0.19854 -0.00920 -0.18836 240 ASN A ND2 
3438 N N   . ASN A 240 ? 1.72850 1.32618 1.75305 -0.14755 -0.03194 -0.08758 241 ASN A N   
3439 C CA  . ASN A 240 ? 1.58520 1.13955 1.68378 -0.11376 -0.06279 -0.06925 241 ASN A CA  
3440 C C   . ASN A 240 ? 1.70225 1.30789 1.86505 -0.09916 -0.09191 -0.03409 241 ASN A C   
3441 O O   . ASN A 240 ? 1.58713 1.15299 1.77661 -0.07386 -0.12388 -0.03223 241 ASN A O   
3442 C CB  . ASN A 240 ? 1.61297 1.07001 1.68724 -0.09553 -0.07736 -0.10079 241 ASN A CB  
3443 C CG  . ASN A 240 ? 1.73800 1.13233 1.78310 -0.09865 -0.05794 -0.12450 241 ASN A CG  
3444 O OD1 . ASN A 240 ? 1.92719 1.35007 1.95469 -0.11689 -0.02917 -0.12236 241 ASN A OD1 
3445 N ND2 . ASN A 240 ? 1.93472 1.24102 1.97194 -0.07927 -0.07359 -0.14710 241 ASN A ND2 
3452 N N   . GLY A 241 ? 1.79484 1.48774 1.97903 -0.11446 -0.08098 -0.00616 242 GLY A N   
3453 C CA  . GLY A 241 ? 1.81112 1.56017 2.05960 -0.10262 -0.10597 0.03040  242 GLY A CA  
3454 C C   . GLY A 241 ? 1.64793 1.43835 1.86803 -0.11044 -0.11136 0.02702  242 GLY A C   
3455 O O   . GLY A 241 ? 1.61399 1.46712 1.87913 -0.10677 -0.12551 0.05804  242 GLY A O   
3459 N N   . ALA A 242 ? 1.62420 1.38281 1.77334 -0.12054 -0.10040 -0.00770 243 ALA A N   
3460 C CA  . ALA A 242 ? 1.37393 1.17184 1.49391 -0.12816 -0.10272 -0.01005 243 ALA A CA  
3461 C C   . ALA A 242 ? 1.43969 1.28684 1.49425 -0.16767 -0.06949 -0.02442 243 ALA A C   
3462 O O   . ALA A 242 ? 1.58723 1.40981 1.59910 -0.18544 -0.04584 -0.04543 243 ALA A O   
3463 C CB  . ALA A 242 ? 1.70827 1.43295 1.79973 -0.10652 -0.11839 -0.03471 243 ALA A CB  
3469 N N   . LEU A 243 ? 1.37944 1.29450 1.42563 -0.18103 -0.06929 -0.01212 244 LEU A N   
3470 C CA  . LEU A 243 ? 1.39660 1.35952 1.38165 -0.21942 -0.04343 -0.02332 244 LEU A CA  
3471 C C   . LEU A 243 ? 1.43376 1.36263 1.36324 -0.22352 -0.04092 -0.05043 244 LEU A C   
3472 O O   . LEU A 243 ? 1.51386 1.44583 1.45917 -0.20435 -0.05827 -0.04232 244 LEU A O   
3473 C CB  . LEU A 243 ? 1.49199 1.55372 1.50211 -0.23436 -0.04437 0.00864  244 LEU A CB  
3474 C CG  . LEU A 243 ? 1.62217 1.73699 1.57185 -0.27605 -0.02134 0.00088  244 LEU A CG  
3475 C CD1 . LEU A 243 ? 1.38005 1.58390 1.36008 -0.29065 -0.01869 0.03349  244 LEU A CD1 
3476 C CD2 . LEU A 243 ? 1.53618 1.65964 1.44962 -0.28483 -0.02347 -0.00933 244 LEU A CD2 
3488 N N   . HIS A 244 ? 1.56305 1.45924 1.42697 -0.24712 -0.01921 -0.08114 245 HIS A N   
3489 C CA  . HIS A 244 ? 1.57475 1.44630 1.38207 -0.25723 -0.01309 -0.10561 245 HIS A CA  
3490 C C   . HIS A 244 ? 1.56211 1.49837 1.32306 -0.29988 0.00480  -0.10509 245 HIS A C   
3491 O O   . HIS A 244 ? 1.61661 1.56584 1.34984 -0.32548 0.02137  -0.11053 245 HIS A O   
3492 C CB  . HIS A 244 ? 1.58358 1.36283 1.34876 -0.25263 -0.00456 -0.14230 245 HIS A CB  
3493 C CG  . HIS A 244 ? 1.55827 1.31046 1.26794 -0.26142 0.00161  -0.16616 245 HIS A CG  
3494 N ND1 . HIS A 244 ? 1.56073 1.30210 1.28169 -0.23665 -0.01331 -0.16170 245 HIS A ND1 
3495 C CD2 . HIS A 244 ? 1.59723 1.33216 1.23965 -0.29159 0.02094  -0.19266 245 HIS A CD2 
3496 C CE1 . HIS A 244 ? 1.60185 1.32285 1.26784 -0.25066 -0.00187 -0.18319 245 HIS A CE1 
3497 N NE2 . HIS A 244 ? 1.56071 1.27737 1.17970 -0.28525 0.01783  -0.20237 245 HIS A NE2 
3504 N N   . PHE A 245 ? 1.58763 1.56229 1.33909 -0.30633 0.00069  -0.09735 246 PHE A N   
3505 C CA  . PHE A 245 ? 1.56301 1.59906 1.27371 -0.34739 0.01341  -0.09425 246 PHE A CA  
3506 C C   . PHE A 245 ? 1.56524 1.58463 1.23749 -0.35285 0.01551  -0.10809 246 PHE A C   
3507 O O   . PHE A 245 ? 1.91871 1.89322 1.60305 -0.32074 0.00601  -0.11356 246 PHE A O   
3508 C CB  . PHE A 245 ? 1.56067 1.69061 1.31346 -0.35408 0.00572  -0.05705 246 PHE A CB  
3509 C CG  . PHE A 245 ? 1.45747 1.61771 1.24181 -0.33350 -0.00899 -0.03709 246 PHE A CG  
3510 C CD1 . PHE A 245 ? 1.41703 1.55887 1.25703 -0.29101 -0.02823 -0.02276 246 PHE A CD1 
3511 C CD2 . PHE A 245 ? 1.45442 1.66061 1.21222 -0.35589 -0.00444 -0.03093 246 PHE A CD2 
3512 C CE1 . PHE A 245 ? 1.40117 1.56708 1.26439 -0.26893 -0.04136 -0.00438 246 PHE A CE1 
3513 C CE2 . PHE A 245 ? 1.44360 1.67900 1.22931 -0.33423 -0.01565 -0.01035 246 PHE A CE2 
3514 C CZ  . PHE A 245 ? 1.40841 1.62236 1.24429 -0.28953 -0.03349 0.00213  246 PHE A CZ  
3524 N N   . GLY A 246 ? 1.67288 1.72826 1.29842 -0.39315 0.02706  -0.11201 247 GLY A N   
3525 C CA  . GLY A 246 ? 1.62774 1.67656 1.21855 -0.40303 0.03020  -0.12082 247 GLY A CA  
3526 C C   . GLY A 246 ? 1.55901 1.68574 1.12949 -0.44472 0.03407  -0.10403 247 GLY A C   
3527 O O   . GLY A 246 ? 1.75893 1.91851 1.31174 -0.47569 0.03908  -0.10122 247 GLY A O   
3531 N N   . ILE A 247 ? 1.55531 1.71052 1.12751 -0.44438 0.03134  -0.09142 248 ILE A N   
3532 C CA  . ILE A 247 ? 1.56295 1.79425 1.12218 -0.48262 0.03250  -0.07119 248 ILE A CA  
3533 C C   . ILE A 247 ? 1.59322 1.79656 1.10605 -0.50029 0.03962  -0.08700 248 ILE A C   
3534 O O   . ILE A 247 ? 1.65329 1.81395 1.16935 -0.47012 0.04033  -0.09444 248 ILE A O   
3535 C CB  . ILE A 247 ? 1.52681 1.83451 1.14165 -0.46568 0.02230  -0.03184 248 ILE A CB  
3536 C CG1 . ILE A 247 ? 1.49934 1.84345 1.15810 -0.45626 0.01491  -0.01419 248 ILE A CG1 
3537 C CG2 . ILE A 247 ? 1.53646 1.91710 1.13854 -0.50300 0.02343  -0.01032 248 ILE A CG2 
3538 C CD1 . ILE A 247 ? 1.46179 1.86730 1.17930 -0.43062 0.00314  0.02182  248 ILE A CD1 
3550 N N   . SER A 248 ? 1.76401 1.98911 1.23264 -0.54839 0.04372  -0.09138 249 SER A N   
3551 C CA  . SER A 248 ? 1.85769 2.05737 1.28096 -0.57113 0.04910  -0.10552 249 SER A CA  
3552 C C   . SER A 248 ? 1.91926 2.19701 1.33506 -0.61456 0.04446  -0.07946 249 SER A C   
3553 O O   . SER A 248 ? 1.82253 2.15856 1.24730 -0.63753 0.03856  -0.06138 249 SER A O   
3554 C CB  . SER A 248 ? 1.86831 1.98962 1.23131 -0.58896 0.05707  -0.14584 249 SER A CB  
3555 O OG  . SER A 248 ? 1.72010 1.76497 1.09009 -0.54872 0.06123  -0.16955 249 SER A OG  
3561 N N   . PHE A 249 ? 1.76000 2.03800 1.16026 -0.62542 0.04664  -0.07630 250 PHE A N   
3562 C CA  . PHE A 249 ? 1.85932 2.21101 1.25877 -0.66496 0.04080  -0.04752 250 PHE A CA  
3563 C C   . PHE A 249 ? 1.78119 2.10482 1.15276 -0.67574 0.04568  -0.05466 250 PHE A C   
3564 O O   . PHE A 249 ? 1.72196 1.97946 1.08495 -0.64433 0.05411  -0.07632 250 PHE A O   
3565 C CB  . PHE A 249 ? 1.81840 2.25519 1.28021 -0.64652 0.03552  -0.00420 250 PHE A CB  
3566 C CG  . PHE A 249 ? 1.68872 2.10469 1.18894 -0.58881 0.03992  0.00115  250 PHE A CG  
3567 C CD1 . PHE A 249 ? 1.81945 2.23384 1.32327 -0.57319 0.04569  0.01171  250 PHE A CD1 
3568 C CD2 . PHE A 249 ? 1.77312 2.16812 1.30416 -0.54912 0.03734  -0.00347 250 PHE A CD2 
3569 C CE1 . PHE A 249 ? 1.93676 2.32534 1.46846 -0.51707 0.04898  0.01581  250 PHE A CE1 
3570 C CE2 . PHE A 249 ? 1.69443 2.06293 1.25581 -0.49550 0.03775  0.00074  250 PHE A CE2 
3571 C CZ  . PHE A 249 ? 1.63713 2.00036 1.19581 -0.47850 0.04368  0.00942  250 PHE A CZ  
3581 N N   . LYS A 250 ? 2.02314 2.39727 1.38146 -0.72092 0.03919  -0.03503 251 LYS A N   
3582 C CA  . LYS A 250 ? 1.87750 2.23846 1.21760 -0.73369 0.04265  -0.03360 251 LYS A CA  
3583 C C   . LYS A 250 ? 1.98009 2.37268 1.36968 -0.69149 0.04972  -0.00507 251 LYS A C   
3584 O O   . LYS A 250 ? 1.90267 2.36598 1.34086 -0.67712 0.04643  0.02974  251 LYS A O   
3585 C CB  . LYS A 250 ? 2.02831 2.44015 1.34780 -0.79401 0.03040  -0.01454 251 LYS A CB  
3586 C CG  . LYS A 250 ? 2.09907 2.46225 1.35309 -0.83640 0.02308  -0.04690 251 LYS A CG  
3587 C CD  . LYS A 250 ? 2.50785 2.91608 1.73927 -0.89650 0.00646  -0.02690 251 LYS A CD  
3588 C CE  . LYS A 250 ? 2.69897 3.19877 1.96625 -0.91405 -0.00588 0.01100  251 LYS A CE  
3589 N NZ  . LYS A 250 ? 2.48348 2.97186 1.73318 -0.91360 -0.00836 -0.00547 251 LYS A NZ  
3603 N N   . THR A 251 ? 2.05756 2.39544 1.43204 -0.66980 0.05990  -0.01987 252 THR A N   
3604 C CA  . THR A 251 ? 2.03416 2.38637 1.44578 -0.62257 0.06872  0.00285  252 THR A CA  
3605 C C   . THR A 251 ? 2.10621 2.52243 1.53005 -0.64698 0.06989  0.04009  252 THR A C   
3606 O O   . THR A 251 ? 2.09527 2.49799 1.48499 -0.68808 0.06805  0.03216  252 THR A O   
3607 C CB  . THR A 251 ? 2.04463 2.30049 1.43302 -0.58122 0.07938  -0.03199 252 THR A CB  
3608 O OG1 . THR A 251 ? 2.32242 2.58555 1.74578 -0.52561 0.08610  -0.01154 252 THR A OG1 
3609 C CG2 . THR A 251 ? 2.31524 2.52963 1.65918 -0.60917 0.08490  -0.04959 252 THR A CG2 
3617 N N   . SER A 252 ? 2.22097 2.70709 1.69439 -0.62158 0.07227  0.08235  253 SER A N   
3618 C CA  . SER A 252 ? 2.19141 2.74700 1.68623 -0.63890 0.07495  0.12511  253 SER A CA  
3619 C C   . SER A 252 ? 2.23004 2.83381 1.71173 -0.70965 0.06063  0.13736  253 SER A C   
3620 O O   . SER A 252 ? 2.30237 2.99140 1.81767 -0.73135 0.05154  0.17479  253 SER A O   
3621 C CB  . SER A 252 ? 2.09870 2.60443 1.57480 -0.61704 0.08925  0.11739  253 SER A CB  
3622 O OG  . SER A 252 ? 2.20391 2.78063 1.70669 -0.62919 0.09363  0.16364  253 SER A OG  
3623 N N   . THR A 259 ? 2.24607 2.74824 1.86675 -0.23244 0.12731  0.21934  260 THR A N   
3624 C CA  . THR A 259 ? 2.33103 2.78740 1.95158 -0.22617 0.11040  0.18730  260 THR A CA  
3625 C C   . THR A 259 ? 2.34725 2.81853 1.99773 -0.17186 0.10326  0.20886  260 THR A C   
3626 O O   . THR A 259 ? 2.38591 2.81508 2.02701 -0.11119 0.10880  0.21376  260 THR A O   
3627 C CB  . THR A 259 ? 2.20186 2.54058 1.77977 -0.20875 0.10906  0.13494  260 THR A CB  
3628 O OG1 . THR A 259 ? 2.41394 2.69548 1.97446 -0.14604 0.11832  0.13498  260 THR A OG1 
3629 C CG2 . THR A 259 ? 2.23968 2.55971 1.78532 -0.26388 0.11456  0.11082  260 THR A CG2 
3636 N N   . LEU A 260 ? 2.31369 2.84234 1.99747 -0.19325 0.09011  0.22153  261 LEU A N   
3637 C CA  . LEU A 260 ? 2.33274 2.88817 2.04937 -0.14949 0.08133  0.24587  261 LEU A CA  
3638 C C   . LEU A 260 ? 2.09389 2.57442 1.80884 -0.12045 0.06339  0.21354  261 LEU A C   
3639 O O   . LEU A 260 ? 2.02299 2.52281 1.76673 -0.08917 0.05172  0.23101  261 LEU A O   
3640 C CB  . LEU A 260 ? 2.32219 2.99114 2.08101 -0.18859 0.07700  0.28367  261 LEU A CB  
3641 C CG  . LEU A 260 ? 2.49845 3.25905 2.27812 -0.19659 0.09108  0.33367  261 LEU A CG  
3642 C CD1 . LEU A 260 ? 2.36081 3.12108 2.11575 -0.23466 0.10440  0.33023  261 LEU A CD1 
3643 C CD2 . LEU A 260 ? 1.93347 2.79867 1.75615 -0.23380 0.08259  0.36735  261 LEU A CD2 
3655 N N   . VAL A 261 ? 2.02134 2.41737 1.70512 -0.12956 0.06015  0.16875  262 VAL A N   
3656 C CA  . VAL A 261 ? 1.92510 2.25742 1.61280 -0.11357 0.04210  0.13946  262 VAL A CA  
3657 C C   . VAL A 261 ? 1.97878 2.19839 1.63426 -0.06148 0.03973  0.10988  262 VAL A C   
3658 O O   . VAL A 261 ? 2.06286 2.23299 1.68104 -0.06772 0.05176  0.08764  262 VAL A O   
3659 C CB  . VAL A 261 ? 1.89871 2.23090 1.58072 -0.17176 0.03857  0.11313  262 VAL A CB  
3660 C CG1 . VAL A 261 ? 1.67059 1.91616 1.34832 -0.15140 0.02422  0.07778  262 VAL A CG1 
3661 C CG2 . VAL A 261 ? 1.89232 2.32597 1.60977 -0.21277 0.03406  0.14146  262 VAL A CG2 
3671 N N   . ASP A 262 ? 2.02328 2.20083 1.69265 -0.01067 0.02246  0.11004  263 ASP A N   
3672 C CA  . ASP A 262 ? 1.99767 2.06065 1.63945 0.03943  0.01288  0.08045  263 ASP A CA  
3673 C C   . ASP A 262 ? 1.91313 1.93040 1.57229 0.03397  -0.00871 0.05579  263 ASP A C   
3674 O O   . ASP A 262 ? 1.94261 1.99614 1.64066 0.04001  -0.02474 0.07379  263 ASP A O   
3675 C CB  . ASP A 262 ? 1.98520 2.02781 1.62522 0.10787  0.00717  0.10278  263 ASP A CB  
3676 C CG  . ASP A 262 ? 2.04279 1.96145 1.64718 0.16135  -0.00379 0.07271  263 ASP A CG  
3677 O OD1 . ASP A 262 ? 2.08866 1.93945 1.68132 0.14678  -0.01189 0.03593  263 ASP A OD1 
3678 O OD2 . ASP A 262 ? 2.02932 1.91678 1.61579 0.21928  -0.00460 0.08657  263 ASP A OD2 
3683 N N   . PHE A 263 ? 1.82777 1.76705 1.46013 0.02320  -0.00885 0.01661  264 PHE A N   
3684 C CA  . PHE A 263 ? 1.80305 1.70454 1.45382 0.01226  -0.02616 -0.00504 264 PHE A CA  
3685 C C   . PHE A 263 ? 1.91528 1.73799 1.57695 0.06949  -0.05215 -0.01093 264 PHE A C   
3686 O O   . PHE A 263 ? 1.95531 1.75495 1.64333 0.06480  -0.06971 -0.02069 264 PHE A O   
3687 C CB  . PHE A 263 ? 1.73211 1.58290 1.35070 -0.02247 -0.01578 -0.04305 264 PHE A CB  
3688 C CG  . PHE A 263 ? 1.57860 1.50401 1.19575 -0.08741 -0.00001 -0.04009 264 PHE A CG  
3689 C CD1 . PHE A 263 ? 1.71250 1.68120 1.30574 -0.11321 0.01968  -0.03094 264 PHE A CD1 
3690 C CD2 . PHE A 263 ? 1.54578 1.49765 1.18513 -0.12170 -0.00602 -0.04434 264 PHE A CD2 
3691 C CE1 . PHE A 263 ? 1.57383 1.60609 1.16303 -0.17345 0.03007  -0.02784 264 PHE A CE1 
3692 C CE2 . PHE A 263 ? 1.73339 1.74794 1.36481 -0.17936 0.00662  -0.04213 264 PHE A CE2 
3693 C CZ  . PHE A 263 ? 1.76534 1.81833 1.37071 -0.20596 0.02315  -0.03448 264 PHE A CZ  
3703 N N   . GLN A 264 ? 2.15722 1.93664 1.79874 0.12390  -0.05601 -0.00392 265 GLN A N   
3704 C CA  . GLN A 264 ? 2.11843 1.83639 1.77303 0.17956  -0.08504 -0.00077 265 GLN A CA  
3705 C C   . GLN A 264 ? 2.08379 1.87818 1.78288 0.18765  -0.09734 0.03675  265 GLN A C   
3706 O O   . GLN A 264 ? 2.16522 1.91693 1.88152 0.22905  -0.12504 0.04251  265 GLN A O   
3707 C CB  . GLN A 264 ? 2.18791 1.82701 1.79818 0.23895  -0.08590 -0.00633 265 GLN A CB  
3708 C CG  . GLN A 264 ? 2.52053 2.06761 2.08608 0.24073  -0.07857 -0.04513 265 GLN A CG  
3709 C CD  . GLN A 264 ? 2.52202 2.01015 2.10141 0.22219  -0.09571 -0.07536 265 GLN A CD  
3710 O OE1 . GLN A 264 ? 2.53813 1.96235 2.13255 0.25613  -0.12551 -0.08019 265 GLN A OE1 
3711 N NE2 . GLN A 264 ? 2.37796 1.88733 1.95264 0.16825  -0.07771 -0.09412 265 GLN A NE2 
3720 N N   . ASP A 265 ? 2.01514 1.91893 1.73284 0.14866  -0.07917 0.06251  266 ASP A N   
3721 C CA  . ASP A 265 ? 1.97657 1.96419 1.73658 0.15109  -0.08742 0.09996  266 ASP A CA  
3722 C C   . ASP A 265 ? 1.79543 1.85949 1.59034 0.08947  -0.08366 0.10352  266 ASP A C   
3723 O O   . ASP A 265 ? 1.73876 1.87939 1.53130 0.04441  -0.06247 0.11384  266 ASP A O   
3724 C CB  . ASP A 265 ? 1.96207 2.01345 1.71150 0.16490  -0.06864 0.13212  266 ASP A CB  
3725 C CG  . ASP A 265 ? 2.07828 2.22386 1.87146 0.16322  -0.07469 0.17202  266 ASP A CG  
3726 O OD1 . ASP A 265 ? 2.10058 2.25762 1.93146 0.15530  -0.09497 0.17450  266 ASP A OD1 
3727 O OD2 . ASP A 265 ? 2.08839 2.29795 1.87980 0.17042  -0.05876 0.20262  266 ASP A OD2 
3732 N N   . ARG A 266 ? 1.38032 1.90914 1.73292 -0.17322 -0.12939 -0.05600 267 ARG A N   
3733 C CA  . ARG A 266 ? 1.44841 1.97398 1.77378 -0.17978 -0.13518 -0.04056 267 ARG A CA  
3734 C C   . ARG A 266 ? 1.56898 2.14605 1.91321 -0.17752 -0.14722 -0.02074 267 ARG A C   
3735 O O   . ARG A 266 ? 1.59883 2.18964 1.91538 -0.18971 -0.15412 -0.01062 267 ARG A O   
3736 C CB  . ARG A 266 ? 1.31164 1.79998 1.64079 -0.16413 -0.12900 -0.03295 267 ARG A CB  
3737 C CG  . ARG A 266 ? 1.39017 1.89158 1.77161 -0.13889 -0.12875 -0.01724 267 ARG A CG  
3738 C CD  . ARG A 266 ? 1.41616 1.87929 1.79865 -0.12615 -0.12162 -0.01023 267 ARG A CD  
3739 N NE  . ARG A 266 ? 1.24587 1.70818 1.59715 -0.13336 -0.12784 0.00679  267 ARG A NE  
3740 C CZ  . ARG A 266 ? 1.26529 1.75804 1.63359 -0.12504 -0.13528 0.03224  267 ARG A CZ  
3741 N NH1 . ARG A 266 ? 1.48930 2.01340 1.90633 -0.10838 -0.13707 0.04512  267 ARG A NH1 
3742 N NH2 . ARG A 266 ? 1.56025 2.05428 1.89670 -0.13311 -0.14049 0.04566  267 ARG A NH2 
3756 N N   . ASN A 267 ? 1.49689 2.10576 1.88826 -0.16194 -0.14941 -0.01515 268 ASN A N   
3757 C CA  . ASN A 267 ? 1.48008 2.14234 1.89163 -0.15769 -0.16043 0.00558  268 ASN A CA  
3758 C C   . ASN A 267 ? 1.54621 2.24510 1.92841 -0.18306 -0.16892 -0.00124 268 ASN A C   
3759 O O   . ASN A 267 ? 1.53644 2.26952 1.90380 -0.19144 -0.17807 0.01295  268 ASN A O   
3760 C CB  . ASN A 267 ? 1.55910 2.24478 2.02982 -0.13463 -0.15896 0.01138  268 ASN A CB  
3761 C CG  . ASN A 267 ? 1.65541 2.30419 2.15898 -0.11133 -0.14808 0.01414  268 ASN A CG  
3762 O OD1 . ASN A 267 ? 1.73914 2.37738 2.24849 -0.09972 -0.14741 0.03394  268 ASN A OD1 
3763 N ND2 . ASN A 267 ? 1.59746 2.22904 2.12364 -0.10501 -0.13885 -0.00627 268 ASN A ND2 
3770 N N   . SER A 268 ? 1.44943 2.14438 1.82346 -0.19617 -0.16535 -0.02324 269 SER A N   
3771 C CA  . SER A 268 ? 1.54062 2.26703 1.88742 -0.22231 -0.17128 -0.03212 269 SER A CA  
3772 C C   . SER A 268 ? 1.51608 2.22367 1.81101 -0.24518 -0.17108 -0.03600 269 SER A C   
3773 O O   . SER A 268 ? 1.39908 2.14312 1.67374 -0.26536 -0.17807 -0.03630 269 SER A O   
3774 C CB  . SER A 268 ? 1.43707 2.15624 1.78460 -0.23150 -0.16511 -0.05435 269 SER A CB  
3775 O OG  . SER A 268 ? 1.37933 2.04420 1.69669 -0.23942 -0.15405 -0.06957 269 SER A OG  
3781 N N   . VAL A 269 ? 1.47858 2.13176 1.75234 -0.24293 -0.16255 -0.04040 270 VAL A N   
3782 C CA  . VAL A 269 ? 1.35671 1.98884 1.58244 -0.26378 -0.16090 -0.04540 270 VAL A CA  
3783 C C   . VAL A 269 ? 1.58954 2.25135 1.81222 -0.26099 -0.17032 -0.02469 270 VAL A C   
3784 O O   . VAL A 269 ? 1.71317 2.39741 1.90530 -0.28288 -0.17481 -0.02714 270 VAL A O   
3785 C CB  . VAL A 269 ? 1.16031 1.72720 1.36579 -0.26038 -0.14856 -0.05562 270 VAL A CB  
3786 C CG1 . VAL A 269 ? 1.27994 1.82334 1.43652 -0.28232 -0.14539 -0.06265 270 VAL A CG1 
3787 C CG2 . VAL A 269 ? 1.29690 1.84210 1.50812 -0.26082 -0.13920 -0.07334 270 VAL A CG2 
3797 N N   . VAL A 270 ? 1.46824 2.13294 1.72370 -0.23446 -0.17251 -0.00413 271 VAL A N   
3798 C CA  . VAL A 270 ? 1.55636 2.25120 1.81156 -0.22895 -0.18074 0.01955  271 VAL A CA  
3799 C C   . VAL A 270 ? 1.44069 2.20724 1.70241 -0.23818 -0.19261 0.02862  271 VAL A C   
3800 O O   . VAL A 270 ? 1.33629 2.13412 1.57106 -0.25417 -0.19907 0.03330  271 VAL A O   
3801 C CB  . VAL A 270 ? 1.51813 2.20081 1.81335 -0.19716 -0.17855 0.04115  271 VAL A CB  
3802 C CG1 . VAL A 270 ? 1.61200 2.33909 1.91623 -0.18827 -0.18770 0.07101  271 VAL A CG1 
3803 C CG2 . VAL A 270 ? 1.41657 2.03380 1.69743 -0.19166 -0.16766 0.03286  271 VAL A CG2 
3813 N N   . ASP A 271 ? 1.45904 2.25627 1.75703 -0.22854 -0.19543 0.03026  272 ASP A N   
3814 C CA  . ASP A 271 ? 1.56073 2.42937 1.86574 -0.23738 -0.20647 0.03751  272 ASP A CA  
3815 C C   . ASP A 271 ? 1.54679 2.42892 1.80583 -0.27330 -0.20804 0.01658  272 ASP A C   
3816 O O   . ASP A 271 ? 1.79026 2.72825 2.03704 -0.28631 -0.21704 0.02378  272 ASP A O   
3817 C CB  . ASP A 271 ? 1.77923 2.67045 2.12580 -0.22512 -0.20717 0.03548  272 ASP A CB  
3818 C CG  . ASP A 271 ? 1.92283 2.81458 2.32138 -0.18994 -0.20582 0.05806  272 ASP A CG  
3819 O OD1 . ASP A 271 ? 1.87125 2.74662 2.27378 -0.17516 -0.20438 0.07700  272 ASP A OD1 
3820 O OD2 . ASP A 271 ? 2.10448 3.01286 2.54120 -0.17737 -0.20520 0.05645  272 ASP A OD2 
3825 N N   . PHE A 272 ? 1.41196 2.24503 1.64627 -0.28983 -0.19822 -0.00953 273 PHE A N   
3826 C CA  . PHE A 272 ? 1.57875 2.41689 1.77160 -0.32471 -0.19634 -0.03119 273 PHE A CA  
3827 C C   . PHE A 272 ? 1.66304 2.49524 1.81951 -0.33802 -0.19669 -0.02968 273 PHE A C   
3828 O O   . PHE A 272 ? 1.64336 2.52082 1.77892 -0.36090 -0.20210 -0.03440 273 PHE A O   
3829 C CB  . PHE A 272 ? 1.39903 2.18164 1.57718 -0.33574 -0.18353 -0.05582 273 PHE A CB  
3830 C CG  . PHE A 272 ? 1.41689 2.18724 1.55151 -0.37040 -0.17703 -0.07823 273 PHE A CG  
3831 C CD1 . PHE A 272 ? 1.46982 2.28230 1.59898 -0.39464 -0.17934 -0.09111 273 PHE A CD1 
3832 C CD2 . PHE A 272 ? 1.40795 2.12431 1.50857 -0.37905 -0.16740 -0.08717 273 PHE A CD2 
3833 C CE1 . PHE A 272 ? 1.59346 2.39241 1.68528 -0.42776 -0.17100 -0.11326 273 PHE A CE1 
3834 C CE2 . PHE A 272 ? 1.48604 2.18833 1.54946 -0.41081 -0.15916 -0.10858 273 PHE A CE2 
3835 C CZ  . PHE A 272 ? 1.53126 2.27385 1.59092 -0.43563 -0.16038 -0.12203 273 PHE A CZ  
3845 N N   . LEU A 273 ? 1.46145 2.24118 1.61037 -0.32461 -0.19068 -0.02434 274 LEU A N   
3846 C CA  . LEU A 273 ? 1.57879 2.34857 1.69176 -0.33754 -0.18988 -0.02497 274 LEU A CA  
3847 C C   . LEU A 273 ? 1.78117 2.61551 1.90226 -0.33168 -0.20254 -0.00076 274 LEU A C   
3848 O O   . LEU A 273 ? 1.88504 2.74649 1.97581 -0.35297 -0.20544 -0.00580 274 LEU A O   
3849 C CB  . LEU A 273 ? 1.21987 1.92034 1.32528 -0.32270 -0.18056 -0.02395 274 LEU A CB  
3850 C CG  . LEU A 273 ? 1.30921 1.94613 1.39496 -0.33253 -0.16661 -0.04844 274 LEU A CG  
3851 C CD1 . LEU A 273 ? 1.35370 1.93075 1.43560 -0.31482 -0.15852 -0.04483 274 LEU A CD1 
3852 C CD2 . LEU A 273 ? 1.34663 1.97926 1.39061 -0.36703 -0.16105 -0.07123 274 LEU A CD2 
3864 N N   . LEU A 274 ? 1.61039 2.47214 1.77330 -0.30284 -0.20923 0.02581  275 LEU A N   
3865 C CA  . LEU A 274 ? 1.44228 2.36755 1.61567 -0.29387 -0.22040 0.05353  275 LEU A CA  
3866 C C   . LEU A 274 ? 1.61472 2.61754 1.78037 -0.31550 -0.22984 0.04918  275 LEU A C   
3867 O O   . LEU A 274 ? 1.68716 2.74529 1.84147 -0.32160 -0.23788 0.06236  275 LEU A O   
3868 C CB  . LEU A 274 ? 1.36350 2.29701 1.58764 -0.25679 -0.22285 0.08372  275 LEU A CB  
3869 C CG  . LEU A 274 ? 1.28184 2.15093 1.51589 -0.23445 -0.21427 0.09294  275 LEU A CG  
3870 C CD1 . LEU A 274 ? 1.32505 2.20192 1.61434 -0.19975 -0.21419 0.11921  275 LEU A CD1 
3871 C CD2 . LEU A 274 ? 1.30028 2.16697 1.50543 -0.23883 -0.21548 0.10360  275 LEU A CD2 
3883 N N   . LYS A 275 ? 1.53009 2.54177 1.70149 -0.32791 -0.22881 0.03057  276 LYS A N   
3884 C CA  . LYS A 275 ? 1.74045 2.82450 1.90177 -0.35230 -0.23649 0.02203  276 LYS A CA  
3885 C C   . LYS A 275 ? 1.75326 2.83419 1.86573 -0.38875 -0.23237 -0.00335 276 LYS A C   
3886 O O   . LYS A 275 ? 1.76002 2.90815 1.85866 -0.40518 -0.24004 -0.00163 276 LYS A O   
3887 C CB  . LYS A 275 ? 1.73022 2.82040 1.90967 -0.35732 -0.23515 0.00721  276 LYS A CB  
3888 C CG  . LYS A 275 ? 1.56796 2.69271 1.79798 -0.32619 -0.24204 0.03187  276 LYS A CG  
3889 C CD  . LYS A 275 ? 1.45366 2.58451 1.69937 -0.33298 -0.24038 0.01471  276 LYS A CD  
3890 C CE  . LYS A 275 ? 1.47099 2.62760 1.76938 -0.30023 -0.24514 0.03700  276 LYS A CE  
3891 N NZ  . LYS A 275 ? 1.73459 2.87682 2.04943 -0.30271 -0.24067 0.01843  276 LYS A NZ  
3905 N N   . LYS A 276 ? 1.61925 2.62502 1.70630 -0.40166 -0.21940 -0.02740 277 LYS A N   
3906 C CA  . LYS A 276 ? 1.63084 2.62515 1.67350 -0.43508 -0.21273 -0.05236 277 LYS A CA  
3907 C C   . LYS A 276 ? 1.82839 2.83496 1.85455 -0.43122 -0.21667 -0.03828 277 LYS A C   
3908 O O   . LYS A 276 ? 2.00673 3.05130 2.00500 -0.45751 -0.21796 -0.05074 277 LYS A O   
3909 C CB  . LYS A 276 ? 1.54335 2.45091 1.56630 -0.44487 -0.19654 -0.07701 277 LYS A CB  
3910 C CG  . LYS A 276 ? 1.90726 2.81181 1.92558 -0.46888 -0.18940 -0.10261 277 LYS A CG  
3911 C CD  . LYS A 276 ? 1.64261 2.46226 1.63979 -0.47757 -0.17194 -0.12360 277 LYS A CD  
3912 C CE  . LYS A 276 ? 1.84523 2.66257 1.83210 -0.50699 -0.16243 -0.15004 277 LYS A CE  
3913 N NZ  . LYS A 276 ? 2.56975 3.42558 2.52933 -0.54367 -0.16065 -0.17023 277 LYS A NZ  
3927 N N   . PHE A 277 ? 1.72836 2.70509 1.77210 -0.39958 -0.21791 -0.01333 278 PHE A N   
3928 C CA  . PHE A 277 ? 1.77284 2.75473 1.80251 -0.39317 -0.22067 0.00223  278 PHE A CA  
3929 C C   . PHE A 277 ? 1.72756 2.78697 1.78322 -0.37347 -0.23459 0.03765  278 PHE A C   
3930 O O   . PHE A 277 ? 1.66422 2.72439 1.72072 -0.35723 -0.23706 0.06023  278 PHE A O   
3931 C CB  . PHE A 277 ? 1.73783 2.63739 1.76884 -0.37207 -0.21177 0.00745  278 PHE A CB  
3932 C CG  . PHE A 277 ? 1.69305 2.52478 1.68681 -0.39310 -0.19818 -0.02300 278 PHE A CG  
3933 C CD1 . PHE A 277 ? 1.69136 2.49634 1.67502 -0.41297 -0.18939 -0.05077 278 PHE A CD1 
3934 C CD2 . PHE A 277 ? 1.64135 2.43641 1.61129 -0.39217 -0.19336 -0.02256 278 PHE A CD2 
3935 C CE1 . PHE A 277 ? 1.69247 2.43450 1.64401 -0.43052 -0.17522 -0.07617 278 PHE A CE1 
3936 C CE2 . PHE A 277 ? 1.57354 2.30649 1.51070 -0.40989 -0.17992 -0.04944 278 PHE A CE2 
3937 C CZ  . PHE A 277 ? 1.60020 2.30608 1.52873 -0.42853 -0.17042 -0.07556 278 PHE A CZ  
3947 N N   . SER A 278 ? 1.72035 2.84675 1.79763 -0.37413 -0.24320 0.04421  279 SER A N   
3948 C CA  . SER A 278 ? 1.84810 3.05341 1.95143 -0.35416 -0.25578 0.08023  279 SER A CA  
3949 C C   . SER A 278 ? 1.89872 3.15582 1.97355 -0.36850 -0.26117 0.08586  279 SER A C   
3950 O O   . SER A 278 ? 1.83920 3.13251 1.92938 -0.34598 -0.26779 0.12056  279 SER A O   
3951 C CB  . SER A 278 ? 1.79526 3.06918 1.92117 -0.35739 -0.26367 0.08167  279 SER A CB  
3952 O OG  . SER A 278 ? 1.83364 3.15349 1.92828 -0.39568 -0.26519 0.05357  279 SER A OG  
3958 N N   . ASP A 279 ? 1.86746 3.12949 1.90185 -0.40610 -0.25733 0.05190  280 ASP A N   
3959 C CA  . ASP A 279 ? 1.93746 3.25268 1.94294 -0.42388 -0.26158 0.05142  280 ASP A CA  
3960 C C   . ASP A 279 ? 1.91667 3.17699 1.90492 -0.41461 -0.25609 0.05826  280 ASP A C   
3961 O O   . ASP A 279 ? 1.94738 3.25450 1.91632 -0.42298 -0.26054 0.06477  280 ASP A O   
3962 C CB  . ASP A 279 ? 1.92268 3.25712 1.89246 -0.46914 -0.25672 0.00846  280 ASP A CB  
3963 C CG  . ASP A 279 ? 1.90955 3.33318 1.89085 -0.48327 -0.26533 0.00479  280 ASP A CG  
3964 O OD1 . ASP A 279 ? 1.87212 3.34138 1.88924 -0.45651 -0.27530 0.03633  280 ASP A OD1 
3965 O OD2 . ASP A 279 ? 1.85871 3.30734 1.81426 -0.52141 -0.26119 -0.03020 280 ASP A OD2 
3970 N N   . TRP A 280 ? 1.89449 3.06203 1.88917 -0.39805 -0.24665 0.05662  281 TRP A N   
3971 C CA  . TRP A 280 ? 1.81458 2.92346 1.78913 -0.39312 -0.23975 0.05695  281 TRP A CA  
3972 C C   . TRP A 280 ? 1.70392 2.82506 1.70515 -0.35751 -0.24562 0.10036  281 TRP A C   
3973 O O   . TRP A 280 ? 1.61643 2.76578 1.65748 -0.33134 -0.25157 0.12936  281 TRP A O   
3974 C CB  . TRP A 280 ? 1.71518 2.72187 1.68301 -0.39280 -0.22597 0.03402  281 TRP A CB  
3975 C CG  . TRP A 280 ? 1.64090 2.62544 1.57835 -0.42849 -0.21689 -0.00783 281 TRP A CG  
3976 C CD1 . TRP A 280 ? 1.68926 2.71215 1.62882 -0.44902 -0.21838 -0.02534 281 TRP A CD1 
3977 C CD2 . TRP A 280 ? 1.53967 2.45751 1.44195 -0.44747 -0.20342 -0.03668 281 TRP A CD2 
3978 N NE1 . TRP A 280 ? 1.71015 2.69258 1.61890 -0.48016 -0.20582 -0.06309 281 TRP A NE1 
3979 C CE2 . TRP A 280 ? 1.58779 2.50506 1.47371 -0.47910 -0.19622 -0.07020 281 TRP A CE2 
3980 C CE3 . TRP A 280 ? 1.57702 2.43591 1.46103 -0.44048 -0.19598 -0.03703 281 TRP A CE3 
3981 C CZ2 . TRP A 280 ? 1.61763 2.47555 1.47131 -0.50274 -0.18086 -0.10256 281 TRP A CZ2 
3982 C CZ3 . TRP A 280 ? 1.57213 2.37459 1.42297 -0.46354 -0.18184 -0.06955 281 TRP A CZ3 
3983 C CH2 . TRP A 280 ? 1.57786 2.37919 1.41460 -0.49383 -0.17392 -0.10130 281 TRP A CH2 
3994 N N   . ASP A 281 ? 1.65252 2.75146 1.63220 -0.35692 -0.24274 0.10456  282 ASP A N   
3995 C CA  . ASP A 281 ? 1.61451 2.72439 1.61590 -0.32597 -0.24676 0.14538  282 ASP A CA  
3996 C C   . ASP A 281 ? 1.56706 2.61247 1.60658 -0.29343 -0.24092 0.16157  282 ASP A C   
3997 O O   . ASP A 281 ? 1.62854 2.60599 1.66759 -0.29615 -0.23214 0.13771  282 ASP A O   
3998 C CB  . ASP A 281 ? 1.71913 2.80841 1.68667 -0.33462 -0.24313 0.14116  282 ASP A CB  
3999 C CG  . ASP A 281 ? 1.78599 2.88543 1.77454 -0.30396 -0.24617 0.18378  282 ASP A CG  
4000 O OD1 . ASP A 281 ? 1.88322 2.92117 1.89782 -0.27771 -0.23991 0.19795  282 ASP A OD1 
4001 O OD2 . ASP A 281 ? 1.61740 2.78878 1.59742 -0.30653 -0.25411 0.20307  282 ASP A OD2 
4006 N N   . GLU A 282 ? 1.59463 2.66492 1.66907 -0.26225 -0.24495 0.20314  283 GLU A N   
4007 C CA  . GLU A 282 ? 1.58481 2.60155 1.70119 -0.23083 -0.23848 0.21951  283 GLU A CA  
4008 C C   . GLU A 282 ? 1.53621 2.45845 1.63868 -0.22918 -0.22640 0.20121  283 GLU A C   
4009 O O   . GLU A 282 ? 1.45323 2.32004 1.58008 -0.21486 -0.21877 0.19508  283 GLU A O   
4010 C CB  . GLU A 282 ? 1.62814 2.68626 1.78269 -0.19898 -0.24248 0.26836  283 GLU A CB  
4011 C CG  . GLU A 282 ? 1.81840 2.82849 2.02302 -0.16612 -0.23452 0.28625  283 GLU A CG  
4012 C CD  . GLU A 282 ? 1.94018 2.96637 2.17665 -0.16048 -0.23621 0.28114  283 GLU A CD  
4013 O OE1 . GLU A 282 ? 1.73427 2.82320 1.95963 -0.17748 -0.24535 0.27380  283 GLU A OE1 
4014 O OE2 . GLU A 282 ? 1.94107 2.91923 2.21416 -0.13981 -0.22799 0.28309  283 GLU A OE2 
4021 N N   . ARG A 283 ? 1.52030 2.42642 1.58465 -0.24330 -0.22427 0.19207  284 ARG A N   
4022 C CA  . ARG A 283 ? 1.68885 2.50872 1.73759 -0.24235 -0.21276 0.17413  284 ARG A CA  
4023 C C   . ARG A 283 ? 1.68482 2.45243 1.72250 -0.25691 -0.20528 0.13698  284 ARG A C   
4024 O O   . ARG A 283 ? 1.47431 2.17464 1.52182 -0.24498 -0.19570 0.12861  284 ARG A O   
4025 C CB  . ARG A 283 ? 1.77655 2.59534 1.78252 -0.25902 -0.21220 0.16684  284 ARG A CB  
4026 C CG  . ARG A 283 ? 1.62651 2.46863 1.64453 -0.23888 -0.21517 0.20416  284 ARG A CG  
4027 C CD  . ARG A 283 ? 1.55500 2.41383 1.52927 -0.25871 -0.21667 0.19609  284 ARG A CD  
4028 N NE  . ARG A 283 ? 1.65238 2.59622 1.60882 -0.28020 -0.22687 0.19355  284 ARG A NE  
4029 C CZ  . ARG A 283 ? 1.81946 2.79715 1.73883 -0.30152 -0.22948 0.18389  284 ARG A CZ  
4030 N NH1 . ARG A 283 ? 1.91113 2.84373 1.80577 -0.30424 -0.22300 0.17631  284 ARG A NH1 
4031 N NH2 . ARG A 283 ? 1.68372 2.74553 1.59101 -0.32108 -0.23852 0.18054  284 ARG A NH2 
4045 N N   . TYR A 284 ? 1.64756 2.44762 1.66531 -0.28306 -0.20878 0.11447  285 TYR A N   
4046 C CA  . TYR A 284 ? 1.52279 2.27979 1.53443 -0.29581 -0.20146 0.08304  285 TYR A CA  
4047 C C   . TYR A 284 ? 1.45873 2.21366 1.51557 -0.27425 -0.20198 0.09362  285 TYR A C   
4048 O O   . TYR A 284 ? 1.50666 2.20372 1.57198 -0.26781 -0.19309 0.07921  285 TYR A O   
4049 C CB  . TYR A 284 ? 1.59217 2.38758 1.57427 -0.32999 -0.20398 0.05730  285 TYR A CB  
4050 C CG  . TYR A 284 ? 1.62634 2.42010 1.56352 -0.35487 -0.20100 0.03974  285 TYR A CG  
4051 C CD1 . TYR A 284 ? 1.63901 2.36125 1.54722 -0.36676 -0.18828 0.01303  285 TYR A CD1 
4052 C CD2 . TYR A 284 ? 1.70539 2.57239 1.62995 -0.36634 -0.21030 0.04955  285 TYR A CD2 
4053 C CE1 . TYR A 284 ? 1.65750 2.37711 1.52642 -0.38937 -0.18428 -0.00443 285 TYR A CE1 
4054 C CE2 . TYR A 284 ? 1.70041 2.56872 1.58497 -0.39018 -0.20691 0.03089  285 TYR A CE2 
4055 C CZ  . TYR A 284 ? 1.64850 2.44099 1.50585 -0.40171 -0.19359 0.00333  285 TYR A CZ  
4056 O OH  . TYR A 284 ? 1.60445 2.39693 1.42373 -0.42520 -0.18898 -0.01648 285 TYR A OH  
4066 N N   . LYS A 285 ? 1.48373 2.30487 1.57072 -0.26264 -0.21197 0.11871  286 LYS A N   
4067 C CA  . LYS A 285 ? 1.46832 2.29001 1.60206 -0.24008 -0.21195 0.13040  286 LYS A CA  
4068 C C   . LYS A 285 ? 1.53325 2.29378 1.69351 -0.21286 -0.20283 0.14098  286 LYS A C   
4069 O O   . LYS A 285 ? 1.42841 2.15354 1.61283 -0.20262 -0.19652 0.13092  286 LYS A O   
4070 C CB  . LYS A 285 ? 1.51581 2.41942 1.67912 -0.22787 -0.22329 0.16143  286 LYS A CB  
4071 C CG  . LYS A 285 ? 1.51342 2.48449 1.65700 -0.25431 -0.23220 0.14879  286 LYS A CG  
4072 C CD  . LYS A 285 ? 1.48083 2.53924 1.65324 -0.24038 -0.24361 0.18221  286 LYS A CD  
4073 C CE  . LYS A 285 ? 1.63984 2.77184 1.78796 -0.26963 -0.25247 0.16791  286 LYS A CE  
4074 N NZ  . LYS A 285 ? 1.71606 2.94025 1.89235 -0.25560 -0.26384 0.20080  286 LYS A NZ  
4088 N N   . GLU A 286 ? 1.69542 2.44488 1.85163 -0.20194 -0.20145 0.15997  287 GLU A N   
4089 C CA  . GLU A 286 ? 1.59201 2.28198 1.77100 -0.17891 -0.19140 0.16721  287 GLU A CA  
4090 C C   . GLU A 286 ? 1.53161 2.15149 1.68976 -0.18886 -0.18092 0.13324  287 GLU A C   
4091 O O   . GLU A 286 ? 1.60838 2.18708 1.79434 -0.17250 -0.17258 0.12905  287 GLU A O   
4092 C CB  . GLU A 286 ? 1.73533 2.42589 1.90603 -0.17033 -0.19141 0.19063  287 GLU A CB  
4093 C CG  . GLU A 286 ? 1.82186 2.45153 2.01433 -0.14865 -0.18006 0.19724  287 GLU A CG  
4094 C CD  . GLU A 286 ? 1.91062 2.54736 2.09967 -0.13874 -0.18024 0.22471  287 GLU A CD  
4095 O OE1 . GLU A 286 ? 1.64138 2.31738 1.79718 -0.15417 -0.18806 0.22941  287 GLU A OE1 
4096 O OE2 . GLU A 286 ? 1.95771 2.56265 2.17824 -0.11621 -0.17191 0.24097  287 GLU A OE2 
4103 N N   . LEU A 287 ? 1.55308 2.16060 1.66353 -0.21546 -0.18019 0.10866  288 LEU A N   
4104 C CA  . LEU A 287 ? 1.45764 2.00117 1.54686 -0.22446 -0.16938 0.07868  288 LEU A CA  
4105 C C   . LEU A 287 ? 1.43986 1.97515 1.55189 -0.22228 -0.16638 0.06419  288 LEU A C   
4106 O O   . LEU A 287 ? 1.36294 1.85019 1.48635 -0.21187 -0.15695 0.05321  288 LEU A O   
4107 C CB  . LEU A 287 ? 1.34251 1.88063 1.37974 -0.25432 -0.16834 0.05598  288 LEU A CB  
4108 C CG  . LEU A 287 ? 1.18439 1.65852 1.19509 -0.26516 -0.15606 0.02651  288 LEU A CG  
4109 C CD1 . LEU A 287 ? 1.18931 1.61000 1.19842 -0.24901 -0.14772 0.02989  288 LEU A CD1 
4110 C CD2 . LEU A 287 ? 1.21687 1.69475 1.18222 -0.29630 -0.15448 0.00455  288 LEU A CD2 
4122 N N   . ILE A 288 ? 1.45241 2.03808 1.57154 -0.23230 -0.17423 0.06359  289 ILE A N   
4123 C CA  . ILE A 288 ? 1.23964 1.82226 1.37891 -0.23208 -0.17185 0.04934  289 ILE A CA  
4124 C C   . ILE A 288 ? 1.29495 1.87188 1.48601 -0.20238 -0.16957 0.06456  289 ILE A C   
4125 O O   . ILE A 288 ? 1.43079 1.97487 1.63703 -0.19600 -0.16183 0.04960  289 ILE A O   
4126 C CB  . ILE A 288 ? 1.21947 1.86249 1.35486 -0.25022 -0.18114 0.04608  289 ILE A CB  
4127 C CG1 . ILE A 288 ? 1.16615 1.80595 1.25169 -0.28289 -0.17948 0.02298  289 ILE A CG1 
4128 C CG2 . ILE A 288 ? 1.23813 1.88628 1.40193 -0.24596 -0.17995 0.03662  289 ILE A CG2 
4129 C CD1 . ILE A 288 ? 1.62312 2.33079 1.70098 -0.30351 -0.18900 0.02093  289 ILE A CD1 
4141 N N   . ARG A 289 ? 1.35727 1.96748 1.57763 -0.18374 -0.17512 0.09443  290 ARG A N   
4142 C CA  . ARG A 289 ? 1.38845 1.99779 1.66314 -0.15606 -0.17174 0.10916  290 ARG A CA  
4143 C C   . ARG A 289 ? 1.29515 1.84151 1.58104 -0.14220 -0.15900 0.10048  290 ARG A C   
4144 O O   . ARG A 289 ? 1.32076 1.85512 1.64742 -0.12534 -0.15274 0.09817  290 ARG A O   
4145 C CB  . ARG A 289 ? 1.59865 2.25380 1.90179 -0.13814 -0.17823 0.14607  290 ARG A CB  
4146 C CG  . ARG A 289 ? 1.60551 2.33404 1.90650 -0.14761 -0.19101 0.15767  290 ARG A CG  
4147 C CD  . ARG A 289 ? 1.62697 2.40266 1.96185 -0.12521 -0.19603 0.19812  290 ARG A CD  
4148 N NE  . ARG A 289 ? 1.74147 2.59446 2.07121 -0.13460 -0.20869 0.21018  290 ARG A NE  
4149 C CZ  . ARG A 289 ? 1.78092 2.67853 2.08178 -0.14628 -0.21700 0.22301  290 ARG A CZ  
4150 N NH1 . ARG A 289 ? 1.72137 2.59380 1.99546 -0.14972 -0.21443 0.22686  290 ARG A NH1 
4151 N NH2 . ARG A 289 ? 1.53367 2.50681 1.83278 -0.15504 -0.22809 0.23149  290 ARG A NH2 
4165 N N   . VAL A 290 ? 1.39652 1.90484 1.64766 -0.14940 -0.15454 0.09428  291 VAL A N   
4166 C CA  . VAL A 290 ? 1.53833 1.99202 1.79966 -0.13585 -0.14262 0.08799  291 VAL A CA  
4167 C C   . VAL A 290 ? 1.64498 2.05643 1.88491 -0.14643 -0.13430 0.05616  291 VAL A C   
4168 O O   . VAL A 290 ? 1.43295 1.80429 1.68463 -0.13504 -0.12391 0.04772  291 VAL A O   
4169 C CB  . VAL A 290 ? 1.59821 2.03382 1.83698 -0.13465 -0.14140 0.10107  291 VAL A CB  
4170 C CG1 . VAL A 290 ? 1.73872 2.21470 2.00406 -0.12000 -0.14753 0.13637  291 VAL A CG1 
4171 C CG2 . VAL A 290 ? 1.62140 2.05357 1.80240 -0.16046 -0.14507 0.08695  291 VAL A CG2 
4181 N N   . THR A 291 ? 1.65285 2.07357 1.86252 -0.16783 -0.13756 0.03871  292 THR A N   
4182 C CA  . THR A 291 ? 1.37058 1.75217 1.55800 -0.17760 -0.12865 0.01170  292 THR A CA  
4183 C C   . THR A 291 ? 1.47198 1.84673 1.69876 -0.16293 -0.12227 0.00235  292 THR A C   
4184 O O   . THR A 291 ? 1.44782 1.85760 1.70859 -0.15653 -0.12701 0.00803  292 THR A O   
4185 C CB  . THR A 291 ? 1.45885 1.85417 1.61033 -0.20377 -0.13215 -0.00304 292 THR A CB  
4186 O OG1 . THR A 291 ? 1.62148 2.01881 1.73420 -0.21914 -0.13564 0.00041  292 THR A OG1 
4187 C CG2 . THR A 291 ? 1.67285 2.03034 1.80667 -0.21159 -0.12163 -0.02764 292 THR A CG2 
4195 N N   . SER A 292 ? 1.48051 1.81329 1.70290 -0.15765 -0.11122 -0.01268 293 SER A N   
4196 C CA  . SER A 292 ? 1.46449 1.79255 1.72307 -0.14452 -0.10389 -0.02456 293 SER A CA  
4197 C C   . SER A 292 ? 1.50574 1.84340 1.75391 -0.15764 -0.10332 -0.04278 293 SER A C   
4198 O O   . SER A 292 ? 1.48000 1.84848 1.75933 -0.15384 -0.10648 -0.04389 293 SER A O   
4199 C CB  . SER A 292 ? 1.49123 1.77738 1.74911 -0.13426 -0.09199 -0.03423 293 SER A CB  
4200 O OG  . SER A 292 ? 1.75202 2.03882 2.04530 -0.12276 -0.08429 -0.04820 293 SER A OG  
4206 N N   . SER A 293 ? 1.56260 1.87390 1.76809 -0.17271 -0.09836 -0.05645 294 SER A N   
4207 C CA  . SER A 293 ? 1.53742 1.85035 1.73143 -0.18433 -0.09453 -0.07334 294 SER A CA  
4208 C C   . SER A 293 ? 1.35960 1.67232 1.51012 -0.20870 -0.09746 -0.07611 294 SER A C   
4209 O O   . SER A 293 ? 1.23212 1.51819 1.34789 -0.21662 -0.09482 -0.07572 294 SER A O   
4210 C CB  . SER A 293 ? 1.51477 1.79392 1.70231 -0.17774 -0.08166 -0.08836 294 SER A CB  
4211 O OG  . SER A 293 ? 1.88858 2.17189 2.06680 -0.18757 -0.07716 -0.10188 294 SER A OG  
4217 N N   . PHE A 294 ? 1.34198 1.68481 1.49556 -0.22122 -0.10198 -0.08038 295 PHE A N   
4218 C CA  . PHE A 294 ? 1.37125 1.71691 1.48777 -0.24675 -0.10299 -0.08649 295 PHE A CA  
4219 C C   . PHE A 294 ? 1.28117 1.60368 1.38014 -0.25664 -0.09160 -0.10315 295 PHE A C   
4220 O O   . PHE A 294 ? 1.42148 1.74993 1.54440 -0.24672 -0.08785 -0.10877 295 PHE A O   
4221 C CB  . PHE A 294 ? 1.58958 1.98748 1.71994 -0.25628 -0.11489 -0.08019 295 PHE A CB  
4222 C CG  . PHE A 294 ? 1.44741 1.87384 1.59230 -0.24763 -0.12586 -0.06059 295 PHE A CG  
4223 C CD1 . PHE A 294 ? 1.33138 1.75793 1.44551 -0.25994 -0.12939 -0.05508 295 PHE A CD1 
4224 C CD2 . PHE A 294 ? 1.47765 1.93275 1.66825 -0.22695 -0.13171 -0.04716 295 PHE A CD2 
4225 C CE1 . PHE A 294 ? 1.38416 1.84169 1.51167 -0.25123 -0.13924 -0.03459 295 PHE A CE1 
4226 C CE2 . PHE A 294 ? 1.33447 1.81661 1.54004 -0.21739 -0.14048 -0.02573 295 PHE A CE2 
4227 C CZ  . PHE A 294 ? 1.32184 1.80679 1.49527 -0.22932 -0.14463 -0.01845 295 PHE A CZ  
4237 N N   . VAL A 295 ? 1.19103 1.48843 1.24936 -0.27603 -0.08515 -0.11073 296 VAL A N   
4238 C CA  . VAL A 295 ? 1.08174 1.35352 1.12044 -0.28641 -0.07218 -0.12381 296 VAL A CA  
4239 C C   . VAL A 295 ? 1.06317 1.34589 1.07834 -0.31465 -0.07205 -0.13097 296 VAL A C   
4240 O O   . VAL A 295 ? 1.21718 1.48858 1.20421 -0.32914 -0.07167 -0.13250 296 VAL A O   
4241 C CB  . VAL A 295 ? 1.07607 1.29706 1.08872 -0.28089 -0.05947 -0.12719 296 VAL A CB  
4242 C CG1 . VAL A 295 ? 1.20161 1.39802 1.19462 -0.29119 -0.04483 -0.13745 296 VAL A CG1 
4243 C CG2 . VAL A 295 ? 1.30354 1.51734 1.34041 -0.25455 -0.05889 -0.12242 296 VAL A CG2 
4253 N N   . GLY A 296 ? 1.04977 1.35594 1.07689 -0.32345 -0.07164 -0.13674 297 GLY A N   
4254 C CA  . GLY A 296 ? 1.12968 1.44860 1.13795 -0.35171 -0.07004 -0.14565 297 GLY A CA  
4255 C C   . GLY A 296 ? 1.25051 1.52945 1.23454 -0.36425 -0.05198 -0.15657 297 GLY A C   
4256 O O   . GLY A 296 ? 1.46486 1.72720 1.45772 -0.35092 -0.04350 -0.15644 297 GLY A O   
4260 N N   . LEU A 297 ? 1.21863 1.48448 1.17336 -0.39008 -0.04521 -0.16598 298 LEU A N   
4261 C CA  . LEU A 297 ? 1.27502 1.49915 1.20668 -0.40360 -0.02556 -0.17548 298 LEU A CA  
4262 C C   . LEU A 297 ? 1.38790 1.62123 1.30145 -0.43696 -0.02145 -0.18850 298 LEU A C   
4263 O O   . LEU A 297 ? 1.75200 1.99293 1.65012 -0.44993 -0.02651 -0.19273 298 LEU A O   
4264 C CB  . LEU A 297 ? 1.37922 1.54999 1.28745 -0.39402 -0.01392 -0.17422 298 LEU A CB  
4265 C CG  . LEU A 297 ? 1.58452 1.70788 1.46987 -0.40451 0.00866  -0.18115 298 LEU A CG  
4266 C CD1 . LEU A 297 ? 1.51655 1.63903 1.41906 -0.39060 0.01629  -0.17601 298 LEU A CD1 
4267 C CD2 . LEU A 297 ? 1.72218 1.79730 1.58219 -0.39765 0.01873  -0.18063 298 LEU A CD2 
4279 N N   . ALA A 298 ? 1.39620 1.63134 1.31221 -0.45155 -0.01170 -0.19551 299 ALA A N   
4280 C CA  . ALA A 298 ? 1.37696 1.61483 1.27573 -0.48546 -0.00353 -0.21071 299 ALA A CA  
4281 C C   . ALA A 298 ? 1.39011 1.56858 1.25783 -0.49706 0.01723  -0.21926 299 ALA A C   
4282 O O   . ALA A 298 ? 1.28362 1.41774 1.14599 -0.48245 0.03127  -0.21350 299 ALA A O   
4283 C CB  . ALA A 298 ? 1.59901 1.85575 1.51185 -0.49731 0.00191  -0.21493 299 ALA A CB  
4289 N N   . THR A 299 ? 1.54307 1.72356 1.39119 -0.52307 0.01967  -0.23333 300 THR A N   
4290 C CA  . THR A 299 ? 1.48355 1.60863 1.30386 -0.53757 0.04130  -0.24466 300 THR A CA  
4291 C C   . THR A 299 ? 1.39974 1.49623 1.21887 -0.55288 0.06348  -0.25154 300 THR A C   
4292 O O   . THR A 299 ? 1.40770 1.53579 1.23680 -0.57305 0.06287  -0.25968 300 THR A O   
4293 C CB  . THR A 299 ? 1.45583 1.59690 1.25783 -0.56449 0.03905  -0.26133 300 THR A CB  
4294 O OG1 . THR A 299 ? 1.44131 1.62038 1.24813 -0.55050 0.01666  -0.25193 300 THR A OG1 
4295 C CG2 . THR A 299 ? 1.45900 1.53974 1.23364 -0.57510 0.06114  -0.27283 300 THR A CG2 
4303 N N   . ARG A 300 ? 1.37956 1.41748 1.18705 -0.54298 0.08377  -0.24722 301 ARG A N   
4304 C CA  . ARG A 300 ? 1.44162 1.44814 1.24979 -0.55229 0.10693  -0.24844 301 ARG A CA  
4305 C C   . ARG A 300 ? 1.59996 1.54147 1.38447 -0.56055 0.13303  -0.25531 301 ARG A C   
4306 O O   . ARG A 300 ? 1.67385 1.59306 1.44263 -0.55220 0.13208  -0.25601 301 ARG A O   
4307 C CB  . ARG A 300 ? 1.52499 1.53299 1.35163 -0.52326 0.10609  -0.22885 301 ARG A CB  
4308 C CG  . ARG A 300 ? 1.61642 1.68645 1.47002 -0.51541 0.08369  -0.22320 301 ARG A CG  
4309 C CD  . ARG A 300 ? 1.54777 1.62032 1.41922 -0.48456 0.08262  -0.20579 301 ARG A CD  
4310 N NE  . ARG A 300 ? 1.55724 1.68611 1.45636 -0.47986 0.06574  -0.20260 301 ARG A NE  
4311 C CZ  . ARG A 300 ? 1.70866 1.87367 1.62741 -0.45814 0.04502  -0.19545 301 ARG A CZ  
4312 N NH1 . ARG A 300 ? 1.62646 1.77870 1.54074 -0.43878 0.03775  -0.18999 301 ARG A NH1 
4313 N NH2 . ARG A 300 ? 1.74455 1.95924 1.68945 -0.45586 0.03235  -0.19399 301 ARG A NH2 
4327 N N   . ILE A 301 ? 1.69672 1.60759 1.48017 -0.57675 0.15746  -0.25983 302 ILE A N   
4328 C CA  . ILE A 301 ? 1.73280 1.57874 1.49772 -0.58570 0.18660  -0.26603 302 ILE A CA  
4329 C C   . ILE A 301 ? 1.71627 1.52959 1.48938 -0.57805 0.20966  -0.25225 302 ILE A C   
4330 O O   . ILE A 301 ? 1.69840 1.53835 1.48781 -0.58644 0.20922  -0.25012 302 ILE A O   
4331 C CB  . ILE A 301 ? 1.66617 1.50743 1.41923 -0.62615 0.19767  -0.29399 302 ILE A CB  
4332 C CG1 . ILE A 301 ? 1.64672 1.41654 1.38350 -0.63476 0.23058  -0.30121 302 ILE A CG1 
4333 C CG2 . ILE A 301 ? 1.60696 1.48183 1.37445 -0.65327 0.19934  -0.30445 302 ILE A CG2 
4334 C CD1 . ILE A 301 ? 1.88944 1.65236 1.61257 -0.67189 0.24107  -0.33175 302 ILE A CD1 
4346 N N   . PHE A 302 ? 1.62210 1.38058 1.38435 -0.56097 0.22978  -0.24142 303 PHE A N   
4347 C CA  . PHE A 302 ? 1.77712 1.49834 1.54465 -0.55523 0.25692  -0.22741 303 PHE A CA  
4348 C C   . PHE A 302 ? 1.85852 1.52598 1.61439 -0.58373 0.28828  -0.24349 303 PHE A C   
4349 O O   . PHE A 302 ? 1.92387 1.53991 1.66540 -0.57544 0.30627  -0.24157 303 PHE A O   
4350 C CB  . PHE A 302 ? 1.77216 1.47124 1.53743 -0.51632 0.26081  -0.20301 303 PHE A CB  
4351 C CG  . PHE A 302 ? 1.90832 1.58867 1.68370 -0.50414 0.28276  -0.18254 303 PHE A CG  
4352 C CD1 . PHE A 302 ? 1.68373 1.40883 1.47930 -0.49720 0.27239  -0.17146 303 PHE A CD1 
4353 C CD2 . PHE A 302 ? 1.97024 1.59034 1.73591 -0.49874 0.31433  -0.17330 303 PHE A CD2 
4354 C CE1 . PHE A 302 ? 1.63952 1.35238 1.44439 -0.48575 0.29250  -0.15126 303 PHE A CE1 
4355 C CE2 . PHE A 302 ? 1.99988 1.60599 1.77567 -0.48603 0.33524  -0.15119 303 PHE A CE2 
4356 C CZ  . PHE A 302 ? 1.88863 1.54264 1.68355 -0.47976 0.32397  -0.13994 303 PHE A CZ  
4366 N N   . PRO A 303 ? 1.84673 1.52435 1.60950 -0.61778 0.29675  -0.26048 304 PRO A N   
4367 C CA  . PRO A 303 ? 1.88872 1.52070 1.64136 -0.65011 0.32468  -0.28306 304 PRO A CA  
4368 C C   . PRO A 303 ? 1.93759 1.49811 1.68718 -0.63921 0.36090  -0.26908 304 PRO A C   
4369 O O   . PRO A 303 ? 1.81583 1.36764 1.57637 -0.61865 0.37066  -0.24370 304 PRO A O   
4370 C CB  . PRO A 303 ? 2.04991 1.71346 1.81565 -0.68506 0.32671  -0.29967 304 PRO A CB  
4371 C CG  . PRO A 303 ? 2.09238 1.79823 1.87629 -0.66545 0.31067  -0.27752 304 PRO A CG  
4372 C CD  . PRO A 303 ? 1.72549 1.45628 1.50702 -0.62864 0.28325  -0.26054 304 PRO A CD  
4380 N N   . LEU A 304 ? 2.10159 1.61315 1.83678 -0.65251 0.38128  -0.28547 305 LEU A N   
4381 C CA  . LEU A 304 ? 2.22295 1.66152 1.95573 -0.64606 0.41959  -0.27565 305 LEU A CA  
4382 C C   . LEU A 304 ? 2.47772 1.88228 2.21753 -0.68546 0.45206  -0.29696 305 LEU A C   
4383 O O   . LEU A 304 ? 2.59335 1.93705 2.32740 -0.69487 0.48329  -0.30639 305 LEU A O   
4384 C CB  . LEU A 304 ? 2.08327 1.48566 1.79703 -0.63175 0.42328  -0.27888 305 LEU A CB  
4385 C CG  . LEU A 304 ? 1.93689 1.35335 1.64425 -0.58833 0.40233  -0.25321 305 LEU A CG  
4386 C CD1 . LEU A 304 ? 2.27503 1.66437 1.96241 -0.58224 0.40247  -0.26366 305 LEU A CD1 
4387 C CD2 . LEU A 304 ? 2.11481 1.50528 1.83101 -0.55744 0.42067  -0.21928 305 LEU A CD2 
4399 N N   . GLY A 305 ? 2.46342 1.90647 2.21693 -0.70967 0.44632  -0.30605 306 GLY A N   
4400 C CA  . GLY A 305 ? 2.67470 2.09030 2.43693 -0.74954 0.47682  -0.32808 306 GLY A CA  
4401 C C   . GLY A 305 ? 2.72446 2.07878 2.49839 -0.74092 0.51605  -0.30581 306 GLY A C   
4402 O O   . GLY A 305 ? 2.78457 2.07416 2.55668 -0.75234 0.55121  -0.31496 306 GLY A O   
4406 N N   . LYS A 306 ? 2.72032 2.09585 2.50751 -0.72013 0.51120  -0.27585 307 LYS A N   
4407 C CA  . LYS A 306 ? 2.66494 1.99117 2.46517 -0.71031 0.54730  -0.25007 307 LYS A CA  
4408 C C   . LYS A 306 ? 2.55726 1.84630 2.34987 -0.66672 0.55613  -0.21849 307 LYS A C   
4409 O O   . LYS A 306 ? 2.50322 1.82603 2.28664 -0.63615 0.52666  -0.20547 307 LYS A O   
4410 C CB  . LYS A 306 ? 2.79610 2.16754 2.61386 -0.70719 0.53808  -0.23140 307 LYS A CB  
4411 C CG  . LYS A 306 ? 2.63704 1.96403 2.47177 -0.71399 0.57853  -0.21414 307 LYS A CG  
4412 C CD  . LYS A 306 ? 2.42871 1.80786 2.28046 -0.71897 0.56753  -0.20277 307 LYS A CD  
4413 C CE  . LYS A 306 ? 2.29506 1.72847 2.14712 -0.67816 0.53553  -0.17366 307 LYS A CE  
4414 N NZ  . LYS A 306 ? 2.28946 1.76374 2.16005 -0.67838 0.53293  -0.15665 307 LYS A NZ  
4428 N N   . SER A 307 ? 2.53972 1.75948 2.33739 -0.66407 0.59808  -0.20628 308 SER A N   
4429 C CA  . SER A 307 ? 2.44278 1.62612 2.23407 -0.62287 0.61036  -0.17516 308 SER A CA  
4430 C C   . SER A 307 ? 2.52650 1.75254 2.32478 -0.58496 0.59407  -0.13619 308 SER A C   
4431 O O   . SER A 307 ? 2.46121 1.72905 2.27316 -0.59167 0.58471  -0.12936 308 SER A O   
4432 C CB  . SER A 307 ? 2.45574 1.55760 2.25519 -0.62781 0.66151  -0.16724 308 SER A CB  
4433 O OG  . SER A 307 ? 2.50329 1.56348 2.29527 -0.65848 0.67728  -0.20424 308 SER A OG  
4439 N N   . TRP A 308 ? 2.38449 1.60250 2.17347 -0.54518 0.59104  -0.11172 309 TRP A N   
4440 C CA  . TRP A 308 ? 2.29137 1.55427 2.08571 -0.50756 0.57491  -0.07714 309 TRP A CA  
4441 C C   . TRP A 308 ? 2.33153 1.56592 2.14113 -0.49269 0.61045  -0.04157 309 TRP A C   
4442 O O   . TRP A 308 ? 2.39953 1.57069 2.21479 -0.50642 0.64951  -0.04066 309 TRP A O   
4443 C CB  . TRP A 308 ? 2.21082 1.48284 1.98918 -0.47237 0.55644  -0.06756 309 TRP A CB  
4444 C CG  . TRP A 308 ? 2.07149 1.38900 1.83868 -0.48019 0.51574  -0.09419 309 TRP A CG  
4445 C CD1 . TRP A 308 ? 2.01088 1.36548 1.78139 -0.51166 0.49407  -0.12183 309 TRP A CD1 
4446 C CD2 . TRP A 308 ? 1.95402 1.28635 1.70612 -0.45545 0.49284  -0.09399 309 TRP A CD2 
4447 N NE1 . TRP A 308 ? 1.91157 1.30254 1.67071 -0.50682 0.45964  -0.13682 309 TRP A NE1 
4448 C CE2 . TRP A 308 ? 1.83216 1.20888 1.58007 -0.47322 0.45844  -0.12066 309 TRP A CE2 
4449 C CE3 . TRP A 308 ? 1.90772 1.22184 1.65006 -0.41991 0.49862  -0.07328 309 TRP A CE3 
4450 C CZ2 . TRP A 308 ? 1.94128 1.34137 1.67655 -0.45694 0.43087  -0.12644 309 TRP A CZ2 
4451 C CZ3 . TRP A 308 ? 1.91638 1.25479 1.64532 -0.40508 0.47055  -0.08129 309 TRP A CZ3 
4452 C CH2 . TRP A 308 ? 2.13169 1.51111 1.85763 -0.42372 0.43751  -0.10731 309 TRP A CH2 
4463 N N   . LYS A 309 ? 2.22930 1.51317 2.04701 -0.46418 0.59733  -0.01184 310 LYS A N   
4464 C CA  . LYS A 309 ? 2.40496 1.67699 2.23887 -0.45044 0.62719  0.02406  310 LYS A CA  
4465 C C   . LYS A 309 ? 2.34436 1.54877 2.17539 -0.42972 0.66581  0.04738  310 LYS A C   
4466 O O   . LYS A 309 ? 2.28655 1.48039 2.10301 -0.40489 0.66034  0.05172  310 LYS A O   
4467 C CB  . LYS A 309 ? 2.44568 1.78984 2.28650 -0.41943 0.60374  0.05097  310 LYS A CB  
4468 C CG  . LYS A 309 ? 2.43715 1.84395 2.28812 -0.44070 0.57509  0.03431  310 LYS A CG  
4469 C CD  . LYS A 309 ? 2.40192 1.88153 2.26118 -0.41039 0.55248  0.05797  310 LYS A CD  
4470 C CE  . LYS A 309 ? 2.37792 1.91670 2.24966 -0.43216 0.52738  0.04182  310 LYS A CE  
4471 N NZ  . LYS A 309 ? 1.94652 1.56041 1.82677 -0.40420 0.50185  0.05824  310 LYS A NZ  
4485 N N   . SER A 310 ? 2.42169 1.58006 2.26806 -0.43997 0.70620  0.06308  311 SER A N   
4486 C CA  . SER A 310 ? 2.51362 1.59920 2.36104 -0.42486 0.74848  0.08352  311 SER A CA  
4487 C C   . SER A 310 ? 2.51019 1.61499 2.35862 -0.37475 0.75455  0.13160  311 SER A C   
4488 O O   . SER A 310 ? 2.48091 1.55921 2.31795 -0.34849 0.76233  0.14233  311 SER A O   
4489 C CB  . SER A 310 ? 2.71017 1.73987 2.57697 -0.45364 0.79148  0.08443  311 SER A CB  
4490 O OG  . SER A 310 ? 2.72056 1.79002 2.60470 -0.45348 0.79268  0.10750  311 SER A OG  
4496 N N   . LYS A 311 ? 2.57204 1.72653 2.43407 -0.36112 0.75128  0.16056  312 LYS A N   
4497 C CA  . LYS A 311 ? 2.51247 1.69476 2.37780 -0.31499 0.75870  0.20778  312 LYS A CA  
4498 C C   . LYS A 311 ? 2.39920 1.67258 2.25921 -0.29588 0.71396  0.20859  312 LYS A C   
4499 O O   . LYS A 311 ? 2.49465 1.81793 2.36266 -0.31386 0.69169  0.19612  312 LYS A O   
4500 C CB  . LYS A 311 ? 2.53651 1.70554 2.42395 -0.31158 0.79533  0.24508  312 LYS A CB  
4501 C CG  . LYS A 311 ? 2.70056 1.77630 2.59649 -0.31972 0.84621  0.25440  312 LYS A CG  
4502 C CD  . LYS A 311 ? 2.85192 1.91654 2.77149 -0.31335 0.88337  0.29587  312 LYS A CD  
4503 C CE  . LYS A 311 ? 2.99170 1.95922 2.92302 -0.32013 0.93726  0.30643  312 LYS A CE  
4504 N NZ  . LYS A 311 ? 3.04574 1.95814 2.98001 -0.37158 0.94719  0.25853  312 LYS A NZ  
4518 N N   . ARG A 312 ? 2.33599 1.63114 2.18385 -0.25978 0.70223  0.22258  313 ARG A N   
4519 C CA  . ARG A 312 ? 2.33218 1.71022 2.17551 -0.23956 0.66218  0.22166  313 ARG A CA  
4520 C C   . ARG A 312 ? 2.38991 1.80328 2.23644 -0.19416 0.67268  0.26621  313 ARG A C   
4521 O O   . ARG A 312 ? 2.47372 1.84224 2.31716 -0.17301 0.70317  0.29129  313 ARG A O   
4522 C CB  . ARG A 312 ? 2.45856 1.83769 2.28258 -0.24264 0.63188  0.18770  313 ARG A CB  
4523 C CG  . ARG A 312 ? 2.35795 1.70891 2.17775 -0.28657 0.62045  0.14383  313 ARG A CG  
4524 C CD  . ARG A 312 ? 2.32070 1.65917 2.12076 -0.28848 0.59912  0.11498  313 ARG A CD  
4525 N NE  . ARG A 312 ? 2.13078 1.42273 1.92584 -0.32864 0.60302  0.07895  313 ARG A NE  
4526 C CZ  . ARG A 312 ? 2.19436 1.46481 1.97276 -0.33791 0.59065  0.05115  313 ARG A CZ  
4527 N NH1 . ARG A 312 ? 2.42982 1.71722 2.19469 -0.31068 0.57315  0.05456  313 ARG A NH1 
4528 N NH2 . ARG A 312 ? 2.20867 1.44246 1.98425 -0.37611 0.59646  0.01864  313 ARG A NH2 
4542 N N   . PRO A 313 ? 2.32320 1.81986 2.17686 -0.17818 0.64860  0.27663  314 PRO A N   
4543 C CA  . PRO A 313 ? 2.43002 1.96945 2.28889 -0.13648 0.66075  0.32056  314 PRO A CA  
4544 C C   . PRO A 313 ? 2.52935 2.05963 2.37270 -0.10409 0.66294  0.33067  314 PRO A C   
4545 O O   . PRO A 313 ? 2.61182 2.13059 2.45742 -0.07487 0.69228  0.36961  314 PRO A O   
4546 C CB  . PRO A 313 ? 2.34711 1.98232 2.21518 -0.13173 0.62741  0.31652  314 PRO A CB  
4547 C CG  . PRO A 313 ? 2.17885 1.81986 2.04147 -0.16203 0.59268  0.26922  314 PRO A CG  
4548 C CD  . PRO A 313 ? 2.21772 1.77612 2.07615 -0.19661 0.61025  0.24886  314 PRO A CD  
4556 N N   . LEU A 314 ? 2.50474 2.04102 2.33300 -0.10772 0.63360  0.29822  315 LEU A N   
4557 C CA  . LEU A 314 ? 2.45366 1.98531 2.26652 -0.07864 0.63277  0.30439  315 LEU A CA  
4558 C C   . LEU A 314 ? 2.43371 1.91644 2.22982 -0.10048 0.61838  0.26446  315 LEU A C   
4559 O O   . LEU A 314 ? 2.47627 1.95008 2.27316 -0.13481 0.60123  0.23141  315 LEU A O   
4560 C CB  . LEU A 314 ? 2.45491 2.07771 2.26835 -0.04982 0.60579  0.31150  315 LEU A CB  
4561 C CG  . LEU A 314 ? 2.37898 2.06266 2.20754 -0.02337 0.61901  0.35252  315 LEU A CG  
4562 C CD1 . LEU A 314 ? 2.35205 2.13145 2.18271 -0.00244 0.58817  0.34871  315 LEU A CD1 
4563 C CD2 . LEU A 314 ? 2.44498 2.09478 2.27194 0.00610  0.65824  0.39527  315 LEU A CD2 
4575 N N   . PRO A 315 ? 2.50341 1.95720 2.28436 -0.08080 0.62537  0.26761  316 PRO A N   
4576 C CA  . PRO A 315 ? 2.56132 1.96820 2.32580 -0.10113 0.61361  0.23092  316 PRO A CA  
4577 C C   . PRO A 315 ? 2.41383 1.86864 2.17514 -0.11803 0.57004  0.19561  316 PRO A C   
4578 O O   . PRO A 315 ? 2.37213 1.89289 2.13429 -0.09804 0.54575  0.19791  316 PRO A O   
4579 C CB  . PRO A 315 ? 2.71488 2.10696 2.46518 -0.06826 0.62391  0.24616  316 PRO A CB  
4580 C CG  . PRO A 315 ? 2.86627 2.26338 2.62700 -0.03800 0.65630  0.29315  316 PRO A CG  
4581 C CD  . PRO A 315 ? 2.36696 1.82811 2.14533 -0.03953 0.64686  0.30599  316 PRO A CD  
4589 N N   . ILE A 316 ? 2.25110 1.67351 2.01002 -0.15532 0.56139  0.16251  317 ILE A N   
4590 C CA  . ILE A 316 ? 2.21319 1.67539 1.97013 -0.17324 0.52204  0.12941  317 ILE A CA  
4591 C C   . ILE A 316 ? 2.41484 1.82374 2.16270 -0.20951 0.52138  0.09595  317 ILE A C   
4592 O O   . ILE A 316 ? 2.36040 1.71445 2.11082 -0.22916 0.54920  0.09542  317 ILE A O   
4593 C CB  . ILE A 316 ? 2.30195 1.82699 2.07758 -0.18062 0.50500  0.13101  317 ILE A CB  
4594 C CG1 . ILE A 316 ? 2.21443 1.78290 1.98998 -0.19460 0.46463  0.09920  317 ILE A CG1 
4595 C CG2 . ILE A 316 ? 2.43897 1.93248 2.22597 -0.20846 0.52628  0.13233  317 ILE A CG2 
4596 C CD1 . ILE A 316 ? 2.18397 1.81837 1.97875 -0.19945 0.44577  0.09882  317 ILE A CD1 
4608 N N   . THR A 317 ? 2.57024 1.99765 2.30867 -0.21878 0.49033  0.06772  318 THR A N   
4609 C CA  . THR A 317 ? 2.27941 1.67119 2.00915 -0.25353 0.48443  0.03408  318 THR A CA  
4610 C C   . THR A 317 ? 2.09435 1.53607 1.82202 -0.26008 0.44359  0.01036  318 THR A C   
4611 O O   . THR A 317 ? 2.21418 1.71181 1.94854 -0.23880 0.42275  0.01896  318 THR A O   
4612 C CB  . THR A 317 ? 2.13330 1.45960 1.84599 -0.25237 0.50571  0.02915  318 THR A CB  
4613 O OG1 . THR A 317 ? 2.11916 1.41058 1.82615 -0.29014 0.50613  -0.00317 318 THR A OG1 
4614 C CG2 . THR A 317 ? 2.12565 1.46911 1.82387 -0.22700 0.48746  0.02848  318 THR A CG2 
4622 N N   . MET A 318 ? 1.90275 1.32552 1.62240 -0.28980 0.43335  -0.01973 319 MET A N   
4623 C CA  . MET A 318 ? 1.98419 1.45112 1.70311 -0.29817 0.39650  -0.04140 319 MET A CA  
4624 C C   . MET A 318 ? 2.05106 1.48583 1.75097 -0.31009 0.39153  -0.06386 319 MET A C   
4625 O O   . MET A 318 ? 2.02321 1.40332 1.71355 -0.32595 0.41502  -0.07223 319 MET A O   
4626 C CB  . MET A 318 ? 2.07628 1.57406 1.80949 -0.32673 0.38296  -0.05596 319 MET A CB  
4627 C CG  . MET A 318 ? 2.10679 1.62147 1.85787 -0.32380 0.39662  -0.03603 319 MET A CG  
4628 S SD  . MET A 318 ? 2.03541 1.60614 1.80513 -0.34912 0.37221  -0.05132 319 MET A SD  
4629 C CE  . MET A 318 ? 1.91377 1.44298 1.67512 -0.39423 0.38089  -0.08180 319 MET A CE  
4639 N N   . ILE A 319 ? 1.94954 1.41965 1.64537 -0.30255 0.36157  -0.07387 320 ILE A N   
4640 C CA  . ILE A 319 ? 1.81974 1.26980 1.49807 -0.31237 0.35259  -0.09418 320 ILE A CA  
4641 C C   . ILE A 319 ? 1.76765 1.26823 1.45124 -0.32152 0.31692  -0.11019 320 ILE A C   
4642 O O   . ILE A 319 ? 1.71279 1.26266 1.41277 -0.31168 0.29882  -0.10319 320 ILE A O   
4643 C CB  . ILE A 319 ? 1.81948 1.24884 1.48327 -0.28342 0.35922  -0.08295 320 ILE A CB  
4644 C CG1 . ILE A 319 ? 1.83249 1.31270 1.50488 -0.25241 0.34026  -0.06749 320 ILE A CG1 
4645 C CG2 . ILE A 319 ? 1.84818 1.22456 1.50713 -0.27399 0.39644  -0.06635 320 ILE A CG2 
4646 C CD1 . ILE A 319 ? 1.71289 1.18110 1.37144 -0.22464 0.34389  -0.05833 320 ILE A CD1 
4658 N N   . GLY A 320 ? 2.05213 1.54120 1.72263 -0.34024 0.30788  -0.13157 321 GLY A N   
4659 C CA  . GLY A 320 ? 2.04949 1.58389 1.72401 -0.34724 0.27555  -0.14453 321 GLY A CA  
4660 C C   . GLY A 320 ? 1.79648 1.36308 1.48567 -0.37301 0.26474  -0.15533 321 GLY A C   
4661 O O   . GLY A 320 ? 1.73881 1.28538 1.43023 -0.39470 0.28282  -0.16071 321 GLY A O   
4665 N N   . ASP A 321 ? 1.70005 1.31808 1.40073 -0.37029 0.23538  -0.15844 322 ASP A N   
4666 C CA  . ASP A 321 ? 1.71089 1.36647 1.42647 -0.39263 0.22228  -0.16812 322 ASP A CA  
4667 C C   . ASP A 321 ? 1.88580 1.54653 1.61679 -0.39316 0.23571  -0.15717 322 ASP A C   
4668 O O   . ASP A 321 ? 1.87843 1.54813 1.61622 -0.41901 0.23832  -0.16713 322 ASP A O   
4669 C CB  . ASP A 321 ? 1.58385 1.29375 1.31295 -0.38299 0.19037  -0.16844 322 ASP A CB  
4670 C CG  . ASP A 321 ? 1.54045 1.25445 1.25706 -0.39283 0.17540  -0.18194 322 ASP A CG  
4671 O OD1 . ASP A 321 ? 1.70681 1.38089 1.40245 -0.40207 0.18918  -0.19040 322 ASP A OD1 
4672 O OD2 . ASP A 321 ? 1.54561 1.30381 1.27437 -0.39116 0.15067  -0.18363 322 ASP A OD2 
4677 N N   . ALA A 322 ? 1.70928 1.36786 1.44602 -0.36537 0.24465  -0.13669 323 ALA A N   
4678 C CA  . ALA A 322 ? 1.68613 1.34940 1.43657 -0.36453 0.25973  -0.12367 323 ALA A CA  
4679 C C   . ALA A 322 ? 1.83906 1.45392 1.58152 -0.38846 0.28868  -0.12838 323 ALA A C   
4680 O O   . ALA A 322 ? 1.86771 1.48944 1.62251 -0.40118 0.29853  -0.12511 323 ALA A O   
4681 C CB  . ALA A 322 ? 1.83017 1.49730 1.58469 -0.32990 0.26792  -0.10016 323 ALA A CB  
4687 N N   . ALA A 323 ? 1.75831 1.32412 1.48154 -0.39555 0.30351  -0.13697 324 ALA A N   
4688 C CA  . ALA A 323 ? 1.68250 1.19753 1.39964 -0.41901 0.33378  -0.14413 324 ALA A CA  
4689 C C   . ALA A 323 ? 1.73634 1.25600 1.45073 -0.45794 0.32786  -0.17298 324 ALA A C   
4690 O O   . ALA A 323 ? 1.84328 1.34088 1.56185 -0.48337 0.34851  -0.18127 324 ALA A O   
4691 C CB  . ALA A 323 ? 1.78796 1.24586 1.48743 -0.40672 0.35637  -0.13967 324 ALA A CB  
4697 N N   . HIS A 324 ? 1.78097 1.33152 1.48942 -0.46344 0.30091  -0.18811 325 HIS A N   
4698 C CA  . HIS A 324 ? 1.80906 1.36632 1.51178 -0.49939 0.29611  -0.21594 325 HIS A CA  
4699 C C   . HIS A 324 ? 1.68792 1.30094 1.39207 -0.49978 0.26049  -0.22431 325 HIS A C   
4700 O O   . HIS A 324 ? 1.55698 1.16891 1.24703 -0.51034 0.25288  -0.23992 325 HIS A O   
4701 C CB  . HIS A 324 ? 1.69674 1.19889 1.38003 -0.51166 0.31821  -0.23049 325 HIS A CB  
4702 C CG  . HIS A 324 ? 1.67088 1.15227 1.34028 -0.48257 0.31610  -0.21968 325 HIS A CG  
4703 N ND1 . HIS A 324 ? 1.58828 1.10349 1.25178 -0.47089 0.28758  -0.22153 325 HIS A ND1 
4704 C CD2 . HIS A 324 ? 1.72276 1.15467 1.38397 -0.46215 0.33948  -0.20587 325 HIS A CD2 
4705 C CE1 . HIS A 324 ? 1.73516 1.22249 1.38668 -0.44603 0.29321  -0.21104 325 HIS A CE1 
4706 N NE2 . HIS A 324 ? 1.77639 1.21436 1.42596 -0.43981 0.32411  -0.20140 325 HIS A NE2 
4713 N N   . LEU A 325 ? 1.72634 1.38919 1.44854 -0.48773 0.23938  -0.21341 326 LEU A N   
4714 C CA  . LEU A 325 ? 1.80484 1.52251 1.53304 -0.49067 0.20765  -0.22074 326 LEU A CA  
4715 C C   . LEU A 325 ? 1.84526 1.57520 1.56695 -0.52801 0.20598  -0.24577 326 LEU A C   
4716 O O   . LEU A 325 ? 1.79689 1.51539 1.52095 -0.55373 0.22320  -0.25671 326 LEU A O   
4717 C CB  . LEU A 325 ? 1.64548 1.41317 1.39793 -0.47901 0.19053  -0.20884 326 LEU A CB  
4718 C CG  . LEU A 325 ? 1.51262 1.33951 1.27631 -0.48217 0.15935  -0.21467 326 LEU A CG  
4719 C CD1 . LEU A 325 ? 1.53981 1.37557 1.30170 -0.45547 0.14185  -0.20602 326 LEU A CD1 
4720 C CD2 . LEU A 325 ? 1.77962 1.65205 1.56821 -0.48049 0.14865  -0.20836 326 LEU A CD2 
4732 N N   . MET A 326 ? 1.94754 1.70345 1.66168 -0.53134 0.18592  -0.25486 327 MET A N   
4733 C CA  . MET A 326 ? 1.84713 1.62419 1.55407 -0.56565 0.18225  -0.27891 327 MET A CA  
4734 C C   . MET A 326 ? 1.73852 1.56979 1.44809 -0.55935 0.15093  -0.27795 327 MET A C   
4735 O O   . MET A 326 ? 1.98409 1.82005 1.69632 -0.52985 0.13719  -0.26156 327 MET A O   
4736 C CB  . MET A 326 ? 1.63582 1.36258 1.32082 -0.58326 0.20545  -0.29647 327 MET A CB  
4737 C CG  . MET A 326 ? 1.67610 1.38184 1.34509 -0.56223 0.20091  -0.29091 327 MET A CG  
4738 S SD  . MET A 326 ? 1.82138 1.46621 1.46626 -0.58150 0.23023  -0.31214 327 MET A SD  
4739 C CE  . MET A 326 ? 1.88450 1.46151 1.53222 -0.56209 0.26267  -0.29452 327 MET A CE  
4749 N N   . PRO A 327 ? 1.47979 1.35477 1.18993 -0.58646 0.13995  -0.29469 328 PRO A N   
4750 C CA  . PRO A 327 ? 1.52060 1.44804 1.23311 -0.58019 0.11180  -0.29160 328 PRO A CA  
4751 C C   . PRO A 327 ? 1.85137 1.75389 1.54571 -0.56645 0.11057  -0.28933 328 PRO A C   
4752 O O   . PRO A 327 ? 1.91222 1.76674 1.58757 -0.57601 0.13140  -0.30102 328 PRO A O   
4753 C CB  . PRO A 327 ? 1.65434 1.62465 1.36456 -0.61716 0.10823  -0.31410 328 PRO A CB  
4754 C CG  . PRO A 327 ? 1.68181 1.63886 1.40007 -0.63663 0.12654  -0.32285 328 PRO A CG  
4755 C CD  . PRO A 327 ? 1.51100 1.39654 1.22347 -0.62252 0.15194  -0.31484 328 PRO A CD  
4763 N N   . PRO A 328 ? 1.89622 1.82942 1.59702 -0.54386 0.08755  -0.27440 329 PRO A N   
4764 C CA  . PRO A 328 ? 1.61287 1.52410 1.29736 -0.52929 0.08562  -0.27056 329 PRO A CA  
4765 C C   . PRO A 328 ? 1.93803 1.88088 1.60864 -0.54871 0.07579  -0.28393 329 PRO A C   
4766 O O   . PRO A 328 ? 1.96287 1.89460 1.62056 -0.53718 0.07192  -0.28014 329 PRO A O   
4767 C CB  . PRO A 328 ? 1.72194 1.65216 1.42477 -0.49486 0.06688  -0.24678 329 PRO A CB  
4768 C CG  . PRO A 328 ? 1.71006 1.69961 1.43584 -0.50072 0.04900  -0.24353 329 PRO A CG  
4769 C CD  . PRO A 328 ? 1.72003 1.70783 1.44544 -0.52924 0.06338  -0.25947 329 PRO A CD  
4777 N N   . PHE A 329 ? 1.94955 1.93501 1.62260 -0.57783 0.07175  -0.29937 330 PHE A N   
4778 C CA  . PHE A 329 ? 1.74973 1.77899 1.41158 -0.59654 0.06044  -0.31131 330 PHE A CA  
4779 C C   . PHE A 329 ? 1.86133 1.85311 1.49681 -0.61462 0.07897  -0.33246 330 PHE A C   
4780 O O   . PHE A 329 ? 2.01624 2.04403 1.64013 -0.63024 0.07093  -0.34376 330 PHE A O   
4781 C CB  . PHE A 329 ? 1.54189 1.63071 1.21379 -0.62405 0.05283  -0.32380 330 PHE A CB  
4782 C CG  . PHE A 329 ? 1.53096 1.65589 1.22996 -0.60849 0.03694  -0.30540 330 PHE A CG  
4783 C CD1 . PHE A 329 ? 1.50275 1.68018 1.21663 -0.58951 0.01147  -0.28594 330 PHE A CD1 
4784 C CD2 . PHE A 329 ? 1.82707 1.93324 1.53803 -0.61237 0.04861  -0.30703 330 PHE A CD2 
4785 C CE1 . PHE A 329 ? 1.46084 1.67038 1.20165 -0.57487 -0.00176 -0.27026 330 PHE A CE1 
4786 C CE2 . PHE A 329 ? 1.90338 2.04423 1.63971 -0.59833 0.03439  -0.29156 330 PHE A CE2 
4787 C CZ  . PHE A 329 ? 1.79978 1.99187 1.55139 -0.57956 0.00929  -0.27401 330 PHE A CZ  
4797 N N   . ALA A 330 ? 1.91425 1.83775 1.54096 -0.61245 0.10391  -0.33765 331 ALA A N   
4798 C CA  . ALA A 330 ? 1.85374 1.73443 1.45727 -0.62472 0.12324  -0.35584 331 ALA A CA  
4799 C C   . ALA A 330 ? 2.02320 1.85801 1.61762 -0.59297 0.12613  -0.33926 331 ALA A C   
4800 O O   . ALA A 330 ? 1.95791 1.75461 1.53327 -0.59889 0.14200  -0.35212 331 ALA A O   
4801 C CB  . ALA A 330 ? 1.99211 1.82713 1.59259 -0.64932 0.15384  -0.37676 331 ALA A CB  
4807 N N   . GLY A 331 ? 2.18453 2.02404 1.79284 -0.56019 0.11178  -0.31258 332 GLY A N   
4808 C CA  . GLY A 331 ? 2.09022 1.89045 1.69184 -0.52967 0.11445  -0.29689 332 GLY A CA  
4809 C C   . GLY A 331 ? 1.95542 1.68652 1.54553 -0.52787 0.14398  -0.30257 332 GLY A C   
4810 O O   . GLY A 331 ? 2.11765 1.81460 1.69032 -0.52073 0.15333  -0.30536 332 GLY A O   
4814 N N   . GLN A 332 ? 1.93697 1.64779 1.53751 -0.53355 0.15952  -0.30303 333 GLN A N   
4815 C CA  . GLN A 332 ? 2.10951 1.75568 1.70220 -0.53286 0.19025  -0.30648 333 GLN A CA  
4816 C C   . GLN A 332 ? 2.26845 1.89365 1.87514 -0.50569 0.19669  -0.28344 333 GLN A C   
4817 O O   . GLN A 332 ? 2.31550 1.88856 1.91744 -0.50016 0.22252  -0.28085 333 GLN A O   
4818 C CB  . GLN A 332 ? 2.12400 1.75820 1.71493 -0.57007 0.21073  -0.33151 333 GLN A CB  
4819 C CG  . GLN A 332 ? 2.47840 2.12939 2.05382 -0.59973 0.21021  -0.35883 333 GLN A CG  
4820 C CD  . GLN A 332 ? 2.71124 2.32048 2.26627 -0.59219 0.22251  -0.36446 333 GLN A CD  
4821 O OE1 . GLN A 332 ? 2.67867 2.22874 2.22962 -0.57930 0.24602  -0.35907 333 GLN A OE1 
4822 N NE2 . GLN A 332 ? 2.67916 2.32142 2.22170 -0.59953 0.20696  -0.37427 333 GLN A NE2 
4831 N N   . GLY A 333 ? 1.87137 1.53711 1.49608 -0.48806 0.17503  -0.26646 334 GLY A N   
4832 C CA  . GLY A 333 ? 1.83076 1.48608 1.47040 -0.46473 0.18041  -0.24684 334 GLY A CA  
4833 C C   . GLY A 333 ? 1.98319 1.59745 1.61427 -0.43550 0.19262  -0.23242 334 GLY A C   
4834 O O   . GLY A 333 ? 2.13335 1.70486 1.76124 -0.43179 0.21770  -0.22826 334 GLY A O   
4838 N N   . VAL A 334 ? 1.85755 1.48569 1.48578 -0.41418 0.17595  -0.22381 335 VAL A N   
4839 C CA  . VAL A 334 ? 1.95819 1.55524 1.57960 -0.38490 0.18552  -0.20977 335 VAL A CA  
4840 C C   . VAL A 334 ? 1.95454 1.49752 1.55340 -0.39172 0.21029  -0.21902 335 VAL A C   
4841 O O   . VAL A 334 ? 1.81681 1.32284 1.41150 -0.37389 0.23002  -0.20812 335 VAL A O   
4842 C CB  . VAL A 334 ? 1.79357 1.41803 1.41732 -0.36384 0.16284  -0.20128 335 VAL A CB  
4843 C CG1 . VAL A 334 ? 1.80991 1.44081 1.41799 -0.37915 0.15322  -0.21460 335 VAL A CG1 
4844 C CG2 . VAL A 334 ? 1.61604 1.21435 1.23433 -0.33360 0.17261  -0.18743 335 VAL A CG2 
4854 N N   . ASN A 335 ? 2.10950 1.64969 1.69427 -0.41682 0.21010  -0.23914 336 ASN A N   
4855 C CA  . ASN A 335 ? 2.07049 1.55989 1.63515 -0.42480 0.23427  -0.25104 336 ASN A CA  
4856 C C   . ASN A 335 ? 2.11849 1.56426 1.68671 -0.43124 0.26483  -0.25088 336 ASN A C   
4857 O O   . ASN A 335 ? 2.16176 1.55937 1.72067 -0.41873 0.28817  -0.24580 336 ASN A O   
4858 C CB  . ASN A 335 ? 1.96643 1.46860 1.51829 -0.45531 0.22916  -0.27606 336 ASN A CB  
4859 C CG  . ASN A 335 ? 1.97378 1.51691 1.52116 -0.44777 0.20130  -0.27360 336 ASN A CG  
4860 O OD1 . ASN A 335 ? 1.77450 1.32833 1.32712 -0.41950 0.18828  -0.25480 336 ASN A OD1 
4861 N ND2 . ASN A 335 ? 2.53153 2.09938 2.06990 -0.47344 0.19314  -0.29278 336 ASN A ND2 
4868 N N   . SER A 336 ? 1.99372 1.45632 1.57654 -0.44985 0.26581  -0.25502 337 SER A N   
4869 C CA  . SER A 336 ? 1.94129 1.36409 1.53026 -0.45641 0.29538  -0.25288 337 SER A CA  
4870 C C   . SER A 336 ? 2.03406 1.44625 1.63244 -0.42241 0.30235  -0.22422 337 SER A C   
4871 O O   . SER A 336 ? 1.90596 1.27062 1.50110 -0.41267 0.33040  -0.21540 337 SER A O   
4872 C CB  . SER A 336 ? 2.00375 1.45267 1.60638 -0.48604 0.29307  -0.26511 337 SER A CB  
4873 O OG  . SER A 336 ? 2.48493 1.95457 2.07941 -0.51726 0.28451  -0.29176 337 SER A OG  
4879 N N   . GLY A 337 ? 2.11912 1.57729 1.73033 -0.40368 0.27801  -0.20939 338 GLY A N   
4880 C CA  . GLY A 337 ? 1.77491 1.23252 1.39588 -0.37217 0.28332  -0.18404 338 GLY A CA  
4881 C C   . GLY A 337 ? 1.81566 1.23764 1.42236 -0.34661 0.29727  -0.17312 338 GLY A C   
4882 O O   . GLY A 337 ? 1.71089 1.10796 1.32006 -0.32847 0.31848  -0.15561 338 GLY A O   
4886 N N   . LEU A 338 ? 1.82575 1.24718 1.41749 -0.34443 0.28595  -0.18229 339 LEU A N   
4887 C CA  . LEU A 338 ? 1.69536 1.08421 1.27232 -0.32134 0.29877  -0.17377 339 LEU A CA  
4888 C C   . LEU A 338 ? 2.03068 1.35971 1.59747 -0.33010 0.33320  -0.17818 339 LEU A C   
4889 O O   . LEU A 338 ? 2.11381 1.41273 1.67550 -0.30638 0.35231  -0.16254 339 LEU A O   
4890 C CB  . LEU A 338 ? 1.83764 1.24010 1.40102 -0.32058 0.27915  -0.18430 339 LEU A CB  
4891 C CG  . LEU A 338 ? 1.52852 0.98471 1.10367 -0.30662 0.24813  -0.17690 339 LEU A CG  
4892 C CD1 . LEU A 338 ? 1.82272 1.29039 1.38509 -0.30945 0.23070  -0.18717 339 LEU A CD1 
4893 C CD2 . LEU A 338 ? 1.57053 1.03596 1.15435 -0.27277 0.24986  -0.15508 339 LEU A CD2 
4905 N N   . MET A 339 ? 2.07204 1.38456 1.63723 -0.36377 0.34268  -0.19950 340 MET A N   
4906 C CA  . MET A 339 ? 2.05359 1.30688 1.61351 -0.37430 0.37841  -0.20540 340 MET A CA  
4907 C C   . MET A 339 ? 2.11931 1.35281 1.69299 -0.35770 0.40106  -0.18113 340 MET A C   
4908 O O   . MET A 339 ? 2.24150 1.42759 1.81115 -0.34394 0.43000  -0.17031 340 MET A O   
4909 C CB  . MET A 339 ? 2.04072 1.28775 1.60048 -0.41629 0.38404  -0.23491 340 MET A CB  
4910 C CG  . MET A 339 ? 2.26806 1.45174 1.82135 -0.43106 0.42096  -0.24844 340 MET A CG  
4911 S SD  . MET A 339 ? 2.19234 1.35339 1.72184 -0.43261 0.42260  -0.26786 340 MET A SD  
4912 C CE  . MET A 339 ? 2.78808 1.98758 2.31363 -0.47745 0.40398  -0.30508 340 MET A CE  
4922 N N   . ASP A 340 ? 2.11237 1.38375 1.70316 -0.35785 0.38868  -0.17114 341 ASP A N   
4923 C CA  . ASP A 340 ? 2.10560 1.36701 1.71026 -0.34106 0.40803  -0.14599 341 ASP A CA  
4924 C C   . ASP A 340 ? 2.12160 1.38069 1.72219 -0.30053 0.41261  -0.11980 341 ASP A C   
4925 O O   . ASP A 340 ? 2.21706 1.43783 1.81813 -0.28531 0.44217  -0.10223 341 ASP A O   
4926 C CB  . ASP A 340 ? 2.03081 1.34306 1.65404 -0.34687 0.38900  -0.14111 341 ASP A CB  
4927 C CG  . ASP A 340 ? 1.97389 1.29195 1.60229 -0.38670 0.38621  -0.16559 341 ASP A CG  
4928 O OD1 . ASP A 340 ? 2.07584 1.34999 1.69785 -0.41008 0.40908  -0.18246 341 ASP A OD1 
4929 O OD2 . ASP A 340 ? 1.82204 1.19017 1.46191 -0.39484 0.36193  -0.16886 341 ASP A OD2 
4934 N N   . ALA A 341 ? 2.02605 1.32748 1.62370 -0.28250 0.38448  -0.11661 342 ALA A N   
4935 C CA  . ALA A 341 ? 2.09142 1.39846 1.68549 -0.24509 0.38713  -0.09419 342 ALA A CA  
4936 C C   . ALA A 341 ? 2.14088 1.39479 1.71772 -0.23609 0.41130  -0.09349 342 ALA A C   
4937 O O   . ALA A 341 ? 2.22897 1.46834 1.80517 -0.20820 0.43023  -0.07055 342 ALA A O   
4938 C CB  . ALA A 341 ? 2.11385 1.47206 1.70791 -0.23240 0.35351  -0.09676 342 ALA A CB  
4944 N N   . LEU A 342 ? 2.10568 1.33317 1.66896 -0.25904 0.41139  -0.11833 343 LEU A N   
4945 C CA  . LEU A 342 ? 2.28348 1.46012 1.83096 -0.25236 0.43455  -0.12084 343 LEU A CA  
4946 C C   . LEU A 342 ? 2.31064 1.43399 1.86455 -0.25393 0.47394  -0.11087 343 LEU A C   
4947 O O   . LEU A 342 ? 2.37263 1.46660 1.92293 -0.22809 0.49678  -0.09160 343 LEU A O   
4948 C CB  . LEU A 342 ? 2.40263 1.56872 1.93558 -0.27971 0.42527  -0.15222 343 LEU A CB  
4949 C CG  . LEU A 342 ? 2.36032 1.48037 1.87567 -0.27327 0.44458  -0.15876 343 LEU A CG  
4950 C CD1 . LEU A 342 ? 2.48563 1.62420 1.99165 -0.23828 0.43314  -0.14200 343 LEU A CD1 
4951 C CD2 . LEU A 342 ? 2.45030 1.56263 1.95352 -0.30585 0.43801  -0.19237 343 LEU A CD2 
4963 N N   . ILE A 343 ? 2.34849 1.45964 1.91318 -0.28383 0.48332  -0.12306 344 ILE A N   
4964 C CA  . ILE A 343 ? 2.43945 1.49564 2.01255 -0.28934 0.52306  -0.11593 344 ILE A CA  
4965 C C   . ILE A 343 ? 2.47453 1.53728 2.06054 -0.25756 0.53694  -0.07802 344 ILE A C   
4966 O O   . ILE A 343 ? 2.55774 1.57926 2.14420 -0.23741 0.56797  -0.05846 344 ILE A O   
4967 C CB  . ILE A 343 ? 2.29097 1.33916 1.87402 -0.33089 0.52816  -0.13956 344 ILE A CB  
4968 C CG1 . ILE A 343 ? 2.45921 1.49513 2.02876 -0.36220 0.52241  -0.17725 344 ILE A CG1 
4969 C CG2 . ILE A 343 ? 2.27996 1.27648 1.87709 -0.33495 0.56930  -0.12769 344 ILE A CG2 
4970 C CD1 . ILE A 343 ? 2.45012 1.50758 2.02706 -0.40275 0.51193  -0.20369 344 ILE A CD1 
4982 N N   . LEU A 344 ? 2.35565 1.47267 1.95329 -0.25219 0.51492  -0.06664 345 LEU A N   
4983 C CA  . LEU A 344 ? 2.33910 1.47076 1.95005 -0.22413 0.52723  -0.03150 345 LEU A CA  
4984 C C   . LEU A 344 ? 2.38705 1.52023 1.98912 -0.18394 0.53327  -0.00785 345 LEU A C   
4985 O O   . LEU A 344 ? 2.50965 1.61485 2.11629 -0.16271 0.56368  0.01849  345 LEU A O   
4986 C CB  . LEU A 344 ? 2.28232 1.47969 1.90626 -0.22515 0.49828  -0.02761 345 LEU A CB  
4987 C CG  . LEU A 344 ? 2.45116 1.67611 2.09014 -0.19844 0.50751  0.00682  345 LEU A CG  
4988 C CD1 . LEU A 344 ? 2.10838 1.28675 1.75842 -0.20460 0.54583  0.02227  345 LEU A CD1 
4989 C CD2 . LEU A 344 ? 2.25792 1.54905 1.91001 -0.20308 0.47708  0.00454  345 LEU A CD2 
5001 N N   . SER A 345 ? 2.34264 1.50921 1.93264 -0.17286 0.50554  -0.01625 346 SER A N   
5002 C CA  . SER A 345 ? 2.52205 1.69645 2.10339 -0.13556 0.50948  0.00422  346 SER A CA  
5003 C C   . SER A 345 ? 2.62844 1.73833 2.19912 -0.12893 0.54226  0.00726  346 SER A C   
5004 O O   . SER A 345 ? 2.79151 1.89256 2.36253 -0.09739 0.56322  0.03524  346 SER A O   
5005 C CB  . SER A 345 ? 2.51487 1.73221 2.08570 -0.12989 0.47470  -0.00977 346 SER A CB  
5006 O OG  . SER A 345 ? 2.39203 1.58203 1.94835 -0.15323 0.46763  -0.03873 346 SER A OG  
5012 N N   . ASP A 346 ? 2.52368 1.59072 2.08565 -0.15804 0.54767  -0.02151 347 ASP A N   
5013 C CA  . ASP A 346 ? 2.69802 1.70040 2.25228 -0.15490 0.58099  -0.02231 347 ASP A CA  
5014 C C   . ASP A 346 ? 2.81852 1.78149 2.38863 -0.14641 0.62022  0.00311  347 ASP A C   
5015 O O   . ASP A 346 ? 2.91022 1.84532 2.47938 -0.11796 0.64670  0.02689  347 ASP A O   
5016 C CB  . ASP A 346 ? 2.86071 1.82997 2.40610 -0.19304 0.58008  -0.06134 347 ASP A CB  
5017 C CG  . ASP A 346 ? 3.03949 1.95583 2.57183 -0.18732 0.60348  -0.06906 347 ASP A CG  
5018 O OD1 . ASP A 346 ? 3.02864 1.91582 2.56389 -0.15878 0.63176  -0.04278 347 ASP A OD1 
5019 O OD2 . ASP A 346 ? 3.07570 1.98223 2.59537 -0.21078 0.59383  -0.10087 347 ASP A OD2 
5024 N N   . ASN A 347 ? 2.72630 1.68772 2.31203 -0.17033 0.62507  -0.00030 348 ASN A N   
5025 C CA  . ASN A 347 ? 2.77940 1.70230 2.38234 -0.16504 0.66342  0.02398  348 ASN A CA  
5026 C C   . ASN A 347 ? 2.87384 1.82637 2.48332 -0.12158 0.67075  0.06822  348 ASN A C   
5027 O O   . ASN A 347 ? 3.04284 1.95675 2.66044 -0.10203 0.70725  0.09547  348 ASN A O   
5028 C CB  . ASN A 347 ? 2.84439 1.77320 2.46292 -0.19824 0.66172  0.01258  348 ASN A CB  
5029 C CG  . ASN A 347 ? 2.88104 1.76765 2.49731 -0.24165 0.66935  -0.02735 348 ASN A CG  
5030 O OD1 . ASN A 347 ? 2.92993 1.78674 2.53225 -0.24822 0.67282  -0.04873 348 ASN A OD1 
5031 N ND2 . ASN A 347 ? 2.97443 1.86188 2.60462 -0.27228 0.67211  -0.03871 348 ASN A ND2 
5038 N N   . LEU A 348 ? 2.76529 1.78833 2.37272 -0.10587 0.63754  0.07601  349 LEU A N   
5039 C CA  . LEU A 348 ? 2.91743 1.98149 2.53253 -0.06751 0.64187  0.11551  349 LEU A CA  
5040 C C   . LEU A 348 ? 2.94000 2.00117 2.54304 -0.03053 0.65170  0.13423  349 LEU A C   
5041 O O   . LEU A 348 ? 2.77750 1.86509 2.38723 0.00333  0.66395  0.17038  349 LEU A O   
5042 C CB  . LEU A 348 ? 2.98935 2.13280 2.60857 -0.06568 0.60349  0.11336  349 LEU A CB  
5043 C CG  . LEU A 348 ? 2.92871 2.08895 2.56251 -0.09598 0.59250  0.10152  349 LEU A CG  
5044 C CD1 . LEU A 348 ? 2.53143 1.76842 2.16824 -0.09347 0.55263  0.09463  349 LEU A CD1 
5045 C CD2 . LEU A 348 ? 2.93836 2.08449 2.59045 -0.09032 0.62329  0.13131  349 LEU A CD2 
5057 N N   . THR A 349 ? 2.83110 1.86452 2.41673 -0.03577 0.64708  0.11129  350 THR A N   
5058 C CA  . THR A 349 ? 2.93941 1.97766 2.51222 -0.00148 0.65171  0.12605  350 THR A CA  
5059 C C   . THR A 349 ? 2.99530 1.96082 2.55959 -0.00199 0.68186  0.11955  350 THR A C   
5060 O O   . THR A 349 ? 3.07788 2.04277 2.63216 0.02787  0.68987  0.13379  350 THR A O   
5061 C CB  . THR A 349 ? 2.79958 1.89093 2.35795 0.00044  0.61128  0.10655  350 THR A CB  
5062 O OG1 . THR A 349 ? 2.75464 1.81652 2.30091 -0.03147 0.59837  0.06828  350 THR A OG1 
5063 C CG2 . THR A 349 ? 2.84319 2.00455 2.41226 -0.00201 0.58137  0.10820  350 THR A CG2 
5071 N N   . ASN A 350 ? 2.91846 1.82506 2.48716 -0.03500 0.69941  0.09740  351 ASN A N   
5072 C CA  . ASN A 350 ? 2.95540 1.79113 2.51873 -0.03765 0.73052  0.08819  351 ASN A CA  
5073 C C   . ASN A 350 ? 3.04849 1.83621 2.62837 -0.01733 0.77751  0.12232  351 ASN A C   
5074 O O   . ASN A 350 ? 2.93842 1.66292 2.51774 -0.01685 0.80865  0.11772  351 ASN A O   
5075 C CB  . ASN A 350 ? 2.96845 1.76562 2.52922 -0.08474 0.72832  0.04389  351 ASN A CB  
5076 C CG  . ASN A 350 ? 3.00194 1.78225 2.58204 -0.11336 0.74097  0.04012  351 ASN A CG  
5077 O OD1 . ASN A 350 ? 2.96712 1.75019 2.56384 -0.09766 0.75895  0.07256  351 ASN A OD1 
5078 N ND2 . ASN A 350 ? 3.01793 1.78362 2.59604 -0.15596 0.73195  0.00046  351 ASN A ND2 
5085 N N   . GLY A 351 ? 2.82595 1.64268 2.42166 -0.00043 0.78426  0.15660  352 GLY A N   
5086 C CA  . GLY A 351 ? 2.85718 1.63454 2.46989 0.02309  0.82892  0.19505  352 GLY A CA  
5087 C C   . GLY A 351 ? 2.94630 1.64375 2.57424 -0.00598 0.86584  0.18222  352 GLY A C   
5088 O O   . GLY A 351 ? 2.89674 1.54176 2.53679 0.01253  0.90841  0.20734  352 GLY A O   
5092 N N   . LYS A 352 ? 2.90076 1.58877 2.52994 -0.05099 0.85203  0.14395  353 LYS A N   
5093 C CA  . LYS A 352 ? 2.88947 1.50501 2.53343 -0.08411 0.88587  0.12486  353 LYS A CA  
5094 C C   . LYS A 352 ? 3.07183 1.68967 2.73815 -0.09853 0.89786  0.13960  353 LYS A C   
5095 O O   . LYS A 352 ? 3.11296 1.67687 2.79315 -0.13139 0.92325  0.12021  353 LYS A O   
5096 C CB  . LYS A 352 ? 2.88862 1.49114 2.51962 -0.12772 0.86630  0.06945  353 LYS A CB  
5097 C CG  . LYS A 352 ? 2.90265 1.49056 2.51323 -0.11965 0.86078  0.05041  353 LYS A CG  
5098 C CD  . LYS A 352 ? 3.07400 1.64293 2.67544 -0.16570 0.84943  -0.00353 353 LYS A CD  
5099 C CE  . LYS A 352 ? 3.18680 1.73038 2.77061 -0.15975 0.85226  -0.02292 353 LYS A CE  
5100 N NZ  . LYS A 352 ? 2.75024 1.25531 2.33201 -0.20470 0.85971  -0.07243 353 LYS A NZ  
5114 N N   . PHE A 353 ? 3.15478 1.83529 2.82557 -0.07594 0.88093  0.17187  354 PHE A N   
5115 C CA  . PHE A 353 ? 3.22008 1.91238 2.91096 -0.08920 0.88802  0.18606  354 PHE A CA  
5116 C C   . PHE A 353 ? 3.13970 1.85739 2.84322 -0.04594 0.90607  0.24263  354 PHE A C   
5117 O O   . PHE A 353 ? 3.11675 1.88589 2.80955 -0.00953 0.88931  0.26522  354 PHE A O   
5118 C CB  . PHE A 353 ? 3.14149 1.89934 2.82603 -0.11420 0.84141  0.16094  354 PHE A CB  
5119 C CG  . PHE A 353 ? 3.18518 1.92500 2.85923 -0.15815 0.82388  0.10767  354 PHE A CG  
5120 C CD1 . PHE A 353 ? 3.11171 1.81269 2.79877 -0.19944 0.84038  0.08325  354 PHE A CD1 
5121 C CD2 . PHE A 353 ? 3.10199 1.86632 2.75372 -0.15844 0.79187  0.08230  354 PHE A CD2 
5122 C CE1 . PHE A 353 ? 2.88543 1.57691 2.56287 -0.23988 0.82451  0.03427  354 PHE A CE1 
5123 C CE2 . PHE A 353 ? 2.94773 1.70079 2.58996 -0.19791 0.77606  0.03546  354 PHE A CE2 
5124 C CZ  . PHE A 353 ? 2.92242 1.64117 2.57725 -0.23850 0.79209  0.01130  354 PHE A CZ  
5134 N N   . ASN A 354 ? 3.10421 1.78832 2.83128 -0.05079 0.94100  0.26530  355 ASN A N   
5135 C CA  . ASN A 354 ? 3.10789 1.81060 2.84944 -0.00981 0.96456  0.32242  355 ASN A CA  
5136 C C   . ASN A 354 ? 2.94358 1.73989 2.68453 0.00385  0.93067  0.34139  355 ASN A C   
5137 O O   . ASN A 354 ? 2.98246 1.81958 2.72758 0.04486  0.93777  0.38629  355 ASN A O   
5138 C CB  . ASN A 354 ? 3.13865 1.77490 2.90749 -0.02078 1.01388  0.34121  355 ASN A CB  
5139 C CG  . ASN A 354 ? 3.20131 1.74833 2.97606 -0.03232 1.04958  0.32107  355 ASN A CG  
5140 O OD1 . ASN A 354 ? 3.21009 1.73973 2.97033 -0.01527 1.05053  0.31502  355 ASN A OD1 
5141 N ND2 . ASN A 354 ? 3.23358 1.74286 3.03281 -0.05901 1.07085  0.30357  355 ASN A ND2 
5148 N N   . SER A 355 ? 2.86460 1.69859 2.60142 -0.02891 0.89487  0.30837  356 SER A N   
5149 C CA  . SER A 355 ? 2.90876 1.82977 2.64783 -0.01903 0.86400  0.32290  356 SER A CA  
5150 C C   . SER A 355 ? 2.89492 1.86026 2.61893 -0.04533 0.81495  0.27855  356 SER A C   
5151 O O   . SER A 355 ? 2.90916 1.83627 2.62494 -0.07888 0.80759  0.23720  356 SER A O   
5152 C CB  . SER A 355 ? 2.81024 1.73085 2.57283 -0.03092 0.88340  0.34367  356 SER A CB  
5153 O OG  . SER A 355 ? 2.79023 1.66005 2.55938 -0.07808 0.89018  0.30769  356 SER A OG  
5159 N N   . ILE A 356 ? 2.66444 1.71379 2.38616 -0.02911 0.78226  0.28808  357 ILE A N   
5160 C CA  . ILE A 356 ? 2.77822 1.87490 2.48979 -0.05152 0.73630  0.25037  357 ILE A CA  
5161 C C   . ILE A 356 ? 2.73618 1.81348 2.45707 -0.09664 0.73231  0.22194  357 ILE A C   
5162 O O   . ILE A 356 ? 2.65986 1.73438 2.37088 -0.12623 0.70774  0.18146  357 ILE A O   
5163 C CB  . ILE A 356 ? 2.69064 1.88054 2.40371 -0.02597 0.70731  0.26784  357 ILE A CB  
5164 C CG1 . ILE A 356 ? 2.68348 1.89761 2.38442 0.01491  0.70663  0.28762  357 ILE A CG1 
5165 C CG2 . ILE A 356 ? 2.72017 1.95690 2.42893 -0.05139 0.66313  0.23084  357 ILE A CG2 
5166 C CD1 . ILE A 356 ? 2.56492 1.87147 2.26994 0.04340  0.68578  0.30881  357 ILE A CD1 
5178 N N   . GLU A 357 ? 2.52859 1.59484 2.26895 -0.10253 0.75685  0.24343  358 GLU A N   
5179 C CA  . GLU A 357 ? 2.50514 1.55579 2.25557 -0.14571 0.75491  0.21736  358 GLU A CA  
5180 C C   . GLU A 357 ? 2.65417 1.62860 2.39910 -0.17868 0.77133  0.18245  358 GLU A C   
5181 O O   . GLU A 357 ? 2.63692 1.61425 2.37740 -0.21522 0.75017  0.14276  358 GLU A O   
5182 C CB  . GLU A 357 ? 2.61895 1.66700 2.39206 -0.14385 0.78323  0.25020  358 GLU A CB  
5183 C CG  . GLU A 357 ? 2.71977 1.85268 2.50035 -0.11962 0.76372  0.27844  358 GLU A CG  
5184 C CD  . GLU A 357 ? 2.66035 1.81983 2.43867 -0.07033 0.77468  0.32083  358 GLU A CD  
5185 O OE1 . GLU A 357 ? 2.97774 2.08689 2.74900 -0.05360 0.79837  0.33047  358 GLU A OE1 
5186 O OE2 . GLU A 357 ? 2.53879 1.77267 2.32290 -0.04834 0.75992  0.34396  358 GLU A OE2 
5193 N N   . GLU A 358 ? 2.73776 1.64581 2.48396 -0.16610 0.80997  0.19654  359 GLU A N   
5194 C CA  . GLU A 358 ? 2.74254 1.57802 2.48482 -0.19694 0.82840  0.16179  359 GLU A CA  
5195 C C   . GLU A 358 ? 2.78672 1.63852 2.50590 -0.20781 0.79332  0.12313  359 GLU A C   
5196 O O   . GLU A 358 ? 2.85402 1.68385 2.56896 -0.24666 0.78683  0.08184  359 GLU A O   
5197 C CB  . GLU A 358 ? 2.89906 1.66345 2.64805 -0.17583 0.87637  0.18644  359 GLU A CB  
5198 C CG  . GLU A 358 ? 2.88332 1.61341 2.65828 -0.17359 0.91873  0.21966  359 GLU A CG  
5199 C CD  . GLU A 358 ? 2.99235 1.65227 2.77599 -0.14920 0.96730  0.24698  359 GLU A CD  
5200 O OE1 . GLU A 358 ? 3.14947 1.79162 2.91781 -0.13240 0.96638  0.24049  359 GLU A OE1 
5201 O OE2 . GLU A 358 ? 3.06636 1.68882 2.87308 -0.14643 1.00717  0.27566  359 GLU A OE2 
5208 N N   . ALA A 359 ? 2.78018 1.67318 2.48473 -0.17427 0.77099  0.13595  360 ALA A N   
5209 C CA  . ALA A 359 ? 2.84655 1.75895 2.53001 -0.18279 0.73690  0.10223  360 ALA A CA  
5210 C C   . ALA A 359 ? 2.76459 1.72726 2.44713 -0.21315 0.69821  0.07284  360 ALA A C   
5211 O O   . ALA A 359 ? 2.65898 1.61618 2.33003 -0.24040 0.68022  0.03505  360 ALA A O   
5212 C CB  . ALA A 359 ? 2.87415 1.82706 2.54479 -0.14047 0.72073  0.12388  360 ALA A CB  
5218 N N   . ILE A 360 ? 2.63539 1.65006 2.33061 -0.20825 0.68537  0.09039  361 ILE A N   
5219 C CA  . ILE A 360 ? 2.52049 1.58278 2.21798 -0.23622 0.65113  0.06476  361 ILE A CA  
5220 C C   . ILE A 360 ? 2.53933 1.56056 2.24399 -0.28115 0.66546  0.03598  361 ILE A C   
5221 O O   . ILE A 360 ? 2.51796 1.55552 2.21615 -0.31109 0.64076  0.00067  361 ILE A O   
5222 C CB  . ILE A 360 ? 2.29525 1.42192 2.00655 -0.21941 0.63747  0.09107  361 ILE A CB  
5223 C CG1 . ILE A 360 ? 2.35968 1.54149 2.06261 -0.18164 0.61394  0.10777  361 ILE A CG1 
5224 C CG2 . ILE A 360 ? 2.20414 1.36896 1.92297 -0.25220 0.61120  0.06635  361 ILE A CG2 
5225 C CD1 . ILE A 360 ? 2.37047 1.61523 2.08759 -0.15931 0.60674  0.13741  361 ILE A CD1 
5237 N N   . GLU A 361 ? 2.54716 1.51681 2.26639 -0.28671 0.70638  0.05084  362 GLU A N   
5238 C CA  . GLU A 361 ? 2.54578 1.47556 2.27410 -0.33089 0.72377  0.02244  362 GLU A CA  
5239 C C   . GLU A 361 ? 2.64768 1.53989 2.36130 -0.35564 0.72338  -0.01785 362 GLU A C   
5240 O O   . GLU A 361 ? 2.59710 1.49831 2.30907 -0.39410 0.70929  -0.05466 362 GLU A O   
5241 C CB  . GLU A 361 ? 2.59700 1.47084 2.34492 -0.32874 0.77261  0.04811  362 GLU A CB  
5242 C CG  . GLU A 361 ? 2.83292 1.66605 2.59414 -0.37530 0.79461  0.02005  362 GLU A CG  
5243 C CD  . GLU A 361 ? 2.84420 1.73219 2.61415 -0.39974 0.77007  0.00966  362 GLU A CD  
5244 O OE1 . GLU A 361 ? 2.62281 1.57981 2.38839 -0.38137 0.73446  0.02164  362 GLU A OE1 
5245 O OE2 . GLU A 361 ? 2.63692 1.49968 2.41921 -0.43779 0.78733  -0.01150 362 GLU A OE2 
5252 N N   . ASN A 362 ? 2.56574 1.41946 2.26859 -0.33386 0.73877  -0.01151 363 ASN A N   
5253 C CA  . ASN A 362 ? 2.53636 1.35573 2.22505 -0.35594 0.73963  -0.04942 363 ASN A CA  
5254 C C   . ASN A 362 ? 2.53338 1.41076 2.20565 -0.36931 0.69192  -0.07810 363 ASN A C   
5255 O O   . ASN A 362 ? 2.50466 1.37717 2.17186 -0.40612 0.68484  -0.11701 363 ASN A O   
5256 C CB  . ASN A 362 ? 2.76076 1.53691 2.44033 -0.32493 0.76117  -0.03408 363 ASN A CB  
5257 C CG  . ASN A 362 ? 2.83795 1.58047 2.50263 -0.34653 0.76248  -0.07341 363 ASN A CG  
5258 O OD1 . ASN A 362 ? 2.56587 1.34351 2.21159 -0.34293 0.72949  -0.08880 363 ASN A OD1 
5259 N ND2 . ASN A 362 ? 2.82753 1.50256 2.50195 -0.36960 0.80177  -0.09026 363 ASN A ND2 
5266 N N   . TYR A 363 ? 2.44701 1.38179 2.11196 -0.33964 0.65971  -0.05924 364 TYR A N   
5267 C CA  . TYR A 363 ? 2.34680 1.33757 1.99942 -0.34994 0.61524  -0.08265 364 TYR A CA  
5268 C C   . TYR A 363 ? 2.33467 1.35417 1.99667 -0.38800 0.60034  -0.10623 364 TYR A C   
5269 O O   . TYR A 363 ? 2.16402 1.19597 1.81730 -0.41642 0.58227  -0.14020 364 TYR A O   
5270 C CB  . TYR A 363 ? 2.25604 1.30468 1.90552 -0.31285 0.58693  -0.05680 364 TYR A CB  
5271 C CG  . TYR A 363 ? 2.33334 1.44917 1.98398 -0.32505 0.54509  -0.07103 364 TYR A CG  
5272 C CD1 . TYR A 363 ? 2.35469 1.48960 1.99191 -0.34153 0.51765  -0.10043 364 TYR A CD1 
5273 C CD2 . TYR A 363 ? 2.38842 1.54971 2.05475 -0.31961 0.53395  -0.05426 364 TYR A CD2 
5274 C CE1 . TYR A 363 ? 2.29576 1.49103 1.93629 -0.35111 0.48117  -0.11116 364 TYR A CE1 
5275 C CE2 . TYR A 363 ? 2.20479 1.42607 1.87437 -0.32982 0.49729  -0.06716 364 TYR A CE2 
5276 C CZ  . TYR A 363 ? 2.13122 1.36818 1.78843 -0.34495 0.47146  -0.09480 364 TYR A CZ  
5277 O OH  . TYR A 363 ? 2.04334 1.33929 1.70603 -0.35339 0.43662  -0.10520 364 TYR A OH  
5287 N N   . GLU A 364 ? 2.41640 1.45048 2.09634 -0.38866 0.60770  -0.08785 365 GLU A N   
5288 C CA  . GLU A 364 ? 2.47895 1.54521 2.16869 -0.42315 0.59299  -0.10839 365 GLU A CA  
5289 C C   . GLU A 364 ? 2.43483 1.45651 2.12584 -0.46596 0.61512  -0.14287 365 GLU A C   
5290 O O   . GLU A 364 ? 2.34414 1.39572 2.03369 -0.49854 0.59528  -0.17351 365 GLU A O   
5291 C CB  . GLU A 364 ? 2.28762 1.37495 1.99677 -0.41405 0.60031  -0.08009 365 GLU A CB  
5292 C CG  . GLU A 364 ? 2.18458 1.32774 1.89425 -0.37556 0.57570  -0.05073 365 GLU A CG  
5293 C CD  . GLU A 364 ? 2.19599 1.36516 1.92489 -0.36723 0.58277  -0.02365 365 GLU A CD  
5294 O OE1 . GLU A 364 ? 2.40275 1.54192 2.14459 -0.38988 0.60873  -0.02477 365 GLU A OE1 
5295 O OE2 . GLU A 364 ? 2.14377 1.36497 1.87557 -0.33870 0.56300  -0.00210 365 GLU A OE2 
5302 N N   . GLN A 365 ? 2.46943 1.42151 2.16439 -0.46657 0.65719  -0.13896 366 GLN A N   
5303 C CA  . GLN A 365 ? 2.51472 1.42159 2.21142 -0.50751 0.68092  -0.17552 366 GLN A CA  
5304 C C   . GLN A 365 ? 2.50730 1.43016 2.18426 -0.52378 0.65712  -0.21130 366 GLN A C   
5305 O O   . GLN A 365 ? 2.39293 1.33416 2.06923 -0.56266 0.64755  -0.24691 366 GLN A O   
5306 C CB  . GLN A 365 ? 2.47637 1.30287 2.18136 -0.49950 0.73102  -0.16324 366 GLN A CB  
5307 C CG  . GLN A 365 ? 2.89480 1.69618 2.62342 -0.49881 0.76300  -0.13719 366 GLN A CG  
5308 C CD  . GLN A 365 ? 2.98910 1.71633 2.72676 -0.47787 0.81054  -0.11301 366 GLN A CD  
5309 O OE1 . GLN A 365 ? 2.92392 1.61435 2.65054 -0.46767 0.82162  -0.12033 366 GLN A OE1 
5310 N NE2 . GLN A 365 ? 2.87184 1.57792 2.63052 -0.47041 0.83950  -0.08264 366 GLN A NE2 
5319 N N   . GLN A 366 ? 2.51839 1.43821 2.17915 -0.49424 0.64735  -0.20177 367 GLN A N   
5320 C CA  . GLN A 366 ? 2.38664 1.32414 2.02817 -0.50676 0.62423  -0.23237 367 GLN A CA  
5321 C C   . GLN A 366 ? 2.30659 1.32036 1.94388 -0.51692 0.57853  -0.24311 367 GLN A C   
5322 O O   . GLN A 366 ? 2.22983 1.26521 1.85945 -0.54749 0.56361  -0.27692 367 GLN A O   
5323 C CB  . GLN A 366 ? 2.40144 1.32356 2.02746 -0.46994 0.62238  -0.21594 367 GLN A CB  
5324 C CG  . GLN A 366 ? 2.52484 1.37124 2.15313 -0.46029 0.66683  -0.20942 367 GLN A CG  
5325 C CD  . GLN A 366 ? 2.59683 1.43367 2.20813 -0.42604 0.66242  -0.19680 367 GLN A CD  
5326 O OE1 . GLN A 366 ? 2.27005 1.12801 1.86398 -0.43193 0.63918  -0.21844 367 GLN A OE1 
5327 N NE2 . GLN A 366 ? 2.74989 1.55797 2.36638 -0.38960 0.68486  -0.16059 367 GLN A NE2 
5336 N N   . MET A 367 ? 2.32269 1.38035 1.96596 -0.49109 0.55658  -0.21449 368 MET A N   
5337 C CA  . MET A 367 ? 2.38306 1.51220 2.02422 -0.49551 0.51348  -0.22156 368 MET A CA  
5338 C C   . MET A 367 ? 2.25913 1.41264 1.91012 -0.53678 0.50871  -0.24712 368 MET A C   
5339 O O   . MET A 367 ? 1.93819 1.13712 1.58295 -0.55508 0.48021  -0.26915 368 MET A O   
5340 C CB  . MET A 367 ? 2.34246 1.51039 1.99158 -0.45997 0.49584  -0.18678 368 MET A CB  
5341 C CG  . MET A 367 ? 2.30999 1.55033 1.96168 -0.46219 0.45374  -0.19158 368 MET A CG  
5342 S SD  . MET A 367 ? 2.06643 1.34331 1.73913 -0.48774 0.44879  -0.19505 368 MET A SD  
5343 C CE  . MET A 367 ? 2.36607 1.63434 2.05375 -0.45447 0.46739  -0.15371 368 MET A CE  
5353 N N   . PHE A 368 ? 2.27764 1.40352 1.94464 -0.55174 0.53699  -0.24374 369 PHE A N   
5354 C CA  . PHE A 368 ? 2.35049 1.50054 2.02780 -0.59193 0.53437  -0.26836 369 PHE A CA  
5355 C C   . PHE A 368 ? 2.09826 1.24351 1.76507 -0.62907 0.53557  -0.31065 369 PHE A C   
5356 O O   . PHE A 368 ? 2.02591 1.21993 1.69369 -0.65727 0.51459  -0.33395 369 PHE A O   
5357 C CB  . PHE A 368 ? 2.56388 1.67510 2.26024 -0.60232 0.57053  -0.25801 369 PHE A CB  
5358 C CG  . PHE A 368 ? 2.21380 1.36883 1.92541 -0.59328 0.55667  -0.23521 369 PHE A CG  
5359 C CD1 . PHE A 368 ? 2.15030 1.32068 1.86450 -0.55154 0.54792  -0.19737 369 PHE A CD1 
5360 C CD2 . PHE A 368 ? 2.19964 1.38395 1.92335 -0.62714 0.55276  -0.25287 369 PHE A CD2 
5361 C CE1 . PHE A 368 ? 2.34904 1.56283 2.07791 -0.54380 0.53553  -0.17810 369 PHE A CE1 
5362 C CE2 . PHE A 368 ? 2.34059 1.56649 2.07863 -0.61892 0.54014  -0.23261 369 PHE A CE2 
5363 C CZ  . PHE A 368 ? 2.37560 1.61601 2.11639 -0.57725 0.53158  -0.19543 369 PHE A CZ  
5373 N N   . ALA A 369 ? 2.17704 1.26767 1.83415 -0.62927 0.55999  -0.32126 370 ALA A N   
5374 C CA  . ALA A 369 ? 2.33977 1.42433 1.98815 -0.66651 0.56560  -0.36381 370 ALA A CA  
5375 C C   . ALA A 369 ? 2.25726 1.40341 1.88910 -0.66736 0.52395  -0.37738 370 ALA A C   
5376 O O   . ALA A 369 ? 2.13314 1.32918 1.76561 -0.69748 0.50529  -0.40178 370 ALA A O   
5377 C CB  . ALA A 369 ? 2.33229 1.34275 1.97564 -0.66339 0.60272  -0.37058 370 ALA A CB  
5383 N N   . TYR A 370 ? 2.26423 1.40977 1.88181 -0.63409 0.50945  -0.36079 371 TYR A N   
5384 C CA  . TYR A 370 ? 2.28452 1.48332 1.88687 -0.63446 0.47306  -0.37265 371 TYR A CA  
5385 C C   . TYR A 370 ? 2.21345 1.48186 1.82246 -0.62481 0.43505  -0.35749 371 TYR A C   
5386 O O   . TYR A 370 ? 1.95013 1.27260 1.55264 -0.63671 0.40588  -0.37190 371 TYR A O   
5387 C CB  . TYR A 370 ? 2.42910 1.60493 2.01506 -0.60269 0.47054  -0.36004 371 TYR A CB  
5388 C CG  . TYR A 370 ? 2.39700 1.56751 1.98613 -0.55742 0.46515  -0.31938 371 TYR A CG  
5389 C CD1 . TYR A 370 ? 2.26714 1.49472 1.85857 -0.53710 0.42948  -0.30087 371 TYR A CD1 
5390 C CD2 . TYR A 370 ? 2.44735 1.55824 2.03816 -0.53473 0.49658  -0.29999 371 TYR A CD2 
5391 C CE1 . TYR A 370 ? 2.25061 1.47827 1.84576 -0.49761 0.42515  -0.26702 371 TYR A CE1 
5392 C CE2 . TYR A 370 ? 2.32991 1.44335 1.92330 -0.49369 0.49162  -0.26354 371 TYR A CE2 
5393 C CZ  . TYR A 370 ? 2.20126 1.37435 1.79659 -0.47625 0.45570  -0.24863 371 TYR A CZ  
5394 O OH  . TYR A 370 ? 2.15143 1.33185 1.75028 -0.43722 0.45131  -0.21544 371 TYR A OH  
5404 N N   . GLY A 371 ? 2.34124 1.61130 1.96415 -0.60283 0.43544  -0.32813 372 GLY A N   
5405 C CA  . GLY A 371 ? 2.26956 1.60446 1.90175 -0.59476 0.40183  -0.31555 372 GLY A CA  
5406 C C   . GLY A 371 ? 2.14679 1.52128 1.78845 -0.63274 0.39457  -0.33867 372 GLY A C   
5407 O O   . GLY A 371 ? 2.02955 1.46551 1.67150 -0.63806 0.36246  -0.34432 372 GLY A O   
5411 N N   . ARG A 372 ? 2.16106 1.50187 1.81178 -0.65941 0.42522  -0.35179 373 ARG A N   
5412 C CA  . ARG A 372 ? 2.25933 1.63692 1.91821 -0.69960 0.42143  -0.37825 373 ARG A CA  
5413 C C   . ARG A 372 ? 2.06108 1.47260 1.70608 -0.72483 0.40575  -0.41035 373 ARG A C   
5414 O O   . ARG A 372 ? 1.91260 1.38777 1.56076 -0.74316 0.38123  -0.42282 373 ARG A O   
5415 C CB  . ARG A 372 ? 2.16322 1.48986 1.83363 -0.72560 0.46214  -0.38996 373 ARG A CB  
5416 C CG  . ARG A 372 ? 2.30025 1.62195 1.98913 -0.71272 0.47088  -0.36260 373 ARG A CG  
5417 C CD  . ARG A 372 ? 2.52733 1.78489 2.22775 -0.73119 0.51642  -0.36750 373 ARG A CD  
5418 N NE  . ARG A 372 ? 2.67540 1.93992 2.38074 -0.78039 0.52889  -0.40666 373 ARG A NE  
5419 C CZ  . ARG A 372 ? 2.85415 2.16781 2.57084 -0.80479 0.51697  -0.41707 373 ARG A CZ  
5420 N NH1 . ARG A 372 ? 2.55924 1.92049 2.28371 -0.78499 0.49085  -0.39220 373 ARG A NH1 
5421 N NH2 . ARG A 372 ? 2.62038 1.93771 2.34141 -0.85073 0.53207  -0.45477 373 ARG A NH2 
5435 N N   . GLU A 373 ? 2.12525 1.49839 1.75512 -0.72544 0.41967  -0.42336 374 GLU A N   
5436 C CA  . GLU A 373 ? 2.20153 1.60981 1.81720 -0.74800 0.40506  -0.45301 374 GLU A CA  
5437 C C   . GLU A 373 ? 1.98807 1.46209 1.59791 -0.72743 0.36184  -0.43832 374 GLU A C   
5438 O O   . GLU A 373 ? 1.88678 1.42264 1.49515 -0.74862 0.33985  -0.45540 374 GLU A O   
5439 C CB  . GLU A 373 ? 2.32888 1.68180 1.92979 -0.74737 0.42813  -0.46636 374 GLU A CB  
5440 C CG  . GLU A 373 ? 2.46130 1.85030 2.04687 -0.77176 0.41574  -0.49853 374 GLU A CG  
5441 C CD  . GLU A 373 ? 2.68183 2.01555 2.25380 -0.77164 0.44002  -0.51324 374 GLU A CD  
5442 O OE1 . GLU A 373 ? 2.75494 2.03659 2.32421 -0.73851 0.45216  -0.48868 374 GLU A OE1 
5443 O OE2 . GLU A 373 ? 2.78714 2.13249 2.35161 -0.80479 0.44731  -0.55001 374 GLU A OE2 
5450 N N   . ALA A 374 ? 1.93327 1.39635 1.54097 -0.68586 0.35024  -0.40630 375 ALA A N   
5451 C CA  . ALA A 374 ? 1.92430 1.44471 1.52970 -0.66460 0.31174  -0.39091 375 ALA A CA  
5452 C C   . ALA A 374 ? 2.00616 1.58927 1.62765 -0.67394 0.28923  -0.38782 375 ALA A C   
5453 O O   . ALA A 374 ? 1.79004 1.43356 1.41015 -0.67976 0.26123  -0.39306 375 ALA A O   
5454 C CB  . ALA A 374 ? 2.28268 1.77905 1.88721 -0.61980 0.30709  -0.35788 375 ALA A CB  
5460 N N   . GLN A 375 ? 2.08583 1.65723 1.72342 -0.67483 0.30155  -0.37816 376 GLN A N   
5461 C CA  . GLN A 375 ? 1.98717 1.61745 1.64089 -0.68488 0.28203  -0.37649 376 GLN A CA  
5462 C C   . GLN A 375 ? 2.02451 1.69778 1.67581 -0.72627 0.27739  -0.40896 376 GLN A C   
5463 O O   . GLN A 375 ? 1.82859 1.56939 1.48538 -0.73044 0.24905  -0.40943 376 GLN A O   
5464 C CB  . GLN A 375 ? 1.97136 1.57739 1.64165 -0.68314 0.30089  -0.36374 376 GLN A CB  
5465 C CG  . GLN A 375 ? 2.00015 1.58108 1.67567 -0.64135 0.30161  -0.32960 376 GLN A CG  
5466 C CD  . GLN A 375 ? 1.77064 1.35187 1.46518 -0.63824 0.31103  -0.31421 376 GLN A CD  
5467 O OE1 . GLN A 375 ? 1.84290 1.40562 1.54385 -0.66542 0.33372  -0.32700 376 GLN A OE1 
5468 N NE2 . GLN A 375 ? 1.78389 1.38802 1.48850 -0.60581 0.29422  -0.28750 376 GLN A NE2 
5477 N N   . ALA A 376 ? 2.04755 1.68458 1.69184 -0.75718 0.30595  -0.43677 377 ALA A N   
5478 C CA  . ALA A 376 ? 1.87593 1.55611 1.51789 -0.79942 0.30432  -0.47148 377 ALA A CA  
5479 C C   . ALA A 376 ? 1.92213 1.66026 1.55176 -0.79754 0.27419  -0.47678 377 ALA A C   
5480 O O   . ALA A 376 ? 1.88968 1.69889 1.52382 -0.81418 0.25258  -0.48584 377 ALA A O   
5481 C CB  . ALA A 376 ? 1.95113 1.57619 1.58735 -0.83034 0.34247  -0.50201 377 ALA A CB  
5487 N N   . GLU A 377 ? 1.92527 1.63596 1.53968 -0.77675 0.27281  -0.46996 378 GLU A N   
5488 C CA  . GLU A 377 ? 1.95256 1.71576 1.55510 -0.77361 0.24574  -0.47268 378 GLU A CA  
5489 C C   . GLU A 377 ? 1.93803 1.76278 1.55195 -0.75058 0.21018  -0.44641 378 GLU A C   
5490 O O   . GLU A 377 ? 1.84762 1.74180 1.46161 -0.76258 0.18745  -0.45319 378 GLU A O   
5491 C CB  . GLU A 377 ? 2.12629 1.84386 1.71182 -0.75155 0.25162  -0.46622 378 GLU A CB  
5492 C CG  . GLU A 377 ? 2.41702 2.18463 1.98932 -0.74847 0.22630  -0.46856 378 GLU A CG  
5493 C CD  . GLU A 377 ? 2.69200 2.41345 2.24719 -0.72819 0.23360  -0.46365 378 GLU A CD  
5494 O OE1 . GLU A 377 ? 2.90780 2.55932 2.46184 -0.71460 0.25780  -0.45713 378 GLU A OE1 
5495 O OE2 . GLU A 377 ? 2.64847 2.40550 2.19168 -0.72529 0.21547  -0.46522 378 GLU A OE2 
5502 N N   . SER A 378 ? 2.12426 1.92665 1.74923 -0.71699 0.20584  -0.41615 379 SER A N   
5503 C CA  . SER A 378 ? 1.85096 1.70662 1.48912 -0.69281 0.17407  -0.39154 379 SER A CA  
5504 C C   . SER A 378 ? 1.78517 1.70094 1.43914 -0.71417 0.16253  -0.39874 379 SER A C   
5505 O O   . SER A 378 ? 1.72022 1.70097 1.38101 -0.70962 0.13500  -0.39135 379 SER A O   
5506 C CB  . SER A 378 ? 1.71551 1.53461 1.36333 -0.65508 0.17523  -0.36172 379 SER A CB  
5507 O OG  . SER A 378 ? 2.12471 1.92444 1.78604 -0.66132 0.19145  -0.35969 379 SER A OG  
5513 N N   . ILE A 379 ? 1.91632 1.81204 1.57739 -0.73691 0.18396  -0.41199 380 ILE A N   
5514 C CA  . ILE A 379 ? 2.02908 1.98244 1.70456 -0.76001 0.17476  -0.42136 380 ILE A CA  
5515 C C   . ILE A 379 ? 1.97061 1.97753 1.63663 -0.79433 0.16835  -0.44998 380 ILE A C   
5516 O O   . ILE A 379 ? 1.83973 1.92083 1.51367 -0.79938 0.14403  -0.44855 380 ILE A O   
5517 C CB  . ILE A 379 ? 1.75785 1.67365 1.44350 -0.77651 0.20146  -0.42831 380 ILE A CB  
5518 C CG1 . ILE A 379 ? 2.21580 2.09502 1.91309 -0.74132 0.20416  -0.39723 380 ILE A CG1 
5519 C CG2 . ILE A 379 ? 1.72698 1.70446 1.42582 -0.80476 0.19327  -0.44222 380 ILE A CG2 
5520 C CD1 . ILE A 379 ? 2.31350 2.24924 2.02986 -0.72197 0.17624  -0.37626 380 ILE A CD1 
5532 N N   . ILE A 380 ? 1.91011 1.88331 1.55998 -0.81819 0.19067  -0.47656 381 ILE A N   
5533 C CA  . ILE A 380 ? 2.07212 2.09954 1.71237 -0.85270 0.18631  -0.50686 381 ILE A CA  
5534 C C   . ILE A 380 ? 1.94655 2.03568 1.58147 -0.83444 0.15337  -0.49207 381 ILE A C   
5535 O O   . ILE A 380 ? 1.87659 2.04462 1.51499 -0.85039 0.13454  -0.49962 381 ILE A O   
5536 C CB  . ILE A 380 ? 2.25281 2.22804 1.87715 -0.87767 0.21704  -0.53771 381 ILE A CB  
5537 C CG1 . ILE A 380 ? 1.97262 1.89382 1.60591 -0.90096 0.25153  -0.55451 381 ILE A CG1 
5538 C CG2 . ILE A 380 ? 1.97742 2.01558 1.59051 -0.91083 0.21029  -0.56908 381 ILE A CG2 
5539 C CD1 . ILE A 380 ? 2.00206 1.85121 1.62387 -0.91626 0.28660  -0.57791 381 ILE A CD1 
5551 N N   . ASN A 381 ? 1.98762 2.04329 1.61483 -0.80035 0.14670  -0.46976 382 ASN A N   
5552 C CA  . ASN A 381 ? 2.09792 2.20704 1.72223 -0.78034 0.11686  -0.45214 382 ASN A CA  
5553 C C   . ASN A 381 ? 1.94683 2.11234 1.59234 -0.76239 0.09049  -0.42734 382 ASN A C   
5554 O O   . ASN A 381 ? 1.67870 1.91519 1.32710 -0.76113 0.06655  -0.42084 382 ASN A O   
5555 C CB  . ASN A 381 ? 2.00774 2.06457 1.62148 -0.74710 0.11722  -0.43301 382 ASN A CB  
5556 C CG  . ASN A 381 ? 2.28834 2.31640 1.87938 -0.76346 0.13372  -0.45652 382 ASN A CG  
5557 O OD1 . ASN A 381 ? 2.55316 2.50806 2.13610 -0.75917 0.15781  -0.46125 382 ASN A OD1 
5558 N ND2 . ASN A 381 ? 2.45192 2.54038 2.03322 -0.78191 0.12129  -0.47108 382 ASN A ND2 
5565 N N   . GLU A 382 ? 1.85571 1.99230 1.51733 -0.74740 0.09507  -0.41235 383 GLU A N   
5566 C CA  . GLU A 382 ? 1.85092 2.03967 1.53498 -0.73228 0.07251  -0.39176 383 GLU A CA  
5567 C C   . GLU A 382 ? 1.87792 2.14194 1.56781 -0.76432 0.06403  -0.40982 383 GLU A C   
5568 O O   . GLU A 382 ? 1.81210 2.14659 1.50994 -0.75778 0.03908  -0.39866 383 GLU A O   
5569 C CB  . GLU A 382 ? 1.86088 2.00524 1.55988 -0.71642 0.08314  -0.37813 383 GLU A CB  
5570 C CG  . GLU A 382 ? 1.83456 2.02856 1.55858 -0.70144 0.06261  -0.35913 383 GLU A CG  
5571 C CD  . GLU A 382 ? 1.89534 2.04867 1.63289 -0.69002 0.07544  -0.34919 383 GLU A CD  
5572 O OE1 . GLU A 382 ? 2.03456 2.16015 1.76923 -0.71478 0.09802  -0.36642 383 GLU A OE1 
5573 O OE2 . GLU A 382 ? 1.81108 1.96105 1.56292 -0.65675 0.06408  -0.32453 383 GLU A OE2 
5580 N N   . THR A 383 ? 1.87054 2.12165 1.55751 -0.79945 0.08584  -0.43776 384 THR A N   
5581 C CA  . THR A 383 ? 1.86410 2.18774 1.55568 -0.83377 0.08039  -0.45916 384 THR A CA  
5582 C C   . THR A 383 ? 1.76589 2.15124 1.44422 -0.84674 0.06647  -0.47037 384 THR A C   
5583 O O   . THR A 383 ? 1.71369 2.18313 1.39992 -0.85480 0.04643  -0.46940 384 THR A O   
5584 C CB  . THR A 383 ? 1.73782 2.02695 1.42649 -0.87177 0.11102  -0.49121 384 THR A CB  
5585 O OG1 . THR A 383 ? 2.08822 2.31932 1.78897 -0.85761 0.12494  -0.47742 384 THR A OG1 
5586 C CG2 . THR A 383 ? 1.80464 2.17103 1.49999 -0.90810 0.10607  -0.51437 384 THR A CG2 
5594 N N   . GLU A 384 ? 1.81950 2.16711 1.47794 -0.84787 0.07688  -0.47996 385 GLU A N   
5595 C CA  . GLU A 384 ? 1.76889 2.17444 1.41307 -0.86191 0.06591  -0.49241 385 GLU A CA  
5596 C C   . GLU A 384 ? 1.81759 2.27695 1.46856 -0.82894 0.03408  -0.45845 385 GLU A C   
5597 O O   . GLU A 384 ? 1.81959 2.36242 1.46992 -0.83967 0.01677  -0.46074 385 GLU A O   
5598 C CB  . GLU A 384 ? 1.79425 2.13985 1.41647 -0.86946 0.08659  -0.51066 385 GLU A CB  
5599 C CG  . GLU A 384 ? 1.88436 2.28232 1.49013 -0.87828 0.07534  -0.52010 385 GLU A CG  
5600 C CD  . GLU A 384 ? 1.94882 2.28691 1.53392 -0.89090 0.09930  -0.54405 385 GLU A CD  
5601 O OE1 . GLU A 384 ? 1.91149 2.16827 1.49631 -0.89364 0.12557  -0.55324 385 GLU A OE1 
5602 O OE2 . GLU A 384 ? 2.40682 2.78000 1.97681 -0.89736 0.09251  -0.55278 385 GLU A OE2 
5609 N N   . MET A 385 ? 1.84865 2.26366 1.50757 -0.78873 0.02695  -0.42648 386 MET A N   
5610 C CA  . MET A 385 ? 1.96739 2.42368 1.63417 -0.75638 0.00007  -0.39425 386 MET A CA  
5611 C C   . MET A 385 ? 1.85719 2.38761 1.54756 -0.75058 -0.02122 -0.37810 386 MET A C   
5612 O O   . MET A 385 ? 1.60320 2.20607 1.29763 -0.74518 -0.04192 -0.36536 386 MET A O   
5613 C CB  . MET A 385 ? 1.90975 2.29635 1.57976 -0.71724 0.00097  -0.36825 386 MET A CB  
5614 C CG  . MET A 385 ? 2.04625 2.39355 1.69421 -0.71089 0.00777  -0.37099 386 MET A CG  
5615 S SD  . MET A 385 ? 1.74905 1.99592 1.39529 -0.67781 0.02184  -0.35490 386 MET A SD  
5616 C CE  . MET A 385 ? 2.00812 2.28118 1.68123 -0.63536 -0.00397 -0.31451 386 MET A CE  
5626 N N   . PHE A 386 ? 1.97455 2.49025 1.68130 -0.75109 -0.01601 -0.37742 387 PHE A N   
5627 C CA  . PHE A 386 ? 2.08318 2.66420 1.81422 -0.74380 -0.03486 -0.36202 387 PHE A CA  
5628 C C   . PHE A 386 ? 2.07444 2.72628 1.80481 -0.78248 -0.03492 -0.38728 387 PHE A C   
5629 O O   . PHE A 386 ? 2.08554 2.79033 1.83579 -0.78128 -0.04724 -0.37896 387 PHE A O   
5630 C CB  . PHE A 386 ? 1.78825 2.32372 1.53829 -0.72434 -0.03014 -0.34849 387 PHE A CB  
5631 C CG  . PHE A 386 ? 1.77078 2.25086 1.52571 -0.68456 -0.03291 -0.32231 387 PHE A CG  
5632 C CD1 . PHE A 386 ? 1.73243 2.24547 1.50675 -0.65184 -0.05484 -0.29231 387 PHE A CD1 
5633 C CD2 . PHE A 386 ? 1.76626 2.16288 1.50757 -0.67993 -0.01249 -0.32792 387 PHE A CD2 
5634 C CE1 . PHE A 386 ? 1.63710 2.10117 1.41716 -0.61720 -0.05623 -0.27095 387 PHE A CE1 
5635 C CE2 . PHE A 386 ? 1.90707 2.25813 1.65270 -0.64422 -0.01493 -0.30523 387 PHE A CE2 
5636 C CZ  . PHE A 386 ? 1.62413 2.00922 1.38908 -0.61384 -0.03679 -0.27803 387 PHE A CZ  
5646 N N   . SER A 387 ? 1.85171 2.50803 1.56060 -0.81703 -0.02100 -0.41911 388 SER A N   
5647 C CA  . SER A 387 ? 1.98531 2.72056 1.69290 -0.85474 -0.02248 -0.44468 388 SER A CA  
5648 C C   . SER A 387 ? 2.15614 2.98831 1.86797 -0.84511 -0.04944 -0.42695 388 SER A C   
5649 O O   . SER A 387 ? 2.08486 2.91589 1.79445 -0.81642 -0.06227 -0.40186 388 SER A O   
5650 C CB  . SER A 387 ? 2.16768 2.88013 1.85258 -0.89517 0.00189  -0.48634 388 SER A CB  
5651 O OG  . SER A 387 ? 2.27860 3.06874 1.96351 -0.93453 0.00238  -0.51482 388 SER A OG  
5657 N N   . SER A 388 ? 2.27054 3.18970 1.98931 -0.86941 -0.05735 -0.43939 389 SER A N   
5658 C CA  . SER A 388 ? 2.12887 3.14872 1.85501 -0.85878 -0.08306 -0.41909 389 SER A CA  
5659 C C   . SER A 388 ? 2.00122 3.05531 1.70559 -0.86950 -0.08524 -0.42815 389 SER A C   
5660 O O   . SER A 388 ? 1.99953 3.11645 1.70863 -0.84873 -0.10618 -0.40102 389 SER A O   
5661 C CB  . SER A 388 ? 2.16932 3.27791 1.90754 -0.88389 -0.08968 -0.43207 389 SER A CB  
5662 O OG  . SER A 388 ? 2.03491 3.11860 1.79440 -0.87279 -0.08930 -0.42202 389 SER A OG  
5668 N N   . ASP A 389 ? 2.00379 3.01898 1.68576 -0.90090 -0.06332 -0.46496 390 ASP A N   
5669 C CA  . ASP A 389 ? 2.07578 3.12500 1.73738 -0.91309 -0.06170 -0.47762 390 ASP A CA  
5670 C C   . ASP A 389 ? 2.11254 3.09057 1.75941 -0.89231 -0.05892 -0.46675 390 ASP A C   
5671 O O   . ASP A 389 ? 2.04458 3.04812 1.67310 -0.90278 -0.05873 -0.47763 390 ASP A O   
5672 C CB  . ASP A 389 ? 2.20622 3.24835 1.85759 -0.94687 -0.03158 -0.51773 390 ASP A CB  
5673 C CG  . ASP A 389 ? 2.41605 3.51649 2.05267 -0.95779 -0.02919 -0.52907 390 ASP A CG  
5674 O OD1 . ASP A 389 ? 2.64668 3.81066 2.28297 -0.93962 -0.05283 -0.50318 390 ASP A OD1 
5675 O OD2 . ASP A 389 ? 2.38583 3.46981 2.01266 -0.98434 -0.00280 -0.56338 390 ASP A OD2 
5680 N N   . PHE A 390 ? 2.17613 3.06722 1.83147 -0.86036 -0.05553 -0.44403 391 PHE A N   
5681 C CA  . PHE A 390 ? 2.05962 2.87277 1.70090 -0.84058 -0.04758 -0.43632 391 PHE A CA  
5682 C C   . PHE A 390 ? 1.92780 2.78695 1.56627 -0.81550 -0.06849 -0.40737 391 PHE A C   
5683 O O   . PHE A 390 ? 1.82407 2.74315 1.48064 -0.79312 -0.09060 -0.37580 391 PHE A O   
5684 C CB  . PHE A 390 ? 2.06775 2.78956 1.72108 -0.81028 -0.04117 -0.41617 391 PHE A CB  
5685 C CG  . PHE A 390 ? 2.00651 2.64695 1.64577 -0.79020 -0.03151 -0.40932 391 PHE A CG  
5686 C CD1 . PHE A 390 ? 2.07110 2.65150 1.69006 -0.81291 -0.00626 -0.44067 391 PHE A CD1 
5687 C CD2 . PHE A 390 ? 1.98374 2.60798 1.63140 -0.74883 -0.04650 -0.37215 391 PHE A CD2 
5688 C CE1 . PHE A 390 ? 2.01295 2.52105 1.61902 -0.79369 0.00276  -0.43401 391 PHE A CE1 
5689 C CE2 . PHE A 390 ? 1.97242 2.52515 1.60695 -0.73101 -0.03757 -0.36669 391 PHE A CE2 
5690 C CZ  . PHE A 390 ? 2.02968 2.52541 1.64278 -0.75292 -0.01346 -0.39710 391 PHE A CZ  
5700 N N   . SER A 391 ? 1.96238 2.79163 1.57897 -0.81872 -0.06023 -0.41757 392 SER A N   
5701 C CA  . SER A 391 ? 2.00947 2.87921 1.62092 -0.79745 -0.07758 -0.39201 392 SER A CA  
5702 C C   . SER A 391 ? 2.10148 2.89262 1.69385 -0.78693 -0.06531 -0.39489 392 SER A C   
5703 O O   . SER A 391 ? 2.21297 3.03592 1.79002 -0.78872 -0.07032 -0.39466 392 SER A O   
5704 C CB  . SER A 391 ? 1.95050 2.92955 1.55275 -0.82494 -0.08682 -0.40665 392 SER A CB  
5705 O OG  . SER A 391 ? 2.04997 3.07168 1.64848 -0.80294 -0.10366 -0.37833 392 SER A OG  
5711 N N   . PHE A 392 ? 2.00072 2.69375 1.59394 -0.77550 -0.04940 -0.39674 393 PHE A N   
5712 C CA  . PHE A 392 ? 1.89194 2.50654 1.46816 -0.76363 -0.03653 -0.39874 393 PHE A CA  
5713 C C   . PHE A 392 ? 2.01388 2.64475 1.56429 -0.79459 -0.02498 -0.43216 393 PHE A C   
5714 O O   . PHE A 392 ? 1.95774 2.51770 1.49213 -0.79793 -0.00595 -0.44877 393 PHE A O   
5715 C CB  . PHE A 392 ? 1.71227 2.32073 1.29603 -0.72123 -0.05415 -0.35699 393 PHE A CB  
5716 C CG  . PHE A 392 ? 1.97180 2.53322 1.57830 -0.68839 -0.05819 -0.32927 393 PHE A CG  
5717 C CD1 . PHE A 392 ? 2.26058 2.73010 1.86457 -0.68042 -0.03987 -0.33573 393 PHE A CD1 
5718 C CD2 . PHE A 392 ? 2.18277 2.79406 1.81425 -0.66493 -0.07944 -0.29663 393 PHE A CD2 
5719 C CE1 . PHE A 392 ? 1.98219 2.41440 1.60714 -0.65108 -0.04336 -0.31189 393 PHE A CE1 
5720 C CE2 . PHE A 392 ? 2.10321 2.67312 1.75703 -0.63582 -0.08217 -0.27407 393 PHE A CE2 
5721 C CZ  . PHE A 392 ? 1.72004 2.20230 1.37001 -0.62955 -0.06447 -0.28254 393 PHE A CZ  
# 
