data_9AUY
# 
_entry.id   9AUY 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.400 
_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   9AUY         pdb_00009auy 10.2210/pdb9auy/pdb 
WWPDB D_1000282049 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-15 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9AUY 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-01 
_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           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              sethh@gene.com 
_pdbx_contact_author.name_first         Seth 
_pdbx_contact_author.name_last          Harris 
_pdbx_contact_author.name_mi            F 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-1728-9771 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Harris, S.F.' 1 0000-0003-1728-9771 
'Wu, P.'       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            Mbio 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2150-7511 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                e0089724 
_citation.page_last                 e0089724 
_citation.title                     'Discovery of GuaB inhibitors with efficacy against Acinetobacter baumannii infection.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1128/mbio.00897-24 
_citation.pdbx_database_id_PubMed   39207111 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kofoed, E.M.'    1  0000-0002-1779-4914 
primary 'Aliagas, I.'     2  ?                   
primary 'Crawford, T.'    3  ?                   
primary 'Mao, J.'         4  ?                   
primary 'Harris, S.F.'    5  ?                   
primary 'Xu, M.'          6  ?                   
primary 'Wang, S.'        7  ?                   
primary 'Wu, P.'          8  ?                   
primary 'Ma, F.'          9  ?                   
primary 'Clark, K.'       10 ?                   
primary 'Sims, J.'        11 ?                   
primary 'Xu, Y.'          12 ?                   
primary 'Peng, Y.'        13 0000-0002-8663-7330 
primary 'Skippington, E.' 14 ?                   
primary 'Yang, Y.'        15 ?                   
primary 'Reeder, J.'      16 ?                   
primary 'Ubhayakar, S.'   17 ?                   
primary 'Baumgardner, M.' 18 ?                   
primary 'Yan, Z.'         19 ?                   
primary 'Chen, J.'        20 ?                   
primary 'Park, S.'        21 ?                   
primary 'Zhang, H.'       22 ?                   
primary 'Yen, C.-W.'      23 ?                   
primary 'Lorenzo, M.'     24 ?                   
primary 'Skelton, N.'     25 ?                   
primary 'Liang, X.'       26 ?                   
primary 'Chen, L.'        27 ?                   
primary 'Hoag, B.'        28 ?                   
primary 'Li, C.S.'        29 ?                   
primary 'Liu, Z.'         30 ?                   
primary 'Wai, J.'         31 ?                   
primary 'Liu, X.'         32 ?                   
primary 'Liang, J.'       33 ?                   
primary 'Tan, M.W.'       34 0000-0002-7748-212X 
# 
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 
;Inosine-5'-monophosphate dehydrogenase
;
40598.129 1  1.1.1.205 ? ? ? 
2 non-polymer syn 'INOSINIC ACID'                                                                           348.206   1  ?         
? ? ? 
3 non-polymer syn 'N-(6-chloropyridin-3-yl)-N~2~-(1,4-dihydro-2H-pyrano[3,4-c]quinolin-9-yl)-L-alaninamide' 382.843   1  ?         
? ? ? 
4 water       nat water                                                                                     18.015    82 ?         
? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'IMP dehydrogenase,IMPD,IMPDH' 
# 
_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       
;MHHHHHHGENLYFQGSWESKFAKESLTFDDVLLIPAQSDILPKDVDLSVQLSDKVKLNIPVISAGMDTVTESKMAIAMAR
QGGLGVIHKNMGVEEQADEVQKVKRSGGLLVAAAIGISKDTDIRAQKLVEAGVDVLVIDTAHGHSKGVIDQVKHIKKTYP
EITLVAGNVATAEATKDLFEAGADIVKVGIGPGSICTTRVVAGVGVPQITAIYDCATEARKHGKAIIADGGIKFSGDIIK
ALAAGGHAVMLGSLLAGTEESPGATEIFQGRQYKVYRGMGSLGAMEKGSNDRYFQEDKAPKKFVPEGIEGRTAYKGALQD
TIYQLMGGVRAGMGYTGSHDLRELREEAQFTRMGPAGLAESHPHNIQITKESPNYSFGNS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MHHHHHHGENLYFQGSWESKFAKESLTFDDVLLIPAQSDILPKDVDLSVQLSDKVKLNIPVISAGMDTVTESKMAIAMAR
QGGLGVIHKNMGVEEQADEVQKVKRSGGLLVAAAIGISKDTDIRAQKLVEAGVDVLVIDTAHGHSKGVIDQVKHIKKTYP
EITLVAGNVATAEATKDLFEAGADIVKVGIGPGSICTTRVVAGVGVPQITAIYDCATEARKHGKAIIADGGIKFSGDIIK
ALAAGGHAVMLGSLLAGTEESPGATEIFQGRQYKVYRGMGSLGAMEKGSNDRYFQEDKAPKKFVPEGIEGRTAYKGALQD
TIYQLMGGVRAGMGYTGSHDLRELREEAQFTRMGPAGLAESHPHNIQITKESPNYSFGNS
;
_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 'INOSINIC ACID'                                                                           IMP 
3 'N-(6-chloropyridin-3-yl)-N~2~-(1,4-dihydro-2H-pyrano[3,4-c]quinolin-9-yl)-L-alaninamide' VOA 
4 water                                                                                     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   HIS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   GLY n 
1 9   GLU n 
1 10  ASN n 
1 11  LEU n 
1 12  TYR n 
1 13  PHE n 
1 14  GLN n 
1 15  GLY n 
1 16  SER n 
1 17  TRP n 
1 18  GLU n 
1 19  SER n 
1 20  LYS n 
1 21  PHE n 
1 22  ALA n 
1 23  LYS n 
1 24  GLU n 
1 25  SER n 
1 26  LEU n 
1 27  THR n 
1 28  PHE n 
1 29  ASP n 
1 30  ASP n 
1 31  VAL n 
1 32  LEU n 
1 33  LEU n 
1 34  ILE n 
1 35  PRO n 
1 36  ALA n 
1 37  GLN n 
1 38  SER n 
1 39  ASP n 
1 40  ILE n 
1 41  LEU n 
1 42  PRO n 
1 43  LYS n 
1 44  ASP n 
1 45  VAL n 
1 46  ASP n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  GLN n 
1 51  LEU n 
1 52  SER n 
1 53  ASP n 
1 54  LYS n 
1 55  VAL n 
1 56  LYS n 
1 57  LEU n 
1 58  ASN n 
1 59  ILE n 
1 60  PRO n 
1 61  VAL n 
1 62  ILE n 
1 63  SER n 
1 64  ALA n 
1 65  GLY n 
1 66  MET n 
1 67  ASP n 
1 68  THR n 
1 69  VAL n 
1 70  THR n 
1 71  GLU n 
1 72  SER n 
1 73  LYS n 
1 74  MET n 
1 75  ALA n 
1 76  ILE n 
1 77  ALA n 
1 78  MET n 
1 79  ALA n 
1 80  ARG n 
1 81  GLN n 
1 82  GLY n 
1 83  GLY n 
1 84  LEU n 
1 85  GLY n 
1 86  VAL n 
1 87  ILE n 
1 88  HIS n 
1 89  LYS n 
1 90  ASN n 
1 91  MET n 
1 92  GLY n 
1 93  VAL n 
1 94  GLU n 
1 95  GLU n 
1 96  GLN n 
1 97  ALA n 
1 98  ASP n 
1 99  GLU n 
1 100 VAL n 
1 101 GLN n 
1 102 LYS n 
1 103 VAL n 
1 104 LYS n 
1 105 ARG n 
1 106 SER n 
1 107 GLY n 
1 108 GLY n 
1 109 LEU n 
1 110 LEU n 
1 111 VAL n 
1 112 ALA n 
1 113 ALA n 
1 114 ALA n 
1 115 ILE n 
1 116 GLY n 
1 117 ILE n 
1 118 SER n 
1 119 LYS n 
1 120 ASP n 
1 121 THR n 
1 122 ASP n 
1 123 ILE n 
1 124 ARG n 
1 125 ALA n 
1 126 GLN n 
1 127 LYS n 
1 128 LEU n 
1 129 VAL n 
1 130 GLU n 
1 131 ALA n 
1 132 GLY n 
1 133 VAL n 
1 134 ASP n 
1 135 VAL n 
1 136 LEU n 
1 137 VAL n 
1 138 ILE n 
1 139 ASP n 
1 140 THR n 
1 141 ALA n 
1 142 HIS n 
1 143 GLY n 
1 144 HIS n 
1 145 SER n 
1 146 LYS n 
1 147 GLY n 
1 148 VAL n 
1 149 ILE n 
1 150 ASP n 
1 151 GLN n 
1 152 VAL n 
1 153 LYS n 
1 154 HIS n 
1 155 ILE n 
1 156 LYS n 
1 157 LYS n 
1 158 THR n 
1 159 TYR n 
1 160 PRO n 
1 161 GLU n 
1 162 ILE n 
1 163 THR n 
1 164 LEU n 
1 165 VAL n 
1 166 ALA n 
1 167 GLY n 
1 168 ASN n 
1 169 VAL n 
1 170 ALA n 
1 171 THR n 
1 172 ALA n 
1 173 GLU n 
1 174 ALA n 
1 175 THR n 
1 176 LYS n 
1 177 ASP n 
1 178 LEU n 
1 179 PHE n 
1 180 GLU n 
1 181 ALA n 
1 182 GLY n 
1 183 ALA n 
1 184 ASP n 
1 185 ILE n 
1 186 VAL n 
1 187 LYS n 
1 188 VAL n 
1 189 GLY n 
1 190 ILE n 
1 191 GLY n 
1 192 PRO n 
1 193 GLY n 
1 194 SER n 
1 195 ILE n 
1 196 CYS n 
1 197 THR n 
1 198 THR n 
1 199 ARG n 
1 200 VAL n 
1 201 VAL n 
1 202 ALA n 
1 203 GLY n 
1 204 VAL n 
1 205 GLY n 
1 206 VAL n 
1 207 PRO n 
1 208 GLN n 
1 209 ILE n 
1 210 THR n 
1 211 ALA n 
1 212 ILE n 
1 213 TYR n 
1 214 ASP n 
1 215 CYS n 
1 216 ALA n 
1 217 THR n 
1 218 GLU n 
1 219 ALA n 
1 220 ARG n 
1 221 LYS n 
1 222 HIS n 
1 223 GLY n 
1 224 LYS n 
1 225 ALA n 
1 226 ILE n 
1 227 ILE n 
1 228 ALA n 
1 229 ASP n 
1 230 GLY n 
1 231 GLY n 
1 232 ILE n 
1 233 LYS n 
1 234 PHE n 
1 235 SER n 
1 236 GLY n 
1 237 ASP n 
1 238 ILE n 
1 239 ILE n 
1 240 LYS n 
1 241 ALA n 
1 242 LEU n 
1 243 ALA n 
1 244 ALA n 
1 245 GLY n 
1 246 GLY n 
1 247 HIS n 
1 248 ALA n 
1 249 VAL n 
1 250 MET n 
1 251 LEU n 
1 252 GLY n 
1 253 SER n 
1 254 LEU n 
1 255 LEU n 
1 256 ALA n 
1 257 GLY n 
1 258 THR n 
1 259 GLU n 
1 260 GLU n 
1 261 SER n 
1 262 PRO n 
1 263 GLY n 
1 264 ALA n 
1 265 THR n 
1 266 GLU n 
1 267 ILE n 
1 268 PHE n 
1 269 GLN n 
1 270 GLY n 
1 271 ARG n 
1 272 GLN n 
1 273 TYR n 
1 274 LYS n 
1 275 VAL n 
1 276 TYR n 
1 277 ARG n 
1 278 GLY n 
1 279 MET n 
1 280 GLY n 
1 281 SER n 
1 282 LEU n 
1 283 GLY n 
1 284 ALA n 
1 285 MET n 
1 286 GLU n 
1 287 LYS n 
1 288 GLY n 
1 289 SER n 
1 290 ASN n 
1 291 ASP n 
1 292 ARG n 
1 293 TYR n 
1 294 PHE n 
1 295 GLN n 
1 296 GLU n 
1 297 ASP n 
1 298 LYS n 
1 299 ALA n 
1 300 PRO n 
1 301 LYS n 
1 302 LYS n 
1 303 PHE n 
1 304 VAL n 
1 305 PRO n 
1 306 GLU n 
1 307 GLY n 
1 308 ILE n 
1 309 GLU n 
1 310 GLY n 
1 311 ARG n 
1 312 THR n 
1 313 ALA n 
1 314 TYR n 
1 315 LYS n 
1 316 GLY n 
1 317 ALA n 
1 318 LEU n 
1 319 GLN n 
1 320 ASP n 
1 321 THR n 
1 322 ILE n 
1 323 TYR n 
1 324 GLN n 
1 325 LEU n 
1 326 MET n 
1 327 GLY n 
1 328 GLY n 
1 329 VAL n 
1 330 ARG n 
1 331 ALA n 
1 332 GLY n 
1 333 MET n 
1 334 GLY n 
1 335 TYR n 
1 336 THR n 
1 337 GLY n 
1 338 SER n 
1 339 HIS n 
1 340 ASP n 
1 341 LEU n 
1 342 ARG n 
1 343 GLU n 
1 344 LEU n 
1 345 ARG n 
1 346 GLU n 
1 347 GLU n 
1 348 ALA n 
1 349 GLN n 
1 350 PHE n 
1 351 THR n 
1 352 ARG n 
1 353 MET n 
1 354 GLY n 
1 355 PRO n 
1 356 ALA n 
1 357 GLY n 
1 358 LEU n 
1 359 ALA n 
1 360 GLU n 
1 361 SER n 
1 362 HIS n 
1 363 PRO n 
1 364 HIS n 
1 365 ASN n 
1 366 ILE n 
1 367 GLN n 
1 368 ILE n 
1 369 THR n 
1 370 LYS n 
1 371 GLU n 
1 372 SER n 
1 373 PRO n 
1 374 ASN n 
1 375 TYR n 
1 376 SER n 
1 377 PHE n 
1 378 GLY n 
1 379 ASN n 
1 380 SER n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1   108 ? ? 'guaB, SAUSA300_0388' ? ? ? ? ? ? 'Staphylococcus aureus' 1280 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 109 380 ? ? 'guaB, SAUSA300_0388' ? ? ? ? ? ? 'Staphylococcus aureus' 1280 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                                   ? 'C3 H7 N O2' 
89.093  
ARG 'L-peptide linking' y ARGININE                                                                                  ? 
'C6 H15 N4 O2 1'   175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                                ? 
'C4 H8 N2 O3'      132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                                           ? 'C4 H7 N O4' 
133.103 
CYS 'L-peptide linking' y CYSTEINE                                                                                  ? 
'C3 H7 N O2 S'     121.158 
GLN 'L-peptide linking' y GLUTAMINE                                                                                 ? 
'C5 H10 N2 O3'     146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                           ? 'C5 H9 N O4' 
147.129 
GLY 'peptide linking'   y GLYCINE                                                                                   ? 'C2 H5 N O2' 
75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                                 ? 
'C6 H10 N3 O2 1'   156.162 
HOH non-polymer         . WATER                                                                                     ? 'H2 O' 
18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                                ? 
'C6 H13 N O2'      131.173 
IMP non-polymer         n 'INOSINIC ACID'                                                                           ? 
'C10 H13 N4 O8 P'  348.206 
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 
VOA non-polymer         . 'N-(6-chloropyridin-3-yl)-N~2~-(1,4-dihydro-2H-pyrano[3,4-c]quinolin-9-yl)-L-alaninamide' ? 
'C20 H19 Cl N4 O2' 382.843 
# 
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   -14 ?   ?   ?   A . n 
A 1 2   HIS 2   -13 ?   ?   ?   A . n 
A 1 3   HIS 3   -12 ?   ?   ?   A . n 
A 1 4   HIS 4   -11 ?   ?   ?   A . n 
A 1 5   HIS 5   -10 ?   ?   ?   A . n 
A 1 6   HIS 6   -9  ?   ?   ?   A . n 
A 1 7   HIS 7   -8  ?   ?   ?   A . n 
A 1 8   GLY 8   -7  ?   ?   ?   A . n 
A 1 9   GLU 9   -6  ?   ?   ?   A . n 
A 1 10  ASN 10  -5  ?   ?   ?   A . n 
A 1 11  LEU 11  -4  ?   ?   ?   A . n 
A 1 12  TYR 12  -3  ?   ?   ?   A . n 
A 1 13  PHE 13  -2  ?   ?   ?   A . n 
A 1 14  GLN 14  -1  ?   ?   ?   A . n 
A 1 15  GLY 15  0   0   GLY GLY A . n 
A 1 16  SER 16  1   1   SER SER A . n 
A 1 17  TRP 17  2   2   TRP TRP A . n 
A 1 18  GLU 18  3   3   GLU GLU A . n 
A 1 19  SER 19  4   4   SER SER A . n 
A 1 20  LYS 20  5   5   LYS LYS A . n 
A 1 21  PHE 21  6   6   PHE PHE A . n 
A 1 22  ALA 22  7   7   ALA ALA A . n 
A 1 23  LYS 23  8   8   LYS LYS A . n 
A 1 24  GLU 24  9   9   GLU GLU A . n 
A 1 25  SER 25  10  10  SER SER A . n 
A 1 26  LEU 26  11  11  LEU LEU A . n 
A 1 27  THR 27  12  12  THR THR A . n 
A 1 28  PHE 28  13  13  PHE PHE A . n 
A 1 29  ASP 29  14  14  ASP ASP A . n 
A 1 30  ASP 30  15  15  ASP ASP A . n 
A 1 31  VAL 31  16  16  VAL VAL A . n 
A 1 32  LEU 32  17  17  LEU LEU A . n 
A 1 33  LEU 33  18  18  LEU LEU A . n 
A 1 34  ILE 34  19  19  ILE ILE A . n 
A 1 35  PRO 35  20  20  PRO PRO A . n 
A 1 36  ALA 36  21  21  ALA ALA A . n 
A 1 37  GLN 37  22  22  GLN GLN A . n 
A 1 38  SER 38  23  23  SER SER A . n 
A 1 39  ASP 39  24  24  ASP ASP A . n 
A 1 40  ILE 40  25  25  ILE ILE A . n 
A 1 41  LEU 41  26  26  LEU LEU A . n 
A 1 42  PRO 42  27  27  PRO PRO A . n 
A 1 43  LYS 43  28  28  LYS LYS A . n 
A 1 44  ASP 44  29  29  ASP ASP A . n 
A 1 45  VAL 45  30  30  VAL VAL A . n 
A 1 46  ASP 46  31  31  ASP ASP A . n 
A 1 47  LEU 47  32  32  LEU LEU A . n 
A 1 48  SER 48  33  33  SER SER A . n 
A 1 49  VAL 49  34  34  VAL VAL A . n 
A 1 50  GLN 50  35  35  GLN GLN A . n 
A 1 51  LEU 51  36  36  LEU LEU A . n 
A 1 52  SER 52  37  37  SER SER A . n 
A 1 53  ASP 53  38  38  ASP ASP A . n 
A 1 54  LYS 54  39  39  LYS LYS A . n 
A 1 55  VAL 55  40  40  VAL VAL A . n 
A 1 56  LYS 56  41  41  LYS LYS A . n 
A 1 57  LEU 57  42  42  LEU LEU A . n 
A 1 58  ASN 58  43  43  ASN ASN A . n 
A 1 59  ILE 59  44  44  ILE ILE A . n 
A 1 60  PRO 60  45  45  PRO PRO A . n 
A 1 61  VAL 61  46  46  VAL VAL A . n 
A 1 62  ILE 62  47  47  ILE ILE A . n 
A 1 63  SER 63  48  48  SER SER A . n 
A 1 64  ALA 64  49  49  ALA ALA A . n 
A 1 65  GLY 65  50  50  GLY GLY A . n 
A 1 66  MET 66  51  51  MET MET A . n 
A 1 67  ASP 67  52  52  ASP ASP A . n 
A 1 68  THR 68  53  53  THR THR A . n 
A 1 69  VAL 69  54  54  VAL VAL A . n 
A 1 70  THR 70  55  55  THR THR A . n 
A 1 71  GLU 71  56  56  GLU GLU A . n 
A 1 72  SER 72  57  57  SER SER A . n 
A 1 73  LYS 73  58  58  LYS LYS A . n 
A 1 74  MET 74  59  59  MET MET A . n 
A 1 75  ALA 75  60  60  ALA ALA A . n 
A 1 76  ILE 76  61  61  ILE ILE A . n 
A 1 77  ALA 77  62  62  ALA ALA A . n 
A 1 78  MET 78  63  63  MET MET A . n 
A 1 79  ALA 79  64  64  ALA ALA A . n 
A 1 80  ARG 80  65  65  ARG ARG A . n 
A 1 81  GLN 81  66  66  GLN GLN A . n 
A 1 82  GLY 82  67  67  GLY GLY A . n 
A 1 83  GLY 83  68  68  GLY GLY A . n 
A 1 84  LEU 84  69  69  LEU LEU A . n 
A 1 85  GLY 85  70  70  GLY GLY A . n 
A 1 86  VAL 86  71  71  VAL VAL A . n 
A 1 87  ILE 87  72  72  ILE ILE A . n 
A 1 88  HIS 88  73  73  HIS HIS A . n 
A 1 89  LYS 89  74  74  LYS LYS A . n 
A 1 90  ASN 90  75  75  ASN ASN A . n 
A 1 91  MET 91  76  76  MET MET A . n 
A 1 92  GLY 92  77  77  GLY GLY A . n 
A 1 93  VAL 93  78  78  VAL VAL A . n 
A 1 94  GLU 94  79  79  GLU GLU A . n 
A 1 95  GLU 95  80  80  GLU GLU A . n 
A 1 96  GLN 96  81  81  GLN GLN A . n 
A 1 97  ALA 97  82  82  ALA ALA A . n 
A 1 98  ASP 98  83  83  ASP ASP A . n 
A 1 99  GLU 99  84  84  GLU GLU A . n 
A 1 100 VAL 100 85  85  VAL VAL A . n 
A 1 101 GLN 101 86  86  GLN GLN A . n 
A 1 102 LYS 102 87  87  LYS LYS A . n 
A 1 103 VAL 103 88  88  VAL VAL A . n 
A 1 104 LYS 104 89  89  LYS LYS A . n 
A 1 105 ARG 105 90  90  ARG ARG A . n 
A 1 106 SER 106 91  91  SER SER A . n 
A 1 107 GLY 107 92  92  GLY GLY A . n 
A 1 108 GLY 108 93  93  GLY GLY A . n 
A 1 109 LEU 109 220 220 LEU LEU A . n 
A 1 110 LEU 110 221 221 LEU LEU A . n 
A 1 111 VAL 111 222 222 VAL VAL A . n 
A 1 112 ALA 112 223 223 ALA ALA A . n 
A 1 113 ALA 113 224 224 ALA ALA A . n 
A 1 114 ALA 114 225 225 ALA ALA A . n 
A 1 115 ILE 115 226 226 ILE ILE A . n 
A 1 116 GLY 116 227 227 GLY GLY A . n 
A 1 117 ILE 117 228 228 ILE ILE A . n 
A 1 118 SER 118 229 229 SER SER A . n 
A 1 119 LYS 119 230 230 LYS LYS A . n 
A 1 120 ASP 120 231 231 ASP ASP A . n 
A 1 121 THR 121 232 232 THR THR A . n 
A 1 122 ASP 122 233 233 ASP ASP A . n 
A 1 123 ILE 123 234 234 ILE ILE A . n 
A 1 124 ARG 124 235 235 ARG ARG A . n 
A 1 125 ALA 125 236 236 ALA ALA A . n 
A 1 126 GLN 126 237 237 GLN GLN A . n 
A 1 127 LYS 127 238 238 LYS LYS A . n 
A 1 128 LEU 128 239 239 LEU LEU A . n 
A 1 129 VAL 129 240 240 VAL VAL A . n 
A 1 130 GLU 130 241 241 GLU GLU A . n 
A 1 131 ALA 131 242 242 ALA ALA A . n 
A 1 132 GLY 132 243 243 GLY GLY A . n 
A 1 133 VAL 133 244 244 VAL VAL A . n 
A 1 134 ASP 134 245 245 ASP ASP A . n 
A 1 135 VAL 135 246 246 VAL VAL A . n 
A 1 136 LEU 136 247 247 LEU LEU A . n 
A 1 137 VAL 137 248 248 VAL VAL A . n 
A 1 138 ILE 138 249 249 ILE ILE A . n 
A 1 139 ASP 139 250 250 ASP ASP A . n 
A 1 140 THR 140 251 251 THR THR A . n 
A 1 141 ALA 141 252 252 ALA ALA A . n 
A 1 142 HIS 142 253 253 HIS HIS A . n 
A 1 143 GLY 143 254 254 GLY GLY A . n 
A 1 144 HIS 144 255 255 HIS HIS A . n 
A 1 145 SER 145 256 256 SER SER A . n 
A 1 146 LYS 146 257 257 LYS LYS A . n 
A 1 147 GLY 147 258 258 GLY GLY A . n 
A 1 148 VAL 148 259 259 VAL VAL A . n 
A 1 149 ILE 149 260 260 ILE ILE A . n 
A 1 150 ASP 150 261 261 ASP ASP A . n 
A 1 151 GLN 151 262 262 GLN GLN A . n 
A 1 152 VAL 152 263 263 VAL VAL A . n 
A 1 153 LYS 153 264 264 LYS LYS A . n 
A 1 154 HIS 154 265 265 HIS HIS A . n 
A 1 155 ILE 155 266 266 ILE ILE A . n 
A 1 156 LYS 156 267 267 LYS LYS A . n 
A 1 157 LYS 157 268 268 LYS LYS A . n 
A 1 158 THR 158 269 269 THR THR A . n 
A 1 159 TYR 159 270 270 TYR TYR A . n 
A 1 160 PRO 160 271 271 PRO PRO A . n 
A 1 161 GLU 161 272 272 GLU GLU A . n 
A 1 162 ILE 162 273 273 ILE ILE A . n 
A 1 163 THR 163 274 274 THR THR A . n 
A 1 164 LEU 164 275 275 LEU LEU A . n 
A 1 165 VAL 165 276 276 VAL VAL A . n 
A 1 166 ALA 166 277 277 ALA ALA A . n 
A 1 167 GLY 167 278 278 GLY GLY A . n 
A 1 168 ASN 168 279 279 ASN ASN A . n 
A 1 169 VAL 169 280 280 VAL VAL A . n 
A 1 170 ALA 170 281 281 ALA ALA A . n 
A 1 171 THR 171 282 282 THR THR A . n 
A 1 172 ALA 172 283 283 ALA ALA A . n 
A 1 173 GLU 173 284 284 GLU GLU A . n 
A 1 174 ALA 174 285 285 ALA ALA A . n 
A 1 175 THR 175 286 286 THR THR A . n 
A 1 176 LYS 176 287 287 LYS LYS A . n 
A 1 177 ASP 177 288 288 ASP ASP A . n 
A 1 178 LEU 178 289 289 LEU LEU A . n 
A 1 179 PHE 179 290 290 PHE PHE A . n 
A 1 180 GLU 180 291 291 GLU GLU A . n 
A 1 181 ALA 181 292 292 ALA ALA A . n 
A 1 182 GLY 182 293 293 GLY GLY A . n 
A 1 183 ALA 183 294 294 ALA ALA A . n 
A 1 184 ASP 184 295 295 ASP ASP A . n 
A 1 185 ILE 185 296 296 ILE ILE A . n 
A 1 186 VAL 186 297 297 VAL VAL A . n 
A 1 187 LYS 187 298 298 LYS LYS A . n 
A 1 188 VAL 188 299 299 VAL VAL A . n 
A 1 189 GLY 189 300 300 GLY GLY A . n 
A 1 190 ILE 190 301 301 ILE ILE A . n 
A 1 191 GLY 191 302 302 GLY GLY A . n 
A 1 192 PRO 192 303 303 PRO PRO A . n 
A 1 193 GLY 193 304 304 GLY GLY A . n 
A 1 194 SER 194 305 305 SER SER A . n 
A 1 195 ILE 195 306 306 ILE ILE A . n 
A 1 196 CYS 196 307 307 CYS CYS A . n 
A 1 197 THR 197 308 308 THR THR A . n 
A 1 198 THR 198 309 309 THR THR A . n 
A 1 199 ARG 199 310 310 ARG ARG A . n 
A 1 200 VAL 200 311 311 VAL VAL A . n 
A 1 201 VAL 201 312 312 VAL VAL A . n 
A 1 202 ALA 202 313 313 ALA ALA A . n 
A 1 203 GLY 203 314 314 GLY GLY A . n 
A 1 204 VAL 204 315 315 VAL VAL A . n 
A 1 205 GLY 205 316 316 GLY GLY A . n 
A 1 206 VAL 206 317 317 VAL VAL A . n 
A 1 207 PRO 207 318 318 PRO PRO A . n 
A 1 208 GLN 208 319 319 GLN GLN A . n 
A 1 209 ILE 209 320 320 ILE ILE A . n 
A 1 210 THR 210 321 321 THR THR A . n 
A 1 211 ALA 211 322 322 ALA ALA A . n 
A 1 212 ILE 212 323 323 ILE ILE A . n 
A 1 213 TYR 213 324 324 TYR TYR A . n 
A 1 214 ASP 214 325 325 ASP ASP A . n 
A 1 215 CYS 215 326 326 CYS CYS A . n 
A 1 216 ALA 216 327 327 ALA ALA A . n 
A 1 217 THR 217 328 328 THR THR A . n 
A 1 218 GLU 218 329 329 GLU GLU A . n 
A 1 219 ALA 219 330 330 ALA ALA A . n 
A 1 220 ARG 220 331 331 ARG ARG A . n 
A 1 221 LYS 221 332 332 LYS LYS A . n 
A 1 222 HIS 222 333 333 HIS HIS A . n 
A 1 223 GLY 223 334 334 GLY GLY A . n 
A 1 224 LYS 224 335 335 LYS LYS A . n 
A 1 225 ALA 225 336 336 ALA ALA A . n 
A 1 226 ILE 226 337 337 ILE ILE A . n 
A 1 227 ILE 227 338 338 ILE ILE A . n 
A 1 228 ALA 228 339 339 ALA ALA A . n 
A 1 229 ASP 229 340 340 ASP ASP A . n 
A 1 230 GLY 230 341 341 GLY GLY A . n 
A 1 231 GLY 231 342 342 GLY GLY A . n 
A 1 232 ILE 232 343 343 ILE ILE A . n 
A 1 233 LYS 233 344 344 LYS LYS A . n 
A 1 234 PHE 234 345 345 PHE PHE A . n 
A 1 235 SER 235 346 346 SER SER A . n 
A 1 236 GLY 236 347 347 GLY GLY A . n 
A 1 237 ASP 237 348 348 ASP ASP A . n 
A 1 238 ILE 238 349 349 ILE ILE A . n 
A 1 239 ILE 239 350 350 ILE ILE A . n 
A 1 240 LYS 240 351 351 LYS LYS A . n 
A 1 241 ALA 241 352 352 ALA ALA A . n 
A 1 242 LEU 242 353 353 LEU LEU A . n 
A 1 243 ALA 243 354 354 ALA ALA A . n 
A 1 244 ALA 244 355 355 ALA ALA A . n 
A 1 245 GLY 245 356 356 GLY GLY A . n 
A 1 246 GLY 246 357 357 GLY GLY A . n 
A 1 247 HIS 247 358 358 HIS HIS A . n 
A 1 248 ALA 248 359 359 ALA ALA A . n 
A 1 249 VAL 249 360 360 VAL VAL A . n 
A 1 250 MET 250 361 361 MET MET A . n 
A 1 251 LEU 251 362 362 LEU LEU A . n 
A 1 252 GLY 252 363 363 GLY GLY A . n 
A 1 253 SER 253 364 364 SER SER A . n 
A 1 254 LEU 254 365 365 LEU LEU A . n 
A 1 255 LEU 255 366 366 LEU LEU A . n 
A 1 256 ALA 256 367 367 ALA ALA A . n 
A 1 257 GLY 257 368 368 GLY GLY A . n 
A 1 258 THR 258 369 369 THR THR A . n 
A 1 259 GLU 259 370 370 GLU GLU A . n 
A 1 260 GLU 260 371 371 GLU GLU A . n 
A 1 261 SER 261 372 372 SER SER A . n 
A 1 262 PRO 262 373 373 PRO PRO A . n 
A 1 263 GLY 263 374 374 GLY GLY A . n 
A 1 264 ALA 264 375 375 ALA ALA A . n 
A 1 265 THR 265 376 376 THR THR A . n 
A 1 266 GLU 266 377 377 GLU GLU A . n 
A 1 267 ILE 267 378 378 ILE ILE A . n 
A 1 268 PHE 268 379 379 PHE PHE A . n 
A 1 269 GLN 269 380 380 GLN GLN A . n 
A 1 270 GLY 270 381 381 GLY GLY A . n 
A 1 271 ARG 271 382 382 ARG ARG A . n 
A 1 272 GLN 272 383 383 GLN GLN A . n 
A 1 273 TYR 273 384 384 TYR TYR A . n 
A 1 274 LYS 274 385 385 LYS LYS A . n 
A 1 275 VAL 275 386 386 VAL VAL A . n 
A 1 276 TYR 276 387 387 TYR TYR A . n 
A 1 277 ARG 277 388 388 ARG ARG A . n 
A 1 278 GLY 278 389 389 GLY GLY A . n 
A 1 279 MET 279 390 390 MET MET A . n 
A 1 280 GLY 280 391 391 GLY GLY A . n 
A 1 281 SER 281 392 392 SER SER A . n 
A 1 282 LEU 282 393 393 LEU LEU A . n 
A 1 283 GLY 283 394 394 GLY GLY A . n 
A 1 284 ALA 284 395 395 ALA ALA A . n 
A 1 285 MET 285 396 396 MET MET A . n 
A 1 286 GLU 286 397 397 GLU GLU A . n 
A 1 287 LYS 287 398 ?   ?   ?   A . n 
A 1 288 GLY 288 399 ?   ?   ?   A . n 
A 1 289 SER 289 400 ?   ?   ?   A . n 
A 1 290 ASN 290 401 ?   ?   ?   A . n 
A 1 291 ASP 291 402 ?   ?   ?   A . n 
A 1 292 ARG 292 403 ?   ?   ?   A . n 
A 1 293 TYR 293 404 ?   ?   ?   A . n 
A 1 294 PHE 294 405 ?   ?   ?   A . n 
A 1 295 GLN 295 406 ?   ?   ?   A . n 
A 1 296 GLU 296 407 ?   ?   ?   A . n 
A 1 297 ASP 297 408 ?   ?   ?   A . n 
A 1 298 LYS 298 409 ?   ?   ?   A . n 
A 1 299 ALA 299 410 ?   ?   ?   A . n 
A 1 300 PRO 300 411 ?   ?   ?   A . n 
A 1 301 LYS 301 412 ?   ?   ?   A . n 
A 1 302 LYS 302 413 413 LYS ALA A . n 
A 1 303 PHE 303 414 414 PHE PHE A . n 
A 1 304 VAL 304 415 415 VAL VAL A . n 
A 1 305 PRO 305 416 416 PRO PRO A . n 
A 1 306 GLU 306 417 417 GLU GLU A . n 
A 1 307 GLY 307 418 418 GLY GLY A . n 
A 1 308 ILE 308 419 419 ILE ILE A . n 
A 1 309 GLU 309 420 420 GLU GLU A . n 
A 1 310 GLY 310 421 421 GLY GLY A . n 
A 1 311 ARG 311 422 422 ARG ARG A . n 
A 1 312 THR 312 423 423 THR THR A . n 
A 1 313 ALA 313 424 424 ALA ALA A . n 
A 1 314 TYR 314 425 425 TYR TYR A . n 
A 1 315 LYS 315 426 426 LYS LYS A . n 
A 1 316 GLY 316 427 427 GLY GLY A . n 
A 1 317 ALA 317 428 428 ALA ALA A . n 
A 1 318 LEU 318 429 429 LEU LEU A . n 
A 1 319 GLN 319 430 430 GLN GLN A . n 
A 1 320 ASP 320 431 431 ASP ASP A . n 
A 1 321 THR 321 432 432 THR THR A . n 
A 1 322 ILE 322 433 433 ILE ILE A . n 
A 1 323 TYR 323 434 434 TYR TYR A . n 
A 1 324 GLN 324 435 435 GLN GLN A . n 
A 1 325 LEU 325 436 436 LEU LEU A . n 
A 1 326 MET 326 437 437 MET MET A . n 
A 1 327 GLY 327 438 438 GLY GLY A . n 
A 1 328 GLY 328 439 439 GLY GLY A . n 
A 1 329 VAL 329 440 440 VAL VAL A . n 
A 1 330 ARG 330 441 441 ARG ARG A . n 
A 1 331 ALA 331 442 442 ALA ALA A . n 
A 1 332 GLY 332 443 443 GLY GLY A . n 
A 1 333 MET 333 444 444 MET MET A . n 
A 1 334 GLY 334 445 445 GLY GLY A . n 
A 1 335 TYR 335 446 446 TYR TYR A . n 
A 1 336 THR 336 447 447 THR THR A . n 
A 1 337 GLY 337 448 448 GLY GLY A . n 
A 1 338 SER 338 449 449 SER SER A . n 
A 1 339 HIS 339 450 450 HIS HIS A . n 
A 1 340 ASP 340 451 451 ASP ASP A . n 
A 1 341 LEU 341 452 452 LEU LEU A . n 
A 1 342 ARG 342 453 453 ARG ARG A . n 
A 1 343 GLU 343 454 454 GLU GLU A . n 
A 1 344 LEU 344 455 455 LEU LEU A . n 
A 1 345 ARG 345 456 456 ARG ARG A . n 
A 1 346 GLU 346 457 457 GLU GLU A . n 
A 1 347 GLU 347 458 458 GLU GLU A . n 
A 1 348 ALA 348 459 459 ALA ALA A . n 
A 1 349 GLN 349 460 460 GLN GLN A . n 
A 1 350 PHE 350 461 461 PHE PHE A . n 
A 1 351 THR 351 462 462 THR THR A . n 
A 1 352 ARG 352 463 463 ARG ARG A . n 
A 1 353 MET 353 464 464 MET MET A . n 
A 1 354 GLY 354 465 465 GLY GLY A . n 
A 1 355 PRO 355 466 466 PRO PRO A . n 
A 1 356 ALA 356 467 ?   ?   ?   A . n 
A 1 357 GLY 357 468 ?   ?   ?   A . n 
A 1 358 LEU 358 469 ?   ?   ?   A . n 
A 1 359 ALA 359 470 ?   ?   ?   A . n 
A 1 360 GLU 360 471 ?   ?   ?   A . n 
A 1 361 SER 361 472 ?   ?   ?   A . n 
A 1 362 HIS 362 473 ?   ?   ?   A . n 
A 1 363 PRO 363 474 ?   ?   ?   A . n 
A 1 364 HIS 364 475 ?   ?   ?   A . n 
A 1 365 ASN 365 476 ?   ?   ?   A . n 
A 1 366 ILE 366 477 ?   ?   ?   A . n 
A 1 367 GLN 367 478 ?   ?   ?   A . n 
A 1 368 ILE 368 479 ?   ?   ?   A . n 
A 1 369 THR 369 480 ?   ?   ?   A . n 
A 1 370 LYS 370 481 ?   ?   ?   A . n 
A 1 371 GLU 371 482 ?   ?   ?   A . n 
A 1 372 SER 372 483 ?   ?   ?   A . n 
A 1 373 PRO 373 484 ?   ?   ?   A . n 
A 1 374 ASN 374 485 ?   ?   ?   A . n 
A 1 375 TYR 375 486 ?   ?   ?   A . n 
A 1 376 SER 376 487 ?   ?   ?   A . n 
A 1 377 PHE 377 488 ?   ?   ?   A . n 
A 1 378 GLY 378 489 ?   ?   ?   A . n 
A 1 379 ASN 379 490 ?   ?   ?   A . n 
A 1 380 SER 380 491 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        VOA 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   VOA 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 IMP 1  801 801 IMP IMP A . 
C 3 VOA 1  802 1   VOA DRG A . 
D 4 HOH 1  901 19  HOH HOH A . 
D 4 HOH 2  902 44  HOH HOH A . 
D 4 HOH 3  903 23  HOH HOH A . 
D 4 HOH 4  904 92  HOH HOH A . 
D 4 HOH 5  905 65  HOH HOH A . 
D 4 HOH 6  906 7   HOH HOH A . 
D 4 HOH 7  907 8   HOH HOH A . 
D 4 HOH 8  908 49  HOH HOH A . 
D 4 HOH 9  909 43  HOH HOH A . 
D 4 HOH 10 910 77  HOH HOH A . 
D 4 HOH 11 911 3   HOH HOH A . 
D 4 HOH 12 912 15  HOH HOH A . 
D 4 HOH 13 913 18  HOH HOH A . 
D 4 HOH 14 914 5   HOH HOH A . 
D 4 HOH 15 915 34  HOH HOH A . 
D 4 HOH 16 916 66  HOH HOH A . 
D 4 HOH 17 917 64  HOH HOH A . 
D 4 HOH 18 918 17  HOH HOH A . 
D 4 HOH 19 919 87  HOH HOH A . 
D 4 HOH 20 920 20  HOH HOH A . 
D 4 HOH 21 921 9   HOH HOH A . 
D 4 HOH 22 922 13  HOH HOH A . 
D 4 HOH 23 923 48  HOH HOH A . 
D 4 HOH 24 924 46  HOH HOH A . 
D 4 HOH 25 925 85  HOH HOH A . 
D 4 HOH 26 926 56  HOH HOH A . 
D 4 HOH 27 927 11  HOH HOH A . 
D 4 HOH 28 928 31  HOH HOH A . 
D 4 HOH 29 929 36  HOH HOH A . 
D 4 HOH 30 930 1   HOH HOH A . 
D 4 HOH 31 931 29  HOH HOH A . 
D 4 HOH 32 932 76  HOH HOH A . 
D 4 HOH 33 933 62  HOH HOH A . 
D 4 HOH 34 934 16  HOH HOH A . 
D 4 HOH 35 935 68  HOH HOH A . 
D 4 HOH 36 936 2   HOH HOH A . 
D 4 HOH 37 937 6   HOH HOH A . 
D 4 HOH 38 938 84  HOH HOH A . 
D 4 HOH 39 939 37  HOH HOH A . 
D 4 HOH 40 940 41  HOH HOH A . 
D 4 HOH 41 941 55  HOH HOH A . 
D 4 HOH 42 942 45  HOH HOH A . 
D 4 HOH 43 943 72  HOH HOH A . 
D 4 HOH 44 944 27  HOH HOH A . 
D 4 HOH 45 945 58  HOH HOH A . 
D 4 HOH 46 946 74  HOH HOH A . 
D 4 HOH 47 947 69  HOH HOH A . 
D 4 HOH 48 948 35  HOH HOH A . 
D 4 HOH 49 949 61  HOH HOH A . 
D 4 HOH 50 950 60  HOH HOH A . 
D 4 HOH 51 951 51  HOH HOH A . 
D 4 HOH 52 952 28  HOH HOH A . 
D 4 HOH 53 953 22  HOH HOH A . 
D 4 HOH 54 954 4   HOH HOH A . 
D 4 HOH 55 955 50  HOH HOH A . 
D 4 HOH 56 956 21  HOH HOH A . 
D 4 HOH 57 957 12  HOH HOH A . 
D 4 HOH 58 958 73  HOH HOH A . 
D 4 HOH 59 959 33  HOH HOH A . 
D 4 HOH 60 960 75  HOH HOH A . 
D 4 HOH 61 961 57  HOH HOH A . 
D 4 HOH 62 962 67  HOH HOH A . 
D 4 HOH 63 963 78  HOH HOH A . 
D 4 HOH 64 964 83  HOH HOH A . 
D 4 HOH 65 965 89  HOH HOH A . 
D 4 HOH 66 966 63  HOH HOH A . 
D 4 HOH 67 967 80  HOH HOH A . 
D 4 HOH 68 968 53  HOH HOH A . 
D 4 HOH 69 969 14  HOH HOH A . 
D 4 HOH 70 970 54  HOH HOH A . 
D 4 HOH 71 971 39  HOH HOH A . 
D 4 HOH 72 972 32  HOH HOH A . 
D 4 HOH 73 973 94  HOH HOH A . 
D 4 HOH 74 974 82  HOH HOH A . 
D 4 HOH 75 975 91  HOH HOH A . 
D 4 HOH 76 976 38  HOH HOH A . 
D 4 HOH 77 977 93  HOH HOH A . 
D 4 HOH 78 978 90  HOH HOH A . 
D 4 HOH 79 979 30  HOH HOH A . 
D 4 HOH 80 980 79  HOH HOH A . 
D 4 HOH 81 981 52  HOH HOH A . 
D 4 HOH 82 982 42  HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A LYS 413 ? CG ? A LYS 302 CG 
2 1 Y 1 A LYS 413 ? CD ? A LYS 302 CD 
3 1 Y 1 A LYS 413 ? CE ? A LYS 302 CE 
4 1 Y 1 A LYS 413 ? NZ ? A LYS 302 NZ 
# 
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       ? ? ? ? ? ? ? ? ? ? ? BUSTER  ? ? ? 2.11.6 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .      2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .      3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .      4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9AUY 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     104.279 
_cell.length_a_esd                 ? 
_cell.length_b                     104.279 
_cell.length_b_esd                 ? 
_cell.length_c                     63.903 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9AUY 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                79 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'I 4' 
_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                   9AUY 
_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             2.14 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.51 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              9 
_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    '0.1M Bicine pH 9, 0.1M NaCl, 30% PEG550 MME' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS 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         2019-02-28 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9792 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'APS BEAMLINE 24-ID-C' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9792 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   24-ID-C 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9AUY 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.93 
_reflns.d_resolution_low                               52.14 
_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                                     25343 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          24.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.035 
_reflns.pdbx_Rpim_I_all                                0.013 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       169600 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.000 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.032 
_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                                    1.93 
_reflns_shell.d_res_low                                     2.04 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           24783 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3679 
_reflns_shell.percent_possible_obs                          99.2 
_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                               6.7 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.9 
_reflns_shell.pdbx_Rrim_I_all                               0.994 
_reflns_shell.pdbx_Rpim_I_all                               0.380 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.759 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.917 
_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]                            4.50080 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.00000 
_refine.aniso_B[2][2]                            4.50080 
_refine.aniso_B[2][3]                            0.00000 
_refine.aniso_B[3][3]                            -9.00170 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               61.44 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.948 
_refine.correlation_coeff_Fo_to_Fc_free          0.937 
_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                                 9AUY 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.94 
_refine.ls_d_res_low                             52.14 
_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                     25115 
_refine.ls_number_reflns_R_free                  1248 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.5 
_refine.ls_percent_reflns_R_free                 4.970 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.229 
_refine.ls_R_factor_R_free                       0.261 
_refine.ls_R_factor_R_free_error                 0.000 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.227 
_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                    ? 
_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                          0.000 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_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                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.165 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.162 
_refine.pdbx_overall_SU_R_Blow_DPI               0.186 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.190 
_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_analyze.entry_id                        9AUY 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.33 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.94 
_refine_hist.d_res_low                        52.14 
_refine_hist.number_atoms_solvent             82 
_refine_hist.number_atoms_total               2531 
_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        2399 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         50 
_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' ? 0.010 ? 2657 ? t_bond_d                  2.00  HARMONIC     
'X-RAY DIFFRACTION' ? 1.16  ? 3624 ? t_angle_deg               2.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 952  ? t_dihedral_angle_d        2.00  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_incorr_chiral_ct        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_pseud_angle             ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 61   ? t_trig_c_planes           2.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 416  ? t_gen_planes              5.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 2657 ? t_it                      20.00 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_nbd                     ?     ?            
'X-RAY DIFFRACTION' ? 2.87  ? ?    ? t_omega_torsion           ?     ?            
'X-RAY DIFFRACTION' ? 18.24 ? ?    ? t_other_torsion           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_improper_torsion        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 354  ? t_chiral_improper_torsion 5.00  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_sum_occupancies         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_distance        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_angle           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_torsion         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 3236 ? t_ideal_dist_contact      4.00  SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.94 
_refine_ls_shell.d_res_low                        2.02 
_refine_ls_shell.number_reflns_all                2807 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             126 
_refine_ls_shell.number_reflns_R_work             2681 
_refine_ls_shell.percent_reflns_obs               98.25 
_refine_ls_shell.percent_reflns_R_free            4.49 
_refine_ls_shell.R_factor_all                     0.247 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            0.000 
_refine_ls_shell.R_factor_R_work                  0.244 
_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   13 
_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                  0.299 
# 
_struct.entry_id                     9AUY 
_struct.title                        'Crystal structure of S. aureus GuaB dCBS with inhibitor GNE9123' 
_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        9AUY 
_struct_keywords.text            'GuaB, inhibitor, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP IMDH_STAA3 Q2FJM6 ? 1 
;WESKFAKESLTFDDVLLIPAQSDILPKDVDLSVQLSDKVKLNIPVISAGMDTVTESKMAIAMARQGGLGVIHKNMGVEEQ
ADEVQKVKRS
;
2   
2 UNP IMDH_STAA3 Q2FJM6 ? 1 
;LLVAAAIGISKDTDIRAQKLVEAGVDVLVIDTAHGHSKGVIDQVKHIKKTYPEITLVAGNVATAEATKDLFEAGADIVKV
GIGPGSICTTRVVAGVGVPQITAIYDCATEARKHGKAIIADGGIKFSGDIIKALAAGGHAVMLGSLLAGTEESPGATEIF
QGRQYKVYRGMGSLGAMEKGSNDRYFQEDKAPKKFVPEGIEGRTAYKGALQDTIYQLMGGVRAGMGYTGSHDLRELREEA
QFTRMGPAGLAESHPHNIQITKESPNYSF
;
220 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9AUY A 17  ? 106 ? Q2FJM6 2   ? 91  ? 2   91  
2 2 9AUY A 109 ? 377 ? Q2FJM6 220 ? 488 ? 220 488 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9AUY MET A 1   ? UNP Q2FJM6 ? ? 'initiating methionine' -14 1  
1 9AUY HIS A 2   ? UNP Q2FJM6 ? ? 'expression tag'        -13 2  
1 9AUY HIS A 3   ? UNP Q2FJM6 ? ? 'expression tag'        -12 3  
1 9AUY HIS A 4   ? UNP Q2FJM6 ? ? 'expression tag'        -11 4  
1 9AUY HIS A 5   ? UNP Q2FJM6 ? ? 'expression tag'        -10 5  
1 9AUY HIS A 6   ? UNP Q2FJM6 ? ? 'expression tag'        -9  6  
1 9AUY HIS A 7   ? UNP Q2FJM6 ? ? 'expression tag'        -8  7  
1 9AUY GLY A 8   ? UNP Q2FJM6 ? ? 'expression tag'        -7  8  
1 9AUY GLU A 9   ? UNP Q2FJM6 ? ? 'expression tag'        -6  9  
1 9AUY ASN A 10  ? UNP Q2FJM6 ? ? 'expression tag'        -5  10 
1 9AUY LEU A 11  ? UNP Q2FJM6 ? ? 'expression tag'        -4  11 
1 9AUY TYR A 12  ? UNP Q2FJM6 ? ? 'expression tag'        -3  12 
1 9AUY PHE A 13  ? UNP Q2FJM6 ? ? 'expression tag'        -2  13 
1 9AUY GLN A 14  ? UNP Q2FJM6 ? ? 'expression tag'        -1  14 
1 9AUY GLY A 15  ? UNP Q2FJM6 ? ? 'expression tag'        0   15 
1 9AUY SER A 16  ? UNP Q2FJM6 ? ? 'expression tag'        1   16 
1 9AUY GLY A 107 ? UNP Q2FJM6 ? ? linker                  92  17 
1 9AUY GLY A 108 ? UNP Q2FJM6 ? ? linker                  93  18 
2 9AUY GLY A 378 ? UNP Q2FJM6 ? ? 'expression tag'        489 19 
2 9AUY ASN A 379 ? UNP Q2FJM6 ? ? 'expression tag'        490 20 
2 9AUY SER A 380 ? UNP Q2FJM6 ? ? 'expression tag'        491 21 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 16280 ? 
1 MORE         -89   ? 
1 'SSA (A^2)'  46820 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2,3,4 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z   1.0000000000  0.0000000000  0.0000000000 0.0000000000 0.0000000000  1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
2 'crystal symmetry operation' 2_555 -x,-y,z -1.0000000000 0.0000000000  0.0000000000 0.0000000000 0.0000000000  -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
3 'crystal symmetry operation' 3_555 -y,x,z  0.0000000000  -1.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
4 'crystal symmetry operation' 4_555 y,-x,z  0.0000000000  1.0000000000  0.0000000000 0.0000000000 -1.0000000000 0.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 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 THR A 27  ? ASP A 29  ? THR A 12  ASP A 14  5 ? 3  
HELX_P HELX_P2  AA2 LEU A 41  ? VAL A 45  ? LEU A 26  VAL A 30  5 ? 5  
HELX_P HELX_P3  AA3 GLU A 71  ? GLN A 81  ? GLU A 56  GLN A 66  1 ? 11 
HELX_P HELX_P4  AA4 GLY A 92  ? ARG A 105 ? GLY A 77  ARG A 90  1 ? 14 
HELX_P HELX_P5  AA5 ASP A 120 ? ALA A 131 ? ASP A 231 ALA A 242 1 ? 12 
HELX_P HELX_P6  AA6 SER A 145 ? TYR A 159 ? SER A 256 TYR A 270 1 ? 15 
HELX_P HELX_P7  AA7 THR A 171 ? GLY A 182 ? THR A 282 GLY A 293 1 ? 12 
HELX_P HELX_P8  AA8 THR A 197 ? GLY A 203 ? THR A 308 GLY A 314 1 ? 7  
HELX_P HELX_P9  AA9 PRO A 207 ? GLY A 223 ? PRO A 318 GLY A 334 1 ? 17 
HELX_P HELX_P10 AB1 PHE A 234 ? ALA A 244 ? PHE A 345 ALA A 355 1 ? 11 
HELX_P HELX_P11 AB2 GLY A 252 ? GLY A 257 ? GLY A 363 GLY A 368 1 ? 6  
HELX_P HELX_P12 AB3 SER A 281 ? GLU A 286 ? SER A 392 GLU A 397 1 ? 6  
HELX_P HELX_P13 AB4 ALA A 317 ? THR A 336 ? ALA A 428 THR A 447 1 ? 20 
HELX_P HELX_P14 AB5 ASP A 340 ? ALA A 348 ? ASP A 451 ALA A 459 1 ? 9  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          GLY 
_struct_mon_prot_cis.label_seq_id           167 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           GLY 
_struct_mon_prot_cis.auth_seq_id            278 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   ASN 
_struct_mon_prot_cis.pdbx_label_seq_id_2    168 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    ASN 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     279 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -0.05 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
AA3 ? 9 ? 
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 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 5 6 ? parallel      
AA3 6 7 ? parallel      
AA3 7 8 ? parallel      
AA3 8 9 ? 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 31  ? LEU A 33  ? VAL A 16  LEU A 18  
AA1 2 PHE A 350 ? ARG A 352 ? PHE A 461 ARG A 463 
AA2 1 VAL A 49  ? GLN A 50  ? VAL A 34  GLN A 35  
AA2 2 LYS A 56  ? LEU A 57  ? LYS A 41  LEU A 42  
AA3 1 VAL A 61  ? SER A 63  ? VAL A 46  SER A 48  
AA3 2 LEU A 84  ? ILE A 87  ? LEU A 69  ILE A 72  
AA3 3 ALA A 112 ? ILE A 115 ? ALA A 223 ILE A 226 
AA3 4 VAL A 135 ? ASP A 139 ? VAL A 246 ASP A 250 
AA3 5 THR A 163 ? VAL A 169 ? THR A 274 VAL A 280 
AA3 6 ILE A 185 ? VAL A 188 ? ILE A 296 VAL A 299 
AA3 7 ALA A 225 ? ASP A 229 ? ALA A 336 ASP A 340 
AA3 8 ALA A 248 ? LEU A 251 ? ALA A 359 LEU A 362 
AA3 9 VAL A 61  ? SER A 63  ? VAL A 46  SER A 48  
AA4 1 GLU A 266 ? PHE A 268 ? GLU A 377 PHE A 379 
AA4 2 ARG A 271 ? ARG A 277 ? ARG A 382 ARG A 388 
AA4 3 GLU A 309 ? ALA A 313 ? GLU A 420 ALA A 424 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 32  ? N LEU A 17  O THR A 351 ? O THR A 462 
AA2 1 2 N VAL A 49  ? N VAL A 34  O LEU A 57  ? O LEU A 42  
AA3 1 2 N SER A 63  ? N SER A 48  O LEU A 84  ? O LEU A 69  
AA3 2 3 N ILE A 87  ? N ILE A 72  O ALA A 114 ? O ALA A 225 
AA3 3 4 N ILE A 115 ? N ILE A 226 O VAL A 137 ? O VAL A 248 
AA3 4 5 N LEU A 136 ? N LEU A 247 O VAL A 165 ? O VAL A 276 
AA3 5 6 N ALA A 166 ? N ALA A 277 O LYS A 187 ? O LYS A 298 
AA3 6 7 N VAL A 188 ? N VAL A 299 O ILE A 227 ? O ILE A 338 
AA3 7 8 N ALA A 228 ? N ALA A 339 O ALA A 248 ? O ALA A 359 
AA3 8 9 O VAL A 249 ? O VAL A 360 N ILE A 62  ? N ILE A 47  
AA4 1 2 N GLU A 266 ? N GLU A 377 O TYR A 273 ? O TYR A 384 
AA4 2 3 N LYS A 274 ? N LYS A 385 O THR A 312 ? O THR A 423 
# 
_pdbx_entry_details.entry_id                   9AUY 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 VAL A 54  ? ? -131.78 -59.04 
2 1 SER A 91  ? ? -99.05  37.57  
3 1 SER A 91  ? ? -97.04  37.57  
4 1 ALA A 281 ? ? -146.97 10.61  
# 
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 -14 ? A MET 1   
2  1 Y 1 A HIS -13 ? A HIS 2   
3  1 Y 1 A HIS -12 ? A HIS 3   
4  1 Y 1 A HIS -11 ? A HIS 4   
5  1 Y 1 A HIS -10 ? A HIS 5   
6  1 Y 1 A HIS -9  ? A HIS 6   
7  1 Y 1 A HIS -8  ? A HIS 7   
8  1 Y 1 A GLY -7  ? A GLY 8   
9  1 Y 1 A GLU -6  ? A GLU 9   
10 1 Y 1 A ASN -5  ? A ASN 10  
11 1 Y 1 A LEU -4  ? A LEU 11  
12 1 Y 1 A TYR -3  ? A TYR 12  
13 1 Y 1 A PHE -2  ? A PHE 13  
14 1 Y 1 A GLN -1  ? A GLN 14  
15 1 Y 1 A LYS 398 ? A LYS 287 
16 1 Y 1 A GLY 399 ? A GLY 288 
17 1 Y 1 A SER 400 ? A SER 289 
18 1 Y 1 A ASN 401 ? A ASN 290 
19 1 Y 1 A ASP 402 ? A ASP 291 
20 1 Y 1 A ARG 403 ? A ARG 292 
21 1 Y 1 A TYR 404 ? A TYR 293 
22 1 Y 1 A PHE 405 ? A PHE 294 
23 1 Y 1 A GLN 406 ? A GLN 295 
24 1 Y 1 A GLU 407 ? A GLU 296 
25 1 Y 1 A ASP 408 ? A ASP 297 
26 1 Y 1 A LYS 409 ? A LYS 298 
27 1 Y 1 A ALA 410 ? A ALA 299 
28 1 Y 1 A PRO 411 ? A PRO 300 
29 1 Y 1 A LYS 412 ? A LYS 301 
30 1 Y 1 A ALA 467 ? A ALA 356 
31 1 Y 1 A GLY 468 ? A GLY 357 
32 1 Y 1 A LEU 469 ? A LEU 358 
33 1 Y 1 A ALA 470 ? A ALA 359 
34 1 Y 1 A GLU 471 ? A GLU 360 
35 1 Y 1 A SER 472 ? A SER 361 
36 1 Y 1 A HIS 473 ? A HIS 362 
37 1 Y 1 A PRO 474 ? A PRO 363 
38 1 Y 1 A HIS 475 ? A HIS 364 
39 1 Y 1 A ASN 476 ? A ASN 365 
40 1 Y 1 A ILE 477 ? A ILE 366 
41 1 Y 1 A GLN 478 ? A GLN 367 
42 1 Y 1 A ILE 479 ? A ILE 368 
43 1 Y 1 A THR 480 ? A THR 369 
44 1 Y 1 A LYS 481 ? A LYS 370 
45 1 Y 1 A GLU 482 ? A GLU 371 
46 1 Y 1 A SER 483 ? A SER 372 
47 1 Y 1 A PRO 484 ? A PRO 373 
48 1 Y 1 A ASN 485 ? A ASN 374 
49 1 Y 1 A TYR 486 ? A TYR 375 
50 1 Y 1 A SER 487 ? A SER 376 
51 1 Y 1 A PHE 488 ? A PHE 377 
52 1 Y 1 A GLY 489 ? A GLY 378 
53 1 Y 1 A ASN 490 ? A ASN 379 
54 1 Y 1 A SER 491 ? A SER 380 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASN N      N  N N 41  
ASN CA     C  N S 42  
ASN C      C  N N 43  
ASN O      O  N N 44  
ASN CB     C  N N 45  
ASN CG     C  N N 46  
ASN OD1    O  N N 47  
ASN ND2    N  N N 48  
ASN OXT    O  N N 49  
ASN H      H  N N 50  
ASN H2     H  N N 51  
ASN HA     H  N N 52  
ASN HB2    H  N N 53  
ASN HB3    H  N N 54  
ASN HD21   H  N N 55  
ASN HD22   H  N N 56  
ASN HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
CYS N      N  N N 74  
CYS CA     C  N R 75  
CYS C      C  N N 76  
CYS O      O  N N 77  
CYS CB     C  N N 78  
CYS SG     S  N N 79  
CYS OXT    O  N N 80  
CYS H      H  N N 81  
CYS H2     H  N N 82  
CYS HA     H  N N 83  
CYS HB2    H  N N 84  
CYS HB3    H  N N 85  
CYS HG     H  N N 86  
CYS HXT    H  N N 87  
GLN N      N  N N 88  
GLN CA     C  N S 89  
GLN C      C  N N 90  
GLN O      O  N N 91  
GLN CB     C  N N 92  
GLN CG     C  N N 93  
GLN CD     C  N N 94  
GLN OE1    O  N N 95  
GLN NE2    N  N N 96  
GLN OXT    O  N N 97  
GLN H      H  N N 98  
GLN H2     H  N N 99  
GLN HA     H  N N 100 
GLN HB2    H  N N 101 
GLN HB3    H  N N 102 
GLN HG2    H  N N 103 
GLN HG3    H  N N 104 
GLN HE21   H  N N 105 
GLN HE22   H  N N 106 
GLN HXT    H  N N 107 
GLU N      N  N N 108 
GLU CA     C  N S 109 
GLU C      C  N N 110 
GLU O      O  N N 111 
GLU CB     C  N N 112 
GLU CG     C  N N 113 
GLU CD     C  N N 114 
GLU OE1    O  N N 115 
GLU OE2    O  N N 116 
GLU OXT    O  N N 117 
GLU H      H  N N 118 
GLU H2     H  N N 119 
GLU HA     H  N N 120 
GLU HB2    H  N N 121 
GLU HB3    H  N N 122 
GLU HG2    H  N N 123 
GLU HG3    H  N N 124 
GLU HE2    H  N N 125 
GLU HXT    H  N N 126 
GLY N      N  N N 127 
GLY CA     C  N N 128 
GLY C      C  N N 129 
GLY O      O  N N 130 
GLY OXT    O  N N 131 
GLY H      H  N N 132 
GLY H2     H  N N 133 
GLY HA2    H  N N 134 
GLY HA3    H  N N 135 
GLY HXT    H  N N 136 
HIS N      N  N N 137 
HIS CA     C  N S 138 
HIS C      C  N N 139 
HIS O      O  N N 140 
HIS CB     C  N N 141 
HIS CG     C  Y N 142 
HIS ND1    N  Y N 143 
HIS CD2    C  Y N 144 
HIS CE1    C  Y N 145 
HIS NE2    N  Y N 146 
HIS OXT    O  N N 147 
HIS H      H  N N 148 
HIS H2     H  N N 149 
HIS HA     H  N N 150 
HIS HB2    H  N N 151 
HIS HB3    H  N N 152 
HIS HD1    H  N N 153 
HIS HD2    H  N N 154 
HIS HE1    H  N N 155 
HIS HE2    H  N N 156 
HIS HXT    H  N N 157 
HOH O      O  N N 158 
HOH H1     H  N N 159 
HOH H2     H  N N 160 
ILE N      N  N N 161 
ILE CA     C  N S 162 
ILE C      C  N N 163 
ILE O      O  N N 164 
ILE CB     C  N S 165 
ILE CG1    C  N N 166 
ILE CG2    C  N N 167 
ILE CD1    C  N N 168 
ILE OXT    O  N N 169 
ILE H      H  N N 170 
ILE H2     H  N N 171 
ILE HA     H  N N 172 
ILE HB     H  N N 173 
ILE HG12   H  N N 174 
ILE HG13   H  N N 175 
ILE HG21   H  N N 176 
ILE HG22   H  N N 177 
ILE HG23   H  N N 178 
ILE HD11   H  N N 179 
ILE HD12   H  N N 180 
ILE HD13   H  N N 181 
ILE HXT    H  N N 182 
IMP P      P  N N 183 
IMP O1P    O  N N 184 
IMP O2P    O  N N 185 
IMP O3P    O  N N 186 
IMP "O5'"  O  N N 187 
IMP "C5'"  C  N N 188 
IMP "C4'"  C  N R 189 
IMP "O4'"  O  N N 190 
IMP "C3'"  C  N S 191 
IMP "O3'"  O  N N 192 
IMP "C2'"  C  N R 193 
IMP "O2'"  O  N N 194 
IMP "C1'"  C  N R 195 
IMP N9     N  Y N 196 
IMP C8     C  Y N 197 
IMP N7     N  Y N 198 
IMP C5     C  Y N 199 
IMP C6     C  N N 200 
IMP O6     O  N N 201 
IMP N1     N  N N 202 
IMP C2     C  N N 203 
IMP N3     N  N N 204 
IMP C4     C  Y N 205 
IMP HOP2   H  N N 206 
IMP HOP3   H  N N 207 
IMP "H5'1" H  N N 208 
IMP "H5'2" H  N N 209 
IMP "H4'"  H  N N 210 
IMP "H3'"  H  N N 211 
IMP "HO3'" H  N N 212 
IMP "H2'"  H  N N 213 
IMP "HO2'" H  N N 214 
IMP "H1'"  H  N N 215 
IMP H8     H  N N 216 
IMP HN1    H  N N 217 
IMP H2     H  N N 218 
LEU N      N  N N 219 
LEU CA     C  N S 220 
LEU C      C  N N 221 
LEU O      O  N N 222 
LEU CB     C  N N 223 
LEU CG     C  N N 224 
LEU CD1    C  N N 225 
LEU CD2    C  N N 226 
LEU OXT    O  N N 227 
LEU H      H  N N 228 
LEU H2     H  N N 229 
LEU HA     H  N N 230 
LEU HB2    H  N N 231 
LEU HB3    H  N N 232 
LEU HG     H  N N 233 
LEU HD11   H  N N 234 
LEU HD12   H  N N 235 
LEU HD13   H  N N 236 
LEU HD21   H  N N 237 
LEU HD22   H  N N 238 
LEU HD23   H  N N 239 
LEU HXT    H  N N 240 
LYS N      N  N N 241 
LYS CA     C  N S 242 
LYS C      C  N N 243 
LYS O      O  N N 244 
LYS CB     C  N N 245 
LYS CG     C  N N 246 
LYS CD     C  N N 247 
LYS CE     C  N N 248 
LYS NZ     N  N N 249 
LYS OXT    O  N N 250 
LYS H      H  N N 251 
LYS H2     H  N N 252 
LYS HA     H  N N 253 
LYS HB2    H  N N 254 
LYS HB3    H  N N 255 
LYS HG2    H  N N 256 
LYS HG3    H  N N 257 
LYS HD2    H  N N 258 
LYS HD3    H  N N 259 
LYS HE2    H  N N 260 
LYS HE3    H  N N 261 
LYS HZ1    H  N N 262 
LYS HZ2    H  N N 263 
LYS HZ3    H  N N 264 
LYS HXT    H  N N 265 
MET N      N  N N 266 
MET CA     C  N S 267 
MET C      C  N N 268 
MET O      O  N N 269 
MET CB     C  N N 270 
MET CG     C  N N 271 
MET SD     S  N N 272 
MET CE     C  N N 273 
MET OXT    O  N N 274 
MET H      H  N N 275 
MET H2     H  N N 276 
MET HA     H  N N 277 
MET HB2    H  N N 278 
MET HB3    H  N N 279 
MET HG2    H  N N 280 
MET HG3    H  N N 281 
MET HE1    H  N N 282 
MET HE2    H  N N 283 
MET HE3    H  N N 284 
MET HXT    H  N N 285 
PHE N      N  N N 286 
PHE CA     C  N S 287 
PHE C      C  N N 288 
PHE O      O  N N 289 
PHE CB     C  N N 290 
PHE CG     C  Y N 291 
PHE CD1    C  Y N 292 
PHE CD2    C  Y N 293 
PHE CE1    C  Y N 294 
PHE CE2    C  Y N 295 
PHE CZ     C  Y N 296 
PHE OXT    O  N N 297 
PHE H      H  N N 298 
PHE H2     H  N N 299 
PHE HA     H  N N 300 
PHE HB2    H  N N 301 
PHE HB3    H  N N 302 
PHE HD1    H  N N 303 
PHE HD2    H  N N 304 
PHE HE1    H  N N 305 
PHE HE2    H  N N 306 
PHE HZ     H  N N 307 
PHE HXT    H  N N 308 
PRO N      N  N N 309 
PRO CA     C  N S 310 
PRO C      C  N N 311 
PRO O      O  N N 312 
PRO CB     C  N N 313 
PRO CG     C  N N 314 
PRO CD     C  N N 315 
PRO OXT    O  N N 316 
PRO H      H  N N 317 
PRO HA     H  N N 318 
PRO HB2    H  N N 319 
PRO HB3    H  N N 320 
PRO HG2    H  N N 321 
PRO HG3    H  N N 322 
PRO HD2    H  N N 323 
PRO HD3    H  N N 324 
PRO HXT    H  N N 325 
SER N      N  N N 326 
SER CA     C  N S 327 
SER C      C  N N 328 
SER O      O  N N 329 
SER CB     C  N N 330 
SER OG     O  N N 331 
SER OXT    O  N N 332 
SER H      H  N N 333 
SER H2     H  N N 334 
SER HA     H  N N 335 
SER HB2    H  N N 336 
SER HB3    H  N N 337 
SER HG     H  N N 338 
SER HXT    H  N N 339 
THR N      N  N N 340 
THR CA     C  N S 341 
THR C      C  N N 342 
THR O      O  N N 343 
THR CB     C  N R 344 
THR OG1    O  N N 345 
THR CG2    C  N N 346 
THR OXT    O  N N 347 
THR H      H  N N 348 
THR H2     H  N N 349 
THR HA     H  N N 350 
THR HB     H  N N 351 
THR HG1    H  N N 352 
THR HG21   H  N N 353 
THR HG22   H  N N 354 
THR HG23   H  N N 355 
THR HXT    H  N N 356 
TRP N      N  N N 357 
TRP CA     C  N S 358 
TRP C      C  N N 359 
TRP O      O  N N 360 
TRP CB     C  N N 361 
TRP CG     C  Y N 362 
TRP CD1    C  Y N 363 
TRP CD2    C  Y N 364 
TRP NE1    N  Y N 365 
TRP CE2    C  Y N 366 
TRP CE3    C  Y N 367 
TRP CZ2    C  Y N 368 
TRP CZ3    C  Y N 369 
TRP CH2    C  Y N 370 
TRP OXT    O  N N 371 
TRP H      H  N N 372 
TRP H2     H  N N 373 
TRP HA     H  N N 374 
TRP HB2    H  N N 375 
TRP HB3    H  N N 376 
TRP HD1    H  N N 377 
TRP HE1    H  N N 378 
TRP HE3    H  N N 379 
TRP HZ2    H  N N 380 
TRP HZ3    H  N N 381 
TRP HH2    H  N N 382 
TRP HXT    H  N N 383 
TYR N      N  N N 384 
TYR CA     C  N S 385 
TYR C      C  N N 386 
TYR O      O  N N 387 
TYR CB     C  N N 388 
TYR CG     C  Y N 389 
TYR CD1    C  Y N 390 
TYR CD2    C  Y N 391 
TYR CE1    C  Y N 392 
TYR CE2    C  Y N 393 
TYR CZ     C  Y N 394 
TYR OH     O  N N 395 
TYR OXT    O  N N 396 
TYR H      H  N N 397 
TYR H2     H  N N 398 
TYR HA     H  N N 399 
TYR HB2    H  N N 400 
TYR HB3    H  N N 401 
TYR HD1    H  N N 402 
TYR HD2    H  N N 403 
TYR HE1    H  N N 404 
TYR HE2    H  N N 405 
TYR HH     H  N N 406 
TYR HXT    H  N N 407 
VAL N      N  N N 408 
VAL CA     C  N S 409 
VAL C      C  N N 410 
VAL O      O  N N 411 
VAL CB     C  N N 412 
VAL CG1    C  N N 413 
VAL CG2    C  N N 414 
VAL OXT    O  N N 415 
VAL H      H  N N 416 
VAL H2     H  N N 417 
VAL HA     H  N N 418 
VAL HB     H  N N 419 
VAL HG11   H  N N 420 
VAL HG12   H  N N 421 
VAL HG13   H  N N 422 
VAL HG21   H  N N 423 
VAL HG22   H  N N 424 
VAL HG23   H  N N 425 
VAL HXT    H  N N 426 
VOA C4     C  N N 427 
VOA C7     C  Y N 428 
VOA C8     C  Y N 429 
VOA C9     C  Y N 430 
VOA C10    C  Y N 431 
VOA C12    C  Y N 432 
VOA C1     C  N N 433 
VOA C15    C  Y N 434 
VOA C16    C  Y N 435 
VOA C17    C  Y N 436 
VOA C18    C  Y N 437 
VOA C19    C  Y N 438 
VOA C2     C  N S 439 
VOA C20    C  Y N 440 
VOA C21    C  Y N 441 
VOA C22    C  Y N 442 
VOA C23    C  Y N 443 
VOA C25    C  N N 444 
VOA C27    C  N N 445 
VOA C28    C  N N 446 
VOA N11    N  Y N 447 
VOA N14    N  N N 448 
VOA N24    N  Y N 449 
VOA N6     N  N N 450 
VOA O26    O  N N 451 
VOA O5     O  N N 452 
VOA CL13   CL N N 453 
VOA H1     H  N N 454 
VOA H2     H  N N 455 
VOA H4     H  N N 456 
VOA H7     H  N N 457 
VOA H6     H  N N 458 
VOA H5     H  N N 459 
VOA H8     H  N N 460 
VOA H9     H  N N 461 
VOA H3     H  N N 462 
VOA H10    H  N N 463 
VOA H11    H  N N 464 
VOA H13    H  N N 465 
VOA H12    H  N N 466 
VOA H14    H  N N 467 
VOA H15    H  N N 468 
VOA H17    H  N N 469 
VOA H16    H  N N 470 
VOA H18    H  N N 471 
VOA H19    H  N N 472 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
GLN N     CA     sing N N 83  
GLN N     H      sing N N 84  
GLN N     H2     sing N N 85  
GLN CA    C      sing N N 86  
GLN CA    CB     sing N N 87  
GLN CA    HA     sing N N 88  
GLN C     O      doub N N 89  
GLN C     OXT    sing N N 90  
GLN CB    CG     sing N N 91  
GLN CB    HB2    sing N N 92  
GLN CB    HB3    sing N N 93  
GLN CG    CD     sing N N 94  
GLN CG    HG2    sing N N 95  
GLN CG    HG3    sing N N 96  
GLN CD    OE1    doub N N 97  
GLN CD    NE2    sing N N 98  
GLN NE2   HE21   sing N N 99  
GLN NE2   HE22   sing N N 100 
GLN OXT   HXT    sing N N 101 
GLU N     CA     sing N N 102 
GLU N     H      sing N N 103 
GLU N     H2     sing N N 104 
GLU CA    C      sing N N 105 
GLU CA    CB     sing N N 106 
GLU CA    HA     sing N N 107 
GLU C     O      doub N N 108 
GLU C     OXT    sing N N 109 
GLU CB    CG     sing N N 110 
GLU CB    HB2    sing N N 111 
GLU CB    HB3    sing N N 112 
GLU CG    CD     sing N N 113 
GLU CG    HG2    sing N N 114 
GLU CG    HG3    sing N N 115 
GLU CD    OE1    doub N N 116 
GLU CD    OE2    sing N N 117 
GLU OE2   HE2    sing N N 118 
GLU OXT   HXT    sing N N 119 
GLY N     CA     sing N N 120 
GLY N     H      sing N N 121 
GLY N     H2     sing N N 122 
GLY CA    C      sing N N 123 
GLY CA    HA2    sing N N 124 
GLY CA    HA3    sing N N 125 
GLY C     O      doub N N 126 
GLY C     OXT    sing N N 127 
GLY OXT   HXT    sing N N 128 
HIS N     CA     sing N N 129 
HIS N     H      sing N N 130 
HIS N     H2     sing N N 131 
HIS CA    C      sing N N 132 
HIS CA    CB     sing N N 133 
HIS CA    HA     sing N N 134 
HIS C     O      doub N N 135 
HIS C     OXT    sing N N 136 
HIS CB    CG     sing N N 137 
HIS CB    HB2    sing N N 138 
HIS CB    HB3    sing N N 139 
HIS CG    ND1    sing Y N 140 
HIS CG    CD2    doub Y N 141 
HIS ND1   CE1    doub Y N 142 
HIS ND1   HD1    sing N N 143 
HIS CD2   NE2    sing Y N 144 
HIS CD2   HD2    sing N N 145 
HIS CE1   NE2    sing Y N 146 
HIS CE1   HE1    sing N N 147 
HIS NE2   HE2    sing N N 148 
HIS OXT   HXT    sing N N 149 
HOH O     H1     sing N N 150 
HOH O     H2     sing N N 151 
ILE N     CA     sing N N 152 
ILE N     H      sing N N 153 
ILE N     H2     sing N N 154 
ILE CA    C      sing N N 155 
ILE CA    CB     sing N N 156 
ILE CA    HA     sing N N 157 
ILE C     O      doub N N 158 
ILE C     OXT    sing N N 159 
ILE CB    CG1    sing N N 160 
ILE CB    CG2    sing N N 161 
ILE CB    HB     sing N N 162 
ILE CG1   CD1    sing N N 163 
ILE CG1   HG12   sing N N 164 
ILE CG1   HG13   sing N N 165 
ILE CG2   HG21   sing N N 166 
ILE CG2   HG22   sing N N 167 
ILE CG2   HG23   sing N N 168 
ILE CD1   HD11   sing N N 169 
ILE CD1   HD12   sing N N 170 
ILE CD1   HD13   sing N N 171 
ILE OXT   HXT    sing N N 172 
IMP P     O1P    doub N N 173 
IMP P     O2P    sing N N 174 
IMP P     O3P    sing N N 175 
IMP P     "O5'"  sing N N 176 
IMP O2P   HOP2   sing N N 177 
IMP O3P   HOP3   sing N N 178 
IMP "O5'" "C5'"  sing N N 179 
IMP "C5'" "C4'"  sing N N 180 
IMP "C5'" "H5'1" sing N N 181 
IMP "C5'" "H5'2" sing N N 182 
IMP "C4'" "O4'"  sing N N 183 
IMP "C4'" "C3'"  sing N N 184 
IMP "C4'" "H4'"  sing N N 185 
IMP "O4'" "C1'"  sing N N 186 
IMP "C3'" "O3'"  sing N N 187 
IMP "C3'" "C2'"  sing N N 188 
IMP "C3'" "H3'"  sing N N 189 
IMP "O3'" "HO3'" sing N N 190 
IMP "C2'" "O2'"  sing N N 191 
IMP "C2'" "C1'"  sing N N 192 
IMP "C2'" "H2'"  sing N N 193 
IMP "O2'" "HO2'" sing N N 194 
IMP "C1'" N9     sing N N 195 
IMP "C1'" "H1'"  sing N N 196 
IMP N9    C8     sing Y N 197 
IMP N9    C4     sing Y N 198 
IMP C8    N7     doub Y N 199 
IMP C8    H8     sing N N 200 
IMP N7    C5     sing Y N 201 
IMP C5    C6     sing N N 202 
IMP C5    C4     doub Y N 203 
IMP C6    O6     doub N N 204 
IMP C6    N1     sing N N 205 
IMP N1    C2     sing N N 206 
IMP N1    HN1    sing N N 207 
IMP C2    N3     doub N N 208 
IMP C2    H2     sing N N 209 
IMP N3    C4     sing N N 210 
LEU N     CA     sing N N 211 
LEU N     H      sing N N 212 
LEU N     H2     sing N N 213 
LEU CA    C      sing N N 214 
LEU CA    CB     sing N N 215 
LEU CA    HA     sing N N 216 
LEU C     O      doub N N 217 
LEU C     OXT    sing N N 218 
LEU CB    CG     sing N N 219 
LEU CB    HB2    sing N N 220 
LEU CB    HB3    sing N N 221 
LEU CG    CD1    sing N N 222 
LEU CG    CD2    sing N N 223 
LEU CG    HG     sing N N 224 
LEU CD1   HD11   sing N N 225 
LEU CD1   HD12   sing N N 226 
LEU CD1   HD13   sing N N 227 
LEU CD2   HD21   sing N N 228 
LEU CD2   HD22   sing N N 229 
LEU CD2   HD23   sing N N 230 
LEU OXT   HXT    sing N N 231 
LYS N     CA     sing N N 232 
LYS N     H      sing N N 233 
LYS N     H2     sing N N 234 
LYS CA    C      sing N N 235 
LYS CA    CB     sing N N 236 
LYS CA    HA     sing N N 237 
LYS C     O      doub N N 238 
LYS C     OXT    sing N N 239 
LYS CB    CG     sing N N 240 
LYS CB    HB2    sing N N 241 
LYS CB    HB3    sing N N 242 
LYS CG    CD     sing N N 243 
LYS CG    HG2    sing N N 244 
LYS CG    HG3    sing N N 245 
LYS CD    CE     sing N N 246 
LYS CD    HD2    sing N N 247 
LYS CD    HD3    sing N N 248 
LYS CE    NZ     sing N N 249 
LYS CE    HE2    sing N N 250 
LYS CE    HE3    sing N N 251 
LYS NZ    HZ1    sing N N 252 
LYS NZ    HZ2    sing N N 253 
LYS NZ    HZ3    sing N N 254 
LYS OXT   HXT    sing N N 255 
MET N     CA     sing N N 256 
MET N     H      sing N N 257 
MET N     H2     sing N N 258 
MET CA    C      sing N N 259 
MET CA    CB     sing N N 260 
MET CA    HA     sing N N 261 
MET C     O      doub N N 262 
MET C     OXT    sing N N 263 
MET CB    CG     sing N N 264 
MET CB    HB2    sing N N 265 
MET CB    HB3    sing N N 266 
MET CG    SD     sing N N 267 
MET CG    HG2    sing N N 268 
MET CG    HG3    sing N N 269 
MET SD    CE     sing N N 270 
MET CE    HE1    sing N N 271 
MET CE    HE2    sing N N 272 
MET CE    HE3    sing N N 273 
MET OXT   HXT    sing N N 274 
PHE N     CA     sing N N 275 
PHE N     H      sing N N 276 
PHE N     H2     sing N N 277 
PHE CA    C      sing N N 278 
PHE CA    CB     sing N N 279 
PHE CA    HA     sing N N 280 
PHE C     O      doub N N 281 
PHE C     OXT    sing N N 282 
PHE CB    CG     sing N N 283 
PHE CB    HB2    sing N N 284 
PHE CB    HB3    sing N N 285 
PHE CG    CD1    doub Y N 286 
PHE CG    CD2    sing Y N 287 
PHE CD1   CE1    sing Y N 288 
PHE CD1   HD1    sing N N 289 
PHE CD2   CE2    doub Y N 290 
PHE CD2   HD2    sing N N 291 
PHE CE1   CZ     doub Y N 292 
PHE CE1   HE1    sing N N 293 
PHE CE2   CZ     sing Y N 294 
PHE CE2   HE2    sing N N 295 
PHE CZ    HZ     sing N N 296 
PHE OXT   HXT    sing N N 297 
PRO N     CA     sing N N 298 
PRO N     CD     sing N N 299 
PRO N     H      sing N N 300 
PRO CA    C      sing N N 301 
PRO CA    CB     sing N N 302 
PRO CA    HA     sing N N 303 
PRO C     O      doub N N 304 
PRO C     OXT    sing N N 305 
PRO CB    CG     sing N N 306 
PRO CB    HB2    sing N N 307 
PRO CB    HB3    sing N N 308 
PRO CG    CD     sing N N 309 
PRO CG    HG2    sing N N 310 
PRO CG    HG3    sing N N 311 
PRO CD    HD2    sing N N 312 
PRO CD    HD3    sing N N 313 
PRO OXT   HXT    sing N N 314 
SER N     CA     sing N N 315 
SER N     H      sing N N 316 
SER N     H2     sing N N 317 
SER CA    C      sing N N 318 
SER CA    CB     sing N N 319 
SER CA    HA     sing N N 320 
SER C     O      doub N N 321 
SER C     OXT    sing N N 322 
SER CB    OG     sing N N 323 
SER CB    HB2    sing N N 324 
SER CB    HB3    sing N N 325 
SER OG    HG     sing N N 326 
SER OXT   HXT    sing N N 327 
THR N     CA     sing N N 328 
THR N     H      sing N N 329 
THR N     H2     sing N N 330 
THR CA    C      sing N N 331 
THR CA    CB     sing N N 332 
THR CA    HA     sing N N 333 
THR C     O      doub N N 334 
THR C     OXT    sing N N 335 
THR CB    OG1    sing N N 336 
THR CB    CG2    sing N N 337 
THR CB    HB     sing N N 338 
THR OG1   HG1    sing N N 339 
THR CG2   HG21   sing N N 340 
THR CG2   HG22   sing N N 341 
THR CG2   HG23   sing N N 342 
THR OXT   HXT    sing N N 343 
TRP N     CA     sing N N 344 
TRP N     H      sing N N 345 
TRP N     H2     sing N N 346 
TRP CA    C      sing N N 347 
TRP CA    CB     sing N N 348 
TRP CA    HA     sing N N 349 
TRP C     O      doub N N 350 
TRP C     OXT    sing N N 351 
TRP CB    CG     sing N N 352 
TRP CB    HB2    sing N N 353 
TRP CB    HB3    sing N N 354 
TRP CG    CD1    doub Y N 355 
TRP CG    CD2    sing Y N 356 
TRP CD1   NE1    sing Y N 357 
TRP CD1   HD1    sing N N 358 
TRP CD2   CE2    doub Y N 359 
TRP CD2   CE3    sing Y N 360 
TRP NE1   CE2    sing Y N 361 
TRP NE1   HE1    sing N N 362 
TRP CE2   CZ2    sing Y N 363 
TRP CE3   CZ3    doub Y N 364 
TRP CE3   HE3    sing N N 365 
TRP CZ2   CH2    doub Y N 366 
TRP CZ2   HZ2    sing N N 367 
TRP CZ3   CH2    sing Y N 368 
TRP CZ3   HZ3    sing N N 369 
TRP CH2   HH2    sing N N 370 
TRP OXT   HXT    sing N N 371 
TYR N     CA     sing N N 372 
TYR N     H      sing N N 373 
TYR N     H2     sing N N 374 
TYR CA    C      sing N N 375 
TYR CA    CB     sing N N 376 
TYR CA    HA     sing N N 377 
TYR C     O      doub N N 378 
TYR C     OXT    sing N N 379 
TYR CB    CG     sing N N 380 
TYR CB    HB2    sing N N 381 
TYR CB    HB3    sing N N 382 
TYR CG    CD1    doub Y N 383 
TYR CG    CD2    sing Y N 384 
TYR CD1   CE1    sing Y N 385 
TYR CD1   HD1    sing N N 386 
TYR CD2   CE2    doub Y N 387 
TYR CD2   HD2    sing N N 388 
TYR CE1   CZ     doub Y N 389 
TYR CE1   HE1    sing N N 390 
TYR CE2   CZ     sing Y N 391 
TYR CE2   HE2    sing N N 392 
TYR CZ    OH     sing N N 393 
TYR OH    HH     sing N N 394 
TYR OXT   HXT    sing N N 395 
VAL N     CA     sing N N 396 
VAL N     H      sing N N 397 
VAL N     H2     sing N N 398 
VAL CA    C      sing N N 399 
VAL CA    CB     sing N N 400 
VAL CA    HA     sing N N 401 
VAL C     O      doub N N 402 
VAL C     OXT    sing N N 403 
VAL CB    CG1    sing N N 404 
VAL CB    CG2    sing N N 405 
VAL CB    HB     sing N N 406 
VAL CG1   HG11   sing N N 407 
VAL CG1   HG12   sing N N 408 
VAL CG1   HG13   sing N N 409 
VAL CG2   HG21   sing N N 410 
VAL CG2   HG22   sing N N 411 
VAL CG2   HG23   sing N N 412 
VAL OXT   HXT    sing N N 413 
VOA C1    C2     sing N N 414 
VOA N14   C15    sing N N 415 
VOA N14   C2     sing N N 416 
VOA C16   C17    doub Y N 417 
VOA C16   C15    sing Y N 418 
VOA C17   C18    sing Y N 419 
VOA C15   C20    doub Y N 420 
VOA C2    C4     sing N N 421 
VOA C20   C19    sing Y N 422 
VOA C18   N24    doub Y N 423 
VOA C18   C19    sing Y N 424 
VOA N24   C23    sing Y N 425 
VOA C19   C21    doub Y N 426 
VOA C4    O5     doub N N 427 
VOA C4    N6     sing N N 428 
VOA C23   C22    doub Y N 429 
VOA N6    C7     sing N N 430 
VOA C21   C22    sing Y N 431 
VOA C21   C28    sing N N 432 
VOA C22   C25    sing N N 433 
VOA C28   C27    sing N N 434 
VOA C7    C12    doub Y N 435 
VOA C7    C8     sing Y N 436 
VOA C25   O26    sing N N 437 
VOA O26   C27    sing N N 438 
VOA C12   N11    sing Y N 439 
VOA C8    C9     doub Y N 440 
VOA N11   C10    doub Y N 441 
VOA C9    C10    sing Y N 442 
VOA C10   CL13   sing N N 443 
VOA C8    H1     sing N N 444 
VOA C9    H2     sing N N 445 
VOA C12   H4     sing N N 446 
VOA C1    H7     sing N N 447 
VOA C1    H6     sing N N 448 
VOA C1    H5     sing N N 449 
VOA C16   H8     sing N N 450 
VOA C17   H9     sing N N 451 
VOA C2    H3     sing N N 452 
VOA C20   H10    sing N N 453 
VOA C23   H11    sing N N 454 
VOA C25   H13    sing N N 455 
VOA C25   H12    sing N N 456 
VOA C27   H14    sing N N 457 
VOA C27   H15    sing N N 458 
VOA C28   H17    sing N N 459 
VOA C28   H16    sing N N 460 
VOA N14   H18    sing N N 461 
VOA N6    H19    sing N N 462 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'in-house model' 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.type             'experimental model' 
# 
_atom_sites.entry_id                    9AUY 
_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]   0.009590 
_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]   0.009590 
_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]   0.015649 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
H  
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N      . GLY A 1 15  ? -15.753 -11.861 -42.954 1.00 58.16  ?  0   GLY A N      1 
ATOM   2    C  CA     . GLY A 1 15  ? -16.488 -12.780 -42.090 1.00 57.08  ?  0   GLY A CA     1 
ATOM   3    C  C      . GLY A 1 15  ? -16.501 -12.359 -40.632 1.00 57.77  ?  0   GLY A C      1 
ATOM   4    O  O      . GLY A 1 15  ? -15.555 -11.707 -40.168 1.00 55.72  ?  0   GLY A O      1 
ATOM   5    N  N      A SER A 1 16  ? -17.576 -12.741 -39.902 0.54 53.25  ?  1   SER A N      1 
ATOM   6    N  N      B SER A 1 16  ? -17.575 -12.727 -39.901 0.46 53.43  ?  1   SER A N      1 
ATOM   7    C  CA     A SER A 1 16  ? -17.781 -12.453 -38.474 0.54 52.08  ?  1   SER A CA     1 
ATOM   8    C  CA     B SER A 1 16  ? -17.756 -12.411 -38.477 0.46 52.41  ?  1   SER A CA     1 
ATOM   9    C  C      A SER A 1 16  ? -16.653 -13.006 -37.606 0.54 52.05  ?  1   SER A C      1 
ATOM   10   C  C      B SER A 1 16  ? -16.643 -12.997 -37.602 0.46 52.30  ?  1   SER A C      1 
ATOM   11   O  O      A SER A 1 16  ? -16.250 -12.357 -36.637 0.54 51.07  ?  1   SER A O      1 
ATOM   12   O  O      B SER A 1 16  ? -16.241 -12.361 -36.624 0.46 51.41  ?  1   SER A O      1 
ATOM   13   C  CB     A SER A 1 16  ? -19.121 -13.008 -37.998 0.54 54.70  ?  1   SER A CB     1 
ATOM   14   C  CB     B SER A 1 16  ? -19.121 -12.886 -37.988 0.46 55.78  ?  1   SER A CB     1 
ATOM   15   O  OG     A SER A 1 16  ? -20.152 -12.045 -38.133 0.54 60.25  ?  1   SER A OG     1 
ATOM   16   O  OG     B SER A 1 16  ? -19.242 -14.289 -38.136 0.46 63.81  ?  1   SER A OG     1 
ATOM   17   N  N      . TRP A 1 17  ? -16.139 -14.193 -37.971 1.00 46.58  ?  2   TRP A N      1 
ATOM   18   C  CA     . TRP A 1 17  ? -15.064 -14.889 -37.279 1.00 45.70  ?  2   TRP A CA     1 
ATOM   19   C  C      . TRP A 1 17  ? -13.776 -14.103 -37.364 1.00 50.32  ?  2   TRP A C      1 
ATOM   20   O  O      . TRP A 1 17  ? -13.122 -13.890 -36.347 1.00 49.24  ?  2   TRP A O      1 
ATOM   21   C  CB     . TRP A 1 17  ? -14.827 -16.291 -37.872 1.00 43.56  ?  2   TRP A CB     1 
ATOM   22   C  CG     . TRP A 1 17  ? -13.789 -17.071 -37.119 1.00 43.68  ?  2   TRP A CG     1 
ATOM   23   C  CD1    . TRP A 1 17  ? -12.488 -17.290 -37.480 1.00 46.21  ?  2   TRP A CD1    1 
ATOM   24   C  CD2    . TRP A 1 17  ? -13.965 -17.706 -35.850 1.00 43.46  ?  2   TRP A CD2    1 
ATOM   25   N  NE1    . TRP A 1 17  ? -11.842 -18.015 -36.507 1.00 44.94  ?  2   TRP A NE1    1 
ATOM   26   C  CE2    . TRP A 1 17  ? -12.726 -18.282 -35.491 1.00 46.80  ?  2   TRP A CE2    1 
ATOM   27   C  CE3    . TRP A 1 17  ? -15.061 -17.845 -34.976 1.00 44.98  ?  2   TRP A CE3    1 
ATOM   28   C  CZ2    . TRP A 1 17  ? -12.538 -18.958 -34.279 1.00 46.67  ?  2   TRP A CZ2    1 
ATOM   29   C  CZ3    . TRP A 1 17  ? -14.872 -18.513 -33.770 1.00 46.66  ?  2   TRP A CZ3    1 
ATOM   30   C  CH2    . TRP A 1 17  ? -13.624 -19.056 -33.431 1.00 47.09  ?  2   TRP A CH2    1 
ATOM   31   N  N      . GLU A 1 18  ? -13.415 -13.686 -38.584 1.00 45.85  ?  3   GLU A N      1 
ATOM   32   C  CA     . GLU A 1 18  ? -12.178 -12.959 -38.879 1.00 44.67  ?  3   GLU A CA     1 
ATOM   33   C  C      . GLU A 1 18  ? -12.116 -11.584 -38.236 1.00 45.39  ?  3   GLU A C      1 
ATOM   34   O  O      . GLU A 1 18  ? -11.016 -11.103 -37.960 1.00 45.46  ?  3   GLU A O      1 
ATOM   35   C  CB     . GLU A 1 18  ? -11.991 -12.824 -40.407 1.00 45.91  ?  3   GLU A CB     1 
ATOM   36   C  CG     . GLU A 1 18  ? -11.610 -14.116 -41.113 1.00 56.42  ?  3   GLU A CG     1 
ATOM   37   C  CD     . GLU A 1 18  ? -12.679 -15.191 -41.204 1.00 71.66  ?  3   GLU A CD     1 
ATOM   38   O  OE1    . GLU A 1 18  ? -13.882 -14.847 -41.285 1.00 56.76  ?  3   GLU A OE1    1 
ATOM   39   O  OE2    . GLU A 1 18  ? -12.309 -16.386 -41.153 1.00 60.86  -1 3   GLU A OE2    1 
ATOM   40   N  N      . SER A 1 19  ? -13.275 -10.932 -38.051 1.00 40.79  ?  4   SER A N      1 
ATOM   41   C  CA     . SER A 1 19  ? -13.378 -9.565  -37.524 1.00 39.33  ?  4   SER A CA     1 
ATOM   42   C  C      . SER A 1 19  ? -13.564 -9.475  -36.002 1.00 42.82  ?  4   SER A C      1 
ATOM   43   O  O      . SER A 1 19  ? -13.642 -8.362  -35.457 1.00 44.49  ?  4   SER A O      1 
ATOM   44   C  CB     . SER A 1 19  ? -14.496 -8.815  -38.238 1.00 41.02  ?  4   SER A CB     1 
ATOM   45   O  OG     . SER A 1 19  ? -15.770 -9.297  -37.841 1.00 48.51  ?  4   SER A OG     1 
ATOM   46   N  N      . LYS A 1 20  ? -13.620 -10.625 -35.323 1.00 38.43  ?  5   LYS A N      1 
ATOM   47   C  CA     . LYS A 1 20  ? -13.825 -10.745 -33.871 1.00 38.87  ?  5   LYS A CA     1 
ATOM   48   C  C      . LYS A 1 20  ? -13.099 -9.718  -33.016 1.00 42.85  ?  5   LYS A C      1 
ATOM   49   O  O      . LYS A 1 20  ? -13.699 -9.147  -32.120 1.00 44.23  ?  5   LYS A O      1 
ATOM   50   C  CB     . LYS A 1 20  ? -13.425 -12.137 -33.397 1.00 42.13  ?  5   LYS A CB     1 
ATOM   51   C  CG     . LYS A 1 20  ? -14.585 -13.099 -33.400 1.00 56.51  ?  5   LYS A CG     1 
ATOM   52   C  CD     . LYS A 1 20  ? -14.451 -14.183 -32.341 1.00 52.07  ?  5   LYS A CD     1 
ATOM   53   C  CE     . LYS A 1 20  ? -15.598 -15.175 -32.487 1.00 46.17  ?  5   LYS A CE     1 
ATOM   54   N  NZ     . LYS A 1 20  ? -16.909 -14.633 -31.991 1.00 41.12  1  5   LYS A NZ     1 
ATOM   55   N  N      . PHE A 1 21  ? -11.813 -9.498  -33.285 1.00 40.86  ?  6   PHE A N      1 
ATOM   56   C  CA     . PHE A 1 21  ? -10.937 -8.607  -32.504 1.00 38.30  ?  6   PHE A CA     1 
ATOM   57   C  C      . PHE A 1 21  ? -10.458 -7.374  -33.280 1.00 41.87  ?  6   PHE A C      1 
ATOM   58   O  O      . PHE A 1 21  ? -9.496  -6.703  -32.850 1.00 39.58  ?  6   PHE A O      1 
ATOM   59   C  CB     . PHE A 1 21  ? -9.760  -9.423  -31.963 1.00 39.14  ?  6   PHE A CB     1 
ATOM   60   C  CG     . PHE A 1 21  ? -10.227 -10.576 -31.103 1.00 39.35  ?  6   PHE A CG     1 
ATOM   61   C  CD1    . PHE A 1 21  ? -10.689 -10.357 -29.812 1.00 40.61  ?  6   PHE A CD1    1 
ATOM   62   C  CD2    . PHE A 1 21  ? -10.166 -11.879 -31.570 1.00 41.04  ?  6   PHE A CD2    1 
ATOM   63   C  CE1    . PHE A 1 21  ? -11.118 -11.414 -29.018 1.00 42.39  ?  6   PHE A CE1    1 
ATOM   64   C  CE2    . PHE A 1 21  ? -10.595 -12.943 -30.773 1.00 44.40  ?  6   PHE A CE2    1 
ATOM   65   C  CZ     . PHE A 1 21  ? -11.083 -12.703 -29.505 1.00 41.73  ?  6   PHE A CZ     1 
ATOM   66   N  N      . ALA A 1 22  ? -11.168 -7.031  -34.377 1.00 37.76  ?  7   ALA A N      1 
ATOM   67   C  CA     . ALA A 1 22  ? -10.814 -5.879  -35.219 1.00 38.26  ?  7   ALA A CA     1 
ATOM   68   C  C      . ALA A 1 22  ? -10.912 -4.525  -34.504 1.00 42.19  ?  7   ALA A C      1 
ATOM   69   O  O      . ALA A 1 22  ? -9.983  -3.723  -34.594 1.00 42.08  ?  7   ALA A O      1 
ATOM   70   C  CB     . ALA A 1 22  ? -11.688 -5.860  -36.473 1.00 39.13  ?  7   ALA A CB     1 
ATOM   71   N  N      . LYS A 1 23  ? -12.033 -4.272  -33.784 1.00 36.08  ?  8   LYS A N      1 
ATOM   72   C  CA     . LYS A 1 23  ? -12.311 -2.978  -33.156 1.00 33.19  ?  8   LYS A CA     1 
ATOM   73   C  C      . LYS A 1 23  ? -11.375 -2.615  -31.985 1.00 35.05  ?  8   LYS A C      1 
ATOM   74   O  O      . LYS A 1 23  ? -10.953 -3.479  -31.236 1.00 35.49  ?  8   LYS A O      1 
ATOM   75   C  CB     . LYS A 1 23  ? -13.783 -2.918  -32.742 1.00 32.85  ?  8   LYS A CB     1 
ATOM   76   C  CG     . LYS A 1 23  ? -14.243 -1.523  -32.340 1.00 42.35  ?  8   LYS A CG     1 
ATOM   77   C  CD     . LYS A 1 23  ? -15.735 -1.486  -32.024 1.00 40.33  ?  8   LYS A CD     1 
ATOM   78   C  CE     . LYS A 1 23  ? -16.183 -0.117  -31.553 1.00 37.87  ?  8   LYS A CE     1 
ATOM   79   N  NZ     . LYS A 1 23  ? -15.954 0.926   -32.577 1.00 37.12  1  8   LYS A NZ     1 
ATOM   80   N  N      . GLU A 1 24  ? -10.986 -1.333  -31.919 1.00 35.11  ?  9   GLU A N      1 
ATOM   81   C  CA     . GLU A 1 24  ? -10.152 -0.701  -30.891 1.00 36.39  ?  9   GLU A CA     1 
ATOM   82   C  C      . GLU A 1 24  ? -10.965 0.439   -30.328 1.00 36.17  ?  9   GLU A C      1 
ATOM   83   O  O      . GLU A 1 24  ? -11.471 1.252   -31.092 1.00 36.67  ?  9   GLU A O      1 
ATOM   84   C  CB     . GLU A 1 24  ? -8.887  -0.087  -31.520 1.00 39.27  ?  9   GLU A CB     1 
ATOM   85   C  CG     . GLU A 1 24  ? -7.778  -1.083  -31.709 1.00 59.73  ?  9   GLU A CG     1 
ATOM   86   C  CD     . GLU A 1 24  ? -6.562  -0.487  -32.384 1.00 84.85  ?  9   GLU A CD     1 
ATOM   87   O  OE1    . GLU A 1 24  ? -5.831  0.282   -31.717 1.00 84.02  ?  9   GLU A OE1    1 
ATOM   88   O  OE2    . GLU A 1 24  ? -6.351  -0.772  -33.586 1.00 75.86  -1 9   GLU A OE2    1 
ATOM   89   N  N      . SER A 1 25  ? -11.052 0.531   -29.010 1.00 31.88  ?  10  SER A N      1 
ATOM   90   C  CA     . SER A 1 25  ? -11.840 1.548   -28.326 1.00 31.71  ?  10  SER A CA     1 
ATOM   91   C  C      . SER A 1 25  ? -11.056 2.330   -27.273 1.00 37.07  ?  10  SER A C      1 
ATOM   92   O  O      . SER A 1 25  ? -10.120 1.800   -26.665 1.00 36.83  ?  10  SER A O      1 
ATOM   93   C  CB     . SER A 1 25  ? -13.088 0.913   -27.727 1.00 33.28  ?  10  SER A CB     1 
ATOM   94   O  OG     . SER A 1 25  ? -13.921 0.396   -28.752 1.00 38.79  ?  10  SER A OG     1 
ATOM   95   N  N      . LEU A 1 26  ? -11.445 3.591   -27.070 1.00 34.59  ?  11  LEU A N      1 
ATOM   96   C  CA     . LEU A 1 26  ? -10.812 4.517   -26.143 1.00 34.63  ?  11  LEU A CA     1 
ATOM   97   C  C      . LEU A 1 26  ? -11.715 4.934   -24.996 1.00 39.84  ?  11  LEU A C      1 
ATOM   98   O  O      . LEU A 1 26  ? -12.928 5.061   -25.182 1.00 38.00  ?  11  LEU A O      1 
ATOM   99   C  CB     . LEU A 1 26  ? -10.403 5.781   -26.911 1.00 35.08  ?  11  LEU A CB     1 
ATOM   100  C  CG     . LEU A 1 26  ? -9.524  5.599   -28.142 1.00 38.93  ?  11  LEU A CG     1 
ATOM   101  C  CD1    . LEU A 1 26  ? -9.492  6.889   -28.949 1.00 38.04  ?  11  LEU A CD1    1 
ATOM   102  C  CD2    . LEU A 1 26  ? -8.119  5.190   -27.756 1.00 43.17  ?  11  LEU A CD2    1 
ATOM   103  N  N      . THR A 1 27  ? -11.108 5.214   -23.831 1.00 36.41  ?  12  THR A N      1 
ATOM   104  C  CA     . THR A 1 27  ? -11.799 5.743   -22.650 1.00 36.52  ?  12  THR A CA     1 
ATOM   105  C  C      . THR A 1 27  ? -11.297 7.172   -22.348 1.00 35.97  ?  12  THR A C      1 
ATOM   106  O  O      . THR A 1 27  ? -10.376 7.630   -23.016 1.00 31.86  ?  12  THR A O      1 
ATOM   107  C  CB     . THR A 1 27  ? -11.708 4.765   -21.447 1.00 41.43  ?  12  THR A CB     1 
ATOM   108  O  OG1    . THR A 1 27  ? -12.612 5.236   -20.455 1.00 44.08  ?  12  THR A OG1    1 
ATOM   109  C  CG2    . THR A 1 27  ? -10.294 4.642   -20.867 1.00 37.10  ?  12  THR A CG2    1 
ATOM   110  N  N      . PHE A 1 28  ? -11.885 7.876   -21.341 1.00 32.81  ?  13  PHE A N      1 
ATOM   111  C  CA     . PHE A 1 28  ? -11.463 9.236   -20.957 1.00 34.09  ?  13  PHE A CA     1 
ATOM   112  C  C      . PHE A 1 28  ? -9.937  9.377   -20.714 1.00 38.80  ?  13  PHE A C      1 
ATOM   113  O  O      . PHE A 1 28  ? -9.301  10.304  -21.222 1.00 36.75  ?  13  PHE A O      1 
ATOM   114  C  CB     . PHE A 1 28  ? -12.231 9.676   -19.681 1.00 36.60  ?  13  PHE A CB     1 
ATOM   115  C  CG     . PHE A 1 28  ? -13.724 9.764   -19.884 1.00 37.14  ?  13  PHE A CG     1 
ATOM   116  C  CD1    . PHE A 1 28  ? -14.281 10.809  -20.610 1.00 40.69  ?  13  PHE A CD1    1 
ATOM   117  C  CD2    . PHE A 1 28  ? -14.563 8.760   -19.420 1.00 40.27  ?  13  PHE A CD2    1 
ATOM   118  C  CE1    . PHE A 1 28  ? -15.661 10.868  -20.840 1.00 42.35  ?  13  PHE A CE1    1 
ATOM   119  C  CE2    . PHE A 1 28  ? -15.945 8.827   -19.636 1.00 43.40  ?  13  PHE A CE2    1 
ATOM   120  C  CZ     . PHE A 1 28  ? -16.480 9.872   -20.354 1.00 41.37  ?  13  PHE A CZ     1 
ATOM   121  N  N      . ASP A 1 29  ? -9.361  8.436   -19.952 1.00 34.27  ?  14  ASP A N      1 
ATOM   122  C  CA     . ASP A 1 29  ? -7.949  8.454   -19.558 1.00 35.13  ?  14  ASP A CA     1 
ATOM   123  C  C      . ASP A 1 29  ? -6.973  8.220   -20.704 1.00 37.10  ?  14  ASP A C      1 
ATOM   124  O  O      . ASP A 1 29  ? -5.791  8.484   -20.536 1.00 37.78  ?  14  ASP A O      1 
ATOM   125  C  CB     . ASP A 1 29  ? -7.696  7.463   -18.402 1.00 38.04  ?  14  ASP A CB     1 
ATOM   126  C  CG     . ASP A 1 29  ? -8.198  7.949   -17.049 1.00 49.99  ?  14  ASP A CG     1 
ATOM   127  O  OD1    . ASP A 1 29  ? -8.733  9.076   -16.982 1.00 49.49  ?  14  ASP A OD1    1 
ATOM   128  O  OD2    . ASP A 1 29  ? -8.081  7.191   -16.068 1.00 56.83  -1 14  ASP A OD2    1 
ATOM   129  N  N      . ASP A 1 30  ? -7.469  7.795   -21.870 1.00 34.45  ?  15  ASP A N      1 
ATOM   130  C  CA     . ASP A 1 30  ? -6.660  7.544   -23.071 1.00 33.71  ?  15  ASP A CA     1 
ATOM   131  C  C      . ASP A 1 30  ? -6.435  8.809   -23.912 1.00 38.33  ?  15  ASP A C      1 
ATOM   132  O  O      . ASP A 1 30  ? -5.593  8.806   -24.811 1.00 36.84  ?  15  ASP A O      1 
ATOM   133  C  CB     . ASP A 1 30  ? -7.407  6.526   -23.952 1.00 34.95  ?  15  ASP A CB     1 
ATOM   134  C  CG     . ASP A 1 30  ? -7.409  5.130   -23.412 1.00 41.21  ?  15  ASP A CG     1 
ATOM   135  O  OD1    . ASP A 1 30  ? -6.355  4.695   -22.874 1.00 42.00  ?  15  ASP A OD1    1 
ATOM   136  O  OD2    . ASP A 1 30  ? -8.426  4.437   -23.586 1.00 37.42  -1 15  ASP A OD2    1 
ATOM   137  N  N      . VAL A 1 31  ? -7.201  9.883   -23.638 1.00 34.54  ?  16  VAL A N      1 
ATOM   138  C  CA     . VAL A 1 31  ? -7.203  11.071  -24.478 1.00 34.07  ?  16  VAL A CA     1 
ATOM   139  C  C      . VAL A 1 31  ? -7.134  12.394  -23.725 1.00 39.20  ?  16  VAL A C      1 
ATOM   140  O  O      . VAL A 1 31  ? -7.521  12.467  -22.561 1.00 37.60  ?  16  VAL A O      1 
ATOM   141  C  CB     . VAL A 1 31  ? -8.441  11.047  -25.442 1.00 35.95  ?  16  VAL A CB     1 
ATOM   142  C  CG1    . VAL A 1 31  ? -8.455  9.784   -26.303 1.00 34.74  ?  16  VAL A CG1    1 
ATOM   143  C  CG2    . VAL A 1 31  ? -9.770  11.207  -24.689 1.00 35.17  ?  16  VAL A CG2    1 
ATOM   144  N  N      . LEU A 1 32  ? -6.641  13.440  -24.415 1.00 36.95  ?  17  LEU A N      1 
ATOM   145  C  CA     . LEU A 1 32  ? -6.602  14.814  -23.915 1.00 35.71  ?  17  LEU A CA     1 
ATOM   146  C  C      . LEU A 1 32  ? -6.941  15.741  -25.090 1.00 40.95  ?  17  LEU A C      1 
ATOM   147  O  O      . LEU A 1 32  ? -6.586  15.439  -26.236 1.00 39.11  ?  17  LEU A O      1 
ATOM   148  C  CB     . LEU A 1 32  ? -5.200  15.203  -23.382 1.00 35.78  ?  17  LEU A CB     1 
ATOM   149  C  CG     . LEU A 1 32  ? -4.667  14.624  -22.057 1.00 39.49  ?  17  LEU A CG     1 
ATOM   150  C  CD1    . LEU A 1 32  ? -3.179  15.059  -21.838 1.00 37.18  ?  17  LEU A CD1    1 
ATOM   151  C  CD2    . LEU A 1 32  ? -5.520  15.082  -20.864 1.00 39.54  ?  17  LEU A CD2    1 
ATOM   152  N  N      . LEU A 1 33  ? -7.558  16.904  -24.798 1.00 37.95  ?  18  LEU A N      1 
ATOM   153  C  CA     . LEU A 1 33  ? -7.859  17.928  -25.809 1.00 37.48  ?  18  LEU A CA     1 
ATOM   154  C  C      . LEU A 1 33  ? -6.636  18.723  -26.148 1.00 39.05  ?  18  LEU A C      1 
ATOM   155  O  O      . LEU A 1 33  ? -5.816  19.029  -25.286 1.00 38.27  ?  18  LEU A O      1 
ATOM   156  C  CB     . LEU A 1 33  ? -9.021  18.841  -25.373 1.00 38.35  ?  18  LEU A CB     1 
ATOM   157  C  CG     . LEU A 1 33  ? -10.384 18.150  -25.390 1.00 41.79  ?  18  LEU A CG     1 
ATOM   158  C  CD1    . LEU A 1 33  ? -11.385 18.918  -24.608 1.00 41.76  ?  18  LEU A CD1    1 
ATOM   159  C  CD2    . LEU A 1 33  ? -10.891 17.916  -26.821 1.00 42.69  ?  18  LEU A CD2    1 
ATOM   160  N  N      . ILE A 1 34  ? -6.441  18.968  -27.430 1.00 37.53  ?  19  ILE A N      1 
ATOM   161  C  CA     . ILE A 1 34  ? -5.256  19.682  -27.892 1.00 37.59  ?  19  ILE A CA     1 
ATOM   162  C  C      . ILE A 1 34  ? -5.573  21.201  -27.770 1.00 41.40  ?  19  ILE A C      1 
ATOM   163  O  O      . ILE A 1 34  ? -6.617  21.601  -28.265 1.00 40.67  ?  19  ILE A O      1 
ATOM   164  C  CB     . ILE A 1 34  ? -4.955  19.290  -29.363 1.00 40.03  ?  19  ILE A CB     1 
ATOM   165  C  CG1    . ILE A 1 34  ? -4.625  17.759  -29.516 1.00 39.61  ?  19  ILE A CG1    1 
ATOM   166  C  CG2    . ILE A 1 34  ? -3.857  20.173  -29.937 1.00 42.03  ?  19  ILE A CG2    1 
ATOM   167  C  CD1    . ILE A 1 34  ? -4.637  17.286  -30.984 1.00 41.67  ?  19  ILE A CD1    1 
ATOM   168  N  N      . PRO A 1 35  ? -4.723  22.050  -27.162 1.00 40.97  ?  20  PRO A N      1 
ATOM   169  C  CA     . PRO A 1 35  ? -5.052  23.491  -27.119 1.00 42.01  ?  20  PRO A CA     1 
ATOM   170  C  C      . PRO A 1 35  ? -4.999  24.110  -28.526 1.00 46.22  ?  20  PRO A C      1 
ATOM   171  O  O      . PRO A 1 35  ? -4.176  23.694  -29.345 1.00 43.08  ?  20  PRO A O      1 
ATOM   172  C  CB     . PRO A 1 35  ? -3.979  24.070  -26.199 1.00 44.26  ?  20  PRO A CB     1 
ATOM   173  C  CG     . PRO A 1 35  ? -2.805  23.129  -26.346 1.00 48.48  ?  20  PRO A CG     1 
ATOM   174  C  CD     . PRO A 1 35  ? -3.419  21.772  -26.522 1.00 43.72  ?  20  PRO A CD     1 
ATOM   175  N  N      . ALA A 1 36  ? -5.897  25.075  -28.819 1.00 43.32  ?  21  ALA A N      1 
ATOM   176  C  CA     . ALA A 1 36  ? -5.950  25.722  -30.136 1.00 43.10  ?  21  ALA A CA     1 
ATOM   177  C  C      . ALA A 1 36  ? -6.069  27.288  -30.042 1.00 49.22  ?  21  ALA A C      1 
ATOM   178  O  O      . ALA A 1 36  ? -6.231  27.852  -28.940 1.00 46.09  ?  21  ALA A O      1 
ATOM   179  C  CB     . ALA A 1 36  ? -7.126  25.152  -30.936 1.00 43.41  ?  21  ALA A CB     1 
ATOM   180  N  N      . GLN A 1 37  ? -5.960  27.970  -31.207 1.00 49.40  ?  22  GLN A N      1 
ATOM   181  C  CA     . GLN A 1 37  ? -6.112  29.431  -31.316 1.00 50.74  ?  22  GLN A CA     1 
ATOM   182  C  C      . GLN A 1 37  ? -7.414  29.824  -30.619 1.00 54.85  ?  22  GLN A C      1 
ATOM   183  O  O      . GLN A 1 37  ? -8.473  29.278  -30.949 1.00 53.96  ?  22  GLN A O      1 
ATOM   184  C  CB     . GLN A 1 37  ? -6.170  29.855  -32.801 1.00 52.73  ?  22  GLN A CB     1 
ATOM   185  C  CG     . GLN A 1 37  ? -6.002  31.374  -33.048 1.00 58.61  ?  22  GLN A CG     1 
ATOM   186  C  CD     . GLN A 1 37  ? -7.220  32.207  -32.680 1.00 72.74  ?  22  GLN A CD     1 
ATOM   187  O  OE1    . GLN A 1 37  ? -8.383  31.839  -32.928 1.00 67.20  ?  22  GLN A OE1    1 
ATOM   188  N  NE2    . GLN A 1 37  ? -6.976  33.341  -32.047 1.00 64.72  ?  22  GLN A NE2    1 
ATOM   189  N  N      . SER A 1 38  ? -7.324  30.759  -29.654 1.00 53.14  ?  23  SER A N      1 
ATOM   190  C  CA     . SER A 1 38  ? -8.477  31.233  -28.895 1.00 53.94  ?  23  SER A CA     1 
ATOM   191  C  C      . SER A 1 38  ? -8.539  32.755  -28.745 1.00 60.81  ?  23  SER A C      1 
ATOM   192  O  O      . SER A 1 38  ? -7.601  33.362  -28.240 1.00 59.50  ?  23  SER A O      1 
ATOM   193  C  CB     . SER A 1 38  ? -8.482  30.622  -27.501 1.00 56.44  ?  23  SER A CB     1 
ATOM   194  O  OG     . SER A 1 38  ? -9.723  30.889  -26.867 1.00 62.41  ?  23  SER A OG     1 
ATOM   195  N  N      . ASP A 1 39  ? -9.682  33.344  -29.111 1.00 60.95  ?  24  ASP A N      1 
ATOM   196  C  CA     . ASP A 1 39  ? -9.967  34.776  -28.935 1.00 62.31  ?  24  ASP A CA     1 
ATOM   197  C  C      . ASP A 1 39  ? -10.988 34.923  -27.782 1.00 66.84  ?  24  ASP A C      1 
ATOM   198  O  O      . ASP A 1 39  ? -11.376 36.049  -27.460 1.00 67.86  ?  24  ASP A O      1 
ATOM   199  C  CB     . ASP A 1 39  ? -10.584 35.388  -30.216 1.00 64.59  ?  24  ASP A CB     1 
ATOM   200  C  CG     . ASP A 1 39  ? -9.791  35.260  -31.502 1.00 79.12  ?  24  ASP A CG     1 
ATOM   201  O  OD1    . ASP A 1 39  ? -8.600  35.664  -31.513 1.00 79.41  ?  24  ASP A OD1    1 
ATOM   202  O  OD2    . ASP A 1 39  ? -10.393 34.868  -32.529 1.00 88.38  -1 24  ASP A OD2    1 
ATOM   203  N  N      . ILE A 1 40  ? -11.441 33.794  -27.182 1.00 61.67  ?  25  ILE A N      1 
ATOM   204  C  CA     . ILE A 1 40  ? -12.452 33.803  -26.119 1.00 61.03  ?  25  ILE A CA     1 
ATOM   205  C  C      . ILE A 1 40  ? -11.882 33.405  -24.741 1.00 65.84  ?  25  ILE A C      1 
ATOM   206  O  O      . ILE A 1 40  ? -11.062 32.490  -24.625 1.00 65.38  ?  25  ILE A O      1 
ATOM   207  C  CB     . ILE A 1 40  ? -13.704 32.961  -26.513 1.00 63.90  ?  25  ILE A CB     1 
ATOM   208  C  CG1    . ILE A 1 40  ? -14.913 33.276  -25.633 1.00 64.23  ?  25  ILE A CG1    1 
ATOM   209  C  CG2    . ILE A 1 40  ? -13.438 31.454  -26.571 1.00 64.77  ?  25  ILE A CG2    1 
ATOM   210  C  CD1    . ILE A 1 40  ? -16.104 33.751  -26.395 1.00 74.22  ?  25  ILE A CD1    1 
ATOM   211  N  N      . LEU A 1 41  ? -12.341 34.109  -23.701 1.00 62.29  ?  26  LEU A N      1 
ATOM   212  C  CA     . LEU A 1 41  ? -11.951 33.849  -22.322 1.00 61.68  ?  26  LEU A CA     1 
ATOM   213  C  C      . LEU A 1 41  ? -12.938 32.844  -21.697 1.00 59.47  ?  26  LEU A C      1 
ATOM   214  O  O      . LEU A 1 41  ? -14.103 32.817  -22.108 1.00 57.13  ?  26  LEU A O      1 
ATOM   215  C  CB     . LEU A 1 41  ? -11.936 35.169  -21.515 1.00 62.58  ?  26  LEU A CB     1 
ATOM   216  C  CG     . LEU A 1 41  ? -10.770 36.129  -21.784 1.00 68.29  ?  26  LEU A CG     1 
ATOM   217  C  CD1    . LEU A 1 41  ? -11.123 37.550  -21.374 1.00 68.24  ?  26  LEU A CD1    1 
ATOM   218  C  CD2    . LEU A 1 41  ? -9.491  35.674  -21.083 1.00 71.90  ?  26  LEU A CD2    1 
ATOM   219  N  N      . PRO A 1 42  ? -12.480 32.003  -20.729 1.00 53.89  ?  27  PRO A N      1 
ATOM   220  C  CA     . PRO A 1 42  ? -13.379 31.040  -20.069 1.00 53.14  ?  27  PRO A CA     1 
ATOM   221  C  C      . PRO A 1 42  ? -14.693 31.618  -19.528 1.00 57.91  ?  27  PRO A C      1 
ATOM   222  O  O      . PRO A 1 42  ? -15.733 30.991  -19.684 1.00 54.91  ?  27  PRO A O      1 
ATOM   223  C  CB     . PRO A 1 42  ? -12.509 30.492  -18.934 1.00 54.97  ?  27  PRO A CB     1 
ATOM   224  C  CG     . PRO A 1 42  ? -11.129 30.580  -19.475 1.00 59.38  ?  27  PRO A CG     1 
ATOM   225  C  CD     . PRO A 1 42  ? -11.116 31.904  -20.173 1.00 55.03  ?  27  PRO A CD     1 
ATOM   226  N  N      . LYS A 1 43  ? -14.649 32.822  -18.908 1.00 57.39  ?  28  LYS A N      1 
ATOM   227  C  CA     . LYS A 1 43  ? -15.846 33.505  -18.396 1.00 57.88  ?  28  LYS A CA     1 
ATOM   228  C  C      . LYS A 1 43  ? -16.882 33.800  -19.506 1.00 61.91  ?  28  LYS A C      1 
ATOM   229  O  O      . LYS A 1 43  ? -18.079 33.688  -19.265 1.00 61.67  ?  28  LYS A O      1 
ATOM   230  C  CB     . LYS A 1 43  ? -15.467 34.802  -17.644 1.00 60.43  ?  28  LYS A CB     1 
ATOM   231  C  CG     . LYS A 1 43  ? -14.659 35.828  -18.448 1.00 72.55  ?  28  LYS A CG     1 
ATOM   232  C  CD     . LYS A 1 43  ? -14.319 37.061  -17.600 1.00 81.15  ?  28  LYS A CD     1 
ATOM   233  C  CE     . LYS A 1 43  ? -13.694 38.196  -18.380 1.00 85.10  ?  28  LYS A CE     1 
ATOM   234  N  NZ     . LYS A 1 43  ? -14.686 38.902  -19.236 1.00 93.34  1  28  LYS A NZ     1 
ATOM   235  N  N      . ASP A 1 44  ? -16.397 34.093  -20.729 1.00 59.16  ?  29  ASP A N      1 
ATOM   236  C  CA     . ASP A 1 44  ? -17.180 34.473  -21.912 1.00 58.50  ?  29  ASP A CA     1 
ATOM   237  C  C      . ASP A 1 44  ? -17.738 33.333  -22.778 1.00 61.21  ?  29  ASP A C      1 
ATOM   238  O  O      . ASP A 1 44  ? -18.528 33.622  -23.686 1.00 60.29  ?  29  ASP A O      1 
ATOM   239  C  CB     . ASP A 1 44  ? -16.341 35.406  -22.807 1.00 60.53  ?  29  ASP A CB     1 
ATOM   240  C  CG     . ASP A 1 44  ? -15.829 36.654  -22.120 1.00 74.52  ?  29  ASP A CG     1 
ATOM   241  O  OD1    . ASP A 1 44  ? -14.685 37.070  -22.424 1.00 77.15  ?  29  ASP A OD1    1 
ATOM   242  O  OD2    . ASP A 1 44  ? -16.562 37.208  -21.270 1.00 77.77  -1 29  ASP A OD2    1 
ATOM   243  N  N      . VAL A 1 45  ? -17.314 32.061  -22.564 1.00 55.66  ?  30  VAL A N      1 
ATOM   244  C  CA     . VAL A 1 45  ? -17.822 30.971  -23.414 1.00 53.91  ?  30  VAL A CA     1 
ATOM   245  C  C      . VAL A 1 45  ? -19.307 30.689  -23.126 1.00 55.64  ?  30  VAL A C      1 
ATOM   246  O  O      . VAL A 1 45  ? -19.780 30.915  -22.010 1.00 55.09  ?  30  VAL A O      1 
ATOM   247  C  CB     . VAL A 1 45  ? -16.950 29.669  -23.415 1.00 57.19  ?  30  VAL A CB     1 
ATOM   248  C  CG1    . VAL A 1 45  ? -15.481 29.987  -23.686 1.00 56.96  ?  30  VAL A CG1    1 
ATOM   249  C  CG2    . VAL A 1 45  ? -17.099 28.885  -22.124 1.00 56.91  ?  30  VAL A CG2    1 
ATOM   250  N  N      . ASP A 1 46  ? -20.028 30.194  -24.141 1.00 51.49  ?  31  ASP A N      1 
ATOM   251  C  CA     . ASP A 1 46  ? -21.441 29.852  -24.050 1.00 51.35  ?  31  ASP A CA     1 
ATOM   252  C  C      . ASP A 1 46  ? -21.571 28.361  -23.741 1.00 55.84  ?  31  ASP A C      1 
ATOM   253  O  O      . ASP A 1 46  ? -21.139 27.527  -24.545 1.00 56.83  ?  31  ASP A O      1 
ATOM   254  C  CB     . ASP A 1 46  ? -22.156 30.222  -25.371 1.00 53.46  ?  31  ASP A CB     1 
ATOM   255  C  CG     . ASP A 1 46  ? -23.605 29.773  -25.529 1.00 64.24  ?  31  ASP A CG     1 
ATOM   256  O  OD1    . ASP A 1 46  ? -24.261 29.494  -24.499 1.00 65.20  ?  31  ASP A OD1    1 
ATOM   257  O  OD2    . ASP A 1 46  ? -24.096 29.747  -26.682 1.00 71.62  -1 31  ASP A OD2    1 
ATOM   258  N  N      . LEU A 1 47  ? -22.174 28.035  -22.582 1.00 52.09  ?  32  LEU A N      1 
ATOM   259  C  CA     . LEU A 1 47  ? -22.394 26.666  -22.102 1.00 52.51  ?  32  LEU A CA     1 
ATOM   260  C  C      . LEU A 1 47  ? -23.784 26.113  -22.419 1.00 55.53  ?  32  LEU A C      1 
ATOM   261  O  O      . LEU A 1 47  ? -24.106 24.997  -22.009 1.00 53.33  ?  32  LEU A O      1 
ATOM   262  C  CB     . LEU A 1 47  ? -22.111 26.543  -20.584 1.00 52.88  ?  32  LEU A CB     1 
ATOM   263  C  CG     . LEU A 1 47  ? -20.680 26.798  -20.066 1.00 58.42  ?  32  LEU A CG     1 
ATOM   264  C  CD1    . LEU A 1 47  ? -20.587 26.487  -18.581 1.00 57.72  ?  32  LEU A CD1    1 
ATOM   265  C  CD2    . LEU A 1 47  ? -19.631 25.974  -20.812 1.00 60.81  ?  32  LEU A CD2    1 
ATOM   266  N  N      . SER A 1 48  ? -24.616 26.874  -23.153 1.00 53.13  ?  33  SER A N      1 
ATOM   267  C  CA     . SER A 1 48  ? -25.969 26.416  -23.467 1.00 53.11  ?  33  SER A CA     1 
ATOM   268  C  C      . SER A 1 48  ? -26.007 25.353  -24.555 1.00 56.69  ?  33  SER A C      1 
ATOM   269  O  O      . SER A 1 48  ? -25.154 25.345  -25.444 1.00 57.42  ?  33  SER A O      1 
ATOM   270  C  CB     . SER A 1 48  ? -26.880 27.592  -23.838 1.00 56.20  ?  33  SER A CB     1 
ATOM   271  O  OG     . SER A 1 48  ? -26.556 28.135  -25.108 1.00 60.47  ?  33  SER A OG     1 
ATOM   272  N  N      . VAL A 1 49  ? -27.015 24.485  -24.498 1.00 52.89  ?  34  VAL A N      1 
ATOM   273  C  CA     . VAL A 1 49  ? -27.244 23.442  -25.500 1.00 53.73  ?  34  VAL A CA     1 
ATOM   274  C  C      . VAL A 1 49  ? -28.744 23.158  -25.694 1.00 58.74  ?  34  VAL A C      1 
ATOM   275  O  O      . VAL A 1 49  ? -29.481 22.983  -24.723 1.00 58.65  ?  34  VAL A O      1 
ATOM   276  C  CB     . VAL A 1 49  ? -26.421 22.140  -25.241 1.00 57.84  ?  34  VAL A CB     1 
ATOM   277  C  CG1    . VAL A 1 49  ? -26.897 21.395  -23.985 1.00 57.43  ?  34  VAL A CG1    1 
ATOM   278  C  CG2    . VAL A 1 49  ? -26.441 21.219  -26.465 1.00 57.81  ?  34  VAL A CG2    1 
ATOM   279  N  N      . GLN A 1 50  ? -29.153 23.046  -26.969 1.00 56.72  ?  35  GLN A N      1 
ATOM   280  C  CA     . GLN A 1 50  ? -30.500 22.725  -27.435 1.00 57.00  ?  35  GLN A CA     1 
ATOM   281  C  C      . GLN A 1 50  ? -30.580 21.202  -27.600 1.00 62.11  ?  35  GLN A C      1 
ATOM   282  O  O      . GLN A 1 50  ? -30.001 20.654  -28.548 1.00 62.38  ?  35  GLN A O      1 
ATOM   283  C  CB     . GLN A 1 50  ? -30.736 23.432  -28.792 1.00 58.56  ?  35  GLN A CB     1 
ATOM   284  C  CG     . GLN A 1 50  ? -32.167 23.394  -29.309 1.00 73.07  ?  35  GLN A CG     1 
ATOM   285  C  CD     . GLN A 1 50  ? -32.962 24.612  -28.889 1.00 84.51  ?  35  GLN A CD     1 
ATOM   286  O  OE1    . GLN A 1 50  ? -32.458 25.747  -28.830 1.00 78.04  ?  35  GLN A OE1    1 
ATOM   287  N  NE2    . GLN A 1 50  ? -34.239 24.409  -28.642 1.00 71.99  ?  35  GLN A NE2    1 
ATOM   288  N  N      . LEU A 1 51  ? -31.273 20.513  -26.674 1.00 58.98  ?  36  LEU A N      1 
ATOM   289  C  CA     . LEU A 1 51  ? -31.413 19.051  -26.725 1.00 59.52  ?  36  LEU A CA     1 
ATOM   290  C  C      . LEU A 1 51  ? -32.532 18.586  -27.648 1.00 67.70  ?  36  LEU A C      1 
ATOM   291  O  O      . LEU A 1 51  ? -32.520 17.443  -28.116 1.00 66.57  ?  36  LEU A O      1 
ATOM   292  C  CB     . LEU A 1 51  ? -31.588 18.446  -25.323 1.00 59.13  ?  36  LEU A CB     1 
ATOM   293  C  CG     . LEU A 1 51  ? -30.383 18.483  -24.381 1.00 62.71  ?  36  LEU A CG     1 
ATOM   294  C  CD1    . LEU A 1 51  ? -30.735 17.835  -23.056 1.00 62.45  ?  36  LEU A CD1    1 
ATOM   295  C  CD2    . LEU A 1 51  ? -29.161 17.770  -24.988 1.00 62.93  ?  36  LEU A CD2    1 
ATOM   296  N  N      . SER A 1 52  ? -33.515 19.474  -27.881 1.00 67.99  ?  37  SER A N      1 
ATOM   297  C  CA     . SER A 1 52  ? -34.679 19.281  -28.747 1.00 69.41  ?  37  SER A CA     1 
ATOM   298  C  C      . SER A 1 52  ? -35.294 20.657  -29.004 1.00 76.78  ?  37  SER A C      1 
ATOM   299  O  O      . SER A 1 52  ? -34.806 21.652  -28.446 1.00 76.42  ?  37  SER A O      1 
ATOM   300  C  CB     . SER A 1 52  ? -35.696 18.334  -28.101 1.00 73.11  ?  37  SER A CB     1 
ATOM   301  O  OG     . SER A 1 52  ? -36.306 18.887  -26.944 1.00 81.99  ?  37  SER A OG     1 
ATOM   302  N  N      A ASP A 1 53  ? -36.351 20.728  -29.841 0.47 74.70  ?  38  ASP A N      1 
ATOM   303  N  N      B ASP A 1 53  ? -36.358 20.709  -29.835 0.53 74.46  ?  38  ASP A N      1 
ATOM   304  C  CA     A ASP A 1 53  ? -37.040 21.982  -30.170 0.47 74.99  ?  38  ASP A CA     1 
ATOM   305  C  CA     B ASP A 1 53  ? -37.105 21.923  -30.188 0.53 74.62  ?  38  ASP A CA     1 
ATOM   306  C  C      A ASP A 1 53  ? -37.664 22.666  -28.944 0.47 79.22  ?  38  ASP A C      1 
ATOM   307  C  C      B ASP A 1 53  ? -37.664 22.647  -28.955 0.53 79.08  ?  38  ASP A C      1 
ATOM   308  O  O      A ASP A 1 53  ? -37.728 23.896  -28.906 0.47 79.09  ?  38  ASP A O      1 
ATOM   309  O  O      B ASP A 1 53  ? -37.695 23.878  -28.930 0.53 78.96  ?  38  ASP A O      1 
ATOM   310  C  CB     A ASP A 1 53  ? -38.073 21.768  -31.286 0.47 77.09  ?  38  ASP A CB     1 
ATOM   311  C  CB     B ASP A 1 53  ? -38.246 21.593  -31.177 0.53 76.49  ?  38  ASP A CB     1 
ATOM   312  C  CG     A ASP A 1 53  ? -37.452 21.445  -32.632 0.47 88.99  ?  38  ASP A CG     1 
ATOM   313  C  CG     B ASP A 1 53  ? -39.055 20.337  -30.872 0.53 86.64  ?  38  ASP A CG     1 
ATOM   314  O  OD1    A ASP A 1 53  ? -36.741 22.314  -33.183 0.47 89.86  ?  38  ASP A OD1    1 
ATOM   315  O  OD1    B ASP A 1 53  ? -39.417 20.130  -29.690 0.53 86.93  ?  38  ASP A OD1    1 
ATOM   316  O  OD2    A ASP A 1 53  ? -37.694 20.329  -33.145 0.47 95.05  -1 38  ASP A OD2    1 
ATOM   317  O  OD2    B ASP A 1 53  ? -39.358 19.580  -31.824 0.53 93.11  -1 38  ASP A OD2    1 
ATOM   318  N  N      . LYS A 1 54  ? -38.078 21.871  -27.934 1.00 75.62  ?  39  LYS A N      1 
ATOM   319  C  CA     . LYS A 1 54  ? -38.662 22.368  -26.679 1.00 75.31  ?  39  LYS A CA     1 
ATOM   320  C  C      . LYS A 1 54  ? -37.666 22.489  -25.513 1.00 76.61  ?  39  LYS A C      1 
ATOM   321  O  O      . LYS A 1 54  ? -37.882 23.326  -24.632 1.00 76.97  ?  39  LYS A O      1 
ATOM   322  C  CB     . LYS A 1 54  ? -39.845 21.478  -26.254 1.00 78.86  ?  39  LYS A CB     1 
ATOM   323  C  CG     . LYS A 1 54  ? -41.102 21.661  -27.104 1.00 98.52  ?  39  LYS A CG     1 
ATOM   324  C  CD     . LYS A 1 54  ? -42.268 20.837  -26.566 1.00 108.88 ?  39  LYS A CD     1 
ATOM   325  C  CE     . LYS A 1 54  ? -43.538 21.040  -27.357 1.00 121.00 ?  39  LYS A CE     1 
ATOM   326  N  NZ     . LYS A 1 54  ? -43.512 20.309  -28.653 1.00 131.94 1  39  LYS A NZ     1 
ATOM   327  N  N      . VAL A 1 55  ? -36.595 21.656  -25.490 1.00 69.97  ?  40  VAL A N      1 
ATOM   328  C  CA     . VAL A 1 55  ? -35.622 21.631  -24.381 1.00 68.07  ?  40  VAL A CA     1 
ATOM   329  C  C      . VAL A 1 55  ? -34.309 22.404  -24.669 1.00 66.29  ?  40  VAL A C      1 
ATOM   330  O  O      . VAL A 1 55  ? -33.517 22.008  -25.537 1.00 64.40  ?  40  VAL A O      1 
ATOM   331  C  CB     . VAL A 1 55  ? -35.324 20.186  -23.882 1.00 72.21  ?  40  VAL A CB     1 
ATOM   332  C  CG1    . VAL A 1 55  ? -34.391 20.199  -22.667 1.00 72.32  ?  40  VAL A CG1    1 
ATOM   333  C  CG2    . VAL A 1 55  ? -36.610 19.431  -23.553 1.00 71.89  ?  40  VAL A CG2    1 
ATOM   334  N  N      A LYS A 1 56  ? -34.074 23.489  -23.919 0.58 60.93  ?  41  LYS A N      1 
ATOM   335  N  N      B LYS A 1 56  ? -34.093 23.483  -23.901 0.42 61.46  ?  41  LYS A N      1 
ATOM   336  C  CA     A LYS A 1 56  ? -32.853 24.286  -24.029 0.58 60.39  ?  41  LYS A CA     1 
ATOM   337  C  CA     B LYS A 1 56  ? -32.911 24.342  -23.967 0.42 61.02  ?  41  LYS A CA     1 
ATOM   338  C  C      A LYS A 1 56  ? -32.254 24.426  -22.635 0.58 63.70  ?  41  LYS A C      1 
ATOM   339  C  C      B LYS A 1 56  ? -32.283 24.370  -22.577 0.42 63.83  ?  41  LYS A C      1 
ATOM   340  O  O      A LYS A 1 56  ? -32.930 24.916  -21.722 0.58 63.26  ?  41  LYS A O      1 
ATOM   341  O  O      B LYS A 1 56  ? -32.957 24.758  -21.614 0.42 63.31  ?  41  LYS A O      1 
ATOM   342  C  CB     A LYS A 1 56  ? -33.121 25.656  -24.672 0.58 62.82  ?  41  LYS A CB     1 
ATOM   343  C  CB     B LYS A 1 56  ? -33.278 25.784  -24.392 0.42 63.85  ?  41  LYS A CB     1 
ATOM   344  C  CG     A LYS A 1 56  ? -31.929 26.201  -25.447 0.58 74.11  ?  41  LYS A CG     1 
ATOM   345  C  CG     B LYS A 1 56  ? -34.102 25.905  -25.670 0.42 80.40  ?  41  LYS A CG     1 
ATOM   346  C  CD     A LYS A 1 56  ? -31.367 27.450  -24.807 0.58 82.68  ?  41  LYS A CD     1 
ATOM   347  C  CD     B LYS A 1 56  ? -35.571 26.239  -25.382 0.42 88.78  ?  41  LYS A CD     1 
ATOM   348  C  CE     A LYS A 1 56  ? -30.252 28.047  -25.628 0.58 94.08  ?  41  LYS A CE     1 
ATOM   349  C  CE     B LYS A 1 56  ? -36.434 26.222  -26.622 0.42 98.00  ?  41  LYS A CE     1 
ATOM   350  N  NZ     A LYS A 1 56  ? -29.735 29.302  -25.019 0.58 100.14 1  41  LYS A NZ     1 
ATOM   351  N  NZ     B LYS A 1 56  ? -36.152 27.375  -27.520 0.42 107.93 1  41  LYS A NZ     1 
ATOM   352  N  N      . LEU A 1 57  ? -31.012 23.924  -22.457 1.00 58.91  ?  42  LEU A N      1 
ATOM   353  C  CA     . LEU A 1 57  ? -30.307 23.950  -21.168 1.00 57.10  ?  42  LEU A CA     1 
ATOM   354  C  C      . LEU A 1 57  ? -29.234 25.018  -21.195 1.00 58.53  ?  42  LEU A C      1 
ATOM   355  O  O      . LEU A 1 57  ? -28.581 25.207  -22.223 1.00 59.07  ?  42  LEU A O      1 
ATOM   356  C  CB     . LEU A 1 57  ? -29.693 22.582  -20.787 1.00 57.10  ?  42  LEU A CB     1 
ATOM   357  C  CG     . LEU A 1 57  ? -30.604 21.324  -20.746 1.00 61.55  ?  42  LEU A CG     1 
ATOM   358  C  CD1    . LEU A 1 57  ? -29.819 20.112  -20.254 1.00 61.81  ?  42  LEU A CD1    1 
ATOM   359  C  CD2    . LEU A 1 57  ? -31.838 21.515  -19.857 1.00 62.60  ?  42  LEU A CD2    1 
ATOM   360  N  N      . ASN A 1 58  ? -29.056 25.717  -20.073 1.00 51.70  ?  43  ASN A N      1 
ATOM   361  C  CA     . ASN A 1 58  ? -28.036 26.749  -19.919 1.00 51.47  ?  43  ASN A CA     1 
ATOM   362  C  C      . ASN A 1 58  ? -26.646 26.147  -19.637 1.00 53.78  ?  43  ASN A C      1 
ATOM   363  O  O      . ASN A 1 58  ? -25.635 26.799  -19.904 1.00 53.61  ?  43  ASN A O      1 
ATOM   364  C  CB     . ASN A 1 58  ? -28.442 27.751  -18.829 1.00 53.90  ?  43  ASN A CB     1 
ATOM   365  C  CG     . ASN A 1 58  ? -29.456 28.786  -19.282 1.00 76.71  ?  43  ASN A CG     1 
ATOM   366  O  OD1    . ASN A 1 58  ? -29.971 28.761  -20.408 1.00 67.25  ?  43  ASN A OD1    1 
ATOM   367  N  ND2    . ASN A 1 58  ? -29.746 29.736  -18.415 1.00 68.50  ?  43  ASN A ND2    1 
ATOM   368  N  N      . ILE A 1 59  ? -26.610 24.935  -19.057 1.00 49.07  ?  44  ILE A N      1 
ATOM   369  C  CA     . ILE A 1 59  ? -25.393 24.154  -18.766 1.00 49.20  ?  44  ILE A CA     1 
ATOM   370  C  C      . ILE A 1 59  ? -25.608 22.696  -19.290 1.00 53.49  ?  44  ILE A C      1 
ATOM   371  O  O      . ILE A 1 59  ? -26.734 22.193  -19.188 1.00 52.79  ?  44  ILE A O      1 
ATOM   372  C  CB     . ILE A 1 59  ? -24.924 24.218  -17.285 1.00 52.26  ?  44  ILE A CB     1 
ATOM   373  C  CG1    . ILE A 1 59  ? -25.990 23.660  -16.314 1.00 52.01  ?  44  ILE A CG1    1 
ATOM   374  C  CG2    . ILE A 1 59  ? -24.458 25.634  -16.897 1.00 54.20  ?  44  ILE A CG2    1 
ATOM   375  C  CD1    . ILE A 1 59  ? -25.462 23.036  -15.009 1.00 54.47  ?  44  ILE A CD1    1 
ATOM   376  N  N      . PRO A 1 60  ? -24.586 22.023  -19.894 1.00 49.61  ?  45  PRO A N      1 
ATOM   377  C  CA     . PRO A 1 60  ? -24.818 20.671  -20.468 1.00 48.66  ?  45  PRO A CA     1 
ATOM   378  C  C      . PRO A 1 60  ? -24.713 19.513  -19.478 1.00 50.44  ?  45  PRO A C      1 
ATOM   379  O  O      . PRO A 1 60  ? -23.985 18.541  -19.724 1.00 47.87  ?  45  PRO A O      1 
ATOM   380  C  CB     . PRO A 1 60  ? -23.730 20.572  -21.537 1.00 50.49  ?  45  PRO A CB     1 
ATOM   381  C  CG     . PRO A 1 60  ? -22.587 21.367  -20.965 1.00 55.21  ?  45  PRO A CG     1 
ATOM   382  C  CD     . PRO A 1 60  ? -23.191 22.464  -20.110 1.00 50.97  ?  45  PRO A CD     1 
ATOM   383  N  N      . VAL A 1 61  ? -25.432 19.615  -18.353 1.00 44.99  ?  46  VAL A N      1 
ATOM   384  C  CA     . VAL A 1 61  ? -25.387 18.621  -17.282 1.00 43.95  ?  46  VAL A CA     1 
ATOM   385  C  C      . VAL A 1 61  ? -26.766 18.154  -16.913 1.00 50.07  ?  46  VAL A C      1 
ATOM   386  O  O      . VAL A 1 61  ? -27.679 18.964  -16.666 1.00 51.40  ?  46  VAL A O      1 
ATOM   387  C  CB     . VAL A 1 61  ? -24.665 19.138  -16.004 1.00 45.70  ?  46  VAL A CB     1 
ATOM   388  C  CG1    . VAL A 1 61  ? -24.350 18.005  -15.044 1.00 45.10  ?  46  VAL A CG1    1 
ATOM   389  C  CG2    . VAL A 1 61  ? -23.424 19.936  -16.330 1.00 44.95  ?  46  VAL A CG2    1 
ATOM   390  N  N      . ILE A 1 62  ? -26.890 16.841  -16.784 1.00 45.07  ?  47  ILE A N      1 
ATOM   391  C  CA     . ILE A 1 62  ? -28.120 16.178  -16.385 1.00 44.50  ?  47  ILE A CA     1 
ATOM   392  C  C      . ILE A 1 62  ? -27.780 15.246  -15.229 1.00 48.18  ?  47  ILE A C      1 
ATOM   393  O  O      . ILE A 1 62  ? -26.853 14.450  -15.360 1.00 46.93  ?  47  ILE A O      1 
ATOM   394  C  CB     . ILE A 1 62  ? -28.785 15.412  -17.577 1.00 47.10  ?  47  ILE A CB     1 
ATOM   395  C  CG1    . ILE A 1 62  ? -29.006 16.337  -18.805 1.00 47.33  ?  47  ILE A CG1    1 
ATOM   396  C  CG2    . ILE A 1 62  ? -30.096 14.754  -17.126 1.00 48.16  ?  47  ILE A CG2    1 
ATOM   397  C  CD1    . ILE A 1 62  ? -29.411 15.607  -20.171 1.00 49.01  ?  47  ILE A CD1    1 
ATOM   398  N  N      . SER A 1 63  ? -28.506 15.349  -14.095 1.00 44.95  ?  48  SER A N      1 
ATOM   399  C  CA     . SER A 1 63  ? -28.326 14.461  -12.950 1.00 45.01  ?  48  SER A CA     1 
ATOM   400  C  C      . SER A 1 63  ? -28.982 13.108  -13.272 1.00 48.34  ?  48  SER A C      1 
ATOM   401  O  O      . SER A 1 63  ? -30.022 13.075  -13.928 1.00 48.50  ?  48  SER A O      1 
ATOM   402  C  CB     . SER A 1 63  ? -28.888 15.081  -11.671 1.00 49.94  ?  48  SER A CB     1 
ATOM   403  O  OG     . SER A 1 63  ? -30.302 15.048  -11.589 1.00 54.75  ?  48  SER A OG     1 
ATOM   404  N  N      . ALA A 1 64  ? -28.347 12.001  -12.861 1.00 46.44  ?  49  ALA A N      1 
ATOM   405  C  CA     . ALA A 1 64  ? -28.800 10.644  -13.182 1.00 47.10  ?  49  ALA A CA     1 
ATOM   406  C  C      . ALA A 1 64  ? -30.115 10.207  -12.561 1.00 53.41  ?  49  ALA A C      1 
ATOM   407  O  O      . ALA A 1 64  ? -30.372 10.494  -11.391 1.00 52.76  ?  49  ALA A O      1 
ATOM   408  C  CB     . ALA A 1 64  ? -27.725 9.644   -12.825 1.00 47.53  ?  49  ALA A CB     1 
ATOM   409  N  N      . GLY A 1 65  ? -30.880 9.419   -13.325 1.00 51.38  ?  50  GLY A N      1 
ATOM   410  C  CA     . GLY A 1 65  ? -32.147 8.845   -12.891 1.00 51.18  ?  50  GLY A CA     1 
ATOM   411  C  C      . GLY A 1 65  ? -31.938 7.673   -11.956 1.00 52.86  ?  50  GLY A C      1 
ATOM   412  O  O      . GLY A 1 65  ? -32.347 6.546   -12.259 1.00 51.73  ?  50  GLY A O      1 
ATOM   413  N  N      . MET A 1 66  ? -31.311 7.952   -10.793 1.00 48.14  ?  51  MET A N      1 
ATOM   414  C  CA     . MET A 1 66  ? -30.935 6.972   -9.766  1.00 47.09  ?  51  MET A CA     1 
ATOM   415  C  C      . MET A 1 66  ? -31.501 7.348   -8.382  1.00 54.02  ?  51  MET A C      1 
ATOM   416  O  O      . MET A 1 66  ? -31.679 8.541   -8.094  1.00 53.55  ?  51  MET A O      1 
ATOM   417  C  CB     . MET A 1 66  ? -29.406 6.873   -9.699  1.00 48.73  ?  51  MET A CB     1 
ATOM   418  C  CG     . MET A 1 66  ? -28.762 6.467   -11.028 1.00 50.94  ?  51  MET A CG     1 
ATOM   419  S  SD     . MET A 1 66  ? -26.960 6.628   -11.000 1.00 53.13  ?  51  MET A SD     1 
ATOM   420  C  CE     . MET A 1 66  ? -26.506 5.154   -10.101 1.00 48.72  ?  51  MET A CE     1 
ATOM   421  N  N      . ASP A 1 67  ? -31.720 6.335   -7.519  1.00 53.54  ?  52  ASP A N      1 
ATOM   422  C  CA     . ASP A 1 67  ? -32.323 6.498   -6.192  1.00 54.58  ?  52  ASP A CA     1 
ATOM   423  C  C      . ASP A 1 67  ? -31.371 7.085   -5.136  1.00 59.38  ?  52  ASP A C      1 
ATOM   424  O  O      . ASP A 1 67  ? -31.840 7.532   -4.086  1.00 59.65  ?  52  ASP A O      1 
ATOM   425  C  CB     . ASP A 1 67  ? -33.013 5.204   -5.682  1.00 56.55  ?  52  ASP A CB     1 
ATOM   426  C  CG     . ASP A 1 67  ? -32.189 3.943   -5.500  1.00 66.86  ?  52  ASP A CG     1 
ATOM   427  O  OD1    . ASP A 1 67  ? -30.969 4.054   -5.255  1.00 66.92  ?  52  ASP A OD1    1 
ATOM   428  O  OD2    . ASP A 1 67  ? -32.784 2.845   -5.516  1.00 75.54  -1 52  ASP A OD2    1 
ATOM   429  N  N      . THR A 1 68  ? -30.060 7.116   -5.410  1.00 54.46  ?  53  THR A N      1 
ATOM   430  C  CA     . THR A 1 68  ? -29.098 7.746   -4.505  1.00 52.76  ?  53  THR A CA     1 
ATOM   431  C  C      . THR A 1 68  ? -28.628 9.069   -5.132  1.00 54.44  ?  53  THR A C      1 
ATOM   432  O  O      . THR A 1 68  ? -27.635 9.637   -4.676  1.00 53.88  ?  53  THR A O      1 
ATOM   433  C  CB     . THR A 1 68  ? -27.938 6.806   -4.172  1.00 62.86  ?  53  THR A CB     1 
ATOM   434  O  OG1    . THR A 1 68  ? -27.373 6.316   -5.379  1.00 65.46  ?  53  THR A OG1    1 
ATOM   435  C  CG2    . THR A 1 68  ? -28.343 5.656   -3.266  1.00 62.11  ?  53  THR A CG2    1 
ATOM   436  N  N      . VAL A 1 69  ? -29.335 9.547   -6.191  1.00 49.98  ?  54  VAL A N      1 
ATOM   437  C  CA     . VAL A 1 69  ? -28.970 10.768  -6.926  1.00 49.73  ?  54  VAL A CA     1 
ATOM   438  C  C      . VAL A 1 69  ? -30.142 11.739  -7.153  1.00 55.25  ?  54  VAL A C      1 
ATOM   439  O  O      . VAL A 1 69  ? -29.995 12.913  -6.799  1.00 55.42  ?  54  VAL A O      1 
ATOM   440  C  CB     . VAL A 1 69  ? -28.228 10.495  -8.296  1.00 51.66  ?  54  VAL A CB     1 
ATOM   441  C  CG1    . VAL A 1 69  ? -27.849 11.799  -9.012  1.00 50.76  ?  54  VAL A CG1    1 
ATOM   442  C  CG2    . VAL A 1 69  ? -26.991 9.620   -8.118  1.00 51.05  ?  54  VAL A CG2    1 
ATOM   443  N  N      . THR A 1 70  ? -31.238 11.319  -7.834  1.00 52.67  ?  55  THR A N      1 
ATOM   444  C  CA     . THR A 1 70  ? -32.237 12.317  -8.198  1.00 52.96  ?  55  THR A CA     1 
ATOM   445  C  C      . THR A 1 70  ? -33.693 12.037  -7.804  1.00 58.17  ?  55  THR A C      1 
ATOM   446  O  O      . THR A 1 70  ? -34.308 11.039  -8.211  1.00 57.45  ?  55  THR A O      1 
ATOM   447  C  CB     . THR A 1 70  ? -32.182 12.635  -9.711  1.00 58.64  ?  55  THR A CB     1 
ATOM   448  O  OG1    . THR A 1 70  ? -30.835 12.858  -10.134 1.00 57.89  ?  55  THR A OG1    1 
ATOM   449  C  CG2    . THR A 1 70  ? -33.038 13.841  -10.100 1.00 54.95  ?  55  THR A CG2    1 
ATOM   450  N  N      . GLU A 1 71  ? -34.245 13.042  -7.095  1.00 54.47  ?  56  GLU A N      1 
ATOM   451  C  CA     . GLU A 1 71  ? -35.639 13.232  -6.696  1.00 53.74  ?  56  GLU A CA     1 
ATOM   452  C  C      . GLU A 1 71  ? -35.931 14.738  -6.883  1.00 57.78  ?  56  GLU A C      1 
ATOM   453  O  O      . GLU A 1 71  ? -35.142 15.412  -7.577  1.00 57.09  ?  56  GLU A O      1 
ATOM   454  C  CB     . GLU A 1 71  ? -35.897 12.712  -5.279  1.00 55.07  ?  56  GLU A CB     1 
ATOM   455  C  CG     . GLU A 1 71  ? -36.221 11.229  -5.282  1.00 65.89  ?  56  GLU A CG     1 
ATOM   456  C  CD     . GLU A 1 71  ? -36.290 10.524  -3.942  1.00 87.46  ?  56  GLU A CD     1 
ATOM   457  O  OE1    . GLU A 1 71  ? -36.607 11.183  -2.925  1.00 93.22  ?  56  GLU A OE1    1 
ATOM   458  O  OE2    . GLU A 1 71  ? -36.034 9.298   -3.915  1.00 72.91  -1 56  GLU A OE2    1 
ATOM   459  N  N      . SER A 1 72  ? -37.062 15.269  -6.348  1.00 51.78  ?  57  SER A N      1 
ATOM   460  C  CA     . SER A 1 72  ? -37.419 16.676  -6.578  1.00 51.26  ?  57  SER A CA     1 
ATOM   461  C  C      . SER A 1 72  ? -36.356 17.679  -6.132  1.00 54.89  ?  57  SER A C      1 
ATOM   462  O  O      . SER A 1 72  ? -36.124 18.654  -6.853  1.00 56.32  ?  57  SER A O      1 
ATOM   463  C  CB     . SER A 1 72  ? -38.783 17.027  -5.970  1.00 54.23  ?  57  SER A CB     1 
ATOM   464  O  OG     . SER A 1 72  ? -38.938 16.516  -4.654  1.00 60.81  ?  57  SER A OG     1 
ATOM   465  N  N      A LYS A 1 73  ? -35.719 17.441  -4.963  0.22 51.34  ?  58  LYS A N      1 
ATOM   466  N  N      B LYS A 1 73  ? -35.722 17.444  -4.968  0.78 51.38  ?  58  LYS A N      1 
ATOM   467  C  CA     A LYS A 1 73  ? -34.679 18.301  -4.383  0.22 51.28  ?  58  LYS A CA     1 
ATOM   468  C  CA     B LYS A 1 73  ? -34.693 18.312  -4.379  0.78 51.86  ?  58  LYS A CA     1 
ATOM   469  C  C      A LYS A 1 73  ? -33.477 18.480  -5.321  0.22 54.88  ?  58  LYS A C      1 
ATOM   470  C  C      B LYS A 1 73  ? -33.481 18.484  -5.333  0.78 55.79  ?  58  LYS A C      1 
ATOM   471  O  O      A LYS A 1 73  ? -32.976 19.597  -5.460  0.22 54.92  ?  58  LYS A O      1 
ATOM   472  O  O      B LYS A 1 73  ? -33.001 19.605  -5.512  0.78 56.83  ?  58  LYS A O      1 
ATOM   473  C  CB     A LYS A 1 73  ? -34.231 17.764  -3.016  0.22 53.92  ?  58  LYS A CB     1 
ATOM   474  C  CB     B LYS A 1 73  ? -34.271 17.755  -3.006  0.78 54.64  ?  58  LYS A CB     1 
ATOM   475  C  CG     A LYS A 1 73  ? -34.274 18.812  -1.910  0.22 67.32  ?  58  LYS A CG     1 
ATOM   476  C  CG     B LYS A 1 73  ? -33.537 18.732  -2.090  0.78 63.98  ?  58  LYS A CG     1 
ATOM   477  C  CD     A LYS A 1 73  ? -35.403 18.560  -0.911  0.22 76.21  ?  58  LYS A CD     1 
ATOM   478  C  CD     B LYS A 1 73  ? -33.299 18.098  -0.717  0.78 68.68  ?  58  LYS A CD     1 
ATOM   479  C  CE     A LYS A 1 73  ? -36.651 19.371  -1.190  0.22 86.55  ?  58  LYS A CE     1 
ATOM   480  C  CE     B LYS A 1 73  ? -32.177 18.750  0.054   0.78 71.51  ?  58  LYS A CE     1 
ATOM   481  N  NZ     A LYS A 1 73  ? -37.475 18.781  -2.278  0.22 94.52  1  58  LYS A NZ     1 
ATOM   482  N  NZ     B LYS A 1 73  ? -31.804 17.964  1.262   0.78 73.21  1  58  LYS A NZ     1 
ATOM   483  N  N      . MET A 1 74  ? -33.039 17.388  -5.977  1.00 50.70  ?  59  MET A N      1 
ATOM   484  C  CA     . MET A 1 74  ? -31.929 17.395  -6.952  1.00 48.76  ?  59  MET A CA     1 
ATOM   485  C  C      . MET A 1 74  ? -32.394 18.064  -8.243  1.00 52.52  ?  59  MET A C      1 
ATOM   486  O  O      . MET A 1 74  ? -31.712 18.954  -8.747  1.00 53.23  ?  59  MET A O      1 
ATOM   487  C  CB     . MET A 1 74  ? -31.467 15.945  -7.243  1.00 50.42  ?  59  MET A CB     1 
ATOM   488  C  CG     . MET A 1 74  ? -30.335 15.833  -8.278  1.00 52.79  ?  59  MET A CG     1 
ATOM   489  S  SD     . MET A 1 74  ? -28.828 16.744  -7.859  1.00 55.49  ?  59  MET A SD     1 
ATOM   490  C  CE     . MET A 1 74  ? -28.101 15.656  -6.649  1.00 52.55  ?  59  MET A CE     1 
ATOM   491  N  N      . ALA A 1 75  ? -33.578 17.664  -8.758  1.00 50.53  ?  60  ALA A N      1 
ATOM   492  C  CA     . ALA A 1 75  ? -34.148 18.198  -9.996  1.00 49.69  ?  60  ALA A CA     1 
ATOM   493  C  C      . ALA A 1 75  ? -34.366 19.701  -9.985  1.00 57.04  ?  60  ALA A C      1 
ATOM   494  O  O      . ALA A 1 75  ? -34.116 20.348  -11.000 1.00 56.64  ?  60  ALA A O      1 
ATOM   495  C  CB     . ALA A 1 75  ? -35.426 17.474  -10.344 1.00 50.34  ?  60  ALA A CB     1 
ATOM   496  N  N      . ILE A 1 76  ? -34.769 20.268  -8.824  1.00 54.72  ?  61  ILE A N      1 
ATOM   497  C  CA     . ILE A 1 76  ? -35.000 21.707  -8.677  1.00 54.76  ?  61  ILE A CA     1 
ATOM   498  C  C      . ILE A 1 76  ? -33.668 22.433  -8.705  1.00 56.11  ?  61  ILE A C      1 
ATOM   499  O  O      . ILE A 1 76  ? -33.484 23.369  -9.495  1.00 54.46  ?  61  ILE A O      1 
ATOM   500  C  CB     . ILE A 1 76  ? -35.846 22.007  -7.384  1.00 58.58  ?  61  ILE A CB     1 
ATOM   501  C  CG1    . ILE A 1 76  ? -37.329 21.651  -7.599  1.00 59.23  ?  61  ILE A CG1    1 
ATOM   502  C  CG2    . ILE A 1 76  ? -35.697 23.459  -6.924  1.00 60.44  ?  61  ILE A CG2    1 
ATOM   503  C  CD1    . ILE A 1 76  ? -38.113 21.302  -6.309  1.00 66.83  ?  61  ILE A CD1    1 
ATOM   504  N  N      . ALA A 1 77  ? -32.730 21.975  -7.852  1.00 53.90  ?  62  ALA A N      1 
ATOM   505  C  CA     . ALA A 1 77  ? -31.379 22.513  -7.722  1.00 53.13  ?  62  ALA A CA     1 
ATOM   506  C  C      . ALA A 1 77  ? -30.655 22.478  -9.065  1.00 55.59  ?  62  ALA A C      1 
ATOM   507  O  O      . ALA A 1 77  ? -30.072 23.494  -9.445  1.00 55.06  ?  62  ALA A O      1 
ATOM   508  C  CB     . ALA A 1 77  ? -30.610 21.731  -6.676  1.00 53.94  ?  62  ALA A CB     1 
ATOM   509  N  N      . MET A 1 78  ? -30.750 21.338  -9.813  1.00 52.40  ?  63  MET A N      1 
ATOM   510  C  CA     . MET A 1 78  ? -30.126 21.146  -11.148 1.00 50.89  ?  63  MET A CA     1 
ATOM   511  C  C      . MET A 1 78  ? -30.653 22.176  -12.134 1.00 55.27  ?  63  MET A C      1 
ATOM   512  O  O      . MET A 1 78  ? -29.858 22.888  -12.769 1.00 53.03  ?  63  MET A O      1 
ATOM   513  C  CB     . MET A 1 78  ? -30.417 19.741  -11.721 1.00 52.33  ?  63  MET A CB     1 
ATOM   514  C  CG     . MET A 1 78  ? -29.447 18.661  -11.288 1.00 54.92  ?  63  MET A CG     1 
ATOM   515  S  SD     . MET A 1 78  ? -27.673 18.946  -11.585 1.00 57.45  ?  63  MET A SD     1 
ATOM   516  C  CE     . MET A 1 78  ? -27.650 19.416  -13.302 1.00 53.52  ?  63  MET A CE     1 
ATOM   517  N  N      . ALA A 1 79  ? -32.007 22.256  -12.240 1.00 54.38  ?  64  ALA A N      1 
ATOM   518  C  CA     . ALA A 1 79  ? -32.743 23.187  -13.103 1.00 55.52  ?  64  ALA A CA     1 
ATOM   519  C  C      . ALA A 1 79  ? -32.435 24.653  -12.788 1.00 62.69  ?  64  ALA A C      1 
ATOM   520  O  O      . ALA A 1 79  ? -32.351 25.453  -13.719 1.00 63.31  ?  64  ALA A O      1 
ATOM   521  C  CB     . ALA A 1 79  ? -34.236 22.919  -13.020 1.00 56.45  ?  64  ALA A CB     1 
ATOM   522  N  N      . ARG A 1 80  ? -32.197 24.993  -11.494 1.00 60.82  ?  65  ARG A N      1 
ATOM   523  C  CA     . ARG A 1 80  ? -31.822 26.356  -11.067 1.00 60.99  ?  65  ARG A CA     1 
ATOM   524  C  C      . ARG A 1 80  ? -30.391 26.738  -11.473 1.00 64.45  ?  65  ARG A C      1 
ATOM   525  O  O      . ARG A 1 80  ? -30.069 27.927  -11.521 1.00 65.03  ?  65  ARG A O      1 
ATOM   526  C  CB     . ARG A 1 80  ? -32.048 26.573  -9.560  1.00 62.06  ?  65  ARG A CB     1 
ATOM   527  C  CG     . ARG A 1 80  ? -33.516 26.786  -9.217  1.00 69.66  ?  65  ARG A CG     1 
ATOM   528  C  CD     . ARG A 1 80  ? -33.759 27.013  -7.740  1.00 80.88  ?  65  ARG A CD     1 
ATOM   529  N  NE     . ARG A 1 80  ? -35.178 26.843  -7.425  1.00 90.26  ?  65  ARG A NE     1 
ATOM   530  C  CZ     . ARG A 1 80  ? -35.683 26.797  -6.197  1.00 104.44 ?  65  ARG A CZ     1 
ATOM   531  N  NH1    . ARG A 1 80  ? -34.891 26.919  -5.139  1.00 88.80  1  65  ARG A NH1    1 
ATOM   532  N  NH2    . ARG A 1 80  ? -36.980 26.599  -6.017  1.00 96.86  ?  65  ARG A NH2    1 
ATOM   533  N  N      . GLN A 1 81  ? -29.537 25.734  -11.767 1.00 59.57  ?  66  GLN A N      1 
ATOM   534  C  CA     . GLN A 1 81  ? -28.160 25.934  -12.237 1.00 58.28  ?  66  GLN A CA     1 
ATOM   535  C  C      . GLN A 1 81  ? -28.128 26.033  -13.772 1.00 60.53  ?  66  GLN A C      1 
ATOM   536  O  O      . GLN A 1 81  ? -27.084 26.330  -14.354 1.00 59.90  ?  66  GLN A O      1 
ATOM   537  C  CB     . GLN A 1 81  ? -27.255 24.782  -11.760 1.00 59.38  ?  66  GLN A CB     1 
ATOM   538  C  CG     . GLN A 1 81  ? -27.054 24.696  -10.249 1.00 74.90  ?  66  GLN A CG     1 
ATOM   539  C  CD     . GLN A 1 81  ? -26.338 25.897  -9.684  1.00 100.00 ?  66  GLN A CD     1 
ATOM   540  O  OE1    . GLN A 1 81  ? -26.964 26.822  -9.159  1.00 96.63  ?  66  GLN A OE1    1 
ATOM   541  N  NE2    . GLN A 1 81  ? -25.015 25.918  -9.799  1.00 95.38  ?  66  GLN A NE2    1 
ATOM   542  N  N      . GLY A 1 82  ? -29.275 25.786  -14.401 1.00 56.17  ?  67  GLY A N      1 
ATOM   543  C  CA     . GLY A 1 82  ? -29.427 25.812  -15.849 1.00 55.72  ?  67  GLY A CA     1 
ATOM   544  C  C      . GLY A 1 82  ? -29.351 24.422  -16.453 1.00 58.22  ?  67  GLY A C      1 
ATOM   545  O  O      . GLY A 1 82  ? -29.253 24.272  -17.674 1.00 57.70  ?  67  GLY A O      1 
ATOM   546  N  N      . GLY A 1 83  ? -29.405 23.412  -15.591 1.00 53.85  ?  68  GLY A N      1 
ATOM   547  C  CA     . GLY A 1 83  ? -29.316 22.013  -15.988 1.00 53.27  ?  68  GLY A CA     1 
ATOM   548  C  C      . GLY A 1 83  ? -30.641 21.291  -16.013 1.00 54.77  ?  68  GLY A C      1 
ATOM   549  O  O      . GLY A 1 83  ? -31.663 21.884  -16.356 1.00 54.19  ?  68  GLY A O      1 
ATOM   550  N  N      . LEU A 1 84  ? -30.622 19.991  -15.676 1.00 49.82  ?  69  LEU A N      1 
ATOM   551  C  CA     . LEU A 1 84  ? -31.806 19.129  -15.691 1.00 49.70  ?  69  LEU A CA     1 
ATOM   552  C  C      . LEU A 1 84  ? -31.605 17.902  -14.810 1.00 53.74  ?  69  LEU A C      1 
ATOM   553  O  O      . LEU A 1 84  ? -30.489 17.398  -14.693 1.00 52.79  ?  69  LEU A O      1 
ATOM   554  C  CB     . LEU A 1 84  ? -32.105 18.689  -17.140 1.00 50.22  ?  69  LEU A CB     1 
ATOM   555  C  CG     . LEU A 1 84  ? -33.245 17.691  -17.389 1.00 54.46  ?  69  LEU A CG     1 
ATOM   556  C  CD1    . LEU A 1 84  ? -34.625 18.322  -17.080 1.00 54.12  ?  69  LEU A CD1    1 
ATOM   557  C  CD2    . LEU A 1 84  ? -33.213 17.213  -18.820 1.00 57.93  ?  69  LEU A CD2    1 
ATOM   558  N  N      . GLY A 1 85  ? -32.691 17.443  -14.199 1.00 50.62  ?  70  GLY A N      1 
ATOM   559  C  CA     . GLY A 1 85  ? -32.708 16.260  -13.353 1.00 51.06  ?  70  GLY A CA     1 
ATOM   560  C  C      . GLY A 1 85  ? -33.693 15.216  -13.837 1.00 56.79  ?  70  GLY A C      1 
ATOM   561  O  O      . GLY A 1 85  ? -34.810 15.560  -14.238 1.00 58.18  ?  70  GLY A O      1 
ATOM   562  N  N      . VAL A 1 86  ? -33.282 13.941  -13.837 1.00 53.37  ?  71  VAL A N      1 
ATOM   563  C  CA     . VAL A 1 86  ? -34.153 12.836  -14.244 1.00 53.26  ?  71  VAL A CA     1 
ATOM   564  C  C      . VAL A 1 86  ? -34.672 12.184  -12.975 1.00 57.94  ?  71  VAL A C      1 
ATOM   565  O  O      . VAL A 1 86  ? -33.886 11.553  -12.266 1.00 55.98  ?  71  VAL A O      1 
ATOM   566  C  CB     . VAL A 1 86  ? -33.473 11.791  -15.188 1.00 57.21  ?  71  VAL A CB     1 
ATOM   567  C  CG1    . VAL A 1 86  ? -34.431 10.633  -15.512 1.00 56.85  ?  71  VAL A CG1    1 
ATOM   568  C  CG2    . VAL A 1 86  ? -32.967 12.441  -16.476 1.00 56.34  ?  71  VAL A CG2    1 
ATOM   569  N  N      . ILE A 1 87  ? -35.994 12.331  -12.674 1.00 54.87  ?  72  ILE A N      1 
ATOM   570  C  CA     . ILE A 1 87  ? -36.546 11.690  -11.478 1.00 54.97  ?  72  ILE A CA     1 
ATOM   571  C  C      . ILE A 1 87  ? -36.523 10.193  -11.722 1.00 58.97  ?  72  ILE A C      1 
ATOM   572  O  O      . ILE A 1 87  ? -37.027 9.742   -12.756 1.00 58.40  ?  72  ILE A O      1 
ATOM   573  C  CB     . ILE A 1 87  ? -37.981 12.165  -11.052 1.00 57.75  ?  72  ILE A CB     1 
ATOM   574  C  CG1    . ILE A 1 87  ? -38.131 13.712  -11.032 1.00 57.54  ?  72  ILE A CG1    1 
ATOM   575  C  CG2    . ILE A 1 87  ? -38.409 11.529  -9.707  1.00 57.49  ?  72  ILE A CG2    1 
ATOM   576  C  CD1    . ILE A 1 87  ? -37.449 14.465  -9.959  1.00 60.44  ?  72  ILE A CD1    1 
ATOM   577  N  N      . HIS A 1 88  ? -35.936 9.435   -10.775 1.00 56.70  ?  73  HIS A N      1 
ATOM   578  C  CA     . HIS A 1 88  ? -35.854 7.978   -10.847 1.00 57.77  ?  73  HIS A CA     1 
ATOM   579  C  C      . HIS A 1 88  ? -37.222 7.324   -10.753 1.00 64.13  ?  73  HIS A C      1 
ATOM   580  O  O      . HIS A 1 88  ? -38.142 7.903   -10.157 1.00 63.83  ?  73  HIS A O      1 
ATOM   581  C  CB     . HIS A 1 88  ? -34.864 7.393   -9.819  1.00 58.50  ?  73  HIS A CB     1 
ATOM   582  C  CG     . HIS A 1 88  ? -35.353 7.342   -8.402  1.00 61.83  ?  73  HIS A CG     1 
ATOM   583  N  ND1    . HIS A 1 88  ? -35.986 6.222   -7.902  1.00 63.56  ?  73  HIS A ND1    1 
ATOM   584  C  CD2    . HIS A 1 88  ? -35.220 8.247   -7.405  1.00 63.22  ?  73  HIS A CD2    1 
ATOM   585  C  CE1    . HIS A 1 88  ? -36.235 6.482   -6.629  1.00 62.69  ?  73  HIS A CE1    1 
ATOM   586  N  NE2    . HIS A 1 88  ? -35.791 7.689   -6.283  1.00 62.87  ?  73  HIS A NE2    1 
ATOM   587  N  N      . LYS A 1 89  ? -37.348 6.123   -11.355 1.00 61.41  ?  74  LYS A N      1 
ATOM   588  C  CA     . LYS A 1 89  ? -38.582 5.335   -11.393 1.00 61.89  ?  74  LYS A CA     1 
ATOM   589  C  C      . LYS A 1 89  ? -38.688 4.247   -10.296 1.00 66.12  ?  74  LYS A C      1 
ATOM   590  O  O      . LYS A 1 89  ? -39.611 3.433   -10.357 1.00 66.01  ?  74  LYS A O      1 
ATOM   591  C  CB     . LYS A 1 89  ? -38.799 4.725   -12.806 1.00 65.60  ?  74  LYS A CB     1 
ATOM   592  C  CG     . LYS A 1 89  ? -37.807 3.629   -13.201 1.00 83.38  ?  74  LYS A CG     1 
ATOM   593  C  CD     . LYS A 1 89  ? -38.129 3.039   -14.565 1.00 97.01  ?  74  LYS A CD     1 
ATOM   594  C  CE     . LYS A 1 89  ? -37.234 1.874   -14.916 1.00 107.55 ?  74  LYS A CE     1 
ATOM   595  N  NZ     . LYS A 1 89  ? -37.609 0.639   -14.177 1.00 115.79 1  74  LYS A NZ     1 
ATOM   596  N  N      A ASN A 1 90  ? -37.771 4.243   -9.309  0.49 63.14  ?  75  ASN A N      1 
ATOM   597  N  N      B ASN A 1 90  ? -37.767 4.236   -9.308  0.51 63.17  ?  75  ASN A N      1 
ATOM   598  C  CA     A ASN A 1 90  ? -37.778 3.267   -8.211  0.49 63.30  ?  75  ASN A CA     1 
ATOM   599  C  CA     B ASN A 1 90  ? -37.796 3.265   -8.203  0.51 63.35  ?  75  ASN A CA     1 
ATOM   600  C  C      A ASN A 1 90  ? -38.667 3.761   -7.034  0.49 67.51  ?  75  ASN A C      1 
ATOM   601  C  C      B ASN A 1 90  ? -38.673 3.765   -7.030  0.51 67.52  ?  75  ASN A C      1 
ATOM   602  O  O      A ASN A 1 90  ? -38.241 3.792   -5.874  0.49 67.19  ?  75  ASN A O      1 
ATOM   603  O  O      B ASN A 1 90  ? -38.246 3.805   -5.871  0.51 67.20  ?  75  ASN A O      1 
ATOM   604  C  CB     A ASN A 1 90  ? -36.337 2.939   -7.775  0.49 63.62  ?  75  ASN A CB     1 
ATOM   605  C  CB     B ASN A 1 90  ? -36.380 2.868   -7.757  0.51 63.76  ?  75  ASN A CB     1 
ATOM   606  C  CG     A ASN A 1 90  ? -36.103 1.542   -7.247  0.49 86.49  ?  75  ASN A CG     1 
ATOM   607  C  CG     B ASN A 1 90  ? -35.818 1.654   -8.455  0.51 87.91  ?  75  ASN A CG     1 
ATOM   608  O  OD1    A ASN A 1 90  ? -36.980 0.668   -7.261  0.49 82.97  ?  75  ASN A OD1    1 
ATOM   609  O  OD1    B ASN A 1 90  ? -36.024 1.430   -9.656  0.51 83.70  ?  75  ASN A OD1    1 
ATOM   610  N  ND2    A ASN A 1 90  ? -34.884 1.294   -6.794  0.49 77.30  ?  75  ASN A ND2    1 
ATOM   611  N  ND2    B ASN A 1 90  ? -35.040 0.870   -7.724  0.51 79.68  ?  75  ASN A ND2    1 
ATOM   612  N  N      . MET A 1 91  ? -39.910 4.160   -7.370  1.00 64.21  ?  76  MET A N      1 
ATOM   613  C  CA     . MET A 1 91  ? -40.951 4.655   -6.459  1.00 63.87  ?  76  MET A CA     1 
ATOM   614  C  C      . MET A 1 91  ? -42.318 4.421   -7.138  1.00 70.94  ?  76  MET A C      1 
ATOM   615  O  O      . MET A 1 91  ? -42.356 3.987   -8.296  1.00 71.14  ?  76  MET A O      1 
ATOM   616  C  CB     . MET A 1 91  ? -40.735 6.149   -6.107  1.00 65.30  ?  76  MET A CB     1 
ATOM   617  C  CG     . MET A 1 91  ? -40.813 7.098   -7.294  1.00 67.72  ?  76  MET A CG     1 
ATOM   618  S  SD     . MET A 1 91  ? -40.609 8.825   -6.802  1.00 70.85  ?  76  MET A SD     1 
ATOM   619  C  CE     . MET A 1 91  ? -38.831 8.962   -6.801  1.00 67.45  ?  76  MET A CE     1 
ATOM   620  N  N      . GLY A 1 92  ? -43.407 4.689   -6.414  1.00 68.65  ?  77  GLY A N      1 
ATOM   621  C  CA     . GLY A 1 92  ? -44.764 4.543   -6.928  1.00 69.15  ?  77  GLY A CA     1 
ATOM   622  C  C      . GLY A 1 92  ? -45.089 5.601   -7.962  1.00 75.67  ?  77  GLY A C      1 
ATOM   623  O  O      . GLY A 1 92  ? -44.499 6.687   -7.939  1.00 76.25  ?  77  GLY A O      1 
ATOM   624  N  N      . VAL A 1 93  ? -46.017 5.281   -8.885  1.00 72.88  ?  78  VAL A N      1 
ATOM   625  C  CA     . VAL A 1 93  ? -46.469 6.155   -9.979  1.00 73.19  ?  78  VAL A CA     1 
ATOM   626  C  C      . VAL A 1 93  ? -46.855 7.559   -9.463  1.00 79.16  ?  78  VAL A C      1 
ATOM   627  O  O      . VAL A 1 93  ? -46.333 8.563   -9.968  1.00 78.40  ?  78  VAL A O      1 
ATOM   628  C  CB     . VAL A 1 93  ? -47.598 5.480   -10.822 1.00 77.07  ?  78  VAL A CB     1 
ATOM   629  C  CG1    . VAL A 1 93  ? -48.191 6.436   -11.854 1.00 76.86  ?  78  VAL A CG1    1 
ATOM   630  C  CG2    . VAL A 1 93  ? -47.096 4.209   -11.505 1.00 76.74  ?  78  VAL A CG2    1 
ATOM   631  N  N      . GLU A 1 94  ? -47.725 7.608   -8.426  1.00 77.10  ?  79  GLU A N      1 
ATOM   632  C  CA     . GLU A 1 94  ? -48.229 8.832   -7.781  1.00 77.32  ?  79  GLU A CA     1 
ATOM   633  C  C      . GLU A 1 94  ? -47.085 9.614   -7.154  1.00 79.53  ?  79  GLU A C      1 
ATOM   634  O  O      . GLU A 1 94  ? -46.973 10.817  -7.398  1.00 79.05  ?  79  GLU A O      1 
ATOM   635  C  CB     . GLU A 1 94  ? -49.297 8.515   -6.705  1.00 79.12  ?  79  GLU A CB     1 
ATOM   636  C  CG     . GLU A 1 94  ? -50.470 7.662   -7.175  1.00 92.75  ?  79  GLU A CG     1 
ATOM   637  C  CD     . GLU A 1 94  ? -50.199 6.177   -7.345  1.00 116.52 ?  79  GLU A CD     1 
ATOM   638  O  OE1    . GLU A 1 94  ? -50.691 5.604   -8.344  1.00 117.98 ?  79  GLU A OE1    1 
ATOM   639  O  OE2    . GLU A 1 94  ? -49.467 5.595   -6.510  1.00 109.31 -1 79  GLU A OE2    1 
ATOM   640  N  N      . GLU A 1 95  ? -46.218 8.919   -6.378  1.00 75.50  ?  80  GLU A N      1 
ATOM   641  C  CA     . GLU A 1 95  ? -45.039 9.509   -5.731  1.00 75.70  ?  80  GLU A CA     1 
ATOM   642  C  C      . GLU A 1 95  ? -44.116 10.190  -6.764  1.00 78.69  ?  80  GLU A C      1 
ATOM   643  O  O      . GLU A 1 95  ? -43.638 11.299  -6.512  1.00 78.41  ?  80  GLU A O      1 
ATOM   644  C  CB     . GLU A 1 95  ? -44.270 8.454   -4.919  1.00 77.30  ?  80  GLU A CB     1 
ATOM   645  C  CG     . GLU A 1 95  ? -43.269 9.058   -3.945  1.00 90.02  ?  80  GLU A CG     1 
ATOM   646  C  CD     . GLU A 1 95  ? -42.352 8.077   -3.240  1.00 121.35 ?  80  GLU A CD     1 
ATOM   647  O  OE1    . GLU A 1 95  ? -42.834 7.004   -2.808  1.00 120.15 ?  80  GLU A OE1    1 
ATOM   648  O  OE2    . GLU A 1 95  ? -41.152 8.403   -3.088  1.00 118.01 -1 80  GLU A OE2    1 
ATOM   649  N  N      . GLN A 1 96  ? -43.918 9.543   -7.936  1.00 74.32  ?  81  GLN A N      1 
ATOM   650  C  CA     . GLN A 1 96  ? -43.092 10.059  -9.032  1.00 73.58  ?  81  GLN A CA     1 
ATOM   651  C  C      . GLN A 1 96  ? -43.706 11.320  -9.627  1.00 76.63  ?  81  GLN A C      1 
ATOM   652  O  O      . GLN A 1 96  ? -43.014 12.333  -9.759  1.00 74.81  ?  81  GLN A O      1 
ATOM   653  C  CB     . GLN A 1 96  ? -42.864 8.978   -10.098 1.00 74.86  ?  81  GLN A CB     1 
ATOM   654  C  CG     . GLN A 1 96  ? -41.454 9.018   -10.701 1.00 86.79  ?  81  GLN A CG     1 
ATOM   655  C  CD     . GLN A 1 96  ? -41.298 8.191   -11.957 1.00 102.03 ?  81  GLN A CD     1 
ATOM   656  O  OE1    . GLN A 1 96  ? -42.217 7.504   -12.412 1.00 95.71  ?  81  GLN A OE1    1 
ATOM   657  N  NE2    . GLN A 1 96  ? -40.125 8.256   -12.559 1.00 94.66  ?  81  GLN A NE2    1 
ATOM   658  N  N      . ALA A 1 97  ? -45.031 11.274  -9.920  1.00 73.75  ?  82  ALA A N      1 
ATOM   659  C  CA     . ALA A 1 97  ? -45.808 12.404  -10.437 1.00 73.40  ?  82  ALA A CA     1 
ATOM   660  C  C      . ALA A 1 97  ? -45.784 13.579  -9.447  1.00 77.15  ?  82  ALA A C      1 
ATOM   661  O  O      . ALA A 1 97  ? -45.700 14.733  -9.885  1.00 77.98  ?  82  ALA A O      1 
ATOM   662  C  CB     . ALA A 1 97  ? -47.238 11.975  -10.722 1.00 74.12  ?  82  ALA A CB     1 
ATOM   663  N  N      A ASP A 1 98  ? -45.827 13.283  -8.127  0.17 72.95  ?  83  ASP A N      1 
ATOM   664  N  N      B ASP A 1 98  ? -45.838 13.286  -8.128  0.83 73.00  ?  83  ASP A N      1 
ATOM   665  C  CA     A ASP A 1 98  ? -45.778 14.271  -7.045  0.17 72.37  ?  83  ASP A CA     1 
ATOM   666  C  CA     B ASP A 1 98  ? -45.784 14.293  -7.062  0.83 72.36  ?  83  ASP A CA     1 
ATOM   667  C  C      A ASP A 1 98  ? -44.414 14.968  -7.010  0.17 74.69  ?  83  ASP A C      1 
ATOM   668  C  C      B ASP A 1 98  ? -44.414 14.985  -7.045  0.83 74.31  ?  83  ASP A C      1 
ATOM   669  O  O      A ASP A 1 98  ? -44.362 16.176  -6.782  0.17 74.16  ?  83  ASP A O      1 
ATOM   670  O  O      B ASP A 1 98  ? -44.356 16.206  -6.887  0.83 73.31  ?  83  ASP A O      1 
ATOM   671  C  CB     A ASP A 1 98  ? -46.095 13.611  -5.690  0.17 74.37  ?  83  ASP A CB     1 
ATOM   672  C  CB     B ASP A 1 98  ? -46.115 13.673  -5.684  0.83 74.49  ?  83  ASP A CB     1 
ATOM   673  C  CG     A ASP A 1 98  ? -46.469 14.571  -4.572  0.17 84.87  ?  83  ASP A CG     1 
ATOM   674  C  CG     B ASP A 1 98  ? -47.571 13.248  -5.472  0.83 82.36  ?  83  ASP A CG     1 
ATOM   675  O  OD1    A ASP A 1 98  ? -47.274 15.499  -4.824  0.17 85.47  ?  83  ASP A OD1    1 
ATOM   676  O  OD1    B ASP A 1 98  ? -48.478 13.896  -6.055  0.83 82.63  ?  83  ASP A OD1    1 
ATOM   677  O  OD2    A ASP A 1 98  ? -46.021 14.349  -3.429  0.17 90.77  -1 83  ASP A OD2    1 
ATOM   678  O  OD2    B ASP A 1 98  ? -47.804 12.293  -4.693  0.83 85.28  -1 83  ASP A OD2    1 
ATOM   679  N  N      . GLU A 1 99  ? -43.321 14.209  -7.266  1.00 70.16  ?  84  GLU A N      1 
ATOM   680  C  CA     . GLU A 1 99  ? -41.930 14.728  -7.328  1.00 68.34  ?  84  GLU A CA     1 
ATOM   681  C  C      . GLU A 1 99  ? -41.799 15.668  -8.533  1.00 69.27  ?  84  GLU A C      1 
ATOM   682  O  O      . GLU A 1 99  ? -41.245 16.757  -8.395  1.00 68.20  ?  84  GLU A O      1 
ATOM   683  C  CB     . GLU A 1 99  ? -40.890 13.591  -7.426  1.00 69.64  ?  84  GLU A CB     1 
ATOM   684  C  CG     . GLU A 1 99  ? -40.761 12.707  -6.192  1.00 79.80  ?  84  GLU A CG     1 
ATOM   685  C  CD     . GLU A 1 99  ? -40.200 13.354  -4.939  1.00 103.34 ?  84  GLU A CD     1 
ATOM   686  O  OE1    . GLU A 1 99  ? -40.923 13.392  -3.918  1.00 99.98  ?  84  GLU A OE1    1 
ATOM   687  O  OE2    . GLU A 1 99  ? -39.030 13.800  -4.968  1.00 96.79  -1 84  GLU A OE2    1 
ATOM   688  N  N      . VAL A 1 100 ? -42.386 15.272  -9.691  1.00 65.42  ?  85  VAL A N      1 
ATOM   689  C  CA     . VAL A 1 100 ? -42.441 16.059  -10.930 1.00 65.12  ?  85  VAL A CA     1 
ATOM   690  C  C      . VAL A 1 100 ? -43.210 17.371  -10.654 1.00 69.29  ?  85  VAL A C      1 
ATOM   691  O  O      . VAL A 1 100 ? -42.766 18.444  -11.079 1.00 68.35  ?  85  VAL A O      1 
ATOM   692  C  CB     . VAL A 1 100 ? -43.078 15.233  -12.094 1.00 69.20  ?  85  VAL A CB     1 
ATOM   693  C  CG1    . VAL A 1 100 ? -43.364 16.099  -13.322 1.00 68.97  ?  85  VAL A CG1    1 
ATOM   694  C  CG2    . VAL A 1 100 ? -42.192 14.054  -12.480 1.00 69.13  ?  85  VAL A CG2    1 
ATOM   695  N  N      . GLN A 1 101 ? -44.346 17.276  -9.913  1.00 67.11  ?  86  GLN A N      1 
ATOM   696  C  CA     . GLN A 1 101 ? -45.183 18.430  -9.561  1.00 66.94  ?  86  GLN A CA     1 
ATOM   697  C  C      . GLN A 1 101 ? -44.405 19.459  -8.767  1.00 67.61  ?  86  GLN A C      1 
ATOM   698  O  O      . GLN A 1 101 ? -44.420 20.632  -9.131  1.00 66.34  ?  86  GLN A O      1 
ATOM   699  C  CB     . GLN A 1 101 ? -46.451 17.999  -8.804  1.00 68.91  ?  86  GLN A CB     1 
ATOM   700  C  CG     . GLN A 1 101 ? -47.641 17.736  -9.711  1.00 92.59  ?  86  GLN A CG     1 
ATOM   701  C  CD     . GLN A 1 101 ? -48.477 18.973  -9.916  1.00 111.81 ?  86  GLN A CD     1 
ATOM   702  O  OE1    . GLN A 1 101 ? -49.246 19.385  -9.039  1.00 104.87 ?  86  GLN A OE1    1 
ATOM   703  N  NE2    . GLN A 1 101 ? -48.359 19.577  -11.091 1.00 105.08 ?  86  GLN A NE2    1 
ATOM   704  N  N      . LYS A 1 102 ? -43.677 19.013  -7.728  1.00 64.09  ?  87  LYS A N      1 
ATOM   705  C  CA     . LYS A 1 102 ? -42.859 19.879  -6.872  1.00 63.97  ?  87  LYS A CA     1 
ATOM   706  C  C      . LYS A 1 102 ? -41.890 20.730  -7.689  1.00 69.04  ?  87  LYS A C      1 
ATOM   707  O  O      . LYS A 1 102 ? -41.779 21.936  -7.440  1.00 68.13  ?  87  LYS A O      1 
ATOM   708  C  CB     . LYS A 1 102 ? -42.119 19.061  -5.806  1.00 66.15  ?  87  LYS A CB     1 
ATOM   709  C  CG     . LYS A 1 102 ? -43.041 18.449  -4.761  1.00 79.78  ?  87  LYS A CG     1 
ATOM   710  C  CD     . LYS A 1 102 ? -42.383 17.282  -4.041  1.00 89.88  ?  87  LYS A CD     1 
ATOM   711  C  CE     . LYS A 1 102 ? -43.398 16.419  -3.337  1.00 98.68  ?  87  LYS A CE     1 
ATOM   712  N  NZ     . LYS A 1 102 ? -42.754 15.350  -2.532  1.00 105.23 1  87  LYS A NZ     1 
ATOM   713  N  N      . VAL A 1 103 ? -41.240 20.111  -8.710  1.00 66.20  ?  88  VAL A N      1 
ATOM   714  C  CA     . VAL A 1 103 ? -40.307 20.794  -9.615  1.00 65.64  ?  88  VAL A CA     1 
ATOM   715  C  C      . VAL A 1 103 ? -41.043 21.825  -10.452 1.00 68.40  ?  88  VAL A C      1 
ATOM   716  O  O      . VAL A 1 103 ? -40.626 22.981  -10.471 1.00 68.14  ?  88  VAL A O      1 
ATOM   717  C  CB     . VAL A 1 103 ? -39.442 19.841  -10.498 1.00 69.03  ?  88  VAL A CB     1 
ATOM   718  C  CG1    . VAL A 1 103 ? -38.343 20.617  -11.218 1.00 68.66  ?  88  VAL A CG1    1 
ATOM   719  C  CG2    . VAL A 1 103 ? -38.838 18.709  -9.671  1.00 68.63  ?  88  VAL A CG2    1 
ATOM   720  N  N      . LYS A 1 104 ? -42.140 21.428  -11.123 1.00 65.66  ?  89  LYS A N      1 
ATOM   721  C  CA     . LYS A 1 104 ? -42.923 22.362  -11.949 1.00 65.84  ?  89  LYS A CA     1 
ATOM   722  C  C      . LYS A 1 104 ? -43.480 23.545  -11.133 1.00 70.69  ?  89  LYS A C      1 
ATOM   723  O  O      . LYS A 1 104 ? -43.417 24.684  -11.603 1.00 71.19  ?  89  LYS A O      1 
ATOM   724  C  CB     . LYS A 1 104 ? -44.015 21.647  -12.759 1.00 67.71  ?  89  LYS A CB     1 
ATOM   725  C  CG     . LYS A 1 104 ? -43.489 20.766  -13.910 1.00 80.94  ?  89  LYS A CG     1 
ATOM   726  C  CD     . LYS A 1 104 ? -42.634 21.497  -14.974 1.00 88.45  ?  89  LYS A CD     1 
ATOM   727  C  CE     . LYS A 1 104 ? -43.402 22.401  -15.909 1.00 99.10  ?  89  LYS A CE     1 
ATOM   728  N  NZ     . LYS A 1 104 ? -42.510 23.034  -16.917 1.00 107.15 1  89  LYS A NZ     1 
ATOM   729  N  N      A ARG A 1 105 ? -43.965 23.277  -9.908  0.49 67.51  ?  90  ARG A N      1 
ATOM   730  N  N      B ARG A 1 105 ? -43.963 23.279  -9.907  0.51 67.29  ?  90  ARG A N      1 
ATOM   731  C  CA     A ARG A 1 105 ? -44.494 24.292  -8.985  0.49 67.63  ?  90  ARG A CA     1 
ATOM   732  C  CA     B ARG A 1 105 ? -44.495 24.293  -8.984  0.51 67.30  ?  90  ARG A CA     1 
ATOM   733  C  C      A ARG A 1 105 ? -43.383 25.180  -8.379  0.49 72.74  ?  90  ARG A C      1 
ATOM   734  C  C      B ARG A 1 105 ? -43.385 25.204  -8.410  0.51 72.60  ?  90  ARG A C      1 
ATOM   735  O  O      A ARG A 1 105 ? -43.691 26.123  -7.642  0.49 72.43  ?  90  ARG A O      1 
ATOM   736  O  O      B ARG A 1 105 ? -43.696 26.181  -7.721  0.51 72.27  ?  90  ARG A O      1 
ATOM   737  C  CB     A ARG A 1 105 ? -45.352 23.638  -7.885  0.49 67.03  ?  90  ARG A CB     1 
ATOM   738  C  CB     B ARG A 1 105 ? -45.291 23.630  -7.842  0.51 66.10  ?  90  ARG A CB     1 
ATOM   739  C  CG     A ARG A 1 105 ? -46.785 23.343  -8.327  0.49 75.15  ?  90  ARG A CG     1 
ATOM   740  C  CG     B ARG A 1 105 ? -46.657 23.090  -8.261  0.51 72.50  ?  90  ARG A CG     1 
ATOM   741  C  CD     A ARG A 1 105 ? -47.235 21.938  -7.963  0.49 81.20  ?  90  ARG A CD     1 
ATOM   742  C  CD     B ARG A 1 105 ? -47.358 22.419  -7.097  0.51 76.12  ?  90  ARG A CD     1 
ATOM   743  N  NE     A ARG A 1 105 ? -47.502 21.788  -6.530  0.49 85.76  ?  90  ARG A NE     1 
ATOM   744  N  NE     B ARG A 1 105 ? -48.710 21.970  -7.438  0.51 75.54  ?  90  ARG A NE     1 
ATOM   745  C  CZ     A ARG A 1 105 ? -48.713 21.645  -6.000  0.49 93.47  ?  90  ARG A CZ     1 
ATOM   746  C  CZ     B ARG A 1 105 ? -49.556 21.416  -6.573  0.51 85.10  ?  90  ARG A CZ     1 
ATOM   747  N  NH1    A ARG A 1 105 ? -49.788 21.621  -6.778  0.49 78.64  1  90  ARG A NH1    1 
ATOM   748  N  NH1    B ARG A 1 105 ? -49.198 21.233  -5.307  0.51 70.04  1  90  ARG A NH1    1 
ATOM   749  N  NH2    A ARG A 1 105 ? -48.857 21.518  -4.688  0.49 74.25  ?  90  ARG A NH2    1 
ATOM   750  N  NH2    B ARG A 1 105 ? -50.764 21.040  -6.967  0.51 70.03  ?  90  ARG A NH2    1 
ATOM   751  N  N      . SER A 1 106 ? -42.101 24.893  -8.708  1.00 69.75  ?  91  SER A N      1 
ATOM   752  C  CA     . SER A 1 106 ? -40.934 25.658  -8.234  1.00 69.64  ?  91  SER A CA     1 
ATOM   753  C  C      . SER A 1 106 ? -40.407 26.680  -9.257  1.00 74.58  ?  91  SER A C      1 
ATOM   754  O  O      . SER A 1 106 ? -39.195 26.911  -9.338  1.00 74.58  ?  91  SER A O      1 
ATOM   755  C  CB     . SER A 1 106 ? -39.826 24.721  -7.763  1.00 72.90  ?  91  SER A CB     1 
ATOM   756  O  OG     . SER A 1 106 ? -40.244 23.991  -6.623  1.00 82.54  ?  91  SER A OG     1 
ATOM   757  N  N      . GLY A 1 107 ? -41.328 27.318  -9.982  1.00 71.19  ?  92  GLY A N      1 
ATOM   758  C  CA     . GLY A 1 107 ? -41.014 28.345  -10.972 1.00 70.96  ?  92  GLY A CA     1 
ATOM   759  C  C      . GLY A 1 107 ? -41.020 27.875  -12.412 1.00 74.64  ?  92  GLY A C      1 
ATOM   760  O  O      . GLY A 1 107 ? -40.355 28.481  -13.260 1.00 73.99  ?  92  GLY A O      1 
ATOM   761  N  N      . GLY A 1 108 ? -41.781 26.809  -12.683 1.00 71.12  ?  93  GLY A N      1 
ATOM   762  C  CA     . GLY A 1 108 ? -41.912 26.214  -14.012 1.00 71.19  ?  93  GLY A CA     1 
ATOM   763  C  C      . GLY A 1 108 ? -40.619 25.619  -14.536 1.00 73.63  ?  93  GLY A C      1 
ATOM   764  O  O      . GLY A 1 108 ? -40.367 25.652  -15.743 1.00 73.38  ?  93  GLY A O      1 
ATOM   765  N  N      . LEU A 1 109 ? -39.786 25.088  -13.620 1.00 69.13  ?  220 LEU A N      1 
ATOM   766  C  CA     . LEU A 1 109 ? -38.476 24.514  -13.929 1.00 68.72  ?  220 LEU A CA     1 
ATOM   767  C  C      . LEU A 1 109 ? -38.588 23.291  -14.817 1.00 72.51  ?  220 LEU A C      1 
ATOM   768  O  O      . LEU A 1 109 ? -39.527 22.508  -14.651 1.00 72.19  ?  220 LEU A O      1 
ATOM   769  C  CB     . LEU A 1 109 ? -37.699 24.163  -12.637 1.00 68.41  ?  220 LEU A CB     1 
ATOM   770  C  CG     . LEU A 1 109 ? -37.270 25.316  -11.709 1.00 71.83  ?  220 LEU A CG     1 
ATOM   771  C  CD1    . LEU A 1 109 ? -36.729 24.782  -10.394 1.00 71.80  ?  220 LEU A CD1    1 
ATOM   772  C  CD2    . LEU A 1 109 ? -36.234 26.213  -12.358 1.00 73.26  ?  220 LEU A CD2    1 
ATOM   773  N  N      . LEU A 1 110 ? -37.636 23.132  -15.774 1.00 68.74  ?  221 LEU A N      1 
ATOM   774  C  CA     . LEU A 1 110 ? -37.593 21.972  -16.674 1.00 67.73  ?  221 LEU A CA     1 
ATOM   775  C  C      . LEU A 1 110 ? -37.411 20.721  -15.832 1.00 66.95  ?  221 LEU A C      1 
ATOM   776  O  O      . LEU A 1 110 ? -36.610 20.737  -14.895 1.00 66.29  ?  221 LEU A O      1 
ATOM   777  C  CB     . LEU A 1 110 ? -36.435 22.094  -17.681 1.00 68.28  ?  221 LEU A CB     1 
ATOM   778  C  CG     . LEU A 1 110 ? -36.750 22.788  -19.000 1.00 73.83  ?  221 LEU A CG     1 
ATOM   779  C  CD1    . LEU A 1 110 ? -35.533 23.527  -19.522 1.00 74.63  ?  221 LEU A CD1    1 
ATOM   780  C  CD2    . LEU A 1 110 ? -37.211 21.796  -20.042 1.00 77.55  ?  221 LEU A CD2    1 
ATOM   781  N  N      . VAL A 1 111 ? -38.192 19.669  -16.111 1.00 60.66  ?  222 VAL A N      1 
ATOM   782  C  CA     . VAL A 1 111 ? -38.097 18.418  -15.364 1.00 59.91  ?  222 VAL A CA     1 
ATOM   783  C  C      . VAL A 1 111 ? -38.166 17.213  -16.298 1.00 63.83  ?  222 VAL A C      1 
ATOM   784  O  O      . VAL A 1 111 ? -38.901 17.227  -17.291 1.00 64.03  ?  222 VAL A O      1 
ATOM   785  C  CB     . VAL A 1 111 ? -39.099 18.326  -14.178 1.00 63.67  ?  222 VAL A CB     1 
ATOM   786  C  CG1    . VAL A 1 111 ? -40.553 18.265  -14.647 1.00 63.53  ?  222 VAL A CG1    1 
ATOM   787  C  CG2    . VAL A 1 111 ? -38.768 17.167  -13.240 1.00 62.95  ?  222 VAL A CG2    1 
ATOM   788  N  N      . ALA A 1 112 ? -37.366 16.189  -15.982 1.00 59.56  ?  223 ALA A N      1 
ATOM   789  C  CA     . ALA A 1 112 ? -37.302 14.928  -16.718 1.00 59.12  ?  223 ALA A CA     1 
ATOM   790  C  C      . ALA A 1 112 ? -37.678 13.800  -15.778 1.00 59.64  ?  223 ALA A C      1 
ATOM   791  O  O      . ALA A 1 112 ? -37.420 13.883  -14.579 1.00 59.37  ?  223 ALA A O      1 
ATOM   792  C  CB     . ALA A 1 112 ? -35.893 14.704  -17.260 1.00 59.86  ?  223 ALA A CB     1 
ATOM   793  N  N      . ALA A 1 113 ? -38.252 12.732  -16.313 1.00 55.32  ?  224 ALA A N      1 
ATOM   794  C  CA     . ALA A 1 113 ? -38.618 11.597  -15.475 1.00 54.77  ?  224 ALA A CA     1 
ATOM   795  C  C      . ALA A 1 113 ? -38.388 10.297  -16.204 1.00 57.80  ?  224 ALA A C      1 
ATOM   796  O  O      . ALA A 1 113 ? -38.631 10.215  -17.407 1.00 57.23  ?  224 ALA A O      1 
ATOM   797  C  CB     . ALA A 1 113 ? -40.075 11.708  -15.045 1.00 55.76  ?  224 ALA A CB     1 
ATOM   798  N  N      . ALA A 1 114 ? -37.953 9.272   -15.464 1.00 55.33  ?  225 ALA A N      1 
ATOM   799  C  CA     . ALA A 1 114 ? -37.641 7.962   -16.009 1.00 56.55  ?  225 ALA A CA     1 
ATOM   800  C  C      . ALA A 1 114 ? -38.840 7.053   -16.116 1.00 63.76  ?  225 ALA A C      1 
ATOM   801  O  O      . ALA A 1 114 ? -39.676 7.001   -15.205 1.00 63.70  ?  225 ALA A O      1 
ATOM   802  C  CB     . ALA A 1 114 ? -36.565 7.289   -15.174 1.00 57.39  ?  225 ALA A CB     1 
ATOM   803  N  N      . ILE A 1 115 ? -38.892 6.306   -17.228 1.00 62.68  ?  226 ILE A N      1 
ATOM   804  C  CA     . ILE A 1 115 ? -39.892 5.280   -17.552 1.00 64.28  ?  226 ILE A CA     1 
ATOM   805  C  C      . ILE A 1 115 ? -39.163 4.029   -18.056 1.00 71.40  ?  226 ILE A C      1 
ATOM   806  O  O      . ILE A 1 115 ? -38.074 4.141   -18.631 1.00 71.86  ?  226 ILE A O      1 
ATOM   807  C  CB     . ILE A 1 115 ? -41.002 5.770   -18.542 1.00 67.52  ?  226 ILE A CB     1 
ATOM   808  C  CG1    . ILE A 1 115 ? -40.418 6.418   -19.836 1.00 67.41  ?  226 ILE A CG1    1 
ATOM   809  C  CG2    . ILE A 1 115 ? -41.995 6.697   -17.838 1.00 68.29  ?  226 ILE A CG2    1 
ATOM   810  C  CD1    . ILE A 1 115 ? -41.455 6.678   -20.986 1.00 67.77  ?  226 ILE A CD1    1 
ATOM   811  N  N      . GLY A 1 116 ? -39.742 2.861   -17.801 1.00 69.30  ?  227 GLY A N      1 
ATOM   812  C  CA     . GLY A 1 116 ? -39.181 1.581   -18.221 1.00 69.80  ?  227 GLY A CA     1 
ATOM   813  C  C      . GLY A 1 116 ? -39.888 0.999   -19.430 1.00 74.99  ?  227 GLY A C      1 
ATOM   814  O  O      . GLY A 1 116 ? -40.378 1.747   -20.284 1.00 73.83  ?  227 GLY A O      1 
ATOM   815  N  N      . ILE A 1 117 ? -39.921 -0.347  -19.517 1.00 73.19  ?  228 ILE A N      1 
ATOM   816  C  CA     . ILE A 1 117 ? -40.573 -1.100  -20.600 1.00 74.47  ?  228 ILE A CA     1 
ATOM   817  C  C      . ILE A 1 117 ? -41.696 -1.994  -20.057 1.00 82.14  ?  228 ILE A C      1 
ATOM   818  O  O      . ILE A 1 117 ? -42.584 -2.400  -20.819 1.00 81.28  ?  228 ILE A O      1 
ATOM   819  C  CB     . ILE A 1 117 ? -39.577 -1.902  -21.488 1.00 77.55  ?  228 ILE A CB     1 
ATOM   820  C  CG1    . ILE A 1 117 ? -38.593 -2.738  -20.639 1.00 78.20  ?  228 ILE A CG1    1 
ATOM   821  C  CG2    . ILE A 1 117 ? -38.856 -0.986  -22.470 1.00 78.27  ?  228 ILE A CG2    1 
ATOM   822  C  CD1    . ILE A 1 117 ? -38.333 -4.150  -21.164 1.00 88.07  ?  228 ILE A CD1    1 
ATOM   823  N  N      . SER A 1 118 ? -41.646 -2.281  -18.730 1.00 81.33  ?  229 SER A N      1 
ATOM   824  C  CA     . SER A 1 118 ? -42.585 -3.112  -17.968 1.00 82.44  ?  229 SER A CA     1 
ATOM   825  C  C      . SER A 1 118 ? -44.051 -2.667  -18.078 1.00 87.96  ?  229 SER A C      1 
ATOM   826  O  O      . SER A 1 118 ? -44.332 -1.579  -18.582 1.00 87.05  ?  229 SER A O      1 
ATOM   827  C  CB     . SER A 1 118 ? -42.151 -3.206  -16.505 1.00 87.16  ?  229 SER A CB     1 
ATOM   828  O  OG     . SER A 1 118 ? -42.048 -1.932  -15.890 1.00 97.13  ?  229 SER A OG     1 
ATOM   829  N  N      . LYS A 1 119 ? -44.981 -3.525  -17.609 1.00 86.49  ?  230 LYS A N      1 
ATOM   830  C  CA     . LYS A 1 119 ? -46.432 -3.307  -17.661 1.00 87.01  ?  230 LYS A CA     1 
ATOM   831  C  C      . LYS A 1 119 ? -46.890 -1.944  -17.113 1.00 90.90  ?  230 LYS A C      1 
ATOM   832  O  O      . LYS A 1 119 ? -47.717 -1.291  -17.752 1.00 90.55  ?  230 LYS A O      1 
ATOM   833  C  CB     . LYS A 1 119 ? -47.178 -4.463  -16.964 1.00 90.26  ?  230 LYS A CB     1 
ATOM   834  C  CG     . LYS A 1 119 ? -48.616 -4.667  -17.452 1.00 111.76 ?  230 LYS A CG     1 
ATOM   835  C  CD     . LYS A 1 119 ? -48.705 -5.443  -18.776 1.00 125.36 ?  230 LYS A CD     1 
ATOM   836  C  CE     . LYS A 1 119 ? -50.055 -5.275  -19.436 1.00 137.33 ?  230 LYS A CE     1 
ATOM   837  N  NZ     . LYS A 1 119 ? -50.176 -6.099  -20.668 1.00 146.17 1  230 LYS A NZ     1 
ATOM   838  N  N      . ASP A 1 120 ? -46.312 -1.500  -15.974 1.00 87.21  ?  231 ASP A N      1 
ATOM   839  C  CA     . ASP A 1 120 ? -46.639 -0.244  -15.284 1.00 86.89  ?  231 ASP A CA     1 
ATOM   840  C  C      . ASP A 1 120 ? -46.319 1.056   -16.066 1.00 90.49  ?  231 ASP A C      1 
ATOM   841  O  O      . ASP A 1 120 ? -46.792 2.123   -15.664 1.00 89.69  ?  231 ASP A O      1 
ATOM   842  C  CB     . ASP A 1 120 ? -45.977 -0.206  -13.889 1.00 88.77  ?  231 ASP A CB     1 
ATOM   843  C  CG     . ASP A 1 120 ? -44.458 -0.243  -13.879 1.00 98.83  ?  231 ASP A CG     1 
ATOM   844  O  OD1    . ASP A 1 120 ? -43.891 -1.356  -13.777 1.00 99.18  ?  231 ASP A OD1    1 
ATOM   845  O  OD2    . ASP A 1 120 ? -43.837 0.846   -13.900 1.00 103.06 -1 231 ASP A OD2    1 
ATOM   846  N  N      . THR A 1 121 ? -45.544 0.966   -17.171 1.00 86.92  ?  232 THR A N      1 
ATOM   847  C  CA     . THR A 1 121 ? -45.107 2.097   -18.005 1.00 86.71  ?  232 THR A CA     1 
ATOM   848  C  C      . THR A 1 121 ? -46.271 2.939   -18.568 1.00 90.89  ?  232 THR A C      1 
ATOM   849  O  O      . THR A 1 121 ? -46.191 4.174   -18.544 1.00 90.29  ?  232 THR A O      1 
ATOM   850  C  CB     . THR A 1 121 ? -44.160 1.599   -19.116 1.00 92.61  ?  232 THR A CB     1 
ATOM   851  O  OG1    . THR A 1 121 ? -43.103 0.847   -18.521 1.00 87.62  ?  232 THR A OG1    1 
ATOM   852  C  CG2    . THR A 1 121 ? -43.578 2.729   -19.960 1.00 92.17  ?  232 THR A CG2    1 
ATOM   853  N  N      . ASP A 1 122 ? -47.332 2.269   -19.069 1.00 87.16  ?  233 ASP A N      1 
ATOM   854  C  CA     . ASP A 1 122 ? -48.515 2.890   -19.678 1.00 86.53  ?  233 ASP A CA     1 
ATOM   855  C  C      . ASP A 1 122 ? -49.196 3.922   -18.766 1.00 89.30  ?  233 ASP A C      1 
ATOM   856  O  O      . ASP A 1 122 ? -49.410 5.060   -19.195 1.00 89.24  ?  233 ASP A O      1 
ATOM   857  C  CB     . ASP A 1 122 ? -49.508 1.813   -20.170 1.00 88.38  ?  233 ASP A CB     1 
ATOM   858  C  CG     . ASP A 1 122 ? -48.941 0.800   -21.161 1.00 99.02  ?  233 ASP A CG     1 
ATOM   859  O  OD1    . ASP A 1 122 ? -47.738 0.909   -21.513 1.00 99.34  ?  233 ASP A OD1    1 
ATOM   860  O  OD2    . ASP A 1 122 ? -49.693 -0.110  -21.573 1.00 105.22 -1 233 ASP A OD2    1 
ATOM   861  N  N      . ILE A 1 123 ? -49.481 3.547   -17.503 1.00 84.43  ?  234 ILE A N      1 
ATOM   862  C  CA     . ILE A 1 123 ? -50.106 4.450   -16.528 1.00 83.49  ?  234 ILE A CA     1 
ATOM   863  C  C      . ILE A 1 123 ? -49.093 5.482   -15.982 1.00 85.10  ?  234 ILE A C      1 
ATOM   864  O  O      . ILE A 1 123 ? -49.459 6.646   -15.758 1.00 84.17  ?  234 ILE A O      1 
ATOM   865  C  CB     . ILE A 1 123 ? -50.871 3.697   -15.400 1.00 86.86  ?  234 ILE A CB     1 
ATOM   866  C  CG1    . ILE A 1 123 ? -49.950 2.749   -14.578 1.00 87.58  ?  234 ILE A CG1    1 
ATOM   867  C  CG2    . ILE A 1 123 ? -52.093 2.963   -15.969 1.00 87.63  ?  234 ILE A CG2    1 
ATOM   868  C  CD1    . ILE A 1 123 ? -50.385 2.469   -13.121 1.00 95.08  ?  234 ILE A CD1    1 
ATOM   869  N  N      . ARG A 1 124 ? -47.817 5.053   -15.798 1.00 79.61  ?  235 ARG A N      1 
ATOM   870  C  CA     . ARG A 1 124 ? -46.715 5.889   -15.313 1.00 78.09  ?  235 ARG A CA     1 
ATOM   871  C  C      . ARG A 1 124 ? -46.490 7.103   -16.229 1.00 78.43  ?  235 ARG A C      1 
ATOM   872  O  O      . ARG A 1 124 ? -46.482 8.233   -15.739 1.00 77.15  ?  235 ARG A O      1 
ATOM   873  C  CB     . ARG A 1 124 ? -45.429 5.059   -15.164 1.00 78.95  ?  235 ARG A CB     1 
ATOM   874  C  CG     . ARG A 1 124 ? -44.381 5.695   -14.254 1.00 85.39  ?  235 ARG A CG     1 
ATOM   875  C  CD     . ARG A 1 124 ? -43.144 4.823   -14.089 1.00 85.02  ?  235 ARG A CD     1 
ATOM   876  N  NE     . ARG A 1 124 ? -43.321 3.739   -13.117 1.00 87.60  ?  235 ARG A NE     1 
ATOM   877  C  CZ     . ARG A 1 124 ? -43.138 3.854   -11.802 1.00 96.39  ?  235 ARG A CZ     1 
ATOM   878  N  NH1    . ARG A 1 124 ? -42.806 5.025   -11.269 1.00 75.88  1  235 ARG A NH1    1 
ATOM   879  N  NH2    . ARG A 1 124 ? -43.303 2.803   -11.010 1.00 82.99  ?  235 ARG A NH2    1 
ATOM   880  N  N      . ALA A 1 125 ? -46.374 6.867   -17.554 1.00 73.37  ?  236 ALA A N      1 
ATOM   881  C  CA     . ALA A 1 125 ? -46.157 7.905   -18.565 1.00 72.36  ?  236 ALA A CA     1 
ATOM   882  C  C      . ALA A 1 125 ? -47.294 8.929   -18.620 1.00 74.79  ?  236 ALA A C      1 
ATOM   883  O  O      . ALA A 1 125 ? -47.024 10.122  -18.799 1.00 73.62  ?  236 ALA A O      1 
ATOM   884  C  CB     . ALA A 1 125 ? -45.932 7.278   -19.928 1.00 73.02  ?  236 ALA A CB     1 
ATOM   885  N  N      A GLN A 1 126 ? -48.551 8.469   -18.445 0.46 71.19  ?  237 GLN A N      1 
ATOM   886  N  N      B GLN A 1 126 ? -48.554 8.473   -18.448 0.54 71.28  ?  237 GLN A N      1 
ATOM   887  C  CA     A GLN A 1 126 ? -49.746 9.320   -18.441 0.46 70.48  ?  237 GLN A CA     1 
ATOM   888  C  CA     B GLN A 1 126 ? -49.737 9.341   -18.451 0.54 70.54  ?  237 GLN A CA     1 
ATOM   889  C  C      A GLN A 1 126 ? -49.693 10.298  -17.261 0.46 72.63  ?  237 GLN A C      1 
ATOM   890  C  C      B GLN A 1 126 ? -49.694 10.306  -17.259 0.54 72.64  ?  237 GLN A C      1 
ATOM   891  O  O      A GLN A 1 126 ? -49.771 11.508  -17.480 0.46 72.27  ?  237 GLN A O      1 
ATOM   892  O  O      B GLN A 1 126 ? -49.769 11.518  -17.470 0.54 72.29  ?  237 GLN A O      1 
ATOM   893  C  CB     A GLN A 1 126 ? -51.029 8.464   -18.411 0.46 71.87  ?  237 GLN A CB     1 
ATOM   894  C  CB     B GLN A 1 126 ? -51.040 8.510   -18.478 0.54 71.91  ?  237 GLN A CB     1 
ATOM   895  C  CG     A GLN A 1 126 ? -52.310 9.250   -18.709 0.46 85.58  ?  237 GLN A CG     1 
ATOM   896  C  CG     B GLN A 1 126 ? -52.301 9.303   -18.849 0.54 85.06  ?  237 GLN A CG     1 
ATOM   897  C  CD     A GLN A 1 126 ? -53.569 8.617   -18.151 0.46 104.01 ?  237 GLN A CD     1 
ATOM   898  C  CD     B GLN A 1 126 ? -52.419 9.583   -20.330 0.54 103.19 ?  237 GLN A CD     1 
ATOM   899  O  OE1    A GLN A 1 126 ? -53.542 7.761   -17.256 0.46 99.11  ?  237 GLN A OE1    1 
ATOM   900  O  OE1    B GLN A 1 126 ? -52.596 8.677   -21.152 0.54 98.12  ?  237 GLN A OE1    1 
ATOM   901  N  NE2    A GLN A 1 126 ? -54.713 9.064   -18.646 0.46 94.89  ?  237 GLN A NE2    1 
ATOM   902  N  NE2    B GLN A 1 126 ? -52.358 10.853  -20.698 0.54 95.14  ?  237 GLN A NE2    1 
ATOM   903  N  N      . LYS A 1 127 ? -49.498 9.772   -16.030 1.00 68.06  ?  238 LYS A N      1 
ATOM   904  C  CA     . LYS A 1 127 ? -49.405 10.558  -14.785 1.00 67.99  ?  238 LYS A CA     1 
ATOM   905  C  C      . LYS A 1 127 ? -48.251 11.566  -14.789 1.00 72.70  ?  238 LYS A C      1 
ATOM   906  O  O      . LYS A 1 127 ? -48.423 12.695  -14.313 1.00 71.83  ?  238 LYS A O      1 
ATOM   907  C  CB     . LYS A 1 127 ? -49.303 9.638   -13.558 1.00 71.03  ?  238 LYS A CB     1 
ATOM   908  C  CG     . LYS A 1 127 ? -50.634 9.008   -13.136 1.00 90.85  ?  238 LYS A CG     1 
ATOM   909  C  CD     . LYS A 1 127 ? -51.465 9.918   -12.232 1.00 101.21 ?  238 LYS A CD     1 
ATOM   910  C  CE     . LYS A 1 127 ? -52.836 9.355   -11.940 1.00 114.63 ?  238 LYS A CE     1 
ATOM   911  N  NZ     . LYS A 1 127 ? -52.795 8.268   -10.925 1.00 124.13 1  238 LYS A NZ     1 
ATOM   912  N  N      . LEU A 1 128 ? -47.082 11.168  -15.360 1.00 68.74  ?  239 LEU A N      1 
ATOM   913  C  CA     . LEU A 1 128 ? -45.921 12.051  -15.443 1.00 67.96  ?  239 LEU A CA     1 
ATOM   914  C  C      . LEU A 1 128 ? -46.211 13.215  -16.387 1.00 71.30  ?  239 LEU A C      1 
ATOM   915  O  O      . LEU A 1 128 ? -45.969 14.363  -16.007 1.00 69.10  ?  239 LEU A O      1 
ATOM   916  C  CB     . LEU A 1 128 ? -44.635 11.283  -15.818 1.00 67.82  ?  239 LEU A CB     1 
ATOM   917  C  CG     . LEU A 1 128 ? -44.158 10.245  -14.784 1.00 72.14  ?  239 LEU A CG     1 
ATOM   918  C  CD1    . LEU A 1 128 ? -43.273 9.196   -15.416 1.00 72.42  ?  239 LEU A CD1    1 
ATOM   919  C  CD2    . LEU A 1 128 ? -43.477 10.892  -13.595 1.00 73.83  ?  239 LEU A CD2    1 
ATOM   920  N  N      . VAL A 1 129 ? -46.808 12.923  -17.577 1.00 69.28  ?  240 VAL A N      1 
ATOM   921  C  CA     . VAL A 1 129 ? -47.221 13.929  -18.569 1.00 69.98  ?  240 VAL A CA     1 
ATOM   922  C  C      . VAL A 1 129 ? -48.266 14.863  -17.925 1.00 75.86  ?  240 VAL A C      1 
ATOM   923  O  O      . VAL A 1 129 ? -48.134 16.089  -18.039 1.00 75.25  ?  240 VAL A O      1 
ATOM   924  C  CB     . VAL A 1 129 ? -47.701 13.299  -19.914 1.00 74.01  ?  240 VAL A CB     1 
ATOM   925  C  CG1    . VAL A 1 129 ? -48.361 14.336  -20.825 1.00 73.78  ?  240 VAL A CG1    1 
ATOM   926  C  CG2    . VAL A 1 129 ? -46.546 12.626  -20.646 1.00 73.94  ?  240 VAL A CG2    1 
ATOM   927  N  N      . GLU A 1 130 ? -49.252 14.273  -17.191 1.00 73.47  ?  241 GLU A N      1 
ATOM   928  C  CA     . GLU A 1 130 ? -50.307 14.999  -16.460 1.00 73.48  ?  241 GLU A CA     1 
ATOM   929  C  C      . GLU A 1 130 ? -49.702 15.988  -15.463 1.00 75.91  ?  241 GLU A C      1 
ATOM   930  O  O      . GLU A 1 130 ? -50.206 17.105  -15.338 1.00 75.40  ?  241 GLU A O      1 
ATOM   931  C  CB     . GLU A 1 130 ? -51.229 14.023  -15.712 1.00 74.96  ?  241 GLU A CB     1 
ATOM   932  C  CG     . GLU A 1 130 ? -52.333 13.423  -16.567 1.00 85.62  ?  241 GLU A CG     1 
ATOM   933  C  CD     . GLU A 1 130 ? -52.966 12.150  -16.032 1.00 104.46 ?  241 GLU A CD     1 
ATOM   934  O  OE1    . GLU A 1 130 ? -52.629 11.730  -14.901 1.00 89.39  ?  241 GLU A OE1    1 
ATOM   935  O  OE2    . GLU A 1 130 ? -53.802 11.565  -16.758 1.00 103.23 -1 241 GLU A OE2    1 
ATOM   936  N  N      . ALA A 1 131 ? -48.592 15.586  -14.792 1.00 71.09  ?  242 ALA A N      1 
ATOM   937  C  CA     . ALA A 1 131 ? -47.863 16.395  -13.810 1.00 70.33  ?  242 ALA A CA     1 
ATOM   938  C  C      . ALA A 1 131 ? -47.026 17.532  -14.441 1.00 73.13  ?  242 ALA A C      1 
ATOM   939  O  O      . ALA A 1 131 ? -46.424 18.328  -13.714 1.00 73.36  ?  242 ALA A O      1 
ATOM   940  C  CB     . ALA A 1 131 ? -46.998 15.500  -12.928 1.00 70.88  ?  242 ALA A CB     1 
ATOM   941  N  N      . GLY A 1 132 ? -47.037 17.614  -15.774 1.00 68.14  ?  243 GLY A N      1 
ATOM   942  C  CA     . GLY A 1 132 ? -46.345 18.643  -16.540 1.00 67.68  ?  243 GLY A CA     1 
ATOM   943  C  C      . GLY A 1 132 ? -44.889 18.361  -16.872 1.00 71.85  ?  243 GLY A C      1 
ATOM   944  O  O      . GLY A 1 132 ? -44.111 19.310  -17.023 1.00 70.90  ?  243 GLY A O      1 
ATOM   945  N  N      . VAL A 1 133 ? -44.512 17.061  -17.025 1.00 68.52  ?  244 VAL A N      1 
ATOM   946  C  CA     . VAL A 1 133 ? -43.143 16.644  -17.380 1.00 68.51  ?  244 VAL A CA     1 
ATOM   947  C  C      . VAL A 1 133 ? -42.759 17.186  -18.767 1.00 72.64  ?  244 VAL A C      1 
ATOM   948  O  O      . VAL A 1 133 ? -43.618 17.283  -19.646 1.00 73.49  ?  244 VAL A O      1 
ATOM   949  C  CB     . VAL A 1 133 ? -42.908 15.107  -17.223 1.00 72.13  ?  244 VAL A CB     1 
ATOM   950  C  CG1    . VAL A 1 133 ? -43.497 14.306  -18.386 1.00 71.63  ?  244 VAL A CG1    1 
ATOM   951  C  CG2    . VAL A 1 133 ? -41.427 14.784  -17.037 1.00 72.00  ?  244 VAL A CG2    1 
ATOM   952  N  N      . ASP A 1 134 ? -41.490 17.591  -18.939 1.00 67.81  ?  245 ASP A N      1 
ATOM   953  C  CA     . ASP A 1 134 ? -41.001 18.133  -20.206 1.00 66.94  ?  245 ASP A CA     1 
ATOM   954  C  C      . ASP A 1 134 ? -40.360 17.069  -21.086 1.00 70.16  ?  245 ASP A C      1 
ATOM   955  O  O      . ASP A 1 134 ? -40.540 17.082  -22.306 1.00 69.85  ?  245 ASP A O      1 
ATOM   956  C  CB     . ASP A 1 134 ? -40.022 19.284  -19.951 1.00 68.66  ?  245 ASP A CB     1 
ATOM   957  C  CG     . ASP A 1 134 ? -40.699 20.505  -19.357 1.00 79.40  ?  245 ASP A CG     1 
ATOM   958  O  OD1    . ASP A 1 134 ? -41.350 21.252  -20.121 1.00 78.95  ?  245 ASP A OD1    1 
ATOM   959  O  OD2    . ASP A 1 134 ? -40.583 20.708  -18.125 1.00 85.37  -1 245 ASP A OD2    1 
ATOM   960  N  N      . VAL A 1 135 ? -39.609 16.153  -20.461 1.00 66.18  ?  246 VAL A N      1 
ATOM   961  C  CA     . VAL A 1 135 ? -38.875 15.086  -21.143 1.00 65.19  ?  246 VAL A CA     1 
ATOM   962  C  C      . VAL A 1 135 ? -39.102 13.733  -20.453 1.00 66.14  ?  246 VAL A C      1 
ATOM   963  O  O      . VAL A 1 135 ? -39.025 13.638  -19.230 1.00 65.48  ?  246 VAL A O      1 
ATOM   964  C  CB     . VAL A 1 135 ? -37.360 15.454  -21.343 1.00 68.74  ?  246 VAL A CB     1 
ATOM   965  C  CG1    . VAL A 1 135 ? -36.853 16.423  -20.278 1.00 68.47  ?  246 VAL A CG1    1 
ATOM   966  C  CG2    . VAL A 1 135 ? -36.454 14.226  -21.441 1.00 68.41  ?  246 VAL A CG2    1 
ATOM   967  N  N      . LEU A 1 136 ? -39.432 12.702  -21.248 1.00 61.81  ?  247 LEU A N      1 
ATOM   968  C  CA     . LEU A 1 136 ? -39.610 11.331  -20.752 1.00 60.43  ?  247 LEU A CA     1 
ATOM   969  C  C      . LEU A 1 136 ? -38.354 10.535  -21.135 1.00 62.23  ?  247 LEU A C      1 
ATOM   970  O  O      . LEU A 1 136 ? -37.853 10.686  -22.255 1.00 61.13  ?  247 LEU A O      1 
ATOM   971  C  CB     . LEU A 1 136 ? -40.868 10.674  -21.344 1.00 60.34  ?  247 LEU A CB     1 
ATOM   972  C  CG     . LEU A 1 136 ? -42.227 11.114  -20.751 1.00 64.13  ?  247 LEU A CG     1 
ATOM   973  C  CD1    . LEU A 1 136 ? -43.370 10.636  -21.618 1.00 63.86  ?  247 LEU A CD1    1 
ATOM   974  C  CD2    . LEU A 1 136 ? -42.407 10.616  -19.314 1.00 65.29  ?  247 LEU A CD2    1 
ATOM   975  N  N      . VAL A 1 137 ? -37.835 9.722   -20.199 1.00 56.84  ?  248 VAL A N      1 
ATOM   976  C  CA     . VAL A 1 137 ? -36.590 8.966   -20.398 1.00 55.22  ?  248 VAL A CA     1 
ATOM   977  C  C      . VAL A 1 137 ? -36.843 7.467   -20.331 1.00 55.84  ?  248 VAL A C      1 
ATOM   978  O  O      . VAL A 1 137 ? -37.013 6.944   -19.236 1.00 54.30  ?  248 VAL A O      1 
ATOM   979  C  CB     . VAL A 1 137 ? -35.458 9.402   -19.395 1.00 58.39  ?  248 VAL A CB     1 
ATOM   980  C  CG1    . VAL A 1 137 ? -34.125 8.743   -19.738 1.00 58.24  ?  248 VAL A CG1    1 
ATOM   981  C  CG2    . VAL A 1 137 ? -35.294 10.926  -19.322 1.00 57.95  ?  248 VAL A CG2    1 
ATOM   982  N  N      . ILE A 1 138 ? -36.831 6.762   -21.482 1.00 53.17  ?  249 ILE A N      1 
ATOM   983  C  CA     . ILE A 1 138 ? -36.954 5.296   -21.470 1.00 53.20  ?  249 ILE A CA     1 
ATOM   984  C  C      . ILE A 1 138 ? -35.552 4.849   -21.039 1.00 59.57  ?  249 ILE A C      1 
ATOM   985  O  O      . ILE A 1 138 ? -34.597 4.956   -21.814 1.00 59.37  ?  249 ILE A O      1 
ATOM   986  C  CB     . ILE A 1 138 ? -37.431 4.670   -22.816 1.00 56.75  ?  249 ILE A CB     1 
ATOM   987  C  CG1    . ILE A 1 138 ? -38.865 5.146   -23.165 1.00 58.31  ?  249 ILE A CG1    1 
ATOM   988  C  CG2    . ILE A 1 138 ? -37.388 3.137   -22.734 1.00 57.26  ?  249 ILE A CG2    1 
ATOM   989  C  CD1    . ILE A 1 138 ? -39.308 4.964   -24.585 1.00 62.62  ?  249 ILE A CD1    1 
ATOM   990  N  N      . ASP A 1 139 ? -35.425 4.492   -19.756 1.00 57.05  ?  250 ASP A N      1 
ATOM   991  C  CA     . ASP A 1 139 ? -34.164 4.162   -19.109 1.00 56.96  ?  250 ASP A CA     1 
ATOM   992  C  C      . ASP A 1 139 ? -34.006 2.667   -18.920 1.00 59.78  ?  250 ASP A C      1 
ATOM   993  O  O      . ASP A 1 139 ? -34.689 2.082   -18.082 1.00 61.00  ?  250 ASP A O      1 
ATOM   994  C  CB     . ASP A 1 139 ? -34.067 4.907   -17.756 1.00 59.29  ?  250 ASP A CB     1 
ATOM   995  C  CG     . ASP A 1 139 ? -32.819 5.744   -17.516 1.00 77.13  ?  250 ASP A CG     1 
ATOM   996  O  OD1    . ASP A 1 139 ? -31.822 5.553   -18.244 1.00 79.14  ?  250 ASP A OD1    1 
ATOM   997  O  OD2    . ASP A 1 139 ? -32.824 6.556   -16.563 1.00 84.34  -1 250 ASP A OD2    1 
ATOM   998  N  N      . THR A 1 140 ? -33.107 2.047   -19.709 1.00 54.27  ?  251 THR A N      1 
ATOM   999  C  CA     . THR A 1 140 ? -32.815 0.614   -19.632 1.00 53.02  ?  251 THR A CA     1 
ATOM   1000 C  C      . THR A 1 140 ? -31.306 0.309   -19.649 1.00 56.40  ?  251 THR A C      1 
ATOM   1001 O  O      . THR A 1 140 ? -30.493 1.132   -20.085 1.00 56.21  ?  251 THR A O      1 
ATOM   1002 C  CB     . THR A 1 140 ? -33.527 -0.163  -20.753 1.00 59.92  ?  251 THR A CB     1 
ATOM   1003 O  OG1    . THR A 1 140 ? -33.269 -1.559  -20.595 1.00 66.56  ?  251 THR A OG1    1 
ATOM   1004 C  CG2    . THR A 1 140 ? -33.058 0.233   -22.118 1.00 55.56  ?  251 THR A CG2    1 
ATOM   1005 N  N      . ALA A 1 141 ? -30.965 -0.905  -19.229 1.00 51.49  ?  252 ALA A N      1 
ATOM   1006 C  CA     . ALA A 1 141 ? -29.605 -1.419  -19.253 1.00 50.85  ?  252 ALA A CA     1 
ATOM   1007 C  C      . ALA A 1 141 ? -29.193 -1.696  -20.714 1.00 55.28  ?  252 ALA A C      1 
ATOM   1008 O  O      . ALA A 1 141 ? -28.051 -1.427  -21.064 1.00 55.44  ?  252 ALA A O      1 
ATOM   1009 C  CB     . ALA A 1 141 ? -29.545 -2.709  -18.463 1.00 50.88  ?  252 ALA A CB     1 
ATOM   1010 N  N      . HIS A 1 142 ? -30.133 -2.203  -21.560 1.00 49.95  ?  253 HIS A N      1 
ATOM   1011 C  CA     . HIS A 1 142 ? -29.886 -2.597  -22.946 1.00 48.77  ?  253 HIS A CA     1 
ATOM   1012 C  C      . HIS A 1 142 ? -30.936 -2.046  -23.922 1.00 55.30  ?  253 HIS A C      1 
ATOM   1013 O  O      . HIS A 1 142 ? -31.941 -2.705  -24.219 1.00 55.66  ?  253 HIS A O      1 
ATOM   1014 C  CB     . HIS A 1 142 ? -29.744 -4.133  -23.037 1.00 48.63  ?  253 HIS A CB     1 
ATOM   1015 C  CG     . HIS A 1 142 ? -29.255 -4.654  -24.359 1.00 51.23  ?  253 HIS A CG     1 
ATOM   1016 N  ND1    . HIS A 1 142 ? -28.558 -3.856  -25.245 1.00 52.86  ?  253 HIS A ND1    1 
ATOM   1017 C  CD2    . HIS A 1 142 ? -29.327 -5.898  -24.872 1.00 52.31  ?  253 HIS A CD2    1 
ATOM   1018 C  CE1    . HIS A 1 142 ? -28.261 -4.624  -26.275 1.00 51.38  ?  253 HIS A CE1    1 
ATOM   1019 N  NE2    . HIS A 1 142 ? -28.705 -5.858  -26.101 1.00 51.74  ?  253 HIS A NE2    1 
ATOM   1020 N  N      . GLY A 1 143 ? -30.669 -0.833  -24.391 1.00 52.31  ?  254 GLY A N      1 
ATOM   1021 C  CA     . GLY A 1 143 ? -31.492 -0.059  -25.312 1.00 53.46  ?  254 GLY A CA     1 
ATOM   1022 C  C      . GLY A 1 143 ? -31.648 -0.641  -26.699 1.00 60.72  ?  254 GLY A C      1 
ATOM   1023 O  O      . GLY A 1 143 ? -32.651 -0.363  -27.359 1.00 60.21  ?  254 GLY A O      1 
ATOM   1024 N  N      . HIS A 1 144 ? -30.653 -1.429  -27.168 1.00 60.04  ?  255 HIS A N      1 
ATOM   1025 C  CA     . HIS A 1 144 ? -30.696 -2.071  -28.485 1.00 61.22  ?  255 HIS A CA     1 
ATOM   1026 C  C      . HIS A 1 144 ? -31.479 -3.383  -28.394 1.00 67.68  ?  255 HIS A C      1 
ATOM   1027 O  O      . HIS A 1 144 ? -30.927 -4.471  -28.604 1.00 65.75  ?  255 HIS A O      1 
ATOM   1028 C  CB     . HIS A 1 144 ? -29.285 -2.283  -29.062 1.00 62.10  ?  255 HIS A CB     1 
ATOM   1029 C  CG     . HIS A 1 144 ? -29.258 -2.387  -30.560 1.00 65.76  ?  255 HIS A CG     1 
ATOM   1030 N  ND1    . HIS A 1 144 ? -28.153 -2.886  -31.227 1.00 67.39  ?  255 HIS A ND1    1 
ATOM   1031 C  CD2    . HIS A 1 144 ? -30.186 -2.013  -31.475 1.00 67.51  ?  255 HIS A CD2    1 
ATOM   1032 C  CE1    . HIS A 1 144 ? -28.448 -2.813  -32.513 1.00 66.99  ?  255 HIS A CE1    1 
ATOM   1033 N  NE2    . HIS A 1 144 ? -29.664 -2.302  -32.711 1.00 67.32  ?  255 HIS A NE2    1 
ATOM   1034 N  N      A SER A 1 145 ? -32.777 -3.265  -28.073 0.69 66.64  ?  256 SER A N      1 
ATOM   1035 N  N      B SER A 1 145 ? -32.774 -3.274  -28.060 0.31 65.89  ?  256 SER A N      1 
ATOM   1036 C  CA     A SER A 1 145 ? -33.687 -4.395  -27.902 0.69 67.48  ?  256 SER A CA     1 
ATOM   1037 C  CA     B SER A 1 145 ? -33.675 -4.415  -27.917 0.31 66.44  ?  256 SER A CA     1 
ATOM   1038 C  C      A SER A 1 145 ? -35.079 -4.120  -28.487 0.69 72.15  ?  256 SER A C      1 
ATOM   1039 C  C      B SER A 1 145 ? -35.080 -4.129  -28.452 0.31 71.83  ?  256 SER A C      1 
ATOM   1040 O  O      A SER A 1 145 ? -35.459 -2.958  -28.672 0.69 71.44  ?  256 SER A O      1 
ATOM   1041 O  O      B SER A 1 145 ? -35.463 -2.963  -28.591 0.31 71.28  ?  256 SER A O      1 
ATOM   1042 C  CB     A SER A 1 145 ? -33.792 -4.768  -26.424 0.69 71.76  ?  256 SER A CB     1 
ATOM   1043 C  CB     B SER A 1 145 ? -33.713 -4.906  -26.470 0.31 69.85  ?  256 SER A CB     1 
ATOM   1044 O  OG     A SER A 1 145 ? -34.557 -5.949  -26.250 0.69 82.57  ?  256 SER A OG     1 
ATOM   1045 O  OG     B SER A 1 145 ? -34.016 -3.874  -25.551 0.31 77.65  ?  256 SER A OG     1 
ATOM   1046 N  N      . LYS A 1 146 ? -35.829 -5.200  -28.781 1.00 69.87  ?  257 LYS A N      1 
ATOM   1047 C  CA     . LYS A 1 146 ? -37.197 -5.132  -29.325 1.00 70.51  ?  257 LYS A CA     1 
ATOM   1048 C  C      . LYS A 1 146 ? -38.156 -4.450  -28.334 1.00 74.07  ?  257 LYS A C      1 
ATOM   1049 O  O      . LYS A 1 146 ? -38.865 -3.518  -28.723 1.00 73.37  ?  257 LYS A O      1 
ATOM   1050 C  CB     . LYS A 1 146 ? -37.699 -6.535  -29.730 1.00 73.18  ?  257 LYS A CB     1 
ATOM   1051 C  CG     . LYS A 1 146 ? -38.930 -6.529  -30.646 1.00 90.90  ?  257 LYS A CG     1 
ATOM   1052 C  CD     . LYS A 1 146 ? -38.607 -6.096  -32.082 1.00 101.04 ?  257 LYS A CD     1 
ATOM   1053 C  CE     . LYS A 1 146 ? -39.307 -4.823  -32.492 1.00 107.40 ?  257 LYS A CE     1 
ATOM   1054 N  NZ     . LYS A 1 146 ? -40.722 -5.066  -32.879 1.00 115.18 1  257 LYS A NZ     1 
ATOM   1055 N  N      . GLY A 1 147 ? -38.081 -4.858  -27.064 1.00 71.31  ?  258 GLY A N      1 
ATOM   1056 C  CA     . GLY A 1 147 ? -38.873 -4.304  -25.966 1.00 71.32  ?  258 GLY A CA     1 
ATOM   1057 C  C      . GLY A 1 147 ? -38.761 -2.795  -25.840 1.00 75.35  ?  258 GLY A C      1 
ATOM   1058 O  O      . GLY A 1 147 ? -39.753 -2.117  -25.554 1.00 75.64  ?  258 GLY A O      1 
ATOM   1059 N  N      . VAL A 1 148 ? -37.553 -2.258  -26.113 1.00 70.70  ?  259 VAL A N      1 
ATOM   1060 C  CA     . VAL A 1 148 ? -37.256 -0.830  -26.044 1.00 69.79  ?  259 VAL A CA     1 
ATOM   1061 C  C      . VAL A 1 148 ? -37.710 -0.108  -27.320 1.00 74.61  ?  259 VAL A C      1 
ATOM   1062 O  O      . VAL A 1 148 ? -38.303 0.969   -27.208 1.00 73.54  ?  259 VAL A O      1 
ATOM   1063 C  CB     . VAL A 1 148 ? -35.769 -0.567  -25.667 1.00 72.55  ?  259 VAL A CB     1 
ATOM   1064 C  CG1    . VAL A 1 148 ? -35.460 0.925   -25.591 1.00 71.90  ?  259 VAL A CG1    1 
ATOM   1065 C  CG2    . VAL A 1 148 ? -35.435 -1.235  -24.339 1.00 72.25  ?  259 VAL A CG2    1 
ATOM   1066 N  N      . ILE A 1 149 ? -37.453 -0.700  -28.521 1.00 72.14  ?  260 ILE A N      1 
ATOM   1067 C  CA     . ILE A 1 149 ? -37.855 -0.129  -29.821 1.00 72.05  ?  260 ILE A CA     1 
ATOM   1068 C  C      . ILE A 1 149 ? -39.387 0.089   -29.854 1.00 74.93  ?  260 ILE A C      1 
ATOM   1069 O  O      . ILE A 1 149 ? -39.850 1.190   -30.178 1.00 72.63  ?  260 ILE A O      1 
ATOM   1070 C  CB     . ILE A 1 149 ? -37.303 -0.983  -31.013 1.00 75.23  ?  260 ILE A CB     1 
ATOM   1071 C  CG1    . ILE A 1 149 ? -35.801 -0.681  -31.247 1.00 75.82  ?  260 ILE A CG1    1 
ATOM   1072 C  CG2    . ILE A 1 149 ? -38.108 -0.777  -32.315 1.00 75.55  ?  260 ILE A CG2    1 
ATOM   1073 C  CD1    . ILE A 1 149 ? -34.968 -1.845  -31.855 1.00 83.23  ?  260 ILE A CD1    1 
ATOM   1074 N  N      . ASP A 1 150 ? -40.145 -0.952  -29.456 1.00 72.82  ?  261 ASP A N      1 
ATOM   1075 C  CA     . ASP A 1 150 ? -41.611 -0.942  -29.377 1.00 73.13  ?  261 ASP A CA     1 
ATOM   1076 C  C      . ASP A 1 150 ? -42.116 0.157   -28.429 1.00 78.54  ?  261 ASP A C      1 
ATOM   1077 O  O      . ASP A 1 150 ? -43.039 0.891   -28.789 1.00 78.77  ?  261 ASP A O      1 
ATOM   1078 C  CB     . ASP A 1 150 ? -42.137 -2.326  -28.952 1.00 74.53  ?  261 ASP A CB     1 
ATOM   1079 C  CG     . ASP A 1 150 ? -41.885 -3.448  -29.950 1.00 82.57  ?  261 ASP A CG     1 
ATOM   1080 O  OD1    . ASP A 1 150 ? -41.896 -3.174  -31.171 1.00 82.91  ?  261 ASP A OD1    1 
ATOM   1081 O  OD2    . ASP A 1 150 ? -41.706 -4.603  -29.511 1.00 86.92  -1 261 ASP A OD2    1 
ATOM   1082 N  N      . GLN A 1 151 ? -41.472 0.296   -27.245 1.00 75.44  ?  262 GLN A N      1 
ATOM   1083 C  CA     . GLN A 1 151 ? -41.793 1.306   -26.234 1.00 75.29  ?  262 GLN A CA     1 
ATOM   1084 C  C      . GLN A 1 151 ? -41.564 2.711   -26.765 1.00 79.58  ?  262 GLN A C      1 
ATOM   1085 O  O      . GLN A 1 151 ? -42.376 3.591   -26.487 1.00 79.56  ?  262 GLN A O      1 
ATOM   1086 C  CB     . GLN A 1 151 ? -40.990 1.064   -24.945 1.00 76.81  ?  262 GLN A CB     1 
ATOM   1087 C  CG     . GLN A 1 151 ? -41.524 1.787   -23.699 1.00 89.61  ?  262 GLN A CG     1 
ATOM   1088 C  CD     . GLN A 1 151 ? -42.940 1.402   -23.325 1.00 105.71 ?  262 GLN A CD     1 
ATOM   1089 O  OE1    . GLN A 1 151 ? -43.877 2.184   -23.498 1.00 97.85  ?  262 GLN A OE1    1 
ATOM   1090 N  NE2    . GLN A 1 151 ? -43.130 0.195   -22.801 1.00 99.44  ?  262 GLN A NE2    1 
ATOM   1091 N  N      . VAL A 1 152 ? -40.483 2.921   -27.547 1.00 76.32  ?  263 VAL A N      1 
ATOM   1092 C  CA     . VAL A 1 152 ? -40.171 4.225   -28.158 1.00 75.65  ?  263 VAL A CA     1 
ATOM   1093 C  C      . VAL A 1 152 ? -41.313 4.623   -29.123 1.00 80.09  ?  263 VAL A C      1 
ATOM   1094 O  O      . VAL A 1 152 ? -41.830 5.742   -29.026 1.00 79.00  ?  263 VAL A O      1 
ATOM   1095 C  CB     . VAL A 1 152 ? -38.759 4.268   -28.824 1.00 78.66  ?  263 VAL A CB     1 
ATOM   1096 C  CG1    . VAL A 1 152 ? -38.521 5.582   -29.548 1.00 78.26  ?  263 VAL A CG1    1 
ATOM   1097 C  CG2    . VAL A 1 152 ? -37.654 4.040   -27.802 1.00 78.24  ?  263 VAL A CG2    1 
ATOM   1098 N  N      . LYS A 1 153 ? -41.721 3.686   -30.013 1.00 77.30  ?  264 LYS A N      1 
ATOM   1099 C  CA     . LYS A 1 153 ? -42.806 3.867   -30.986 1.00 77.54  ?  264 LYS A CA     1 
ATOM   1100 C  C      . LYS A 1 153 ? -44.112 4.211   -30.260 1.00 83.02  ?  264 LYS A C      1 
ATOM   1101 O  O      . LYS A 1 153 ? -44.777 5.183   -30.624 1.00 82.64  ?  264 LYS A O      1 
ATOM   1102 C  CB     . LYS A 1 153 ? -42.995 2.595   -31.837 1.00 79.89  ?  264 LYS A CB     1 
ATOM   1103 C  CG     . LYS A 1 153 ? -41.915 2.346   -32.883 1.00 86.84  ?  264 LYS A CG     1 
ATOM   1104 C  CD     . LYS A 1 153 ? -42.130 1.011   -33.573 1.00 93.42  ?  264 LYS A CD     1 
ATOM   1105 C  CE     . LYS A 1 153 ? -41.149 0.772   -34.687 1.00 101.33 ?  264 LYS A CE     1 
ATOM   1106 N  NZ     . LYS A 1 153 ? -41.236 -0.623  -35.191 1.00 111.05 1  264 LYS A NZ     1 
ATOM   1107 N  N      . HIS A 1 154 ? -44.430 3.444   -29.195 1.00 80.79  ?  265 HIS A N      1 
ATOM   1108 C  CA     . HIS A 1 154 ? -45.612 3.609   -28.355 1.00 81.36  ?  265 HIS A CA     1 
ATOM   1109 C  C      . HIS A 1 154 ? -45.652 4.986   -27.688 1.00 84.49  ?  265 HIS A C      1 
ATOM   1110 O  O      . HIS A 1 154 ? -46.572 5.757   -27.969 1.00 84.28  ?  265 HIS A O      1 
ATOM   1111 C  CB     . HIS A 1 154 ? -45.703 2.464   -27.327 1.00 82.96  ?  265 HIS A CB     1 
ATOM   1112 C  CG     . HIS A 1 154 ? -46.940 2.472   -26.474 1.00 87.18  ?  265 HIS A CG     1 
ATOM   1113 N  ND1    . HIS A 1 154 ? -48.193 2.766   -27.004 1.00 89.29  ?  265 HIS A ND1    1 
ATOM   1114 C  CD2    . HIS A 1 154 ? -47.084 2.167   -25.162 1.00 89.34  ?  265 HIS A CD2    1 
ATOM   1115 C  CE1    . HIS A 1 154 ? -49.044 2.656   -25.995 1.00 88.89  ?  265 HIS A CE1    1 
ATOM   1116 N  NE2    . HIS A 1 154 ? -48.426 2.293   -24.868 1.00 89.21  ?  265 HIS A NE2    1 
ATOM   1117 N  N      . ILE A 1 155 ? -44.629 5.320   -26.866 1.00 79.68  ?  266 ILE A N      1 
ATOM   1118 C  CA     . ILE A 1 155 ? -44.540 6.601   -26.150 1.00 78.82  ?  266 ILE A CA     1 
ATOM   1119 C  C      . ILE A 1 155 ? -44.564 7.802   -27.111 1.00 82.90  ?  266 ILE A C      1 
ATOM   1120 O  O      . ILE A 1 155 ? -45.221 8.791   -26.793 1.00 82.86  ?  266 ILE A O      1 
ATOM   1121 C  CB     . ILE A 1 155 ? -43.336 6.655   -25.144 1.00 81.23  ?  266 ILE A CB     1 
ATOM   1122 C  CG1    . ILE A 1 155 ? -43.391 5.523   -24.074 1.00 81.26  ?  266 ILE A CG1    1 
ATOM   1123 C  CG2    . ILE A 1 155 ? -43.172 8.033   -24.484 1.00 81.59  ?  266 ILE A CG2    1 
ATOM   1124 C  CD1    . ILE A 1 155 ? -44.637 5.491   -23.075 1.00 88.52  ?  266 ILE A CD1    1 
ATOM   1125 N  N      . LYS A 1 156 ? -43.890 7.716   -28.280 1.00 80.04  ?  267 LYS A N      1 
ATOM   1126 C  CA     . LYS A 1 156 ? -43.866 8.834   -29.232 1.00 79.93  ?  267 LYS A CA     1 
ATOM   1127 C  C      . LYS A 1 156 ? -45.211 9.038   -29.959 1.00 85.84  ?  267 LYS A C      1 
ATOM   1128 O  O      . LYS A 1 156 ? -45.568 10.185  -30.253 1.00 85.74  ?  267 LYS A O      1 
ATOM   1129 C  CB     . LYS A 1 156 ? -42.690 8.724   -30.223 1.00 81.65  ?  267 LYS A CB     1 
ATOM   1130 C  CG     . LYS A 1 156 ? -42.318 10.040  -30.923 1.00 89.29  ?  267 LYS A CG     1 
ATOM   1131 C  CD     . LYS A 1 156 ? -41.869 11.140  -29.951 1.00 97.47  ?  267 LYS A CD     1 
ATOM   1132 C  CE     . LYS A 1 156 ? -41.555 12.433  -30.657 1.00 108.26 ?  267 LYS A CE     1 
ATOM   1133 N  NZ     . LYS A 1 156 ? -41.249 13.521  -29.694 1.00 115.06 1  267 LYS A NZ     1 
ATOM   1134 N  N      . LYS A 1 157 ? -45.957 7.944   -30.233 1.00 83.23  ?  268 LYS A N      1 
ATOM   1135 C  CA     . LYS A 1 157 ? -47.264 8.030   -30.894 1.00 83.48  ?  268 LYS A CA     1 
ATOM   1136 C  C      . LYS A 1 157 ? -48.279 8.652   -29.918 1.00 87.07  ?  268 LYS A C      1 
ATOM   1137 O  O      . LYS A 1 157 ? -48.922 9.646   -30.262 1.00 86.94  ?  268 LYS A O      1 
ATOM   1138 C  CB     . LYS A 1 157 ? -47.733 6.648   -31.394 1.00 86.47  ?  268 LYS A CB     1 
ATOM   1139 C  CG     . LYS A 1 157 ? -48.904 6.717   -32.375 1.00 102.59 ?  268 LYS A CG     1 
ATOM   1140 C  CD     . LYS A 1 157 ? -49.414 5.335   -32.774 1.00 113.48 ?  268 LYS A CD     1 
ATOM   1141 C  CE     . LYS A 1 157 ? -50.699 5.393   -33.572 1.00 122.14 ?  268 LYS A CE     1 
ATOM   1142 N  NZ     . LYS A 1 157 ? -50.482 5.860   -34.967 1.00 128.05 1  268 LYS A NZ     1 
ATOM   1143 N  N      . THR A 1 158 ? -48.359 8.094   -28.686 1.00 82.68  ?  269 THR A N      1 
ATOM   1144 C  CA     . THR A 1 158 ? -49.235 8.529   -27.594 1.00 82.11  ?  269 THR A CA     1 
ATOM   1145 C  C      . THR A 1 158 ? -48.944 9.970   -27.134 1.00 86.96  ?  269 THR A C      1 
ATOM   1146 O  O      . THR A 1 158 ? -49.887 10.736  -26.934 1.00 86.57  ?  269 THR A O      1 
ATOM   1147 C  CB     . THR A 1 158 ? -49.183 7.517   -26.435 1.00 84.25  ?  269 THR A CB     1 
ATOM   1148 O  OG1    . THR A 1 158 ? -49.305 6.193   -26.955 1.00 79.35  ?  269 THR A OG1    1 
ATOM   1149 C  CG2    . THR A 1 158 ? -50.274 7.751   -25.401 1.00 83.37  ?  269 THR A CG2    1 
ATOM   1150 N  N      . TYR A 1 159 ? -47.655 10.338  -26.963 1.00 84.11  ?  270 TYR A N      1 
ATOM   1151 C  CA     . TYR A 1 159 ? -47.274 11.679  -26.505 1.00 84.28  ?  270 TYR A CA     1 
ATOM   1152 C  C      . TYR A 1 159 ? -46.276 12.380  -27.461 1.00 90.67  ?  270 TYR A C      1 
ATOM   1153 O  O      . TYR A 1 159 ? -45.100 12.525  -27.105 1.00 91.04  ?  270 TYR A O      1 
ATOM   1154 C  CB     . TYR A 1 159 ? -46.749 11.658  -25.045 1.00 84.95  ?  270 TYR A CB     1 
ATOM   1155 C  CG     . TYR A 1 159 ? -47.471 10.705  -24.117 1.00 86.09  ?  270 TYR A CG     1 
ATOM   1156 C  CD1    . TYR A 1 159 ? -48.677 11.061  -23.517 1.00 88.07  ?  270 TYR A CD1    1 
ATOM   1157 C  CD2    . TYR A 1 159 ? -46.940 9.453   -23.821 1.00 86.60  ?  270 TYR A CD2    1 
ATOM   1158 C  CE1    . TYR A 1 159 ? -49.344 10.186  -22.658 1.00 88.79  ?  270 TYR A CE1    1 
ATOM   1159 C  CE2    . TYR A 1 159 ? -47.598 8.570   -22.966 1.00 87.47  ?  270 TYR A CE2    1 
ATOM   1160 C  CZ     . TYR A 1 159 ? -48.798 8.942   -22.383 1.00 95.52  ?  270 TYR A CZ     1 
ATOM   1161 O  OH     . TYR A 1 159 ? -49.454 8.062   -21.558 1.00 97.20  ?  270 TYR A OH     1 
ATOM   1162 N  N      . PRO A 1 160 ? -46.713 12.853  -28.657 1.00 88.17  ?  271 PRO A N      1 
ATOM   1163 C  CA     . PRO A 1 160 ? -45.765 13.515  -29.574 1.00 88.26  ?  271 PRO A CA     1 
ATOM   1164 C  C      . PRO A 1 160 ? -45.235 14.885  -29.124 1.00 92.38  ?  271 PRO A C      1 
ATOM   1165 O  O      . PRO A 1 160 ? -44.219 15.335  -29.658 1.00 92.41  ?  271 PRO A O      1 
ATOM   1166 C  CB     . PRO A 1 160 ? -46.546 13.610  -30.887 1.00 90.15  ?  271 PRO A CB     1 
ATOM   1167 C  CG     . PRO A 1 160 ? -47.968 13.645  -30.474 1.00 94.61  ?  271 PRO A CG     1 
ATOM   1168 C  CD     . PRO A 1 160 ? -48.062 12.767  -29.259 1.00 90.17  ?  271 PRO A CD     1 
ATOM   1169 N  N      . GLU A 1 161 ? -45.906 15.548  -28.161 1.00 88.33  ?  272 GLU A N      1 
ATOM   1170 C  CA     . GLU A 1 161 ? -45.476 16.859  -27.652 1.00 87.59  ?  272 GLU A CA     1 
ATOM   1171 C  C      . GLU A 1 161 ? -44.382 16.759  -26.575 1.00 88.98  ?  272 GLU A C      1 
ATOM   1172 O  O      . GLU A 1 161 ? -43.696 17.755  -26.318 1.00 88.63  ?  272 GLU A O      1 
ATOM   1173 C  CB     . GLU A 1 161 ? -46.672 17.689  -27.144 1.00 89.16  ?  272 GLU A CB     1 
ATOM   1174 C  CG     . GLU A 1 161 ? -47.462 18.380  -28.243 1.00 100.97 ?  272 GLU A CG     1 
ATOM   1175 C  CD     . GLU A 1 161 ? -46.889 19.708  -28.700 1.00 121.34 ?  272 GLU A CD     1 
ATOM   1176 O  OE1    . GLU A 1 161 ? -47.002 20.698  -27.940 1.00 108.20 ?  272 GLU A OE1    1 
ATOM   1177 O  OE2    . GLU A 1 161 ? -46.341 19.764  -29.824 1.00 117.09 -1 272 GLU A OE2    1 
ATOM   1178 N  N      . ILE A 1 162 ? -44.219 15.573  -25.947 1.00 83.30  ?  273 ILE A N      1 
ATOM   1179 C  CA     . ILE A 1 162 ? -43.201 15.363  -24.906 1.00 82.40  ?  273 ILE A CA     1 
ATOM   1180 C  C      . ILE A 1 162 ? -41.883 14.823  -25.502 1.00 82.59  ?  273 ILE A C      1 
ATOM   1181 O  O      . ILE A 1 162 ? -41.896 13.799  -26.197 1.00 81.91  ?  273 ILE A O      1 
ATOM   1182 C  CB     . ILE A 1 162 ? -43.727 14.493  -23.715 1.00 85.74  ?  273 ILE A CB     1 
ATOM   1183 C  CG1    . ILE A 1 162 ? -45.094 15.008  -23.151 1.00 85.96  ?  273 ILE A CG1    1 
ATOM   1184 C  CG2    . ILE A 1 162 ? -42.663 14.331  -22.601 1.00 86.48  ?  273 ILE A CG2    1 
ATOM   1185 C  CD1    . ILE A 1 162 ? -45.157 16.478  -22.555 1.00 92.28  ?  273 ILE A CD1    1 
ATOM   1186 N  N      . THR A 1 163 ? -40.753 15.523  -25.215 1.00 76.19  ?  274 THR A N      1 
ATOM   1187 C  CA     . THR A 1 163 ? -39.402 15.157  -25.663 1.00 74.11  ?  274 THR A CA     1 
ATOM   1188 C  C      . THR A 1 163 ? -39.018 13.770  -25.114 1.00 73.01  ?  274 THR A C      1 
ATOM   1189 O  O      . THR A 1 163 ? -39.002 13.575  -23.896 1.00 72.16  ?  274 THR A O      1 
ATOM   1190 C  CB     . THR A 1 163 ? -38.387 16.256  -25.292 1.00 82.15  ?  274 THR A CB     1 
ATOM   1191 O  OG1    . THR A 1 163 ? -38.697 17.447  -26.011 1.00 84.94  ?  274 THR A OG1    1 
ATOM   1192 C  CG2    . THR A 1 163 ? -36.955 15.856  -25.604 1.00 80.67  ?  274 THR A CG2    1 
ATOM   1193 N  N      . LEU A 1 164 ? -38.732 12.809  -26.014 1.00 65.81  ?  275 LEU A N      1 
ATOM   1194 C  CA     . LEU A 1 164 ? -38.382 11.452  -25.600 1.00 63.43  ?  275 LEU A CA     1 
ATOM   1195 C  C      . LEU A 1 164 ? -36.878 11.126  -25.704 1.00 62.09  ?  275 LEU A C      1 
ATOM   1196 O  O      . LEU A 1 164 ? -36.289 11.260  -26.779 1.00 60.58  ?  275 LEU A O      1 
ATOM   1197 C  CB     . LEU A 1 164 ? -39.225 10.407  -26.360 1.00 63.17  ?  275 LEU A CB     1 
ATOM   1198 C  CG     . LEU A 1 164 ? -39.081 8.934   -25.936 1.00 67.12  ?  275 LEU A CG     1 
ATOM   1199 C  CD1    . LEU A 1 164 ? -39.519 8.706   -24.496 1.00 67.58  ?  275 LEU A CD1    1 
ATOM   1200 C  CD2    . LEU A 1 164 ? -39.872 8.028   -26.846 1.00 69.22  ?  275 LEU A CD2    1 
ATOM   1201 N  N      . VAL A 1 165 ? -36.279 10.703  -24.567 1.00 55.55  ?  276 VAL A N      1 
ATOM   1202 C  CA     . VAL A 1 165 ? -34.890 10.222  -24.468 1.00 53.59  ?  276 VAL A CA     1 
ATOM   1203 C  C      . VAL A 1 165 ? -35.035 8.708   -24.384 1.00 55.94  ?  276 VAL A C      1 
ATOM   1204 O  O      . VAL A 1 165 ? -35.910 8.223   -23.665 1.00 57.40  ?  276 VAL A O      1 
ATOM   1205 C  CB     . VAL A 1 165 ? -34.089 10.760  -23.231 1.00 56.10  ?  276 VAL A CB     1 
ATOM   1206 C  CG1    . VAL A 1 165 ? -32.730 10.060  -23.093 1.00 55.19  ?  276 VAL A CG1    1 
ATOM   1207 C  CG2    . VAL A 1 165 ? -33.900 12.270  -23.279 1.00 55.35  ?  276 VAL A CG2    1 
ATOM   1208 N  N      . ALA A 1 166 ? -34.213 7.969   -25.137 1.00 50.69  ?  277 ALA A N      1 
ATOM   1209 C  CA     . ALA A 1 166 ? -34.158 6.509   -25.096 1.00 49.12  ?  277 ALA A CA     1 
ATOM   1210 C  C      . ALA A 1 166 ? -32.683 6.053   -25.042 1.00 51.73  ?  277 ALA A C      1 
ATOM   1211 O  O      . ALA A 1 166 ? -31.830 6.656   -25.687 1.00 50.27  ?  277 ALA A O      1 
ATOM   1212 C  CB     . ALA A 1 166 ? -34.858 5.909   -26.303 1.00 49.61  ?  277 ALA A CB     1 
ATOM   1213 N  N      . GLY A 1 167 ? -32.424 5.003   -24.279 1.00 48.76  ?  278 GLY A N      1 
ATOM   1214 C  CA     . GLY A 1 167 ? -31.103 4.404   -24.095 1.00 49.46  ?  278 GLY A CA     1 
ATOM   1215 C  C      . GLY A 1 167 ? -31.187 3.242   -23.120 1.00 54.68  ?  278 GLY A C      1 
ATOM   1216 O  O      . GLY A 1 167 ? -32.292 2.879   -22.729 1.00 54.95  ?  278 GLY A O      1 
ATOM   1217 N  N      . ASN A 1 168 ? -30.063 2.647   -22.675 1.00 51.55  ?  279 ASN A N      1 
ATOM   1218 C  CA     . ASN A 1 168 ? -28.680 2.992   -23.029 1.00 50.80  ?  279 ASN A CA     1 
ATOM   1219 C  C      . ASN A 1 168 ? -28.142 2.128   -24.163 1.00 50.56  ?  279 ASN A C      1 
ATOM   1220 O  O      . ASN A 1 168 ? -28.497 0.954   -24.275 1.00 49.19  ?  279 ASN A O      1 
ATOM   1221 C  CB     . ASN A 1 168 ? -27.766 2.940   -21.782 1.00 51.34  ?  279 ASN A CB     1 
ATOM   1222 C  CG     . ASN A 1 168 ? -27.752 4.222   -20.972 1.00 66.36  ?  279 ASN A CG     1 
ATOM   1223 O  OD1    . ASN A 1 168 ? -28.729 4.979   -20.936 1.00 63.86  ?  279 ASN A OD1    1 
ATOM   1224 N  ND2    . ASN A 1 168 ? -26.642 4.501   -20.296 1.00 53.66  ?  279 ASN A ND2    1 
ATOM   1225 N  N      . VAL A 1 169 ? -27.319 2.739   -25.030 1.00 45.54  ?  280 VAL A N      1 
ATOM   1226 C  CA     . VAL A 1 169 ? -26.717 2.092   -26.205 1.00 45.03  ?  280 VAL A CA     1 
ATOM   1227 C  C      . VAL A 1 169 ? -25.212 2.456   -26.294 1.00 45.55  ?  280 VAL A C      1 
ATOM   1228 O  O      . VAL A 1 169 ? -24.762 3.369   -25.600 1.00 43.99  ?  280 VAL A O      1 
ATOM   1229 C  CB     . VAL A 1 169 ? -27.461 2.446   -27.534 1.00 49.00  ?  280 VAL A CB     1 
ATOM   1230 C  CG1    . VAL A 1 169 ? -28.959 2.168   -27.442 1.00 49.69  ?  280 VAL A CG1    1 
ATOM   1231 C  CG2    . VAL A 1 169 ? -27.203 3.888   -27.955 1.00 48.54  ?  280 VAL A CG2    1 
ATOM   1232 N  N      . ALA A 1 170 ? -24.460 1.794   -27.184 1.00 43.81  ?  281 ALA A N      1 
ATOM   1233 C  CA     . ALA A 1 170 ? -23.013 2.084   -27.334 1.00 43.95  ?  281 ALA A CA     1 
ATOM   1234 C  C      . ALA A 1 170 ? -22.495 1.912   -28.779 1.00 47.06  ?  281 ALA A C      1 
ATOM   1235 O  O      . ALA A 1 170 ? -21.275 1.906   -29.015 1.00 44.17  ?  281 ALA A O      1 
ATOM   1236 C  CB     . ALA A 1 170 ? -22.216 1.206   -26.375 1.00 44.57  ?  281 ALA A CB     1 
ATOM   1237 N  N      . THR A 1 171 ? -23.420 1.748   -29.736 1.00 44.61  ?  282 THR A N      1 
ATOM   1238 C  CA     . THR A 1 171 ? -23.070 1.576   -31.152 1.00 45.49  ?  282 THR A CA     1 
ATOM   1239 C  C      . THR A 1 171 ? -23.910 2.507   -32.046 1.00 51.05  ?  282 THR A C      1 
ATOM   1240 O  O      . THR A 1 171 ? -24.998 2.930   -31.644 1.00 52.26  ?  282 THR A O      1 
ATOM   1241 C  CB     . THR A 1 171 ? -23.323 0.118   -31.610 1.00 48.19  ?  282 THR A CB     1 
ATOM   1242 O  OG1    . THR A 1 171 ? -24.726 -0.078  -31.746 1.00 53.85  ?  282 THR A OG1    1 
ATOM   1243 C  CG2    . THR A 1 171 ? -22.744 -0.934  -30.680 1.00 43.83  ?  282 THR A CG2    1 
ATOM   1244 N  N      . ALA A 1 172 ? -23.447 2.721   -33.292 1.00 47.13  ?  283 ALA A N      1 
ATOM   1245 C  CA     . ALA A 1 172 ? -24.131 3.486   -34.330 1.00 47.19  ?  283 ALA A CA     1 
ATOM   1246 C  C      . ALA A 1 172 ? -25.468 2.811   -34.712 1.00 52.71  ?  283 ALA A C      1 
ATOM   1247 O  O      . ALA A 1 172 ? -26.474 3.513   -34.816 1.00 52.42  ?  283 ALA A O      1 
ATOM   1248 C  CB     . ALA A 1 172 ? -23.241 3.602   -35.561 1.00 48.03  ?  283 ALA A CB     1 
ATOM   1249 N  N      . GLU A 1 173 ? -25.473 1.465   -34.903 1.00 49.21  ?  284 GLU A N      1 
ATOM   1250 C  CA     . GLU A 1 173 ? -26.661 0.686   -35.284 1.00 49.82  ?  284 GLU A CA     1 
ATOM   1251 C  C      . GLU A 1 173 ? -27.815 0.875   -34.273 1.00 54.27  ?  284 GLU A C      1 
ATOM   1252 O  O      . GLU A 1 173 ? -28.963 1.074   -34.685 1.00 52.74  ?  284 GLU A O      1 
ATOM   1253 C  CB     . GLU A 1 173 ? -26.307 -0.802  -35.457 1.00 50.53  ?  284 GLU A CB     1 
ATOM   1254 C  CG     . GLU A 1 173 ? -27.394 -1.624  -36.131 1.00 61.51  ?  284 GLU A CG     1 
ATOM   1255 C  CD     . GLU A 1 173 ? -27.066 -3.093  -36.341 1.00 80.93  ?  284 GLU A CD     1 
ATOM   1256 O  OE1    . GLU A 1 173 ? -26.295 -3.406  -37.277 1.00 70.30  ?  284 GLU A OE1    1 
ATOM   1257 O  OE2    . GLU A 1 173 ? -27.609 -3.936  -35.592 1.00 78.01  -1 284 GLU A OE2    1 
ATOM   1258 N  N      . ALA A 1 174 ? -27.485 0.848   -32.967 1.00 51.08  ?  285 ALA A N      1 
ATOM   1259 C  CA     . ALA A 1 174 ? -28.415 1.038   -31.858 1.00 50.75  ?  285 ALA A CA     1 
ATOM   1260 C  C      . ALA A 1 174 ? -28.971 2.451   -31.824 1.00 55.18  ?  285 ALA A C      1 
ATOM   1261 O  O      . ALA A 1 174 ? -30.178 2.627   -31.624 1.00 55.65  ?  285 ALA A O      1 
ATOM   1262 C  CB     . ALA A 1 174 ? -27.736 0.698   -30.550 1.00 51.47  ?  285 ALA A CB     1 
ATOM   1263 N  N      . THR A 1 175 ? -28.110 3.448   -32.093 1.00 50.96  ?  286 THR A N      1 
ATOM   1264 C  CA     . THR A 1 175 ? -28.448 4.869   -32.138 1.00 51.13  ?  286 THR A CA     1 
ATOM   1265 C  C      . THR A 1 175 ? -29.408 5.148   -33.320 1.00 57.43  ?  286 THR A C      1 
ATOM   1266 O  O      . THR A 1 175 ? -30.361 5.914   -33.163 1.00 55.23  ?  286 THR A O      1 
ATOM   1267 C  CB     . THR A 1 175 ? -27.159 5.681   -32.167 1.00 50.62  ?  286 THR A CB     1 
ATOM   1268 O  OG1    . THR A 1 175 ? -26.453 5.461   -30.931 1.00 48.09  ?  286 THR A OG1    1 
ATOM   1269 C  CG2    . THR A 1 175 ? -27.390 7.158   -32.421 1.00 44.20  ?  286 THR A CG2    1 
ATOM   1270 N  N      . LYS A 1 176 ? -29.142 4.504   -34.484 1.00 56.12  ?  287 LYS A N      1 
ATOM   1271 C  CA     . LYS A 1 176 ? -29.933 4.596   -35.721 1.00 56.72  ?  287 LYS A CA     1 
ATOM   1272 C  C      . LYS A 1 176 ? -31.343 4.112   -35.439 1.00 60.65  ?  287 LYS A C      1 
ATOM   1273 O  O      . LYS A 1 176 ? -32.292 4.866   -35.627 1.00 61.28  ?  287 LYS A O      1 
ATOM   1274 C  CB     . LYS A 1 176 ? -29.285 3.742   -36.837 1.00 59.38  ?  287 LYS A CB     1 
ATOM   1275 C  CG     . LYS A 1 176 ? -29.956 3.870   -38.208 1.00 67.57  ?  287 LYS A CG     1 
ATOM   1276 C  CD     . LYS A 1 176 ? -29.227 3.032   -39.254 1.00 79.66  ?  287 LYS A CD     1 
ATOM   1277 C  CE     . LYS A 1 176 ? -29.451 3.528   -40.665 1.00 92.79  ?  287 LYS A CE     1 
ATOM   1278 N  NZ     . LYS A 1 176 ? -30.744 3.055   -41.224 1.00 102.89 1  287 LYS A NZ     1 
ATOM   1279 N  N      . ASP A 1 177 ? -31.458 2.877   -34.930 1.00 57.60  ?  288 ASP A N      1 
ATOM   1280 C  CA     . ASP A 1 177 ? -32.702 2.206   -34.576 1.00 57.42  ?  288 ASP A CA     1 
ATOM   1281 C  C      . ASP A 1 177 ? -33.552 2.951   -33.562 1.00 62.44  ?  288 ASP A C      1 
ATOM   1282 O  O      . ASP A 1 177 ? -34.772 2.880   -33.653 1.00 61.78  ?  288 ASP A O      1 
ATOM   1283 C  CB     . ASP A 1 177 ? -32.428 0.773   -34.102 1.00 59.24  ?  288 ASP A CB     1 
ATOM   1284 C  CG     . ASP A 1 177 ? -31.907 -0.154  -35.193 1.00 65.74  ?  288 ASP A CG     1 
ATOM   1285 O  OD1    . ASP A 1 177 ? -31.639 -1.337  -34.888 1.00 66.39  ?  288 ASP A OD1    1 
ATOM   1286 O  OD2    . ASP A 1 177 ? -31.743 0.314   -36.350 1.00 66.90  -1 288 ASP A OD2    1 
ATOM   1287 N  N      . LEU A 1 178 ? -32.937 3.676   -32.615 1.00 59.09  ?  289 LEU A N      1 
ATOM   1288 C  CA     . LEU A 1 178 ? -33.722 4.415   -31.630 1.00 58.70  ?  289 LEU A CA     1 
ATOM   1289 C  C      . LEU A 1 178 ? -34.275 5.683   -32.218 1.00 63.18  ?  289 LEU A C      1 
ATOM   1290 O  O      . LEU A 1 178 ? -35.436 6.029   -31.955 1.00 63.85  ?  289 LEU A O      1 
ATOM   1291 C  CB     . LEU A 1 178 ? -32.929 4.704   -30.345 1.00 58.58  ?  289 LEU A CB     1 
ATOM   1292 C  CG     . LEU A 1 178 ? -32.707 3.541   -29.379 1.00 62.67  ?  289 LEU A CG     1 
ATOM   1293 C  CD1    . LEU A 1 178 ? -32.046 4.041   -28.110 1.00 62.86  ?  289 LEU A CD1    1 
ATOM   1294 C  CD2    . LEU A 1 178 ? -34.017 2.857   -29.010 1.00 64.29  ?  289 LEU A CD2    1 
ATOM   1295 N  N      . PHE A 1 179 ? -33.454 6.366   -33.041 1.00 58.30  ?  290 PHE A N      1 
ATOM   1296 C  CA     . PHE A 1 179 ? -33.843 7.595   -33.718 1.00 57.55  ?  290 PHE A CA     1 
ATOM   1297 C  C      . PHE A 1 179 ? -34.963 7.328   -34.726 1.00 65.43  ?  290 PHE A C      1 
ATOM   1298 O  O      . PHE A 1 179 ? -35.901 8.126   -34.819 1.00 65.63  ?  290 PHE A O      1 
ATOM   1299 C  CB     . PHE A 1 179 ? -32.635 8.275   -34.373 1.00 57.75  ?  290 PHE A CB     1 
ATOM   1300 C  CG     . PHE A 1 179 ? -31.750 9.059   -33.426 1.00 57.85  ?  290 PHE A CG     1 
ATOM   1301 C  CD1    . PHE A 1 179 ? -30.385 9.175   -33.659 1.00 59.04  ?  290 PHE A CD1    1 
ATOM   1302 C  CD2    . PHE A 1 179 ? -32.286 9.694   -32.307 1.00 58.87  ?  290 PHE A CD2    1 
ATOM   1303 C  CE1    . PHE A 1 179 ? -29.575 9.922   -32.797 1.00 59.11  ?  290 PHE A CE1    1 
ATOM   1304 C  CE2    . PHE A 1 179 ? -31.474 10.458  -31.460 1.00 61.14  ?  290 PHE A CE2    1 
ATOM   1305 C  CZ     . PHE A 1 179 ? -30.122 10.551  -31.702 1.00 58.08  ?  290 PHE A CZ     1 
ATOM   1306 N  N      . GLU A 1 180 ? -34.880 6.183   -35.428 1.00 63.27  ?  291 GLU A N      1 
ATOM   1307 C  CA     . GLU A 1 180 ? -35.880 5.736   -36.396 1.00 64.01  ?  291 GLU A CA     1 
ATOM   1308 C  C      . GLU A 1 180 ? -37.182 5.315   -35.705 1.00 70.56  ?  291 GLU A C      1 
ATOM   1309 O  O      . GLU A 1 180 ? -38.255 5.551   -36.258 1.00 71.22  ?  291 GLU A O      1 
ATOM   1310 C  CB     . GLU A 1 180 ? -35.329 4.609   -37.284 1.00 64.86  ?  291 GLU A CB     1 
ATOM   1311 C  CG     . GLU A 1 180 ? -34.335 5.116   -38.317 1.00 70.53  ?  291 GLU A CG     1 
ATOM   1312 C  CD     . GLU A 1 180 ? -33.652 4.086   -39.197 1.00 83.35  ?  291 GLU A CD     1 
ATOM   1313 O  OE1    . GLU A 1 180 ? -33.878 2.868   -39.004 1.00 71.20  ?  291 GLU A OE1    1 
ATOM   1314 O  OE2    . GLU A 1 180 ? -32.873 4.507   -40.083 1.00 78.59  -1 291 GLU A OE2    1 
ATOM   1315 N  N      . ALA A 1 181 ? -37.096 4.727   -34.491 1.00 68.05  ?  292 ALA A N      1 
ATOM   1316 C  CA     . ALA A 1 181 ? -38.272 4.301   -33.720 1.00 67.73  ?  292 ALA A CA     1 
ATOM   1317 C  C      . ALA A 1 181 ? -39.090 5.479   -33.151 1.00 71.88  ?  292 ALA A C      1 
ATOM   1318 O  O      . ALA A 1 181 ? -40.269 5.301   -32.835 1.00 71.86  ?  292 ALA A O      1 
ATOM   1319 C  CB     . ALA A 1 181 ? -37.872 3.336   -32.613 1.00 68.39  ?  292 ALA A CB     1 
ATOM   1320 N  N      . GLY A 1 182 ? -38.472 6.657   -33.038 1.00 68.11  ?  293 GLY A N      1 
ATOM   1321 C  CA     . GLY A 1 182 ? -39.141 7.857   -32.542 1.00 67.39  ?  293 GLY A CA     1 
ATOM   1322 C  C      . GLY A 1 182 ? -38.479 8.598   -31.394 1.00 69.93  ?  293 GLY A C      1 
ATOM   1323 O  O      . GLY A 1 182 ? -39.089 9.509   -30.829 1.00 69.04  ?  293 GLY A O      1 
ATOM   1324 N  N      . ALA A 1 183 ? -37.222 8.245   -31.038 1.00 65.09  ?  294 ALA A N      1 
ATOM   1325 C  CA     . ALA A 1 183 ? -36.538 8.962   -29.960 1.00 63.12  ?  294 ALA A CA     1 
ATOM   1326 C  C      . ALA A 1 183 ? -36.017 10.301  -30.470 1.00 63.36  ?  294 ALA A C      1 
ATOM   1327 O  O      . ALA A 1 183 ? -35.634 10.419  -31.635 1.00 62.19  ?  294 ALA A O      1 
ATOM   1328 C  CB     . ALA A 1 183 ? -35.399 8.128   -29.391 1.00 63.88  ?  294 ALA A CB     1 
ATOM   1329 N  N      . ASP A 1 184 ? -36.041 11.316  -29.601 1.00 58.37  ?  295 ASP A N      1 
ATOM   1330 C  CA     . ASP A 1 184 ? -35.550 12.652  -29.915 1.00 57.96  ?  295 ASP A CA     1 
ATOM   1331 C  C      . ASP A 1 184 ? -34.072 12.777  -29.528 1.00 61.00  ?  295 ASP A C      1 
ATOM   1332 O  O      . ASP A 1 184 ? -33.325 13.543  -30.153 1.00 60.04  ?  295 ASP A O      1 
ATOM   1333 C  CB     . ASP A 1 184 ? -36.365 13.705  -29.160 1.00 60.04  ?  295 ASP A CB     1 
ATOM   1334 C  CG     . ASP A 1 184 ? -37.837 13.704  -29.540 1.00 72.12  ?  295 ASP A CG     1 
ATOM   1335 O  OD1    . ASP A 1 184 ? -38.616 12.951  -28.902 1.00 71.70  ?  295 ASP A OD1    1 
ATOM   1336 O  OD2    . ASP A 1 184 ? -38.198 14.413  -30.510 1.00 76.87  -1 295 ASP A OD2    1 
ATOM   1337 N  N      . ILE A 1 185 ? -33.692 12.090  -28.429 1.00 56.84  ?  296 ILE A N      1 
ATOM   1338 C  CA     . ILE A 1 185 ? -32.352 12.084  -27.831 1.00 55.26  ?  296 ILE A CA     1 
ATOM   1339 C  C      . ILE A 1 185 ? -31.992 10.642  -27.499 1.00 57.78  ?  296 ILE A C      1 
ATOM   1340 O  O      . ILE A 1 185 ? -32.826 9.916   -26.967 1.00 58.23  ?  296 ILE A O      1 
ATOM   1341 C  CB     . ILE A 1 185 ? -32.299 12.984  -26.549 1.00 57.58  ?  296 ILE A CB     1 
ATOM   1342 C  CG1    . ILE A 1 185 ? -32.820 14.421  -26.807 1.00 57.37  ?  296 ILE A CG1    1 
ATOM   1343 C  CG2    . ILE A 1 185 ? -30.878 13.044  -25.971 1.00 57.94  ?  296 ILE A CG2    1 
ATOM   1344 C  CD1    . ILE A 1 185 ? -33.320 15.179  -25.541 1.00 57.20  ?  296 ILE A CD1    1 
ATOM   1345 N  N      . VAL A 1 186 ? -30.753 10.221  -27.820 1.00 52.78  ?  297 VAL A N      1 
ATOM   1346 C  CA     . VAL A 1 186 ? -30.270 8.877   -27.485 1.00 50.72  ?  297 VAL A CA     1 
ATOM   1347 C  C      . VAL A 1 186 ? -29.205 8.990   -26.375 1.00 52.17  ?  297 VAL A C      1 
ATOM   1348 O  O      . VAL A 1 186 ? -28.326 9.848   -26.460 1.00 51.04  ?  297 VAL A O      1 
ATOM   1349 C  CB     . VAL A 1 186 ? -29.810 8.071   -28.729 1.00 53.87  ?  297 VAL A CB     1 
ATOM   1350 C  CG1    . VAL A 1 186 ? -28.980 6.850   -28.344 1.00 53.24  ?  297 VAL A CG1    1 
ATOM   1351 C  CG2    . VAL A 1 186 ? -31.004 7.640   -29.563 1.00 53.26  ?  297 VAL A CG2    1 
ATOM   1352 N  N      . LYS A 1 187 ? -29.332 8.174   -25.315 1.00 48.09  ?  298 LYS A N      1 
ATOM   1353 C  CA     . LYS A 1 187 ? -28.425 8.178   -24.162 1.00 46.39  ?  298 LYS A CA     1 
ATOM   1354 C  C      . LYS A 1 187 ? -27.377 7.086   -24.336 1.00 48.21  ?  298 LYS A C      1 
ATOM   1355 O  O      . LYS A 1 187 ? -27.713 5.913   -24.501 1.00 46.01  ?  298 LYS A O      1 
ATOM   1356 C  CB     . LYS A 1 187 ? -29.197 8.025   -22.845 1.00 48.66  ?  298 LYS A CB     1 
ATOM   1357 C  CG     . LYS A 1 187 ? -28.348 8.317   -21.610 1.00 51.76  ?  298 LYS A CG     1 
ATOM   1358 C  CD     . LYS A 1 187 ? -29.127 8.978   -20.476 1.00 48.25  ?  298 LYS A CD     1 
ATOM   1359 C  CE     . LYS A 1 187 ? -30.161 8.098   -19.814 1.00 47.87  ?  298 LYS A CE     1 
ATOM   1360 N  NZ     . LYS A 1 187 ? -29.565 6.937   -19.103 1.00 42.11  1  298 LYS A NZ     1 
ATOM   1361 N  N      . VAL A 1 188 ? -26.097 7.495   -24.294 1.00 43.44  ?  299 VAL A N      1 
ATOM   1362 C  CA     . VAL A 1 188 ? -24.959 6.602   -24.568 1.00 42.09  ?  299 VAL A CA     1 
ATOM   1363 C  C      . VAL A 1 188 ? -24.191 6.223   -23.340 1.00 43.94  ?  299 VAL A C      1 
ATOM   1364 O  O      . VAL A 1 188 ? -23.709 7.107   -22.609 1.00 44.77  ?  299 VAL A O      1 
ATOM   1365 C  CB     . VAL A 1 188 ? -24.043 7.252   -25.656 1.00 44.88  ?  299 VAL A CB     1 
ATOM   1366 C  CG1    . VAL A 1 188 ? -22.770 6.430   -25.918 1.00 44.47  ?  299 VAL A CG1    1 
ATOM   1367 C  CG2    . VAL A 1 188 ? -24.826 7.453   -26.946 1.00 44.17  ?  299 VAL A CG2    1 
ATOM   1368 N  N      . GLY A 1 189 ? -24.021 4.919   -23.175 1.00 40.13  ?  300 GLY A N      1 
ATOM   1369 C  CA     . GLY A 1 189 ? -23.220 4.337   -22.108 1.00 40.55  ?  300 GLY A CA     1 
ATOM   1370 C  C      . GLY A 1 189 ? -23.552 2.912   -21.729 1.00 44.55  ?  300 GLY A C      1 
ATOM   1371 O  O      . GLY A 1 189 ? -24.573 2.678   -21.086 1.00 45.77  ?  300 GLY A O      1 
ATOM   1372 N  N      . ILE A 1 190 ? -22.657 1.947   -22.062 1.00 40.86  ?  301 ILE A N      1 
ATOM   1373 C  CA     . ILE A 1 190 ? -22.783 0.536   -21.676 1.00 40.62  ?  301 ILE A CA     1 
ATOM   1374 C  C      . ILE A 1 190 ? -21.501 0.113   -20.944 1.00 45.80  ?  301 ILE A C      1 
ATOM   1375 O  O      . ILE A 1 190 ? -20.444 -0.039  -21.579 1.00 43.58  ?  301 ILE A O      1 
ATOM   1376 C  CB     . ILE A 1 190 ? -23.112 -0.402  -22.875 1.00 43.61  ?  301 ILE A CB     1 
ATOM   1377 C  CG1    . ILE A 1 190 ? -24.417 0.014   -23.607 1.00 43.98  ?  301 ILE A CG1    1 
ATOM   1378 C  CG2    . ILE A 1 190 ? -23.130 -1.882  -22.468 1.00 42.96  ?  301 ILE A CG2    1 
ATOM   1379 C  CD1    . ILE A 1 190 ? -25.721 -0.155  -22.809 1.00 45.86  ?  301 ILE A CD1    1 
ATOM   1380 N  N      . GLY A 1 191 ? -21.595 0.018   -19.613 1.00 43.28  ?  302 GLY A N      1 
ATOM   1381 C  CA     . GLY A 1 191 ? -20.477 -0.353  -18.746 1.00 42.67  ?  302 GLY A CA     1 
ATOM   1382 C  C      . GLY A 1 191 ? -19.497 0.695   -18.225 1.00 44.02  ?  302 GLY A C      1 
ATOM   1383 O  O      . GLY A 1 191 ? -18.581 0.300   -17.506 1.00 45.03  ?  302 GLY A O      1 
ATOM   1384 N  N      . PRO A 1 192 ? -19.580 2.017   -18.484 1.00 38.85  ?  303 PRO A N      1 
ATOM   1385 C  CA     . PRO A 1 192 ? -18.530 2.909   -17.950 1.00 39.36  ?  303 PRO A CA     1 
ATOM   1386 C  C      . PRO A 1 192 ? -18.735 3.481   -16.545 1.00 45.61  ?  303 PRO A C      1 
ATOM   1387 O  O      . PRO A 1 192 ? -17.801 4.091   -16.016 1.00 45.41  ?  303 PRO A O      1 
ATOM   1388 C  CB     . PRO A 1 192 ? -18.517 4.052   -18.972 1.00 40.32  ?  303 PRO A CB     1 
ATOM   1389 C  CG     . PRO A 1 192 ? -19.960 4.169   -19.392 1.00 43.21  ?  303 PRO A CG     1 
ATOM   1390 C  CD     . PRO A 1 192 ? -20.538 2.781   -19.318 1.00 39.66  ?  303 PRO A CD     1 
ATOM   1391 N  N      . GLY A 1 193 ? -19.956 3.369   -16.003 1.00 42.92  ?  304 GLY A N      1 
ATOM   1392 C  CA     . GLY A 1 193 ? -20.339 3.938   -14.713 1.00 43.02  ?  304 GLY A CA     1 
ATOM   1393 C  C      . GLY A 1 193 ? -19.413 3.597   -13.561 1.00 47.87  ?  304 GLY A C      1 
ATOM   1394 O  O      . GLY A 1 193 ? -18.974 2.455   -13.452 1.00 47.58  ?  304 GLY A O      1 
ATOM   1395 N  N      . SER A 1 194 ? -19.126 4.582   -12.676 1.00 45.45  ?  305 SER A N      1 
ATOM   1396 C  CA     . SER A 1 194 ? -18.247 4.402   -11.497 1.00 46.32  ?  305 SER A CA     1 
ATOM   1397 C  C      . SER A 1 194 ? -18.620 3.189   -10.619 1.00 50.86  ?  305 SER A C      1 
ATOM   1398 O  O      . SER A 1 194 ? -17.738 2.500   -10.111 1.00 50.81  ?  305 SER A O      1 
ATOM   1399 C  CB     . SER A 1 194 ? -18.252 5.661   -10.638 1.00 48.98  ?  305 SER A CB     1 
ATOM   1400 O  OG     . SER A 1 194 ? -19.497 5.802   -9.976  1.00 50.28  ?  305 SER A OG     1 
ATOM   1401 N  N      . ILE A 1 195 ? -19.934 2.957   -10.439 1.00 48.28  ?  306 ILE A N      1 
ATOM   1402 C  CA     . ILE A 1 195 ? -20.509 1.869   -9.623  1.00 47.53  ?  306 ILE A CA     1 
ATOM   1403 C  C      . ILE A 1 195 ? -20.909 0.633   -10.424 1.00 52.47  ?  306 ILE A C      1 
ATOM   1404 O  O      . ILE A 1 195 ? -21.478 -0.310  -9.875  1.00 52.83  ?  306 ILE A O      1 
ATOM   1405 C  CB     . ILE A 1 195 ? -21.705 2.394   -8.788  1.00 49.29  ?  306 ILE A CB     1 
ATOM   1406 C  CG1    . ILE A 1 195 ? -22.647 3.315   -9.616  1.00 48.57  ?  306 ILE A CG1    1 
ATOM   1407 C  CG2    . ILE A 1 195 ? -21.185 3.086   -7.527  1.00 49.82  ?  306 ILE A CG2    1 
ATOM   1408 C  CD1    . ILE A 1 195 ? -23.462 2.652   -10.832 1.00 51.86  ?  306 ILE A CD1    1 
ATOM   1409 N  N      . CYS A 1 196 ? -20.667 0.664   -11.722 1.00 50.51  ?  307 CYS A N      1 
ATOM   1410 C  CA     . CYS A 1 196 ? -21.019 -0.420  -12.638 1.00 51.01  ?  307 CYS A CA     1 
ATOM   1411 C  C      . CYS A 1 196 ? -20.104 -1.654  -12.464 1.00 51.88  ?  307 CYS A C      1 
ATOM   1412 O  O      . CYS A 1 196 ? -18.902 -1.513  -12.284 1.00 51.66  ?  307 CYS A O      1 
ATOM   1413 C  CB     . CYS A 1 196 ? -20.963 0.106   -14.068 1.00 52.30  ?  307 CYS A CB     1 
ATOM   1414 S  SG     . CYS A 1 196 ? -21.150 -1.165  -15.341 1.00 56.68  ?  307 CYS A SG     1 
ATOM   1415 H  HA     . CYS A 1 196 ? -22.044 -0.731  -12.442 1.00 50.06  ?  307 CYS A HA     1 
ATOM   1416 N  N      . THR A 1 197 ? -20.676 -2.857  -12.564 1.00 45.27  ?  308 THR A N      1 
ATOM   1417 C  CA     . THR A 1 197 ? -19.911 -4.120  -12.517 1.00 43.27  ?  308 THR A CA     1 
ATOM   1418 C  C      . THR A 1 197 ? -20.239 -4.947  -13.759 1.00 43.95  ?  308 THR A C      1 
ATOM   1419 O  O      . THR A 1 197 ? -19.764 -6.064  -13.872 1.00 42.94  ?  308 THR A O      1 
ATOM   1420 C  CB     . THR A 1 197 ? -20.117 -4.909  -11.192 1.00 49.92  ?  308 THR A CB     1 
ATOM   1421 O  OG1    . THR A 1 197 ? -21.491 -5.261  -11.042 1.00 50.66  ?  308 THR A OG1    1 
ATOM   1422 C  CG2    . THR A 1 197 ? -19.642 -4.150  -9.962  1.00 48.77  ?  308 THR A CG2    1 
ATOM   1423 N  N      . THR A 1 198 ? -21.029 -4.380  -14.711 1.00 42.47  ?  309 THR A N      1 
ATOM   1424 C  CA     . THR A 1 198 ? -21.403 -5.041  -15.975 1.00 42.15  ?  309 THR A CA     1 
ATOM   1425 C  C      . THR A 1 198 ? -20.194 -5.628  -16.716 1.00 44.04  ?  309 THR A C      1 
ATOM   1426 O  O      . THR A 1 198 ? -20.282 -6.720  -17.258 1.00 43.82  ?  309 THR A O      1 
ATOM   1427 C  CB     . THR A 1 198 ? -22.177 -4.080  -16.885 1.00 51.40  ?  309 THR A CB     1 
ATOM   1428 O  OG1    . THR A 1 198 ? -23.328 -3.584  -16.193 1.00 52.26  ?  309 THR A OG1    1 
ATOM   1429 C  CG2    . THR A 1 198 ? -22.586 -4.720  -18.221 1.00 48.49  ?  309 THR A CG2    1 
ATOM   1430 N  N      . ARG A 1 199 ? -19.074 -4.908  -16.742 1.00 40.86  ?  310 ARG A N      1 
ATOM   1431 C  CA     . ARG A 1 199 ? -17.884 -5.378  -17.456 1.00 40.43  ?  310 ARG A CA     1 
ATOM   1432 C  C      . ARG A 1 199 ? -17.337 -6.661  -16.869 1.00 42.38  ?  310 ARG A C      1 
ATOM   1433 O  O      . ARG A 1 199 ? -16.984 -7.565  -17.604 1.00 42.24  ?  310 ARG A O      1 
ATOM   1434 C  CB     . ARG A 1 199 ? -16.805 -4.284  -17.460 1.00 39.32  ?  310 ARG A CB     1 
ATOM   1435 C  CG     . ARG A 1 199 ? -17.095 -3.115  -18.400 1.00 42.89  ?  310 ARG A CG     1 
ATOM   1436 C  CD     . ARG A 1 199 ? -15.962 -2.137  -18.219 1.00 51.63  ?  310 ARG A CD     1 
ATOM   1437 N  NE     . ARG A 1 199 ? -16.107 -0.892  -18.974 1.00 56.97  ?  310 ARG A NE     1 
ATOM   1438 C  CZ     . ARG A 1 199 ? -15.084 -0.096  -19.259 1.00 69.11  ?  310 ARG A CZ     1 
ATOM   1439 N  NH1    . ARG A 1 199 ? -15.281 1.039   -19.916 1.00 50.07  1  310 ARG A NH1    1 
ATOM   1440 N  NH2    . ARG A 1 199 ? -13.854 -0.421  -18.875 1.00 54.41  ?  310 ARG A NH2    1 
ATOM   1441 N  N      A VAL A 1 200 ? -17.279 -6.725  -15.553 0.63 39.53  ?  311 VAL A N      1 
ATOM   1442 N  N      B VAL A 1 200 ? -17.247 -6.756  -15.532 0.37 38.85  ?  311 VAL A N      1 
ATOM   1443 C  CA     A VAL A 1 200 ? -16.751 -7.861  -14.825 0.63 39.91  ?  311 VAL A CA     1 
ATOM   1444 C  CA     B VAL A 1 200 ? -16.721 -7.967  -14.890 0.37 38.80  ?  311 VAL A CA     1 
ATOM   1445 C  C      A VAL A 1 200 ? -17.792 -9.007  -14.747 0.63 44.73  ?  311 VAL A C      1 
ATOM   1446 C  C      B VAL A 1 200 ? -17.798 -9.055  -14.740 0.37 44.16  ?  311 VAL A C      1 
ATOM   1447 O  O      A VAL A 1 200 ? -17.420 -10.175 -14.855 0.63 45.12  ?  311 VAL A O      1 
ATOM   1448 O  O      B VAL A 1 200 ? -17.459 -10.238 -14.753 0.37 44.34  ?  311 VAL A O      1 
ATOM   1449 C  CB     A VAL A 1 200 ? -16.234 -7.371  -13.439 0.63 43.71  ?  311 VAL A CB     1 
ATOM   1450 C  CB     B VAL A 1 200 ? -15.952 -7.722  -13.561 0.37 42.07  ?  311 VAL A CB     1 
ATOM   1451 C  CG1    A VAL A 1 200 ? -15.855 -8.528  -12.540 0.63 43.36  ?  311 VAL A CG1    1 
ATOM   1452 C  CG1    B VAL A 1 200 ? -14.550 -7.189  -13.833 0.37 41.61  ?  311 VAL A CG1    1 
ATOM   1453 C  CG2    A VAL A 1 200 ? -15.044 -6.424  -13.607 0.63 43.41  ?  311 VAL A CG2    1 
ATOM   1454 C  CG2    B VAL A 1 200 ? -16.719 -6.799  -12.616 0.37 41.55  ?  311 VAL A CG2    1 
ATOM   1455 N  N      . VAL A 1 201 ? -19.078 -8.667  -14.612 1.00 41.53  ?  312 VAL A N      1 
ATOM   1456 C  CA     . VAL A 1 201 ? -20.185 -9.646  -14.502 1.00 42.01  ?  312 VAL A CA     1 
ATOM   1457 C  C      . VAL A 1 201 ? -20.579 -10.223 -15.886 1.00 44.22  ?  312 VAL A C      1 
ATOM   1458 O  O      . VAL A 1 201 ? -20.568 -11.440 -16.089 1.00 45.08  ?  312 VAL A O      1 
ATOM   1459 C  CB     . VAL A 1 201 ? -21.396 -9.052  -13.720 1.00 47.07  ?  312 VAL A CB     1 
ATOM   1460 C  CG1    . VAL A 1 201 ? -22.632 -9.947  -13.813 1.00 47.66  ?  312 VAL A CG1    1 
ATOM   1461 C  CG2    . VAL A 1 201 ? -21.035 -8.777  -12.252 1.00 47.07  ?  312 VAL A CG2    1 
ATOM   1462 N  N      . ALA A 1 202 ? -20.915 -9.355  -16.820 1.00 40.14  ?  313 ALA A N      1 
ATOM   1463 C  CA     . ALA A 1 202 ? -21.408 -9.736  -18.146 1.00 40.60  ?  313 ALA A CA     1 
ATOM   1464 C  C      . ALA A 1 202 ? -20.335 -9.796  -19.254 1.00 44.19  ?  313 ALA A C      1 
ATOM   1465 O  O      . ALA A 1 202 ? -20.623 -10.292 -20.335 1.00 43.86  ?  313 ALA A O      1 
ATOM   1466 C  CB     . ALA A 1 202 ? -22.545 -8.797  -18.546 1.00 41.51  ?  313 ALA A CB     1 
ATOM   1467 N  N      . GLY A 1 203 ? -19.138 -9.258  -19.001 1.00 41.53  ?  314 GLY A N      1 
ATOM   1468 C  CA     . GLY A 1 203 ? -18.055 -9.253  -19.989 1.00 40.89  ?  314 GLY A CA     1 
ATOM   1469 C  C      . GLY A 1 203 ? -18.258 -8.278  -21.136 1.00 41.25  ?  314 GLY A C      1 
ATOM   1470 O  O      . GLY A 1 203 ? -17.551 -8.353  -22.139 1.00 40.42  ?  314 GLY A O      1 
ATOM   1471 N  N      . VAL A 1 204 ? -19.201 -7.342  -20.963 1.00 37.28  ?  315 VAL A N      1 
ATOM   1472 C  CA     . VAL A 1 204 ? -19.697 -6.407  -21.967 1.00 36.73  ?  315 VAL A CA     1 
ATOM   1473 C  C      . VAL A 1 204 ? -19.413 -4.975  -21.620 1.00 42.25  ?  315 VAL A C      1 
ATOM   1474 O  O      . VAL A 1 204 ? -19.693 -4.535  -20.497 1.00 41.86  ?  315 VAL A O      1 
ATOM   1475 C  CB     . VAL A 1 204 ? -21.244 -6.634  -22.198 1.00 38.98  ?  315 VAL A CB     1 
ATOM   1476 C  CG1    . VAL A 1 204 ? -21.850 -5.568  -23.108 1.00 38.89  ?  315 VAL A CG1    1 
ATOM   1477 C  CG2    . VAL A 1 204 ? -21.520 -8.023  -22.773 1.00 38.27  ?  315 VAL A CG2    1 
ATOM   1478 N  N      . GLY A 1 205 ? -19.028 -4.220  -22.644 1.00 38.64  ?  316 GLY A N      1 
ATOM   1479 C  CA     . GLY A 1 205 ? -18.824 -2.786  -22.523 1.00 38.31  ?  316 GLY A CA     1 
ATOM   1480 C  C      . GLY A 1 205 ? -18.146 -2.189  -23.728 1.00 41.03  ?  316 GLY A C      1 
ATOM   1481 O  O      . GLY A 1 205 ? -17.579 -2.914  -24.550 1.00 40.78  ?  316 GLY A O      1 
ATOM   1482 N  N      . VAL A 1 206 ? -18.292 -0.874  -23.889 1.00 37.62  ?  317 VAL A N      1 
ATOM   1483 C  CA     . VAL A 1 206 ? -17.598 -0.142  -24.941 1.00 37.27  ?  317 VAL A CA     1 
ATOM   1484 C  C      . VAL A 1 206 ? -16.938 1.026   -24.228 1.00 40.77  ?  317 VAL A C      1 
ATOM   1485 O  O      . VAL A 1 206 ? -17.666 1.873   -23.708 1.00 40.57  ?  317 VAL A O      1 
ATOM   1486 C  CB     . VAL A 1 206 ? -18.489 0.341   -26.148 1.00 40.95  ?  317 VAL A CB     1 
ATOM   1487 C  CG1    . VAL A 1 206 ? -17.656 1.140   -27.167 1.00 41.05  ?  317 VAL A CG1    1 
ATOM   1488 C  CG2    . VAL A 1 206 ? -19.188 -0.835  -26.839 1.00 40.11  ?  317 VAL A CG2    1 
ATOM   1489 N  N      . PRO A 1 207 ? -15.572 1.102   -24.187 1.00 35.61  ?  318 PRO A N      1 
ATOM   1490 C  CA     . PRO A 1 207 ? -14.901 2.269   -23.588 1.00 34.53  ?  318 PRO A CA     1 
ATOM   1491 C  C      . PRO A 1 207 ? -15.606 3.536   -24.056 1.00 38.00  ?  318 PRO A C      1 
ATOM   1492 O  O      . PRO A 1 207 ? -15.896 3.691   -25.243 1.00 39.36  ?  318 PRO A O      1 
ATOM   1493 C  CB     . PRO A 1 207 ? -13.468 2.117   -24.095 1.00 35.65  ?  318 PRO A CB     1 
ATOM   1494 C  CG     . PRO A 1 207 ? -13.261 0.644   -24.099 1.00 40.24  ?  318 PRO A CG     1 
ATOM   1495 C  CD     . PRO A 1 207 ? -14.582 0.127   -24.693 1.00 36.56  ?  318 PRO A CD     1 
ATOM   1496 N  N      . GLN A 1 208 ? -16.011 4.351   -23.093 1.00 34.80  ?  319 GLN A N      1 
ATOM   1497 C  CA     . GLN A 1 208 ? -16.961 5.457   -23.226 1.00 36.34  ?  319 GLN A CA     1 
ATOM   1498 C  C      . GLN A 1 208 ? -16.615 6.520   -24.281 1.00 39.67  ?  319 GLN A C      1 
ATOM   1499 O  O      . GLN A 1 208 ? -17.539 6.999   -24.922 1.00 41.19  ?  319 GLN A O      1 
ATOM   1500 C  CB     . GLN A 1 208 ? -17.243 6.101   -21.848 1.00 37.99  ?  319 GLN A CB     1 
ATOM   1501 C  CG     . GLN A 1 208 ? -18.400 7.142   -21.790 1.00 41.47  ?  319 GLN A CG     1 
ATOM   1502 C  CD     . GLN A 1 208 ? -19.772 6.667   -22.203 1.00 43.86  ?  319 GLN A CD     1 
ATOM   1503 O  OE1    . GLN A 1 208 ? -19.958 5.556   -22.723 1.00 43.24  ?  319 GLN A OE1    1 
ATOM   1504 N  NE2    . GLN A 1 208 ? -20.796 7.500   -21.931 1.00 39.35  ?  319 GLN A NE2    1 
ATOM   1505 N  N      . ILE A 1 209 ? -15.339 6.872   -24.500 1.00 35.20  ?  320 ILE A N      1 
ATOM   1506 C  CA     . ILE A 1 209 ? -15.006 7.885   -25.501 1.00 34.10  ?  320 ILE A CA     1 
ATOM   1507 C  C      . ILE A 1 209 ? -15.400 7.395   -26.889 1.00 37.25  ?  320 ILE A C      1 
ATOM   1508 O  O      . ILE A 1 209 ? -16.040 8.138   -27.635 1.00 35.61  ?  320 ILE A O      1 
ATOM   1509 C  CB     . ILE A 1 209 ? -13.524 8.351   -25.371 1.00 37.28  ?  320 ILE A CB     1 
ATOM   1510 C  CG1    . ILE A 1 209 ? -13.357 9.311   -24.168 1.00 38.32  ?  320 ILE A CG1    1 
ATOM   1511 C  CG2    . ILE A 1 209 ? -12.991 8.973   -26.646 1.00 35.70  ?  320 ILE A CG2    1 
ATOM   1512 C  CD1    . ILE A 1 209 ? -13.948 10.846  -24.329 1.00 43.93  ?  320 ILE A CD1    1 
ATOM   1513 N  N      . THR A 1 210 ? -15.081 6.109   -27.194 1.00 36.04  ?  321 THR A N      1 
ATOM   1514 C  CA     . THR A 1 210 ? -15.425 5.481   -28.468 1.00 36.00  ?  321 THR A CA     1 
ATOM   1515 C  C      . THR A 1 210 ? -16.927 5.322   -28.585 1.00 40.69  ?  321 THR A C      1 
ATOM   1516 O  O      . THR A 1 210 ? -17.475 5.616   -29.638 1.00 41.22  ?  321 THR A O      1 
ATOM   1517 C  CB     . THR A 1 210 ? -14.634 4.206   -28.660 1.00 37.66  ?  321 THR A CB     1 
ATOM   1518 O  OG1    . THR A 1 210 ? -13.280 4.585   -28.893 1.00 38.34  ?  321 THR A OG1    1 
ATOM   1519 C  CG2    . THR A 1 210 ? -15.149 3.353   -29.818 1.00 37.12  ?  321 THR A CG2    1 
ATOM   1520 N  N      . ALA A 1 211 ? -17.592 4.877   -27.511 1.00 38.75  ?  322 ALA A N      1 
ATOM   1521 C  CA     . ALA A 1 211 ? -19.053 4.735   -27.511 1.00 38.66  ?  322 ALA A CA     1 
ATOM   1522 C  C      . ALA A 1 211 ? -19.742 6.057   -27.909 1.00 42.09  ?  322 ALA A C      1 
ATOM   1523 O  O      . ALA A 1 211 ? -20.581 6.043   -28.806 1.00 42.51  ?  322 ALA A O      1 
ATOM   1524 C  CB     . ALA A 1 211 ? -19.528 4.277   -26.142 1.00 39.29  ?  322 ALA A CB     1 
ATOM   1525 N  N      . ILE A 1 212 ? -19.365 7.188   -27.274 1.00 37.92  ?  323 ILE A N      1 
ATOM   1526 C  CA     . ILE A 1 212 ? -19.895 8.538   -27.545 1.00 37.95  ?  323 ILE A CA     1 
ATOM   1527 C  C      . ILE A 1 212 ? -19.639 8.906   -29.014 1.00 43.96  ?  323 ILE A C      1 
ATOM   1528 O  O      . ILE A 1 212 ? -20.585 9.254   -29.722 1.00 44.23  ?  323 ILE A O      1 
ATOM   1529 C  CB     . ILE A 1 212 ? -19.303 9.620   -26.590 1.00 40.21  ?  323 ILE A CB     1 
ATOM   1530 C  CG1    . ILE A 1 212 ? -19.695 9.383   -25.109 1.00 39.84  ?  323 ILE A CG1    1 
ATOM   1531 C  CG2    . ILE A 1 212 ? -19.692 11.047  -27.035 1.00 41.70  ?  323 ILE A CG2    1 
ATOM   1532 C  CD1    . ILE A 1 212 ? -18.713 10.118  -24.137 1.00 39.32  ?  323 ILE A CD1    1 
ATOM   1533 N  N      . TYR A 1 213 ? -18.373 8.792   -29.471 1.00 40.21  ?  324 TYR A N      1 
ATOM   1534 C  CA     . TYR A 1 213 ? -17.971 9.147   -30.835 1.00 40.43  ?  324 TYR A CA     1 
ATOM   1535 C  C      . TYR A 1 213 ? -18.701 8.350   -31.922 1.00 45.10  ?  324 TYR A C      1 
ATOM   1536 O  O      . TYR A 1 213 ? -19.180 8.957   -32.882 1.00 43.75  ?  324 TYR A O      1 
ATOM   1537 C  CB     . TYR A 1 213 ? -16.443 9.061   -31.007 1.00 41.67  ?  324 TYR A CB     1 
ATOM   1538 C  CG     . TYR A 1 213 ? -15.940 9.447   -32.384 1.00 41.76  ?  324 TYR A CG     1 
ATOM   1539 C  CD1    . TYR A 1 213 ? -15.985 10.768  -32.820 1.00 42.03  ?  324 TYR A CD1    1 
ATOM   1540 C  CD2    . TYR A 1 213 ? -15.369 8.498   -33.227 1.00 43.99  ?  324 TYR A CD2    1 
ATOM   1541 C  CE1    . TYR A 1 213 ? -15.485 11.134  -34.070 1.00 42.13  ?  324 TYR A CE1    1 
ATOM   1542 C  CE2    . TYR A 1 213 ? -14.849 8.854   -34.470 1.00 44.17  ?  324 TYR A CE2    1 
ATOM   1543 C  CZ     . TYR A 1 213 ? -14.923 10.168  -34.893 1.00 50.21  ?  324 TYR A CZ     1 
ATOM   1544 O  OH     . TYR A 1 213 ? -14.411 10.486  -36.122 1.00 51.34  ?  324 TYR A OH     1 
ATOM   1545 N  N      . ASP A 1 214 ? -18.813 7.022   -31.753 1.00 42.51  ?  325 ASP A N      1 
ATOM   1546 C  CA     . ASP A 1 214 ? -19.502 6.120   -32.695 1.00 42.16  ?  325 ASP A CA     1 
ATOM   1547 C  C      . ASP A 1 214 ? -21.004 6.433   -32.738 1.00 49.15  ?  325 ASP A C      1 
ATOM   1548 O  O      . ASP A 1 214 ? -21.627 6.342   -33.800 1.00 48.89  ?  325 ASP A O      1 
ATOM   1549 C  CB     . ASP A 1 214 ? -19.326 4.666   -32.251 1.00 42.92  ?  325 ASP A CB     1 
ATOM   1550 C  CG     . ASP A 1 214 ? -17.950 4.049   -32.488 1.00 41.20  ?  325 ASP A CG     1 
ATOM   1551 O  OD1    . ASP A 1 214 ? -17.135 4.665   -33.187 1.00 40.23  ?  325 ASP A OD1    1 
ATOM   1552 O  OD2    . ASP A 1 214 ? -17.719 2.943   -32.011 1.00 40.97  -1 325 ASP A OD2    1 
ATOM   1553 N  N      . CYS A 1 215 ? -21.591 6.783   -31.577 1.00 45.41  ?  326 CYS A N      1 
ATOM   1554 C  CA     . CYS A 1 215 ? -23.021 7.092   -31.506 1.00 44.40  ?  326 CYS A CA     1 
ATOM   1555 C  C      . CYS A 1 215 ? -23.347 8.476   -32.045 1.00 49.02  ?  326 CYS A C      1 
ATOM   1556 O  O      . CYS A 1 215 ? -24.316 8.601   -32.786 1.00 50.14  ?  326 CYS A O      1 
ATOM   1557 C  CB     . CYS A 1 215 ? -23.558 6.867   -30.097 1.00 42.98  ?  326 CYS A CB     1 
ATOM   1558 S  SG     . CYS A 1 215 ? -23.623 5.126   -29.624 1.00 45.98  ?  326 CYS A SG     1 
ATOM   1559 N  N      . ALA A 1 216 ? -22.506 9.488   -31.745 1.00 46.33  ?  327 ALA A N      1 
ATOM   1560 C  CA     . ALA A 1 216 ? -22.613 10.863  -32.231 1.00 46.23  ?  327 ALA A CA     1 
ATOM   1561 C  C      . ALA A 1 216 ? -22.368 10.958  -33.752 1.00 50.86  ?  327 ALA A C      1 
ATOM   1562 O  O      . ALA A 1 216 ? -22.928 11.850  -34.390 1.00 50.28  ?  327 ALA A O      1 
ATOM   1563 C  CB     . ALA A 1 216 ? -21.636 11.758  -31.502 1.00 47.06  ?  327 ALA A CB     1 
ATOM   1564 N  N      . THR A 1 217 ? -21.509 10.071  -34.323 1.00 46.88  ?  328 THR A N      1 
ATOM   1565 C  CA     . THR A 1 217 ? -21.247 9.987   -35.773 1.00 46.49  ?  328 THR A CA     1 
ATOM   1566 C  C      . THR A 1 217 ? -22.601 9.684   -36.482 1.00 53.06  ?  328 THR A C      1 
ATOM   1567 O  O      . THR A 1 217 ? -22.928 10.319  -37.496 1.00 53.50  ?  328 THR A O      1 
ATOM   1568 C  CB     . THR A 1 217 ? -20.183 8.890   -36.089 1.00 45.46  ?  328 THR A CB     1 
ATOM   1569 O  OG1    . THR A 1 217 ? -18.929 9.292   -35.539 1.00 46.81  ?  328 THR A OG1    1 
ATOM   1570 C  CG2    . THR A 1 217 ? -19.991 8.682   -37.585 1.00 42.24  ?  328 THR A CG2    1 
ATOM   1571 N  N      . GLU A 1 218 ? -23.373 8.731   -35.920 1.00 49.75  ?  329 GLU A N      1 
ATOM   1572 C  CA     . GLU A 1 218 ? -24.707 8.370   -36.385 1.00 50.95  ?  329 GLU A CA     1 
ATOM   1573 C  C      . GLU A 1 218 ? -25.716 9.518   -36.152 1.00 57.80  ?  329 GLU A C      1 
ATOM   1574 O  O      . GLU A 1 218 ? -26.423 9.881   -37.088 1.00 58.69  ?  329 GLU A O      1 
ATOM   1575 C  CB     . GLU A 1 218 ? -25.179 7.066   -35.719 1.00 52.39  ?  329 GLU A CB     1 
ATOM   1576 C  CG     . GLU A 1 218 ? -26.458 6.472   -36.298 1.00 60.21  ?  329 GLU A CG     1 
ATOM   1577 C  CD     . GLU A 1 218 ? -26.458 6.096   -37.772 1.00 76.20  ?  329 GLU A CD     1 
ATOM   1578 O  OE1    . GLU A 1 218 ? -25.390 5.716   -38.304 1.00 60.66  ?  329 GLU A OE1    1 
ATOM   1579 O  OE2    . GLU A 1 218 ? -27.539 6.181   -38.397 1.00 70.39  -1 329 GLU A OE2    1 
ATOM   1580 N  N      . ALA A 1 219 ? -25.761 10.100  -34.925 1.00 54.80  ?  330 ALA A N      1 
ATOM   1581 C  CA     . ALA A 1 219 ? -26.650 11.207  -34.527 1.00 54.99  ?  330 ALA A CA     1 
ATOM   1582 C  C      . ALA A 1 219 ? -26.565 12.435  -35.426 1.00 59.39  ?  330 ALA A C      1 
ATOM   1583 O  O      . ALA A 1 219 ? -27.585 13.096  -35.659 1.00 59.47  ?  330 ALA A O      1 
ATOM   1584 C  CB     . ALA A 1 219 ? -26.362 11.624  -33.096 1.00 55.64  ?  330 ALA A CB     1 
ATOM   1585 N  N      . ARG A 1 220 ? -25.344 12.752  -35.906 1.00 54.97  ?  331 ARG A N      1 
ATOM   1586 C  CA     . ARG A 1 220 ? -25.075 13.867  -36.802 1.00 54.57  ?  331 ARG A CA     1 
ATOM   1587 C  C      . ARG A 1 220 ? -25.867 13.765  -38.104 1.00 60.16  ?  331 ARG A C      1 
ATOM   1588 O  O      . ARG A 1 220 ? -26.291 14.797  -38.620 1.00 61.34  ?  331 ARG A O      1 
ATOM   1589 C  CB     . ARG A 1 220 ? -23.583 13.977  -37.083 1.00 51.84  ?  331 ARG A CB     1 
ATOM   1590 C  CG     . ARG A 1 220 ? -22.840 14.787  -36.033 1.00 54.85  ?  331 ARG A CG     1 
ATOM   1591 C  CD     . ARG A 1 220 ? -21.358 14.555  -36.165 1.00 58.28  ?  331 ARG A CD     1 
ATOM   1592 N  NE     . ARG A 1 220 ? -20.660 15.616  -36.896 1.00 59.76  ?  331 ARG A NE     1 
ATOM   1593 C  CZ     . ARG A 1 220 ? -20.135 15.476  -38.110 1.00 67.37  ?  331 ARG A CZ     1 
ATOM   1594 N  NH1    . ARG A 1 220 ? -19.468 16.475  -38.668 1.00 51.97  1  331 ARG A NH1    1 
ATOM   1595 N  NH2    . ARG A 1 220 ? -20.264 14.332  -38.770 1.00 56.02  ?  331 ARG A NH2    1 
ATOM   1596 N  N      . LYS A 1 221 ? -26.104 12.526  -38.597 1.00 56.17  ?  332 LYS A N      1 
ATOM   1597 C  CA     . LYS A 1 221 ? -26.858 12.251  -39.824 1.00 56.11  ?  332 LYS A CA     1 
ATOM   1598 C  C      . LYS A 1 221 ? -28.340 12.628  -39.642 1.00 63.13  ?  332 LYS A C      1 
ATOM   1599 O  O      . LYS A 1 221 ? -28.915 13.293  -40.513 1.00 63.22  ?  332 LYS A O      1 
ATOM   1600 C  CB     . LYS A 1 221 ? -26.734 10.772  -40.238 1.00 57.44  ?  332 LYS A CB     1 
ATOM   1601 C  CG     . LYS A 1 221 ? -25.315 10.275  -40.489 1.00 59.33  ?  332 LYS A CG     1 
ATOM   1602 C  CD     . LYS A 1 221 ? -25.328 8.785   -40.843 1.00 62.18  ?  332 LYS A CD     1 
ATOM   1603 C  CE     . LYS A 1 221 ? -24.088 8.035   -40.410 1.00 66.46  ?  332 LYS A CE     1 
ATOM   1604 N  NZ     . LYS A 1 221 ? -22.890 8.371   -41.227 1.00 71.84  1  332 LYS A NZ     1 
ATOM   1605 N  N      . HIS A 1 222 ? -28.934 12.226  -38.492 1.00 60.73  ?  333 HIS A N      1 
ATOM   1606 C  CA     . HIS A 1 222 ? -30.327 12.480  -38.101 1.00 60.91  ?  333 HIS A CA     1 
ATOM   1607 C  C      . HIS A 1 222 ? -30.585 13.909  -37.601 1.00 64.31  ?  333 HIS A C      1 
ATOM   1608 O  O      . HIS A 1 222 ? -31.743 14.280  -37.416 1.00 64.13  ?  333 HIS A O      1 
ATOM   1609 C  CB     . HIS A 1 222 ? -30.772 11.478  -37.020 1.00 61.76  ?  333 HIS A CB     1 
ATOM   1610 C  CG     . HIS A 1 222 ? -30.628 10.039  -37.411 1.00 65.43  ?  333 HIS A CG     1 
ATOM   1611 N  ND1    . HIS A 1 222 ? -31.695 9.318   -37.901 1.00 67.40  ?  333 HIS A ND1    1 
ATOM   1612 C  CD2    . HIS A 1 222 ? -29.547 9.229   -37.343 1.00 67.26  ?  333 HIS A CD2    1 
ATOM   1613 C  CE1    . HIS A 1 222 ? -31.235 8.098   -38.122 1.00 66.73  ?  333 HIS A CE1    1 
ATOM   1614 N  NE2    . HIS A 1 222 ? -29.944 8.001   -37.805 1.00 67.14  ?  333 HIS A NE2    1 
ATOM   1615 N  N      . GLY A 1 223 ? -29.520 14.672  -37.349 1.00 61.13  ?  334 GLY A N      1 
ATOM   1616 C  CA     . GLY A 1 223 ? -29.590 16.032  -36.817 1.00 60.96  ?  334 GLY A CA     1 
ATOM   1617 C  C      . GLY A 1 223 ? -30.116 16.062  -35.393 1.00 65.04  ?  334 GLY A C      1 
ATOM   1618 O  O      . GLY A 1 223 ? -30.723 17.047  -34.967 1.00 64.91  ?  334 GLY A O      1 
ATOM   1619 N  N      . LYS A 1 224 ? -29.878 14.972  -34.644 1.00 60.37  ?  335 LYS A N      1 
ATOM   1620 C  CA     . LYS A 1 224 ? -30.382 14.798  -33.283 1.00 59.36  ?  335 LYS A CA     1 
ATOM   1621 C  C      . LYS A 1 224 ? -29.268 14.776  -32.214 1.00 61.60  ?  335 LYS A C      1 
ATOM   1622 O  O      . LYS A 1 224 ? -28.084 14.702  -32.544 1.00 60.48  ?  335 LYS A O      1 
ATOM   1623 C  CB     . LYS A 1 224 ? -31.288 13.559  -33.209 1.00 60.45  ?  335 LYS A CB     1 
ATOM   1624 C  CG     . LYS A 1 224 ? -32.606 13.741  -33.981 1.00 68.07  ?  335 LYS A CG     1 
ATOM   1625 C  CD     . LYS A 1 224 ? -33.577 12.578  -33.809 1.00 74.97  ?  335 LYS A CD     1 
ATOM   1626 C  CE     . LYS A 1 224 ? -34.830 12.720  -34.651 1.00 82.18  ?  335 LYS A CE     1 
ATOM   1627 N  NZ     . LYS A 1 224 ? -35.716 11.530  -34.535 1.00 81.09  1  335 LYS A NZ     1 
ATOM   1628 N  N      . ALA A 1 225 ? -29.667 14.874  -30.938 1.00 57.38  ?  336 ALA A N      1 
ATOM   1629 C  CA     . ALA A 1 225 ? -28.760 14.978  -29.793 1.00 55.62  ?  336 ALA A CA     1 
ATOM   1630 C  C      . ALA A 1 225 ? -28.477 13.665  -29.052 1.00 53.99  ?  336 ALA A C      1 
ATOM   1631 O  O      . ALA A 1 225 ? -29.312 12.756  -29.053 1.00 51.39  ?  336 ALA A O      1 
ATOM   1632 C  CB     . ALA A 1 225 ? -29.277 16.030  -28.822 1.00 56.15  ?  336 ALA A CB     1 
ATOM   1633 N  N      A ILE A 1 226 ? -27.282 13.602  -28.416 0.49 49.20  ?  337 ILE A N      1 
ATOM   1634 N  N      B ILE A 1 226 ? -27.278 13.561  -28.436 0.51 49.20  ?  337 ILE A N      1 
ATOM   1635 C  CA     A ILE A 1 226 ? -26.743 12.475  -27.654 0.49 47.53  ?  337 ILE A CA     1 
ATOM   1636 C  CA     B ILE A 1 226 ? -26.904 12.406  -27.617 0.51 47.54  ?  337 ILE A CA     1 
ATOM   1637 C  C      A ILE A 1 226 ? -26.427 12.880  -26.201 0.49 47.61  ?  337 ILE A C      1 
ATOM   1638 C  C      B ILE A 1 226 ? -26.464 12.846  -26.221 0.51 47.52  ?  337 ILE A C      1 
ATOM   1639 O  O      A ILE A 1 226 ? -25.869 13.962  -25.981 0.49 46.66  ?  337 ILE A O      1 
ATOM   1640 O  O      B ILE A 1 226 ? -25.876 13.923  -26.060 0.51 46.46  ?  337 ILE A O      1 
ATOM   1641 C  CB     A ILE A 1 226 ? -25.473 11.948  -28.406 0.49 50.93  ?  337 ILE A CB     1 
ATOM   1642 C  CB     B ILE A 1 226 ? -25.905 11.396  -28.245 0.51 51.03  ?  337 ILE A CB     1 
ATOM   1643 C  CG1    A ILE A 1 226 ? -25.847 11.050  -29.624 0.49 51.07  ?  337 ILE A CG1    1 
ATOM   1644 C  CG1    B ILE A 1 226 ? -24.553 12.058  -28.606 0.51 51.60  ?  337 ILE A CG1    1 
ATOM   1645 C  CG2    A ILE A 1 226 ? -24.427 11.265  -27.495 0.49 51.82  ?  337 ILE A CG2    1 
ATOM   1646 C  CG2    B ILE A 1 226 ? -26.522 10.635  -29.426 0.51 51.38  ?  337 ILE A CG2    1 
ATOM   1647 C  CD1    A ILE A 1 226 ? -26.554 9.703   -29.361 0.49 52.02  ?  337 ILE A CD1    1 
ATOM   1648 C  CD1    B ILE A 1 226 ? -23.351 11.198  -28.198 0.51 59.49  ?  337 ILE A CD1    1 
ATOM   1649 N  N      . ILE A 1 227 ? -26.761 12.004  -25.219 1.00 42.80  ?  338 ILE A N      1 
ATOM   1650 C  CA     . ILE A 1 227 ? -26.404 12.228  -23.809 1.00 42.29  ?  338 ILE A CA     1 
ATOM   1651 C  C      . ILE A 1 227 ? -25.211 11.287  -23.504 1.00 45.64  ?  338 ILE A C      1 
ATOM   1652 O  O      . ILE A 1 227 ? -25.366 10.079  -23.634 1.00 44.36  ?  338 ILE A O      1 
ATOM   1653 C  CB     . ILE A 1 227 ? -27.578 11.981  -22.808 1.00 45.83  ?  338 ILE A CB     1 
ATOM   1654 C  CG1    . ILE A 1 227 ? -28.739 13.004  -23.019 1.00 45.75  ?  338 ILE A CG1    1 
ATOM   1655 C  CG2    . ILE A 1 227 ? -27.052 12.036  -21.361 1.00 47.38  ?  338 ILE A CG2    1 
ATOM   1656 C  CD1    . ILE A 1 227 ? -30.086 12.622  -22.344 1.00 52.86  ?  338 ILE A CD1    1 
ATOM   1657 N  N      . ALA A 1 228 ? -24.049 11.837  -23.089 1.00 43.76  ?  339 ALA A N      1 
ATOM   1658 C  CA     . ALA A 1 228 ? -22.877 11.019  -22.698 1.00 42.85  ?  339 ALA A CA     1 
ATOM   1659 C  C      . ALA A 1 228 ? -23.082 10.637  -21.218 1.00 43.85  ?  339 ALA A C      1 
ATOM   1660 O  O      . ALA A 1 228 ? -22.828 11.439  -20.306 1.00 42.91  ?  339 ALA A O      1 
ATOM   1661 C  CB     . ALA A 1 228 ? -21.597 11.818  -22.871 1.00 43.56  ?  339 ALA A CB     1 
ATOM   1662 N  N      . ASP A 1 229 ? -23.523 9.415   -20.998 1.00 38.99  ?  340 ASP A N      1 
ATOM   1663 C  CA     . ASP A 1 229 ? -23.872 8.885   -19.677 1.00 39.41  ?  340 ASP A CA     1 
ATOM   1664 C  C      . ASP A 1 229 ? -22.886 7.897   -19.009 1.00 42.78  ?  340 ASP A C      1 
ATOM   1665 O  O      . ASP A 1 229 ? -22.829 6.742   -19.396 1.00 41.54  ?  340 ASP A O      1 
ATOM   1666 C  CB     . ASP A 1 229 ? -25.256 8.210   -19.792 1.00 40.83  ?  340 ASP A CB     1 
ATOM   1667 C  CG     . ASP A 1 229 ? -25.828 7.694   -18.493 1.00 48.08  ?  340 ASP A CG     1 
ATOM   1668 O  OD1    . ASP A 1 229 ? -25.328 8.100   -17.422 1.00 49.07  ?  340 ASP A OD1    1 
ATOM   1669 O  OD2    . ASP A 1 229 ? -26.787 6.896   -18.546 1.00 50.45  -1 340 ASP A OD2    1 
ATOM   1670 N  N      . GLY A 1 230 ? -22.253 8.323   -17.908 1.00 39.20  ?  341 GLY A N      1 
ATOM   1671 C  CA     . GLY A 1 230 ? -21.399 7.446   -17.123 1.00 38.60  ?  341 GLY A CA     1 
ATOM   1672 C  C      . GLY A 1 230 ? -19.907 7.629   -17.315 1.00 41.71  ?  341 GLY A C      1 
ATOM   1673 O  O      . GLY A 1 230 ? -19.454 8.061   -18.378 1.00 39.87  ?  341 GLY A O      1 
ATOM   1674 N  N      . GLY A 1 231 ? -19.154 7.303   -16.267 1.00 37.78  ?  342 GLY A N      1 
ATOM   1675 C  CA     . GLY A 1 231 ? -17.692 7.321   -16.277 1.00 36.54  ?  342 GLY A CA     1 
ATOM   1676 C  C      . GLY A 1 231 ? -17.016 8.650   -16.041 1.00 42.51  ?  342 GLY A C      1 
ATOM   1677 O  O      . GLY A 1 231 ? -15.785 8.703   -16.032 1.00 41.77  ?  342 GLY A O      1 
ATOM   1678 N  N      A ILE A 1 232 ? -17.798 9.733   -15.895 0.86 39.72  ?  343 ILE A N      1 
ATOM   1679 N  N      B ILE A 1 232 ? -17.805 9.729   -15.845 0.14 39.98  ?  343 ILE A N      1 
ATOM   1680 C  CA     A ILE A 1 232 ? -17.247 11.064  -15.663 0.86 40.05  ?  343 ILE A CA     1 
ATOM   1681 C  CA     B ILE A 1 232 ? -17.283 11.075  -15.591 0.14 40.26  ?  343 ILE A CA     1 
ATOM   1682 C  C      A ILE A 1 232 ? -16.773 11.167  -14.203 0.86 44.72  ?  343 ILE A C      1 
ATOM   1683 C  C      B ILE A 1 232 ? -16.763 11.150  -14.156 0.14 44.48  ?  343 ILE A C      1 
ATOM   1684 O  O      A ILE A 1 232 ? -17.585 11.017  -13.289 0.86 45.25  ?  343 ILE A O      1 
ATOM   1685 O  O      B ILE A 1 232 ? -17.547 11.034  -13.211 0.14 44.22  ?  343 ILE A O      1 
ATOM   1686 C  CB     A ILE A 1 232 ? -18.251 12.162  -16.123 0.86 42.53  ?  343 ILE A CB     1 
ATOM   1687 C  CB     B ILE A 1 232 ? -18.335 12.192  -15.865 0.14 43.49  ?  343 ILE A CB     1 
ATOM   1688 C  CG1    A ILE A 1 232 ? -18.363 12.145  -17.672 0.86 42.86  ?  343 ILE A CG1    1 
ATOM   1689 C  CG1    B ILE A 1 232 ? -19.030 12.054  -17.258 0.14 44.25  ?  343 ILE A CG1    1 
ATOM   1690 C  CG2    A ILE A 1 232 ? -17.831 13.551  -15.651 0.86 42.22  ?  343 ILE A CG2    1 
ATOM   1691 C  CG2    B ILE A 1 232 ? -17.739 13.586  -15.657 0.14 44.16  ?  343 ILE A CG2    1 
ATOM   1692 C  CD1    A ILE A 1 232 ? -19.705 12.451  -18.223 0.86 49.32  ?  343 ILE A CD1    1 
ATOM   1693 C  CD1    B ILE A 1 232 ? -18.235 12.367  -18.498 0.14 52.07  ?  343 ILE A CD1    1 
ATOM   1694 N  N      . LYS A 1 233 ? -15.451 11.371  -13.998 1.00 41.29  ?  344 LYS A N      1 
ATOM   1695 C  CA     . LYS A 1 233 ? -14.828 11.474  -12.670 1.00 41.95  ?  344 LYS A CA     1 
ATOM   1696 C  C      . LYS A 1 233 ? -14.530 12.904  -12.274 1.00 48.86  ?  344 LYS A C      1 
ATOM   1697 O  O      . LYS A 1 233 ? -14.509 13.199  -11.084 1.00 50.88  ?  344 LYS A O      1 
ATOM   1698 C  CB     . LYS A 1 233 ? -13.549 10.613  -12.553 1.00 43.95  ?  344 LYS A CB     1 
ATOM   1699 C  CG     . LYS A 1 233 ? -13.670 9.174   -13.088 1.00 51.11  ?  344 LYS A CG     1 
ATOM   1700 C  CD     . LYS A 1 233 ? -12.295 8.442   -13.285 1.00 54.97  ?  344 LYS A CD     1 
ATOM   1701 C  CE     . LYS A 1 233 ? -11.344 9.035   -14.338 1.00 60.39  ?  344 LYS A CE     1 
ATOM   1702 N  NZ     . LYS A 1 233 ? -11.922 9.106   -15.718 1.00 45.43  1  344 LYS A NZ     1 
ATOM   1703 N  N      . PHE A 1 234 ? -14.249 13.788  -13.253 1.00 44.30  ?  345 PHE A N      1 
ATOM   1704 C  CA     . PHE A 1 234 ? -13.839 15.160  -13.002 1.00 45.09  ?  345 PHE A CA     1 
ATOM   1705 C  C      . PHE A 1 234 ? -14.378 16.081  -14.095 1.00 46.32  ?  345 PHE A C      1 
ATOM   1706 O  O      . PHE A 1 234 ? -14.884 15.591  -15.092 1.00 46.86  ?  345 PHE A O      1 
ATOM   1707 C  CB     . PHE A 1 234 ? -12.291 15.235  -13.033 1.00 48.73  ?  345 PHE A CB     1 
ATOM   1708 C  CG     . PHE A 1 234 ? -11.505 14.154  -12.335 1.00 52.23  ?  345 PHE A CG     1 
ATOM   1709 C  CD1    . PHE A 1 234 ? -11.309 14.193  -10.958 1.00 57.27  ?  345 PHE A CD1    1 
ATOM   1710 C  CD2    . PHE A 1 234 ? -10.870 13.156  -13.063 1.00 56.14  ?  345 PHE A CD2    1 
ATOM   1711 C  CE1    . PHE A 1 234 ? -10.549 13.208  -10.311 1.00 58.31  ?  345 PHE A CE1    1 
ATOM   1712 C  CE2    . PHE A 1 234 ? -10.100 12.180  -12.419 1.00 59.67  ?  345 PHE A CE2    1 
ATOM   1713 C  CZ     . PHE A 1 234 ? -9.951  12.211  -11.046 1.00 57.72  ?  345 PHE A CZ     1 
ATOM   1714 N  N      . SER A 1 235 ? -14.210 17.411  -13.949 1.00 42.33  ?  346 SER A N      1 
ATOM   1715 C  CA     . SER A 1 235 ? -14.633 18.389  -14.973 1.00 40.89  ?  346 SER A CA     1 
ATOM   1716 C  C      . SER A 1 235 ? -13.922 18.144  -16.346 1.00 44.36  ?  346 SER A C      1 
ATOM   1717 O  O      . SER A 1 235 ? -14.512 18.409  -17.398 1.00 43.94  ?  346 SER A O      1 
ATOM   1718 C  CB     . SER A 1 235 ? -14.384 19.808  -14.488 1.00 42.46  ?  346 SER A CB     1 
ATOM   1719 O  OG     . SER A 1 235 ? -13.052 19.949  -14.031 1.00 46.97  ?  346 SER A OG     1 
ATOM   1720 N  N      . GLY A 1 236 ? -12.694 17.603  -16.318 1.00 41.01  ?  347 GLY A N      1 
ATOM   1721 C  CA     . GLY A 1 236 ? -11.960 17.270  -17.541 1.00 40.76  ?  347 GLY A CA     1 
ATOM   1722 C  C      . GLY A 1 236 ? -12.676 16.206  -18.362 1.00 44.11  ?  347 GLY A C      1 
ATOM   1723 O  O      . GLY A 1 236 ? -12.702 16.282  -19.591 1.00 43.41  ?  347 GLY A O      1 
ATOM   1724 N  N      . ASP A 1 237 ? -13.326 15.241  -17.683 1.00 40.64  ?  348 ASP A N      1 
ATOM   1725 C  CA     . ASP A 1 237 ? -14.092 14.181  -18.350 1.00 39.31  ?  348 ASP A CA     1 
ATOM   1726 C  C      . ASP A 1 237 ? -15.370 14.719  -18.965 1.00 42.41  ?  348 ASP A C      1 
ATOM   1727 O  O      . ASP A 1 237 ? -15.886 14.142  -19.920 1.00 42.25  ?  348 ASP A O      1 
ATOM   1728 C  CB     . ASP A 1 237 ? -14.409 13.041  -17.388 1.00 39.39  ?  348 ASP A CB     1 
ATOM   1729 C  CG     . ASP A 1 237 ? -13.214 12.273  -16.855 1.00 47.81  ?  348 ASP A CG     1 
ATOM   1730 O  OD1    . ASP A 1 237 ? -12.084 12.473  -17.386 1.00 45.60  ?  348 ASP A OD1    1 
ATOM   1731 O  OD2    . ASP A 1 237 ? -13.400 11.481  -15.902 1.00 50.58  -1 348 ASP A OD2    1 
ATOM   1732 N  N      . ILE A 1 238 ? -15.917 15.778  -18.378 1.00 39.68  ?  349 ILE A N      1 
ATOM   1733 C  CA     . ILE A 1 238 ? -17.114 16.428  -18.915 1.00 39.23  ?  349 ILE A CA     1 
ATOM   1734 C  C      . ILE A 1 238 ? -16.798 17.018  -20.283 1.00 39.90  ?  349 ILE A C      1 
ATOM   1735 O  O      . ILE A 1 238 ? -17.496 16.715  -21.240 1.00 41.22  ?  349 ILE A O      1 
ATOM   1736 C  CB     . ILE A 1 238 ? -17.720 17.529  -17.973 1.00 42.35  ?  349 ILE A CB     1 
ATOM   1737 C  CG1    . ILE A 1 238 ? -18.126 16.963  -16.597 1.00 42.00  ?  349 ILE A CG1    1 
ATOM   1738 C  CG2    . ILE A 1 238 ? -18.928 18.197  -18.660 1.00 42.18  ?  349 ILE A CG2    1 
ATOM   1739 C  CD1    . ILE A 1 238 ? -18.848 18.002  -15.629 1.00 43.80  ?  349 ILE A CD1    1 
ATOM   1740 N  N      . ILE A 1 239 ? -15.775 17.861  -20.381 1.00 38.73  ?  350 ILE A N      1 
ATOM   1741 C  CA     . ILE A 1 239 ? -15.447 18.499  -21.658 1.00 38.52  ?  350 ILE A CA     1 
ATOM   1742 C  C      . ILE A 1 239 ? -14.999 17.441  -22.705 1.00 43.36  ?  350 ILE A C      1 
ATOM   1743 O  O      . ILE A 1 239 ? -15.414 17.539  -23.857 1.00 41.43  ?  350 ILE A O      1 
ATOM   1744 C  CB     . ILE A 1 239 ? -14.483 19.680  -21.482 1.00 41.52  ?  350 ILE A CB     1 
ATOM   1745 C  CG1    . ILE A 1 239 ? -14.366 20.482  -22.807 1.00 40.70  ?  350 ILE A CG1    1 
ATOM   1746 C  CG2    . ILE A 1 239 ? -13.129 19.264  -20.868 1.00 40.87  ?  350 ILE A CG2    1 
ATOM   1747 C  CD1    . ILE A 1 239 ? -13.528 21.664  -22.781 1.00 45.38  ?  350 ILE A CD1    1 
ATOM   1748 N  N      . LYS A 1 240 ? -14.262 16.381  -22.278 1.00 39.65  ?  351 LYS A N      1 
ATOM   1749 C  CA     . LYS A 1 240 ? -13.841 15.297  -23.190 1.00 38.54  ?  351 LYS A CA     1 
ATOM   1750 C  C      . LYS A 1 240 ? -15.087 14.601  -23.737 1.00 39.45  ?  351 LYS A C      1 
ATOM   1751 O  O      . LYS A 1 240 ? -15.158 14.334  -24.926 1.00 39.10  ?  351 LYS A O      1 
ATOM   1752 C  CB     . LYS A 1 240 ? -12.971 14.256  -22.457 1.00 39.27  ?  351 LYS A CB     1 
ATOM   1753 C  CG     . LYS A 1 240 ? -11.530 14.639  -22.197 1.00 41.86  ?  351 LYS A CG     1 
ATOM   1754 C  CD     . LYS A 1 240 ? -10.839 13.451  -21.482 1.00 40.99  ?  351 LYS A CD     1 
ATOM   1755 C  CE     . LYS A 1 240 ? -9.739  13.967  -20.610 1.00 38.14  ?  351 LYS A CE     1 
ATOM   1756 N  NZ     . LYS A 1 240 ? -8.810  12.912  -20.174 1.00 35.32  1  351 LYS A NZ     1 
ATOM   1757 N  N      . ALA A 1 241 ? -16.088 14.322  -22.879 1.00 38.26  ?  352 ALA A N      1 
ATOM   1758 C  CA     . ALA A 1 241 ? -17.332 13.660  -23.300 1.00 37.39  ?  352 ALA A CA     1 
ATOM   1759 C  C      . ALA A 1 241 ? -18.127 14.502  -24.326 1.00 41.05  ?  352 ALA A C      1 
ATOM   1760 O  O      . ALA A 1 241 ? -18.758 13.938  -25.236 1.00 41.48  ?  352 ALA A O      1 
ATOM   1761 C  CB     . ALA A 1 241 ? -18.214 13.370  -22.095 1.00 37.75  ?  352 ALA A CB     1 
ATOM   1762 N  N      . LEU A 1 242 ? -18.121 15.832  -24.152 1.00 38.69  ?  353 LEU A N      1 
ATOM   1763 C  CA     . LEU A 1 242 ? -18.833 16.730  -25.058 1.00 40.20  ?  353 LEU A CA     1 
ATOM   1764 C  C      . LEU A 1 242 ? -18.051 16.837  -26.347 1.00 44.27  ?  353 LEU A C      1 
ATOM   1765 O  O      . LEU A 1 242 ? -18.618 16.613  -27.411 1.00 45.35  ?  353 LEU A O      1 
ATOM   1766 C  CB     . LEU A 1 242 ? -19.104 18.115  -24.426 1.00 40.89  ?  353 LEU A CB     1 
ATOM   1767 C  CG     . LEU A 1 242 ? -19.905 18.138  -23.098 1.00 44.39  ?  353 LEU A CG     1 
ATOM   1768 C  CD1    . LEU A 1 242 ? -19.787 19.491  -22.409 1.00 43.84  ?  353 LEU A CD1    1 
ATOM   1769 C  CD2    . LEU A 1 242 ? -21.352 17.748  -23.300 1.00 43.33  ?  353 LEU A CD2    1 
ATOM   1770 N  N      . ALA A 1 243 ? -16.729 17.062  -26.254 1.00 41.83  ?  354 ALA A N      1 
ATOM   1771 C  CA     . ALA A 1 243 ? -15.859 17.172  -27.425 1.00 40.53  ?  354 ALA A CA     1 
ATOM   1772 C  C      . ALA A 1 243 ? -15.823 15.900  -28.286 1.00 44.56  ?  354 ALA A C      1 
ATOM   1773 O  O      . ALA A 1 243 ? -15.554 16.004  -29.478 1.00 45.12  ?  354 ALA A O      1 
ATOM   1774 C  CB     . ALA A 1 243 ? -14.473 17.584  -27.008 1.00 41.16  ?  354 ALA A CB     1 
ATOM   1775 N  N      . ALA A 1 244 ? -16.143 14.719  -27.701 1.00 39.93  ?  355 ALA A N      1 
ATOM   1776 C  CA     . ALA A 1 244 ? -16.217 13.442  -28.421 1.00 40.30  ?  355 ALA A CA     1 
ATOM   1777 C  C      . ALA A 1 244 ? -17.540 13.300  -29.175 1.00 45.13  ?  355 ALA A C      1 
ATOM   1778 O  O      . ALA A 1 244 ? -17.706 12.343  -29.941 1.00 41.67  ?  355 ALA A O      1 
ATOM   1779 C  CB     . ALA A 1 244 ? -16.041 12.265  -27.460 1.00 40.95  ?  355 ALA A CB     1 
ATOM   1780 N  N      . GLY A 1 245 ? -18.484 14.222  -28.927 1.00 43.64  ?  356 GLY A N      1 
ATOM   1781 C  CA     . GLY A 1 245 ? -19.771 14.206  -29.617 1.00 44.08  ?  356 GLY A CA     1 
ATOM   1782 C  C      . GLY A 1 245 ? -21.034 14.350  -28.792 1.00 49.79  ?  356 GLY A C      1 
ATOM   1783 O  O      . GLY A 1 245 ? -22.119 14.502  -29.362 1.00 48.51  ?  356 GLY A O      1 
ATOM   1784 N  N      . GLY A 1 246 ? -20.909 14.260  -27.467 1.00 46.86  ?  357 GLY A N      1 
ATOM   1785 C  CA     . GLY A 1 246 ? -22.048 14.376  -26.556 1.00 45.93  ?  357 GLY A CA     1 
ATOM   1786 C  C      . GLY A 1 246 ? -22.625 15.776  -26.512 1.00 47.10  ?  357 GLY A C      1 
ATOM   1787 O  O      . GLY A 1 246 ? -21.869 16.733  -26.502 1.00 44.77  ?  357 GLY A O      1 
ATOM   1788 N  N      . HIS A 1 247 ? -23.966 15.921  -26.516 1.00 49.00  ?  358 HIS A N      1 
ATOM   1789 C  CA     . HIS A 1 247 ? -24.594 17.252  -26.418 1.00 50.49  ?  358 HIS A CA     1 
ATOM   1790 C  C      . HIS A 1 247 ? -24.653 17.708  -24.963 1.00 51.94  ?  358 HIS A C      1 
ATOM   1791 O  O      . HIS A 1 247 ? -24.457 18.885  -24.648 1.00 51.74  ?  358 HIS A O      1 
ATOM   1792 C  CB     . HIS A 1 247 ? -25.979 17.250  -27.072 1.00 52.72  ?  358 HIS A CB     1 
ATOM   1793 C  CG     . HIS A 1 247 ? -25.879 17.257  -28.560 1.00 57.44  ?  358 HIS A CG     1 
ATOM   1794 N  ND1    . HIS A 1 247 ? -25.618 16.093  -29.276 1.00 60.14  ?  358 HIS A ND1    1 
ATOM   1795 C  CD2    . HIS A 1 247 ? -25.920 18.302  -29.418 1.00 59.79  ?  358 HIS A CD2    1 
ATOM   1796 C  CE1    . HIS A 1 247 ? -25.529 16.469  -30.540 1.00 59.95  ?  358 HIS A CE1    1 
ATOM   1797 N  NE2    . HIS A 1 247 ? -25.688 17.792  -30.671 1.00 60.11  ?  358 HIS A NE2    1 
ATOM   1798 N  N      . ALA A 1 248 ? -24.877 16.754  -24.079 1.00 47.27  ?  359 ALA A N      1 
ATOM   1799 C  CA     . ALA A 1 248 ? -24.908 16.962  -22.641 1.00 46.58  ?  359 ALA A CA     1 
ATOM   1800 C  C      . ALA A 1 248 ? -24.407 15.681  -21.969 1.00 49.05  ?  359 ALA A C      1 
ATOM   1801 O  O      . ALA A 1 248 ? -24.415 14.610  -22.574 1.00 48.74  ?  359 ALA A O      1 
ATOM   1802 C  CB     . ALA A 1 248 ? -26.333 17.281  -22.185 1.00 47.03  ?  359 ALA A CB     1 
ATOM   1803 N  N      . VAL A 1 249 ? -23.998 15.798  -20.712 1.00 43.96  ?  360 VAL A N      1 
ATOM   1804 C  CA     . VAL A 1 249 ? -23.512 14.679  -19.924 1.00 43.17  ?  360 VAL A CA     1 
ATOM   1805 C  C      . VAL A 1 249 ? -24.490 14.377  -18.826 1.00 48.02  ?  360 VAL A C      1 
ATOM   1806 O  O      . VAL A 1 249 ? -25.193 15.288  -18.358 1.00 47.06  ?  360 VAL A O      1 
ATOM   1807 C  CB     . VAL A 1 249 ? -22.090 14.936  -19.331 1.00 45.29  ?  360 VAL A CB     1 
ATOM   1808 C  CG1    . VAL A 1 249 ? -21.057 15.173  -20.432 1.00 44.06  ?  360 VAL A CG1    1 
ATOM   1809 C  CG2    . VAL A 1 249 ? -22.085 16.078  -18.307 1.00 44.80  ?  360 VAL A CG2    1 
ATOM   1810 N  N      . MET A 1 250 ? -24.472 13.115  -18.372 1.00 45.09  ?  361 MET A N      1 
ATOM   1811 C  CA     . MET A 1 250 ? -25.235 12.599  -17.238 1.00 44.24  ?  361 MET A CA     1 
ATOM   1812 C  C      . MET A 1 250 ? -24.277 12.146  -16.133 1.00 50.23  ?  361 MET A C      1 
ATOM   1813 O  O      . MET A 1 250 ? -23.361 11.348  -16.386 1.00 48.67  ?  361 MET A O      1 
ATOM   1814 C  CB     . MET A 1 250 ? -26.178 11.474  -17.634 1.00 45.89  ?  361 MET A CB     1 
ATOM   1815 C  CG     . MET A 1 250 ? -26.933 10.921  -16.434 1.00 48.51  ?  361 MET A CG     1 
ATOM   1816 S  SD     . MET A 1 250 ? -28.262 9.808   -16.843 1.00 50.76  ?  361 MET A SD     1 
ATOM   1817 C  CE     . MET A 1 250 ? -29.529 11.012  -17.338 1.00 47.60  ?  361 MET A CE     1 
ATOM   1818 N  N      . LEU A 1 251 ? -24.492 12.674  -14.910 1.00 46.07  ?  362 LEU A N      1 
ATOM   1819 C  CA     . LEU A 1 251 ? -23.658 12.396  -13.756 1.00 45.53  ?  362 LEU A CA     1 
ATOM   1820 C  C      . LEU A 1 251 ? -24.399 11.667  -12.660 1.00 52.22  ?  362 LEU A C      1 
ATOM   1821 O  O      . LEU A 1 251 ? -25.516 12.042  -12.299 1.00 53.17  ?  362 LEU A O      1 
ATOM   1822 C  CB     . LEU A 1 251 ? -23.054 13.696  -13.179 1.00 45.46  ?  362 LEU A CB     1 
ATOM   1823 C  CG     . LEU A 1 251 ? -22.472 14.751  -14.149 1.00 49.42  ?  362 LEU A CG     1 
ATOM   1824 C  CD1    . LEU A 1 251 ? -21.868 15.910  -13.385 1.00 48.77  ?  362 LEU A CD1    1 
ATOM   1825 C  CD2    . LEU A 1 251 ? -21.393 14.154  -15.052 1.00 51.71  ?  362 LEU A CD2    1 
ATOM   1826 N  N      . GLY A 1 252 ? -23.731 10.670  -12.109 1.00 48.60  ?  363 GLY A N      1 
ATOM   1827 C  CA     . GLY A 1 252 ? -24.159 9.890   -10.961 1.00 48.30  ?  363 GLY A CA     1 
ATOM   1828 C  C      . GLY A 1 252 ? -23.266 10.218  -9.777  1.00 50.95  ?  363 GLY A C      1 
ATOM   1829 O  O      . GLY A 1 252 ? -23.621 11.083  -8.971  1.00 51.87  ?  363 GLY A O      1 
ATOM   1830 N  N      A SER A 1 253 ? -22.078 9.577   -9.718  0.53 46.26  ?  364 SER A N      1 
ATOM   1831 N  N      B SER A 1 253 ? -22.072 9.581   -9.714  0.47 47.26  ?  364 SER A N      1 
ATOM   1832 C  CA     A SER A 1 253 ? -21.038 9.699   -8.685  0.53 45.36  ?  364 SER A CA     1 
ATOM   1833 C  CA     B SER A 1 253 ? -21.053 9.695   -8.657  0.47 46.88  ?  364 SER A CA     1 
ATOM   1834 C  C      A SER A 1 253 ? -20.733 11.116  -8.226  0.53 50.29  ?  364 SER A C      1 
ATOM   1835 C  C      B SER A 1 253 ? -20.701 11.113  -8.218  0.47 50.91  ?  364 SER A C      1 
ATOM   1836 O  O      A SER A 1 253 ? -20.688 11.354  -7.023  0.53 50.79  ?  364 SER A O      1 
ATOM   1837 O  O      B SER A 1 253 ? -20.594 11.347  -7.018  0.47 51.30  ?  364 SER A O      1 
ATOM   1838 C  CB     A SER A 1 253 ? -19.749 9.016   -9.139  0.53 46.94  ?  364 SER A CB     1 
ATOM   1839 C  CB     B SER A 1 253 ? -19.776 8.955   -9.046  0.47 50.31  ?  364 SER A CB     1 
ATOM   1840 O  OG     A SER A 1 253 ? -18.594 9.526   -8.488  0.53 47.84  ?  364 SER A OG     1 
ATOM   1841 O  OG     B SER A 1 253 ? -19.052 9.621   -10.069 0.47 58.43  ?  364 SER A OG     1 
ATOM   1842 N  N      . LEU A 1 254 ? -20.490 12.037  -9.167  1.00 46.96  ?  365 LEU A N      1 
ATOM   1843 C  CA     . LEU A 1 254 ? -20.127 13.428  -8.857  1.00 47.29  ?  365 LEU A CA     1 
ATOM   1844 C  C      . LEU A 1 254 ? -21.188 14.239  -8.115  1.00 53.13  ?  365 LEU A C      1 
ATOM   1845 O  O      . LEU A 1 254 ? -20.843 15.236  -7.474  1.00 53.68  ?  365 LEU A O      1 
ATOM   1846 C  CB     . LEU A 1 254 ? -19.713 14.170  -10.127 1.00 47.04  ?  365 LEU A CB     1 
ATOM   1847 C  CG     . LEU A 1 254 ? -18.318 13.880  -10.663 1.00 50.46  ?  365 LEU A CG     1 
ATOM   1848 C  CD1    . LEU A 1 254 ? -18.122 14.572  -11.972 1.00 50.65  ?  365 LEU A CD1    1 
ATOM   1849 C  CD2    . LEU A 1 254 ? -17.247 14.317  -9.676  1.00 53.97  ?  365 LEU A CD2    1 
ATOM   1850 N  N      . LEU A 1 255 ? -22.460 13.821  -8.207  1.00 48.98  ?  366 LEU A N      1 
ATOM   1851 C  CA     . LEU A 1 255 ? -23.600 14.512  -7.605  1.00 49.19  ?  366 LEU A CA     1 
ATOM   1852 C  C      . LEU A 1 255 ? -24.214 13.820  -6.387  1.00 57.68  ?  366 LEU A C      1 
ATOM   1853 O  O      . LEU A 1 255 ? -24.947 14.467  -5.634  1.00 58.27  ?  366 LEU A O      1 
ATOM   1854 C  CB     . LEU A 1 255 ? -24.681 14.729  -8.666  1.00 48.43  ?  366 LEU A CB     1 
ATOM   1855 C  CG     . LEU A 1 255 ? -24.304 15.524  -9.913  1.00 51.06  ?  366 LEU A CG     1 
ATOM   1856 C  CD1    . LEU A 1 255 ? -25.469 15.612  -10.838 1.00 49.58  ?  366 LEU A CD1    1 
ATOM   1857 C  CD2    . LEU A 1 255 ? -23.803 16.940  -9.569  1.00 53.85  ?  366 LEU A CD2    1 
ATOM   1858 N  N      . ALA A 1 256 ? -23.936 12.520  -6.203  1.00 54.88  ?  367 ALA A N      1 
ATOM   1859 C  CA     . ALA A 1 256 ? -24.469 11.697  -5.118  1.00 55.52  ?  367 ALA A CA     1 
ATOM   1860 C  C      . ALA A 1 256 ? -24.108 12.152  -3.703  1.00 61.26  ?  367 ALA A C      1 
ATOM   1861 O  O      . ALA A 1 256 ? -24.846 11.851  -2.759  1.00 60.02  ?  367 ALA A O      1 
ATOM   1862 C  CB     . ALA A 1 256 ? -24.037 10.258  -5.313  1.00 56.18  ?  367 ALA A CB     1 
ATOM   1863 N  N      . GLY A 1 257 ? -22.951 12.800  -3.564  1.00 59.96  ?  368 GLY A N      1 
ATOM   1864 C  CA     . GLY A 1 257 ? -22.444 13.269  -2.277  1.00 60.61  ?  368 GLY A CA     1 
ATOM   1865 C  C      . GLY A 1 257 ? -23.011 14.595  -1.815  1.00 65.09  ?  368 GLY A C      1 
ATOM   1866 O  O      . GLY A 1 257 ? -22.804 14.978  -0.660  1.00 64.74  ?  368 GLY A O      1 
ATOM   1867 N  N      . THR A 1 258 ? -23.739 15.299  -2.706  1.00 61.62  ?  369 THR A N      1 
ATOM   1868 C  CA     . THR A 1 258 ? -24.318 16.610  -2.400  1.00 61.35  ?  369 THR A CA     1 
ATOM   1869 C  C      . THR A 1 258 ? -25.542 16.491  -1.486  1.00 65.47  ?  369 THR A C      1 
ATOM   1870 O  O      . THR A 1 258 ? -26.161 15.426  -1.415  1.00 63.73  ?  369 THR A O      1 
ATOM   1871 C  CB     . THR A 1 258 ? -24.587 17.439  -3.672  1.00 62.99  ?  369 THR A CB     1 
ATOM   1872 O  OG1    . THR A 1 258 ? -25.624 16.837  -4.441  1.00 61.03  ?  369 THR A OG1    1 
ATOM   1873 C  CG2    . THR A 1 258 ? -23.328 17.653  -4.518  1.00 59.57  ?  369 THR A CG2    1 
ATOM   1874 N  N      . GLU A 1 259 ? -25.865 17.588  -0.772  1.00 63.47  ?  370 GLU A N      1 
ATOM   1875 C  CA     . GLU A 1 259 ? -26.994 17.669  0.165   1.00 64.16  ?  370 GLU A CA     1 
ATOM   1876 C  C      . GLU A 1 259 ? -28.341 17.385  -0.524  1.00 68.76  ?  370 GLU A C      1 
ATOM   1877 O  O      . GLU A 1 259 ? -29.164 16.653  0.026   1.00 69.36  ?  370 GLU A O      1 
ATOM   1878 C  CB     . GLU A 1 259 ? -26.999 19.034  0.895   1.00 65.51  ?  370 GLU A CB     1 
ATOM   1879 C  CG     . GLU A 1 259 ? -28.050 19.195  1.992   1.00 75.76  ?  370 GLU A CG     1 
ATOM   1880 C  CD     . GLU A 1 259 ? -28.074 18.139  3.083   1.00 98.06  ?  370 GLU A CD     1 
ATOM   1881 O  OE1    . GLU A 1 259 ? -29.110 17.447  3.212   1.00 98.76  ?  370 GLU A OE1    1 
ATOM   1882 O  OE2    . GLU A 1 259 ? -27.054 17.991  3.795   1.00 86.82  -1 370 GLU A OE2    1 
ATOM   1883 N  N      . GLU A 1 260 ? -28.521 17.914  -1.751  1.00 64.95  ?  371 GLU A N      1 
ATOM   1884 C  CA     . GLU A 1 260 ? -29.718 17.781  -2.583  1.00 64.00  ?  371 GLU A CA     1 
ATOM   1885 C  C      . GLU A 1 260 ? -30.024 16.336  -3.044  1.00 68.40  ?  371 GLU A C      1 
ATOM   1886 O  O      . GLU A 1 260 ? -31.158 16.069  -3.447  1.00 67.46  ?  371 GLU A O      1 
ATOM   1887 C  CB     . GLU A 1 260 ? -29.657 18.739  -3.777  1.00 64.94  ?  371 GLU A CB     1 
ATOM   1888 C  CG     . GLU A 1 260 ? -29.786 20.202  -3.377  1.00 74.85  ?  371 GLU A CG     1 
ATOM   1889 C  CD     . GLU A 1 260 ? -28.510 20.963  -3.051  1.00 88.03  ?  371 GLU A CD     1 
ATOM   1890 O  OE1    . GLU A 1 260 ? -27.496 20.329  -2.674  1.00 79.03  ?  371 GLU A OE1    1 
ATOM   1891 O  OE2    . GLU A 1 260 ? -28.524 22.207  -3.199  1.00 72.00  -1 371 GLU A OE2    1 
ATOM   1892 N  N      . SER A 1 261 ? -29.045 15.406  -2.977  1.00 67.23  ?  372 SER A N      1 
ATOM   1893 C  CA     . SER A 1 261 ? -29.303 14.008  -3.349  1.00 68.00  ?  372 SER A CA     1 
ATOM   1894 C  C      . SER A 1 261 ? -30.260 13.375  -2.299  1.00 74.16  ?  372 SER A C      1 
ATOM   1895 O  O      . SER A 1 261 ? -30.178 13.759  -1.127  1.00 73.09  ?  372 SER A O      1 
ATOM   1896 C  CB     . SER A 1 261 ? -28.004 13.219  -3.503  1.00 71.37  ?  372 SER A CB     1 
ATOM   1897 O  OG     . SER A 1 261 ? -27.392 12.892  -2.267  1.00 81.26  ?  372 SER A OG     1 
ATOM   1898 N  N      . PRO A 1 262 ? -31.186 12.455  -2.684  1.00 72.94  ?  373 PRO A N      1 
ATOM   1899 C  CA     . PRO A 1 262 ? -32.177 11.942  -1.711  1.00 73.69  ?  373 PRO A CA     1 
ATOM   1900 C  C      . PRO A 1 262 ? -31.655 11.197  -0.478  1.00 80.61  ?  373 PRO A C      1 
ATOM   1901 O  O      . PRO A 1 262 ? -32.419 11.015  0.474   1.00 81.29  ?  373 PRO A O      1 
ATOM   1902 C  CB     . PRO A 1 262 ? -33.077 11.032  -2.554  1.00 75.24  ?  373 PRO A CB     1 
ATOM   1903 C  CG     . PRO A 1 262 ? -32.323 10.749  -3.780  1.00 79.38  ?  373 PRO A CG     1 
ATOM   1904 C  CD     . PRO A 1 262 ? -31.463 11.936  -4.036  1.00 74.61  ?  373 PRO A CD     1 
ATOM   1905 N  N      . GLY A 1 263 ? -30.389 10.798  -0.484  1.00 78.39  ?  374 GLY A N      1 
ATOM   1906 C  CA     . GLY A 1 263 ? -29.789 10.075  0.633   1.00 79.34  ?  374 GLY A CA     1 
ATOM   1907 C  C      . GLY A 1 263 ? -29.666 10.870  1.922   1.00 85.06  ?  374 GLY A C      1 
ATOM   1908 O  O      . GLY A 1 263 ? -29.725 12.105  1.910   1.00 84.36  ?  374 GLY A O      1 
ATOM   1909 N  N      . ALA A 1 264 ? -29.504 10.157  3.050   1.00 82.56  ?  375 ALA A N      1 
ATOM   1910 C  CA     . ALA A 1 264 ? -29.332 10.773  4.362   1.00 82.81  ?  375 ALA A CA     1 
ATOM   1911 C  C      . ALA A 1 264 ? -27.844 10.900  4.686   1.00 87.22  ?  375 ALA A C      1 
ATOM   1912 O  O      . ALA A 1 264 ? -27.074 9.969   4.420   1.00 86.29  ?  375 ALA A O      1 
ATOM   1913 C  CB     . ALA A 1 264 ? -30.033 9.945   5.427   1.00 83.71  ?  375 ALA A CB     1 
ATOM   1914 N  N      . THR A 1 265 ? -27.439 12.058  5.243   1.00 84.98  ?  376 THR A N      1 
ATOM   1915 C  CA     . THR A 1 265 ? -26.046 12.313  5.615   1.00 85.70  ?  376 THR A CA     1 
ATOM   1916 C  C      . THR A 1 265 ? -25.700 11.481  6.843   1.00 92.29  ?  376 THR A C      1 
ATOM   1917 O  O      . THR A 1 265 ? -26.395 11.550  7.861   1.00 91.85  ?  376 THR A O      1 
ATOM   1918 C  CB     . THR A 1 265 ? -25.757 13.814  5.782   1.00 92.85  ?  376 THR A CB     1 
ATOM   1919 O  OG1    . THR A 1 265 ? -26.328 14.532  4.686   1.00 94.05  ?  376 THR A OG1    1 
ATOM   1920 C  CG2    . THR A 1 265 ? -24.257 14.116  5.880   1.00 89.92  ?  376 THR A CG2    1 
ATOM   1921 N  N      . GLU A 1 266 ? -24.652 10.662  6.716   1.00 90.78  ?  377 GLU A N      1 
ATOM   1922 C  CA     . GLU A 1 266 ? -24.200 9.766   7.774   1.00 91.70  ?  377 GLU A CA     1 
ATOM   1923 C  C      . GLU A 1 266 ? -22.771 10.082  8.208   1.00 96.93  ?  377 GLU A C      1 
ATOM   1924 O  O      . GLU A 1 266 ? -22.026 10.730  7.471   1.00 95.99  ?  377 GLU A O      1 
ATOM   1925 C  CB     . GLU A 1 266 ? -24.326 8.291   7.338   1.00 93.30  ?  377 GLU A CB     1 
ATOM   1926 C  CG     . GLU A 1 266 ? -25.710 7.856   6.867   1.00 107.05 ?  377 GLU A CG     1 
ATOM   1927 C  CD     . GLU A 1 266 ? -26.841 7.893   7.879   1.00 134.65 ?  377 GLU A CD     1 
ATOM   1928 O  OE1    . GLU A 1 266 ? -26.587 7.642   9.080   1.00 131.53 ?  377 GLU A OE1    1 
ATOM   1929 O  OE2    . GLU A 1 266 ? -27.994 8.139   7.459   1.00 133.57 -1 377 GLU A OE2    1 
ATOM   1930 N  N      . ILE A 1 267 ? -22.406 9.636   9.419   1.00 95.18  ?  378 ILE A N      1 
ATOM   1931 C  CA     . ILE A 1 267 ? -21.085 9.833   10.014  1.00 95.63  ?  378 ILE A CA     1 
ATOM   1932 C  C      . ILE A 1 267 ? -20.431 8.477   10.307  1.00 100.92 ?  378 ILE A C      1 
ATOM   1933 O  O      . ILE A 1 267 ? -21.084 7.572   10.833  1.00 100.84 ?  378 ILE A O      1 
ATOM   1934 C  CB     . ILE A 1 267 ? -21.141 10.803  11.239  1.00 98.82  ?  378 ILE A CB     1 
ATOM   1935 C  CG1    . ILE A 1 267 ? -19.727 11.153  11.769  1.00 99.24  ?  378 ILE A CG1    1 
ATOM   1936 C  CG2    . ILE A 1 267 ? -22.072 10.298  12.364  1.00 99.88  ?  378 ILE A CG2    1 
ATOM   1937 C  CD1    . ILE A 1 267 ? -19.583 12.580  12.343  1.00 106.99 ?  378 ILE A CD1    1 
ATOM   1938 N  N      . PHE A 1 268 ? -19.162 8.328   9.909   1.00 98.45  ?  379 PHE A N      1 
ATOM   1939 C  CA     . PHE A 1 268 ? -18.389 7.105   10.123  1.00 98.95  ?  379 PHE A CA     1 
ATOM   1940 C  C      . PHE A 1 268 ? -16.935 7.463   10.385  1.00 101.63 ?  379 PHE A C      1 
ATOM   1941 O  O      . PHE A 1 268 ? -16.221 7.892   9.469   1.00 101.47 ?  379 PHE A O      1 
ATOM   1942 C  CB     . PHE A 1 268 ? -18.528 6.140   8.932   1.00 101.45 ?  379 PHE A CB     1 
ATOM   1943 C  CG     . PHE A 1 268 ? -18.002 4.742   9.153   1.00 103.65 ?  379 PHE A CG     1 
ATOM   1944 C  CD1    . PHE A 1 268 ? -18.771 3.788   9.810   1.00 107.26 ?  379 PHE A CD1    1 
ATOM   1945 C  CD2    . PHE A 1 268 ? -16.762 4.361   8.653   1.00 106.46 ?  379 PHE A CD2    1 
ATOM   1946 C  CE1    . PHE A 1 268 ? -18.292 2.486   9.996   1.00 108.52 ?  379 PHE A CE1    1 
ATOM   1947 C  CE2    . PHE A 1 268 ? -16.286 3.058   8.832   1.00 109.65 ?  379 PHE A CE2    1 
ATOM   1948 C  CZ     . PHE A 1 268 ? -17.053 2.130   9.505   1.00 107.86 ?  379 PHE A CZ     1 
ATOM   1949 N  N      . GLN A 1 269 ? -16.517 7.307   11.660  1.00 96.53  ?  380 GLN A N      1 
ATOM   1950 C  CA     . GLN A 1 269 ? -15.176 7.602   12.174  1.00 95.37  ?  380 GLN A CA     1 
ATOM   1951 C  C      . GLN A 1 269 ? -14.799 9.071   11.912  1.00 97.16  ?  380 GLN A C      1 
ATOM   1952 O  O      . GLN A 1 269 ? -13.775 9.373   11.291  1.00 96.17  ?  380 GLN A O      1 
ATOM   1953 C  CB     . GLN A 1 269 ? -14.130 6.588   11.663  1.00 96.68  ?  380 GLN A CB     1 
ATOM   1954 C  CG     . GLN A 1 269 ? -14.444 5.146   12.068  1.00 111.50 ?  380 GLN A CG     1 
ATOM   1955 C  CD     . GLN A 1 269 ? -13.374 4.175   11.639  1.00 131.08 ?  380 GLN A CD     1 
ATOM   1956 O  OE1    . GLN A 1 269 ? -12.556 3.723   12.448  1.00 127.27 ?  380 GLN A OE1    1 
ATOM   1957 N  NE2    . GLN A 1 269 ? -13.369 3.814   10.361  1.00 120.29 ?  380 GLN A NE2    1 
ATOM   1958 N  N      . GLY A 1 270 ? -15.690 9.961   12.356  1.00 92.67  ?  381 GLY A N      1 
ATOM   1959 C  CA     . GLY A 1 270 ? -15.553 11.409  12.236  1.00 91.73  ?  381 GLY A CA     1 
ATOM   1960 C  C      . GLY A 1 270 ? -15.988 11.997  10.908  1.00 93.18  ?  381 GLY A C      1 
ATOM   1961 O  O      . GLY A 1 270 ? -16.601 13.070  10.880  1.00 92.92  ?  381 GLY A O      1 
ATOM   1962 N  N      . ARG A 1 271 ? -15.652 11.304  9.799   1.00 87.19  ?  382 ARG A N      1 
ATOM   1963 C  CA     . ARG A 1 271 ? -15.921 11.726  8.421   1.00 85.48  ?  382 ARG A CA     1 
ATOM   1964 C  C      . ARG A 1 271 ? -17.382 11.567  7.988   1.00 85.48  ?  382 ARG A C      1 
ATOM   1965 O  O      . ARG A 1 271 ? -17.990 10.524  8.233   1.00 84.72  ?  382 ARG A O      1 
ATOM   1966 C  CB     . ARG A 1 271 ? -14.974 11.009  7.433   1.00 85.52  ?  382 ARG A CB     1 
ATOM   1967 C  CG     . ARG A 1 271 ? -13.484 11.307  7.633   1.00 99.40  ?  382 ARG A CG     1 
ATOM   1968 C  CD     . ARG A 1 271 ? -13.057 12.657  7.069   1.00 113.01 ?  382 ARG A CD     1 
ATOM   1969 N  NE     . ARG A 1 271 ? -11.628 12.908  7.272   1.00 123.71 ?  382 ARG A NE     1 
ATOM   1970 C  CZ     . ARG A 1 271 ? -10.679 12.621  6.385   1.00 139.08 ?  382 ARG A CZ     1 
ATOM   1971 N  NH1    . ARG A 1 271 ? -9.408  12.885  6.656   1.00 125.55 1  382 ARG A NH1    1 
ATOM   1972 N  NH2    . ARG A 1 271 ? -10.994 12.070  5.218   1.00 127.52 ?  382 ARG A NH2    1 
ATOM   1973 N  N      . GLN A 1 272 ? -17.929 12.613  7.327   1.00 79.52  ?  383 GLN A N      1 
ATOM   1974 C  CA     . GLN A 1 272 ? -19.293 12.660  6.793   1.00 78.10  ?  383 GLN A CA     1 
ATOM   1975 C  C      . GLN A 1 272 ? -19.369 11.986  5.419   1.00 78.85  ?  383 GLN A C      1 
ATOM   1976 O  O      . GLN A 1 272 ? -18.576 12.319  4.524   1.00 78.10  ?  383 GLN A O      1 
ATOM   1977 C  CB     . GLN A 1 272 ? -19.774 14.112  6.666   1.00 79.44  ?  383 GLN A CB     1 
ATOM   1978 C  CG     . GLN A 1 272 ? -20.338 14.714  7.942   1.00 92.02  ?  383 GLN A CG     1 
ATOM   1979 C  CD     . GLN A 1 272 ? -21.041 16.018  7.653   1.00 109.78 ?  383 GLN A CD     1 
ATOM   1980 O  OE1    . GLN A 1 272 ? -20.466 16.961  7.090   1.00 103.57 ?  383 GLN A OE1    1 
ATOM   1981 N  NE2    . GLN A 1 272 ? -22.310 16.098  8.025   1.00 103.57 ?  383 GLN A NE2    1 
ATOM   1982 N  N      A TYR A 1 273 ? -20.311 11.036  5.259   0.58 74.48  ?  384 TYR A N      1 
ATOM   1983 N  N      B TYR A 1 273 ? -20.322 11.052  5.255   0.42 73.99  ?  384 TYR A N      1 
ATOM   1984 C  CA     A TYR A 1 273 ? -20.525 10.284  4.019   0.58 73.82  ?  384 TYR A CA     1 
ATOM   1985 C  CA     B TYR A 1 273 ? -20.534 10.333  4.000   0.42 73.09  ?  384 TYR A CA     1 
ATOM   1986 C  C      A TYR A 1 273 ? -22.001 10.232  3.594   0.58 75.78  ?  384 TYR A C      1 
ATOM   1987 C  C      B TYR A 1 273 ? -22.007 10.295  3.568   0.42 75.35  ?  384 TYR A C      1 
ATOM   1988 O  O      A TYR A 1 273 ? -22.894 10.508  4.399   0.58 75.68  ?  384 TYR A O      1 
ATOM   1989 O  O      B TYR A 1 273 ? -22.899 10.640  4.347   0.42 75.13  ?  384 TYR A O      1 
ATOM   1990 C  CB     A TYR A 1 273 ? -19.985 8.846   4.156   0.58 75.27  ?  384 TYR A CB     1 
ATOM   1991 C  CB     B TYR A 1 273 ? -19.914 8.915   4.051   0.42 74.16  ?  384 TYR A CB     1 
ATOM   1992 C  CG     A TYR A 1 273 ? -18.493 8.733   4.381   0.58 77.44  ?  384 TYR A CG     1 
ATOM   1993 C  CG     B TYR A 1 273 ? -20.724 7.870   4.794   0.42 75.70  ?  384 TYR A CG     1 
ATOM   1994 C  CD1    A TYR A 1 273 ? -17.982 8.358   5.619   0.58 79.51  ?  384 TYR A CD1    1 
ATOM   1995 C  CD1    B TYR A 1 273 ? -21.685 7.104   4.136   0.42 77.66  ?  384 TYR A CD1    1 
ATOM   1996 C  CD2    A TYR A 1 273 ? -17.592 8.939   3.339   0.58 78.22  ?  384 TYR A CD2    1 
ATOM   1997 C  CD2    B TYR A 1 273 ? -20.475 7.589   6.133   0.42 76.28  ?  384 TYR A CD2    1 
ATOM   1998 C  CE1    A TYR A 1 273 ? -16.611 8.211   5.822   0.58 80.54  ?  384 TYR A CE1    1 
ATOM   1999 C  CE1    B TYR A 1 273 ? -22.422 6.131   4.810   0.42 78.16  ?  384 TYR A CE1    1 
ATOM   2000 C  CE2    A TYR A 1 273 ? -16.218 8.812   3.534   0.58 79.15  ?  384 TYR A CE2    1 
ATOM   2001 C  CE2    B TYR A 1 273 ? -21.197 6.607   6.813   0.42 77.02  ?  384 TYR A CE2    1 
ATOM   2002 C  CZ     A TYR A 1 273 ? -15.732 8.447   4.778   0.58 87.38  ?  384 TYR A CZ     1 
ATOM   2003 C  CZ     B TYR A 1 273 ? -22.159 5.871   6.144   0.42 83.77  ?  384 TYR A CZ     1 
ATOM   2004 O  OH     A TYR A 1 273 ? -14.379 8.318   4.979   0.58 89.80  ?  384 TYR A OH     1 
ATOM   2005 O  OH     B TYR A 1 273 ? -22.877 4.911   6.815   0.42 84.37  ?  384 TYR A OH     1 
ATOM   2006 N  N      . LYS A 1 274 ? -22.242 9.855   2.320   1.00 70.25  ?  385 LYS A N      1 
ATOM   2007 C  CA     . LYS A 1 274 ? -23.563 9.669   1.705   1.00 68.20  ?  385 LYS A CA     1 
ATOM   2008 C  C      . LYS A 1 274 ? -23.505 8.334   0.949   1.00 69.30  ?  385 LYS A C      1 
ATOM   2009 O  O      . LYS A 1 274 ? -22.445 7.966   0.437   1.00 69.42  ?  385 LYS A O      1 
ATOM   2010 C  CB     . LYS A 1 274 ? -23.912 10.814  0.747   1.00 69.40  ?  385 LYS A CB     1 
ATOM   2011 C  CG     . LYS A 1 274 ? -24.677 11.948  1.404   1.00 68.01  ?  385 LYS A CG     1 
ATOM   2012 C  CD     . LYS A 1 274 ? -26.006 12.227  0.714   1.00 62.48  ?  385 LYS A CD     1 
ATOM   2013 C  CE     . LYS A 1 274 ? -26.632 13.484  1.264   1.00 65.89  ?  385 LYS A CE     1 
ATOM   2014 N  NZ     . LYS A 1 274 ? -27.772 13.951  0.436   1.00 70.86  1  385 LYS A NZ     1 
ATOM   2015 N  N      . VAL A 1 275 ? -24.622 7.604   0.903   1.00 63.03  ?  386 VAL A N      1 
ATOM   2016 C  CA     . VAL A 1 275 ? -24.706 6.305   0.225   1.00 61.40  ?  386 VAL A CA     1 
ATOM   2017 C  C      . VAL A 1 275 ? -24.920 6.493   -1.285  1.00 63.02  ?  386 VAL A C      1 
ATOM   2018 O  O      . VAL A 1 275 ? -25.817 7.227   -1.697  1.00 62.43  ?  386 VAL A O      1 
ATOM   2019 C  CB     . VAL A 1 275 ? -25.806 5.402   0.860   1.00 65.08  ?  386 VAL A CB     1 
ATOM   2020 C  CG1    . VAL A 1 275 ? -25.977 4.086   0.092   1.00 64.53  ?  386 VAL A CG1    1 
ATOM   2021 C  CG2    . VAL A 1 275 ? -25.509 5.132   2.332   1.00 65.09  ?  386 VAL A CG2    1 
ATOM   2022 N  N      . TYR A 1 276 ? -24.097 5.818   -2.101  1.00 57.94  ?  387 TYR A N      1 
ATOM   2023 C  CA     . TYR A 1 276 ? -24.237 5.853   -3.554  1.00 55.64  ?  387 TYR A CA     1 
ATOM   2024 C  C      . TYR A 1 276 ? -24.235 4.424   -4.043  1.00 56.71  ?  387 TYR A C      1 
ATOM   2025 O  O      . TYR A 1 276 ? -23.364 3.641   -3.666  1.00 55.94  ?  387 TYR A O      1 
ATOM   2026 C  CB     . TYR A 1 276 ? -23.121 6.682   -4.222  1.00 55.77  ?  387 TYR A CB     1 
ATOM   2027 C  CG     . TYR A 1 276 ? -23.227 6.729   -5.732  1.00 54.97  ?  387 TYR A CG     1 
ATOM   2028 C  CD1    . TYR A 1 276 ? -24.428 7.056   -6.359  1.00 55.48  ?  387 TYR A CD1    1 
ATOM   2029 C  CD2    . TYR A 1 276 ? -22.129 6.437   -6.538  1.00 54.96  ?  387 TYR A CD2    1 
ATOM   2030 C  CE1    . TYR A 1 276 ? -24.536 7.090   -7.745  1.00 54.30  ?  387 TYR A CE1    1 
ATOM   2031 C  CE2    . TYR A 1 276 ? -22.226 6.464   -7.930  1.00 55.14  ?  387 TYR A CE2    1 
ATOM   2032 C  CZ     . TYR A 1 276 ? -23.427 6.813   -8.529  1.00 58.27  ?  387 TYR A CZ     1 
ATOM   2033 O  OH     . TYR A 1 276 ? -23.550 6.846   -9.899  1.00 50.48  ?  387 TYR A OH     1 
ATOM   2034 N  N      . ARG A 1 277 ? -25.219 4.073   -4.864  1.00 52.57  ?  388 ARG A N      1 
ATOM   2035 C  CA     . ARG A 1 277 ? -25.328 2.707   -5.359  1.00 51.98  ?  388 ARG A CA     1 
ATOM   2036 C  C      . ARG A 1 277 ? -25.816 2.601   -6.793  1.00 56.20  ?  388 ARG A C      1 
ATOM   2037 O  O      . ARG A 1 277 ? -26.553 3.471   -7.273  1.00 56.82  ?  388 ARG A O      1 
ATOM   2038 C  CB     . ARG A 1 277 ? -26.231 1.865   -4.436  1.00 51.86  ?  388 ARG A CB     1 
ATOM   2039 C  CG     . ARG A 1 277 ? -27.716 2.209   -4.515  1.00 57.29  ?  388 ARG A CG     1 
ATOM   2040 C  CD     . ARG A 1 277 ? -28.562 1.384   -3.577  1.00 65.07  ?  388 ARG A CD     1 
ATOM   2041 N  NE     . ARG A 1 277 ? -29.983 1.723   -3.692  1.00 67.59  ?  388 ARG A NE     1 
ATOM   2042 C  CZ     . ARG A 1 277 ? -30.933 1.234   -2.898  1.00 79.61  ?  388 ARG A CZ     1 
ATOM   2043 N  NH1    . ARG A 1 277 ? -30.622 0.394   -1.918  1.00 65.91  1  388 ARG A NH1    1 
ATOM   2044 N  NH2    . ARG A 1 277 ? -32.201 1.578   -3.081  1.00 60.64  ?  388 ARG A NH2    1 
ATOM   2045 N  N      . GLY A 1 278 ? -25.461 1.490   -7.425  1.00 53.06  ?  389 GLY A N      1 
ATOM   2046 C  CA     . GLY A 1 278 ? -25.915 1.166   -8.764  1.00 53.18  ?  389 GLY A CA     1 
ATOM   2047 C  C      . GLY A 1 278 ? -27.379 0.803   -8.747  1.00 58.10  ?  389 GLY A C      1 
ATOM   2048 O  O      . GLY A 1 278 ? -27.869 0.234   -7.769  1.00 57.99  ?  389 GLY A O      1 
ATOM   2049 N  N      . MET A 1 279 ? -28.092 1.125   -9.829  1.00 54.44  ?  390 MET A N      1 
ATOM   2050 C  CA     . MET A 1 279 ? -29.513 0.800   -9.969  1.00 53.00  ?  390 MET A CA     1 
ATOM   2051 C  C      . MET A 1 279 ? -29.692 -0.700  -10.246 1.00 55.25  ?  390 MET A C      1 
ATOM   2052 O  O      . MET A 1 279 ? -30.814 -1.202  -10.299 1.00 55.13  ?  390 MET A O      1 
ATOM   2053 C  CB     . MET A 1 279 ? -30.171 1.692   -11.030 1.00 54.84  ?  390 MET A CB     1 
ATOM   2054 C  CG     . MET A 1 279 ? -30.365 3.130   -10.554 1.00 58.12  ?  390 MET A CG     1 
ATOM   2055 S  SD     . MET A 1 279 ? -31.589 3.318   -9.209  1.00 61.25  ?  390 MET A SD     1 
ATOM   2056 C  CE     . MET A 1 279 ? -33.101 3.256   -10.145 1.00 57.53  ?  390 MET A CE     1 
ATOM   2057 N  N      . GLY A 1 280 ? -28.562 -1.388  -10.387 1.00 50.42  ?  391 GLY A N      1 
ATOM   2058 C  CA     . GLY A 1 280 ? -28.452 -2.825  -10.602 1.00 49.41  ?  391 GLY A CA     1 
ATOM   2059 C  C      . GLY A 1 280 ? -27.773 -3.498  -9.424  1.00 52.93  ?  391 GLY A C      1 
ATOM   2060 O  O      . GLY A 1 280 ? -27.364 -4.653  -9.529  1.00 51.26  ?  391 GLY A O      1 
ATOM   2061 N  N      . SER A 1 281 ? -27.639 -2.779  -8.281  1.00 50.82  ?  392 SER A N      1 
ATOM   2062 C  CA     . SER A 1 281 ? -27.095 -3.372  -7.055  1.00 52.30  ?  392 SER A CA     1 
ATOM   2063 C  C      . SER A 1 281 ? -28.233 -4.111  -6.364  1.00 60.19  ?  392 SER A C      1 
ATOM   2064 O  O      . SER A 1 281 ? -29.398 -3.799  -6.637  1.00 58.79  ?  392 SER A O      1 
ATOM   2065 C  CB     . SER A 1 281 ? -26.544 -2.305  -6.113  1.00 55.89  ?  392 SER A CB     1 
ATOM   2066 O  OG     . SER A 1 281 ? -27.563 -1.422  -5.669  1.00 65.86  ?  392 SER A OG     1 
ATOM   2067 N  N      . LEU A 1 282 ? -27.887 -5.056  -5.455  1.00 60.78  ?  393 LEU A N      1 
ATOM   2068 C  CA     . LEU A 1 282 ? -28.804 -5.869  -4.649  1.00 62.72  ?  393 LEU A CA     1 
ATOM   2069 C  C      . LEU A 1 282 ? -29.929 -5.032  -4.018  1.00 69.02  ?  393 LEU A C      1 
ATOM   2070 O  O      . LEU A 1 282 ? -31.098 -5.277  -4.322  1.00 68.77  ?  393 LEU A O      1 
ATOM   2071 C  CB     . LEU A 1 282 ? -28.031 -6.651  -3.568  1.00 63.12  ?  393 LEU A CB     1 
ATOM   2072 C  CG     . LEU A 1 282 ? -27.267 -7.888  -4.051  1.00 68.85  ?  393 LEU A CG     1 
ATOM   2073 C  CD1    . LEU A 1 282 ? -26.008 -8.111  -3.230  1.00 69.35  ?  393 LEU A CD1    1 
ATOM   2074 C  CD2    . LEU A 1 282 ? -28.152 -9.136  -4.041  1.00 71.26  ?  393 LEU A CD2    1 
ATOM   2075 N  N      . GLY A 1 283 ? -29.555 -4.016  -3.233  1.00 66.88  ?  394 GLY A N      1 
ATOM   2076 C  CA     . GLY A 1 283 ? -30.483 -3.114  -2.555  1.00 67.28  ?  394 GLY A CA     1 
ATOM   2077 C  C      . GLY A 1 283 ? -31.434 -2.355  -3.462  1.00 72.70  ?  394 GLY A C      1 
ATOM   2078 O  O      . GLY A 1 283 ? -32.615 -2.207  -3.135  1.00 72.23  ?  394 GLY A O      1 
ATOM   2079 N  N      . ALA A 1 284 ? -30.924 -1.857  -4.606  1.00 69.87  ?  395 ALA A N      1 
ATOM   2080 C  CA     . ALA A 1 284 ? -31.719 -1.094  -5.571  1.00 69.41  ?  395 ALA A CA     1 
ATOM   2081 C  C      . ALA A 1 284 ? -32.700 -1.955  -6.346  1.00 72.62  ?  395 ALA A C      1 
ATOM   2082 O  O      . ALA A 1 284 ? -33.761 -1.458  -6.734  1.00 72.62  ?  395 ALA A O      1 
ATOM   2083 C  CB     . ALA A 1 284 ? -30.818 -0.330  -6.526  1.00 69.94  ?  395 ALA A CB     1 
ATOM   2084 N  N      . MET A 1 285 ? -32.354 -3.233  -6.580  1.00 68.88  ?  396 MET A N      1 
ATOM   2085 C  CA     . MET A 1 285 ? -33.222 -4.168  -7.305  1.00 68.69  ?  396 MET A CA     1 
ATOM   2086 C  C      . MET A 1 285 ? -34.459 -4.515  -6.453  1.00 74.98  ?  396 MET A C      1 
ATOM   2087 O  O      . MET A 1 285 ? -35.530 -4.769  -7.007  1.00 75.59  ?  396 MET A O      1 
ATOM   2088 C  CB     . MET A 1 285 ? -32.450 -5.421  -7.790  1.00 70.54  ?  396 MET A CB     1 
ATOM   2089 C  CG     . MET A 1 285 ? -31.421 -5.125  -8.923  1.00 73.28  ?  396 MET A CG     1 
ATOM   2090 S  SD     . MET A 1 285 ? -30.481 -6.533  -9.622  1.00 76.46  ?  396 MET A SD     1 
ATOM   2091 C  CE     . MET A 1 285 ? -29.702 -7.189  -8.156  1.00 72.75  ?  396 MET A CE     1 
ATOM   2092 N  N      . GLU A 1 286 ? -34.319 -4.447  -5.110  1.00 71.95  ?  397 GLU A N      1 
ATOM   2093 C  CA     . GLU A 1 286 ? -35.393 -4.679  -4.137  1.00 92.29  ?  397 GLU A CA     1 
ATOM   2094 C  C      . GLU A 1 286 ? -36.385 -3.510  -4.169  1.00 112.62 ?  397 GLU A C      1 
ATOM   2095 O  O      . GLU A 1 286 ? -35.978 -2.345  -4.181  1.00 67.77  ?  397 GLU A O      1 
ATOM   2096 C  CB     . GLU A 1 286 ? -34.821 -4.832  -2.716  1.00 93.58  ?  397 GLU A CB     1 
ATOM   2097 C  CG     . GLU A 1 286 ? -33.995 -6.087  -2.500  1.00 103.23 ?  397 GLU A CG     1 
ATOM   2098 C  CD     . GLU A 1 286 ? -33.366 -6.189  -1.124  1.00 125.39 ?  397 GLU A CD     1 
ATOM   2099 O  OE1    . GLU A 1 286 ? -32.459 -5.381  -0.819  1.00 117.98 ?  397 GLU A OE1    1 
ATOM   2100 O  OE2    . GLU A 1 286 ? -33.770 -7.091  -0.355  1.00 122.60 -1 397 GLU A OE2    1 
ATOM   2101 N  N      . LYS A 1 302 ? -34.480 -14.205 -11.254 1.00 82.18  ?  413 LYS A N      1 
ATOM   2102 C  CA     . LYS A 1 302 ? -34.081 -12.827 -10.969 1.00 81.74  ?  413 LYS A CA     1 
ATOM   2103 C  C      . LYS A 1 302 ? -32.680 -12.510 -11.505 1.00 84.27  ?  413 LYS A C      1 
ATOM   2104 O  O      . LYS A 1 302 ? -31.834 -13.410 -11.594 1.00 83.34  ?  413 LYS A O      1 
ATOM   2105 C  CB     . LYS A 1 302 ? -34.144 -12.558 -9.472  1.00 82.49  ?  413 LYS A CB     1 
ATOM   2106 N  N      . PHE A 1 303 ? -32.446 -11.221 -11.857 1.00 79.27  ?  414 PHE A N      1 
ATOM   2107 C  CA     . PHE A 1 303 ? -31.171 -10.724 -12.383 1.00 77.93  ?  414 PHE A CA     1 
ATOM   2108 C  C      . PHE A 1 303 ? -30.052 -10.755 -11.341 1.00 78.27  ?  414 PHE A C      1 
ATOM   2109 O  O      . PHE A 1 303 ? -30.253 -10.351 -10.190 1.00 78.78  ?  414 PHE A O      1 
ATOM   2110 C  CB     . PHE A 1 303 ? -31.299 -9.282  -12.921 1.00 79.84  ?  414 PHE A CB     1 
ATOM   2111 C  CG     . PHE A 1 303 ? -31.955 -9.085  -14.270 1.00 81.32  ?  414 PHE A CG     1 
ATOM   2112 C  CD1    . PHE A 1 303 ? -31.550 -9.826  -15.375 1.00 84.26  ?  414 PHE A CD1    1 
ATOM   2113 C  CD2    . PHE A 1 303 ? -32.918 -8.100  -14.454 1.00 83.60  ?  414 PHE A CD2    1 
ATOM   2114 C  CE1    . PHE A 1 303 ? -32.152 -9.636  -16.622 1.00 85.19  ?  414 PHE A CE1    1 
ATOM   2115 C  CE2    . PHE A 1 303 ? -33.505 -7.897  -15.707 1.00 86.34  ?  414 PHE A CE2    1 
ATOM   2116 C  CZ     . PHE A 1 303 ? -33.115 -8.664  -16.783 1.00 84.41  ?  414 PHE A CZ     1 
ATOM   2117 N  N      . VAL A 1 304 ? -28.859 -11.198 -11.776 1.00 70.31  ?  415 VAL A N      1 
ATOM   2118 C  CA     . VAL A 1 304 ? -27.636 -11.233 -10.971 1.00 67.13  ?  415 VAL A CA     1 
ATOM   2119 C  C      . VAL A 1 304 ? -27.163 -9.749  -10.833 1.00 65.03  ?  415 VAL A C      1 
ATOM   2120 O  O      . VAL A 1 304 ? -27.436 -8.971  -11.746 1.00 64.03  ?  415 VAL A O      1 
ATOM   2121 C  CB     . VAL A 1 304 ? -26.629 -12.226 -11.630 1.00 70.14  ?  415 VAL A CB     1 
ATOM   2122 C  CG1    . VAL A 1 304 ? -25.197 -11.705 -11.651 1.00 70.13  ?  415 VAL A CG1    1 
ATOM   2123 C  CG2    . VAL A 1 304 ? -26.706 -13.596 -10.965 1.00 69.36  ?  415 VAL A CG2    1 
ATOM   2124 N  N      . PRO A 1 305 ? -26.602 -9.284  -9.688  1.00 58.42  ?  416 PRO A N      1 
ATOM   2125 C  CA     . PRO A 1 305 ? -26.254 -7.847  -9.585  1.00 56.61  ?  416 PRO A CA     1 
ATOM   2126 C  C      . PRO A 1 305 ? -25.184 -7.362  -10.573 1.00 55.61  ?  416 PRO A C      1 
ATOM   2127 O  O      . PRO A 1 305 ? -24.235 -8.080  -10.856 1.00 54.34  ?  416 PRO A O      1 
ATOM   2128 C  CB     . PRO A 1 305 ? -25.823 -7.674  -8.126  1.00 58.36  ?  416 PRO A CB     1 
ATOM   2129 C  CG     . PRO A 1 305 ? -25.377 -9.037  -7.706  1.00 64.09  ?  416 PRO A CG     1 
ATOM   2130 C  CD     . PRO A 1 305 ? -26.232 -10.021 -8.460  1.00 59.98  ?  416 PRO A CD     1 
ATOM   2131 N  N      . GLU A 1 306 ? -25.387 -6.149  -11.120 1.00 49.93  ?  417 GLU A N      1 
ATOM   2132 C  CA     . GLU A 1 306 ? -24.486 -5.486  -12.062 1.00 48.78  ?  417 GLU A CA     1 
ATOM   2133 C  C      . GLU A 1 306 ? -24.024 -4.126  -11.546 1.00 54.79  ?  417 GLU A C      1 
ATOM   2134 O  O      . GLU A 1 306 ? -23.418 -3.350  -12.285 1.00 54.06  ?  417 GLU A O      1 
ATOM   2135 C  CB     . GLU A 1 306 ? -25.151 -5.343  -13.429 1.00 49.31  ?  417 GLU A CB     1 
ATOM   2136 C  CG     . GLU A 1 306 ? -25.202 -6.650  -14.194 1.00 53.59  ?  417 GLU A CG     1 
ATOM   2137 C  CD     . GLU A 1 306 ? -25.732 -6.501  -15.602 1.00 61.93  ?  417 GLU A CD     1 
ATOM   2138 O  OE1    . GLU A 1 306 ? -26.547 -7.353  -16.020 1.00 64.70  ?  417 GLU A OE1    1 
ATOM   2139 O  OE2    . GLU A 1 306 ? -25.384 -5.496  -16.264 1.00 54.32  -1 417 GLU A OE2    1 
ATOM   2140 N  N      . GLY A 1 307 ? -24.270 -3.874  -10.267 1.00 53.00  ?  418 GLY A N      1 
ATOM   2141 C  CA     . GLY A 1 307 ? -23.901 -2.632  -9.608  1.00 53.56  ?  418 GLY A CA     1 
ATOM   2142 C  C      . GLY A 1 307 ? -23.501 -2.835  -8.168  1.00 59.79  ?  418 GLY A C      1 
ATOM   2143 O  O      . GLY A 1 307 ? -23.832 -3.860  -7.567  1.00 59.82  ?  418 GLY A O      1 
ATOM   2144 N  N      . ILE A 1 308 ? -22.758 -1.871  -7.619  1.00 57.37  ?  419 ILE A N      1 
ATOM   2145 C  CA     . ILE A 1 308 ? -22.298 -1.937  -6.234  1.00 58.03  ?  419 ILE A CA     1 
ATOM   2146 C  C      . ILE A 1 308 ? -22.931 -0.848  -5.384  1.00 63.57  ?  419 ILE A C      1 
ATOM   2147 O  O      . ILE A 1 308 ? -23.438 0.145   -5.915  1.00 61.40  ?  419 ILE A O      1 
ATOM   2148 C  CB     . ILE A 1 308 ? -20.742 -1.950  -6.096  1.00 60.85  ?  419 ILE A CB     1 
ATOM   2149 C  CG1    . ILE A 1 308 ? -20.069 -0.848  -6.932  1.00 61.39  ?  419 ILE A CG1    1 
ATOM   2150 C  CG2    . ILE A 1 308 ? -20.163 -3.317  -6.393  1.00 61.16  ?  419 ILE A CG2    1 
ATOM   2151 C  CD1    . ILE A 1 308 ? -19.177 0.084   -6.139  1.00 69.04  ?  419 ILE A CD1    1 
ATOM   2152 N  N      . GLU A 1 309 ? -22.898 -1.048  -4.054  1.00 62.97  ?  420 GLU A N      1 
ATOM   2153 C  CA     . GLU A 1 309 ? -23.397 -0.099  -3.067  1.00 63.60  ?  420 GLU A CA     1 
ATOM   2154 C  C      . GLU A 1 309 ? -22.215 0.248   -2.181  1.00 68.87  ?  420 GLU A C      1 
ATOM   2155 O  O      . GLU A 1 309 ? -21.493 -0.647  -1.716  1.00 68.27  ?  420 GLU A O      1 
ATOM   2156 C  CB     . GLU A 1 309 ? -24.557 -0.697  -2.260  1.00 65.33  ?  420 GLU A CB     1 
ATOM   2157 C  CG     . GLU A 1 309 ? -25.219 0.303   -1.316  1.00 78.42  ?  420 GLU A CG     1 
ATOM   2158 C  CD     . GLU A 1 309 ? -26.567 -0.070  -0.723  1.00 102.40 ?  420 GLU A CD     1 
ATOM   2159 O  OE1    . GLU A 1 309 ? -27.105 -1.151  -1.060  1.00 99.41  ?  420 GLU A OE1    1 
ATOM   2160 O  OE2    . GLU A 1 309 ? -27.092 0.736   0.078   1.00 96.31  -1 420 GLU A OE2    1 
ATOM   2161 N  N      . GLY A 1 310 ? -21.996 1.543   -2.005  1.00 65.98  ?  421 GLY A N      1 
ATOM   2162 C  CA     . GLY A 1 310 ? -20.877 2.043   -1.222  1.00 66.02  ?  421 GLY A CA     1 
ATOM   2163 C  C      . GLY A 1 310 ? -21.095 3.401   -0.596  1.00 70.44  ?  421 GLY A C      1 
ATOM   2164 O  O      . GLY A 1 310 ? -22.218 3.916   -0.541  1.00 69.13  ?  421 GLY A O      1 
ATOM   2165 N  N      . ARG A 1 311 ? -19.991 3.984   -0.130  1.00 67.81  ?  422 ARG A N      1 
ATOM   2166 C  CA     . ARG A 1 311 ? -19.982 5.262   0.559   1.00 67.68  ?  422 ARG A CA     1 
ATOM   2167 C  C      . ARG A 1 311 ? -19.185 6.270   -0.236  1.00 70.43  ?  422 ARG A C      1 
ATOM   2168 O  O      . ARG A 1 311 ? -18.142 5.928   -0.800  1.00 69.96  ?  422 ARG A O      1 
ATOM   2169 C  CB     . ARG A 1 311 ? -19.382 5.098   1.975   1.00 69.06  ?  422 ARG A CB     1 
ATOM   2170 C  CG     . ARG A 1 311 ? -20.122 4.091   2.851   1.00 82.67  ?  422 ARG A CG     1 
ATOM   2171 C  CD     . ARG A 1 311 ? -19.419 3.827   4.170   1.00 100.53 ?  422 ARG A CD     1 
ATOM   2172 N  NE     . ARG A 1 311 ? -20.283 3.087   5.095   1.00 115.23 ?  422 ARG A NE     1 
ATOM   2173 C  CZ     . ARG A 1 311 ? -19.848 2.306   6.079   1.00 128.36 ?  422 ARG A CZ     1 
ATOM   2174 N  NH1    . ARG A 1 311 ? -18.546 2.139   6.280   1.00 114.48 1  422 ARG A NH1    1 
ATOM   2175 N  NH2    . ARG A 1 311 ? -20.712 1.678   6.866   1.00 113.59 ?  422 ARG A NH2    1 
ATOM   2176 N  N      . THR A 1 312 ? -19.693 7.510   -0.288  1.00 66.08  ?  423 THR A N      1 
ATOM   2177 C  CA     . THR A 1 312 ? -19.074 8.650   -0.961  1.00 65.48  ?  423 THR A CA     1 
ATOM   2178 C  C      . THR A 1 312 ? -19.093 9.856   -0.027  1.00 69.09  ?  423 THR A C      1 
ATOM   2179 O  O      . THR A 1 312 ? -20.092 10.090  0.653   1.00 67.07  ?  423 THR A O      1 
ATOM   2180 C  CB     . THR A 1 312 ? -19.677 8.899   -2.366  1.00 72.01  ?  423 THR A CB     1 
ATOM   2181 O  OG1    . THR A 1 312 ? -18.873 9.861   -3.055  1.00 73.32  ?  423 THR A OG1    1 
ATOM   2182 C  CG2    . THR A 1 312 ? -21.153 9.341   -2.339  1.00 66.11  ?  423 THR A CG2    1 
ATOM   2183 N  N      . ALA A 1 313 ? -17.979 10.600  0.024   1.00 66.94  ?  424 ALA A N      1 
ATOM   2184 C  CA     . ALA A 1 313 ? -17.827 11.766  0.894   1.00 67.35  ?  424 ALA A CA     1 
ATOM   2185 C  C      . ALA A 1 313 ? -18.913 12.817  0.661   1.00 71.60  ?  424 ALA A C      1 
ATOM   2186 O  O      . ALA A 1 313 ? -19.337 13.033  -0.481  1.00 71.58  ?  424 ALA A O      1 
ATOM   2187 C  CB     . ALA A 1 313 ? -16.451 12.381  0.699   1.00 68.24  ?  424 ALA A CB     1 
ATOM   2188 N  N      . TYR A 1 314 ? -19.396 13.432  1.755   1.00 68.01  ?  425 TYR A N      1 
ATOM   2189 C  CA     . TYR A 1 314 ? -20.388 14.504  1.706   1.00 67.37  ?  425 TYR A CA     1 
ATOM   2190 C  C      . TYR A 1 314 ? -19.737 15.717  1.019   1.00 69.47  ?  425 TYR A C      1 
ATOM   2191 O  O      . TYR A 1 314 ? -18.640 16.135  1.405   1.00 68.21  ?  425 TYR A O      1 
ATOM   2192 C  CB     . TYR A 1 314 ? -20.896 14.835  3.120   1.00 69.15  ?  425 TYR A CB     1 
ATOM   2193 C  CG     . TYR A 1 314 ? -21.895 15.973  3.164   1.00 71.26  ?  425 TYR A CG     1 
ATOM   2194 C  CD1    . TYR A 1 314 ? -23.200 15.800  2.711   1.00 73.13  ?  425 TYR A CD1    1 
ATOM   2195 C  CD2    . TYR A 1 314 ? -21.538 17.219  3.670   1.00 72.13  ?  425 TYR A CD2    1 
ATOM   2196 C  CE1    . TYR A 1 314 ? -24.123 16.845  2.749   1.00 74.20  ?  425 TYR A CE1    1 
ATOM   2197 C  CE2    . TYR A 1 314 ? -22.447 18.273  3.702   1.00 73.10  ?  425 TYR A CE2    1 
ATOM   2198 C  CZ     . TYR A 1 314 ? -23.744 18.078  3.257   1.00 81.32  ?  425 TYR A CZ     1 
ATOM   2199 O  OH     . TYR A 1 314 ? -24.640 19.118  3.300   1.00 83.14  ?  425 TYR A OH     1 
ATOM   2200 N  N      . LYS A 1 315 ? -20.374 16.214  -0.052  1.00 66.18  ?  426 LYS A N      1 
ATOM   2201 C  CA     . LYS A 1 315 ? -19.852 17.291  -0.899  1.00 65.71  ?  426 LYS A CA     1 
ATOM   2202 C  C      . LYS A 1 315 ? -20.316 18.679  -0.525  1.00 69.00  ?  426 LYS A C      1 
ATOM   2203 O  O      . LYS A 1 315 ? -19.598 19.654  -0.776  1.00 68.55  ?  426 LYS A O      1 
ATOM   2204 C  CB     . LYS A 1 315 ? -20.165 17.014  -2.380  1.00 68.01  ?  426 LYS A CB     1 
ATOM   2205 C  CG     . LYS A 1 315 ? -19.182 16.049  -3.027  1.00 75.13  ?  426 LYS A CG     1 
ATOM   2206 C  CD     . LYS A 1 315 ? -19.366 15.959  -4.533  1.00 83.27  ?  426 LYS A CD     1 
ATOM   2207 C  CE     . LYS A 1 315 ? -18.264 16.646  -5.301  1.00 90.69  ?  426 LYS A CE     1 
ATOM   2208 N  NZ     . LYS A 1 315 ? -18.372 16.389  -6.762  1.00 95.73  1  426 LYS A NZ     1 
ATOM   2209 N  N      . GLY A 1 316 ? -21.513 18.759  0.043   1.00 64.85  ?  427 GLY A N      1 
ATOM   2210 C  CA     . GLY A 1 316 ? -22.137 20.016  0.430   1.00 64.01  ?  427 GLY A CA     1 
ATOM   2211 C  C      . GLY A 1 316 ? -23.214 20.408  -0.554  1.00 64.17  ?  427 GLY A C      1 
ATOM   2212 O  O      . GLY A 1 316 ? -23.929 19.544  -1.054  1.00 63.62  ?  427 GLY A O      1 
ATOM   2213 N  N      . ALA A 1 317 ? -23.330 21.707  -0.849  1.00 57.88  ?  428 ALA A N      1 
ATOM   2214 C  CA     . ALA A 1 317 ? -24.331 22.211  -1.782  1.00 56.79  ?  428 ALA A CA     1 
ATOM   2215 C  C      . ALA A 1 317 ? -23.984 21.852  -3.230  1.00 58.78  ?  428 ALA A C      1 
ATOM   2216 O  O      . ALA A 1 317 ? -22.840 22.054  -3.658  1.00 56.88  ?  428 ALA A O      1 
ATOM   2217 C  CB     . ALA A 1 317 ? -24.465 23.722  -1.641  1.00 57.30  ?  428 ALA A CB     1 
ATOM   2218 N  N      . LEU A 1 318 ? -25.004 21.362  -3.985  1.00 54.61  ?  429 LEU A N      1 
ATOM   2219 C  CA     . LEU A 1 318 ? -24.957 21.011  -5.412  1.00 54.27  ?  429 LEU A CA     1 
ATOM   2220 C  C      . LEU A 1 318 ? -24.392 22.185  -6.223  1.00 56.60  ?  429 LEU A C      1 
ATOM   2221 O  O      . LEU A 1 318 ? -23.526 21.990  -7.075  1.00 54.54  ?  429 LEU A O      1 
ATOM   2222 C  CB     . LEU A 1 318 ? -26.390 20.681  -5.902  1.00 54.28  ?  429 LEU A CB     1 
ATOM   2223 C  CG     . LEU A 1 318 ? -26.614 20.408  -7.397  1.00 58.12  ?  429 LEU A CG     1 
ATOM   2224 C  CD1    . LEU A 1 318 ? -27.800 19.584  -7.581  1.00 58.70  ?  429 LEU A CD1    1 
ATOM   2225 C  CD2    . LEU A 1 318 ? -26.912 21.649  -8.155  1.00 57.02  ?  429 LEU A CD2    1 
ATOM   2226 N  N      . GLN A 1 319 ? -24.932 23.393  -5.966  1.00 52.80  ?  430 GLN A N      1 
ATOM   2227 C  CA     . GLN A 1 319 ? -24.595 24.668  -6.587  1.00 52.71  ?  430 GLN A CA     1 
ATOM   2228 C  C      . GLN A 1 319 ? -23.075 24.889  -6.633  1.00 56.03  ?  430 GLN A C      1 
ATOM   2229 O  O      . GLN A 1 319 ? -22.569 25.377  -7.638  1.00 56.65  ?  430 GLN A O      1 
ATOM   2230 C  CB     . GLN A 1 319 ? -25.296 25.801  -5.801  1.00 54.38  ?  430 GLN A CB     1 
ATOM   2231 C  CG     . GLN A 1 319 ? -25.088 27.204  -6.351  1.00 73.50  ?  430 GLN A CG     1 
ATOM   2232 C  CD     . GLN A 1 319 ? -25.750 28.223  -5.462  1.00 92.74  ?  430 GLN A CD     1 
ATOM   2233 O  OE1    . GLN A 1 319 ? -26.942 28.503  -5.595  1.00 87.44  ?  430 GLN A OE1    1 
ATOM   2234 N  NE2    . GLN A 1 319 ? -24.997 28.780  -4.521  1.00 85.09  ?  430 GLN A NE2    1 
ATOM   2235 N  N      . ASP A 1 320 ? -22.360 24.519  -5.551  1.00 52.76  ?  431 ASP A N      1 
ATOM   2236 C  CA     . ASP A 1 320 ? -20.902 24.670  -5.439  1.00 51.78  ?  431 ASP A CA     1 
ATOM   2237 C  C      . ASP A 1 320 ? -20.172 23.587  -6.269  1.00 53.75  ?  431 ASP A C      1 
ATOM   2238 O  O      . ASP A 1 320 ? -19.133 23.867  -6.866  1.00 51.19  ?  431 ASP A O      1 
ATOM   2239 C  CB     . ASP A 1 320 ? -20.457 24.629  -3.963  1.00 53.34  ?  431 ASP A CB     1 
ATOM   2240 C  CG     . ASP A 1 320 ? -21.224 25.553  -3.023  1.00 65.52  ?  431 ASP A CG     1 
ATOM   2241 O  OD1    . ASP A 1 320 ? -21.677 26.627  -3.480  1.00 64.66  ?  431 ASP A OD1    1 
ATOM   2242 O  OD2    . ASP A 1 320 ? -21.364 25.201  -1.828  1.00 73.53  -1 431 ASP A OD2    1 
ATOM   2243 N  N      . THR A 1 321 ? -20.730 22.355  -6.293  1.00 50.98  ?  432 THR A N      1 
ATOM   2244 C  CA     . THR A 1 321 ? -20.181 21.237  -7.054  1.00 50.11  ?  432 THR A CA     1 
ATOM   2245 C  C      . THR A 1 321 ? -20.237 21.587  -8.538  1.00 52.86  ?  432 THR A C      1 
ATOM   2246 O  O      . THR A 1 321 ? -19.225 21.478  -9.233  1.00 50.70  ?  432 THR A O      1 
ATOM   2247 C  CB     . THR A 1 321 ? -20.858 19.907  -6.643  1.00 56.15  ?  432 THR A CB     1 
ATOM   2248 O  OG1    . THR A 1 321 ? -20.224 19.429  -5.452  1.00 52.02  ?  432 THR A OG1    1 
ATOM   2249 C  CG2    . THR A 1 321 ? -20.754 18.818  -7.721  1.00 56.50  ?  432 THR A CG2    1 
ATOM   2250 N  N      . ILE A 1 322 ? -21.409 22.081  -8.987  1.00 49.28  ?  433 ILE A N      1 
ATOM   2251 C  CA     . ILE A 1 322 ? -21.679 22.502  -10.360 1.00 48.28  ?  433 ILE A CA     1 
ATOM   2252 C  C      . ILE A 1 322 ? -20.776 23.653  -10.771 1.00 54.24  ?  433 ILE A C      1 
ATOM   2253 O  O      . ILE A 1 322 ? -20.211 23.603  -11.865 1.00 53.87  ?  433 ILE A O      1 
ATOM   2254 C  CB     . ILE A 1 322 ? -23.196 22.797  -10.567 1.00 50.53  ?  433 ILE A CB     1 
ATOM   2255 C  CG1    . ILE A 1 322 ? -24.059 21.513  -10.391 1.00 50.55  ?  433 ILE A CG1    1 
ATOM   2256 C  CG2    . ILE A 1 322 ? -23.505 23.522  -11.894 1.00 50.46  ?  433 ILE A CG2    1 
ATOM   2257 C  CD1    . ILE A 1 322 ? -23.917 20.336  -11.468 1.00 52.79  ?  433 ILE A CD1    1 
ATOM   2258 N  N      . TYR A 1 323 ? -20.610 24.665  -9.896  1.00 52.28  ?  434 TYR A N      1 
ATOM   2259 C  CA     . TYR A 1 323 ? -19.768 25.815  -10.197 1.00 53.45  ?  434 TYR A CA     1 
ATOM   2260 C  C      . TYR A 1 323 ? -18.329 25.401  -10.466 1.00 54.75  ?  434 TYR A C      1 
ATOM   2261 O  O      . TYR A 1 323 ? -17.731 25.924  -11.400 1.00 55.33  ?  434 TYR A O      1 
ATOM   2262 C  CB     . TYR A 1 323 ? -19.840 26.903  -9.105  1.00 56.71  ?  434 TYR A CB     1 
ATOM   2263 C  CG     . TYR A 1 323 ? -19.075 28.159  -9.479  1.00 62.08  ?  434 TYR A CG     1 
ATOM   2264 C  CD1    . TYR A 1 323 ? -19.656 29.143  -10.278 1.00 65.39  ?  434 TYR A CD1    1 
ATOM   2265 C  CD2    . TYR A 1 323 ? -17.759 28.349  -9.063  1.00 63.70  ?  434 TYR A CD2    1 
ATOM   2266 C  CE1    . TYR A 1 323 ? -18.945 30.285  -10.655 1.00 67.39  ?  434 TYR A CE1    1 
ATOM   2267 C  CE2    . TYR A 1 323 ? -17.043 29.493  -9.425  1.00 65.38  ?  434 TYR A CE2    1 
ATOM   2268 C  CZ     . TYR A 1 323 ? -17.641 30.458  -10.221 1.00 75.00  ?  434 TYR A CZ     1 
ATOM   2269 O  OH     . TYR A 1 323 ? -16.939 31.581  -10.591 1.00 80.18  ?  434 TYR A OH     1 
ATOM   2270 N  N      . GLN A 1 324 ? -17.771 24.485  -9.648  1.00 51.27  ?  435 GLN A N      1 
ATOM   2271 C  CA     . GLN A 1 324 ? -16.400 24.002  -9.839  1.00 50.97  ?  435 GLN A CA     1 
ATOM   2272 C  C      . GLN A 1 324 ? -16.273 23.267  -11.166 1.00 51.94  ?  435 GLN A C      1 
ATOM   2273 O  O      . GLN A 1 324 ? -15.377 23.595  -11.943 1.00 52.04  ?  435 GLN A O      1 
ATOM   2274 C  CB     . GLN A 1 324 ? -15.920 23.122  -8.669  1.00 52.61  ?  435 GLN A CB     1 
ATOM   2275 C  CG     . GLN A 1 324 ? -15.722 23.892  -7.355  1.00 75.26  ?  435 GLN A CG     1 
ATOM   2276 C  CD     . GLN A 1 324 ? -14.641 24.951  -7.413  1.00 92.77  ?  435 GLN A CD     1 
ATOM   2277 O  OE1    . GLN A 1 324 ? -14.921 26.151  -7.508  1.00 88.62  ?  435 GLN A OE1    1 
ATOM   2278 N  NE2    . GLN A 1 324 ? -13.384 24.534  -7.334  1.00 83.39  ?  435 GLN A NE2    1 
ATOM   2279 N  N      . LEU A 1 325 ? -17.219 22.347  -11.446 1.00 45.70  ?  436 LEU A N      1 
ATOM   2280 C  CA     . LEU A 1 325 ? -17.292 21.539  -12.664 1.00 44.90  ?  436 LEU A CA     1 
ATOM   2281 C  C      . LEU A 1 325 ? -17.381 22.395  -13.913 1.00 49.20  ?  436 LEU A C      1 
ATOM   2282 O  O      . LEU A 1 325 ? -16.656 22.141  -14.872 1.00 47.79  ?  436 LEU A O      1 
ATOM   2283 C  CB     . LEU A 1 325 ? -18.475 20.551  -12.630 1.00 43.98  ?  436 LEU A CB     1 
ATOM   2284 C  CG     . LEU A 1 325 ? -18.408 19.371  -11.634 1.00 47.59  ?  436 LEU A CG     1 
ATOM   2285 C  CD1    . LEU A 1 325 ? -19.677 18.528  -11.708 1.00 47.68  ?  436 LEU A CD1    1 
ATOM   2286 C  CD2    . LEU A 1 325 ? -17.183 18.472  -11.879 1.00 47.48  ?  436 LEU A CD2    1 
ATOM   2287 N  N      . MET A 1 326 ? -18.262 23.408  -13.912 1.00 45.23  ?  437 MET A N      1 
ATOM   2288 C  CA     . MET A 1 326 ? -18.421 24.258  -15.090 1.00 44.48  ?  437 MET A CA     1 
ATOM   2289 C  C      . MET A 1 326 ? -17.239 25.195  -15.273 1.00 46.54  ?  437 MET A C      1 
ATOM   2290 O  O      . MET A 1 326 ? -16.893 25.548  -16.402 1.00 46.19  ?  437 MET A O      1 
ATOM   2291 C  CB     . MET A 1 326 ? -19.779 24.973  -15.078 1.00 47.51  ?  437 MET A CB     1 
ATOM   2292 C  CG     . MET A 1 326 ? -20.990 24.010  -15.155 1.00 51.09  ?  437 MET A CG     1 
ATOM   2293 S  SD     . MET A 1 326 ? -21.144 23.020  -16.689 1.00 55.36  ?  437 MET A SD     1 
ATOM   2294 C  CE     . MET A 1 326 ? -20.374 21.432  -16.144 1.00 51.07  ?  437 MET A CE     1 
ATOM   2295 N  N      . GLY A 1 327 ? -16.564 25.514  -14.180 1.00 44.02  ?  438 GLY A N      1 
ATOM   2296 C  CA     . GLY A 1 327 ? -15.347 26.319  -14.218 1.00 44.93  ?  438 GLY A CA     1 
ATOM   2297 C  C      . GLY A 1 327 ? -14.248 25.637  -15.019 1.00 48.14  ?  438 GLY A C      1 
ATOM   2298 O  O      . GLY A 1 327 ? -13.564 26.280  -15.818 1.00 48.14  ?  438 GLY A O      1 
ATOM   2299 N  N      . GLY A 1 328 ? -14.110 24.329  -14.820 1.00 45.03  ?  439 GLY A N      1 
ATOM   2300 C  CA     . GLY A 1 328 ? -13.138 23.488  -15.516 1.00 43.62  ?  439 GLY A CA     1 
ATOM   2301 C  C      . GLY A 1 328 ? -13.500 23.306  -16.974 1.00 44.78  ?  439 GLY A C      1 
ATOM   2302 O  O      . GLY A 1 328 ? -12.642 23.372  -17.853 1.00 43.33  ?  439 GLY A O      1 
ATOM   2303 N  N      . VAL A 1 329 ? -14.786 23.149  -17.236 1.00 42.90  ?  440 VAL A N      1 
ATOM   2304 C  CA     . VAL A 1 329 ? -15.289 23.039  -18.604 1.00 43.72  ?  440 VAL A CA     1 
ATOM   2305 C  C      . VAL A 1 329 ? -15.013 24.348  -19.365 1.00 48.54  ?  440 VAL A C      1 
ATOM   2306 O  O      . VAL A 1 329 ? -14.543 24.289  -20.489 1.00 48.79  ?  440 VAL A O      1 
ATOM   2307 C  CB     . VAL A 1 329 ? -16.764 22.563  -18.628 1.00 46.85  ?  440 VAL A CB     1 
ATOM   2308 C  CG1    . VAL A 1 329 ? -17.368 22.635  -20.032 1.00 47.39  ?  440 VAL A CG1    1 
ATOM   2309 C  CG2    . VAL A 1 329 ? -16.872 21.149  -18.079 1.00 46.12  ?  440 VAL A CG2    1 
ATOM   2310 N  N      . ARG A 1 330 ? -15.200 25.512  -18.712 1.00 45.65  ?  441 ARG A N      1 
ATOM   2311 C  CA     . ARG A 1 330 ? -14.922 26.840  -19.261 1.00 45.96  ?  441 ARG A CA     1 
ATOM   2312 C  C      . ARG A 1 330 ? -13.469 27.039  -19.528 1.00 50.27  ?  441 ARG A C      1 
ATOM   2313 O  O      . ARG A 1 330 ? -13.139 27.649  -20.541 1.00 50.32  ?  441 ARG A O      1 
ATOM   2314 C  CB     . ARG A 1 330 ? -15.410 27.939  -18.305 1.00 47.43  ?  441 ARG A CB     1 
ATOM   2315 C  CG     . ARG A 1 330 ? -16.922 28.083  -18.327 1.00 49.38  ?  441 ARG A CG     1 
ATOM   2316 C  CD     . ARG A 1 330 ? -17.418 29.189  -17.400 1.00 55.39  ?  441 ARG A CD     1 
ATOM   2317 N  NE     . ARG A 1 330 ? -18.854 29.379  -17.604 1.00 53.00  ?  441 ARG A NE     1 
ATOM   2318 C  CZ     . ARG A 1 330 ? -19.392 30.046  -18.622 1.00 63.20  ?  441 ARG A CZ     1 
ATOM   2319 N  NH1    . ARG A 1 330 ? -18.615 30.656  -19.511 1.00 42.60  1  441 ARG A NH1    1 
ATOM   2320 N  NH2    . ARG A 1 330 ? -20.707 30.105  -18.760 1.00 57.37  ?  441 ARG A NH2    1 
ATOM   2321 N  N      . ALA A 1 331 ? -12.585 26.566  -18.605 1.00 46.60  ?  442 ALA A N      1 
ATOM   2322 C  CA     . ALA A 1 331 ? -11.137 26.635  -18.784 1.00 47.90  ?  442 ALA A CA     1 
ATOM   2323 C  C      . ALA A 1 331 ? -10.750 25.891  -20.077 1.00 50.68  ?  442 ALA A C      1 
ATOM   2324 O  O      . ALA A 1 331 ? -10.069 26.454  -20.924 1.00 50.89  ?  442 ALA A O      1 
ATOM   2325 C  CB     . ALA A 1 331 ? -10.434 26.005  -17.586 1.00 48.96  ?  442 ALA A CB     1 
ATOM   2326 N  N      . GLY A 1 332 ? -11.269 24.677  -20.240 1.00 48.21  ?  443 GLY A N      1 
ATOM   2327 C  CA     . GLY A 1 332 ? -11.014 23.831  -21.404 1.00 47.92  ?  443 GLY A CA     1 
ATOM   2328 C  C      . GLY A 1 332 ? -11.528 24.426  -22.698 1.00 49.86  ?  443 GLY A C      1 
ATOM   2329 O  O      . GLY A 1 332 ? -10.885 24.271  -23.745 1.00 47.38  ?  443 GLY A O      1 
ATOM   2330 N  N      A MET A 1 333 ? -12.675 25.126  -22.642 0.75 46.24  ?  444 MET A N      1 
ATOM   2331 N  N      B MET A 1 333 ? -12.693 25.114  -22.634 0.25 46.51  ?  444 MET A N      1 
ATOM   2332 C  CA     A MET A 1 333 ? -13.213 25.741  -23.858 0.75 45.96  ?  444 MET A CA     1 
ATOM   2333 C  CA     B MET A 1 333 ? -13.319 25.785  -23.783 0.25 46.36  ?  444 MET A CA     1 
ATOM   2334 C  C      A MET A 1 333 ? -12.408 26.935  -24.300 0.75 52.01  ?  444 MET A C      1 
ATOM   2335 C  C      B MET A 1 333 ? -12.427 26.921  -24.282 0.25 51.26  ?  444 MET A C      1 
ATOM   2336 O  O      A MET A 1 333 ? -12.320 27.185  -25.505 0.75 53.43  ?  444 MET A O      1 
ATOM   2337 O  O      B MET A 1 333 ? -12.346 27.149  -25.491 0.25 51.47  ?  444 MET A O      1 
ATOM   2338 C  CB     A MET A 1 333 ? -14.684 26.050  -23.741 0.75 47.70  ?  444 MET A CB     1 
ATOM   2339 C  CB     B MET A 1 333 ? -14.702 26.345  -23.418 0.25 48.48  ?  444 MET A CB     1 
ATOM   2340 C  CG     A MET A 1 333 ? -15.524 24.809  -23.887 0.75 50.54  ?  444 MET A CG     1 
ATOM   2341 C  CG     B MET A 1 333 ? -15.742 25.293  -23.071 0.25 51.76  ?  444 MET A CG     1 
ATOM   2342 S  SD     A MET A 1 333 ? -17.189 25.089  -23.295 0.75 54.23  ?  444 MET A SD     1 
ATOM   2343 S  SD     B MET A 1 333 ? -16.418 24.380  -24.469 0.25 55.31  ?  444 MET A SD     1 
ATOM   2344 C  CE     A MET A 1 333 ? -17.869 26.009  -24.689 0.75 51.34  ?  444 MET A CE     1 
ATOM   2345 C  CE     B MET A 1 333 ? -17.565 25.573  -25.090 0.25 52.17  ?  444 MET A CE     1 
ATOM   2346 N  N      . GLY A 1 334 ? -11.760 27.599  -23.345 1.00 47.83  ?  445 GLY A N      1 
ATOM   2347 C  CA     . GLY A 1 334 ? -10.844 28.704  -23.607 1.00 47.38  ?  445 GLY A CA     1 
ATOM   2348 C  C      . GLY A 1 334 ? -9.544  28.198  -24.206 1.00 48.09  ?  445 GLY A C      1 
ATOM   2349 O  O      . GLY A 1 334 ? -9.029  28.789  -25.148 1.00 46.07  ?  445 GLY A O      1 
ATOM   2350 N  N      . TYR A 1 335 ? -9.023  27.063  -23.692 1.00 44.01  ?  446 TYR A N      1 
ATOM   2351 C  CA     . TYR A 1 335 ? -7.824  26.412  -24.226 1.00 42.95  ?  446 TYR A CA     1 
ATOM   2352 C  C      . TYR A 1 335 ? -7.999  25.974  -25.679 1.00 46.97  ?  446 TYR A C      1 
ATOM   2353 O  O      . TYR A 1 335 ? -7.046  26.029  -26.452 1.00 47.09  ?  446 TYR A O      1 
ATOM   2354 C  CB     . TYR A 1 335 ? -7.462  25.173  -23.392 1.00 42.78  ?  446 TYR A CB     1 
ATOM   2355 C  CG     . TYR A 1 335 ? -6.715  25.480  -22.118 1.00 42.87  ?  446 TYR A CG     1 
ATOM   2356 C  CD1    . TYR A 1 335 ? -5.481  26.120  -22.149 1.00 45.08  ?  446 TYR A CD1    1 
ATOM   2357 C  CD2    . TYR A 1 335 ? -7.208  25.069  -20.883 1.00 43.22  ?  446 TYR A CD2    1 
ATOM   2358 C  CE1    . TYR A 1 335 ? -4.797  26.427  -20.975 1.00 46.22  ?  446 TYR A CE1    1 
ATOM   2359 C  CE2    . TYR A 1 335 ? -6.527  25.359  -19.702 1.00 43.54  ?  446 TYR A CE2    1 
ATOM   2360 C  CZ     . TYR A 1 335 ? -5.335  26.060  -19.754 1.00 50.90  ?  446 TYR A CZ     1 
ATOM   2361 O  OH     . TYR A 1 335 ? -4.650  26.351  -18.605 1.00 48.10  ?  446 TYR A OH     1 
ATOM   2362 N  N      . THR A 1 336 ? -9.191  25.528  -26.036 1.00 44.79  ?  447 THR A N      1 
ATOM   2363 C  CA     . THR A 1 336 ? -9.462  24.995  -27.367 1.00 46.62  ?  447 THR A CA     1 
ATOM   2364 C  C      . THR A 1 336 ? -10.050 26.025  -28.332 1.00 53.66  ?  447 THR A C      1 
ATOM   2365 O  O      . THR A 1 336 ? -10.265 25.710  -29.511 1.00 53.80  ?  447 THR A O      1 
ATOM   2366 C  CB     . THR A 1 336 ? -10.336 23.733  -27.270 1.00 49.18  ?  447 THR A CB     1 
ATOM   2367 O  OG1    . THR A 1 336 ? -11.566 24.051  -26.625 1.00 45.77  ?  447 THR A OG1    1 
ATOM   2368 C  CG2    . THR A 1 336 ? -9.635  22.571  -26.527 1.00 45.34  ?  447 THR A CG2    1 
ATOM   2369 N  N      . GLY A 1 337 ? -10.322 27.229  -27.830 1.00 50.92  ?  448 GLY A N      1 
ATOM   2370 C  CA     . GLY A 1 337 ? -10.921 28.289  -28.630 1.00 51.17  ?  448 GLY A CA     1 
ATOM   2371 C  C      . GLY A 1 337 ? -12.335 27.970  -29.061 1.00 53.54  ?  448 GLY A C      1 
ATOM   2372 O  O      . GLY A 1 337 ? -12.743 28.329  -30.166 1.00 53.30  ?  448 GLY A O      1 
ATOM   2373 N  N      . SER A 1 338 ? -13.070 27.251  -28.201 1.00 49.91  ?  449 SER A N      1 
ATOM   2374 C  CA     . SER A 1 338 ? -14.450 26.834  -28.402 1.00 49.43  ?  449 SER A CA     1 
ATOM   2375 C  C      . SER A 1 338 ? -15.354 27.905  -27.771 1.00 56.25  ?  449 SER A C      1 
ATOM   2376 O  O      . SER A 1 338 ? -15.516 27.938  -26.543 1.00 55.95  ?  449 SER A O      1 
ATOM   2377 C  CB     . SER A 1 338 ? -14.691 25.467  -27.759 1.00 51.01  ?  449 SER A CB     1 
ATOM   2378 O  OG     . SER A 1 338 ? -13.818 24.466  -28.268 1.00 53.64  ?  449 SER A OG     1 
ATOM   2379 N  N      . HIS A 1 339 ? -15.882 28.831  -28.608 1.00 53.92  ?  450 HIS A N      1 
ATOM   2380 C  CA     . HIS A 1 339 ? -16.760 29.920  -28.148 1.00 54.38  ?  450 HIS A CA     1 
ATOM   2381 C  C      . HIS A 1 339 ? -18.096 29.355  -27.625 1.00 55.74  ?  450 HIS A C      1 
ATOM   2382 O  O      . HIS A 1 339 ? -18.733 29.944  -26.752 1.00 55.38  ?  450 HIS A O      1 
ATOM   2383 C  CB     . HIS A 1 339 ? -16.977 30.970  -29.266 1.00 56.26  ?  450 HIS A CB     1 
ATOM   2384 C  CG     . HIS A 1 339 ? -17.658 30.425  -30.487 1.00 60.63  ?  450 HIS A CG     1 
ATOM   2385 N  ND1    . HIS A 1 339 ? -16.934 29.972  -31.578 1.00 62.82  ?  450 HIS A ND1    1 
ATOM   2386 C  CD2    . HIS A 1 339 ? -18.976 30.251  -30.738 1.00 62.83  ?  450 HIS A CD2    1 
ATOM   2387 C  CE1    . HIS A 1 339 ? -17.831 29.551  -32.455 1.00 62.26  ?  450 HIS A CE1    1 
ATOM   2388 N  NE2    . HIS A 1 339 ? -19.072 29.694  -31.991 1.00 62.63  ?  450 HIS A NE2    1 
ATOM   2389 N  N      . ASP A 1 340 ? -18.487 28.186  -28.149 1.00 50.93  ?  451 ASP A N      1 
ATOM   2390 C  CA     . ASP A 1 340 ? -19.709 27.487  -27.778 1.00 49.74  ?  451 ASP A CA     1 
ATOM   2391 C  C      . ASP A 1 340 ? -19.542 25.967  -27.903 1.00 52.43  ?  451 ASP A C      1 
ATOM   2392 O  O      . ASP A 1 340 ? -18.506 25.503  -28.405 1.00 50.60  ?  451 ASP A O      1 
ATOM   2393 C  CB     . ASP A 1 340 ? -20.906 28.024  -28.590 1.00 51.57  ?  451 ASP A CB     1 
ATOM   2394 C  CG     . ASP A 1 340 ? -20.998 27.697  -30.083 1.00 63.23  ?  451 ASP A CG     1 
ATOM   2395 O  OD1    . ASP A 1 340 ? -20.109 26.980  -30.603 1.00 60.15  ?  451 ASP A OD1    1 
ATOM   2396 O  OD2    . ASP A 1 340 ? -21.975 28.144  -30.726 1.00 74.49  -1 451 ASP A OD2    1 
ATOM   2397 N  N      . LEU A 1 341 ? -20.553 25.201  -27.454 1.00 48.38  ?  452 LEU A N      1 
ATOM   2398 C  CA     . LEU A 1 341 ? -20.538 23.740  -27.470 1.00 48.33  ?  452 LEU A CA     1 
ATOM   2399 C  C      . LEU A 1 341 ? -20.559 23.123  -28.868 1.00 55.20  ?  452 LEU A C      1 
ATOM   2400 O  O      . LEU A 1 341 ? -20.016 22.026  -29.055 1.00 52.87  ?  452 LEU A O      1 
ATOM   2401 C  CB     . LEU A 1 341 ? -21.654 23.165  -26.609 1.00 47.74  ?  452 LEU A CB     1 
ATOM   2402 C  CG     . LEU A 1 341 ? -21.507 23.400  -25.106 1.00 52.00  ?  452 LEU A CG     1 
ATOM   2403 C  CD1    . LEU A 1 341 ? -22.685 22.824  -24.374 1.00 50.59  ?  452 LEU A CD1    1 
ATOM   2404 C  CD2    . LEU A 1 341 ? -20.195 22.763  -24.555 1.00 55.72  ?  452 LEU A CD2    1 
ATOM   2405 N  N      . ARG A 1 342 ? -21.203 23.811  -29.840 1.00 53.26  ?  453 ARG A N      1 
ATOM   2406 C  CA     . ARG A 1 342 ? -21.240 23.408  -31.253 1.00 53.31  ?  453 ARG A CA     1 
ATOM   2407 C  C      . ARG A 1 342 ? -19.799 23.416  -31.801 1.00 55.10  ?  453 ARG A C      1 
ATOM   2408 O  O      . ARG A 1 342 ? -19.417 22.466  -32.485 1.00 55.33  ?  453 ARG A O      1 
ATOM   2409 C  CB     . ARG A 1 342 ? -22.142 24.365  -32.058 1.00 56.90  ?  453 ARG A CB     1 
ATOM   2410 C  CG     . ARG A 1 342 ? -22.556 23.858  -33.441 1.00 68.26  ?  453 ARG A CG     1 
ATOM   2411 C  CD     . ARG A 1 342 ? -23.620 24.757  -34.069 1.00 79.85  ?  453 ARG A CD     1 
ATOM   2412 N  NE     . ARG A 1 342 ? -24.911 24.675  -33.371 1.00 85.94  ?  453 ARG A NE     1 
ATOM   2413 C  CZ     . ARG A 1 342 ? -25.400 25.616  -32.566 1.00 96.35  ?  453 ARG A CZ     1 
ATOM   2414 N  NH1    . ARG A 1 342 ? -24.722 26.736  -32.353 1.00 84.83  1  453 ARG A NH1    1 
ATOM   2415 N  NH2    . ARG A 1 342 ? -26.570 25.443  -31.968 1.00 81.93  ?  453 ARG A NH2    1 
ATOM   2416 N  N      A GLU A 1 343 ? -19.000 24.462  -31.478 0.54 52.09  ?  454 GLU A N      1 
ATOM   2417 N  N      B GLU A 1 343 ? -19.005 24.453  -31.463 0.46 51.48  ?  454 GLU A N      1 
ATOM   2418 C  CA     A GLU A 1 343 ? -17.600 24.544  -31.909 0.54 52.08  ?  454 GLU A CA     1 
ATOM   2419 C  CA     B GLU A 1 343 ? -17.604 24.570  -31.869 0.46 51.16  ?  454 GLU A CA     1 
ATOM   2420 C  C      A GLU A 1 343 ? -16.728 23.468  -31.237 0.54 55.55  ?  454 GLU A C      1 
ATOM   2421 C  C      B GLU A 1 343 ? -16.741 23.467  -31.233 0.46 55.12  ?  454 GLU A C      1 
ATOM   2422 O  O      A GLU A 1 343 ? -15.772 23.002  -31.854 0.54 54.22  ?  454 GLU A O      1 
ATOM   2423 O  O      B GLU A 1 343 ? -15.804 22.989  -31.871 0.46 53.86  ?  454 GLU A O      1 
ATOM   2424 C  CB     A GLU A 1 343 ? -17.002 25.939  -31.704 0.54 53.81  ?  454 GLU A CB     1 
ATOM   2425 C  CB     B GLU A 1 343 ? -17.043 25.957  -31.525 0.46 52.60  ?  454 GLU A CB     1 
ATOM   2426 C  CG     A GLU A 1 343 ? -16.141 26.367  -32.879 0.54 67.77  ?  454 GLU A CG     1 
ATOM   2427 C  CG     B GLU A 1 343 ? -15.836 26.364  -32.357 0.46 62.24  ?  454 GLU A CG     1 
ATOM   2428 C  CD     A GLU A 1 343 ? -14.819 27.020  -32.525 0.54 95.18  ?  454 GLU A CD     1 
ATOM   2429 C  CD     B GLU A 1 343 ? -16.044 26.556  -33.851 0.46 76.60  ?  454 GLU A CD     1 
ATOM   2430 O  OE1    A GLU A 1 343 ? -14.828 28.219  -32.165 0.54 94.80  ?  454 GLU A OE1    1 
ATOM   2431 O  OE1    B GLU A 1 343 ? -17.201 26.775  -34.278 0.46 65.98  ?  454 GLU A OE1    1 
ATOM   2432 O  OE2    A GLU A 1 343 ? -13.768 26.350  -32.655 0.54 87.60  -1 454 GLU A OE2    1 
ATOM   2433 O  OE2    B GLU A 1 343 ? -15.038 26.511  -34.595 0.46 67.04  -1 454 GLU A OE2    1 
ATOM   2434 N  N      . LEU A 1 344 ? -17.077 23.061  -29.991 1.00 51.75  ?  455 LEU A N      1 
ATOM   2435 C  CA     . LEU A 1 344 ? -16.368 22.010  -29.244 1.00 51.12  ?  455 LEU A CA     1 
ATOM   2436 C  C      . LEU A 1 344 ? -16.617 20.632  -29.908 1.00 52.75  ?  455 LEU A C      1 
ATOM   2437 O  O      . LEU A 1 344 ? -15.673 20.002  -30.369 1.00 49.90  ?  455 LEU A O      1 
ATOM   2438 C  CB     . LEU A 1 344 ? -16.825 21.995  -27.772 1.00 51.21  ?  455 LEU A CB     1 
ATOM   2439 C  CG     . LEU A 1 344 ? -16.038 21.080  -26.820 1.00 54.68  ?  455 LEU A CG     1 
ATOM   2440 C  CD1    . LEU A 1 344 ? -14.689 21.671  -26.465 1.00 54.49  ?  455 LEU A CD1    1 
ATOM   2441 C  CD2    . LEU A 1 344 ? -16.821 20.815  -25.579 1.00 57.41  ?  455 LEU A CD2    1 
ATOM   2442 N  N      . ARG A 1 345 ? -17.882 20.215  -29.992 1.00 48.37  ?  456 ARG A N      1 
ATOM   2443 C  CA     . ARG A 1 345 ? -18.335 18.963  -30.585 1.00 49.19  ?  456 ARG A CA     1 
ATOM   2444 C  C      . ARG A 1 345 ? -17.870 18.746  -32.020 1.00 54.95  ?  456 ARG A C      1 
ATOM   2445 O  O      . ARG A 1 345 ? -17.616 17.605  -32.393 1.00 55.97  ?  456 ARG A O      1 
ATOM   2446 C  CB     . ARG A 1 345 ? -19.863 18.916  -30.609 1.00 50.40  ?  456 ARG A CB     1 
ATOM   2447 C  CG     . ARG A 1 345 ? -20.560 18.625  -29.293 1.00 54.40  ?  456 ARG A CG     1 
ATOM   2448 C  CD     . ARG A 1 345 ? -22.013 18.237  -29.544 1.00 62.25  ?  456 ARG A CD     1 
ATOM   2449 N  NE     . ARG A 1 345 ? -22.722 19.167  -30.441 1.00 61.60  ?  456 ARG A NE     1 
ATOM   2450 C  CZ     . ARG A 1 345 ? -23.307 20.295  -30.050 1.00 67.86  ?  456 ARG A CZ     1 
ATOM   2451 N  NH1    . ARG A 1 345 ? -23.936 21.066  -30.932 1.00 54.23  1  456 ARG A NH1    1 
ATOM   2452 N  NH2    . ARG A 1 345 ? -23.275 20.660  -28.776 1.00 46.96  ?  456 ARG A NH2    1 
ATOM   2453 N  N      . GLU A 1 346 ? -17.824 19.812  -32.834 1.00 49.90  ?  457 GLU A N      1 
ATOM   2454 C  CA     . GLU A 1 346 ? -17.504 19.716  -34.252 1.00 49.04  ?  457 GLU A CA     1 
ATOM   2455 C  C      . GLU A 1 346 ? -16.058 19.911  -34.583 1.00 52.39  ?  457 GLU A C      1 
ATOM   2456 O  O      . GLU A 1 346 ? -15.586 19.329  -35.560 1.00 53.12  ?  457 GLU A O      1 
ATOM   2457 C  CB     . GLU A 1 346 ? -18.368 20.718  -35.071 1.00 50.40  ?  457 GLU A CB     1 
ATOM   2458 C  CG     . GLU A 1 346 ? -19.831 20.310  -35.196 1.00 56.24  ?  457 GLU A CG     1 
ATOM   2459 C  CD     . GLU A 1 346 ? -20.129 19.092  -36.051 1.00 70.67  ?  457 GLU A CD     1 
ATOM   2460 O  OE1    . GLU A 1 346 ? -19.465 18.917  -37.098 1.00 74.92  ?  457 GLU A OE1    1 
ATOM   2461 O  OE2    . GLU A 1 346 ? -21.059 18.333  -35.696 1.00 61.36  -1 457 GLU A OE2    1 
ATOM   2462 N  N      . GLU A 1 347 ? -15.350 20.772  -33.846 1.00 47.70  ?  458 GLU A N      1 
ATOM   2463 C  CA     . GLU A 1 347 ? -13.978 21.068  -34.239 1.00 48.31  ?  458 GLU A CA     1 
ATOM   2464 C  C      . GLU A 1 347 ? -12.885 20.619  -33.286 1.00 50.58  ?  458 GLU A C      1 
ATOM   2465 O  O      . GLU A 1 347 ? -11.757 20.479  -33.754 1.00 50.43  ?  458 GLU A O      1 
ATOM   2466 C  CB     . GLU A 1 347 ? -13.805 22.578  -34.515 1.00 50.55  ?  458 GLU A CB     1 
ATOM   2467 C  CG     . GLU A 1 347 ? -14.658 23.106  -35.666 1.00 64.33  ?  458 GLU A CG     1 
ATOM   2468 C  CD     . GLU A 1 347 ? -14.300 22.550  -37.036 1.00 88.71  ?  458 GLU A CD     1 
ATOM   2469 O  OE1    . GLU A 1 347 ? -15.124 21.798  -37.604 1.00 84.19  ?  458 GLU A OE1    1 
ATOM   2470 O  OE2    . GLU A 1 347 ? -13.191 22.854  -37.534 1.00 84.84  -1 458 GLU A OE2    1 
ATOM   2471 N  N      . ALA A 1 348 ? -13.165 20.487  -31.959 1.00 44.32  ?  459 ALA A N      1 
ATOM   2472 C  CA     . ALA A 1 348 ? -12.094 20.176  -31.006 1.00 43.35  ?  459 ALA A CA     1 
ATOM   2473 C  C      . ALA A 1 348 ? -11.395 18.858  -31.319 1.00 42.77  ?  459 ALA A C      1 
ATOM   2474 O  O      . ALA A 1 348 ? -12.043 17.887  -31.697 1.00 43.31  ?  459 ALA A O      1 
ATOM   2475 C  CB     . ALA A 1 348 ? -12.590 20.230  -29.552 1.00 44.33  ?  459 ALA A CB     1 
ATOM   2476 N  N      . GLN A 1 349 ? -10.067 18.881  -31.290 1.00 39.42  ?  460 GLN A N      1 
ATOM   2477 C  CA     . GLN A 1 349 ? -9.225  17.711  -31.616 1.00 37.82  ?  460 GLN A CA     1 
ATOM   2478 C  C      . GLN A 1 349 ? -8.586  17.183  -30.351 1.00 40.79  ?  460 GLN A C      1 
ATOM   2479 O  O      . GLN A 1 349 ? -8.225  17.959  -29.451 1.00 39.40  ?  460 GLN A O      1 
ATOM   2480 C  CB     . GLN A 1 349 ? -8.118  18.088  -32.632 1.00 38.27  ?  460 GLN A CB     1 
ATOM   2481 C  CG     . GLN A 1 349 ? -8.621  18.691  -33.963 1.00 41.88  ?  460 GLN A CG     1 
ATOM   2482 C  CD     . GLN A 1 349 ? -9.372  17.682  -34.797 1.00 49.53  ?  460 GLN A CD     1 
ATOM   2483 O  OE1    . GLN A 1 349 ? -8.793  16.762  -35.357 1.00 45.20  ?  460 GLN A OE1    1 
ATOM   2484 N  NE2    . GLN A 1 349 ? -10.669 17.841  -34.929 1.00 45.51  ?  460 GLN A NE2    1 
ATOM   2485 N  N      . PHE A 1 350 ? -8.429  15.851  -30.307 1.00 37.49  ?  461 PHE A N      1 
ATOM   2486 C  CA     . PHE A 1 350 ? -7.816  15.121  -29.205 1.00 36.38  ?  461 PHE A CA     1 
ATOM   2487 C  C      . PHE A 1 350 ? -6.498  14.499  -29.625 1.00 41.08  ?  461 PHE A C      1 
ATOM   2488 O  O      . PHE A 1 350 ? -6.267  14.253  -30.808 1.00 41.22  ?  461 PHE A O      1 
ATOM   2489 C  CB     . PHE A 1 350 ? -8.713  13.945  -28.816 1.00 37.85  ?  461 PHE A CB     1 
ATOM   2490 C  CG     . PHE A 1 350 ? -10.036 14.233  -28.172 1.00 38.77  ?  461 PHE A CG     1 
ATOM   2491 C  CD1    . PHE A 1 350 ? -10.189 14.129  -26.796 1.00 40.01  ?  461 PHE A CD1    1 
ATOM   2492 C  CD2    . PHE A 1 350 ? -11.167 14.482  -28.949 1.00 38.66  ?  461 PHE A CD2    1 
ATOM   2493 C  CE1    . PHE A 1 350 ? -11.430 14.316  -26.203 1.00 41.54  ?  461 PHE A CE1    1 
ATOM   2494 C  CE2    . PHE A 1 350 ? -12.414 14.637  -28.356 1.00 41.82  ?  461 PHE A CE2    1 
ATOM   2495 C  CZ     . PHE A 1 350 ? -12.543 14.549  -26.986 1.00 41.05  ?  461 PHE A CZ     1 
ATOM   2496 N  N      . THR A 1 351 ? -5.666  14.173  -28.641 1.00 37.52  ?  462 THR A N      1 
ATOM   2497 C  CA     . THR A 1 351 ? -4.485  13.343  -28.865 1.00 36.81  ?  462 THR A CA     1 
ATOM   2498 C  C      . THR A 1 351 ? -4.664  12.101  -28.001 1.00 38.31  ?  462 THR A C      1 
ATOM   2499 O  O      . THR A 1 351 ? -5.194  12.176  -26.906 1.00 35.48  ?  462 THR A O      1 
ATOM   2500 C  CB     . THR A 1 351 ? -3.153  14.027  -28.603 1.00 41.12  ?  462 THR A CB     1 
ATOM   2501 O  OG1    . THR A 1 351 ? -2.117  13.055  -28.829 1.00 35.46  ?  462 THR A OG1    1 
ATOM   2502 C  CG2    . THR A 1 351 ? -3.039  14.606  -27.187 1.00 38.61  ?  462 THR A CG2    1 
ATOM   2503 N  N      . ARG A 1 352 ? -4.258  10.966  -28.528 1.00 35.94  ?  463 ARG A N      1 
ATOM   2504 C  CA     . ARG A 1 352 ? -4.241  9.721   -27.787 1.00 35.25  ?  463 ARG A CA     1 
ATOM   2505 C  C      . ARG A 1 352 ? -2.896  9.749   -27.088 1.00 40.44  ?  463 ARG A C      1 
ATOM   2506 O  O      . ARG A 1 352 ? -2.004  10.513  -27.503 1.00 37.99  ?  463 ARG A O      1 
ATOM   2507 C  CB     . ARG A 1 352 ? -4.302  8.527   -28.754 1.00 34.14  ?  463 ARG A CB     1 
ATOM   2508 C  CG     . ARG A 1 352 ? -5.692  8.325   -29.310 1.00 37.19  ?  463 ARG A CG     1 
ATOM   2509 C  CD     . ARG A 1 352 ? -5.709  7.207   -30.329 1.00 44.77  ?  463 ARG A CD     1 
ATOM   2510 N  NE     . ARG A 1 352 ? -5.097  7.640   -31.582 1.00 43.99  ?  463 ARG A NE     1 
ATOM   2511 C  CZ     . ARG A 1 352 ? -4.229  6.930   -32.289 1.00 64.91  ?  463 ARG A CZ     1 
ATOM   2512 N  NH1    . ARG A 1 352 ? -3.726  7.419   -33.414 1.00 50.20  1  463 ARG A NH1    1 
ATOM   2513 N  NH2    . ARG A 1 352 ? -3.839  5.734   -31.868 1.00 60.15  ?  463 ARG A NH2    1 
ATOM   2514 N  N      A MET A 1 353 ? -2.745  8.923   -26.038 0.75 39.37  ?  464 MET A N      1 
ATOM   2515 N  N      B MET A 1 353 ? -2.758  8.979   -25.987 0.25 38.79  ?  464 MET A N      1 
ATOM   2516 C  CA     A MET A 1 353 ? -1.519  8.795   -25.242 0.75 41.26  ?  464 MET A CA     1 
ATOM   2517 C  CA     B MET A 1 353 ? -1.529  8.847   -25.188 0.25 39.75  ?  464 MET A CA     1 
ATOM   2518 C  C      A MET A 1 353 ? -1.560  7.495   -24.433 0.75 49.31  ?  464 MET A C      1 
ATOM   2519 C  C      B MET A 1 353 ? -1.575  7.590   -24.307 0.25 47.93  ?  464 MET A C      1 
ATOM   2520 O  O      A MET A 1 353 ? -2.638  6.930   -24.218 0.75 49.49  ?  464 MET A O      1 
ATOM   2521 O  O      B MET A 1 353 ? -2.666  7.116   -23.983 0.25 47.38  ?  464 MET A O      1 
ATOM   2522 C  CB     A MET A 1 353 ? -1.379  9.979   -24.279 0.75 43.94  ?  464 MET A CB     1 
ATOM   2523 C  CB     B MET A 1 353 ? -1.209  10.126  -24.378 0.25 41.82  ?  464 MET A CB     1 
ATOM   2524 C  CG     A MET A 1 353 ? -2.326  9.894   -23.098 0.75 48.13  ?  464 MET A CG     1 
ATOM   2525 C  CG     B MET A 1 353 ? -1.832  10.192  -22.995 0.25 45.18  ?  464 MET A CG     1 
ATOM   2526 S  SD     A MET A 1 353 ? -2.410  11.436  -22.231 0.75 53.03  ?  464 MET A SD     1 
ATOM   2527 S  SD     B MET A 1 353 ? -3.435  11.007  -22.987 0.25 48.97  ?  464 MET A SD     1 
ATOM   2528 C  CE     A MET A 1 353 ? -3.545  11.012  -20.959 0.75 50.04  ?  464 MET A CE     1 
ATOM   2529 C  CE     B MET A 1 353 ? -3.744  11.040  -21.248 0.25 45.81  ?  464 MET A CE     1 
ATOM   2530 N  N      . GLY A 1 354 ? -0.402  7.072   -23.933 1.00 48.04  ?  465 GLY A N      1 
ATOM   2531 C  CA     . GLY A 1 354 ? -0.292  5.864   -23.117 1.00 47.82  ?  465 GLY A CA     1 
ATOM   2532 C  C      . GLY A 1 354 ? -0.555  6.068   -21.633 1.00 56.81  ?  465 GLY A C      1 
ATOM   2533 O  O      . GLY A 1 354 ? -0.873  7.185   -21.198 1.00 58.05  ?  465 GLY A O      1 
ATOM   2534 N  N      . PRO A 1 355 ? -0.395  4.994   -20.811 1.00 54.60  ?  466 PRO A N      1 
ATOM   2535 C  CA     . PRO A 1 355 ? -0.574  5.138   -19.357 1.00 59.38  ?  466 PRO A CA     1 
ATOM   2536 C  C      . PRO A 1 355 ? 0.593   5.909   -18.736 1.00 98.36  ?  466 PRO A C      1 
ATOM   2537 O  O      . PRO A 1 355 ? 0.447   7.063   -18.338 1.00 64.55  ?  466 PRO A O      1 
ATOM   2538 C  CB     . PRO A 1 355 ? -0.582  3.681   -18.858 1.00 59.99  ?  466 PRO A CB     1 
ATOM   2539 C  CG     . PRO A 1 355 ? -0.720  2.823   -20.090 1.00 62.31  ?  466 PRO A CG     1 
ATOM   2540 C  CD     . PRO A 1 355 ? -0.028  3.608   -21.153 1.00 57.43  ?  466 PRO A CD     1 
HETATM 2541 P  P      . IMP B 2 .   ? -21.205 7.594   -12.889 1.00 43.05  ?  801 IMP A P      1 
HETATM 2542 O  O1P    . IMP B 2 .   ? -19.828 7.213   -13.375 1.00 46.43  ?  801 IMP A O1P    1 
HETATM 2543 O  O2P    . IMP B 2 .   ? -21.522 9.046   -13.092 1.00 43.68  ?  801 IMP A O2P    1 
HETATM 2544 O  O3P    . IMP B 2 .   ? -21.388 7.161   -11.448 1.00 46.24  ?  801 IMP A O3P    1 
HETATM 2545 O  "O5'"  . IMP B 2 .   ? -22.254 6.735   -13.714 1.00 42.70  ?  801 IMP A "O5'"  1 
HETATM 2546 C  "C5'"  . IMP B 2 .   ? -23.674 6.787   -13.491 1.00 44.43  ?  801 IMP A "C5'"  1 
HETATM 2547 C  "C4'"  . IMP B 2 .   ? -24.392 5.987   -14.551 1.00 43.53  ?  801 IMP A "C4'"  1 
HETATM 2548 O  "O4'"  . IMP B 2 .   ? -24.176 4.575   -14.355 1.00 42.90  ?  801 IMP A "O4'"  1 
HETATM 2549 C  "C3'"  . IMP B 2 .   ? -25.908 6.106   -14.550 1.00 45.13  ?  801 IMP A "C3'"  1 
HETATM 2550 O  "O3'"  . IMP B 2 .   ? -26.333 7.345   -15.102 1.00 45.75  ?  801 IMP A "O3'"  1 
HETATM 2551 C  "C2'"  . IMP B 2 .   ? -26.331 4.863   -15.342 1.00 46.54  ?  801 IMP A "C2'"  1 
HETATM 2552 O  "O2'"  . IMP B 2 .   ? -26.333 4.995   -16.755 1.00 50.00  ?  801 IMP A "O2'"  1 
HETATM 2553 C  "C1'"  . IMP B 2 .   ? -25.243 3.851   -14.951 1.00 44.20  ?  801 IMP A "C1'"  1 
HETATM 2554 N  N9     . IMP B 2 .   ? -25.707 2.844   -13.989 1.00 47.49  ?  801 IMP A N9     1 
HETATM 2555 C  C8     . IMP B 2 .   ? -26.580 3.032   -12.947 1.00 46.56  ?  801 IMP A C8     1 
HETATM 2556 N  N7     . IMP B 2 .   ? -26.731 1.970   -12.199 1.00 49.74  ?  801 IMP A N7     1 
HETATM 2557 C  C5     . IMP B 2 .   ? -25.926 1.014   -12.795 1.00 48.12  ?  801 IMP A C5     1 
HETATM 2558 C  C6     . IMP B 2 .   ? -25.702 -0.371  -12.466 1.00 49.54  ?  801 IMP A C6     1 
HETATM 2559 O  O6     . IMP B 2 .   ? -26.006 -0.947  -11.424 1.00 50.34  ?  801 IMP A O6     1 
HETATM 2560 N  N1     . IMP B 2 .   ? -24.923 -1.002  -13.420 1.00 49.87  ?  801 IMP A N1     1 
HETATM 2561 C  C2     . IMP B 2 .   ? -24.356 -0.382  -14.478 1.00 49.31  ?  801 IMP A C2     1 
HETATM 2562 N  N3     . IMP B 2 .   ? -24.465 0.903   -14.759 1.00 47.24  ?  801 IMP A N3     1 
HETATM 2563 C  C4     . IMP B 2 .   ? -25.293 1.543   -13.906 1.00 46.68  ?  801 IMP A C4     1 
HETATM 2564 H  HOP2   . IMP B 2 .   ? -22.250 9.393   -13.671 1.00 43.83  ?  801 IMP A HOP2   1 
HETATM 2565 H  HOP3   . IMP B 2 .   ? -21.601 6.197   -11.340 1.00 45.39  ?  801 IMP A HOP3   1 
HETATM 2566 H  "H5'1" . IMP B 2 .   ? -24.004 7.821   -13.570 1.00 44.79  ?  801 IMP A "H5'1" 1 
HETATM 2567 H  "H5'2" . IMP B 2 .   ? -23.846 6.426   -12.478 1.00 45.24  ?  801 IMP A "H5'2" 1 
HETATM 2568 H  "H4'"  . IMP B 2 .   ? -23.997 6.259   -15.529 1.00 42.44  ?  801 IMP A "H4'"  1 
HETATM 2569 H  "H3'"  . IMP B 2 .   ? -26.326 6.090   -13.547 1.00 44.88  ?  801 IMP A "H3'"  1 
HETATM 2570 H  "HO3'" . IMP B 2 .   ? -27.066 7.259   -15.765 1.00 45.79  ?  801 IMP A "HO3'" 1 
HETATM 2571 H  "H2'"  . IMP B 2 .   ? -27.328 4.545   -15.045 1.00 46.88  ?  801 IMP A "H2'"  1 
HETATM 2572 H  "HO2'" . IMP B 2 .   ? -25.449 5.382   -16.986 1.00 49.61  ?  801 IMP A "HO2'" 1 
HETATM 2573 H  "H1'"  . IMP B 2 .   ? -24.827 3.323   -15.808 1.00 44.12  ?  801 IMP A "H1'"  1 
HETATM 2574 H  H8     . IMP B 2 .   ? -27.105 3.971   -12.783 1.00 46.08  ?  801 IMP A H8     1 
HETATM 2575 H  HN1    . IMP B 2 .   ? -24.828 -2.010  -13.390 1.00 49.49  ?  801 IMP A HN1    1 
HETATM 2576 H  H2     . IMP B 2 .   ? -23.833 -0.996  -15.208 1.00 49.45  ?  801 IMP A H2     1 
HETATM 2577 C  C4     . VOA C 3 .   ? -29.577 -5.284  -15.863 1.00 56.87  ?  802 VOA A C4     1 
HETATM 2578 C  C7     . VOA C 3 .   ? -29.441 -6.633  -17.969 1.00 54.03  ?  802 VOA A C7     1 
HETATM 2579 C  C8     . VOA C 3 .   ? -28.593 -7.483  -18.687 1.00 51.27  ?  802 VOA A C8     1 
HETATM 2580 C  C9     . VOA C 3 .   ? -28.925 -7.819  -19.990 1.00 49.88  ?  802 VOA A C9     1 
HETATM 2581 C  C10    . VOA C 3 .   ? -30.123 -7.343  -20.517 1.00 52.48  ?  802 VOA A C10    1 
HETATM 2582 C  C12    . VOA C 3 .   ? -30.615 -6.168  -18.595 1.00 51.68  ?  802 VOA A C12    1 
HETATM 2583 C  C1     . VOA C 3 .   ? -29.168 -6.134  -13.595 1.00 53.11  ?  802 VOA A C1     1 
HETATM 2584 C  C15    . VOA C 3 .   ? -28.929 -2.429  -14.514 1.00 47.56  ?  802 VOA A C15    1 
HETATM 2585 C  C16    . VOA C 3 .   ? -29.704 -1.361  -14.043 1.00 49.11  ?  802 VOA A C16    1 
HETATM 2586 C  C17    . VOA C 3 .   ? -29.510 -0.084  -14.489 1.00 51.51  ?  802 VOA A C17    1 
HETATM 2587 C  C18    . VOA C 3 .   ? -28.511 0.188   -15.457 1.00 51.32  ?  802 VOA A C18    1 
HETATM 2588 C  C19    . VOA C 3 .   ? -27.688 -0.874  -15.953 1.00 49.69  ?  802 VOA A C19    1 
HETATM 2589 C  C2     . VOA C 3 .   ? -28.863 -4.994  -14.567 1.00 52.25  ?  802 VOA A C2     1 
HETATM 2590 C  C20    . VOA C 3 .   ? -27.910 -2.186  -15.440 1.00 48.34  ?  802 VOA A C20    1 
HETATM 2591 C  C21    . VOA C 3 .   ? -26.690 -0.546  -16.935 1.00 48.87  ?  802 VOA A C21    1 
HETATM 2592 C  C22    . VOA C 3 .   ? -26.582 0.762   -17.334 1.00 48.89  ?  802 VOA A C22    1 
HETATM 2593 C  C23    . VOA C 3 .   ? -27.443 1.743   -16.808 1.00 51.05  ?  802 VOA A C23    1 
HETATM 2594 C  C25    . VOA C 3 .   ? -25.553 1.209   -18.356 1.00 48.84  ?  802 VOA A C25    1 
HETATM 2595 C  C27    . VOA C 3 .   ? -25.055 -1.103  -18.804 1.00 45.97  ?  802 VOA A C27    1 
HETATM 2596 C  C28    . VOA C 3 .   ? -25.757 -1.603  -17.518 1.00 49.08  ?  802 VOA A C28    1 
HETATM 2597 N  N11    . VOA C 3 .   ? -30.910 -6.515  -19.838 1.00 49.15  ?  802 VOA A N11    1 
HETATM 2598 N  N14    . VOA C 3 .   ? -29.225 -3.694  -13.975 1.00 47.79  ?  802 VOA A N14    1 
HETATM 2599 N  N24    . VOA C 3 .   ? -28.339 1.445   -15.897 1.00 51.11  ?  802 VOA A N24    1 
HETATM 2600 N  N6     . VOA C 3 .   ? -29.009 -6.217  -16.687 1.00 57.08  ?  802 VOA A N6     1 
HETATM 2601 O  O26    . VOA C 3 .   ? -24.536 0.222   -18.557 1.00 47.02  ?  802 VOA A O26    1 
HETATM 2602 O  O5     . VOA C 3 .   ? -30.642 -4.735  -16.112 1.00 57.73  ?  802 VOA A O5     1 
HETATM 2603 CL CL13   . VOA C 3 .   ? -30.551 -7.794  -22.134 1.00 55.53  ?  802 VOA A CL13   1 
HETATM 2604 H  H3     . VOA C 3 .   ? -27.799 -4.989  -14.765 1.00 52.67  ?  802 VOA A H3     1 
HETATM 2605 O  O      . HOH D 4 .   ? -8.394  21.328  -30.186 1.00 41.52  ?  901 HOH A O      1 
HETATM 2606 O  O      . HOH D 4 .   ? -27.655 -1.471  -25.900 1.00 47.76  ?  902 HOH A O      1 
HETATM 2607 O  O      . HOH D 4 .   ? -14.494 4.500   -33.418 1.00 45.49  ?  903 HOH A O      1 
HETATM 2608 O  O      . HOH D 4 .   ? -21.599 11.942  -39.136 1.00 56.96  ?  904 HOH A O      1 
HETATM 2609 O  O      . HOH D 4 .   ? -17.809 -8.754  -39.472 1.00 53.11  ?  905 HOH A O      1 
HETATM 2610 O  O      . HOH D 4 .   ? -9.771  11.351  -18.112 1.00 43.09  ?  906 HOH A O      1 
HETATM 2611 O  O      . HOH D 4 .   ? -17.642 8.453   -12.466 1.00 41.23  ?  907 HOH A O      1 
HETATM 2612 O  O      . HOH D 4 .   ? -22.994 26.658  -26.334 1.00 57.91  ?  908 HOH A O      1 
HETATM 2613 O  O      . HOH D 4 .   ? -28.944 4.712   -6.884  1.00 52.89  ?  909 HOH A O      1 
HETATM 2614 O  O      . HOH D 4 .   ? -3.838  5.398   -22.255 1.00 61.11  ?  910 HOH A O      1 
HETATM 2615 O  O      . HOH D 4 .   ? -6.327  14.457  -33.486 1.00 37.59  ?  911 HOH A O      1 
HETATM 2616 O  O      . HOH D 4 .   ? -20.380 11.347  -12.304 1.00 40.59  ?  912 HOH A O      1 
HETATM 2617 O  O      . HOH D 4 .   ? -20.150 9.740   -20.357 1.00 41.48  ?  913 HOH A O      1 
HETATM 2618 O  O      . HOH D 4 .   ? -19.397 1.035   -30.731 1.00 46.89  ?  914 HOH A O      1 
HETATM 2619 O  O      . HOH D 4 .   ? -13.414 2.109   -32.742 1.00 45.88  ?  915 HOH A O      1 
HETATM 2620 O  O      . HOH D 4 .   ? -16.970 18.955  -38.108 1.00 69.00  ?  916 HOH A O      1 
HETATM 2621 O  O      . HOH D 4 .   ? -3.633  6.976   -19.974 1.00 67.01  ?  917 HOH A O      1 
HETATM 2622 O  O      . HOH D 4 .   ? -9.143  1.863   -23.923 1.00 50.62  ?  918 HOH A O      1 
HETATM 2623 O  O      . HOH D 4 .   ? -4.475  6.356   -26.105 1.00 49.87  ?  919 HOH A O      1 
HETATM 2624 O  O      . HOH D 4 .   ? -20.957 10.144  -15.497 1.00 44.66  ?  920 HOH A O      1 
HETATM 2625 O  O      . HOH D 4 .   ? -17.804 1.018   -20.904 1.00 45.58  ?  921 HOH A O      1 
HETATM 2626 O  O      . HOH D 4 .   ? -49.512 0.575   -16.934 1.00 68.08  ?  922 HOH A O      1 
HETATM 2627 O  O      . HOH D 4 .   ? -33.199 14.696  -4.618  1.00 57.47  ?  923 HOH A O      1 
HETATM 2628 O  O      . HOH D 4 .   ? -23.695 4.406   -18.290 1.00 43.77  ?  924 HOH A O      1 
HETATM 2629 O  O      . HOH D 4 .   ? -34.611 19.404  -13.509 1.00 60.52  ?  925 HOH A O      1 
HETATM 2630 O  O      . HOH D 4 .   ? -32.505 16.117  -30.524 1.00 55.53  ?  926 HOH A O      1 
HETATM 2631 O  O      . HOH D 4 .   ? -20.301 12.765  -4.704  1.00 51.28  ?  927 HOH A O      1 
HETATM 2632 O  O      . HOH D 4 .   ? -13.245 23.751  -30.849 1.00 57.62  ?  928 HOH A O      1 
HETATM 2633 O  O      . HOH D 4 .   ? -10.019 -10.892 -35.413 1.00 45.87  ?  929 HOH A O      1 
HETATM 2634 O  O      . HOH D 4 .   ? -20.262 2.864   -23.213 1.00 39.56  ?  930 HOH A O      1 
HETATM 2635 O  O      . HOH D 4 .   ? -2.385  25.707  -29.943 1.00 43.98  ?  931 HOH A O      1 
HETATM 2636 O  O      . HOH D 4 .   ? -16.389 8.833   -10.070 1.00 56.23  ?  932 HOH A O      1 
HETATM 2637 O  O      . HOH D 4 .   ? -26.383 -5.389  -33.567 1.00 62.66  ?  933 HOH A O      1 
HETATM 2638 O  O      . HOH D 4 .   ? -29.920 29.205  -15.692 1.00 60.76  ?  934 HOH A O      1 
HETATM 2639 O  O      . HOH D 4 .   ? -36.384 10.353  -0.279  1.00 72.28  ?  935 HOH A O      1 
HETATM 2640 O  O      . HOH D 4 .   ? -15.050 3.915   -20.212 1.00 39.40  ?  936 HOH A O      1 
HETATM 2641 O  O      . HOH D 4 .   ? -22.067 19.726  -26.445 1.00 43.19  ?  937 HOH A O      1 
HETATM 2642 O  O      . HOH D 4 .   ? -25.144 -5.522  -5.258  1.00 60.46  ?  938 HOH A O      1 
HETATM 2643 O  O      . HOH D 4 .   ? -14.183 6.418   -16.091 1.00 48.54  ?  939 HOH A O      1 
HETATM 2644 O  O      . HOH D 4 .   ? -18.751 13.870  -41.078 1.00 67.68  ?  940 HOH A O      1 
HETATM 2645 O  O      . HOH D 4 .   ? -48.261 14.997  -26.731 1.00 64.57  ?  941 HOH A O      1 
HETATM 2646 O  O      . HOH D 4 .   ? -25.634 -0.687  -27.837 1.00 43.94  ?  942 HOH A O      1 
HETATM 2647 O  O      . HOH D 4 .   ? -22.139 -3.605  -3.132  1.00 79.66  ?  943 HOH A O      1 
HETATM 2648 O  O      . HOH D 4 .   ? -33.536 22.152  -4.308  1.00 50.91  ?  944 HOH A O      1 
HETATM 2649 O  O      . HOH D 4 .   ? -22.165 15.302  -32.130 1.00 57.34  ?  945 HOH A O      1 
HETATM 2650 O  O      . HOH D 4 .   ? -20.852 1.569   -33.818 1.00 53.28  ?  946 HOH A O      1 
HETATM 2651 O  O      . HOH D 4 .   ? -27.466 24.020  -29.138 1.00 63.87  ?  947 HOH A O      1 
HETATM 2652 O  O      . HOH D 4 .   ? -18.009 28.235  -13.178 1.00 47.69  ?  948 HOH A O      1 
HETATM 2653 O  O      . HOH D 4 .   ? -10.135 23.294  -31.180 1.00 50.53  ?  949 HOH A O      1 
HETATM 2654 O  O      . HOH D 4 .   ? -15.490 4.738   -17.756 1.00 50.98  ?  950 HOH A O      1 
HETATM 2655 O  O      . HOH D 4 .   ? -11.002 6.504   -18.306 1.00 42.25  ?  951 HOH A O      1 
HETATM 2656 O  O      . HOH D 4 .   ? -41.585 29.339  -7.807  1.00 76.60  ?  952 HOH A O      1 
HETATM 2657 O  O      . HOH D 4 .   ? -11.515 0.221   -34.422 1.00 40.40  ?  953 HOH A O      1 
HETATM 2658 O  O      . HOH D 4 .   ? -18.218 -1.851  -15.424 1.00 72.83  ?  954 HOH A O      1 
HETATM 2659 O  O      . HOH D 4 .   ? -23.390 26.126  -28.988 1.00 56.69  ?  955 HOH A O      1 
HETATM 2660 O  O      . HOH D 4 .   ? -22.507 1.967   -16.806 1.00 53.09  ?  956 HOH A O      1 
HETATM 2661 O  O      . HOH D 4 .   ? -13.398 18.009  -11.098 1.00 46.98  ?  957 HOH A O      1 
HETATM 2662 O  O      . HOH D 4 .   ? -57.315 9.186   -17.107 1.00 77.55  ?  958 HOH A O      1 
HETATM 2663 O  O      . HOH D 4 .   ? -31.278 23.451  -3.493  1.00 74.15  ?  959 HOH A O      1 
HETATM 2664 O  O      . HOH D 4 .   ? -27.203 13.416  -43.046 1.00 74.97  ?  960 HOH A O      1 
HETATM 2665 O  O      . HOH D 4 .   ? -31.737 -3.458  -12.176 1.00 57.42  ?  961 HOH A O      1 
HETATM 2666 O  O      . HOH D 4 .   ? -30.641 7.303   3.243   1.00 68.16  ?  962 HOH A O      1 
HETATM 2667 O  O      . HOH D 4 .   ? -22.983 -0.369  -35.151 1.00 46.55  ?  963 HOH A O      1 
HETATM 2668 O  O      . HOH D 4 .   ? -32.851 24.581  -5.344  1.00 70.87  ?  964 HOH A O      1 
HETATM 2669 O  O      . HOH D 4 .   ? 2.090   6.181   -25.576 1.00 69.38  ?  965 HOH A O      1 
HETATM 2670 O  O      . HOH D 4 .   ? -29.442 7.009   -15.238 1.00 59.36  ?  966 HOH A O      1 
HETATM 2671 O  O      . HOH D 4 .   ? -10.687 4.181   -31.938 1.00 64.50  ?  967 HOH A O      1 
HETATM 2672 O  O      . HOH D 4 .   ? -12.970 6.939   -30.986 1.00 54.48  ?  968 HOH A O      1 
HETATM 2673 O  O      . HOH D 4 .   ? -1.308  9.699   -18.757 1.00 67.95  ?  969 HOH A O      1 
HETATM 2674 O  O      . HOH D 4 .   ? -17.322 2.146   -0.087  1.00 78.87  ?  970 HOH A O      1 
HETATM 2675 O  O      . HOH D 4 .   ? -27.378 26.311  -27.663 1.00 62.26  ?  971 HOH A O      1 
HETATM 2676 O  O      . HOH D 4 .   ? -24.742 23.839  -29.351 1.00 63.65  ?  972 HOH A O      1 
HETATM 2677 O  O      . HOH D 4 .   ? -7.163  1.449   -28.159 1.00 83.66  ?  973 HOH A O      1 
HETATM 2678 O  O      . HOH D 4 .   ? 3.744   6.941   -19.268 1.00 62.90  ?  974 HOH A O      1 
HETATM 2679 O  O      . HOH D 4 .   ? -4.582  4.639   -28.439 1.00 64.50  ?  975 HOH A O      1 
HETATM 2680 O  O      . HOH D 4 .   ? -1.288  5.816   -27.502 1.00 66.87  ?  976 HOH A O      1 
HETATM 2681 O  O      . HOH D 4 .   ? -32.065 19.637  -31.745 1.00 75.43  ?  977 HOH A O      1 
HETATM 2682 O  O      . HOH D 4 .   ? -34.052 14.520  -0.408  1.00 71.46  ?  978 HOH A O      1 
HETATM 2683 O  O      . HOH D 4 .   ? -8.082  3.811   -31.501 1.00 66.87  ?  979 HOH A O      1 
HETATM 2684 O  O      . HOH D 4 .   ? -19.695 2.796   -35.970 1.00 50.12  ?  980 HOH A O      1 
HETATM 2685 O  O      . HOH D 4 .   ? -6.509  21.674  -32.615 1.00 52.49  ?  981 HOH A O      1 
HETATM 2686 O  O      . HOH D 4 .   ? -13.517 5.330   -35.820 1.00 67.48  ?  982 HOH A O      1 
# 
