data_9AZU
# 
_entry.id   9AZU 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9AZU         pdb_00009azu 10.2210/pdb9azu/pdb 
WWPDB D_1000282378 ?            ?                   
# 
_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       2025-03-19 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9AZU 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-11 
_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              focco.vandenakker@case.edu 
_pdbx_contact_author.name_first         Focco 
_pdbx_contact_author.name_last          'van den Akker' 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-9210-3565 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Kumar, V.'         1 0000-0002-2741-8891 
'van den Akker, F.' 2 0000-0001-9210-3565 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Mechanisms of Antibiotic Resistance and Inhibition of PDC-88, a Cefepime-Hydrolyzing R2-loop Deletion Variant of Pseudomonas-derived Cephalosporinase
;
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Mack, A.R.'         1  ? 
primary 'Kumar, V.'          2  ? 
primary 'Bethel, C.R.'       3  ? 
primary 'Taracila, M.A.'     4  ? 
primary 'Miller, B.A.'       5  ? 
primary 'Six, D.A.'          6  ? 
primary 'Uehara, T.'         7  ? 
primary 'Papp-Wallace, K.M.' 8  ? 
primary 'van den Akker, F.'  9  ? 
primary 'Bonomo, R.A.'       10 ? 
# 
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 Beta-lactamase 43419.195 1   3.5.2.6 ? ? ? 
2 non-polymer syn 
'(3~{R})-3-[2-[4-(2-azanylethylamino)cyclohexyl]ethanoylamino]-2-oxidanyl-3,4-dihydro-1,2-benzoxaborinine-8-carboxylic acid' 
389.254   1   ?       ? ? ? 
3 water       nat water 18.015    300 ?       ? ? ? 
# 
_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       
;MRDTRFPCLCGIAASTLLFATTPAIAGEAPADRLKALVDAAVQPVMKANDIPGLAVAISLKGEPHYFSYGLASKEDGRRV
TPETLFEIGSVSKTFTATLAGYALAQDKMRLDDRASQHWPALQGSRFDGISLLDLATYTAGGLPLQFPDSVQKDQAQIRD
YYRQWQPTYAPGSQRLYSNPSIGLFGYLAARSLGQPFERLMEQQVFPALGLEQTHLDVPEAALAQYAQGYGKDDRPLRVG
PGPLDAEGYGVKTSAADLLRFVDANLHPERLDRPWAQALDATHRGYYKVGDMTQGLGWEAYDWPISLKRLQAGNSTPMAL
QPHRIARLPAPQALEGQRLLNKTGSTNGFGAYVAFVPGRDLGLVILANRNYPNAERVKIAYAILSGLEQQGKVPLKR
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MRDTRFPCLCGIAASTLLFATTPAIAGEAPADRLKALVDAAVQPVMKANDIPGLAVAISLKGEPHYFSYGLASKEDGRRV
TPETLFEIGSVSKTFTATLAGYALAQDKMRLDDRASQHWPALQGSRFDGISLLDLATYTAGGLPLQFPDSVQKDQAQIRD
YYRQWQPTYAPGSQRLYSNPSIGLFGYLAARSLGQPFERLMEQQVFPALGLEQTHLDVPEAALAQYAQGYGKDDRPLRVG
PGPLDAEGYGVKTSAADLLRFVDANLHPERLDRPWAQALDATHRGYYKVGDMTQGLGWEAYDWPISLKRLQAGNSTPMAL
QPHRIARLPAPQALEGQRLLNKTGSTNGFGAYVAFVPGRDLGLVILANRNYPNAERVKIAYAILSGLEQQGKVPLKR
;
_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 '(3~{R})-3-[2-[4-(2-azanylethylamino)cyclohexyl]ethanoylamino]-2-oxidanyl-3,4-dihydro-1,2-benzoxaborinine-8-carboxylic acid' KJK 
3 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   ARG n 
1 3   ASP n 
1 4   THR n 
1 5   ARG n 
1 6   PHE n 
1 7   PRO n 
1 8   CYS n 
1 9   LEU n 
1 10  CYS n 
1 11  GLY n 
1 12  ILE n 
1 13  ALA n 
1 14  ALA n 
1 15  SER n 
1 16  THR n 
1 17  LEU n 
1 18  LEU n 
1 19  PHE n 
1 20  ALA n 
1 21  THR n 
1 22  THR n 
1 23  PRO n 
1 24  ALA n 
1 25  ILE n 
1 26  ALA n 
1 27  GLY n 
1 28  GLU n 
1 29  ALA n 
1 30  PRO n 
1 31  ALA n 
1 32  ASP n 
1 33  ARG n 
1 34  LEU n 
1 35  LYS n 
1 36  ALA n 
1 37  LEU n 
1 38  VAL n 
1 39  ASP n 
1 40  ALA n 
1 41  ALA n 
1 42  VAL n 
1 43  GLN n 
1 44  PRO n 
1 45  VAL n 
1 46  MET n 
1 47  LYS n 
1 48  ALA n 
1 49  ASN n 
1 50  ASP n 
1 51  ILE n 
1 52  PRO n 
1 53  GLY n 
1 54  LEU n 
1 55  ALA n 
1 56  VAL n 
1 57  ALA n 
1 58  ILE n 
1 59  SER n 
1 60  LEU n 
1 61  LYS n 
1 62  GLY n 
1 63  GLU n 
1 64  PRO n 
1 65  HIS n 
1 66  TYR n 
1 67  PHE n 
1 68  SER n 
1 69  TYR n 
1 70  GLY n 
1 71  LEU n 
1 72  ALA n 
1 73  SER n 
1 74  LYS n 
1 75  GLU n 
1 76  ASP n 
1 77  GLY n 
1 78  ARG n 
1 79  ARG n 
1 80  VAL n 
1 81  THR n 
1 82  PRO n 
1 83  GLU n 
1 84  THR n 
1 85  LEU n 
1 86  PHE n 
1 87  GLU n 
1 88  ILE n 
1 89  GLY n 
1 90  SER n 
1 91  VAL n 
1 92  SER n 
1 93  LYS n 
1 94  THR n 
1 95  PHE n 
1 96  THR n 
1 97  ALA n 
1 98  THR n 
1 99  LEU n 
1 100 ALA n 
1 101 GLY n 
1 102 TYR n 
1 103 ALA n 
1 104 LEU n 
1 105 ALA n 
1 106 GLN n 
1 107 ASP n 
1 108 LYS n 
1 109 MET n 
1 110 ARG n 
1 111 LEU n 
1 112 ASP n 
1 113 ASP n 
1 114 ARG n 
1 115 ALA n 
1 116 SER n 
1 117 GLN n 
1 118 HIS n 
1 119 TRP n 
1 120 PRO n 
1 121 ALA n 
1 122 LEU n 
1 123 GLN n 
1 124 GLY n 
1 125 SER n 
1 126 ARG n 
1 127 PHE n 
1 128 ASP n 
1 129 GLY n 
1 130 ILE n 
1 131 SER n 
1 132 LEU n 
1 133 LEU n 
1 134 ASP n 
1 135 LEU n 
1 136 ALA n 
1 137 THR n 
1 138 TYR n 
1 139 THR n 
1 140 ALA n 
1 141 GLY n 
1 142 GLY n 
1 143 LEU n 
1 144 PRO n 
1 145 LEU n 
1 146 GLN n 
1 147 PHE n 
1 148 PRO n 
1 149 ASP n 
1 150 SER n 
1 151 VAL n 
1 152 GLN n 
1 153 LYS n 
1 154 ASP n 
1 155 GLN n 
1 156 ALA n 
1 157 GLN n 
1 158 ILE n 
1 159 ARG n 
1 160 ASP n 
1 161 TYR n 
1 162 TYR n 
1 163 ARG n 
1 164 GLN n 
1 165 TRP n 
1 166 GLN n 
1 167 PRO n 
1 168 THR n 
1 169 TYR n 
1 170 ALA n 
1 171 PRO n 
1 172 GLY n 
1 173 SER n 
1 174 GLN n 
1 175 ARG n 
1 176 LEU n 
1 177 TYR n 
1 178 SER n 
1 179 ASN n 
1 180 PRO n 
1 181 SER n 
1 182 ILE n 
1 183 GLY n 
1 184 LEU n 
1 185 PHE n 
1 186 GLY n 
1 187 TYR n 
1 188 LEU n 
1 189 ALA n 
1 190 ALA n 
1 191 ARG n 
1 192 SER n 
1 193 LEU n 
1 194 GLY n 
1 195 GLN n 
1 196 PRO n 
1 197 PHE n 
1 198 GLU n 
1 199 ARG n 
1 200 LEU n 
1 201 MET n 
1 202 GLU n 
1 203 GLN n 
1 204 GLN n 
1 205 VAL n 
1 206 PHE n 
1 207 PRO n 
1 208 ALA n 
1 209 LEU n 
1 210 GLY n 
1 211 LEU n 
1 212 GLU n 
1 213 GLN n 
1 214 THR n 
1 215 HIS n 
1 216 LEU n 
1 217 ASP n 
1 218 VAL n 
1 219 PRO n 
1 220 GLU n 
1 221 ALA n 
1 222 ALA n 
1 223 LEU n 
1 224 ALA n 
1 225 GLN n 
1 226 TYR n 
1 227 ALA n 
1 228 GLN n 
1 229 GLY n 
1 230 TYR n 
1 231 GLY n 
1 232 LYS n 
1 233 ASP n 
1 234 ASP n 
1 235 ARG n 
1 236 PRO n 
1 237 LEU n 
1 238 ARG n 
1 239 VAL n 
1 240 GLY n 
1 241 PRO n 
1 242 GLY n 
1 243 PRO n 
1 244 LEU n 
1 245 ASP n 
1 246 ALA n 
1 247 GLU n 
1 248 GLY n 
1 249 TYR n 
1 250 GLY n 
1 251 VAL n 
1 252 LYS n 
1 253 THR n 
1 254 SER n 
1 255 ALA n 
1 256 ALA n 
1 257 ASP n 
1 258 LEU n 
1 259 LEU n 
1 260 ARG n 
1 261 PHE n 
1 262 VAL n 
1 263 ASP n 
1 264 ALA n 
1 265 ASN n 
1 266 LEU n 
1 267 HIS n 
1 268 PRO n 
1 269 GLU n 
1 270 ARG n 
1 271 LEU n 
1 272 ASP n 
1 273 ARG n 
1 274 PRO n 
1 275 TRP n 
1 276 ALA n 
1 277 GLN n 
1 278 ALA n 
1 279 LEU n 
1 280 ASP n 
1 281 ALA n 
1 282 THR n 
1 283 HIS n 
1 284 ARG n 
1 285 GLY n 
1 286 TYR n 
1 287 TYR n 
1 288 LYS n 
1 289 VAL n 
1 290 GLY n 
1 291 ASP n 
1 292 MET n 
1 293 THR n 
1 294 GLN n 
1 295 GLY n 
1 296 LEU n 
1 297 GLY n 
1 298 TRP n 
1 299 GLU n 
1 300 ALA n 
1 301 TYR n 
1 302 ASP n 
1 303 TRP n 
1 304 PRO n 
1 305 ILE n 
1 306 SER n 
1 307 LEU n 
1 308 LYS n 
1 309 ARG n 
1 310 LEU n 
1 311 GLN n 
1 312 ALA n 
1 313 GLY n 
1 314 ASN n 
1 315 SER n 
1 316 THR n 
1 317 PRO n 
1 318 MET n 
1 319 ALA n 
1 320 LEU n 
1 321 GLN n 
1 322 PRO n 
1 323 HIS n 
1 324 ARG n 
1 325 ILE n 
1 326 ALA n 
1 327 ARG n 
1 328 LEU n 
1 329 PRO n 
1 330 ALA n 
1 331 PRO n 
1 332 GLN n 
1 333 ALA n 
1 334 LEU n 
1 335 GLU n 
1 336 GLY n 
1 337 GLN n 
1 338 ARG n 
1 339 LEU n 
1 340 LEU n 
1 341 ASN n 
1 342 LYS n 
1 343 THR n 
1 344 GLY n 
1 345 SER n 
1 346 THR n 
1 347 ASN n 
1 348 GLY n 
1 349 PHE n 
1 350 GLY n 
1 351 ALA n 
1 352 TYR n 
1 353 VAL n 
1 354 ALA n 
1 355 PHE n 
1 356 VAL n 
1 357 PRO n 
1 358 GLY n 
1 359 ARG n 
1 360 ASP n 
1 361 LEU n 
1 362 GLY n 
1 363 LEU n 
1 364 VAL n 
1 365 ILE n 
1 366 LEU n 
1 367 ALA n 
1 368 ASN n 
1 369 ARG n 
1 370 ASN n 
1 371 TYR n 
1 372 PRO n 
1 373 ASN n 
1 374 ALA n 
1 375 GLU n 
1 376 ARG n 
1 377 VAL n 
1 378 LYS n 
1 379 ILE n 
1 380 ALA n 
1 381 TYR n 
1 382 ALA n 
1 383 ILE n 
1 384 LEU n 
1 385 SER n 
1 386 GLY n 
1 387 LEU n 
1 388 GLU n 
1 389 GLN n 
1 390 GLN n 
1 391 GLY n 
1 392 LYS n 
1 393 VAL n 
1 394 PRO n 
1 395 LEU n 
1 396 LYS n 
1 397 ARG n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   397 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ampC 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Pseudomonas aeruginosa' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     287 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
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 
KJK non-polymer         . 
'(3~{R})-3-[2-[4-(2-azanylethylamino)cyclohexyl]ethanoylamino]-2-oxidanyl-3,4-dihydro-1,2-benzoxaborinine-8-carboxylic acid' ? 
'C19 H28 B N3 O5' 389.254 
LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'     131.173 
LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'  147.195 
MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'   149.211 
PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'     165.189 
PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2'      115.130 
SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3'      105.093 
THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3'      119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'   204.225 
TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'     181.189 
VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2'     117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -25 ?   ?   ?   A . n 
A 1 2   ARG 2   -24 ?   ?   ?   A . n 
A 1 3   ASP 3   -23 ?   ?   ?   A . n 
A 1 4   THR 4   -22 ?   ?   ?   A . n 
A 1 5   ARG 5   -21 ?   ?   ?   A . n 
A 1 6   PHE 6   -20 ?   ?   ?   A . n 
A 1 7   PRO 7   -19 ?   ?   ?   A . n 
A 1 8   CYS 8   -18 ?   ?   ?   A . n 
A 1 9   LEU 9   -17 ?   ?   ?   A . n 
A 1 10  CYS 10  -16 ?   ?   ?   A . n 
A 1 11  GLY 11  -15 ?   ?   ?   A . n 
A 1 12  ILE 12  -14 ?   ?   ?   A . n 
A 1 13  ALA 13  -13 ?   ?   ?   A . n 
A 1 14  ALA 14  -12 ?   ?   ?   A . n 
A 1 15  SER 15  -11 ?   ?   ?   A . n 
A 1 16  THR 16  -10 ?   ?   ?   A . n 
A 1 17  LEU 17  -9  ?   ?   ?   A . n 
A 1 18  LEU 18  -8  ?   ?   ?   A . n 
A 1 19  PHE 19  -7  ?   ?   ?   A . n 
A 1 20  ALA 20  -6  ?   ?   ?   A . n 
A 1 21  THR 21  -5  ?   ?   ?   A . n 
A 1 22  THR 22  -4  ?   ?   ?   A . n 
A 1 23  PRO 23  -3  ?   ?   ?   A . n 
A 1 24  ALA 24  -2  ?   ?   ?   A . n 
A 1 25  ILE 25  -1  ?   ?   ?   A . n 
A 1 26  ALA 26  0   ?   ?   ?   A . n 
A 1 27  GLY 27  1   ?   ?   ?   A . n 
A 1 28  GLU 28  2   ?   ?   ?   A . n 
A 1 29  ALA 29  3   3   ALA ALA A . n 
A 1 30  PRO 30  4   4   PRO PRO A . n 
A 1 31  ALA 31  5   5   ALA ALA A . n 
A 1 32  ASP 32  6   6   ASP ASP A . n 
A 1 33  ARG 33  7   7   ARG ARG A . n 
A 1 34  LEU 34  8   8   LEU LEU A . n 
A 1 35  LYS 35  9   9   LYS LYS A . n 
A 1 36  ALA 36  10  10  ALA ALA A . n 
A 1 37  LEU 37  11  11  LEU LEU A . n 
A 1 38  VAL 38  12  12  VAL VAL A . n 
A 1 39  ASP 39  13  13  ASP ASP A . n 
A 1 40  ALA 40  14  14  ALA ALA A . n 
A 1 41  ALA 41  15  15  ALA ALA A . n 
A 1 42  VAL 42  16  16  VAL VAL A . n 
A 1 43  GLN 43  17  17  GLN GLN A . n 
A 1 44  PRO 44  18  18  PRO PRO A . n 
A 1 45  VAL 45  19  19  VAL VAL A . n 
A 1 46  MET 46  20  20  MET MET A . n 
A 1 47  LYS 47  21  21  LYS LYS A . n 
A 1 48  ALA 48  22  22  ALA ALA A . n 
A 1 49  ASN 49  23  23  ASN ASN A . n 
A 1 50  ASP 50  24  24  ASP ASP A . n 
A 1 51  ILE 51  25  25  ILE ILE A . n 
A 1 52  PRO 52  26  26  PRO PRO A . n 
A 1 53  GLY 53  27  27  GLY GLY A . n 
A 1 54  LEU 54  28  28  LEU LEU A . n 
A 1 55  ALA 55  29  29  ALA ALA A . n 
A 1 56  VAL 56  30  30  VAL VAL A . n 
A 1 57  ALA 57  31  31  ALA ALA A . n 
A 1 58  ILE 58  32  32  ILE ILE A . n 
A 1 59  SER 59  33  33  SER SER A . n 
A 1 60  LEU 60  34  34  LEU LEU A . n 
A 1 61  LYS 61  35  35  LYS LYS A . n 
A 1 62  GLY 62  36  36  GLY GLY A . n 
A 1 63  GLU 63  37  37  GLU GLU A . n 
A 1 64  PRO 64  38  38  PRO PRO A . n 
A 1 65  HIS 65  39  39  HIS HIS A . n 
A 1 66  TYR 66  40  40  TYR TYR A . n 
A 1 67  PHE 67  41  41  PHE PHE A . n 
A 1 68  SER 68  42  42  SER SER A . n 
A 1 69  TYR 69  43  43  TYR TYR A . n 
A 1 70  GLY 70  44  44  GLY GLY A . n 
A 1 71  LEU 71  45  45  LEU LEU A . n 
A 1 72  ALA 72  46  46  ALA ALA A . n 
A 1 73  SER 73  47  47  SER SER A . n 
A 1 74  LYS 74  48  48  LYS LYS A . n 
A 1 75  GLU 75  49  49  GLU GLU A . n 
A 1 76  ASP 76  50  50  ASP ASP A . n 
A 1 77  GLY 77  51  51  GLY GLY A . n 
A 1 78  ARG 78  52  52  ARG ARG A . n 
A 1 79  ARG 79  53  53  ARG ARG A . n 
A 1 80  VAL 80  54  54  VAL VAL A . n 
A 1 81  THR 81  55  55  THR THR A . n 
A 1 82  PRO 82  56  56  PRO PRO A . n 
A 1 83  GLU 83  57  57  GLU GLU A . n 
A 1 84  THR 84  58  58  THR THR A . n 
A 1 85  LEU 85  59  59  LEU LEU A . n 
A 1 86  PHE 86  60  60  PHE PHE A . n 
A 1 87  GLU 87  61  61  GLU GLU A . n 
A 1 88  ILE 88  62  62  ILE ILE A . n 
A 1 89  GLY 89  63  63  GLY GLY A . n 
A 1 90  SER 90  64  64  SER SER A . n 
A 1 91  VAL 91  65  65  VAL VAL A . n 
A 1 92  SER 92  66  66  SER SER A . n 
A 1 93  LYS 93  67  67  LYS LYS A . n 
A 1 94  THR 94  68  68  THR THR A . n 
A 1 95  PHE 95  69  69  PHE PHE A . n 
A 1 96  THR 96  70  70  THR THR A . n 
A 1 97  ALA 97  71  71  ALA ALA A . n 
A 1 98  THR 98  72  72  THR THR A . n 
A 1 99  LEU 99  73  73  LEU LEU A . n 
A 1 100 ALA 100 74  74  ALA ALA A . n 
A 1 101 GLY 101 75  75  GLY GLY A . n 
A 1 102 TYR 102 76  76  TYR TYR A . n 
A 1 103 ALA 103 77  77  ALA ALA A . n 
A 1 104 LEU 104 78  78  LEU LEU A . n 
A 1 105 ALA 105 79  79  ALA ALA A . n 
A 1 106 GLN 106 80  80  GLN GLN A . n 
A 1 107 ASP 107 81  81  ASP ASP A . n 
A 1 108 LYS 108 82  82  LYS LYS A . n 
A 1 109 MET 109 83  83  MET MET A . n 
A 1 110 ARG 110 84  84  ARG ARG A . n 
A 1 111 LEU 111 85  85  LEU LEU A . n 
A 1 112 ASP 112 86  86  ASP ASP A . n 
A 1 113 ASP 113 87  87  ASP ASP A . n 
A 1 114 ARG 114 88  88  ARG ARG A . n 
A 1 115 ALA 115 89  89  ALA ALA A . n 
A 1 116 SER 116 90  90  SER SER A . n 
A 1 117 GLN 117 91  91  GLN GLN A . n 
A 1 118 HIS 118 92  92  HIS HIS A . n 
A 1 119 TRP 119 93  93  TRP TRP A . n 
A 1 120 PRO 120 94  94  PRO PRO A . n 
A 1 121 ALA 121 95  95  ALA ALA A . n 
A 1 122 LEU 122 96  96  LEU LEU A . n 
A 1 123 GLN 123 97  97  GLN GLN A . n 
A 1 124 GLY 124 98  98  GLY GLY A . n 
A 1 125 SER 125 99  99  SER SER A . n 
A 1 126 ARG 126 100 100 ARG ARG A . n 
A 1 127 PHE 127 101 101 PHE PHE A . n 
A 1 128 ASP 128 102 102 ASP ASP A . n 
A 1 129 GLY 129 103 103 GLY GLY A . n 
A 1 130 ILE 130 104 104 ILE ILE A . n 
A 1 131 SER 131 105 105 SER SER A . n 
A 1 132 LEU 132 106 106 LEU LEU A . n 
A 1 133 LEU 133 107 107 LEU LEU A . n 
A 1 134 ASP 134 108 108 ASP ASP A . n 
A 1 135 LEU 135 109 109 LEU LEU A . n 
A 1 136 ALA 136 110 110 ALA ALA A . n 
A 1 137 THR 137 111 111 THR THR A . n 
A 1 138 TYR 138 112 112 TYR TYR A . n 
A 1 139 THR 139 113 113 THR THR A . n 
A 1 140 ALA 140 114 114 ALA ALA A . n 
A 1 141 GLY 141 115 115 GLY GLY A . n 
A 1 142 GLY 142 116 116 GLY GLY A . n 
A 1 143 LEU 143 117 117 LEU LEU A . n 
A 1 144 PRO 144 118 118 PRO PRO A . n 
A 1 145 LEU 145 119 119 LEU LEU A . n 
A 1 146 GLN 146 120 120 GLN GLN A . n 
A 1 147 PHE 147 121 121 PHE PHE A . n 
A 1 148 PRO 148 122 122 PRO PRO A . n 
A 1 149 ASP 149 123 123 ASP ASP A . n 
A 1 150 SER 150 124 124 SER SER A . n 
A 1 151 VAL 151 125 125 VAL VAL A . n 
A 1 152 GLN 152 126 126 GLN GLN A . n 
A 1 153 LYS 153 127 127 LYS LYS A . n 
A 1 154 ASP 154 128 128 ASP ASP A . n 
A 1 155 GLN 155 129 129 GLN GLN A . n 
A 1 156 ALA 156 130 130 ALA ALA A . n 
A 1 157 GLN 157 131 131 GLN GLN A . n 
A 1 158 ILE 158 132 132 ILE ILE A . n 
A 1 159 ARG 159 133 133 ARG ARG A . n 
A 1 160 ASP 160 134 134 ASP ASP A . n 
A 1 161 TYR 161 135 135 TYR TYR A . n 
A 1 162 TYR 162 136 136 TYR TYR A . n 
A 1 163 ARG 163 137 137 ARG ARG A . n 
A 1 164 GLN 164 138 138 GLN GLN A . n 
A 1 165 TRP 165 139 139 TRP TRP A . n 
A 1 166 GLN 166 140 140 GLN GLN A . n 
A 1 167 PRO 167 141 141 PRO PRO A . n 
A 1 168 THR 168 142 142 THR THR A . n 
A 1 169 TYR 169 143 143 TYR TYR A . n 
A 1 170 ALA 170 144 144 ALA ALA A . n 
A 1 171 PRO 171 145 145 PRO PRO A . n 
A 1 172 GLY 172 146 146 GLY GLY A . n 
A 1 173 SER 173 147 147 SER SER A . n 
A 1 174 GLN 174 148 148 GLN GLN A . n 
A 1 175 ARG 175 149 149 ARG ARG A . n 
A 1 176 LEU 176 150 150 LEU LEU A . n 
A 1 177 TYR 177 151 151 TYR TYR A . n 
A 1 178 SER 178 152 152 SER SER A . n 
A 1 179 ASN 179 153 153 ASN ASN A . n 
A 1 180 PRO 180 154 154 PRO PRO A . n 
A 1 181 SER 181 155 155 SER SER A . n 
A 1 182 ILE 182 156 156 ILE ILE A . n 
A 1 183 GLY 183 157 157 GLY GLY A . n 
A 1 184 LEU 184 158 158 LEU LEU A . n 
A 1 185 PHE 185 159 159 PHE PHE A . n 
A 1 186 GLY 186 160 160 GLY GLY A . n 
A 1 187 TYR 187 161 161 TYR TYR A . n 
A 1 188 LEU 188 162 162 LEU LEU A . n 
A 1 189 ALA 189 163 163 ALA ALA A . n 
A 1 190 ALA 190 164 164 ALA ALA A . n 
A 1 191 ARG 191 165 165 ARG ARG A . n 
A 1 192 SER 192 166 166 SER SER A . n 
A 1 193 LEU 193 167 167 LEU LEU A . n 
A 1 194 GLY 194 168 168 GLY GLY A . n 
A 1 195 GLN 195 169 169 GLN GLN A . n 
A 1 196 PRO 196 170 170 PRO PRO A . n 
A 1 197 PHE 197 171 171 PHE PHE A . n 
A 1 198 GLU 198 172 172 GLU GLU A . n 
A 1 199 ARG 199 173 173 ARG ARG A . n 
A 1 200 LEU 200 174 174 LEU LEU A . n 
A 1 201 MET 201 175 175 MET MET A . n 
A 1 202 GLU 202 176 176 GLU GLU A . n 
A 1 203 GLN 203 177 177 GLN GLN A . n 
A 1 204 GLN 204 178 178 GLN GLN A . n 
A 1 205 VAL 205 179 179 VAL VAL A . n 
A 1 206 PHE 206 180 180 PHE PHE A . n 
A 1 207 PRO 207 181 181 PRO PRO A . n 
A 1 208 ALA 208 182 182 ALA ALA A . n 
A 1 209 LEU 209 183 183 LEU LEU A . n 
A 1 210 GLY 210 184 184 GLY GLY A . n 
A 1 211 LEU 211 185 185 LEU LEU A . n 
A 1 212 GLU 212 186 186 GLU GLU A . n 
A 1 213 GLN 213 187 187 GLN GLN A . n 
A 1 214 THR 214 188 188 THR THR A . n 
A 1 215 HIS 215 189 189 HIS HIS A . n 
A 1 216 LEU 216 190 190 LEU LEU A . n 
A 1 217 ASP 217 191 191 ASP ASP A . n 
A 1 218 VAL 218 192 192 VAL VAL A . n 
A 1 219 PRO 219 193 193 PRO PRO A . n 
A 1 220 GLU 220 194 194 GLU GLU A . n 
A 1 221 ALA 221 195 195 ALA ALA A . n 
A 1 222 ALA 222 196 196 ALA ALA A . n 
A 1 223 LEU 223 197 197 LEU LEU A . n 
A 1 224 ALA 224 198 198 ALA ALA A . n 
A 1 225 GLN 225 199 199 GLN GLN A . n 
A 1 226 TYR 226 200 200 TYR TYR A . n 
A 1 227 ALA 227 201 201 ALA ALA A . n 
A 1 228 GLN 228 202 202 GLN GLN A . n 
A 1 229 GLY 229 203 203 GLY GLY A . n 
A 1 230 TYR 230 204 204 TYR TYR A . n 
A 1 231 GLY 231 205 205 GLY GLY A . n 
A 1 232 LYS 232 206 206 LYS LYS A . n 
A 1 233 ASP 233 207 207 ASP ASP A . n 
A 1 234 ASP 234 208 208 ASP ASP A . n 
A 1 235 ARG 235 209 209 ARG ARG A . n 
A 1 236 PRO 236 210 210 PRO PRO A . n 
A 1 237 LEU 237 211 211 LEU LEU A . n 
A 1 238 ARG 238 212 212 ARG ARG A . n 
A 1 239 VAL 239 213 213 VAL VAL A . n 
A 1 240 GLY 240 214 214 GLY GLY A . n 
A 1 241 PRO 241 215 215 PRO PRO A . n 
A 1 242 GLY 242 216 216 GLY GLY A . n 
A 1 243 PRO 243 217 217 PRO PRO A . n 
A 1 244 LEU 244 218 218 LEU LEU A . n 
A 1 245 ASP 245 219 219 ASP ASP A . n 
A 1 246 ALA 246 220 220 ALA ALA A . n 
A 1 247 GLU 247 221 221 GLU GLU A . n 
A 1 248 GLY 248 222 222 GLY GLY A . n 
A 1 249 TYR 249 223 223 TYR TYR A . n 
A 1 250 GLY 250 224 224 GLY GLY A . n 
A 1 251 VAL 251 225 225 VAL VAL A . n 
A 1 252 LYS 252 226 226 LYS LYS A . n 
A 1 253 THR 253 227 227 THR THR A . n 
A 1 254 SER 254 228 228 SER SER A . n 
A 1 255 ALA 255 229 229 ALA ALA A . n 
A 1 256 ALA 256 230 230 ALA ALA A . n 
A 1 257 ASP 257 231 231 ASP ASP A . n 
A 1 258 LEU 258 232 232 LEU LEU A . n 
A 1 259 LEU 259 233 233 LEU LEU A . n 
A 1 260 ARG 260 234 234 ARG ARG A . n 
A 1 261 PHE 261 235 235 PHE PHE A . n 
A 1 262 VAL 262 236 236 VAL VAL A . n 
A 1 263 ASP 263 237 237 ASP ASP A . n 
A 1 264 ALA 264 238 238 ALA ALA A . n 
A 1 265 ASN 265 239 239 ASN ASN A . n 
A 1 266 LEU 266 240 240 LEU LEU A . n 
A 1 267 HIS 267 241 241 HIS HIS A . n 
A 1 268 PRO 268 242 242 PRO PRO A . n 
A 1 269 GLU 269 243 243 GLU GLU A . n 
A 1 270 ARG 270 244 244 ARG ARG A . n 
A 1 271 LEU 271 245 245 LEU LEU A . n 
A 1 272 ASP 272 246 246 ASP ASP A . n 
A 1 273 ARG 273 247 247 ARG ARG A . n 
A 1 274 PRO 274 248 248 PRO PRO A . n 
A 1 275 TRP 275 249 249 TRP TRP A . n 
A 1 276 ALA 276 250 250 ALA ALA A . n 
A 1 277 GLN 277 251 251 GLN GLN A . n 
A 1 278 ALA 278 252 252 ALA ALA A . n 
A 1 279 LEU 279 253 253 LEU LEU A . n 
A 1 280 ASP 280 254 254 ASP ASP A . n 
A 1 281 ALA 281 255 255 ALA ALA A . n 
A 1 282 THR 282 256 256 THR THR A . n 
A 1 283 HIS 283 257 257 HIS HIS A . n 
A 1 284 ARG 284 258 258 ARG ARG A . n 
A 1 285 GLY 285 259 259 GLY GLY A . n 
A 1 286 TYR 286 260 260 TYR TYR A . n 
A 1 287 TYR 287 261 261 TYR TYR A . n 
A 1 288 LYS 288 262 262 LYS LYS A . n 
A 1 289 VAL 289 263 263 VAL VAL A . n 
A 1 290 GLY 290 264 264 GLY GLY A . n 
A 1 291 ASP 291 265 265 ASP ASP A . n 
A 1 292 MET 292 266 266 MET MET A . n 
A 1 293 THR 293 267 267 THR THR A . n 
A 1 294 GLN 294 268 268 GLN GLN A . n 
A 1 295 GLY 295 269 269 GLY GLY A . n 
A 1 296 LEU 296 270 270 LEU LEU A . n 
A 1 297 GLY 297 271 271 GLY GLY A . n 
A 1 298 TRP 298 272 272 TRP TRP A . n 
A 1 299 GLU 299 273 273 GLU GLU A . n 
A 1 300 ALA 300 274 274 ALA ALA A . n 
A 1 301 TYR 301 275 275 TYR TYR A . n 
A 1 302 ASP 302 276 276 ASP ASP A . n 
A 1 303 TRP 303 277 277 TRP TRP A . n 
A 1 304 PRO 304 278 278 PRO PRO A . n 
A 1 305 ILE 305 279 279 ILE ILE A . n 
A 1 306 SER 306 280 280 SER SER A . n 
A 1 307 LEU 307 281 281 LEU LEU A . n 
A 1 308 LYS 308 282 282 LYS LYS A . n 
A 1 309 ARG 309 283 283 ARG ARG A . n 
A 1 310 LEU 310 284 284 LEU LEU A . n 
A 1 311 GLN 311 285 285 GLN GLN A . n 
A 1 312 ALA 312 286 286 ALA ALA A . n 
A 1 313 GLY 313 287 287 GLY GLY A . n 
A 1 314 ASN 314 288 288 ASN ASN A . n 
A 1 315 SER 315 289 289 SER SER A . n 
A 1 316 THR 316 290 290 THR THR A . n 
A 1 317 PRO 317 291 291 PRO PRO A . n 
A 1 318 MET 318 292 292 MET MET A . n 
A 1 319 ALA 319 293 293 ALA ALA A . n 
A 1 320 LEU 320 294 294 LEU LEU A . n 
A 1 321 GLN 321 295 295 GLN GLN A . n 
A 1 322 PRO 322 296 296 PRO PRO A . n 
A 1 323 HIS 323 297 297 HIS HIS A . n 
A 1 324 ARG 324 298 298 ARG ARG A . n 
A 1 325 ILE 325 299 299 ILE ILE A . n 
A 1 326 ALA 326 300 300 ALA ALA A . n 
A 1 327 ARG 327 301 301 ARG ARG A . n 
A 1 328 LEU 328 302 302 LEU LEU A . n 
A 1 329 PRO 329 303 303 PRO PRO A . n 
A 1 330 ALA 330 304 304 ALA ALA A . n 
A 1 331 PRO 331 305 305 PRO PRO A . n 
A 1 332 GLN 332 306 306 GLN GLN A . n 
A 1 333 ALA 333 307 307 ALA ALA A . n 
A 1 334 LEU 334 308 308 LEU LEU A . n 
A 1 335 GLU 335 309 309 GLU GLU A . n 
A 1 336 GLY 336 310 310 GLY GLY A . n 
A 1 337 GLN 337 311 311 GLN GLN A . n 
A 1 338 ARG 338 312 312 ARG ARG A . n 
A 1 339 LEU 339 313 313 LEU LEU A . n 
A 1 340 LEU 340 314 314 LEU LEU A . n 
A 1 341 ASN 341 315 315 ASN ASN A . n 
A 1 342 LYS 342 316 316 LYS LYS A . n 
A 1 343 THR 343 317 317 THR THR A . n 
A 1 344 GLY 344 318 318 GLY GLY A . n 
A 1 345 SER 345 319 319 SER SER A . n 
A 1 346 THR 346 320 320 THR THR A . n 
A 1 347 ASN 347 321 321 ASN ASN A . n 
A 1 348 GLY 348 322 322 GLY GLY A . n 
A 1 349 PHE 349 323 323 PHE PHE A . n 
A 1 350 GLY 350 324 324 GLY GLY A . n 
A 1 351 ALA 351 325 325 ALA ALA A . n 
A 1 352 TYR 352 326 326 TYR TYR A . n 
A 1 353 VAL 353 327 327 VAL VAL A . n 
A 1 354 ALA 354 328 328 ALA ALA A . n 
A 1 355 PHE 355 329 329 PHE PHE A . n 
A 1 356 VAL 356 330 330 VAL VAL A . n 
A 1 357 PRO 357 331 331 PRO PRO A . n 
A 1 358 GLY 358 332 332 GLY GLY A . n 
A 1 359 ARG 359 333 333 ARG ARG A . n 
A 1 360 ASP 360 334 334 ASP ASP A . n 
A 1 361 LEU 361 335 335 LEU LEU A . n 
A 1 362 GLY 362 336 336 GLY GLY A . n 
A 1 363 LEU 363 337 337 LEU LEU A . n 
A 1 364 VAL 364 338 338 VAL VAL A . n 
A 1 365 ILE 365 339 339 ILE ILE A . n 
A 1 366 LEU 366 340 340 LEU LEU A . n 
A 1 367 ALA 367 341 341 ALA ALA A . n 
A 1 368 ASN 368 342 342 ASN ASN A . n 
A 1 369 ARG 369 343 343 ARG ARG A . n 
A 1 370 ASN 370 344 344 ASN ASN A . n 
A 1 371 TYR 371 345 345 TYR TYR A . n 
A 1 372 PRO 372 346 346 PRO PRO A . n 
A 1 373 ASN 373 347 347 ASN ASN A . n 
A 1 374 ALA 374 348 348 ALA ALA A . n 
A 1 375 GLU 375 349 349 GLU GLU A . n 
A 1 376 ARG 376 350 350 ARG ARG A . n 
A 1 377 VAL 377 351 351 VAL VAL A . n 
A 1 378 LYS 378 352 352 LYS LYS A . n 
A 1 379 ILE 379 353 353 ILE ILE A . n 
A 1 380 ALA 380 354 354 ALA ALA A . n 
A 1 381 TYR 381 355 355 TYR TYR A . n 
A 1 382 ALA 382 356 356 ALA ALA A . n 
A 1 383 ILE 383 357 357 ILE ILE A . n 
A 1 384 LEU 384 358 358 LEU LEU A . n 
A 1 385 SER 385 359 359 SER SER A . n 
A 1 386 GLY 386 360 360 GLY GLY A . n 
A 1 387 LEU 387 361 361 LEU LEU A . n 
A 1 388 GLU 388 362 ?   ?   ?   A . n 
A 1 389 GLN 389 363 ?   ?   ?   A . n 
A 1 390 GLN 390 364 ?   ?   ?   A . n 
A 1 391 GLY 391 365 ?   ?   ?   A . n 
A 1 392 LYS 392 366 ?   ?   ?   A . n 
A 1 393 VAL 393 367 ?   ?   ?   A . n 
A 1 394 PRO 394 368 ?   ?   ?   A . n 
A 1 395 LEU 395 369 ?   ?   ?   A . n 
A 1 396 LYS 396 370 ?   ?   ?   A . n 
A 1 397 ARG 397 371 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        KJK 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   KJK 
_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 KJK 1   401 1   KJK TNB A . 
C 3 HOH 1   501 236 HOH HOH A . 
C 3 HOH 2   502 93  HOH HOH A . 
C 3 HOH 3   503 147 HOH HOH A . 
C 3 HOH 4   504 73  HOH HOH A . 
C 3 HOH 5   505 231 HOH HOH A . 
C 3 HOH 6   506 58  HOH HOH A . 
C 3 HOH 7   507 85  HOH HOH A . 
C 3 HOH 8   508 274 HOH HOH A . 
C 3 HOH 9   509 234 HOH HOH A . 
C 3 HOH 10  510 213 HOH HOH A . 
C 3 HOH 11  511 155 HOH HOH A . 
C 3 HOH 12  512 309 HOH HOH A . 
C 3 HOH 13  513 239 HOH HOH A . 
C 3 HOH 14  514 185 HOH HOH A . 
C 3 HOH 15  515 224 HOH HOH A . 
C 3 HOH 16  516 113 HOH HOH A . 
C 3 HOH 17  517 235 HOH HOH A . 
C 3 HOH 18  518 256 HOH HOH A . 
C 3 HOH 19  519 103 HOH HOH A . 
C 3 HOH 20  520 292 HOH HOH A . 
C 3 HOH 21  521 24  HOH HOH A . 
C 3 HOH 22  522 154 HOH HOH A . 
C 3 HOH 23  523 183 HOH HOH A . 
C 3 HOH 24  524 126 HOH HOH A . 
C 3 HOH 25  525 116 HOH HOH A . 
C 3 HOH 26  526 215 HOH HOH A . 
C 3 HOH 27  527 130 HOH HOH A . 
C 3 HOH 28  528 14  HOH HOH A . 
C 3 HOH 29  529 44  HOH HOH A . 
C 3 HOH 30  530 253 HOH HOH A . 
C 3 HOH 31  531 40  HOH HOH A . 
C 3 HOH 32  532 280 HOH HOH A . 
C 3 HOH 33  533 83  HOH HOH A . 
C 3 HOH 34  534 138 HOH HOH A . 
C 3 HOH 35  535 62  HOH HOH A . 
C 3 HOH 36  536 244 HOH HOH A . 
C 3 HOH 37  537 8   HOH HOH A . 
C 3 HOH 38  538 221 HOH HOH A . 
C 3 HOH 39  539 33  HOH HOH A . 
C 3 HOH 40  540 283 HOH HOH A . 
C 3 HOH 41  541 96  HOH HOH A . 
C 3 HOH 42  542 312 HOH HOH A . 
C 3 HOH 43  543 108 HOH HOH A . 
C 3 HOH 44  544 160 HOH HOH A . 
C 3 HOH 45  545 229 HOH HOH A . 
C 3 HOH 46  546 95  HOH HOH A . 
C 3 HOH 47  547 272 HOH HOH A . 
C 3 HOH 48  548 246 HOH HOH A . 
C 3 HOH 49  549 52  HOH HOH A . 
C 3 HOH 50  550 67  HOH HOH A . 
C 3 HOH 51  551 111 HOH HOH A . 
C 3 HOH 52  552 290 HOH HOH A . 
C 3 HOH 53  553 295 HOH HOH A . 
C 3 HOH 54  554 127 HOH HOH A . 
C 3 HOH 55  555 63  HOH HOH A . 
C 3 HOH 56  556 89  HOH HOH A . 
C 3 HOH 57  557 45  HOH HOH A . 
C 3 HOH 58  558 68  HOH HOH A . 
C 3 HOH 59  559 81  HOH HOH A . 
C 3 HOH 60  560 6   HOH HOH A . 
C 3 HOH 61  561 16  HOH HOH A . 
C 3 HOH 62  562 10  HOH HOH A . 
C 3 HOH 63  563 22  HOH HOH A . 
C 3 HOH 64  564 254 HOH HOH A . 
C 3 HOH 65  565 53  HOH HOH A . 
C 3 HOH 66  566 141 HOH HOH A . 
C 3 HOH 67  567 79  HOH HOH A . 
C 3 HOH 68  568 175 HOH HOH A . 
C 3 HOH 69  569 1   HOH HOH A . 
C 3 HOH 70  570 144 HOH HOH A . 
C 3 HOH 71  571 38  HOH HOH A . 
C 3 HOH 72  572 161 HOH HOH A . 
C 3 HOH 73  573 48  HOH HOH A . 
C 3 HOH 74  574 75  HOH HOH A . 
C 3 HOH 75  575 118 HOH HOH A . 
C 3 HOH 76  576 128 HOH HOH A . 
C 3 HOH 77  577 166 HOH HOH A . 
C 3 HOH 78  578 35  HOH HOH A . 
C 3 HOH 79  579 78  HOH HOH A . 
C 3 HOH 80  580 106 HOH HOH A . 
C 3 HOH 81  581 149 HOH HOH A . 
C 3 HOH 82  582 252 HOH HOH A . 
C 3 HOH 83  583 167 HOH HOH A . 
C 3 HOH 84  584 306 HOH HOH A . 
C 3 HOH 85  585 163 HOH HOH A . 
C 3 HOH 86  586 39  HOH HOH A . 
C 3 HOH 87  587 13  HOH HOH A . 
C 3 HOH 88  588 297 HOH HOH A . 
C 3 HOH 89  589 47  HOH HOH A . 
C 3 HOH 90  590 25  HOH HOH A . 
C 3 HOH 91  591 190 HOH HOH A . 
C 3 HOH 92  592 88  HOH HOH A . 
C 3 HOH 93  593 20  HOH HOH A . 
C 3 HOH 94  594 165 HOH HOH A . 
C 3 HOH 95  595 112 HOH HOH A . 
C 3 HOH 96  596 186 HOH HOH A . 
C 3 HOH 97  597 28  HOH HOH A . 
C 3 HOH 98  598 230 HOH HOH A . 
C 3 HOH 99  599 162 HOH HOH A . 
C 3 HOH 100 600 181 HOH HOH A . 
C 3 HOH 101 601 261 HOH HOH A . 
C 3 HOH 102 602 55  HOH HOH A . 
C 3 HOH 103 603 29  HOH HOH A . 
C 3 HOH 104 604 64  HOH HOH A . 
C 3 HOH 105 605 223 HOH HOH A . 
C 3 HOH 106 606 2   HOH HOH A . 
C 3 HOH 107 607 86  HOH HOH A . 
C 3 HOH 108 608 15  HOH HOH A . 
C 3 HOH 109 609 82  HOH HOH A . 
C 3 HOH 110 610 117 HOH HOH A . 
C 3 HOH 111 611 4   HOH HOH A . 
C 3 HOH 112 612 222 HOH HOH A . 
C 3 HOH 113 613 299 HOH HOH A . 
C 3 HOH 114 614 97  HOH HOH A . 
C 3 HOH 115 615 132 HOH HOH A . 
C 3 HOH 116 616 169 HOH HOH A . 
C 3 HOH 117 617 12  HOH HOH A . 
C 3 HOH 118 618 157 HOH HOH A . 
C 3 HOH 119 619 125 HOH HOH A . 
C 3 HOH 120 620 225 HOH HOH A . 
C 3 HOH 121 621 287 HOH HOH A . 
C 3 HOH 122 622 60  HOH HOH A . 
C 3 HOH 123 623 23  HOH HOH A . 
C 3 HOH 124 624 94  HOH HOH A . 
C 3 HOH 125 625 273 HOH HOH A . 
C 3 HOH 126 626 51  HOH HOH A . 
C 3 HOH 127 627 115 HOH HOH A . 
C 3 HOH 128 628 156 HOH HOH A . 
C 3 HOH 129 629 92  HOH HOH A . 
C 3 HOH 130 630 172 HOH HOH A . 
C 3 HOH 131 631 258 HOH HOH A . 
C 3 HOH 132 632 164 HOH HOH A . 
C 3 HOH 133 633 137 HOH HOH A . 
C 3 HOH 134 634 153 HOH HOH A . 
C 3 HOH 135 635 136 HOH HOH A . 
C 3 HOH 136 636 257 HOH HOH A . 
C 3 HOH 137 637 41  HOH HOH A . 
C 3 HOH 138 638 9   HOH HOH A . 
C 3 HOH 139 639 65  HOH HOH A . 
C 3 HOH 140 640 212 HOH HOH A . 
C 3 HOH 141 641 54  HOH HOH A . 
C 3 HOH 142 642 228 HOH HOH A . 
C 3 HOH 143 643 26  HOH HOH A . 
C 3 HOH 144 644 143 HOH HOH A . 
C 3 HOH 145 645 100 HOH HOH A . 
C 3 HOH 146 646 87  HOH HOH A . 
C 3 HOH 147 647 293 HOH HOH A . 
C 3 HOH 148 648 238 HOH HOH A . 
C 3 HOH 149 649 61  HOH HOH A . 
C 3 HOH 150 650 140 HOH HOH A . 
C 3 HOH 151 651 124 HOH HOH A . 
C 3 HOH 152 652 21  HOH HOH A . 
C 3 HOH 153 653 129 HOH HOH A . 
C 3 HOH 154 654 66  HOH HOH A . 
C 3 HOH 155 655 76  HOH HOH A . 
C 3 HOH 156 656 173 HOH HOH A . 
C 3 HOH 157 657 303 HOH HOH A . 
C 3 HOH 158 658 178 HOH HOH A . 
C 3 HOH 159 659 226 HOH HOH A . 
C 3 HOH 160 660 3   HOH HOH A . 
C 3 HOH 161 661 237 HOH HOH A . 
C 3 HOH 162 662 101 HOH HOH A . 
C 3 HOH 163 663 19  HOH HOH A . 
C 3 HOH 164 664 107 HOH HOH A . 
C 3 HOH 165 665 302 HOH HOH A . 
C 3 HOH 166 666 289 HOH HOH A . 
C 3 HOH 167 667 98  HOH HOH A . 
C 3 HOH 168 668 7   HOH HOH A . 
C 3 HOH 169 669 34  HOH HOH A . 
C 3 HOH 170 670 242 HOH HOH A . 
C 3 HOH 171 671 119 HOH HOH A . 
C 3 HOH 172 672 159 HOH HOH A . 
C 3 HOH 173 673 84  HOH HOH A . 
C 3 HOH 174 674 279 HOH HOH A . 
C 3 HOH 175 675 151 HOH HOH A . 
C 3 HOH 176 676 264 HOH HOH A . 
C 3 HOH 177 677 37  HOH HOH A . 
C 3 HOH 178 678 220 HOH HOH A . 
C 3 HOH 179 679 218 HOH HOH A . 
C 3 HOH 180 680 50  HOH HOH A . 
C 3 HOH 181 681 32  HOH HOH A . 
C 3 HOH 182 682 18  HOH HOH A . 
C 3 HOH 183 683 57  HOH HOH A . 
C 3 HOH 184 684 245 HOH HOH A . 
C 3 HOH 185 685 271 HOH HOH A . 
C 3 HOH 186 686 179 HOH HOH A . 
C 3 HOH 187 687 27  HOH HOH A . 
C 3 HOH 188 688 77  HOH HOH A . 
C 3 HOH 189 689 310 HOH HOH A . 
C 3 HOH 190 690 311 HOH HOH A . 
C 3 HOH 191 691 17  HOH HOH A . 
C 3 HOH 192 692 291 HOH HOH A . 
C 3 HOH 193 693 43  HOH HOH A . 
C 3 HOH 194 694 214 HOH HOH A . 
C 3 HOH 195 695 174 HOH HOH A . 
C 3 HOH 196 696 80  HOH HOH A . 
C 3 HOH 197 697 110 HOH HOH A . 
C 3 HOH 198 698 104 HOH HOH A . 
C 3 HOH 199 699 120 HOH HOH A . 
C 3 HOH 200 700 59  HOH HOH A . 
C 3 HOH 201 701 288 HOH HOH A . 
C 3 HOH 202 702 121 HOH HOH A . 
C 3 HOH 203 703 216 HOH HOH A . 
C 3 HOH 204 704 46  HOH HOH A . 
C 3 HOH 205 705 188 HOH HOH A . 
C 3 HOH 206 706 71  HOH HOH A . 
C 3 HOH 207 707 131 HOH HOH A . 
C 3 HOH 208 708 150 HOH HOH A . 
C 3 HOH 209 709 232 HOH HOH A . 
C 3 HOH 210 710 5   HOH HOH A . 
C 3 HOH 211 711 122 HOH HOH A . 
C 3 HOH 212 712 197 HOH HOH A . 
C 3 HOH 213 713 219 HOH HOH A . 
C 3 HOH 214 714 158 HOH HOH A . 
C 3 HOH 215 715 146 HOH HOH A . 
C 3 HOH 216 716 307 HOH HOH A . 
C 3 HOH 217 717 139 HOH HOH A . 
C 3 HOH 218 718 42  HOH HOH A . 
C 3 HOH 219 719 217 HOH HOH A . 
C 3 HOH 220 720 191 HOH HOH A . 
C 3 HOH 221 721 36  HOH HOH A . 
C 3 HOH 222 722 134 HOH HOH A . 
C 3 HOH 223 723 241 HOH HOH A . 
C 3 HOH 224 724 243 HOH HOH A . 
C 3 HOH 225 725 177 HOH HOH A . 
C 3 HOH 226 726 193 HOH HOH A . 
C 3 HOH 227 727 227 HOH HOH A . 
C 3 HOH 228 728 285 HOH HOH A . 
C 3 HOH 229 729 105 HOH HOH A . 
C 3 HOH 230 730 250 HOH HOH A . 
C 3 HOH 231 731 304 HOH HOH A . 
C 3 HOH 232 732 170 HOH HOH A . 
C 3 HOH 233 733 142 HOH HOH A . 
C 3 HOH 234 734 305 HOH HOH A . 
C 3 HOH 235 735 262 HOH HOH A . 
C 3 HOH 236 736 259 HOH HOH A . 
C 3 HOH 237 737 182 HOH HOH A . 
C 3 HOH 238 738 72  HOH HOH A . 
C 3 HOH 239 739 233 HOH HOH A . 
C 3 HOH 240 740 123 HOH HOH A . 
C 3 HOH 241 741 240 HOH HOH A . 
C 3 HOH 242 742 267 HOH HOH A . 
C 3 HOH 243 743 11  HOH HOH A . 
C 3 HOH 244 744 248 HOH HOH A . 
C 3 HOH 245 745 298 HOH HOH A . 
C 3 HOH 246 746 70  HOH HOH A . 
C 3 HOH 247 747 281 HOH HOH A . 
C 3 HOH 248 748 208 HOH HOH A . 
C 3 HOH 249 749 30  HOH HOH A . 
C 3 HOH 250 750 266 HOH HOH A . 
C 3 HOH 251 751 168 HOH HOH A . 
C 3 HOH 252 752 255 HOH HOH A . 
C 3 HOH 253 753 195 HOH HOH A . 
C 3 HOH 254 754 205 HOH HOH A . 
C 3 HOH 255 755 49  HOH HOH A . 
C 3 HOH 256 756 74  HOH HOH A . 
C 3 HOH 257 757 209 HOH HOH A . 
C 3 HOH 258 758 275 HOH HOH A . 
C 3 HOH 259 759 91  HOH HOH A . 
C 3 HOH 260 760 187 HOH HOH A . 
C 3 HOH 261 761 211 HOH HOH A . 
C 3 HOH 262 762 308 HOH HOH A . 
C 3 HOH 263 763 102 HOH HOH A . 
C 3 HOH 264 764 282 HOH HOH A . 
C 3 HOH 265 765 203 HOH HOH A . 
C 3 HOH 266 766 184 HOH HOH A . 
C 3 HOH 267 767 206 HOH HOH A . 
C 3 HOH 268 768 109 HOH HOH A . 
C 3 HOH 269 769 265 HOH HOH A . 
C 3 HOH 270 770 152 HOH HOH A . 
C 3 HOH 271 771 210 HOH HOH A . 
C 3 HOH 272 772 286 HOH HOH A . 
C 3 HOH 273 773 300 HOH HOH A . 
C 3 HOH 274 774 198 HOH HOH A . 
C 3 HOH 275 775 269 HOH HOH A . 
C 3 HOH 276 776 251 HOH HOH A . 
C 3 HOH 277 777 278 HOH HOH A . 
C 3 HOH 278 778 114 HOH HOH A . 
C 3 HOH 279 779 200 HOH HOH A . 
C 3 HOH 280 780 194 HOH HOH A . 
C 3 HOH 281 781 196 HOH HOH A . 
C 3 HOH 282 782 294 HOH HOH A . 
C 3 HOH 283 783 270 HOH HOH A . 
C 3 HOH 284 784 148 HOH HOH A . 
C 3 HOH 285 785 263 HOH HOH A . 
C 3 HOH 286 786 202 HOH HOH A . 
C 3 HOH 287 787 133 HOH HOH A . 
C 3 HOH 288 788 199 HOH HOH A . 
C 3 HOH 289 789 90  HOH HOH A . 
C 3 HOH 290 790 135 HOH HOH A . 
C 3 HOH 291 791 247 HOH HOH A . 
C 3 HOH 292 792 189 HOH HOH A . 
C 3 HOH 293 793 192 HOH HOH A . 
C 3 HOH 294 794 296 HOH HOH A . 
C 3 HOH 295 795 204 HOH HOH A . 
C 3 HOH 296 796 171 HOH HOH A . 
C 3 HOH 297 797 301 HOH HOH A . 
C 3 HOH 298 798 176 HOH HOH A . 
C 3 HOH 299 799 207 HOH HOH A . 
C 3 HOH 300 800 201 HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? .        2 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0267 3 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.27     4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? .        5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9AZU 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     44.767 
_cell.length_a_esd                 ? 
_cell.length_b                     70.573 
_cell.length_b_esd                 ? 
_cell.length_c                     105.192 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         9AZU 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9AZU 
_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             1.91 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          35.72 
_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              7.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'100 mM imidazole, pH 7.0, 2-15% isopropyl alcohol, 16-34% PEG3340, crystals soaked with 5-10 mM taniborbactam' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-02-11 
_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   0.92010 
_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                        'NSLS-II BEAMLINE 17-ID-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.92010 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID-1 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9AZU 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.73 
_reflns.d_resolution_low                               27.73 
_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                                     34824 
_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                           98.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.99 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.123 
_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                                    1.73 
_reflns_shell.d_res_low                                     1.78 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.7 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1957 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               5.7 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.91 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          76 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.616 
_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]                            -0.0000 
_refine.aniso_B[1][2]                            -0.0000 
_refine.aniso_B[1][3]                            -0.0000 
_refine.aniso_B[2][2]                            -0.0000 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            0.0000 
_refine.B_iso_max                                84.320 
_refine.B_iso_mean                               26.0970 
_refine.B_iso_min                                14.650 
_refine.correlation_coeff_Fo_to_Fc               0.9700 
_refine.correlation_coeff_Fo_to_Fc_free          0.9540 
_refine.details                                  
'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES      : REFINED INDIVIDUALLY' 
_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                                 9AZU 
_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                            1.7300 
_refine.ls_d_res_low                             27.7300 
_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                     33070 
_refine.ls_number_reflns_R_free                  1715 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.0700 
_refine.ls_percent_reflns_R_free                 4.9000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1683 
_refine.ls_R_factor_R_free                       0.2046 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1664 
_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                    MASK 
_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       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.1150 
_refine.pdbx_overall_ESU_R_Free                  0.1120 
_refine.pdbx_solvent_vdw_probe_radii             1.2000 
_refine.pdbx_solvent_ion_probe_radii             0.8000 
_refine.pdbx_solvent_shrinkage_radii             0.8000 
_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   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             2.7620 
_refine.overall_SU_ML                            0.0850 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         final 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.7300 
_refine_hist.d_res_low                        27.7300 
_refine_hist.number_atoms_solvent             300 
_refine_hist.number_atoms_total               3107 
_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       359 
_refine_hist.pdbx_B_iso_mean_ligand           43.46 
_refine_hist.pdbx_B_iso_mean_solvent          36.72 
_refine_hist.pdbx_number_atoms_protein        2779 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         28 
_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  0.013  2905 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.017  2754 ? r_bond_other_d         ? ? 
'X-RAY DIFFRACTION' ? 1.599  1.650  3958 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 1.424  1.580  6331 ? r_angle_other_deg      ? ? 
'X-RAY DIFFRACTION' ? 6.979  5.000  366  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 31.068 21.266 158  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 14.789 15.000 453  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 19.563 15.000 24   ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.083  0.200  359  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.010  0.020  3347 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  693  ? r_gen_planes_other     ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.7320 
_refine_ls_shell.d_res_low                        1.7770 
_refine_ls_shell.number_reflns_all                1954 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             95 
_refine_ls_shell.number_reflns_R_work             1859 
_refine_ls_shell.percent_reflns_obs               75.8800 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.R_factor_R_work                  0.2790 
_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   20 
_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                  0.3290 
# 
_struct.entry_id                     9AZU 
_struct.title                        'Crystal structure of PDC-3 beta-lactamase in complex with taniborbactam' 
_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        9AZU 
_struct_keywords.text            'Beta-lactamase, boronic acid inhibitor, HYDROLASE-ANTIBIOTIC complex' 
_struct_keywords.pdbx_keywords   HYDROLASE/ANTIBIOTIC 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q4H482_PSEAI 
_struct_ref.pdbx_db_accession          Q4H482 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MRDTRFPCLCGIAASTLLFATTPAIAGEAPADRLKALVDAAVQPVMKANDIPGLAVAISLKGEPHYFSYGLASKEDGRRV
TPETLFEIGSVSKTFTATLAGYALAQDKMRLDDRASQHWPALQGSRFDGISLLDLATYTAGGLPLQFPDSVQKDQAQIRD
YYRQWQPTYAPGSQRLYSNPSIGLFGYLAARSLGQPFERLMEQQVFPALGLEQTHLDVPEAALAQYAQGYGKDDRPLRVG
PGPLDAEGYGVKTSAADLLRFVDANLHPERLDRPWAQALDATHRGYYKVGDMTQGLGWEAYDWPISLKRLQAGNSTPMAL
QPHRIARLPAPQALEGQRLLNKTGSTNGFGAYVAFVPGRDLGLVILANRNYPNAERVKIAYAILSGLEQQGKVPLKR
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9AZU 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 397 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q4H482 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  397 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       -25 
_struct_ref_seq.pdbx_auth_seq_align_end       371 
# 
_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   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
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)' 0     ? 
1 MORE         0     ? 
1 'SSA (A^2)'  14640 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ALA A 29  ? ASN A 49  ? ALA A 3   ASN A 23  1 ? 21 
HELX_P HELX_P2  AA2 VAL A 91  ? GLN A 106 ? VAL A 65  GLN A 80  1 ? 16 
HELX_P HELX_P3  AA3 ARG A 114 ? GLN A 123 ? ARG A 88  GLN A 97  5 ? 10 
HELX_P HELX_P4  AA4 SER A 125 ? ILE A 130 ? SER A 99  ILE A 104 5 ? 6  
HELX_P HELX_P5  AA5 SER A 131 ? THR A 137 ? SER A 105 THR A 111 1 ? 7  
HELX_P HELX_P6  AA6 ASP A 154 ? TRP A 165 ? ASP A 128 TRP A 139 1 ? 12 
HELX_P HELX_P7  AA7 SER A 178 ? LEU A 193 ? SER A 152 LEU A 167 1 ? 16 
HELX_P HELX_P8  AA8 PRO A 196 ? GLN A 204 ? PRO A 170 GLN A 178 1 ? 9  
HELX_P HELX_P9  AA9 GLN A 204 ? LEU A 209 ? GLN A 178 LEU A 183 1 ? 6  
HELX_P HELX_P10 AB1 PRO A 219 ? TYR A 226 ? PRO A 193 TYR A 200 5 ? 8  
HELX_P HELX_P11 AB2 GLY A 231 ? ARG A 235 ? GLY A 205 ARG A 209 5 ? 5  
HELX_P HELX_P12 AB3 LEU A 244 ? TYR A 249 ? LEU A 218 TYR A 223 1 ? 6  
HELX_P HELX_P13 AB4 SER A 254 ? HIS A 267 ? SER A 228 HIS A 241 1 ? 14 
HELX_P HELX_P14 AB5 PRO A 268 ? LEU A 271 ? PRO A 242 LEU A 245 5 ? 4  
HELX_P HELX_P15 AB6 ASP A 272 ? ALA A 281 ? ASP A 246 ALA A 255 1 ? 10 
HELX_P HELX_P16 AB7 SER A 306 ? ASN A 314 ? SER A 280 ASN A 288 1 ? 9  
HELX_P HELX_P17 AB8 SER A 315 ? GLN A 321 ? SER A 289 GLN A 295 1 ? 7  
HELX_P HELX_P18 AB9 PRO A 357 ? ARG A 359 ? PRO A 331 ARG A 333 5 ? 3  
HELX_P HELX_P19 AC1 PRO A 372 ? LEU A 387 ? PRO A 346 LEU A 361 1 ? 16 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            covale1 
_struct_conn.conn_type_id                  covale 
_struct_conn.pdbx_leaving_atom_flag        none 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           SER 
_struct_conn.ptnr1_label_seq_id            90 
_struct_conn.ptnr1_label_atom_id           OG 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           B 
_struct_conn.ptnr2_label_comp_id           KJK 
_struct_conn.ptnr2_label_seq_id            . 
_struct_conn.ptnr2_label_atom_id           B07 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            SER 
_struct_conn.ptnr1_auth_seq_id             64 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            KJK 
_struct_conn.ptnr2_auth_seq_id             401 
_struct_conn.ptnr2_symmetry                1_555 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               1.517 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      KJK 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       . 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     SER 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      90 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       KJK 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        401 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      SER 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       64 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               B07 
_pdbx_modification_feature.modified_residue_id_linking_atom   OG 
_pdbx_modification_feature.modified_residue_id                SER 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        KJK 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Covalent chemical modification' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          TRP 
_struct_mon_prot_cis.label_seq_id           303 
_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           TRP 
_struct_mon_prot_cis.auth_seq_id            277 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    304 
_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    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     278 
_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       5.75 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 9 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA1 8 9 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 63  ? GLY A 70  ? GLU A 37  GLY A 44  
AA1 2 GLY A 53  ? LEU A 60  ? GLY A 27  LEU A 34  
AA1 3 LEU A 361 ? ALA A 367 ? LEU A 335 ALA A 341 
AA1 4 GLY A 350 ? VAL A 356 ? GLY A 324 VAL A 330 
AA1 5 ARG A 338 ? SER A 345 ? ARG A 312 SER A 319 
AA1 6 GLU A 299 ? ASP A 302 ? GLU A 273 ASP A 276 
AA1 7 MET A 292 ? GLN A 294 ? MET A 266 GLN A 268 
AA1 8 ARG A 284 ? VAL A 289 ? ARG A 258 VAL A 263 
AA1 9 ALA A 326 ? ALA A 333 ? ALA A 300 ALA A 307 
AA2 1 PHE A 86  ? GLU A 87  ? PHE A 60  GLU A 61  
AA2 2 LYS A 252 ? THR A 253 ? LYS A 226 THR A 227 
AA2 3 THR A 214 ? HIS A 215 ? THR A 188 HIS A 189 
AA3 1 GLN A 174 ? ARG A 175 ? GLN A 148 ARG A 149 
AA3 2 HIS A 323 ? ARG A 324 ? HIS A 297 ARG A 298 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O PHE A 67  ? O PHE A 41  N VAL A 56  ? N VAL A 30  
AA1 2 3 N ALA A 55  ? N ALA A 29  O LEU A 366 ? O LEU A 340 
AA1 3 4 O LEU A 361 ? O LEU A 335 N VAL A 356 ? N VAL A 330 
AA1 4 5 O ALA A 351 ? O ALA A 325 N GLY A 344 ? N GLY A 318 
AA1 5 6 O ASN A 341 ? O ASN A 315 N GLU A 299 ? N GLU A 273 
AA1 6 7 O ALA A 300 ? O ALA A 274 N THR A 293 ? N THR A 267 
AA1 7 8 O GLN A 294 ? O GLN A 268 N TYR A 286 ? N TYR A 260 
AA1 8 9 N GLY A 285 ? N GLY A 259 O GLN A 332 ? O GLN A 306 
AA2 1 2 N PHE A 86  ? N PHE A 60  O THR A 253 ? O THR A 227 
AA2 2 3 O LYS A 252 ? O LYS A 226 N HIS A 215 ? N HIS A 189 
AA3 1 2 N ARG A 175 ? N ARG A 149 O HIS A 323 ? O HIS A 297 
# 
_pdbx_entry_details.entry_id                   9AZU 
_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   Y 
# 
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 GLN A 178 ? ? -120.60 -55.70 
2 1 TYR A 223 ? ? -160.70 22.46  
# 
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 -25 ? A MET 1   
2  1 Y 1 A ARG -24 ? A ARG 2   
3  1 Y 1 A ASP -23 ? A ASP 3   
4  1 Y 1 A THR -22 ? A THR 4   
5  1 Y 1 A ARG -21 ? A ARG 5   
6  1 Y 1 A PHE -20 ? A PHE 6   
7  1 Y 1 A PRO -19 ? A PRO 7   
8  1 Y 1 A CYS -18 ? A CYS 8   
9  1 Y 1 A LEU -17 ? A LEU 9   
10 1 Y 1 A CYS -16 ? A CYS 10  
11 1 Y 1 A GLY -15 ? A GLY 11  
12 1 Y 1 A ILE -14 ? A ILE 12  
13 1 Y 1 A ALA -13 ? A ALA 13  
14 1 Y 1 A ALA -12 ? A ALA 14  
15 1 Y 1 A SER -11 ? A SER 15  
16 1 Y 1 A THR -10 ? A THR 16  
17 1 Y 1 A LEU -9  ? A LEU 17  
18 1 Y 1 A LEU -8  ? A LEU 18  
19 1 Y 1 A PHE -7  ? A PHE 19  
20 1 Y 1 A ALA -6  ? A ALA 20  
21 1 Y 1 A THR -5  ? A THR 21  
22 1 Y 1 A THR -4  ? A THR 22  
23 1 Y 1 A PRO -3  ? A PRO 23  
24 1 Y 1 A ALA -2  ? A ALA 24  
25 1 Y 1 A ILE -1  ? A ILE 25  
26 1 Y 1 A ALA 0   ? A ALA 26  
27 1 Y 1 A GLY 1   ? A GLY 27  
28 1 Y 1 A GLU 2   ? A GLU 28  
29 1 Y 1 A GLU 362 ? A GLU 388 
30 1 Y 1 A GLN 363 ? A GLN 389 
31 1 Y 1 A GLN 364 ? A GLN 390 
32 1 Y 1 A GLY 365 ? A GLY 391 
33 1 Y 1 A LYS 366 ? A LYS 392 
34 1 Y 1 A VAL 367 ? A VAL 393 
35 1 Y 1 A PRO 368 ? A PRO 394 
36 1 Y 1 A LEU 369 ? A LEU 395 
37 1 Y 1 A LYS 370 ? A LYS 396 
38 1 Y 1 A ARG 371 ? A ARG 397 
# 
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 
KJK B07  B N N 183 
KJK C10  C Y N 184 
KJK C11  C Y N 185 
KJK C12  C N N 186 
KJK C15  C Y N 187 
KJK C16  C Y N 188 
KJK C17  C Y N 189 
KJK C18  C Y N 190 
KJK C19  C N N 191 
KJK C20  C N R 192 
KJK C22  C N N 193 
KJK C23  C N N 194 
KJK C24  C N N 195 
KJK C25  C N N 196 
KJK C26  C N N 197 
KJK C27  C N N 198 
KJK C29  C N N 199 
KJK C30  C N N 200 
KJK C32  C N N 201 
KJK C33  C N N 202 
KJK N21  N N N 203 
KJK N28  N N N 204 
KJK N31  N N N 205 
KJK O08  O N N 206 
KJK O09  O N N 207 
KJK O13  O N N 208 
KJK O14  O N N 209 
KJK O34  O N N 210 
KJK H1   H N N 211 
KJK H2   H N N 212 
KJK H3   H N N 213 
KJK H4   H N N 214 
KJK H5   H N N 215 
KJK H6   H N N 216 
KJK H7   H N N 217 
KJK H8   H N N 218 
KJK H9   H N N 219 
KJK H10  H N N 220 
KJK H11  H N N 221 
KJK H12  H N N 222 
KJK H13  H N N 223 
KJK H14  H N N 224 
KJK H15  H N N 225 
KJK H16  H N N 226 
KJK H17  H N N 227 
KJK H18  H N N 228 
KJK H19  H N N 229 
KJK H20  H N N 230 
KJK H21  H N N 231 
KJK H22  H N N 232 
KJK H23  H N N 233 
KJK H24  H N N 234 
KJK H26  H N N 235 
KJK H27  H N N 236 
KJK H29  H N N 237 
KJK H30  H N N 238 
LEU N    N N N 239 
LEU CA   C N S 240 
LEU C    C N N 241 
LEU O    O N N 242 
LEU CB   C N N 243 
LEU CG   C N N 244 
LEU CD1  C N N 245 
LEU CD2  C N N 246 
LEU OXT  O N N 247 
LEU H    H N N 248 
LEU H2   H N N 249 
LEU HA   H N N 250 
LEU HB2  H N N 251 
LEU HB3  H N N 252 
LEU HG   H N N 253 
LEU HD11 H N N 254 
LEU HD12 H N N 255 
LEU HD13 H N N 256 
LEU HD21 H N N 257 
LEU HD22 H N N 258 
LEU HD23 H N N 259 
LEU HXT  H N N 260 
LYS N    N N N 261 
LYS CA   C N S 262 
LYS C    C N N 263 
LYS O    O N N 264 
LYS CB   C N N 265 
LYS CG   C N N 266 
LYS CD   C N N 267 
LYS CE   C N N 268 
LYS NZ   N N N 269 
LYS OXT  O N N 270 
LYS H    H N N 271 
LYS H2   H N N 272 
LYS HA   H N N 273 
LYS HB2  H N N 274 
LYS HB3  H N N 275 
LYS HG2  H N N 276 
LYS HG3  H N N 277 
LYS HD2  H N N 278 
LYS HD3  H N N 279 
LYS HE2  H N N 280 
LYS HE3  H N N 281 
LYS HZ1  H N N 282 
LYS HZ2  H N N 283 
LYS HZ3  H N N 284 
LYS HXT  H N N 285 
MET N    N N N 286 
MET CA   C N S 287 
MET C    C N N 288 
MET O    O N N 289 
MET CB   C N N 290 
MET CG   C N N 291 
MET SD   S N N 292 
MET CE   C N N 293 
MET OXT  O N N 294 
MET H    H N N 295 
MET H2   H N N 296 
MET HA   H N N 297 
MET HB2  H N N 298 
MET HB3  H N N 299 
MET HG2  H N N 300 
MET HG3  H N N 301 
MET HE1  H N N 302 
MET HE2  H N N 303 
MET HE3  H N N 304 
MET HXT  H N N 305 
PHE N    N N N 306 
PHE CA   C N S 307 
PHE C    C N N 308 
PHE O    O N N 309 
PHE CB   C N N 310 
PHE CG   C Y N 311 
PHE CD1  C Y N 312 
PHE CD2  C Y N 313 
PHE CE1  C Y N 314 
PHE CE2  C Y N 315 
PHE CZ   C Y N 316 
PHE OXT  O N N 317 
PHE H    H N N 318 
PHE H2   H N N 319 
PHE HA   H N N 320 
PHE HB2  H N N 321 
PHE HB3  H N N 322 
PHE HD1  H N N 323 
PHE HD2  H N N 324 
PHE HE1  H N N 325 
PHE HE2  H N N 326 
PHE HZ   H N N 327 
PHE HXT  H N N 328 
PRO N    N N N 329 
PRO CA   C N S 330 
PRO C    C N N 331 
PRO O    O N N 332 
PRO CB   C N N 333 
PRO CG   C N N 334 
PRO CD   C N N 335 
PRO OXT  O N N 336 
PRO H    H N N 337 
PRO HA   H N N 338 
PRO HB2  H N N 339 
PRO HB3  H N N 340 
PRO HG2  H N N 341 
PRO HG3  H N N 342 
PRO HD2  H N N 343 
PRO HD3  H N N 344 
PRO HXT  H N N 345 
SER N    N N N 346 
SER CA   C N S 347 
SER C    C N N 348 
SER O    O N N 349 
SER CB   C N N 350 
SER OG   O N N 351 
SER OXT  O N N 352 
SER H    H N N 353 
SER H2   H N N 354 
SER HA   H N N 355 
SER HB2  H N N 356 
SER HB3  H N N 357 
SER HG   H N N 358 
SER HXT  H N N 359 
THR N    N N N 360 
THR CA   C N S 361 
THR C    C N N 362 
THR O    O N N 363 
THR CB   C N R 364 
THR OG1  O N N 365 
THR CG2  C N N 366 
THR OXT  O N N 367 
THR H    H N N 368 
THR H2   H N N 369 
THR HA   H N N 370 
THR HB   H N N 371 
THR HG1  H N N 372 
THR HG21 H N N 373 
THR HG22 H N N 374 
THR HG23 H N N 375 
THR HXT  H N N 376 
TRP N    N N N 377 
TRP CA   C N S 378 
TRP C    C N N 379 
TRP O    O N N 380 
TRP CB   C N N 381 
TRP CG   C Y N 382 
TRP CD1  C Y N 383 
TRP CD2  C Y N 384 
TRP NE1  N Y N 385 
TRP CE2  C Y N 386 
TRP CE3  C Y N 387 
TRP CZ2  C Y N 388 
TRP CZ3  C Y N 389 
TRP CH2  C Y N 390 
TRP OXT  O N N 391 
TRP H    H N N 392 
TRP H2   H N N 393 
TRP HA   H N N 394 
TRP HB2  H N N 395 
TRP HB3  H N N 396 
TRP HD1  H N N 397 
TRP HE1  H N N 398 
TRP HE3  H N N 399 
TRP HZ2  H N N 400 
TRP HZ3  H N N 401 
TRP HH2  H N N 402 
TRP HXT  H N N 403 
TYR N    N N N 404 
TYR CA   C N S 405 
TYR C    C N N 406 
TYR O    O N N 407 
TYR CB   C N N 408 
TYR CG   C Y N 409 
TYR CD1  C Y N 410 
TYR CD2  C Y N 411 
TYR CE1  C Y N 412 
TYR CE2  C Y N 413 
TYR CZ   C Y N 414 
TYR OH   O N N 415 
TYR OXT  O N N 416 
TYR H    H N N 417 
TYR H2   H N N 418 
TYR HA   H N N 419 
TYR HB2  H N N 420 
TYR HB3  H N N 421 
TYR HD1  H N N 422 
TYR HD2  H N N 423 
TYR HE1  H N N 424 
TYR HE2  H N N 425 
TYR HH   H N N 426 
TYR HXT  H N N 427 
VAL N    N N N 428 
VAL CA   C N S 429 
VAL C    C N N 430 
VAL O    O N N 431 
VAL CB   C N N 432 
VAL CG1  C N N 433 
VAL CG2  C N N 434 
VAL OXT  O N N 435 
VAL H    H N N 436 
VAL H2   H N N 437 
VAL HA   H N N 438 
VAL HB   H N N 439 
VAL HG11 H N N 440 
VAL HG12 H N N 441 
VAL HG13 H N N 442 
VAL HG21 H N N 443 
VAL HG22 H N N 444 
VAL HG23 H N N 445 
VAL HXT  H N N 446 
# 
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 
KJK C33 C32  sing N N 173 
KJK C33 C24  sing N N 174 
KJK C32 C27  sing N N 175 
KJK C23 C24  sing N N 176 
KJK C23 C22  sing N N 177 
KJK C27 N28  sing N N 178 
KJK C27 C26  sing N N 179 
KJK C24 C25  sing N N 180 
KJK N28 C29  sing N N 181 
KJK C25 C26  sing N N 182 
KJK C29 C30  sing N N 183 
KJK O08 B07  sing N N 184 
KJK C22 N21  sing N N 185 
KJK C22 O34  doub N N 186 
KJK O13 C12  doub N N 187 
KJK N21 C20  sing N N 188 
KJK C30 N31  sing N N 189 
KJK B07 C20  sing N N 190 
KJK B07 O09  sing N N 191 
KJK C20 C19  sing N N 192 
KJK C12 C11  sing N N 193 
KJK C12 O14  sing N N 194 
KJK O09 C10  sing N N 195 
KJK C11 C10  doub Y N 196 
KJK C11 C15  sing Y N 197 
KJK C10 C18  sing Y N 198 
KJK C15 C16  doub Y N 199 
KJK C18 C19  sing N N 200 
KJK C18 C17  doub Y N 201 
KJK C16 C17  sing Y N 202 
KJK C15 H1   sing N N 203 
KJK C16 H2   sing N N 204 
KJK C17 H3   sing N N 205 
KJK C19 H4   sing N N 206 
KJK C19 H5   sing N N 207 
KJK C20 H6   sing N N 208 
KJK C23 H7   sing N N 209 
KJK C23 H8   sing N N 210 
KJK C24 H9   sing N N 211 
KJK C25 H10  sing N N 212 
KJK C25 H11  sing N N 213 
KJK C26 H12  sing N N 214 
KJK C26 H13  sing N N 215 
KJK C27 H14  sing N N 216 
KJK C29 H15  sing N N 217 
KJK C29 H16  sing N N 218 
KJK C30 H17  sing N N 219 
KJK C30 H18  sing N N 220 
KJK C32 H19  sing N N 221 
KJK C32 H20  sing N N 222 
KJK C33 H21  sing N N 223 
KJK C33 H22  sing N N 224 
KJK N21 H23  sing N N 225 
KJK N28 H24  sing N N 226 
KJK N31 H26  sing N N 227 
KJK N31 H27  sing N N 228 
KJK O08 H29  sing N N 229 
KJK O14 H30  sing N N 230 
LEU N   CA   sing N N 231 
LEU N   H    sing N N 232 
LEU N   H2   sing N N 233 
LEU CA  C    sing N N 234 
LEU CA  CB   sing N N 235 
LEU CA  HA   sing N N 236 
LEU C   O    doub N N 237 
LEU C   OXT  sing N N 238 
LEU CB  CG   sing N N 239 
LEU CB  HB2  sing N N 240 
LEU CB  HB3  sing N N 241 
LEU CG  CD1  sing N N 242 
LEU CG  CD2  sing N N 243 
LEU CG  HG   sing N N 244 
LEU CD1 HD11 sing N N 245 
LEU CD1 HD12 sing N N 246 
LEU CD1 HD13 sing N N 247 
LEU CD2 HD21 sing N N 248 
LEU CD2 HD22 sing N N 249 
LEU CD2 HD23 sing N N 250 
LEU OXT HXT  sing N N 251 
LYS N   CA   sing N N 252 
LYS N   H    sing N N 253 
LYS N   H2   sing N N 254 
LYS CA  C    sing N N 255 
LYS CA  CB   sing N N 256 
LYS CA  HA   sing N N 257 
LYS C   O    doub N N 258 
LYS C   OXT  sing N N 259 
LYS CB  CG   sing N N 260 
LYS CB  HB2  sing N N 261 
LYS CB  HB3  sing N N 262 
LYS CG  CD   sing N N 263 
LYS CG  HG2  sing N N 264 
LYS CG  HG3  sing N N 265 
LYS CD  CE   sing N N 266 
LYS CD  HD2  sing N N 267 
LYS CD  HD3  sing N N 268 
LYS CE  NZ   sing N N 269 
LYS CE  HE2  sing N N 270 
LYS CE  HE3  sing N N 271 
LYS NZ  HZ1  sing N N 272 
LYS NZ  HZ2  sing N N 273 
LYS NZ  HZ3  sing N N 274 
LYS OXT HXT  sing N N 275 
MET N   CA   sing N N 276 
MET N   H    sing N N 277 
MET N   H2   sing N N 278 
MET CA  C    sing N N 279 
MET CA  CB   sing N N 280 
MET CA  HA   sing N N 281 
MET C   O    doub N N 282 
MET C   OXT  sing N N 283 
MET CB  CG   sing N N 284 
MET CB  HB2  sing N N 285 
MET CB  HB3  sing N N 286 
MET CG  SD   sing N N 287 
MET CG  HG2  sing N N 288 
MET CG  HG3  sing N N 289 
MET SD  CE   sing N N 290 
MET CE  HE1  sing N N 291 
MET CE  HE2  sing N N 292 
MET CE  HE3  sing N N 293 
MET OXT HXT  sing N N 294 
PHE N   CA   sing N N 295 
PHE N   H    sing N N 296 
PHE N   H2   sing N N 297 
PHE CA  C    sing N N 298 
PHE CA  CB   sing N N 299 
PHE CA  HA   sing N N 300 
PHE C   O    doub N N 301 
PHE C   OXT  sing N N 302 
PHE CB  CG   sing N N 303 
PHE CB  HB2  sing N N 304 
PHE CB  HB3  sing N N 305 
PHE CG  CD1  doub Y N 306 
PHE CG  CD2  sing Y N 307 
PHE CD1 CE1  sing Y N 308 
PHE CD1 HD1  sing N N 309 
PHE CD2 CE2  doub Y N 310 
PHE CD2 HD2  sing N N 311 
PHE CE1 CZ   doub Y N 312 
PHE CE1 HE1  sing N N 313 
PHE CE2 CZ   sing Y N 314 
PHE CE2 HE2  sing N N 315 
PHE CZ  HZ   sing N N 316 
PHE OXT HXT  sing N N 317 
PRO N   CA   sing N N 318 
PRO N   CD   sing N N 319 
PRO N   H    sing N N 320 
PRO CA  C    sing N N 321 
PRO CA  CB   sing N N 322 
PRO CA  HA   sing N N 323 
PRO C   O    doub N N 324 
PRO C   OXT  sing N N 325 
PRO CB  CG   sing N N 326 
PRO CB  HB2  sing N N 327 
PRO CB  HB3  sing N N 328 
PRO CG  CD   sing N N 329 
PRO CG  HG2  sing N N 330 
PRO CG  HG3  sing N N 331 
PRO CD  HD2  sing N N 332 
PRO CD  HD3  sing N N 333 
PRO OXT HXT  sing N N 334 
SER N   CA   sing N N 335 
SER N   H    sing N N 336 
SER N   H2   sing N N 337 
SER CA  C    sing N N 338 
SER CA  CB   sing N N 339 
SER CA  HA   sing N N 340 
SER C   O    doub N N 341 
SER C   OXT  sing N N 342 
SER CB  OG   sing N N 343 
SER CB  HB2  sing N N 344 
SER CB  HB3  sing N N 345 
SER OG  HG   sing N N 346 
SER OXT HXT  sing N N 347 
THR N   CA   sing N N 348 
THR N   H    sing N N 349 
THR N   H2   sing N N 350 
THR CA  C    sing N N 351 
THR CA  CB   sing N N 352 
THR CA  HA   sing N N 353 
THR C   O    doub N N 354 
THR C   OXT  sing N N 355 
THR CB  OG1  sing N N 356 
THR CB  CG2  sing N N 357 
THR CB  HB   sing N N 358 
THR OG1 HG1  sing N N 359 
THR CG2 HG21 sing N N 360 
THR CG2 HG22 sing N N 361 
THR CG2 HG23 sing N N 362 
THR OXT HXT  sing N N 363 
TRP N   CA   sing N N 364 
TRP N   H    sing N N 365 
TRP N   H2   sing N N 366 
TRP CA  C    sing N N 367 
TRP CA  CB   sing N N 368 
TRP CA  HA   sing N N 369 
TRP C   O    doub N N 370 
TRP C   OXT  sing N N 371 
TRP CB  CG   sing N N 372 
TRP CB  HB2  sing N N 373 
TRP CB  HB3  sing N N 374 
TRP CG  CD1  doub Y N 375 
TRP CG  CD2  sing Y N 376 
TRP CD1 NE1  sing Y N 377 
TRP CD1 HD1  sing N N 378 
TRP CD2 CE2  doub Y N 379 
TRP CD2 CE3  sing Y N 380 
TRP NE1 CE2  sing Y N 381 
TRP NE1 HE1  sing N N 382 
TRP CE2 CZ2  sing Y N 383 
TRP CE3 CZ3  doub Y N 384 
TRP CE3 HE3  sing N N 385 
TRP CZ2 CH2  doub Y N 386 
TRP CZ2 HZ2  sing N N 387 
TRP CZ3 CH2  sing Y N 388 
TRP CZ3 HZ3  sing N N 389 
TRP CH2 HH2  sing N N 390 
TRP OXT HXT  sing N N 391 
TYR N   CA   sing N N 392 
TYR N   H    sing N N 393 
TYR N   H2   sing N N 394 
TYR CA  C    sing N N 395 
TYR CA  CB   sing N N 396 
TYR CA  HA   sing N N 397 
TYR C   O    doub N N 398 
TYR C   OXT  sing N N 399 
TYR CB  CG   sing N N 400 
TYR CB  HB2  sing N N 401 
TYR CB  HB3  sing N N 402 
TYR CG  CD1  doub Y N 403 
TYR CG  CD2  sing Y N 404 
TYR CD1 CE1  sing Y N 405 
TYR CD1 HD1  sing N N 406 
TYR CD2 CE2  doub Y N 407 
TYR CD2 HD2  sing N N 408 
TYR CE1 CZ   doub Y N 409 
TYR CE1 HE1  sing N N 410 
TYR CE2 CZ   sing Y N 411 
TYR CE2 HE2  sing N N 412 
TYR CZ  OH   sing N N 413 
TYR OH  HH   sing N N 414 
TYR OXT HXT  sing N N 415 
VAL N   CA   sing N N 416 
VAL N   H    sing N N 417 
VAL N   H2   sing N N 418 
VAL CA  C    sing N N 419 
VAL CA  CB   sing N N 420 
VAL CA  HA   sing N N 421 
VAL C   O    doub N N 422 
VAL C   OXT  sing N N 423 
VAL CB  CG1  sing N N 424 
VAL CB  CG2  sing N N 425 
VAL CB  HB   sing N N 426 
VAL CG1 HG11 sing N N 427 
VAL CG1 HG12 sing N N 428 
VAL CG1 HG13 sing N N 429 
VAL CG2 HG21 sing N N 430 
VAL CG2 HG22 sing N N 431 
VAL CG2 HG23 sing N N 432 
VAL OXT HXT  sing N N 433 
# 
_pdbx_audit_support.funding_organization   'VenatoRx Pharmaceuticals' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4GZB 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9AZU 
_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]   0.022338 
_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]   0.014170 
_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]   0.009506 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
B 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ALA A 1 29  ? 4.920   -11.421 12.506  1.00 61.60 ?  3   ALA A N   1 
ATOM   2    C CA  . ALA A 1 29  ? 6.112   -10.756 11.896  1.00 66.13 ?  3   ALA A CA  1 
ATOM   3    C C   . ALA A 1 29  ? 5.847   -10.444 10.419  1.00 67.81 ?  3   ALA A C   1 
ATOM   4    O O   . ALA A 1 29  ? 6.108   -9.319  9.996   1.00 64.87 ?  3   ALA A O   1 
ATOM   5    C CB  . ALA A 1 29  ? 7.368   -11.583 12.102  1.00 60.56 ?  3   ALA A CB  1 
ATOM   6    N N   . PRO A 1 30  ? 5.341   -11.389 9.580   1.00 66.26 ?  4   PRO A N   1 
ATOM   7    C CA  . PRO A 1 30  ? 5.100   -11.113 8.157   1.00 65.20 ?  4   PRO A CA  1 
ATOM   8    C C   . PRO A 1 30  ? 4.067   -10.010 7.868   1.00 59.80 ?  4   PRO A C   1 
ATOM   9    O O   . PRO A 1 30  ? 4.290   -9.246  6.944   1.00 50.77 ?  4   PRO A O   1 
ATOM   10   C CB  . PRO A 1 30  ? 4.581   -12.441 7.587   1.00 65.92 ?  4   PRO A CB  1 
ATOM   11   C CG  . PRO A 1 30  ? 5.111   -13.474 8.557   1.00 68.52 ?  4   PRO A CG  1 
ATOM   12   C CD  . PRO A 1 30  ? 5.044   -12.792 9.910   1.00 68.71 ?  4   PRO A CD  1 
ATOM   13   N N   . ALA A 1 31  ? 2.964   -9.968  8.627   1.00 54.73 ?  5   ALA A N   1 
ATOM   14   C CA  . ALA A 1 31  ? 2.017   -8.828  8.637   1.00 52.10 ?  5   ALA A CA  1 
ATOM   15   C C   . ALA A 1 31  ? 2.796   -7.549  8.975   1.00 54.34 ?  5   ALA A C   1 
ATOM   16   O O   . ALA A 1 31  ? 2.654   -6.576  8.227   1.00 49.67 ?  5   ALA A O   1 
ATOM   17   C CB  . ALA A 1 31  ? 0.894   -9.058  9.612   1.00 45.87 ?  5   ALA A CB  1 
ATOM   18   N N   . ASP A 1 32  ? 3.616   -7.566  10.033  1.00 49.47 ?  6   ASP A N   1 
ATOM   19   C CA  . ASP A 1 32  ? 4.380   -6.378  10.501  1.00 50.40 ?  6   ASP A CA  1 
ATOM   20   C C   . ASP A 1 32  ? 5.400   -5.981  9.441   1.00 49.40 ?  6   ASP A C   1 
ATOM   21   O O   . ASP A 1 32  ? 5.530   -4.778  9.217   1.00 46.28 ?  6   ASP A O   1 
ATOM   22   C CB  . ASP A 1 32  ? 5.123   -6.606  11.815  1.00 53.71 ?  6   ASP A CB  1 
ATOM   23   C CG  . ASP A 1 32  ? 4.206   -7.082  12.922  1.00 60.18 ?  6   ASP A CG  1 
ATOM   24   O OD1 . ASP A 1 32  ? 3.852   -8.285  12.903  1.00 60.27 ?  6   ASP A OD1 1 
ATOM   25   O OD2 . ASP A 1 32  ? 3.832   -6.245  13.764  1.00 61.30 ?  6   ASP A OD2 1 
ATOM   26   N N   . ARG A 1 33  ? 6.119   -6.952  8.875   1.00 43.25 ?  7   ARG A N   1 
ATOM   27   C CA  . ARG A 1 33  ? 7.125   -6.735  7.804   1.00 47.64 ?  7   ARG A CA  1 
ATOM   28   C C   . ARG A 1 33  ? 6.416   -6.043  6.632   1.00 38.20 ?  7   ARG A C   1 
ATOM   29   O O   . ARG A 1 33  ? 6.917   -5.013  6.166   1.00 35.61 ?  7   ARG A O   1 
ATOM   30   C CB  . ARG A 1 33  ? 7.766   -8.067  7.385   1.00 51.79 ?  7   ARG A CB  1 
ATOM   31   C CG  . ARG A 1 33  ? 9.019   -7.921  6.526   1.00 63.39 ?  7   ARG A CG  1 
ATOM   32   C CD  . ARG A 1 33  ? 9.773   -9.223  6.278   1.00 67.70 ?  7   ARG A CD  1 
ATOM   33   N NE  . ARG A 1 33  ? 9.792   -10.064 7.476   1.00 72.64 ?  7   ARG A NE  1 
ATOM   34   C CZ  . ARG A 1 33  ? 9.310   -11.312 7.575   1.00 80.82 ?  7   ARG A CZ  1 
ATOM   35   N NH1 . ARG A 1 33  ? 8.784   -11.934 6.529   1.00 75.25 ?  7   ARG A NH1 1 
ATOM   36   N NH2 . ARG A 1 33  ? 9.370   -11.945 8.737   1.00 78.34 ?  7   ARG A NH2 1 
ATOM   37   N N   . LEU A 1 34  ? 5.258   -6.568  6.227   1.00 34.36 ?  8   LEU A N   1 
ATOM   38   C CA  . LEU A 1 34  ? 4.533   -6.098  5.023   1.00 36.65 ?  8   LEU A CA  1 
ATOM   39   C C   . LEU A 1 34  ? 3.967   -4.701  5.284   1.00 35.75 ?  8   LEU A C   1 
ATOM   40   O O   . LEU A 1 34  ? 4.149   -3.800  4.422   1.00 31.22 ?  8   LEU A O   1 
ATOM   41   C CB  . LEU A 1 34  ? 3.431   -7.094  4.677   1.00 39.87 ?  8   LEU A CB  1 
ATOM   42   C CG  . LEU A 1 34  ? 2.670   -6.809  3.383   1.00 44.74 ?  8   LEU A CG  1 
ATOM   43   C CD1 . LEU A 1 34  ? 3.611   -6.542  2.210   1.00 42.79 ?  8   LEU A CD1 1 
ATOM   44   C CD2 . LEU A 1 34  ? 1.746   -7.971  3.061   1.00 45.98 ?  8   LEU A CD2 1 
ATOM   45   N N   . LYS A 1 35  ? 3.397   -4.491  6.467   1.00 34.16 ?  9   LYS A N   1 
ATOM   46   C CA  . LYS A 1 35  ? 2.908   -3.146  6.877   1.00 38.29 ?  9   LYS A CA  1 
ATOM   47   C C   . LYS A 1 35  ? 4.121   -2.225  6.957   1.00 37.32 ?  9   LYS A C   1 
ATOM   48   O O   . LYS A 1 35  ? 4.006   -1.127  6.416   1.00 34.70 ?  9   LYS A O   1 
ATOM   49   C CB  . LYS A 1 35  ? 2.064   -3.178  8.159   1.00 42.49 ?  9   LYS A CB  1 
ATOM   50   C CG  . LYS A 1 35  ? 1.652   -1.812  8.716   1.00 48.31 ?  9   LYS A CG  1 
ATOM   51   C CD  . LYS A 1 35  ? 0.153   -1.548  8.752   1.00 56.66 ?  9   LYS A CD  1 
ATOM   52   C CE  . LYS A 1 35  ? -0.328  -0.699  9.922   1.00 60.07 ?  9   LYS A CE  1 
ATOM   53   N NZ  . LYS A 1 35  ? 0.655   0.334   10.340  1.00 61.56 ?  9   LYS A NZ  1 
ATOM   54   N N   . ALA A 1 36  ? 5.268   -2.667  7.500   1.00 33.52 ?  10  ALA A N   1 
ATOM   55   C CA  . ALA A 1 36  ? 6.479   -1.809  7.586   1.00 35.88 ?  10  ALA A CA  1 
ATOM   56   C C   . ALA A 1 36  ? 6.919   -1.379  6.174   1.00 28.01 ?  10  ALA A C   1 
ATOM   57   O O   . ALA A 1 36  ? 7.297   -0.216  6.003   1.00 29.00 ?  10  ALA A O   1 
ATOM   58   C CB  . ALA A 1 36  ? 7.616   -2.496  8.334   1.00 34.60 ?  10  ALA A CB  1 
ATOM   59   N N   . LEU A 1 37  ? 6.957   -2.323  5.243   1.00 28.50 ?  11  LEU A N   1 
ATOM   60   C CA  . LEU A 1 37  ? 7.425   -2.098  3.851   1.00 28.43 ?  11  LEU A CA  1 
ATOM   61   C C   . LEU A 1 37  ? 6.527   -1.059  3.177   1.00 27.87 ?  11  LEU A C   1 
ATOM   62   O O   . LEU A 1 37  ? 7.017   -0.067  2.540   1.00 26.40 ?  11  LEU A O   1 
ATOM   63   C CB  . LEU A 1 37  ? 7.378   -3.446  3.123   1.00 30.11 ?  11  LEU A CB  1 
ATOM   64   C CG  . LEU A 1 37  ? 7.528   -3.353  1.604   1.00 31.01 ?  11  LEU A CG  1 
ATOM   65   C CD1 . LEU A 1 37  ? 8.921   -2.855  1.228   1.00 32.05 ?  11  LEU A CD1 1 
ATOM   66   C CD2 . LEU A 1 37  ? 7.224   -4.679  0.965   1.00 33.78 ?  11  LEU A CD2 1 
ATOM   67   N N   . VAL A 1 38  ? 5.214   -1.242  3.317   1.00 25.21 ?  12  VAL A N   1 
ATOM   68   C CA  . VAL A 1 38  ? 4.250   -0.386  2.587   1.00 22.81 ?  12  VAL A CA  1 
ATOM   69   C C   . VAL A 1 38  ? 4.234   0.999   3.249   1.00 23.09 ?  12  VAL A C   1 
ATOM   70   O O   . VAL A 1 38  ? 4.307   2.006   2.507   1.00 20.46 ?  12  VAL A O   1 
ATOM   71   C CB  . VAL A 1 38  ? 2.855   -1.021  2.509   1.00 23.38 ?  12  VAL A CB  1 
ATOM   72   C CG1 . VAL A 1 38  ? 1.894   -0.050  1.861   1.00 25.21 ?  12  VAL A CG1 1 
ATOM   73   C CG2 . VAL A 1 38  ? 2.856   -2.325  1.733   1.00 25.51 ?  12  VAL A CG2 1 
ATOM   74   N N   . ASP A 1 39  ? 4.254   1.055   4.589   1.00 23.96 ?  13  ASP A N   1 
ATOM   75   C CA  . ASP A 1 39  ? 4.318   2.322   5.354   1.00 24.30 ?  13  ASP A CA  1 
ATOM   76   C C   . ASP A 1 39  ? 5.547   3.125   4.922   1.00 23.32 ?  13  ASP A C   1 
ATOM   77   O O   . ASP A 1 39  ? 5.405   4.307   4.633   1.00 22.77 ?  13  ASP A O   1 
ATOM   78   C CB  . ASP A 1 39  ? 4.368   2.062   6.863   1.00 25.98 ?  13  ASP A CB  1 
ATOM   79   C CG  . ASP A 1 39  ? 3.035   1.680   7.486   1.00 29.76 ?  13  ASP A CG  1 
ATOM   80   O OD1 . ASP A 1 39  ? 2.040   1.654   6.772   1.00 27.75 ?  13  ASP A OD1 1 
ATOM   81   O OD2 . ASP A 1 39  ? 3.010   1.423   8.707   1.00 30.20 ?  13  ASP A OD2 1 
ATOM   82   N N   . ALA A 1 40  ? 6.699   2.470   4.835   1.00 23.30 ?  14  ALA A N   1 
ATOM   83   C CA  . ALA A 1 40  ? 7.995   3.101   4.497   1.00 25.32 ?  14  ALA A CA  1 
ATOM   84   C C   . ALA A 1 40  ? 7.916   3.654   3.069   1.00 24.56 ?  14  ALA A C   1 
ATOM   85   O O   . ALA A 1 40  ? 8.509   4.685   2.806   1.00 26.11 ?  14  ALA A O   1 
ATOM   86   C CB  . ALA A 1 40  ? 9.110   2.095   4.650   1.00 26.52 ?  14  ALA A CB  1 
ATOM   87   N N   . ALA A 1 41  ? 7.143   3.017   2.185   1.00 23.10 ?  15  ALA A N   1 
ATOM   88   C CA  . ALA A 1 41  ? 7.023   3.463   0.785   1.00 22.15 ?  15  ALA A CA  1 
ATOM   89   C C   . ALA A 1 41  ? 6.025   4.616   0.722   1.00 23.26 ?  15  ALA A C   1 
ATOM   90   O O   . ALA A 1 41  ? 6.306   5.636   0.024   1.00 21.23 ?  15  ALA A O   1 
ATOM   91   C CB  . ALA A 1 41  ? 6.641   2.311   -0.103  1.00 23.27 ?  15  ALA A CB  1 
ATOM   92   N N   . VAL A 1 42  ? 4.888   4.456   1.397   1.00 22.42 ?  16  VAL A N   1 
ATOM   93   C CA  . VAL A 1 42  ? 3.745   5.392   1.246   1.00 22.31 ?  16  VAL A CA  1 
ATOM   94   C C   . VAL A 1 42  ? 3.948   6.663   2.071   1.00 22.49 ?  16  VAL A C   1 
ATOM   95   O O   . VAL A 1 42  ? 3.687   7.763   1.546   1.00 24.61 ?  16  VAL A O   1 
ATOM   96   C CB  . VAL A 1 42  ? 2.438   4.700   1.654   1.00 22.94 ?  16  VAL A CB  1 
ATOM   97   C CG1 . VAL A 1 42  ? 1.287   5.690   1.770   1.00 22.48 ?  16  VAL A CG1 1 
ATOM   98   C CG2 . VAL A 1 42  ? 2.094   3.575   0.706   1.00 23.72 ?  16  VAL A CG2 1 
ATOM   99   N N   . GLN A 1 43  ? 4.254   6.532   3.347   1.00 23.96 ?  17  GLN A N   1 
ATOM   100  C CA  . GLN A 1 43  ? 4.095   7.683   4.289   1.00 23.88 ?  17  GLN A CA  1 
ATOM   101  C C   . GLN A 1 43  ? 4.899   8.893   3.817   1.00 22.89 ?  17  GLN A C   1 
ATOM   102  O O   . GLN A 1 43  ? 4.374   10.006  3.712   1.00 23.03 ?  17  GLN A O   1 
ATOM   103  C CB  . GLN A 1 43  ? 4.383   7.187   5.707   1.00 29.27 ?  17  GLN A CB  1 
ATOM   104  C CG  . GLN A 1 43  ? 3.277   6.252   6.193   1.00 34.03 ?  17  GLN A CG  1 
ATOM   105  C CD  . GLN A 1 43  ? 3.418   5.761   7.617   1.00 39.53 ?  17  GLN A CD  1 
ATOM   106  O OE1 . GLN A 1 43  ? 2.427   5.497   8.293   1.00 44.83 ?  17  GLN A OE1 1 
ATOM   107  N NE2 . GLN A 1 43  ? 4.645   5.637   8.085   1.00 39.57 ?  17  GLN A NE2 1 
ATOM   108  N N   . PRO A 1 44  ? 6.197   8.766   3.486   1.00 23.77 ?  18  PRO A N   1 
ATOM   109  C CA  . PRO A 1 44  ? 6.955   9.935   3.033   1.00 24.23 ?  18  PRO A CA  1 
ATOM   110  C C   . PRO A 1 44  ? 6.400   10.575  1.756   1.00 24.00 ?  18  PRO A C   1 
ATOM   111  O O   . PRO A 1 44  ? 6.341   11.781  1.640   1.00 23.41 ?  18  PRO A O   1 
ATOM   112  C CB  . PRO A 1 44  ? 8.382   9.423   2.782   1.00 26.02 ?  18  PRO A CB  1 
ATOM   113  C CG  . PRO A 1 44  ? 8.389   7.954   3.165   1.00 27.86 ?  18  PRO A CG  1 
ATOM   114  C CD  . PRO A 1 44  ? 7.016   7.567   3.659   1.00 25.50 ?  18  PRO A CD  1 
ATOM   115  N N   . VAL A 1 45  ? 5.924   9.759   0.809   1.00 24.94 ?  19  VAL A N   1 
ATOM   116  C CA  . VAL A 1 45  ? 5.354   10.313  -0.453  1.00 21.82 ?  19  VAL A CA  1 
ATOM   117  C C   . VAL A 1 45  ? 4.034   11.035  -0.167  1.00 20.62 ?  19  VAL A C   1 
ATOM   118  O O   . VAL A 1 45  ? 3.760   12.061  -0.804  1.00 21.67 ?  19  VAL A O   1 
ATOM   119  C CB  . VAL A 1 45  ? 5.227   9.196   -1.514  1.00 22.77 ?  19  VAL A CB  1 
ATOM   120  C CG1 . VAL A 1 45  ? 4.592   9.716   -2.782  1.00 25.53 ?  19  VAL A CG1 1 
ATOM   121  C CG2 . VAL A 1 45  ? 6.599   8.624   -1.806  1.00 23.81 ?  19  VAL A CG2 1 
ATOM   122  N N   . MET A 1 46  ? 3.202   10.520  0.727   1.00 24.90 ?  20  MET A N   1 
ATOM   123  C CA  . MET A 1 46  ? 1.970   11.242  1.158   1.00 26.98 ?  20  MET A CA  1 
ATOM   124  C C   . MET A 1 46  ? 2.327   12.587  1.797   1.00 27.15 ?  20  MET A C   1 
ATOM   125  O O   . MET A 1 46  ? 1.678   13.582  1.467   1.00 25.37 ?  20  MET A O   1 
ATOM   126  C CB  . MET A 1 46  ? 1.144   10.449  2.167   1.00 30.27 ?  20  MET A CB  1 
ATOM   127  C CG  . MET A 1 46  ? 0.429   9.259   1.564   1.00 29.35 ?  20  MET A CG  1 
ATOM   128  S SD  . MET A 1 46  ? -0.681  8.471   2.723   1.00 27.98 ?  20  MET A SD  1 
ATOM   129  C CE  . MET A 1 46  ? -2.064  9.617   2.672   1.00 29.96 ?  20  MET A CE  1 
ATOM   130  N N   . LYS A 1 47  ? 3.330   12.631  2.668   1.00 27.33 ?  21  LYS A N   1 
ATOM   131  C CA  . LYS A 1 47  ? 3.711   13.918  3.311   1.00 30.11 ?  21  LYS A CA  1 
ATOM   132  C C   . LYS A 1 47  ? 4.259   14.858  2.257   1.00 29.27 ?  21  LYS A C   1 
ATOM   133  O O   . LYS A 1 47  ? 3.791   16.003  2.213   1.00 29.74 ?  21  LYS A O   1 
ATOM   134  C CB  . LYS A 1 47  ? 4.703   13.718  4.453   1.00 34.93 ?  21  LYS A CB  1 
ATOM   135  C CG  . LYS A 1 47  ? 4.062   13.322  5.769   1.00 42.16 ?  21  LYS A CG  1 
ATOM   136  C CD  . LYS A 1 47  ? 5.091   12.876  6.765   1.00 54.26 ?  21  LYS A CD  1 
ATOM   137  C CE  . LYS A 1 47  ? 4.528   12.025  7.881   1.00 58.77 ?  21  LYS A CE  1 
ATOM   138  N NZ  . LYS A 1 47  ? 5.534   11.911  8.961   1.00 68.13 ?  21  LYS A NZ  1 
ATOM   139  N N   . ALA A 1 48  ? 5.200   14.389  1.420   1.00 28.80 ?  22  ALA A N   1 
ATOM   140  C CA  . ALA A 1 48  ? 5.886   15.221  0.402   1.00 26.68 ?  22  ALA A CA  1 
ATOM   141  C C   . ALA A 1 48  ? 4.908   15.760  -0.649  1.00 28.74 ?  22  ALA A C   1 
ATOM   142  O O   . ALA A 1 48  ? 5.144   16.871  -1.135  1.00 27.44 ?  22  ALA A O   1 
ATOM   143  C CB  . ALA A 1 48  ? 7.029   14.449  -0.210  1.00 26.08 ?  22  ALA A CB  1 
ATOM   144  N N   . ASN A 1 49  ? 3.805   15.064  -0.965  1.00 24.01 ?  23  ASN A N   1 
ATOM   145  C CA  . ASN A 1 49  ? 2.867   15.523  -2.017  1.00 23.91 ?  23  ASN A CA  1 
ATOM   146  C C   . ASN A 1 49  ? 1.560   16.011  -1.372  1.00 23.51 ?  23  ASN A C   1 
ATOM   147  O O   . ASN A 1 49  ? 0.633   16.298  -2.137  1.00 22.63 ?  23  ASN A O   1 
ATOM   148  C CB  . ASN A 1 49  ? 2.702   14.417  -3.078  1.00 21.89 ?  23  ASN A CB  1 
ATOM   149  C CG  . ASN A 1 49  ? 4.028   14.117  -3.748  1.00 19.15 ?  23  ASN A CG  1 
ATOM   150  O OD1 . ASN A 1 49  ? 4.382   14.763  -4.722  1.00 20.62 ?  23  ASN A OD1 1 
ATOM   151  N ND2 . ASN A 1 49  ? 4.745   13.117  -3.259  1.00 19.97 ?  23  ASN A ND2 1 
ATOM   152  N N   . ASP A 1 50  ? 1.510   16.110  -0.027  1.00 24.61 ?  24  ASP A N   1 
ATOM   153  C CA  . ASP A 1 50  ? 0.309   16.581  0.727   1.00 24.15 ?  24  ASP A CA  1 
ATOM   154  C C   . ASP A 1 50  ? -0.912  15.828  0.193   1.00 23.20 ?  24  ASP A C   1 
ATOM   155  O O   . ASP A 1 50  ? -1.909  16.452  -0.159  1.00 23.67 ?  24  ASP A O   1 
ATOM   156  C CB  . ASP A 1 50  ? 0.139   18.097  0.619   1.00 29.17 ?  24  ASP A CB  1 
ATOM   157  C CG  . ASP A 1 50  ? -0.955  18.695  1.488   1.00 31.52 ?  24  ASP A CG  1 
ATOM   158  O OD1 . ASP A 1 50  ? -1.191  18.163  2.584   1.00 37.73 ?  24  ASP A OD1 1 
ATOM   159  O OD2 . ASP A 1 50  ? -1.542  19.694  1.049   1.00 35.66 ?  24  ASP A OD2 1 
ATOM   160  N N   . ILE A 1 51  ? -0.826  14.508  0.184   1.00 22.84 ?  25  ILE A N   1 
ATOM   161  C CA  . ILE A 1 51  ? -1.945  13.639  -0.255  1.00 22.34 ?  25  ILE A CA  1 
ATOM   162  C C   . ILE A 1 51  ? -2.854  13.407  0.937   1.00 21.05 ?  25  ILE A C   1 
ATOM   163  O O   . ILE A 1 51  ? -2.463  12.747  1.905   1.00 23.89 ?  25  ILE A O   1 
ATOM   164  C CB  . ILE A 1 51  ? -1.414  12.300  -0.795  1.00 22.62 ?  25  ILE A CB  1 
ATOM   165  C CG1 . ILE A 1 51  ? -0.378  12.480  -1.916  1.00 21.87 ?  25  ILE A CG1 1 
ATOM   166  C CG2 . ILE A 1 51  ? -2.599  11.411  -1.163  1.00 21.14 ?  25  ILE A CG2 1 
ATOM   167  C CD1 . ILE A 1 51  ? 0.175   11.148  -2.471  1.00 20.75 ?  25  ILE A CD1 1 
ATOM   168  N N   . PRO A 1 52  ? -4.129  13.836  0.869   1.00 22.77 ?  26  PRO A N   1 
ATOM   169  C CA  . PRO A 1 52  ? -5.035  13.618  1.989   1.00 23.31 ?  26  PRO A CA  1 
ATOM   170  C C   . PRO A 1 52  ? -5.307  12.149  2.305   1.00 20.97 ?  26  PRO A C   1 
ATOM   171  O O   . PRO A 1 52  ? -5.248  11.751  3.457   1.00 19.76 ?  26  PRO A O   1 
ATOM   172  C CB  . PRO A 1 52  ? -6.315  14.349  1.542   1.00 23.00 ?  26  PRO A CB  1 
ATOM   173  C CG  . PRO A 1 52  ? -5.857  15.363  0.535   1.00 23.46 ?  26  PRO A CG  1 
ATOM   174  C CD  . PRO A 1 52  ? -4.711  14.667  -0.195  1.00 23.21 ?  26  PRO A CD  1 
ATOM   175  N N   . GLY A 1 53  ? -5.616  11.361  1.269   1.00 19.96 ?  27  GLY A N   1 
ATOM   176  C CA  . GLY A 1 53  ? -5.872  9.928   1.462   1.00 19.99 ?  27  GLY A CA  1 
ATOM   177  C C   . GLY A 1 53  ? -5.330  9.076   0.340   1.00 18.09 ?  27  GLY A C   1 
ATOM   178  O O   . GLY A 1 53  ? -5.288  9.515   -0.820  1.00 17.58 ?  27  GLY A O   1 
ATOM   179  N N   . LEU A 1 54  ? -4.964  7.870   0.697   1.00 19.39 ?  28  LEU A N   1 
ATOM   180  C CA  . LEU A 1 54  ? -4.361  6.940   -0.263  1.00 21.31 ?  28  LEU A CA  1 
ATOM   181  C C   . LEU A 1 54  ? -4.709  5.538   0.161   1.00 20.96 ?  28  LEU A C   1 
ATOM   182  O O   . LEU A 1 54  ? -4.636  5.230   1.362   1.00 22.21 ?  28  LEU A O   1 
ATOM   183  C CB  . LEU A 1 54  ? -2.854  7.212   -0.278  1.00 22.14 ?  28  LEU A CB  1 
ATOM   184  C CG  . LEU A 1 54  ? -2.038  6.473   -1.325  1.00 22.43 ?  28  LEU A CG  1 
ATOM   185  C CD1 . LEU A 1 54  ? -0.820  7.292   -1.760  1.00 21.91 ?  28  LEU A CD1 1 
ATOM   186  C CD2 . LEU A 1 54  ? -1.590  5.143   -0.792  1.00 21.99 ?  28  LEU A CD2 1 
ATOM   187  N N   . ALA A 1 55  ? -5.101  4.720   -0.827  1.00 21.42 ?  29  ALA A N   1 
ATOM   188  C CA  . ALA A 1 55  ? -5.405  3.301   -0.602  1.00 19.09 ?  29  ALA A CA  1 
ATOM   189  C C   . ALA A 1 55  ? -4.455  2.469   -1.451  1.00 20.00 ?  29  ALA A C   1 
ATOM   190  O O   . ALA A 1 55  ? -4.347  2.747   -2.687  1.00 16.02 ?  29  ALA A O   1 
ATOM   191  C CB  . ALA A 1 55  ? -6.841  2.989   -0.963  1.00 20.56 ?  29  ALA A CB  1 
ATOM   192  N N   . VAL A 1 56  ? -3.843  1.484   -0.803  1.00 18.51 ?  30  VAL A N   1 
ATOM   193  C CA  . VAL A 1 56  ? -2.978  0.487   -1.464  1.00 19.99 ?  30  VAL A CA  1 
ATOM   194  C C   . VAL A 1 56  ? -3.666  -0.878  -1.390  1.00 20.06 ?  30  VAL A C   1 
ATOM   195  O O   . VAL A 1 56  ? -4.214  -1.233  -0.335  1.00 22.06 ?  30  VAL A O   1 
ATOM   196  C CB  . VAL A 1 56  ? -1.571  0.458   -0.862  1.00 20.26 ?  30  VAL A CB  1 
ATOM   197  C CG1 . VAL A 1 56  ? -0.760  -0.621  -1.505  1.00 19.70 ?  30  VAL A CG1 1 
ATOM   198  C CG2 . VAL A 1 56  ? -0.871  1.807   -0.960  1.00 22.21 ?  30  VAL A CG2 1 
ATOM   199  N N   . ALA A 1 57  ? -3.601  -1.624  -2.491  1.00 19.17 ?  31  ALA A N   1 
ATOM   200  C CA  . ALA A 1 57  ? -3.972  -3.053  -2.492  1.00 19.19 ?  31  ALA A CA  1 
ATOM   201  C C   . ALA A 1 57  ? -2.880  -3.827  -3.213  1.00 20.33 ?  31  ALA A C   1 
ATOM   202  O O   . ALA A 1 57  ? -2.434  -3.397  -4.274  1.00 18.55 ?  31  ALA A O   1 
ATOM   203  C CB  . ALA A 1 57  ? -5.337  -3.247  -3.110  1.00 20.33 ?  31  ALA A CB  1 
ATOM   204  N N   . ILE A 1 58  ? -2.452  -4.932  -2.609  1.00 20.30 ?  32  ILE A N   1 
ATOM   205  C CA  . ILE A 1 58  ? -1.416  -5.845  -3.140  1.00 22.29 ?  32  ILE A CA  1 
ATOM   206  C C   . ILE A 1 58  ? -1.997  -7.249  -3.266  1.00 19.98 ?  32  ILE A C   1 
ATOM   207  O O   . ILE A 1 58  ? -2.608  -7.734  -2.287  1.00 19.95 ?  32  ILE A O   1 
ATOM   208  C CB  . ILE A 1 58  ? -0.189  -5.810  -2.223  1.00 24.75 ?  32  ILE A CB  1 
ATOM   209  C CG1 . ILE A 1 58  ? 0.372   -4.390  -2.110  1.00 26.26 ?  32  ILE A CG1 1 
ATOM   210  C CG2 . ILE A 1 58  ? 0.834   -6.820  -2.695  1.00 27.98 ?  32  ILE A CG2 1 
ATOM   211  C CD1 . ILE A 1 58  ? 1.137   -4.109  -0.836  1.00 29.43 ?  32  ILE A CD1 1 
ATOM   212  N N   . SER A 1 59  ? -1.778  -7.869  -4.416  1.00 20.62 ?  33  SER A N   1 
ATOM   213  C CA  . SER A 1 59  ? -1.998  -9.318  -4.645  1.00 21.85 ?  33  SER A CA  1 
ATOM   214  C C   . SER A 1 59  ? -0.636  -10.013 -4.630  1.00 24.06 ?  33  SER A C   1 
ATOM   215  O O   . SER A 1 59  ? 0.200   -9.629  -5.445  1.00 23.34 ?  33  SER A O   1 
ATOM   216  C CB  . SER A 1 59  ? -2.724  -9.551  -5.932  1.00 22.98 ?  33  SER A CB  1 
ATOM   217  O OG  . SER A 1 59  ? -2.982  -10.932 -6.069  1.00 24.39 ?  33  SER A OG  1 
ATOM   218  N N   . LEU A 1 60  ? -0.411  -10.922 -3.665  1.00 24.46 ?  34  LEU A N   1 
ATOM   219  C CA  . LEU A 1 60  ? 0.877   -11.587 -3.375  1.00 29.75 ?  34  LEU A CA  1 
ATOM   220  C C   . LEU A 1 60  ? 0.583   -13.086 -3.309  1.00 30.29 ?  34  LEU A C   1 
ATOM   221  O O   . LEU A 1 60  ? -0.105  -13.473 -2.377  1.00 28.80 ?  34  LEU A O   1 
ATOM   222  C CB  . LEU A 1 60  ? 1.384   -11.050 -2.027  1.00 34.58 ?  34  LEU A CB  1 
ATOM   223  C CG  . LEU A 1 60  ? 2.741   -11.545 -1.528  1.00 37.90 ?  34  LEU A CG  1 
ATOM   224  C CD1 . LEU A 1 60  ? 3.820   -11.488 -2.597  1.00 40.24 ?  34  LEU A CD1 1 
ATOM   225  C CD2 . LEU A 1 60  ? 3.159   -10.736 -0.311  1.00 40.48 ?  34  LEU A CD2 1 
ATOM   226  N N   . LYS A 1 61  ? 1.010   -13.860 -4.308  1.00 37.04 ?  35  LYS A N   1 
ATOM   227  C CA  . LYS A 1 61  ? 0.879   -15.341 -4.278  1.00 42.34 ?  35  LYS A CA  1 
ATOM   228  C C   . LYS A 1 61  ? -0.599  -15.730 -4.127  1.00 39.38 ?  35  LYS A C   1 
ATOM   229  O O   . LYS A 1 61  ? -0.863  -16.701 -3.387  1.00 39.10 ?  35  LYS A O   1 
ATOM   230  C CB  . LYS A 1 61  ? 1.630   -15.936 -3.081  1.00 51.24 ?  35  LYS A CB  1 
ATOM   231  C CG  . LYS A 1 61  ? 3.056   -15.445 -2.839  1.00 59.18 ?  35  LYS A CG  1 
ATOM   232  C CD  . LYS A 1 61  ? 3.471   -15.474 -1.362  1.00 62.82 ?  35  LYS A CD  1 
ATOM   233  C CE  . LYS A 1 61  ? 4.141   -16.764 -0.939  1.00 67.02 ?  35  LYS A CE  1 
ATOM   234  N NZ  . LYS A 1 61  ? 3.339   -17.959 -1.310  1.00 71.26 ?  35  LYS A NZ  1 
ATOM   235  N N   . GLY A 1 62  ? -1.519  -14.958 -4.719  1.00 37.99 ?  36  GLY A N   1 
ATOM   236  C CA  . GLY A 1 62  ? -2.972  -15.222 -4.701  1.00 37.13 ?  36  GLY A CA  1 
ATOM   237  C C   . GLY A 1 62  ? -3.653  -14.792 -3.412  1.00 39.22 ?  36  GLY A C   1 
ATOM   238  O O   . GLY A 1 62  ? -4.792  -15.229 -3.191  1.00 40.68 ?  36  GLY A O   1 
ATOM   239  N N   . GLU A 1 63  ? -3.014  -13.951 -2.597  1.00 35.95 ?  37  GLU A N   1 
ATOM   240  C CA  . GLU A 1 63  ? -3.624  -13.384 -1.368  1.00 39.09 ?  37  GLU A CA  1 
ATOM   241  C C   . GLU A 1 63  ? -3.680  -11.866 -1.472  1.00 31.44 ?  37  GLU A C   1 
ATOM   242  O O   . GLU A 1 63  ? -2.682  -11.229 -1.774  1.00 25.41 ?  37  GLU A O   1 
ATOM   243  C CB  . GLU A 1 63  ? -2.821  -13.793 -0.143  1.00 43.44 ?  37  GLU A CB  1 
ATOM   244  C CG  . GLU A 1 63  ? -2.642  -15.304 -0.060  1.00 54.99 ?  37  GLU A CG  1 
ATOM   245  C CD  . GLU A 1 63  ? -2.876  -15.911 1.312   1.00 62.51 ?  37  GLU A CD  1 
ATOM   246  O OE1 . GLU A 1 63  ? -3.105  -15.139 2.273   1.00 67.11 ?  37  GLU A OE1 1 
ATOM   247  O OE2 . GLU A 1 63  ? -2.838  -17.161 1.415   1.00 77.97 ?  37  GLU A OE2 1 
ATOM   248  N N   . PRO A 1 64  ? -4.843  -11.269 -1.154  1.00 27.60 ?  38  PRO A N   1 
ATOM   249  C CA  . PRO A 1 64  ? -5.000  -9.822  -1.150  1.00 26.75 ?  38  PRO A CA  1 
ATOM   250  C C   . PRO A 1 64  ? -4.547  -9.229  0.186   1.00 27.97 ?  38  PRO A C   1 
ATOM   251  O O   . PRO A 1 64  ? -4.698  -9.844  1.267   1.00 28.31 ?  38  PRO A O   1 
ATOM   252  C CB  . PRO A 1 64  ? -6.507  -9.667  -1.408  1.00 28.38 ?  38  PRO A CB  1 
ATOM   253  C CG  . PRO A 1 64  ? -7.128  -10.880 -0.718  1.00 28.63 ?  38  PRO A CG  1 
ATOM   254  C CD  . PRO A 1 64  ? -6.093  -11.970 -0.810  1.00 29.05 ?  38  PRO A CD  1 
ATOM   255  N N   . HIS A 1 65  ? -3.996  -8.031  0.107   1.00 24.59 ?  39  HIS A N   1 
ATOM   256  C CA  . HIS A 1 65  ? -3.554  -7.249  1.272   1.00 24.44 ?  39  HIS A CA  1 
ATOM   257  C C   . HIS A 1 65  ? -3.932  -5.798  1.039   1.00 25.81 ?  39  HIS A C   1 
ATOM   258  O O   . HIS A 1 65  ? -3.686  -5.312  -0.095  1.00 23.46 ?  39  HIS A O   1 
ATOM   259  C CB  . HIS A 1 65  ? -2.043  -7.369  1.431   1.00 26.20 ?  39  HIS A CB  1 
ATOM   260  C CG  . HIS A 1 65  ? -1.589  -8.777  1.596   1.00 27.45 ?  39  HIS A CG  1 
ATOM   261  N ND1 . HIS A 1 65  ? -1.552  -9.397  2.832   1.00 29.76 ?  39  HIS A ND1 1 
ATOM   262  C CD2 . HIS A 1 65  ? -1.152  -9.670  0.690   1.00 29.35 ?  39  HIS A CD2 1 
ATOM   263  C CE1 . HIS A 1 65  ? -1.103  -10.625 2.679   1.00 31.76 ?  39  HIS A CE1 1 
ATOM   264  N NE2 . HIS A 1 65  ? -0.830  -10.809 1.369   1.00 28.21 ?  39  HIS A NE2 1 
ATOM   265  N N   . TYR A 1 66  ? -4.523  -5.151  2.031   1.00 22.16 ?  40  TYR A N   1 
ATOM   266  C CA  . TYR A 1 66  ? -4.991  -3.745  1.871   1.00 24.24 ?  40  TYR A CA  1 
ATOM   267  C C   . TYR A 1 66  ? -4.336  -2.858  2.916   1.00 24.47 ?  40  TYR A C   1 
ATOM   268  O O   . TYR A 1 66  ? -4.194  -3.266  4.074   1.00 25.72 ?  40  TYR A O   1 
ATOM   269  C CB  . TYR A 1 66  ? -6.511  -3.651  1.998   1.00 25.33 ?  40  TYR A CB  1 
ATOM   270  C CG  . TYR A 1 66  ? -7.237  -4.626  1.125   1.00 27.07 ?  40  TYR A CG  1 
ATOM   271  C CD1 . TYR A 1 66  ? -7.327  -4.422  -0.243  1.00 25.85 ?  40  TYR A CD1 1 
ATOM   272  C CD2 . TYR A 1 66  ? -7.841  -5.759  1.648   1.00 30.28 ?  40  TYR A CD2 1 
ATOM   273  C CE1 . TYR A 1 66  ? -7.979  -5.320  -1.066  1.00 27.67 ?  40  TYR A CE1 1 
ATOM   274  C CE2 . TYR A 1 66  ? -8.521  -6.654  0.827   1.00 32.66 ?  40  TYR A CE2 1 
ATOM   275  C CZ  . TYR A 1 66  ? -8.586  -6.435  -0.538  1.00 29.24 ?  40  TYR A CZ  1 
ATOM   276  O OH  . TYR A 1 66  ? -9.249  -7.286  -1.372  1.00 30.21 ?  40  TYR A OH  1 
ATOM   277  N N   . PHE A 1 67  ? -3.958  -1.659  2.511   1.00 20.38 ?  41  PHE A N   1 
ATOM   278  C CA  . PHE A 1 67  ? -3.359  -0.656  3.409   1.00 22.77 ?  41  PHE A CA  1 
ATOM   279  C C   . PHE A 1 67  ? -4.043  0.646   3.085   1.00 23.49 ?  41  PHE A C   1 
ATOM   280  O O   . PHE A 1 67  ? -4.017  1.067   1.909   1.00 20.75 ?  41  PHE A O   1 
ATOM   281  C CB  . PHE A 1 67  ? -1.841  -0.573  3.245   1.00 23.55 ?  41  PHE A CB  1 
ATOM   282  C CG  . PHE A 1 67  ? -1.155  -1.898  3.443   1.00 27.74 ?  41  PHE A CG  1 
ATOM   283  C CD1 . PHE A 1 67  ? -1.058  -2.795  2.402   1.00 28.64 ?  41  PHE A CD1 1 
ATOM   284  C CD2 . PHE A 1 67  ? -0.771  -2.303  4.713   1.00 35.50 ?  41  PHE A CD2 1 
ATOM   285  C CE1 . PHE A 1 67  ? -0.506  -4.051  2.601   1.00 32.69 ?  41  PHE A CE1 1 
ATOM   286  C CE2 . PHE A 1 67  ? -0.218  -3.558  4.911   1.00 33.65 ?  41  PHE A CE2 1 
ATOM   287  C CZ  . PHE A 1 67  ? -0.074  -4.416  3.850   1.00 31.16 ?  41  PHE A CZ  1 
ATOM   288  N N   . SER A 1 68  ? -4.625  1.279   4.100   1.00 23.60 ?  42  SER A N   1 
ATOM   289  C CA  . SER A 1 68  ? -5.440  2.484   3.887   1.00 21.81 ?  42  SER A CA  1 
ATOM   290  C C   . SER A 1 68  ? -4.855  3.588   4.730   1.00 21.13 ?  42  SER A C   1 
ATOM   291  O O   . SER A 1 68  ? -4.509  3.314   5.885   1.00 24.66 ?  42  SER A O   1 
ATOM   292  C CB  . SER A 1 68  ? -6.898  2.244   4.190   1.00 22.56 ?  42  SER A CB  1 
ATOM   293  O OG  . SER A 1 68  ? -7.409  1.146   3.442   1.00 22.60 ?  42  SER A OG  1 
ATOM   294  N N   . TYR A 1 69  ? -4.769  4.770   4.172   1.00 20.68 ?  43  TYR A N   1 
ATOM   295  C CA  . TYR A 1 69  ? -4.099  5.928   4.819   1.00 22.19 ?  43  TYR A CA  1 
ATOM   296  C C   . TYR A 1 69  ? -4.972  7.162   4.696   1.00 21.19 ?  43  TYR A C   1 
ATOM   297  O O   . TYR A 1 69  ? -5.451  7.503   3.612   1.00 21.08 ?  43  TYR A O   1 
ATOM   298  C CB  . TYR A 1 69  ? -2.722  6.219   4.215   1.00 23.99 ?  43  TYR A CB  1 
ATOM   299  C CG  . TYR A 1 69  ? -1.756  5.065   4.293   1.00 24.41 ?  43  TYR A CG  1 
ATOM   300  C CD1 . TYR A 1 69  ? -1.751  4.088   3.320   1.00 22.21 ?  43  TYR A CD1 1 
ATOM   301  C CD2 . TYR A 1 69  ? -0.846  4.946   5.350   1.00 25.34 ?  43  TYR A CD2 1 
ATOM   302  C CE1 . TYR A 1 69  ? -0.904  2.998   3.408   1.00 23.27 ?  43  TYR A CE1 1 
ATOM   303  C CE2 . TYR A 1 69  ? 0.000   3.850   5.452   1.00 22.48 ?  43  TYR A CE2 1 
ATOM   304  C CZ  . TYR A 1 69  ? -0.020  2.882   4.463   1.00 24.09 ?  43  TYR A CZ  1 
ATOM   305  O OH  . TYR A 1 69  ? 0.790   1.794   4.483   1.00 25.97 ?  43  TYR A OH  1 
ATOM   306  N N   . GLY A 1 70  ? -5.064  7.923   5.786   1.00 20.21 ?  44  GLY A N   1 
ATOM   307  C CA  . GLY A 1 70  ? -5.595  9.282   5.704   1.00 20.53 ?  44  GLY A CA  1 
ATOM   308  C C   . GLY A 1 70  ? -7.084  9.301   5.417   1.00 19.40 ?  44  GLY A C   1 
ATOM   309  O O   . GLY A 1 70  ? -7.792  8.324   5.742   1.00 22.55 ?  44  GLY A O   1 
ATOM   310  N N   . LEU A 1 71  ? -7.487  10.376  4.754   1.00 20.22 ?  45  LEU A N   1 
ATOM   311  C CA  . LEU A 1 71  ? -8.859  10.894  4.709   1.00 22.02 ?  45  LEU A CA  1 
ATOM   312  C C   . LEU A 1 71  ? -9.391  10.860  3.278   1.00 22.76 ?  45  LEU A C   1 
ATOM   313  O O   . LEU A 1 71  ? -8.741  11.379  2.351   1.00 22.28 ?  45  LEU A O   1 
ATOM   314  C CB  . LEU A 1 71  ? -8.817  12.324  5.253   1.00 25.60 ?  45  LEU A CB  1 
ATOM   315  C CG  . LEU A 1 71  ? -8.393  12.426  6.718   1.00 25.65 ?  45  LEU A CG  1 
ATOM   316  C CD1 . LEU A 1 71  ? -8.446  13.865  7.194   1.00 27.83 ?  45  LEU A CD1 1 
ATOM   317  C CD2 . LEU A 1 71  ? -9.294  11.572  7.592   1.00 30.79 ?  45  LEU A CD2 1 
ATOM   318  N N   . ALA A 1 72  ? -10.591 10.320  3.130   1.00 24.07 ?  46  ALA A N   1 
ATOM   319  C CA  . ALA A 1 72  ? -11.341 10.388  1.868   1.00 23.47 ?  46  ALA A CA  1 
ATOM   320  C C   . ALA A 1 72  ? -11.903 11.796  1.704   1.00 23.00 ?  46  ALA A C   1 
ATOM   321  O O   . ALA A 1 72  ? -11.878 12.314  0.611   1.00 21.08 ?  46  ALA A O   1 
ATOM   322  C CB  . ALA A 1 72  ? -12.385 9.314   1.906   1.00 23.59 ?  46  ALA A CB  1 
ATOM   323  N N   . SER A 1 73  ? -12.247 12.464  2.803   1.00 23.93 ?  47  SER A N   1 
ATOM   324  C CA  . SER A 1 73  ? -12.707 13.865  2.775   1.00 26.67 ?  47  SER A CA  1 
ATOM   325  C C   . SER A 1 73  ? -12.170 14.559  4.024   1.00 25.29 ?  47  SER A C   1 
ATOM   326  O O   . SER A 1 73  ? -12.310 14.024  5.160   1.00 27.10 ?  47  SER A O   1 
ATOM   327  C CB  . SER A 1 73  ? -14.217 13.974  2.723   1.00 32.57 ?  47  SER A CB  1 
ATOM   328  O OG  . SER A 1 73  ? -14.606 15.317  3.083   1.00 36.04 ?  47  SER A OG  1 
ATOM   329  N N   . LYS A 1 74  ? -11.471 15.643  3.806   1.00 25.81 ?  48  LYS A N   1 
ATOM   330  C CA  . LYS A 1 74  ? -10.862 16.391  4.923   1.00 30.85 ?  48  LYS A CA  1 
ATOM   331  C C   . LYS A 1 74  ? -11.981 17.042  5.742   1.00 31.80 ?  48  LYS A C   1 
ATOM   332  O O   . LYS A 1 74  ? -11.869 17.132  6.981   1.00 36.25 ?  48  LYS A O   1 
ATOM   333  C CB  . LYS A 1 74  ? -9.879  17.386  4.328   1.00 30.99 ?  48  LYS A CB  1 
ATOM   334  C CG  . LYS A 1 74  ? -8.635  16.738  3.738   1.00 35.36 ?  48  LYS A CG  1 
ATOM   335  C CD  . LYS A 1 74  ? -7.778  17.669  2.921   1.00 39.61 ?  48  LYS A CD  1 
ATOM   336  C CE  . LYS A 1 74  ? -7.480  18.958  3.637   1.00 47.20 ?  48  LYS A CE  1 
ATOM   337  N NZ  . LYS A 1 74  ? -6.113  19.444  3.351   1.00 48.89 ?  48  LYS A NZ  1 
ATOM   338  N N   . GLU A 1 75  ? -13.031 17.453  5.073   1.00 29.05 ?  49  GLU A N   1 
ATOM   339  C CA  . GLU A 1 75  ? -14.071 18.328  5.676   1.00 33.32 ?  49  GLU A CA  1 
ATOM   340  C C   . GLU A 1 75  ? -14.851 17.560  6.749   1.00 32.81 ?  49  GLU A C   1 
ATOM   341  O O   . GLU A 1 75  ? -15.101 18.135  7.828   1.00 31.89 ?  49  GLU A O   1 
ATOM   342  C CB  . GLU A 1 75  ? -14.898 18.925  4.550   1.00 32.34 ?  49  GLU A CB  1 
ATOM   343  C CG  . GLU A 1 75  ? -14.134 20.003  3.797   1.00 34.98 ?  49  GLU A CG  1 
ATOM   344  C CD  . GLU A 1 75  ? -13.208 19.574  2.659   1.00 36.07 ?  49  GLU A CD  1 
ATOM   345  O OE1 . GLU A 1 75  ? -13.195 18.386  2.272   1.00 30.89 ?  49  GLU A OE1 1 
ATOM   346  O OE2 . GLU A 1 75  ? -12.551 20.465  2.130   1.00 34.80 ?  49  GLU A OE2 1 
ATOM   347  N N   . ASP A 1 76  ? -15.180 16.300  6.514   1.00 35.56 ?  50  ASP A N   1 
ATOM   348  C CA  . ASP A 1 76  ? -15.965 15.496  7.489   1.00 40.36 ?  50  ASP A CA  1 
ATOM   349  C C   . ASP A 1 76  ? -15.066 14.451  8.169   1.00 35.62 ?  50  ASP A C   1 
ATOM   350  O O   . ASP A 1 76  ? -15.576 13.686  8.989   1.00 39.24 ?  50  ASP A O   1 
ATOM   351  C CB  . ASP A 1 76  ? -17.213 14.930  6.801   1.00 42.17 ?  50  ASP A CB  1 
ATOM   352  C CG  . ASP A 1 76  ? -16.887 13.904  5.734   1.00 47.27 ?  50  ASP A CG  1 
ATOM   353  O OD1 . ASP A 1 76  ? -15.738 13.421  5.740   1.00 46.79 ?  50  ASP A OD1 1 
ATOM   354  O OD2 . ASP A 1 76  ? -17.763 13.628  4.890   1.00 53.15 ?  50  ASP A OD2 1 
ATOM   355  N N   . GLY A 1 77  ? -13.770 14.411  7.857   1.00 34.42 ?  51  GLY A N   1 
ATOM   356  C CA  . GLY A 1 77  ? -12.825 13.401  8.370   1.00 32.88 ?  51  GLY A CA  1 
ATOM   357  C C   . GLY A 1 77  ? -13.230 11.942  8.134   1.00 31.26 ?  51  GLY A C   1 
ATOM   358  O O   . GLY A 1 77  ? -12.706 11.084  8.856   1.00 33.59 ?  51  GLY A O   1 
ATOM   359  N N   . ARG A 1 78  ? -14.014 11.613  7.110   1.00 30.18 ?  52  ARG A N   1 
ATOM   360  C CA  . ARG A 1 78  ? -14.188 10.191  6.668   1.00 30.55 ?  52  ARG A CA  1 
ATOM   361  C C   . ARG A 1 78  ? -12.820 9.580   6.307   1.00 29.00 ?  52  ARG A C   1 
ATOM   362  O O   . ARG A 1 78  ? -12.091 10.189  5.516   1.00 24.97 ?  52  ARG A O   1 
ATOM   363  C CB  . ARG A 1 78  ? -15.118 10.084  5.457   1.00 37.49 ?  52  ARG A CB  1 
ATOM   364  C CG  . ARG A 1 78  ? -16.561 9.730   5.805   1.00 50.98 ?  52  ARG A CG  1 
ATOM   365  C CD  . ARG A 1 78  ? -17.545 10.019  4.674   1.00 57.91 ?  52  ARG A CD  1 
ATOM   366  N NE  . ARG A 1 78  ? -16.908 9.943   3.353   1.00 60.91 ?  52  ARG A NE  1 
ATOM   367  C CZ  . ARG A 1 78  ? -16.860 10.928  2.443   1.00 63.10 ?  52  ARG A CZ  1 
ATOM   368  N NH1 . ARG A 1 78  ? -17.440 12.101  2.680   1.00 53.82 ?  52  ARG A NH1 1 
ATOM   369  N NH2 . ARG A 1 78  ? -16.227 10.726  1.288   1.00 53.17 ?  52  ARG A NH2 1 
ATOM   370  N N   . ARG A 1 79  ? -12.502 8.402   6.837   1.00 27.17 ?  53  ARG A N   1 
ATOM   371  C CA  . ARG A 1 79  ? -11.196 7.746   6.551   1.00 28.94 ?  53  ARG A CA  1 
ATOM   372  C C   . ARG A 1 79  ? -11.271 6.981   5.223   1.00 27.28 ?  53  ARG A C   1 
ATOM   373  O O   . ARG A 1 79  ? -12.297 6.407   4.955   1.00 23.28 ?  53  ARG A O   1 
ATOM   374  C CB  . ARG A 1 79  ? -10.773 6.766   7.641   1.00 34.91 ?  53  ARG A CB  1 
ATOM   375  C CG  . ARG A 1 79  ? -9.855  7.378   8.688   1.00 43.19 ?  53  ARG A CG  1 
ATOM   376  C CD  . ARG A 1 79  ? -10.665 8.161   9.677   1.00 48.93 ?  53  ARG A CD  1 
ATOM   377  N NE  . ARG A 1 79  ? -9.888  9.279   10.189  1.00 63.61 ?  53  ARG A NE  1 
ATOM   378  C CZ  . ARG A 1 79  ? -8.984  9.201   11.160  1.00 70.89 ?  53  ARG A CZ  1 
ATOM   379  N NH1 . ARG A 1 79  ? -8.730  8.039   11.747  1.00 73.68 ?  53  ARG A NH1 1 
ATOM   380  N NH2 . ARG A 1 79  ? -8.352  10.300  11.545  1.00 69.27 ?  53  ARG A NH2 1 
ATOM   381  N N   . VAL A 1 80  ? -10.151 6.909   4.503   1.00 23.64 ?  54  VAL A N   1 
ATOM   382  C CA  . VAL A 1 80  ? -9.935  5.921   3.394   1.00 23.48 ?  54  VAL A CA  1 
ATOM   383  C C   . VAL A 1 80  ? -10.066 4.497   3.937   1.00 22.68 ?  54  VAL A C   1 
ATOM   384  O O   . VAL A 1 80  ? -9.540  4.185   5.020   1.00 24.95 ?  54  VAL A O   1 
ATOM   385  C CB  . VAL A 1 80  ? -8.568  6.129   2.703   1.00 20.02 ?  54  VAL A CB  1 
ATOM   386  C CG1 . VAL A 1 80  ? -8.299  5.014   1.680   1.00 19.95 ?  54  VAL A CG1 1 
ATOM   387  C CG2 . VAL A 1 80  ? -8.517  7.488   2.048   1.00 19.84 ?  54  VAL A CG2 1 
ATOM   388  N N   . THR A 1 81  ? -10.784 3.636   3.206   1.00 21.04 ?  55  THR A N   1 
ATOM   389  C CA  . THR A 1 81  ? -10.852 2.173   3.431   1.00 22.00 ?  55  THR A CA  1 
ATOM   390  C C   . THR A 1 81  ? -10.621 1.530   2.069   1.00 21.05 ?  55  THR A C   1 
ATOM   391  O O   . THR A 1 81  ? -10.634 2.224   1.055   1.00 20.28 ?  55  THR A O   1 
ATOM   392  C CB  . THR A 1 81  ? -12.214 1.748   4.009   1.00 25.81 ?  55  THR A CB  1 
ATOM   393  O OG1 . THR A 1 81  ? -13.168 1.822   2.942   1.00 27.01 ?  55  THR A OG1 1 
ATOM   394  C CG2 . THR A 1 81  ? -12.674 2.619   5.162   1.00 26.76 ?  55  THR A CG2 1 
ATOM   395  N N   . PRO A 1 82  ? -10.479 0.196   2.003   1.00 20.62 ?  56  PRO A N   1 
ATOM   396  C CA  . PRO A 1 82  ? -10.425 -0.505  0.713   1.00 22.87 ?  56  PRO A CA  1 
ATOM   397  C C   . PRO A 1 82  ? -11.713 -0.455  -0.132  1.00 22.66 ?  56  PRO A C   1 
ATOM   398  O O   . PRO A 1 82  ? -11.647 -0.899  -1.294  1.00 22.77 ?  56  PRO A O   1 
ATOM   399  C CB  . PRO A 1 82  ? -10.106 -1.956  1.118   1.00 20.59 ?  56  PRO A CB  1 
ATOM   400  C CG  . PRO A 1 82  ? -9.614  -1.875  2.547   1.00 22.22 ?  56  PRO A CG  1 
ATOM   401  C CD  . PRO A 1 82  ? -10.371 -0.715  3.141   1.00 21.68 ?  56  PRO A CD  1 
ATOM   402  N N   . GLU A 1 83  ? -12.804 0.117   0.399   1.00 24.09 ?  57  GLU A N   1 
ATOM   403  C CA  A GLU A 1 83  ? -14.104 0.293   -0.299  0.50 24.03 ?  57  GLU A CA  1 
ATOM   404  C CA  B GLU A 1 83  ? -14.084 0.284   -0.335  0.50 24.45 ?  57  GLU A CA  1 
ATOM   405  C C   . GLU A 1 83  ? -14.310 1.747   -0.733  1.00 23.74 ?  57  GLU A C   1 
ATOM   406  O O   . GLU A 1 83  ? -15.300 2.005   -1.418  1.00 21.87 ?  57  GLU A O   1 
ATOM   407  C CB  A GLU A 1 83  ? -15.246 -0.141  0.612   0.50 25.46 ?  57  GLU A CB  1 
ATOM   408  C CB  B GLU A 1 83  ? -15.200 -0.317  0.510   0.50 26.34 ?  57  GLU A CB  1 
ATOM   409  C CG  A GLU A 1 83  ? -15.162 -1.600  1.014   0.50 26.96 ?  57  GLU A CG  1 
ATOM   410  C CG  B GLU A 1 83  ? -15.040 -1.821  0.624   0.50 28.58 ?  57  GLU A CG  1 
ATOM   411  C CD  A GLU A 1 83  ? -14.291 -1.874  2.229   0.50 28.67 ?  57  GLU A CD  1 
ATOM   412  C CD  B GLU A 1 83  ? -16.033 -2.554  1.504   0.50 31.50 ?  57  GLU A CD  1 
ATOM   413  O OE1 A GLU A 1 83  ? -14.278 -1.036  3.156   0.50 31.45 ?  57  GLU A OE1 1 
ATOM   414  O OE1 B GLU A 1 83  ? -16.563 -1.939  2.452   0.50 32.09 ?  57  GLU A OE1 1 
ATOM   415  O OE2 A GLU A 1 83  ? -13.618 -2.912  2.232   0.50 30.09 ?  57  GLU A OE2 1 
ATOM   416  O OE2 B GLU A 1 83  ? -16.252 -3.755  1.244   0.50 36.82 ?  57  GLU A OE2 1 
ATOM   417  N N   . THR A 1 84  ? -13.417 2.669   -0.335  1.00 21.34 ?  58  THR A N   1 
ATOM   418  C CA  . THR A 1 84  ? -13.520 4.071   -0.747  1.00 19.87 ?  58  THR A CA  1 
ATOM   419  C C   . THR A 1 84  ? -13.450 4.084   -2.283  1.00 20.15 ?  58  THR A C   1 
ATOM   420  O O   . THR A 1 84  ? -12.560 3.414   -2.803  1.00 17.58 ?  58  THR A O   1 
ATOM   421  C CB  . THR A 1 84  ? -12.404 4.951   -0.155  1.00 20.82 ?  58  THR A CB  1 
ATOM   422  O OG1 . THR A 1 84  ? -12.518 4.875   1.273   1.00 20.40 ?  58  THR A OG1 1 
ATOM   423  C CG2 . THR A 1 84  ? -12.468 6.386   -0.598  1.00 20.57 ?  58  THR A CG2 1 
ATOM   424  N N   . LEU A 1 85  ? -14.296 4.873   -2.936  1.00 18.11 ?  59  LEU A N   1 
ATOM   425  C CA  . LEU A 1 85  ? -14.236 5.094   -4.410  1.00 17.81 ?  59  LEU A CA  1 
ATOM   426  C C   . LEU A 1 85  ? -13.299 6.238   -4.717  1.00 19.85 ?  59  LEU A C   1 
ATOM   427  O O   . LEU A 1 85  ? -13.466 7.349   -4.154  1.00 20.35 ?  59  LEU A O   1 
ATOM   428  C CB  . LEU A 1 85  ? -15.622 5.375   -4.974  1.00 18.72 ?  59  LEU A CB  1 
ATOM   429  C CG  . LEU A 1 85  ? -16.606 4.232   -4.808  1.00 19.07 ?  59  LEU A CG  1 
ATOM   430  C CD1 . LEU A 1 85  ? -18.003 4.702   -5.170  1.00 20.81 ?  59  LEU A CD1 1 
ATOM   431  C CD2 . LEU A 1 85  ? -16.191 3.028   -5.628  1.00 22.31 ?  59  LEU A CD2 1 
ATOM   432  N N   . PHE A 1 86  ? -12.411 5.996   -5.672  1.00 18.31 ?  60  PHE A N   1 
ATOM   433  C CA  . PHE A 1 86  ? -11.488 7.000   -6.224  1.00 16.21 ?  60  PHE A CA  1 
ATOM   434  C C   . PHE A 1 86  ? -11.727 7.077   -7.718  1.00 17.73 ?  60  PHE A C   1 
ATOM   435  O O   . PHE A 1 86  ? -12.033 6.011   -8.354  1.00 17.01 ?  60  PHE A O   1 
ATOM   436  C CB  . PHE A 1 86  ? -10.049 6.543   -5.963  1.00 17.28 ?  60  PHE A CB  1 
ATOM   437  C CG  . PHE A 1 86  ? -9.585  6.588   -4.528  1.00 17.67 ?  60  PHE A CG  1 
ATOM   438  C CD1 . PHE A 1 86  ? -9.757  5.507   -3.680  1.00 18.19 ?  60  PHE A CD1 1 
ATOM   439  C CD2 . PHE A 1 86  ? -8.908  7.691   -4.042  1.00 19.97 ?  60  PHE A CD2 1 
ATOM   440  C CE1 . PHE A 1 86  ? -9.338  5.560   -2.355  1.00 18.91 ?  60  PHE A CE1 1 
ATOM   441  C CE2 . PHE A 1 86  ? -8.454  7.724   -2.733  1.00 18.67 ?  60  PHE A CE2 1 
ATOM   442  C CZ  . PHE A 1 86  ? -8.629  6.643   -1.906  1.00 17.61 ?  60  PHE A CZ  1 
ATOM   443  N N   . GLU A 1 87  ? -11.548 8.251   -8.278  1.00 16.27 ?  61  GLU A N   1 
ATOM   444  C CA  . GLU A 1 87  ? -11.373 8.409   -9.735  1.00 16.11 ?  61  GLU A CA  1 
ATOM   445  C C   . GLU A 1 87  ? -10.046 7.771   -10.136 1.00 16.93 ?  61  GLU A C   1 
ATOM   446  O O   . GLU A 1 87  ? -9.038  8.095   -9.501  1.00 17.82 ?  61  GLU A O   1 
ATOM   447  C CB  . GLU A 1 87  ? -11.392 9.892   -10.101 1.00 17.63 ?  61  GLU A CB  1 
ATOM   448  C CG  . GLU A 1 87  ? -12.766 10.506  -9.883  1.00 19.98 ?  61  GLU A CG  1 
ATOM   449  C CD  . GLU A 1 87  ? -12.789 12.014  -10.035 1.00 20.93 ?  61  GLU A CD  1 
ATOM   450  O OE1 . GLU A 1 87  ? -11.775 12.575  -10.537 1.00 20.58 ?  61  GLU A OE1 1 
ATOM   451  O OE2 . GLU A 1 87  ? -13.836 12.620  -9.661  1.00 22.82 ?  61  GLU A OE2 1 
ATOM   452  N N   . ILE A 1 88  ? -10.023 6.923   -11.168 1.00 17.58 ?  62  ILE A N   1 
ATOM   453  C CA  . ILE A 1 88  ? -8.750  6.307   -11.646 1.00 17.33 ?  62  ILE A CA  1 
ATOM   454  C C   . ILE A 1 88  ? -8.281  6.909   -12.991 1.00 18.99 ?  62  ILE A C   1 
ATOM   455  O O   . ILE A 1 88  ? -7.198  6.480   -13.470 1.00 17.38 ?  62  ILE A O   1 
ATOM   456  C CB  . ILE A 1 88  ? -8.885  4.775   -11.697 1.00 17.92 ?  62  ILE A CB  1 
ATOM   457  C CG1 . ILE A 1 88  ? -9.859  4.280   -12.755 1.00 19.06 ?  62  ILE A CG1 1 
ATOM   458  C CG2 . ILE A 1 88  ? -9.244  4.266   -10.322 1.00 19.94 ?  62  ILE A CG2 1 
ATOM   459  C CD1 . ILE A 1 88  ? -9.878  2.773   -12.955 1.00 18.24 ?  62  ILE A CD1 1 
ATOM   460  N N   . GLY A 1 89  ? -9.015  7.875   -13.533 1.00 17.08 ?  63  GLY A N   1 
ATOM   461  C CA  . GLY A 1 89  ? -8.672  8.598   -14.764 1.00 16.66 ?  63  GLY A CA  1 
ATOM   462  C C   . GLY A 1 89  ? -8.331  7.615   -15.880 1.00 18.04 ?  63  GLY A C   1 
ATOM   463  O O   . GLY A 1 89  ? -9.099  6.675   -16.084 1.00 16.62 ?  63  GLY A O   1 
ATOM   464  N N   . SER A 1 90  ? -7.121  7.720   -16.425 1.00 16.41 ?  64  SER A N   1 
ATOM   465  C CA  . SER A 1 90  ? -6.734  6.979   -17.658 1.00 16.17 ?  64  SER A CA  1 
ATOM   466  C C   . SER A 1 90  ? -6.488  5.512   -17.356 1.00 15.72 ?  64  SER A C   1 
ATOM   467  O O   . SER A 1 90  ? -6.359  4.765   -18.320 1.00 17.56 ?  64  SER A O   1 
ATOM   468  C CB  . SER A 1 90  ? -5.524  7.579   -18.271 1.00 17.76 ?  64  SER A CB  1 
ATOM   469  O OG  . SER A 1 90  ? -5.913  8.816   -18.838 1.00 20.03 ?  64  SER A OG  1 
ATOM   470  N N   . VAL A 1 91  ? -6.495  5.065   -16.088 1.00 15.46 ?  65  VAL A N   1 
ATOM   471  C CA  . VAL A 1 91  ? -6.504  3.588   -15.857 1.00 14.65 ?  65  VAL A CA  1 
ATOM   472  C C   . VAL A 1 91  ? -7.797  3.042   -16.486 1.00 15.92 ?  65  VAL A C   1 
ATOM   473  O O   . VAL A 1 91  ? -7.831  1.834   -16.883 1.00 16.91 ?  65  VAL A O   1 
ATOM   474  C CB  . VAL A 1 91  ? -6.341  3.217   -14.364 1.00 15.31 ?  65  VAL A CB  1 
ATOM   475  C CG1 . VAL A 1 91  ? -6.414  1.708   -14.116 1.00 14.70 ?  65  VAL A CG1 1 
ATOM   476  C CG2 . VAL A 1 91  ? -5.009  3.753   -13.821 1.00 17.37 ?  65  VAL A CG2 1 
ATOM   477  N N   . SER A 1 92  ? -8.803  3.898   -16.695 1.00 16.02 ?  66  SER A N   1 
ATOM   478  C CA  . SER A 1 92  ? -10.090 3.513   -17.328 1.00 15.04 ?  66  SER A CA  1 
ATOM   479  C C   . SER A 1 92  ? -9.814  2.925   -18.729 1.00 17.06 ?  66  SER A C   1 
ATOM   480  O O   . SER A 1 92  ? -10.531 2.057   -19.176 1.00 16.65 ?  66  SER A O   1 
ATOM   481  C CB  . SER A 1 92  ? -11.033 4.693   -17.459 1.00 17.10 ?  66  SER A CB  1 
ATOM   482  O OG  . SER A 1 92  ? -11.281 5.232   -16.174 1.00 18.13 ?  66  SER A OG  1 
ATOM   483  N N   . LYS A 1 93  ? -8.729  3.322   -19.352 1.00 15.92 ?  67  LYS A N   1 
ATOM   484  C CA  A LYS A 1 93  ? -8.402  2.857   -20.723 0.50 16.81 ?  67  LYS A CA  1 
ATOM   485  C CA  B LYS A 1 93  ? -8.361  2.869   -20.719 0.50 16.25 ?  67  LYS A CA  1 
ATOM   486  C C   . LYS A 1 93  ? -8.135  1.355   -20.718 1.00 15.75 ?  67  LYS A C   1 
ATOM   487  O O   . LYS A 1 93  ? -8.316  0.730   -21.815 1.00 17.34 ?  67  LYS A O   1 
ATOM   488  C CB  A LYS A 1 93  ? -7.214  3.627   -21.282 0.50 16.91 ?  67  LYS A CB  1 
ATOM   489  C CB  B LYS A 1 93  ? -7.130  3.629   -21.212 0.50 15.68 ?  67  LYS A CB  1 
ATOM   490  C CG  A LYS A 1 93  ? -7.535  5.072   -21.598 0.50 18.05 ?  67  LYS A CG  1 
ATOM   491  C CG  B LYS A 1 93  ? -7.352  5.118   -21.443 0.50 16.03 ?  67  LYS A CG  1 
ATOM   492  C CD  A LYS A 1 93  ? -6.312  5.929   -21.641 0.50 18.19 ?  67  LYS A CD  1 
ATOM   493  C CD  B LYS A 1 93  ? -6.125  5.844   -21.943 0.50 15.28 ?  67  LYS A CD  1 
ATOM   494  C CE  A LYS A 1 93  ? -6.675  7.396   -21.727 0.50 19.67 ?  67  LYS A CE  1 
ATOM   495  C CE  B LYS A 1 93  ? -6.435  7.253   -22.425 0.50 15.98 ?  67  LYS A CE  1 
ATOM   496  N NZ  A LYS A 1 93  ? -5.475  8.227   -21.970 0.50 20.64 ?  67  LYS A NZ  1 
ATOM   497  N NZ  B LYS A 1 93  ? -6.888  8.137   -21.325 0.50 16.07 ?  67  LYS A NZ  1 
ATOM   498  N N   . THR A 1 94  ? -7.735  0.783   -19.587 1.00 17.27 ?  68  THR A N   1 
ATOM   499  C CA  . THR A 1 94  ? -7.495  -0.688  -19.496 1.00 15.52 ?  68  THR A CA  1 
ATOM   500  C C   . THR A 1 94  ? -8.868  -1.397  -19.495 1.00 15.30 ?  68  THR A C   1 
ATOM   501  O O   . THR A 1 94  ? -8.947  -2.479  -20.106 1.00 17.77 ?  68  THR A O   1 
ATOM   502  C CB  . THR A 1 94  ? -6.610  -1.090  -18.327 1.00 17.02 ?  68  THR A CB  1 
ATOM   503  O OG1 . THR A 1 94  ? -7.276  -0.797  -17.111 1.00 16.14 ?  68  THR A OG1 1 
ATOM   504  C CG2 . THR A 1 94  ? -5.245  -0.453  -18.384 1.00 16.70 ?  68  THR A CG2 1 
ATOM   505  N N   . PHE A 1 95  ? -9.892  -0.798  -18.891 1.00 17.08 ?  69  PHE A N   1 
ATOM   506  C CA  . PHE A 1 95  ? -11.279 -1.310  -18.961 1.00 17.47 ?  69  PHE A CA  1 
ATOM   507  C C   . PHE A 1 95  ? -11.756 -1.219  -20.406 1.00 17.61 ?  69  PHE A C   1 
ATOM   508  O O   . PHE A 1 95  ? -12.349 -2.173  -20.870 1.00 18.30 ?  69  PHE A O   1 
ATOM   509  C CB  . PHE A 1 95  ? -12.197 -0.573  -17.984 1.00 17.23 ?  69  PHE A CB  1 
ATOM   510  C CG  . PHE A 1 95  ? -11.971 -0.987  -16.553 1.00 19.04 ?  69  PHE A CG  1 
ATOM   511  C CD1 . PHE A 1 95  ? -12.512 -2.160  -16.056 1.00 20.01 ?  69  PHE A CD1 1 
ATOM   512  C CD2 . PHE A 1 95  ? -11.070 -0.288  -15.752 1.00 20.05 ?  69  PHE A CD2 1 
ATOM   513  C CE1 . PHE A 1 95  ? -12.291 -2.540  -14.733 1.00 23.47 ?  69  PHE A CE1 1 
ATOM   514  C CE2 . PHE A 1 95  ? -10.867 -0.655  -14.433 1.00 21.56 ?  69  PHE A CE2 1 
ATOM   515  C CZ  . PHE A 1 95  ? -11.461 -1.790  -13.921 1.00 21.38 ?  69  PHE A CZ  1 
ATOM   516  N N   . THR A 1 96  ? -11.599 -0.052  -21.039 1.00 16.61 ?  70  THR A N   1 
ATOM   517  C CA  . THR A 1 96  ? -11.968 0.192   -22.445 1.00 15.88 ?  70  THR A CA  1 
ATOM   518  C C   . THR A 1 96  ? -11.317 -0.874  -23.332 1.00 16.51 ?  70  THR A C   1 
ATOM   519  O O   . THR A 1 96  ? -11.987 -1.443  -24.227 1.00 16.81 ?  70  THR A O   1 
ATOM   520  C CB  . THR A 1 96  ? -11.576 1.626   -22.794 1.00 17.17 ?  70  THR A CB  1 
ATOM   521  O OG1 . THR A 1 96  ? -12.267 2.506   -21.890 1.00 17.48 ?  70  THR A OG1 1 
ATOM   522  C CG2 . THR A 1 96  ? -11.951 1.978   -24.216 1.00 17.10 ?  70  THR A CG2 1 
ATOM   523  N N   . ALA A 1 97  ? -10.023 -1.108  -23.161 1.00 16.85 ?  71  ALA A N   1 
ATOM   524  C CA  . ALA A 1 97  ? -9.316  -2.161  -23.919 1.00 15.75 ?  71  ALA A CA  1 
ATOM   525  C C   . ALA A 1 97  ? -9.946  -3.533  -23.689 1.00 16.37 ?  71  ALA A C   1 
ATOM   526  O O   . ALA A 1 97  ? -9.974  -4.358  -24.668 1.00 17.64 ?  71  ALA A O   1 
ATOM   527  C CB  . ALA A 1 97  ? -7.856  -2.158  -23.567 1.00 17.46 ?  71  ALA A CB  1 
ATOM   528  N N   . THR A 1 98  ? -10.397 -3.822  -22.474 1.00 16.95 ?  72  THR A N   1 
ATOM   529  C CA  . THR A 1 98  ? -11.016 -5.119  -22.142 1.00 18.02 ?  72  THR A CA  1 
ATOM   530  C C   . THR A 1 98  ? -12.345 -5.282  -22.895 1.00 19.19 ?  72  THR A C   1 
ATOM   531  O O   . THR A 1 98  ? -12.541 -6.396  -23.488 1.00 17.59 ?  72  THR A O   1 
ATOM   532  C CB  . THR A 1 98  ? -11.194 -5.278  -20.626 1.00 18.96 ?  72  THR A CB  1 
ATOM   533  O OG1 . THR A 1 98  ? -9.919  -5.102  -19.996 1.00 18.93 ?  72  THR A OG1 1 
ATOM   534  C CG2 . THR A 1 98  ? -11.765 -6.626  -20.271 1.00 19.94 ?  72  THR A CG2 1 
ATOM   535  N N   . LEU A 1 99  ? -13.163 -4.229  -22.981 1.00 18.19 ?  73  LEU A N   1 
ATOM   536  C CA  A LEU A 1 99  ? -14.417 -4.274  -23.791 0.50 20.01 ?  73  LEU A CA  1 
ATOM   537  C CA  B LEU A 1 99  ? -14.411 -4.234  -23.795 0.50 19.87 ?  73  LEU A CA  1 
ATOM   538  C C   . LEU A 1 99  ? -14.030 -4.492  -25.259 1.00 19.86 ?  73  LEU A C   1 
ATOM   539  O O   . LEU A 1 99  ? -14.647 -5.353  -25.888 1.00 21.26 ?  73  LEU A O   1 
ATOM   540  C CB  A LEU A 1 99  ? -15.265 -3.009  -23.647 0.50 20.02 ?  73  LEU A CB  1 
ATOM   541  C CB  B LEU A 1 99  ? -15.111 -2.890  -23.622 0.50 19.80 ?  73  LEU A CB  1 
ATOM   542  C CG  A LEU A 1 99  ? -16.476 -2.951  -24.591 0.50 19.17 ?  73  LEU A CG  1 
ATOM   543  C CG  B LEU A 1 99  ? -16.530 -2.769  -24.184 0.50 18.71 ?  73  LEU A CG  1 
ATOM   544  C CD1 A LEU A 1 99  ? -17.531 -3.956  -24.185 0.50 18.68 ?  73  LEU A CD1 1 
ATOM   545  C CD1 B LEU A 1 99  ? -17.305 -1.794  -23.327 0.50 18.77 ?  73  LEU A CD1 1 
ATOM   546  C CD2 A LEU A 1 99  ? -17.072 -1.554  -24.688 0.50 19.51 ?  73  LEU A CD2 1 
ATOM   547  C CD2 B LEU A 1 99  ? -16.525 -2.282  -25.627 0.50 18.72 ?  73  LEU A CD2 1 
ATOM   548  N N   . ALA A 1 100 ? -12.970 -3.834  -25.750 1.00 19.85 ?  74  ALA A N   1 
ATOM   549  C CA  . ALA A 1 100 ? -12.532 -4.039  -27.158 1.00 20.00 ?  74  ALA A CA  1 
ATOM   550  C C   . ALA A 1 100 ? -12.062 -5.501  -27.338 1.00 19.40 ?  74  ALA A C   1 
ATOM   551  O O   . ALA A 1 100 ? -12.383 -6.091  -28.383 1.00 20.56 ?  74  ALA A O   1 
ATOM   552  C CB  . ALA A 1 100 ? -11.444 -3.086  -27.573 1.00 19.67 ?  74  ALA A CB  1 
ATOM   553  N N   . GLY A 1 101 ? -11.312 -6.046  -26.369 1.00 21.65 ?  75  GLY A N   1 
ATOM   554  C CA  . GLY A 1 101 ? -10.879 -7.452  -26.329 1.00 20.14 ?  75  GLY A CA  1 
ATOM   555  C C   . GLY A 1 101 ? -12.042 -8.399  -26.466 1.00 20.39 ?  75  GLY A C   1 
ATOM   556  O O   . GLY A 1 101 ? -11.896 -9.445  -27.158 1.00 25.84 ?  75  GLY A O   1 
ATOM   557  N N   . TYR A 1 102 ? -13.181 -8.045  -25.892 1.00 20.42 ?  76  TYR A N   1 
ATOM   558  C CA  . TYR A 1 102 ? -14.425 -8.853  -25.917 1.00 22.71 ?  76  TYR A CA  1 
ATOM   559  C C   . TYR A 1 102 ? -15.029 -8.792  -27.326 1.00 23.22 ?  76  TYR A C   1 
ATOM   560  O O   . TYR A 1 102 ? -15.403 -9.885  -27.845 1.00 27.75 ?  76  TYR A O   1 
ATOM   561  C CB  . TYR A 1 102 ? -15.408 -8.352  -24.878 1.00 22.42 ?  76  TYR A CB  1 
ATOM   562  C CG  . TYR A 1 102 ? -16.680 -9.155  -24.793 1.00 24.22 ?  76  TYR A CG  1 
ATOM   563  C CD1 . TYR A 1 102 ? -16.657 -10.448 -24.316 1.00 26.95 ?  76  TYR A CD1 1 
ATOM   564  C CD2 . TYR A 1 102 ? -17.893 -8.593  -25.112 1.00 28.39 ?  76  TYR A CD2 1 
ATOM   565  C CE1 . TYR A 1 102 ? -17.821 -11.188 -24.188 1.00 28.51 ?  76  TYR A CE1 1 
ATOM   566  C CE2 . TYR A 1 102 ? -19.072 -9.321  -25.009 1.00 32.41 ?  76  TYR A CE2 1 
ATOM   567  C CZ  . TYR A 1 102 ? -19.033 -10.614 -24.516 1.00 31.84 ?  76  TYR A CZ  1 
ATOM   568  O OH  . TYR A 1 102 ? -20.178 -11.358 -24.350 1.00 37.80 ?  76  TYR A OH  1 
ATOM   569  N N   . ALA A 1 103 ? -15.124 -7.603  -27.930 1.00 24.27 ?  77  ALA A N   1 
ATOM   570  C CA  . ALA A 1 103 ? -15.543 -7.428  -29.352 1.00 24.14 ?  77  ALA A CA  1 
ATOM   571  C C   . ALA A 1 103 ? -14.616 -8.252  -30.261 1.00 26.12 ?  77  ALA A C   1 
ATOM   572  O O   . ALA A 1 103 ? -15.131 -8.946  -31.188 1.00 26.81 ?  77  ALA A O   1 
ATOM   573  C CB  . ALA A 1 103 ? -15.586 -5.976  -29.755 1.00 24.07 ?  77  ALA A CB  1 
ATOM   574  N N   . LEU A 1 104 ? -13.293 -8.187  -30.061 1.00 23.76 ?  78  LEU A N   1 
ATOM   575  C CA  . LEU A 1 104 ? -12.347 -9.040  -30.829 1.00 25.29 ?  78  LEU A CA  1 
ATOM   576  C C   . LEU A 1 104 ? -12.655 -10.521 -30.612 1.00 27.34 ?  78  LEU A C   1 
ATOM   577  O O   . LEU A 1 104 ? -12.751 -11.265 -31.620 1.00 33.65 ?  78  LEU A O   1 
ATOM   578  C CB  . LEU A 1 104 ? -10.909 -8.720  -30.417 1.00 25.53 ?  78  LEU A CB  1 
ATOM   579  C CG  . LEU A 1 104 ? -10.453 -7.309  -30.757 1.00 26.11 ?  78  LEU A CG  1 
ATOM   580  C CD1 . LEU A 1 104 ? -9.134  -7.015  -30.057 1.00 26.01 ?  78  LEU A CD1 1 
ATOM   581  C CD2 . LEU A 1 104 ? -10.358 -7.110  -32.264 1.00 25.05 ?  78  LEU A CD2 1 
ATOM   582  N N   . ALA A 1 105 ? -12.779 -10.958 -29.365 1.00 28.62 ?  79  ALA A N   1 
ATOM   583  C CA  . ALA A 1 105 ? -13.027 -12.375 -29.008 1.00 29.64 ?  79  ALA A CA  1 
ATOM   584  C C   . ALA A 1 105 ? -14.300 -12.884 -29.691 1.00 31.91 ?  79  ALA A C   1 
ATOM   585  O O   . ALA A 1 105 ? -14.358 -14.086 -30.005 1.00 35.03 ?  79  ALA A O   1 
ATOM   586  C CB  . ALA A 1 105 ? -13.125 -12.546 -27.511 1.00 29.54 ?  79  ALA A CB  1 
ATOM   587  N N   . GLN A 1 106 ? -15.305 -12.032 -29.883 1.00 33.75 ?  80  GLN A N   1 
ATOM   588  C CA  . GLN A 1 106 ? -16.599 -12.429 -30.494 1.00 36.06 ?  80  GLN A CA  1 
ATOM   589  C C   . GLN A 1 106 ? -16.589 -12.220 -32.015 1.00 32.70 ?  80  GLN A C   1 
ATOM   590  O O   . GLN A 1 106 ? -17.678 -12.329 -32.596 1.00 35.18 ?  80  GLN A O   1 
ATOM   591  C CB  . GLN A 1 106 ? -17.735 -11.635 -29.861 1.00 39.40 ?  80  GLN A CB  1 
ATOM   592  C CG  . GLN A 1 106 ? -17.982 -12.053 -28.427 1.00 42.50 ?  80  GLN A CG  1 
ATOM   593  C CD  . GLN A 1 106 ? -19.449 -12.053 -28.097 1.00 46.69 ?  80  GLN A CD  1 
ATOM   594  O OE1 . GLN A 1 106 ? -20.187 -11.147 -28.467 1.00 56.04 ?  80  GLN A OE1 1 
ATOM   595  N NE2 . GLN A 1 106 ? -19.882 -13.082 -27.391 1.00 54.48 ?  80  GLN A NE2 1 
ATOM   596  N N   . ASP A 1 107 ? -15.440 -11.876 -32.616 1.00 34.37 ?  81  ASP A N   1 
ATOM   597  C CA  . ASP A 1 107 ? -15.284 -11.638 -34.078 1.00 39.14 ?  81  ASP A CA  1 
ATOM   598  C C   . ASP A 1 107 ? -16.226 -10.530 -34.555 1.00 37.37 ?  81  ASP A C   1 
ATOM   599  O O   . ASP A 1 107 ? -16.702 -10.605 -35.693 1.00 36.47 ?  81  ASP A O   1 
ATOM   600  C CB  . ASP A 1 107 ? -15.650 -12.877 -34.914 1.00 46.85 ?  81  ASP A CB  1 
ATOM   601  C CG  . ASP A 1 107 ? -14.950 -14.161 -34.508 1.00 55.85 ?  81  ASP A CG  1 
ATOM   602  O OD1 . ASP A 1 107 ? -13.749 -14.088 -34.172 1.00 52.91 ?  81  ASP A OD1 1 
ATOM   603  O OD2 . ASP A 1 107 ? -15.613 -15.236 -34.549 1.00 63.55 ?  81  ASP A OD2 1 
ATOM   604  N N   . LYS A 1 108 ? -16.487 -9.508  -33.751 1.00 29.48 ?  82  LYS A N   1 
ATOM   605  C CA  . LYS A 1 108 ? -17.339 -8.384  -34.194 1.00 26.87 ?  82  LYS A CA  1 
ATOM   606  C C   . LYS A 1 108 ? -16.485 -7.291  -34.841 1.00 23.46 ?  82  LYS A C   1 
ATOM   607  O O   . LYS A 1 108 ? -17.042 -6.405  -35.490 1.00 24.29 ?  82  LYS A O   1 
ATOM   608  C CB  . LYS A 1 108 ? -18.144 -7.918  -32.985 1.00 31.68 ?  82  LYS A CB  1 
ATOM   609  C CG  . LYS A 1 108 ? -19.057 -8.989  -32.407 1.00 36.23 ?  82  LYS A CG  1 
ATOM   610  C CD  . LYS A 1 108 ? -19.860 -9.726  -33.474 1.00 40.79 ?  82  LYS A CD  1 
ATOM   611  C CE  . LYS A 1 108 ? -21.306 -9.299  -33.573 1.00 47.85 ?  82  LYS A CE  1 
ATOM   612  N NZ  . LYS A 1 108 ? -22.150 -10.128 -32.683 1.00 50.15 ?  82  LYS A NZ  1 
ATOM   613  N N   . MET A 1 109 ? -15.170 -7.362  -34.676 1.00 24.67 ?  83  MET A N   1 
ATOM   614  C CA  . MET A 1 109 ? -14.241 -6.366  -35.232 1.00 24.25 ?  83  MET A CA  1 
ATOM   615  C C   . MET A 1 109 ? -12.878 -7.028  -35.266 1.00 22.47 ?  83  MET A C   1 
ATOM   616  O O   . MET A 1 109 ? -12.699 -8.051  -34.566 1.00 23.74 ?  83  MET A O   1 
ATOM   617  C CB  . MET A 1 109 ? -14.186 -5.099  -34.357 1.00 24.85 ?  83  MET A CB  1 
ATOM   618  C CG  . MET A 1 109 ? -13.534 -5.284  -33.009 1.00 25.88 ?  83  MET A CG  1 
ATOM   619  S SD  . MET A 1 109 ? -13.561 -3.710  -32.046 1.00 25.79 ?  83  MET A SD  1 
ATOM   620  C CE  . MET A 1 109 ? -11.835 -3.670  -31.592 1.00 25.28 ?  83  MET A CE  1 
ATOM   621  N N   . ARG A 1 110 ? -11.964 -6.442  -36.017 1.00 26.13 ?  84  ARG A N   1 
ATOM   622  C CA  . ARG A 1 110 ? -10.552 -6.891  -36.074 1.00 27.08 ?  84  ARG A CA  1 
ATOM   623  C C   . ARG A 1 110 ? -9.689  -5.646  -35.966 1.00 23.67 ?  84  ARG A C   1 
ATOM   624  O O   . ARG A 1 110 ? -10.107 -4.584  -36.471 1.00 27.16 ?  84  ARG A O   1 
ATOM   625  C CB  . ARG A 1 110 ? -10.264 -7.689  -37.354 1.00 31.14 ?  84  ARG A CB  1 
ATOM   626  C CG  . ARG A 1 110 ? -10.968 -9.043  -37.403 1.00 36.44 ?  84  ARG A CG  1 
ATOM   627  C CD  . ARG A 1 110 ? -11.119 -9.686  -38.772 1.00 45.80 ?  84  ARG A CD  1 
ATOM   628  N NE  . ARG A 1 110 ? -10.058 -9.311  -39.700 1.00 56.69 ?  84  ARG A NE  1 
ATOM   629  C CZ  . ARG A 1 110 ? -9.840  -9.859  -40.900 1.00 62.33 ?  84  ARG A CZ  1 
ATOM   630  N NH1 . ARG A 1 110 ? -10.612 -10.840 -41.361 1.00 52.50 ?  84  ARG A NH1 1 
ATOM   631  N NH2 . ARG A 1 110 ? -8.841  -9.398  -41.638 1.00 65.28 ?  84  ARG A NH2 1 
ATOM   632  N N   . LEU A 1 111 ? -8.511  -5.786  -35.366 1.00 27.01 ?  85  LEU A N   1 
ATOM   633  C CA  . LEU A 1 111 ? -7.630  -4.606  -35.112 1.00 27.32 ?  85  LEU A CA  1 
ATOM   634  C C   . LEU A 1 111 ? -7.216  -3.958  -36.445 1.00 27.12 ?  85  LEU A C   1 
ATOM   635  O O   . LEU A 1 111 ? -7.048  -2.731  -36.474 1.00 25.32 ?  85  LEU A O   1 
ATOM   636  C CB  . LEU A 1 111 ? -6.418  -5.035  -34.295 1.00 26.27 ?  85  LEU A CB  1 
ATOM   637  C CG  . LEU A 1 111 ? -6.706  -5.366  -32.829 1.00 29.55 ?  85  LEU A CG  1 
ATOM   638  C CD1 . LEU A 1 111 ? -5.504  -6.031  -32.196 1.00 31.27 ?  85  LEU A CD1 1 
ATOM   639  C CD2 . LEU A 1 111 ? -7.082  -4.122  -32.043 1.00 29.51 ?  85  LEU A CD2 1 
ATOM   640  N N   . ASP A 1 112 ? -7.112  -4.704  -37.551 1.00 28.15 ?  86  ASP A N   1 
ATOM   641  C CA  . ASP A 1 112 ? -6.751  -4.049  -38.840 1.00 31.50 ?  86  ASP A CA  1 
ATOM   642  C C   . ASP A 1 112 ? -7.983  -3.541  -39.585 1.00 32.58 ?  86  ASP A C   1 
ATOM   643  O O   . ASP A 1 112 ? -7.783  -2.978  -40.695 1.00 34.05 ?  86  ASP A O   1 
ATOM   644  C CB  . ASP A 1 112 ? -5.842  -4.890  -39.739 1.00 36.87 ?  86  ASP A CB  1 
ATOM   645  C CG  . ASP A 1 112 ? -6.325  -6.301  -39.997 1.00 45.10 ?  86  ASP A CG  1 
ATOM   646  O OD1 . ASP A 1 112 ? -7.483  -6.612  -39.602 1.00 42.38 ?  86  ASP A OD1 1 
ATOM   647  O OD2 . ASP A 1 112 ? -5.522  -7.089  -40.574 1.00 48.94 ?  86  ASP A OD2 1 
ATOM   648  N N   . ASP A 1 113 ? -9.184  -3.602  -39.004 1.00 29.19 ?  87  ASP A N   1 
ATOM   649  C CA  . ASP A 1 113 ? -10.364 -2.949  -39.618 1.00 26.69 ?  87  ASP A CA  1 
ATOM   650  C C   . ASP A 1 113 ? -10.104 -1.458  -39.750 1.00 30.56 ?  87  ASP A C   1 
ATOM   651  O O   . ASP A 1 113 ? -9.508  -0.853  -38.812 1.00 25.51 ?  87  ASP A O   1 
ATOM   652  C CB  . ASP A 1 113 ? -11.652 -3.107  -38.819 1.00 26.14 ?  87  ASP A CB  1 
ATOM   653  C CG  . ASP A 1 113 ? -12.231 -4.503  -38.773 1.00 30.30 ?  87  ASP A CG  1 
ATOM   654  O OD1 . ASP A 1 113 ? -11.743 -5.400  -39.535 1.00 32.83 ?  87  ASP A OD1 1 
ATOM   655  O OD2 . ASP A 1 113 ? -13.138 -4.694  -37.942 1.00 32.78 ?  87  ASP A OD2 1 
ATOM   656  N N   . ARG A 1 114 ? -10.572 -0.857  -40.848 1.00 30.38 ?  88  ARG A N   1 
ATOM   657  C CA  . ARG A 1 114 ? -10.607 0.613   -40.997 1.00 29.69 ?  88  ARG A CA  1 
ATOM   658  C C   . ARG A 1 114 ? -11.656 1.173   -40.024 1.00 30.20 ?  88  ARG A C   1 
ATOM   659  O O   . ARG A 1 114 ? -12.782 0.603   -39.959 1.00 29.15 ?  88  ARG A O   1 
ATOM   660  C CB  . ARG A 1 114 ? -10.939 0.988   -42.448 1.00 34.99 ?  88  ARG A CB  1 
ATOM   661  C CG  . ARG A 1 114 ? -10.093 0.300   -43.511 1.00 39.67 ?  88  ARG A CG  1 
ATOM   662  C CD  . ARG A 1 114 ? -8.619  0.656   -43.401 1.00 46.62 ?  88  ARG A CD  1 
ATOM   663  N NE  . ARG A 1 114 ? -7.864  -0.467  -42.855 1.00 60.00 ?  88  ARG A NE  1 
ATOM   664  C CZ  . ARG A 1 114 ? -6.599  -0.423  -42.429 1.00 60.00 ?  88  ARG A CZ  1 
ATOM   665  N NH1 . ARG A 1 114 ? -5.920  0.713   -42.474 1.00 63.65 ?  88  ARG A NH1 1 
ATOM   666  N NH2 . ARG A 1 114 ? -6.021  -1.520  -41.960 1.00 51.92 ?  88  ARG A NH2 1 
ATOM   667  N N   . ALA A 1 115 ? -11.340 2.250   -39.301 1.00 29.19 ?  89  ALA A N   1 
ATOM   668  C CA  . ALA A 1 115 ? -12.198 2.828   -38.235 1.00 30.47 ?  89  ALA A CA  1 
ATOM   669  C C   . ALA A 1 115 ? -13.616 3.101   -38.748 1.00 30.49 ?  89  ALA A C   1 
ATOM   670  O O   . ALA A 1 115 ? -14.591 2.778   -38.042 1.00 30.54 ?  89  ALA A O   1 
ATOM   671  C CB  . ALA A 1 115 ? -11.586 4.099   -37.677 1.00 31.26 ?  89  ALA A CB  1 
ATOM   672  N N   . SER A 1 116 ? -13.747 3.708   -39.925 1.00 26.70 ?  90  SER A N   1 
ATOM   673  C CA  . SER A 1 116 ? -15.053 4.145   -40.455 1.00 26.76 ?  90  SER A CA  1 
ATOM   674  C C   . SER A 1 116 ? -15.951 2.930   -40.761 1.00 24.97 ?  90  SER A C   1 
ATOM   675  O O   . SER A 1 116 ? -17.174 3.133   -40.898 1.00 28.97 ?  90  SER A O   1 
ATOM   676  C CB  . SER A 1 116 ? -14.895 5.051   -41.639 1.00 25.84 ?  90  SER A CB  1 
ATOM   677  O OG  . SER A 1 116 ? -14.215 4.368   -42.690 1.00 27.56 ?  90  SER A OG  1 
ATOM   678  N N   . GLN A 1 117 ? -15.440 1.698   -40.810 1.00 27.79 ?  91  GLN A N   1 
ATOM   679  C CA  . GLN A 1 117 ? -16.340 0.530   -41.065 1.00 30.58 ?  91  GLN A CA  1 
ATOM   680  C C   . GLN A 1 117 ? -17.356 0.402   -39.926 1.00 29.39 ?  91  GLN A C   1 
ATOM   681  O O   . GLN A 1 117 ? -18.418 -0.186  -40.141 1.00 29.59 ?  91  GLN A O   1 
ATOM   682  C CB  . GLN A 1 117 ? -15.595 -0.793  -41.282 1.00 34.13 ?  91  GLN A CB  1 
ATOM   683  C CG  . GLN A 1 117 ? -14.917 -0.908  -42.651 1.00 40.77 ?  91  GLN A CG  1 
ATOM   684  C CD  . GLN A 1 117 ? -15.833 -1.119  -43.846 1.00 45.13 ?  91  GLN A CD  1 
ATOM   685  O OE1 . GLN A 1 117 ? -16.155 -2.239  -44.252 1.00 40.95 ?  91  GLN A OE1 1 
ATOM   686  N NE2 . GLN A 1 117 ? -16.180 -0.034  -44.510 1.00 47.86 ?  91  GLN A NE2 1 
ATOM   687  N N   . HIS A 1 118 ? -17.069 0.962   -38.758 1.00 28.92 ?  92  HIS A N   1 
ATOM   688  C CA  . HIS A 1 118 ? -17.838 0.723   -37.517 1.00 28.40 ?  92  HIS A CA  1 
ATOM   689  C C   . HIS A 1 118 ? -18.681 1.937   -37.152 1.00 28.76 ?  92  HIS A C   1 
ATOM   690  O O   . HIS A 1 118 ? -19.366 1.862   -36.110 1.00 29.98 ?  92  HIS A O   1 
ATOM   691  C CB  . HIS A 1 118 ? -16.862 0.299   -36.410 1.00 26.42 ?  92  HIS A CB  1 
ATOM   692  C CG  . HIS A 1 118 ? -16.231 -1.018  -36.667 1.00 26.18 ?  92  HIS A CG  1 
ATOM   693  N ND1 . HIS A 1 118 ? -16.941 -2.188  -36.605 1.00 25.99 ?  92  HIS A ND1 1 
ATOM   694  C CD2 . HIS A 1 118 ? -14.988 -1.349  -37.065 1.00 25.48 ?  92  HIS A CD2 1 
ATOM   695  C CE1 . HIS A 1 118 ? -16.148 -3.202  -36.888 1.00 24.35 ?  92  HIS A CE1 1 
ATOM   696  N NE2 . HIS A 1 118 ? -14.929 -2.715  -37.154 1.00 27.22 ?  92  HIS A NE2 1 
ATOM   697  N N   . TRP A 1 119 ? -18.673 2.982   -37.991 1.00 27.16 ?  93  TRP A N   1 
ATOM   698  C CA  . TRP A 1 119 ? -19.470 4.211   -37.766 1.00 28.56 ?  93  TRP A CA  1 
ATOM   699  C C   . TRP A 1 119 ? -19.679 4.924   -39.092 1.00 28.67 ?  93  TRP A C   1 
ATOM   700  O O   . TRP A 1 119 ? -18.802 5.646   -39.536 1.00 28.48 ?  93  TRP A O   1 
ATOM   701  C CB  . TRP A 1 119 ? -18.796 5.126   -36.730 1.00 25.59 ?  93  TRP A CB  1 
ATOM   702  C CG  . TRP A 1 119 ? -19.648 6.244   -36.211 1.00 27.52 ?  93  TRP A CG  1 
ATOM   703  C CD1 . TRP A 1 119 ? -20.987 6.450   -36.416 1.00 28.11 ?  93  TRP A CD1 1 
ATOM   704  C CD2 . TRP A 1 119 ? -19.206 7.340   -35.384 1.00 25.30 ?  93  TRP A CD2 1 
ATOM   705  N NE1 . TRP A 1 119 ? -21.397 7.592   -35.780 1.00 27.84 ?  93  TRP A NE1 1 
ATOM   706  C CE2 . TRP A 1 119 ? -20.328 8.159   -35.137 1.00 25.61 ?  93  TRP A CE2 1 
ATOM   707  C CE3 . TRP A 1 119 ? -17.970 7.705   -34.830 1.00 26.70 ?  93  TRP A CE3 1 
ATOM   708  C CZ2 . TRP A 1 119 ? -20.263 9.280   -34.310 1.00 26.72 ?  93  TRP A CZ2 1 
ATOM   709  C CZ3 . TRP A 1 119 ? -17.901 8.830   -34.042 1.00 25.51 ?  93  TRP A CZ3 1 
ATOM   710  C CH2 . TRP A 1 119 ? -19.033 9.608   -33.789 1.00 26.66 ?  93  TRP A CH2 1 
ATOM   711  N N   . PRO A 1 120 ? -20.878 4.795   -39.722 1.00 30.74 ?  94  PRO A N   1 
ATOM   712  C CA  . PRO A 1 120 ? -21.150 5.415   -41.019 1.00 27.87 ?  94  PRO A CA  1 
ATOM   713  C C   . PRO A 1 120 ? -20.912 6.922   -41.102 1.00 27.18 ?  94  PRO A C   1 
ATOM   714  O O   . PRO A 1 120 ? -20.470 7.406   -42.110 1.00 27.47 ?  94  PRO A O   1 
ATOM   715  C CB  . PRO A 1 120 ? -22.641 5.090   -41.205 1.00 32.22 ?  94  PRO A CB  1 
ATOM   716  C CG  . PRO A 1 120 ? -22.737 3.728   -40.599 1.00 31.15 ?  94  PRO A CG  1 
ATOM   717  C CD  . PRO A 1 120 ? -21.966 3.897   -39.300 1.00 29.87 ?  94  PRO A CD  1 
ATOM   718  N N   . ALA A 1 121 ? -21.123 7.642   -40.010 1.00 26.42 ?  95  ALA A N   1 
ATOM   719  C CA  . ALA A 1 121 ? -20.970 9.100   -39.982 1.00 28.93 ?  95  ALA A CA  1 
ATOM   720  C C   . ALA A 1 121 ? -19.501 9.439   -40.262 1.00 27.11 ?  95  ALA A C   1 
ATOM   721  O O   . ALA A 1 121 ? -19.221 10.546  -40.727 1.00 31.61 ?  95  ALA A O   1 
ATOM   722  C CB  . ALA A 1 121 ? -21.480 9.610   -38.645 1.00 33.09 ?  95  ALA A CB  1 
ATOM   723  N N   . LEU A 1 122 ? -18.573 8.508   -40.040 1.00 25.98 ?  96  LEU A N   1 
ATOM   724  C CA  . LEU A 1 122 ? -17.143 8.770   -40.338 1.00 27.59 ?  96  LEU A CA  1 
ATOM   725  C C   . LEU A 1 122 ? -16.781 8.384   -41.780 1.00 28.90 ?  96  LEU A C   1 
ATOM   726  O O   . LEU A 1 122 ? -15.622 8.627   -42.151 1.00 27.54 ?  96  LEU A O   1 
ATOM   727  C CB  . LEU A 1 122 ? -16.277 7.972   -39.365 1.00 30.54 ?  96  LEU A CB  1 
ATOM   728  C CG  . LEU A 1 122 ? -16.391 8.357   -37.894 1.00 31.87 ?  96  LEU A CG  1 
ATOM   729  C CD1 . LEU A 1 122 ? -15.266 7.704   -37.137 1.00 31.88 ?  96  LEU A CD1 1 
ATOM   730  C CD2 . LEU A 1 122 ? -16.401 9.864   -37.691 1.00 32.59 ?  96  LEU A CD2 1 
ATOM   731  N N   . GLN A 1 123 ? -17.656 7.692   -42.514 1.00 27.39 ?  97  GLN A N   1 
ATOM   732  C CA  . GLN A 1 123 ? -17.308 7.257   -43.897 1.00 31.47 ?  97  GLN A CA  1 
ATOM   733  C C   . GLN A 1 123 ? -17.095 8.509   -44.756 1.00 32.01 ?  97  GLN A C   1 
ATOM   734  O O   . GLN A 1 123 ? -17.811 9.516   -44.560 1.00 35.81 ?  97  GLN A O   1 
ATOM   735  C CB  . GLN A 1 123 ? -18.369 6.355   -44.503 1.00 34.49 ?  97  GLN A CB  1 
ATOM   736  C CG  . GLN A 1 123 ? -18.357 4.955   -43.940 1.00 38.71 ?  97  GLN A CG  1 
ATOM   737  C CD  . GLN A 1 123 ? -19.534 4.228   -44.545 1.00 49.56 ?  97  GLN A CD  1 
ATOM   738  O OE1 . GLN A 1 123 ? -20.665 4.684   -44.422 1.00 46.88 ?  97  GLN A OE1 1 
ATOM   739  N NE2 . GLN A 1 123 ? -19.274 3.135   -45.251 1.00 57.84 ?  97  GLN A NE2 1 
ATOM   740  N N   . GLY A 1 124 ? -16.066 8.487   -45.608 1.00 34.90 ?  98  GLY A N   1 
ATOM   741  C CA  . GLY A 1 124 ? -15.620 9.673   -46.363 1.00 33.01 ?  98  GLY A CA  1 
ATOM   742  C C   . GLY A 1 124 ? -14.667 10.558  -45.571 1.00 33.29 ?  98  GLY A C   1 
ATOM   743  O O   . GLY A 1 124 ? -14.146 11.503  -46.175 1.00 34.79 ?  98  GLY A O   1 
ATOM   744  N N   . SER A 1 125 ? -14.415 10.299  -44.272 1.00 30.49 ?  99  SER A N   1 
ATOM   745  C CA  . SER A 1 125 ? -13.473 11.128  -43.462 1.00 26.54 ?  99  SER A CA  1 
ATOM   746  C C   . SER A 1 125 ? -12.086 10.505  -43.593 1.00 26.22 ?  99  SER A C   1 
ATOM   747  O O   . SER A 1 125 ? -11.979 9.429   -44.201 1.00 28.94 ?  99  SER A O   1 
ATOM   748  C CB  . SER A 1 125 ? -13.873 11.222  -42.003 1.00 24.81 ?  99  SER A CB  1 
ATOM   749  O OG  . SER A 1 125 ? -13.608 9.976   -41.322 1.00 23.94 ?  99  SER A OG  1 
ATOM   750  N N   . ARG A 1 126 ? -11.080 11.100  -42.950 1.00 26.03 ?  100 ARG A N   1 
ATOM   751  C CA  . ARG A 1 126 ? -9.717  10.519  -42.900 1.00 27.47 ?  100 ARG A CA  1 
ATOM   752  C C   . ARG A 1 126 ? -9.732  9.192   -42.114 1.00 28.55 ?  100 ARG A C   1 
ATOM   753  O O   . ARG A 1 126 ? -8.735  8.469   -42.195 1.00 25.57 ?  100 ARG A O   1 
ATOM   754  C CB  . ARG A 1 126 ? -8.756  11.573  -42.346 1.00 27.75 ?  100 ARG A CB  1 
ATOM   755  C CG  . ARG A 1 126 ? -8.677  12.832  -43.194 1.00 31.03 ?  100 ARG A CG  1 
ATOM   756  C CD  . ARG A 1 126 ? -8.226  12.579  -44.616 1.00 34.13 ?  100 ARG A CD  1 
ATOM   757  N NE  . ARG A 1 126 ? -6.876  12.032  -44.591 1.00 46.01 ?  100 ARG A NE  1 
ATOM   758  C CZ  . ARG A 1 126 ? -5.751  12.747  -44.713 1.00 49.82 ?  100 ARG A CZ  1 
ATOM   759  N NH1 . ARG A 1 126 ? -5.800  14.058  -44.908 1.00 50.64 ?  100 ARG A NH1 1 
ATOM   760  N NH2 . ARG A 1 126 ? -4.578  12.138  -44.638 1.00 44.95 ?  100 ARG A NH2 1 
ATOM   761  N N   . PHE A 1 127 ? -10.819 8.860   -41.397 1.00 26.48 ?  101 PHE A N   1 
ATOM   762  C CA  . PHE A 1 127 ? -10.910 7.602   -40.603 1.00 26.65 ?  101 PHE A CA  1 
ATOM   763  C C   . PHE A 1 127 ? -11.164 6.399   -41.517 1.00 25.33 ?  101 PHE A C   1 
ATOM   764  O O   . PHE A 1 127 ? -11.122 5.248   -41.054 1.00 27.24 ?  101 PHE A O   1 
ATOM   765  C CB  . PHE A 1 127 ? -11.928 7.766   -39.477 1.00 27.07 ?  101 PHE A CB  1 
ATOM   766  C CG  . PHE A 1 127 ? -11.364 8.628   -38.380 1.00 25.08 ?  101 PHE A CG  1 
ATOM   767  C CD1 . PHE A 1 127 ? -10.391 8.118   -37.530 1.00 27.15 ?  101 PHE A CD1 1 
ATOM   768  C CD2 . PHE A 1 127 ? -11.690 9.970   -38.295 1.00 26.60 ?  101 PHE A CD2 1 
ATOM   769  C CE1 . PHE A 1 127 ? -9.783  8.925   -36.569 1.00 25.39 ?  101 PHE A CE1 1 
ATOM   770  C CE2 . PHE A 1 127 ? -11.118 10.765  -37.305 1.00 26.87 ?  101 PHE A CE2 1 
ATOM   771  C CZ  . PHE A 1 127 ? -10.159 10.241  -36.454 1.00 26.26 ?  101 PHE A CZ  1 
ATOM   772  N N   . ASP A 1 128 ? -11.368 6.647   -42.800 1.00 26.54 ?  102 ASP A N   1 
ATOM   773  C CA  . ASP A 1 128 ? -11.355 5.581   -43.841 1.00 26.79 ?  102 ASP A CA  1 
ATOM   774  C C   . ASP A 1 128 ? -9.949  4.963   -43.938 1.00 27.26 ?  102 ASP A C   1 
ATOM   775  O O   . ASP A 1 128 ? -9.841  3.847   -44.485 1.00 29.86 ?  102 ASP A O   1 
ATOM   776  C CB  . ASP A 1 128 ? -11.766 6.165   -45.198 1.00 28.43 ?  102 ASP A CB  1 
ATOM   777  C CG  . ASP A 1 128 ? -13.237 6.520   -45.350 1.00 32.91 ?  102 ASP A CG  1 
ATOM   778  O OD1 . ASP A 1 128 ? -14.060 6.129   -44.496 1.00 31.86 ?  102 ASP A OD1 1 
ATOM   779  O OD2 . ASP A 1 128 ? -13.542 7.241   -46.312 1.00 38.14 ?  102 ASP A OD2 1 
ATOM   780  N N   . GLY A 1 129 ? -8.906  5.693   -43.514 1.00 27.88 ?  103 GLY A N   1 
ATOM   781  C CA  . GLY A 1 129 ? -7.495  5.319   -43.726 1.00 28.36 ?  103 GLY A CA  1 
ATOM   782  C C   . GLY A 1 129 ? -6.766  4.991   -42.441 1.00 30.48 ?  103 GLY A C   1 
ATOM   783  O O   . GLY A 1 129 ? -5.517  4.875   -42.464 1.00 29.67 ?  103 GLY A O   1 
ATOM   784  N N   . ILE A 1 130 ? -7.518  4.838   -41.357 1.00 28.84 ?  104 ILE A N   1 
ATOM   785  C CA  . ILE A 1 130 ? -6.969  4.645   -39.992 1.00 26.05 ?  104 ILE A CA  1 
ATOM   786  C C   . ILE A 1 130 ? -7.545  3.337   -39.444 1.00 23.95 ?  104 ILE A C   1 
ATOM   787  O O   . ILE A 1 130 ? -8.771  3.128   -39.474 1.00 23.30 ?  104 ILE A O   1 
ATOM   788  C CB  . ILE A 1 130 ? -7.268  5.903   -39.151 1.00 25.96 ?  104 ILE A CB  1 
ATOM   789  C CG1 . ILE A 1 130 ? -6.536  7.086   -39.793 1.00 26.44 ?  104 ILE A CG1 1 
ATOM   790  C CG2 . ILE A 1 130 ? -6.916  5.706   -37.670 1.00 27.77 ?  104 ILE A CG2 1 
ATOM   791  C CD1 . ILE A 1 130 ? -6.816  8.431   -39.216 1.00 30.77 ?  104 ILE A CD1 1 
ATOM   792  N N   . SER A 1 131 ? -6.676  2.473   -38.952 1.00 23.47 ?  105 SER A N   1 
ATOM   793  C CA  . SER A 1 131 ? -7.067  1.174   -38.352 1.00 24.08 ?  105 SER A CA  1 
ATOM   794  C C   . SER A 1 131 ? -7.535  1.368   -36.898 1.00 23.55 ?  105 SER A C   1 
ATOM   795  O O   . SER A 1 131 ? -7.232  2.381   -36.287 1.00 21.17 ?  105 SER A O   1 
ATOM   796  C CB  . SER A 1 131 ? -5.940  0.212   -38.438 1.00 27.05 ?  105 SER A CB  1 
ATOM   797  O OG  . SER A 1 131 ? -4.963  0.531   -37.470 1.00 25.91 ?  105 SER A OG  1 
ATOM   798  N N   . LEU A 1 132 ? -8.319  0.426   -36.386 1.00 24.10 ?  106 LEU A N   1 
ATOM   799  C CA  . LEU A 1 132 ? -8.661  0.344   -34.942 1.00 23.95 ?  106 LEU A CA  1 
ATOM   800  C C   . LEU A 1 132 ? -7.366  0.247   -34.105 1.00 23.01 ?  106 LEU A C   1 
ATOM   801  O O   . LEU A 1 132 ? -7.278  0.963   -33.045 1.00 21.76 ?  106 LEU A O   1 
ATOM   802  C CB  . LEU A 1 132 ? -9.565  -0.867  -34.731 1.00 22.84 ?  106 LEU A CB  1 
ATOM   803  C CG  . LEU A 1 132 ? -10.945 -0.763  -35.378 1.00 23.59 ?  106 LEU A CG  1 
ATOM   804  C CD1 . LEU A 1 132 ? -11.823 -1.960  -35.054 1.00 25.06 ?  106 LEU A CD1 1 
ATOM   805  C CD2 . LEU A 1 132 ? -11.643 0.534   -35.020 1.00 23.31 ?  106 LEU A CD2 1 
ATOM   806  N N   . LEU A 1 133 ? -6.403  -0.576  -34.524 1.00 22.44 ?  107 LEU A N   1 
ATOM   807  C CA  . LEU A 1 133 ? -5.098  -0.693  -33.812 1.00 22.04 ?  107 LEU A CA  1 
ATOM   808  C C   . LEU A 1 133 ? -4.441  0.689   -33.621 1.00 23.18 ?  107 LEU A C   1 
ATOM   809  O O   . LEU A 1 133 ? -4.001  0.990   -32.482 1.00 21.26 ?  107 LEU A O   1 
ATOM   810  C CB  . LEU A 1 133 ? -4.158  -1.634  -34.556 1.00 24.80 ?  107 LEU A CB  1 
ATOM   811  C CG  . LEU A 1 133 ? -2.807  -1.894  -33.875 1.00 25.40 ?  107 LEU A CG  1 
ATOM   812  C CD1 . LEU A 1 133 ? -2.955  -2.389  -32.435 1.00 25.35 ?  107 LEU A CD1 1 
ATOM   813  C CD2 . LEU A 1 133 ? -1.988  -2.859  -34.715 1.00 26.73 ?  107 LEU A CD2 1 
ATOM   814  N N   . ASP A 1 134 ? -4.361  1.480   -34.688 1.00 21.56 ?  108 ASP A N   1 
ATOM   815  C CA  . ASP A 1 134 ? -3.832  2.864   -34.677 1.00 23.25 ?  108 ASP A CA  1 
ATOM   816  C C   . ASP A 1 134 ? -4.550  3.666   -33.598 1.00 20.24 ?  108 ASP A C   1 
ATOM   817  O O   . ASP A 1 134 ? -3.913  4.414   -32.876 1.00 20.34 ?  108 ASP A O   1 
ATOM   818  C CB  . ASP A 1 134 ? -4.072  3.579   -36.003 1.00 25.47 ?  108 ASP A CB  1 
ATOM   819  C CG  . ASP A 1 134 ? -3.236  3.121   -37.183 1.00 35.93 ?  108 ASP A CG  1 
ATOM   820  O OD1 . ASP A 1 134 ? -2.085  2.672   -36.969 1.00 36.00 ?  108 ASP A OD1 1 
ATOM   821  O OD2 . ASP A 1 134 ? -3.749  3.261   -38.331 1.00 38.83 ?  108 ASP A OD2 1 
ATOM   822  N N   . LEU A 1 135 ? -5.895  3.658   -33.568 1.00 19.83 ?  109 LEU A N   1 
ATOM   823  C CA  . LEU A 1 135 ? -6.567  4.457   -32.521 1.00 17.66 ?  109 LEU A CA  1 
ATOM   824  C C   . LEU A 1 135 ? -6.199  3.901   -31.134 1.00 18.30 ?  109 LEU A C   1 
ATOM   825  O O   . LEU A 1 135 ? -6.041  4.712   -30.189 1.00 18.41 ?  109 LEU A O   1 
ATOM   826  C CB  . LEU A 1 135 ? -8.082  4.360   -32.710 1.00 19.48 ?  109 LEU A CB  1 
ATOM   827  C CG  . LEU A 1 135 ? -8.622  4.922   -34.016 1.00 20.56 ?  109 LEU A CG  1 
ATOM   828  C CD1 . LEU A 1 135 ? -10.067 4.505   -34.139 1.00 21.73 ?  109 LEU A CD1 1 
ATOM   829  C CD2 . LEU A 1 135 ? -8.516  6.430   -34.064 1.00 21.16 ?  109 LEU A CD2 1 
ATOM   830  N N   . ALA A 1 136 ? -6.210  2.581   -30.976 1.00 17.02 ?  110 ALA A N   1 
ATOM   831  C CA  . ALA A 1 136 ? -6.043  1.922   -29.661 1.00 17.04 ?  110 ALA A CA  1 
ATOM   832  C C   . ALA A 1 136 ? -4.673  2.301   -29.077 1.00 17.84 ?  110 ALA A C   1 
ATOM   833  O O   . ALA A 1 136 ? -4.564  2.509   -27.860 1.00 18.32 ?  110 ALA A O   1 
ATOM   834  C CB  . ALA A 1 136 ? -6.171  0.442   -29.807 1.00 17.52 ?  110 ALA A CB  1 
ATOM   835  N N   . THR A 1 137 ? -3.685  2.436   -29.949 1.00 18.40 ?  111 THR A N   1 
ATOM   836  C CA  . THR A 1 137 ? -2.254  2.595   -29.563 1.00 18.04 ?  111 THR A CA  1 
ATOM   837  C C   . THR A 1 137 ? -1.737  4.002   -29.862 1.00 16.75 ?  111 THR A C   1 
ATOM   838  O O   . THR A 1 137 ? -0.492  4.195   -29.835 1.00 17.23 ?  111 THR A O   1 
ATOM   839  C CB  . THR A 1 137 ? -1.401  1.487   -30.186 1.00 17.62 ?  111 THR A CB  1 
ATOM   840  O OG1 . THR A 1 137 ? -1.373  1.645   -31.598 1.00 18.77 ?  111 THR A OG1 1 
ATOM   841  C CG2 . THR A 1 137 ? -1.885  0.129   -29.758 1.00 19.67 ?  111 THR A CG2 1 
ATOM   842  N N   . TYR A 1 138 ? -2.621  4.954   -30.101 1.00 17.81 ?  112 TYR A N   1 
ATOM   843  C CA  . TYR A 1 138 ? -2.316  6.402   -30.205 1.00 19.19 ?  112 TYR A CA  1 
ATOM   844  C C   . TYR A 1 138 ? -1.419  6.725   -31.408 1.00 20.02 ?  112 TYR A C   1 
ATOM   845  O O   . TYR A 1 138 ? -0.657  7.743   -31.336 1.00 20.78 ?  112 TYR A O   1 
ATOM   846  C CB  . TYR A 1 138 ? -1.672  6.910   -28.909 1.00 20.04 ?  112 TYR A CB  1 
ATOM   847  C CG  . TYR A 1 138 ? -2.181  6.321   -27.619 1.00 18.66 ?  112 TYR A CG  1 
ATOM   848  C CD1 . TYR A 1 138 ? -3.459  6.574   -27.157 1.00 18.82 ?  112 TYR A CD1 1 
ATOM   849  C CD2 . TYR A 1 138 ? -1.396  5.491   -26.862 1.00 18.77 ?  112 TYR A CD2 1 
ATOM   850  C CE1 . TYR A 1 138 ? -3.921  6.053   -25.962 1.00 17.41 ?  112 TYR A CE1 1 
ATOM   851  C CE2 . TYR A 1 138 ? -1.835  4.959   -25.662 1.00 18.79 ?  112 TYR A CE2 1 
ATOM   852  C CZ  . TYR A 1 138 ? -3.120  5.222   -25.215 1.00 18.21 ?  112 TYR A CZ  1 
ATOM   853  O OH  . TYR A 1 138 ? -3.531  4.703   -24.011 1.00 18.30 ?  112 TYR A OH  1 
ATOM   854  N N   . THR A 1 139 ? -1.518  5.952   -32.499 1.00 20.74 ?  113 THR A N   1 
ATOM   855  C CA  . THR A 1 139 ? -0.664  6.142   -33.698 1.00 23.56 ?  113 THR A CA  1 
ATOM   856  C C   . THR A 1 139 ? -1.494  6.547   -34.912 1.00 23.29 ?  113 THR A C   1 
ATOM   857  O O   . THR A 1 139 ? -0.989  6.432   -36.030 1.00 26.02 ?  113 THR A O   1 
ATOM   858  C CB  . THR A 1 139 ? 0.212   4.911   -33.965 1.00 25.53 ?  113 THR A CB  1 
ATOM   859  O OG1 . THR A 1 139 ? -0.613  3.748   -34.082 1.00 26.55 ?  113 THR A OG1 1 
ATOM   860  C CG2 . THR A 1 139 ? 1.213   4.681   -32.861 1.00 24.38 ?  113 THR A CG2 1 
ATOM   861  N N   . ALA A 1 140 ? -2.699  7.084   -34.716 1.00 23.53 ?  114 ALA A N   1 
ATOM   862  C CA  . ALA A 1 140 ? -3.590  7.449   -35.828 1.00 23.38 ?  114 ALA A CA  1 
ATOM   863  C C   . ALA A 1 140 ? -3.045  8.649   -36.618 1.00 24.78 ?  114 ALA A C   1 
ATOM   864  O O   . ALA A 1 140 ? -3.445  8.796   -37.788 1.00 26.21 ?  114 ALA A O   1 
ATOM   865  C CB  . ALA A 1 140 ? -4.989  7.698   -35.320 1.00 22.85 ?  114 ALA A CB  1 
ATOM   866  N N   . GLY A 1 141 ? -2.115  9.431   -36.063 1.00 24.79 ?  115 GLY A N   1 
ATOM   867  C CA  . GLY A 1 141 ? -1.455  10.516  -36.812 1.00 23.62 ?  115 GLY A CA  1 
ATOM   868  C C   . GLY A 1 141 ? -1.658  11.887  -36.197 1.00 24.43 ?  115 GLY A C   1 
ATOM   869  O O   . GLY A 1 141 ? -1.792  12.828  -36.967 1.00 22.77 ?  115 GLY A O   1 
ATOM   870  N N   . GLY A 1 142 ? -1.639  11.987  -34.861 1.00 22.77 ?  116 GLY A N   1 
ATOM   871  C CA  . GLY A 1 142 ? -1.606  13.257  -34.119 1.00 23.62 ?  116 GLY A CA  1 
ATOM   872  C C   . GLY A 1 142 ? -2.937  13.710  -33.528 1.00 23.15 ?  116 GLY A C   1 
ATOM   873  O O   . GLY A 1 142 ? -3.048  14.902  -33.214 1.00 26.05 ?  116 GLY A O   1 
ATOM   874  N N   . LEU A 1 143 ? -3.923  12.829  -33.352 1.00 22.07 ?  117 LEU A N   1 
ATOM   875  C CA  . LEU A 1 143 ? -5.095  13.121  -32.494 1.00 21.82 ?  117 LEU A CA  1 
ATOM   876  C C   . LEU A 1 143 ? -4.521  13.580  -31.164 1.00 19.92 ?  117 LEU A C   1 
ATOM   877  O O   . LEU A 1 143 ? -3.568  12.980  -30.665 1.00 20.04 ?  117 LEU A O   1 
ATOM   878  C CB  . LEU A 1 143 ? -5.973  11.886  -32.292 1.00 22.65 ?  117 LEU A CB  1 
ATOM   879  C CG  . LEU A 1 143 ? -6.991  11.586  -33.397 1.00 23.36 ?  117 LEU A CG  1 
ATOM   880  C CD1 . LEU A 1 143 ? -7.552  10.190  -33.192 1.00 22.00 ?  117 LEU A CD1 1 
ATOM   881  C CD2 . LEU A 1 143 ? -8.119  12.619  -33.426 1.00 22.06 ?  117 LEU A CD2 1 
ATOM   882  N N   . PRO A 1 144 ? -5.024  14.704  -30.634 1.00 20.69 ?  118 PRO A N   1 
ATOM   883  C CA  . PRO A 1 144 ? -4.417  15.409  -29.519 1.00 21.00 ?  118 PRO A CA  1 
ATOM   884  C C   . PRO A 1 144 ? -4.721  14.739  -28.175 1.00 19.91 ?  118 PRO A C   1 
ATOM   885  O O   . PRO A 1 144 ? -5.543  13.816  -28.118 1.00 21.18 ?  118 PRO A O   1 
ATOM   886  C CB  . PRO A 1 144 ? -5.057  16.806  -29.614 1.00 21.85 ?  118 PRO A CB  1 
ATOM   887  C CG  . PRO A 1 144 ? -6.411  16.525  -30.128 1.00 20.99 ?  118 PRO A CG  1 
ATOM   888  C CD  . PRO A 1 144 ? -6.202  15.418  -31.142 1.00 22.44 ?  118 PRO A CD  1 
ATOM   889  N N   . LEU A 1 145 ? -4.037  15.197  -27.134 1.00 20.06 ?  119 LEU A N   1 
ATOM   890  C CA  . LEU A 1 145 ? -4.219  14.640  -25.770 1.00 20.89 ?  119 LEU A CA  1 
ATOM   891  C C   . LEU A 1 145 ? -5.707  14.651  -25.394 1.00 22.93 ?  119 LEU A C   1 
ATOM   892  O O   . LEU A 1 145 ? -6.240  13.651  -24.882 1.00 22.81 ?  119 LEU A O   1 
ATOM   893  C CB  . LEU A 1 145 ? -3.409  15.475  -24.789 1.00 20.56 ?  119 LEU A CB  1 
ATOM   894  C CG  . LEU A 1 145 ? -3.495  14.957  -23.356 1.00 23.01 ?  119 LEU A CG  1 
ATOM   895  C CD1 . LEU A 1 145 ? -2.896  13.554  -23.242 1.00 23.47 ?  119 LEU A CD1 1 
ATOM   896  C CD2 . LEU A 1 145 ? -2.837  15.927  -22.403 1.00 24.66 ?  119 LEU A CD2 1 
ATOM   897  N N   . GLN A 1 146 ? -6.327  15.817  -25.552 1.00 24.32 ?  120 GLN A N   1 
ATOM   898  C CA  . GLN A 1 146 ? -7.735  16.049  -25.162 1.00 22.94 ?  120 GLN A CA  1 
ATOM   899  C C   . GLN A 1 146 ? -8.498  16.534  -26.382 1.00 23.96 ?  120 GLN A C   1 
ATOM   900  O O   . GLN A 1 146 ? -7.909  17.166  -27.296 1.00 22.04 ?  120 GLN A O   1 
ATOM   901  C CB  . GLN A 1 146 ? -7.765  17.026  -23.980 1.00 26.90 ?  120 GLN A CB  1 
ATOM   902  C CG  . GLN A 1 146 ? -7.303  16.316  -22.706 1.00 33.82 ?  120 GLN A CG  1 
ATOM   903  C CD  . GLN A 1 146 ? -6.907  17.199  -21.547 1.00 42.99 ?  120 GLN A CD  1 
ATOM   904  O OE1 . GLN A 1 146 ? -7.098  18.410  -21.568 1.00 48.55 ?  120 GLN A OE1 1 
ATOM   905  N NE2 . GLN A 1 146 ? -6.354  16.579  -20.510 1.00 44.02 ?  120 GLN A NE2 1 
ATOM   906  N N   . PHE A 1 147 ? -9.792  16.283  -26.381 1.00 23.25 ?  121 PHE A N   1 
ATOM   907  C CA  . PHE A 1 147 ? -10.723 17.059  -27.209 1.00 24.84 ?  121 PHE A CA  1 
ATOM   908  C C   . PHE A 1 147 ? -10.515 18.529  -26.878 1.00 23.93 ?  121 PHE A C   1 
ATOM   909  O O   . PHE A 1 147 ? -10.346 18.894  -25.719 1.00 22.02 ?  121 PHE A O   1 
ATOM   910  C CB  . PHE A 1 147 ? -12.172 16.674  -26.907 1.00 24.33 ?  121 PHE A CB  1 
ATOM   911  C CG  . PHE A 1 147 ? -12.623 15.360  -27.495 1.00 22.92 ?  121 PHE A CG  1 
ATOM   912  C CD1 . PHE A 1 147 ? -12.968 15.268  -28.835 1.00 22.28 ?  121 PHE A CD1 1 
ATOM   913  C CD2 . PHE A 1 147 ? -12.636 14.201  -26.724 1.00 23.07 ?  121 PHE A CD2 1 
ATOM   914  C CE1 . PHE A 1 147 ? -13.366 14.052  -29.383 1.00 21.29 ?  121 PHE A CE1 1 
ATOM   915  C CE2 . PHE A 1 147 ? -13.020 12.989  -27.283 1.00 21.29 ?  121 PHE A CE2 1 
ATOM   916  C CZ  . PHE A 1 147 ? -13.415 12.922  -28.592 1.00 22.02 ?  121 PHE A CZ  1 
ATOM   917  N N   . PRO A 1 148 ? -10.562 19.426  -27.870 1.00 26.97 ?  122 PRO A N   1 
ATOM   918  C CA  . PRO A 1 148 ? -10.556 20.858  -27.577 1.00 29.83 ?  122 PRO A CA  1 
ATOM   919  C C   . PRO A 1 148 ? -11.769 21.255  -26.722 1.00 30.11 ?  122 PRO A C   1 
ATOM   920  O O   . PRO A 1 148 ? -12.758 20.542  -26.745 1.00 25.76 ?  122 PRO A O   1 
ATOM   921  C CB  . PRO A 1 148 ? -10.609 21.545  -28.956 1.00 29.55 ?  122 PRO A CB  1 
ATOM   922  C CG  . PRO A 1 148 ? -11.023 20.452  -29.929 1.00 29.93 ?  122 PRO A CG  1 
ATOM   923  C CD  . PRO A 1 148 ? -10.630 19.129  -29.306 1.00 28.70 ?  122 PRO A CD  1 
ATOM   924  N N   . ASP A 1 149 ? -11.623 22.335  -25.950 1.00 31.99 ?  123 ASP A N   1 
ATOM   925  C CA  . ASP A 1 149 ? -12.655 22.856  -25.022 1.00 37.66 ?  123 ASP A CA  1 
ATOM   926  C C   . ASP A 1 149 ? -13.967 23.071  -25.766 1.00 35.92 ?  123 ASP A C   1 
ATOM   927  O O   . ASP A 1 149 ? -15.004 22.941  -25.133 1.00 39.69 ?  123 ASP A O   1 
ATOM   928  C CB  . ASP A 1 149 ? -12.286 24.212  -24.425 1.00 43.96 ?  123 ASP A CB  1 
ATOM   929  C CG  . ASP A 1 149 ? -11.460 24.072  -23.177 1.00 53.52 ?  123 ASP A CG  1 
ATOM   930  O OD1 . ASP A 1 149 ? -10.765 23.048  -23.081 1.00 57.29 ?  123 ASP A OD1 1 
ATOM   931  O OD2 . ASP A 1 149 ? -11.531 24.984  -22.315 1.00 63.19 ?  123 ASP A OD2 1 
ATOM   932  N N   . SER A 1 150 ? -13.915 23.395  -27.058 1.00 34.59 ?  124 SER A N   1 
ATOM   933  C CA  . SER A 1 150 ? -15.136 23.668  -27.853 1.00 37.87 ?  124 SER A CA  1 
ATOM   934  C C   . SER A 1 150 ? -15.977 22.388  -28.020 1.00 38.75 ?  124 SER A C   1 
ATOM   935  O O   . SER A 1 150 ? -17.146 22.514  -28.362 1.00 43.66 ?  124 SER A O   1 
ATOM   936  C CB  . SER A 1 150 ? -14.794 24.295  -29.174 1.00 38.43 ?  124 SER A CB  1 
ATOM   937  O OG  . SER A 1 150 ? -13.950 23.450  -29.932 1.00 45.52 ?  124 SER A OG  1 
ATOM   938  N N   . VAL A 1 151 ? -15.432 21.190  -27.792 1.00 32.62 ?  125 VAL A N   1 
ATOM   939  C CA  . VAL A 1 151 ? -16.215 19.930  -27.961 1.00 28.43 ?  125 VAL A CA  1 
ATOM   940  C C   . VAL A 1 151 ? -16.802 19.499  -26.617 1.00 31.04 ?  125 VAL A C   1 
ATOM   941  O O   . VAL A 1 151 ? -16.044 19.121  -25.711 1.00 30.66 ?  125 VAL A O   1 
ATOM   942  C CB  . VAL A 1 151 ? -15.397 18.804  -28.617 1.00 28.72 ?  125 VAL A CB  1 
ATOM   943  C CG1 . VAL A 1 151 ? -16.239 17.550  -28.803 1.00 27.02 ?  125 VAL A CG1 1 
ATOM   944  C CG2 . VAL A 1 151 ? -14.854 19.264  -29.964 1.00 30.10 ?  125 VAL A CG2 1 
ATOM   945  N N   . GLN A 1 152 ? -18.131 19.534  -26.521 1.00 28.36 ?  126 GLN A N   1 
ATOM   946  C CA  . GLN A 1 152 ? -18.876 19.187  -25.298 1.00 31.38 ?  126 GLN A CA  1 
ATOM   947  C C   . GLN A 1 152 ? -19.257 17.717  -25.425 1.00 30.40 ?  126 GLN A C   1 
ATOM   948  O O   . GLN A 1 152 ? -19.061 17.128  -26.517 1.00 28.04 ?  126 GLN A O   1 
ATOM   949  C CB  . GLN A 1 152 ? -20.067 20.134  -25.124 1.00 34.38 ?  126 GLN A CB  1 
ATOM   950  C CG  . GLN A 1 152 ? -19.625 21.594  -25.083 1.00 38.04 ?  126 GLN A CG  1 
ATOM   951  C CD  . GLN A 1 152 ? -20.796 22.538  -24.972 1.00 43.49 ?  126 GLN A CD  1 
ATOM   952  O OE1 . GLN A 1 152 ? -21.830 22.334  -25.583 1.00 41.75 ?  126 GLN A OE1 1 
ATOM   953  N NE2 . GLN A 1 152 ? -20.638 23.576  -24.171 1.00 50.07 ?  126 GLN A NE2 1 
ATOM   954  N N   . LYS A 1 153 ? -19.740 17.136  -24.332 1.00 29.74 ?  127 LYS A N   1 
ATOM   955  C CA  . LYS A 1 153 ? -20.289 15.766  -24.331 1.00 28.11 ?  127 LYS A CA  1 
ATOM   956  C C   . LYS A 1 153 ? -21.612 15.820  -25.082 1.00 29.32 ?  127 LYS A C   1 
ATOM   957  O O   . LYS A 1 153 ? -22.645 15.931  -24.446 1.00 29.55 ?  127 LYS A O   1 
ATOM   958  C CB  . LYS A 1 153 ? -20.437 15.221  -22.904 1.00 29.01 ?  127 LYS A CB  1 
ATOM   959  C CG  . LYS A 1 153 ? -20.815 13.750  -22.877 1.00 29.29 ?  127 LYS A CG  1 
ATOM   960  C CD  . LYS A 1 153 ? -20.961 13.132  -21.500 1.00 31.48 ?  127 LYS A CD  1 
ATOM   961  C CE  . LYS A 1 153 ? -20.954 11.625  -21.602 1.00 31.16 ?  127 LYS A CE  1 
ATOM   962  N NZ  . LYS A 1 153 ? -20.944 10.972  -20.279 1.00 39.01 ?  127 LYS A NZ  1 
ATOM   963  N N   . ASP A 1 154 ? -21.538 15.697  -26.403 1.00 29.39 ?  128 ASP A N   1 
ATOM   964  C CA  . ASP A 1 154 ? -22.678 15.792  -27.331 1.00 31.00 ?  128 ASP A CA  1 
ATOM   965  C C   . ASP A 1 154 ? -22.292 14.985  -28.567 1.00 32.72 ?  128 ASP A C   1 
ATOM   966  O O   . ASP A 1 154 ? -21.202 15.255  -29.148 1.00 30.97 ?  128 ASP A O   1 
ATOM   967  C CB  . ASP A 1 154 ? -22.988 17.252  -27.643 1.00 33.43 ?  128 ASP A CB  1 
ATOM   968  C CG  . ASP A 1 154 ? -24.035 17.344  -28.727 1.00 39.61 ?  128 ASP A CG  1 
ATOM   969  O OD1 . ASP A 1 154 ? -25.224 17.077  -28.405 1.00 39.13 ?  128 ASP A OD1 1 
ATOM   970  O OD2 . ASP A 1 154 ? -23.644 17.578  -29.902 1.00 38.68 ?  128 ASP A OD2 1 
ATOM   971  N N   . GLN A 1 155 ? -23.124 14.015  -28.919 1.00 29.58 ?  129 GLN A N   1 
ATOM   972  C CA  . GLN A 1 155 ? -22.918 13.053  -30.033 1.00 34.59 ?  129 GLN A CA  1 
ATOM   973  C C   . GLN A 1 155 ? -22.559 13.807  -31.327 1.00 34.70 ?  129 GLN A C   1 
ATOM   974  O O   . GLN A 1 155 ? -21.565 13.426  -31.992 1.00 33.32 ?  129 GLN A O   1 
ATOM   975  C CB  . GLN A 1 155 ? -24.179 12.205  -30.175 1.00 40.79 ?  129 GLN A CB  1 
ATOM   976  C CG  . GLN A 1 155 ? -23.901 10.725  -30.376 1.00 54.88 ?  129 GLN A CG  1 
ATOM   977  C CD  . GLN A 1 155 ? -23.717 10.376  -31.826 1.00 62.78 ?  129 GLN A CD  1 
ATOM   978  O OE1 . GLN A 1 155 ? -24.067 11.146  -32.719 1.00 77.70 ?  129 GLN A OE1 1 
ATOM   979  N NE2 . GLN A 1 155 ? -23.178 9.192   -32.069 1.00 64.80 ?  129 GLN A NE2 1 
ATOM   980  N N   . ALA A 1 156 ? -23.307 14.863  -31.668 1.00 33.69 ?  130 ALA A N   1 
ATOM   981  C CA  . ALA A 1 156 ? -23.119 15.601  -32.939 1.00 30.32 ?  130 ALA A CA  1 
ATOM   982  C C   . ALA A 1 156 ? -21.771 16.330  -32.940 1.00 30.30 ?  130 ALA A C   1 
ATOM   983  O O   . ALA A 1 156 ? -21.097 16.310  -33.994 1.00 30.93 ?  130 ALA A O   1 
ATOM   984  C CB  . ALA A 1 156 ? -24.262 16.560  -33.183 1.00 32.20 ?  130 ALA A CB  1 
ATOM   985  N N   . GLN A 1 157 ? -21.402 16.998  -31.837 1.00 27.96 ?  131 GLN A N   1 
ATOM   986  C CA  . GLN A 1 157 ? -20.118 17.733  -31.743 1.00 27.00 ?  131 GLN A CA  1 
ATOM   987  C C   . GLN A 1 157 ? -18.969 16.739  -31.899 1.00 27.82 ?  131 GLN A C   1 
ATOM   988  O O   . GLN A 1 157 ? -17.971 17.101  -32.552 1.00 26.60 ?  131 GLN A O   1 
ATOM   989  C CB  . GLN A 1 157 ? -19.985 18.514  -30.441 1.00 28.46 ?  131 GLN A CB  1 
ATOM   990  C CG  . GLN A 1 157 ? -20.986 19.646  -30.337 1.00 28.43 ?  131 GLN A CG  1 
ATOM   991  C CD  . GLN A 1 157 ? -20.759 20.528  -29.138 1.00 32.59 ?  131 GLN A CD  1 
ATOM   992  O OE1 . GLN A 1 157 ? -19.632 20.876  -28.775 1.00 32.39 ?  131 GLN A OE1 1 
ATOM   993  N NE2 . GLN A 1 157 ? -21.859 20.964  -28.549 1.00 36.76 ?  131 GLN A NE2 1 
ATOM   994  N N   . ILE A 1 158 ? -19.098 15.566  -31.297 1.00 24.19 ?  132 ILE A N   1 
ATOM   995  C CA  . ILE A 1 158 ? -18.024 14.538  -31.340 1.00 23.22 ?  132 ILE A CA  1 
ATOM   996  C C   . ILE A 1 158 ? -17.911 14.008  -32.781 1.00 22.73 ?  132 ILE A C   1 
ATOM   997  O O   . ILE A 1 158 ? -16.801 13.897  -33.278 1.00 21.97 ?  132 ILE A O   1 
ATOM   998  C CB  . ILE A 1 158 ? -18.279 13.435  -30.296 1.00 22.85 ?  132 ILE A CB  1 
ATOM   999  C CG1 . ILE A 1 158 ? -18.181 13.985  -28.870 1.00 21.54 ?  132 ILE A CG1 1 
ATOM   1000 C CG2 . ILE A 1 158 ? -17.387 12.238  -30.559 1.00 24.34 ?  132 ILE A CG2 1 
ATOM   1001 C CD1 . ILE A 1 158 ? -18.796 13.088  -27.805 1.00 24.20 ?  132 ILE A CD1 1 
ATOM   1002 N N   . ARG A 1 159 ? -19.031 13.641  -33.397 1.00 24.60 ?  133 ARG A N   1 
ATOM   1003 C CA  . ARG A 1 159 ? -19.109 13.231  -34.832 1.00 26.67 ?  133 ARG A CA  1 
ATOM   1004 C C   . ARG A 1 159 ? -18.451 14.315  -35.713 1.00 26.25 ?  133 ARG A C   1 
ATOM   1005 O O   . ARG A 1 159 ? -17.630 13.942  -36.571 1.00 25.99 ?  133 ARG A O   1 
ATOM   1006 C CB  . ARG A 1 159 ? -20.589 12.994  -35.189 1.00 29.22 ?  133 ARG A CB  1 
ATOM   1007 C CG  . ARG A 1 159 ? -20.890 12.696  -36.654 1.00 32.91 ?  133 ARG A CG  1 
ATOM   1008 C CD  . ARG A 1 159 ? -22.341 13.060  -36.994 1.00 33.95 ?  133 ARG A CD  1 
ATOM   1009 N NE  . ARG A 1 159 ? -22.538 14.508  -37.072 1.00 35.28 ?  133 ARG A NE  1 
ATOM   1010 C CZ  . ARG A 1 159 ? -23.673 15.184  -36.812 1.00 35.67 ?  133 ARG A CZ  1 
ATOM   1011 N NH1 . ARG A 1 159 ? -24.777 14.578  -36.416 1.00 34.09 ?  133 ARG A NH1 1 
ATOM   1012 N NH2 . ARG A 1 159 ? -23.691 16.497  -36.940 1.00 37.41 ?  133 ARG A NH2 1 
ATOM   1013 N N   . ASP A 1 160 ? -18.780 15.610  -35.511 1.00 24.30 ?  134 ASP A N   1 
ATOM   1014 C CA  . ASP A 1 160 ? -18.297 16.717  -36.390 1.00 24.88 ?  134 ASP A CA  1 
ATOM   1015 C C   . ASP A 1 160 ? -16.794 16.915  -36.176 1.00 25.47 ?  134 ASP A C   1 
ATOM   1016 O O   . ASP A 1 160 ? -16.079 17.119  -37.173 1.00 26.23 ?  134 ASP A O   1 
ATOM   1017 C CB  . ASP A 1 160 ? -19.061 18.017  -36.160 1.00 24.20 ?  134 ASP A CB  1 
ATOM   1018 C CG  . ASP A 1 160 ? -20.497 17.895  -36.637 1.00 29.93 ?  134 ASP A CG  1 
ATOM   1019 O OD1 . ASP A 1 160 ? -20.813 16.885  -37.355 1.00 32.34 ?  134 ASP A OD1 1 
ATOM   1020 O OD2 . ASP A 1 160 ? -21.295 18.781  -36.273 1.00 33.96 ?  134 ASP A OD2 1 
ATOM   1021 N N   . TYR A 1 161 ? -16.333 16.744  -34.932 1.00 24.42 ?  135 TYR A N   1 
ATOM   1022 C CA  . TYR A 1 161 ? -14.889 16.813  -34.598 1.00 23.87 ?  135 TYR A CA  1 
ATOM   1023 C C   . TYR A 1 161 ? -14.139 15.777  -35.442 1.00 22.74 ?  135 TYR A C   1 
ATOM   1024 O O   . TYR A 1 161 ? -13.170 16.111  -36.109 1.00 21.78 ?  135 TYR A O   1 
ATOM   1025 C CB  . TYR A 1 161 ? -14.616 16.625  -33.089 1.00 22.42 ?  135 TYR A CB  1 
ATOM   1026 C CG  . TYR A 1 161 ? -13.141 16.519  -32.808 1.00 22.05 ?  135 TYR A CG  1 
ATOM   1027 C CD1 . TYR A 1 161 ? -12.344 17.652  -32.796 1.00 22.67 ?  135 TYR A CD1 1 
ATOM   1028 C CD2 . TYR A 1 161 ? -12.517 15.292  -32.686 1.00 24.07 ?  135 TYR A CD2 1 
ATOM   1029 C CE1 . TYR A 1 161 ? -10.973 17.563  -32.626 1.00 22.14 ?  135 TYR A CE1 1 
ATOM   1030 C CE2 . TYR A 1 161 ? -11.152 15.188  -32.509 1.00 24.45 ?  135 TYR A CE2 1 
ATOM   1031 C CZ  . TYR A 1 161 ? -10.381 16.328  -32.432 1.00 24.15 ?  135 TYR A CZ  1 
ATOM   1032 O OH  . TYR A 1 161 ? -9.021  16.193  -32.276 1.00 26.71 ?  135 TYR A OH  1 
ATOM   1033 N N   . TYR A 1 162 ? -14.509 14.509  -35.349 1.00 22.93 ?  136 TYR A N   1 
ATOM   1034 C CA  . TYR A 1 162 ? -13.796 13.427  -36.066 1.00 21.99 ?  136 TYR A CA  1 
ATOM   1035 C C   . TYR A 1 162 ? -13.945 13.620  -37.583 1.00 20.99 ?  136 TYR A C   1 
ATOM   1036 O O   . TYR A 1 162 ? -13.010 13.383  -38.300 1.00 22.10 ?  136 TYR A O   1 
ATOM   1037 C CB  . TYR A 1 162 ? -14.308 12.060  -35.629 1.00 22.04 ?  136 TYR A CB  1 
ATOM   1038 C CG  . TYR A 1 162 ? -13.833 11.639  -34.264 1.00 24.93 ?  136 TYR A CG  1 
ATOM   1039 C CD1 . TYR A 1 162 ? -12.484 11.524  -33.973 1.00 22.67 ?  136 TYR A CD1 1 
ATOM   1040 C CD2 . TYR A 1 162 ? -14.738 11.335  -33.273 1.00 24.27 ?  136 TYR A CD2 1 
ATOM   1041 C CE1 . TYR A 1 162 ? -12.059 11.186  -32.703 1.00 23.47 ?  136 TYR A CE1 1 
ATOM   1042 C CE2 . TYR A 1 162 ? -14.333 10.948  -32.015 1.00 25.58 ?  136 TYR A CE2 1 
ATOM   1043 C CZ  . TYR A 1 162 ? -12.983 10.860  -31.735 1.00 21.76 ?  136 TYR A CZ  1 
ATOM   1044 O OH  . TYR A 1 162 ? -12.644 10.460  -30.493 1.00 21.88 ?  136 TYR A OH  1 
ATOM   1045 N N   . ARG A 1 163 ? -15.113 14.029  -38.061 1.00 22.59 ?  137 ARG A N   1 
ATOM   1046 C CA  . ARG A 1 163 ? -15.327 14.191  -39.527 1.00 26.49 ?  137 ARG A CA  1 
ATOM   1047 C C   . ARG A 1 163 ? -14.320 15.211  -40.077 1.00 26.77 ?  137 ARG A C   1 
ATOM   1048 O O   . ARG A 1 163 ? -13.866 15.002  -41.212 1.00 30.79 ?  137 ARG A O   1 
ATOM   1049 C CB  . ARG A 1 163 ? -16.777 14.573  -39.863 1.00 27.53 ?  137 ARG A CB  1 
ATOM   1050 C CG  . ARG A 1 163 ? -17.771 13.434  -39.694 1.00 31.63 ?  137 ARG A CG  1 
ATOM   1051 C CD  . ARG A 1 163 ? -19.186 13.790  -40.164 1.00 35.47 ?  137 ARG A CD  1 
ATOM   1052 N NE  . ARG A 1 163 ? -19.188 14.242  -41.553 1.00 44.63 ?  137 ARG A NE  1 
ATOM   1053 C CZ  . ARG A 1 163 ? -18.852 13.501  -42.624 1.00 49.20 ?  137 ARG A CZ  1 
ATOM   1054 N NH1 . ARG A 1 163 ? -18.497 12.226  -42.519 1.00 51.10 ?  137 ARG A NH1 1 
ATOM   1055 N NH2 . ARG A 1 163 ? -18.871 14.062  -43.819 1.00 56.23 ?  137 ARG A NH2 1 
ATOM   1056 N N   . GLN A 1 164 ? -13.967 16.255  -39.325 1.00 25.05 ?  138 GLN A N   1 
ATOM   1057 C CA  . GLN A 1 164 ? -13.182 17.393  -39.869 1.00 27.32 ?  138 GLN A CA  1 
ATOM   1058 C C   . GLN A 1 164 ? -11.688 17.177  -39.589 1.00 27.82 ?  138 GLN A C   1 
ATOM   1059 O O   . GLN A 1 164 ? -10.846 17.959  -40.120 1.00 27.14 ?  138 GLN A O   1 
ATOM   1060 C CB  . GLN A 1 164 ? -13.720 18.726  -39.345 1.00 28.20 ?  138 GLN A CB  1 
ATOM   1061 C CG  . GLN A 1 164 ? -13.519 18.973  -37.864 1.00 31.89 ?  138 GLN A CG  1 
ATOM   1062 C CD  . GLN A 1 164 ? -12.062 19.111  -37.476 1.00 34.25 ?  138 GLN A CD  1 
ATOM   1063 O OE1 . GLN A 1 164 ? -11.289 19.773  -38.175 1.00 42.37 ?  138 GLN A OE1 1 
ATOM   1064 N NE2 . GLN A 1 164 ? -11.683 18.483  -36.368 1.00 27.11 ?  138 GLN A NE2 1 
ATOM   1065 N N   . TRP A 1 165 ? -11.353 16.175  -38.772 1.00 24.54 ?  139 TRP A N   1 
ATOM   1066 C CA  . TRP A 1 165 ? -9.954  15.932  -38.334 1.00 22.77 ?  139 TRP A CA  1 
ATOM   1067 C C   . TRP A 1 165 ? -9.066  15.470  -39.497 1.00 25.42 ?  139 TRP A C   1 
ATOM   1068 O O   . TRP A 1 165 ? -9.477  14.601  -40.267 1.00 26.21 ?  139 TRP A O   1 
ATOM   1069 C CB  . TRP A 1 165 ? -9.899  14.959  -37.149 1.00 23.87 ?  139 TRP A CB  1 
ATOM   1070 C CG  . TRP A 1 165 ? -8.500  14.737  -36.694 1.00 22.65 ?  139 TRP A CG  1 
ATOM   1071 C CD1 . TRP A 1 165 ? -7.764  15.522  -35.869 1.00 25.51 ?  139 TRP A CD1 1 
ATOM   1072 C CD2 . TRP A 1 165 ? -7.669  13.634  -37.040 1.00 23.10 ?  139 TRP A CD2 1 
ATOM   1073 N NE1 . TRP A 1 165 ? -6.514  14.994  -35.692 1.00 25.47 ?  139 TRP A NE1 1 
ATOM   1074 C CE2 . TRP A 1 165 ? -6.420  13.849  -36.414 1.00 25.75 ?  139 TRP A CE2 1 
ATOM   1075 C CE3 . TRP A 1 165 ? -7.836  12.522  -37.858 1.00 25.16 ?  139 TRP A CE3 1 
ATOM   1076 C CZ2 . TRP A 1 165 ? -5.384  12.941  -36.511 1.00 26.55 ?  139 TRP A CZ2 1 
ATOM   1077 C CZ3 . TRP A 1 165 ? -6.806  11.619  -37.949 1.00 28.04 ?  139 TRP A CZ3 1 
ATOM   1078 C CH2 . TRP A 1 165 ? -5.593  11.844  -37.307 1.00 26.15 ?  139 TRP A CH2 1 
ATOM   1079 N N   . GLN A 1 166 ? -7.835  15.996  -39.561 1.00 27.26 ?  140 GLN A N   1 
ATOM   1080 C CA  . GLN A 1 166 ? -6.804  15.596  -40.553 1.00 30.15 ?  140 GLN A CA  1 
ATOM   1081 C C   . GLN A 1 166 ? -5.525  15.217  -39.821 1.00 26.89 ?  140 GLN A C   1 
ATOM   1082 O O   . GLN A 1 166 ? -5.071  15.946  -38.964 1.00 28.88 ?  140 GLN A O   1 
ATOM   1083 C CB  . GLN A 1 166 ? -6.566  16.726  -41.574 1.00 30.78 ?  140 GLN A CB  1 
ATOM   1084 C CG  . GLN A 1 166 ? -7.838  17.063  -42.341 1.00 37.93 ?  140 GLN A CG  1 
ATOM   1085 C CD  . GLN A 1 166 ? -7.722  18.208  -43.323 1.00 38.55 ?  140 GLN A CD  1 
ATOM   1086 O OE1 . GLN A 1 166 ? -6.642  18.713  -43.595 1.00 39.45 ?  140 GLN A OE1 1 
ATOM   1087 N NE2 . GLN A 1 166 ? -8.859  18.618  -43.860 1.00 41.18 ?  140 GLN A NE2 1 
ATOM   1088 N N   . PRO A 1 167 ? -4.918  14.053  -40.112 1.00 28.67 ?  141 PRO A N   1 
ATOM   1089 C CA  . PRO A 1 167 ? -3.623  13.694  -39.552 1.00 27.53 ?  141 PRO A CA  1 
ATOM   1090 C C   . PRO A 1 167 ? -2.510  14.717  -39.813 1.00 28.80 ?  141 PRO A C   1 
ATOM   1091 O O   . PRO A 1 167 ? -2.446  15.291  -40.862 1.00 26.84 ?  141 PRO A O   1 
ATOM   1092 C CB  . PRO A 1 167 ? -3.274  12.352  -40.201 1.00 28.16 ?  141 PRO A CB  1 
ATOM   1093 C CG  . PRO A 1 167 ? -4.201  12.216  -41.363 1.00 30.03 ?  141 PRO A CG  1 
ATOM   1094 C CD  . PRO A 1 167 ? -5.449  12.966  -40.953 1.00 30.86 ?  141 PRO A CD  1 
ATOM   1095 N N   . THR A 1 168 ? -1.637  14.868  -38.834 1.00 27.48 ?  142 THR A N   1 
ATOM   1096 C CA  . THR A 1 168 ? -0.407  15.686  -38.953 1.00 29.58 ?  142 THR A CA  1 
ATOM   1097 C C   . THR A 1 168 ? 0.709   14.856  -39.575 1.00 29.91 ?  142 THR A C   1 
ATOM   1098 O O   . THR A 1 168 ? 1.622   15.452  -40.139 1.00 27.70 ?  142 THR A O   1 
ATOM   1099 C CB  . THR A 1 168 ? 0.074   16.157  -37.582 1.00 32.39 ?  142 THR A CB  1 
ATOM   1100 O OG1 . THR A 1 168 ? -1.087  16.653  -36.957 1.00 29.84 ?  142 THR A OG1 1 
ATOM   1101 C CG2 . THR A 1 168 ? 1.142   17.228  -37.647 1.00 34.47 ?  142 THR A CG2 1 
ATOM   1102 N N   . TYR A 1 169 ? 0.690   13.542  -39.375 1.00 27.71 ?  143 TYR A N   1 
ATOM   1103 C CA  . TYR A 1 169 ? 1.664   12.609  -40.004 1.00 30.10 ?  143 TYR A CA  1 
ATOM   1104 C C   . TYR A 1 169 ? 0.995   11.280  -40.299 1.00 26.69 ?  143 TYR A C   1 
ATOM   1105 O O   . TYR A 1 169 ? -0.197  11.096  -39.990 1.00 25.38 ?  143 TYR A O   1 
ATOM   1106 C CB  . TYR A 1 169 ? 2.907   12.447  -39.134 1.00 28.77 ?  143 TYR A CB  1 
ATOM   1107 C CG  . TYR A 1 169 ? 2.630   12.641  -37.669 1.00 29.39 ?  143 TYR A CG  1 
ATOM   1108 C CD1 . TYR A 1 169 ? 1.987   11.665  -36.925 1.00 29.35 ?  143 TYR A CD1 1 
ATOM   1109 C CD2 . TYR A 1 169 ? 2.960   13.827  -37.046 1.00 28.40 ?  143 TYR A CD2 1 
ATOM   1110 C CE1 . TYR A 1 169 ? 1.713   11.862  -35.581 1.00 27.87 ?  143 TYR A CE1 1 
ATOM   1111 C CE2 . TYR A 1 169 ? 2.685   14.044  -35.711 1.00 28.79 ?  143 TYR A CE2 1 
ATOM   1112 C CZ  . TYR A 1 169 ? 2.067   13.052  -34.975 1.00 27.58 ?  143 TYR A CZ  1 
ATOM   1113 O OH  . TYR A 1 169 ? 1.814   13.280  -33.664 1.00 27.20 ?  143 TYR A OH  1 
ATOM   1114 N N   . ALA A 1 170 ? 1.769   10.395  -40.934 1.00 29.03 ?  144 ALA A N   1 
ATOM   1115 C CA  . ALA A 1 170 ? 1.279   9.105   -41.458 1.00 30.70 ?  144 ALA A CA  1 
ATOM   1116 C C   . ALA A 1 170 ? 0.744   8.324   -40.281 1.00 28.03 ?  144 ALA A C   1 
ATOM   1117 O O   . ALA A 1 170 ? 1.367   8.302   -39.221 1.00 25.16 ?  144 ALA A O   1 
ATOM   1118 C CB  . ALA A 1 170 ? 2.387   8.320   -42.114 1.00 29.62 ?  144 ALA A CB  1 
ATOM   1119 N N   . PRO A 1 171 ? -0.425  7.673   -40.438 1.00 34.45 ?  145 PRO A N   1 
ATOM   1120 C CA  . PRO A 1 171 ? -0.863  6.677   -39.475 1.00 32.57 ?  145 PRO A CA  1 
ATOM   1121 C C   . PRO A 1 171 ? 0.227   5.628   -39.289 1.00 31.12 ?  145 PRO A C   1 
ATOM   1122 O O   . PRO A 1 171 ? 0.884   5.237   -40.237 1.00 34.55 ?  145 PRO A O   1 
ATOM   1123 C CB  . PRO A 1 171 ? -2.128  6.115   -40.115 1.00 35.27 ?  145 PRO A CB  1 
ATOM   1124 C CG  . PRO A 1 171 ? -2.687  7.321   -40.847 1.00 38.63 ?  145 PRO A CG  1 
ATOM   1125 C CD  . PRO A 1 171 ? -1.459  7.991   -41.439 1.00 37.98 ?  145 PRO A CD  1 
ATOM   1126 N N   . GLY A 1 172 ? 0.411   5.208   -38.057 1.00 26.58 ?  146 GLY A N   1 
ATOM   1127 C CA  . GLY A 1 172 ? 1.247   4.057   -37.727 1.00 28.16 ?  146 GLY A CA  1 
ATOM   1128 C C   . GLY A 1 172 ? 2.696   4.440   -37.496 1.00 28.04 ?  146 GLY A C   1 
ATOM   1129 O O   . GLY A 1 172 ? 3.490   3.520   -37.394 1.00 34.53 ?  146 GLY A O   1 
ATOM   1130 N N   . SER A 1 173 ? 3.051   5.731   -37.448 1.00 27.26 ?  147 SER A N   1 
ATOM   1131 C CA  . SER A 1 173 ? 4.476   6.186   -37.393 1.00 29.01 ?  147 SER A CA  1 
ATOM   1132 C C   . SER A 1 173 ? 4.854   6.827   -36.045 1.00 28.92 ?  147 SER A C   1 
ATOM   1133 O O   . SER A 1 173 ? 6.010   6.706   -35.632 1.00 31.01 ?  147 SER A O   1 
ATOM   1134 C CB  . SER A 1 173 ? 4.779   7.134   -38.521 1.00 29.98 ?  147 SER A CB  1 
ATOM   1135 O OG  . SER A 1 173 ? 4.039   8.346   -38.417 1.00 33.51 ?  147 SER A OG  1 
ATOM   1136 N N   . GLN A 1 174 ? 3.960   7.584   -35.432 1.00 27.55 ?  148 GLN A N   1 
ATOM   1137 C CA  . GLN A 1 174 ? 4.263   8.382   -34.213 1.00 28.61 ?  148 GLN A CA  1 
ATOM   1138 C C   . GLN A 1 174 ? 3.197   8.146   -33.153 1.00 26.54 ?  148 GLN A C   1 
ATOM   1139 O O   . GLN A 1 174 ? 1.949   8.281   -33.481 1.00 23.89 ?  148 GLN A O   1 
ATOM   1140 C CB  . GLN A 1 174 ? 4.208   9.879   -34.492 1.00 32.30 ?  148 GLN A CB  1 
ATOM   1141 C CG  . GLN A 1 174 ? 5.155   10.337  -35.576 1.00 34.24 ?  148 GLN A CG  1 
ATOM   1142 C CD  . GLN A 1 174 ? 6.323   11.129  -35.056 1.00 36.60 ?  148 GLN A CD  1 
ATOM   1143 O OE1 . GLN A 1 174 ? 6.592   11.203  -33.853 1.00 34.44 ?  148 GLN A OE1 1 
ATOM   1144 N NE2 . GLN A 1 174 ? 7.017   11.755  -35.989 1.00 38.50 ?  148 GLN A NE2 1 
ATOM   1145 N N   . ARG A 1 175 ? 3.640   7.855   -31.932 1.00 24.16 ?  149 ARG A N   1 
ATOM   1146 C CA  . ARG A 1 175 ? 2.731   7.702   -30.785 1.00 21.90 ?  149 ARG A CA  1 
ATOM   1147 C C   . ARG A 1 175 ? 2.521   9.073   -30.161 1.00 20.17 ?  149 ARG A C   1 
ATOM   1148 O O   . ARG A 1 175 ? 3.497   9.725   -29.836 1.00 19.47 ?  149 ARG A O   1 
ATOM   1149 C CB  . ARG A 1 175 ? 3.302   6.753   -29.739 1.00 22.09 ?  149 ARG A CB  1 
ATOM   1150 C CG  . ARG A 1 175 ? 2.519   6.752   -28.443 1.00 21.06 ?  149 ARG A CG  1 
ATOM   1151 C CD  . ARG A 1 175 ? 3.243   5.857   -27.451 1.00 21.27 ?  149 ARG A CD  1 
ATOM   1152 N NE  . ARG A 1 175 ? 2.473   5.431   -26.325 1.00 20.51 ?  149 ARG A NE  1 
ATOM   1153 C CZ  . ARG A 1 175 ? 2.278   6.147   -25.221 1.00 20.11 ?  149 ARG A CZ  1 
ATOM   1154 N NH1 . ARG A 1 175 ? 2.806   7.356   -25.097 1.00 21.02 ?  149 ARG A NH1 1 
ATOM   1155 N NH2 . ARG A 1 175 ? 1.559   5.658   -24.252 1.00 21.55 ?  149 ARG A NH2 1 
ATOM   1156 N N   . LEU A 1 176 ? 1.276   9.524   -30.100 1.00 19.42 ?  150 LEU A N   1 
ATOM   1157 C CA  . LEU A 1 176 ? 0.898   10.727  -29.329 1.00 20.35 ?  150 LEU A CA  1 
ATOM   1158 C C   . LEU A 1 176 ? -0.251  10.328  -28.422 1.00 19.56 ?  150 LEU A C   1 
ATOM   1159 O O   . LEU A 1 176 ? -1.400  10.152  -28.904 1.00 17.74 ?  150 LEU A O   1 
ATOM   1160 C CB  . LEU A 1 176 ? 0.511   11.902  -30.260 1.00 20.60 ?  150 LEU A CB  1 
ATOM   1161 C CG  . LEU A 1 176 ? 0.225   13.226  -29.527 1.00 22.40 ?  150 LEU A CG  1 
ATOM   1162 C CD1 . LEU A 1 176 ? 1.495   13.777  -28.896 1.00 23.09 ?  150 LEU A CD1 1 
ATOM   1163 C CD2 . LEU A 1 176 ? -0.402  14.258  -30.479 1.00 24.02 ?  150 LEU A CD2 1 
ATOM   1164 N N   . TYR A 1 177 ? 0.023   10.258  -27.119 1.00 21.75 ?  151 TYR A N   1 
ATOM   1165 C CA  . TYR A 1 177 ? -0.971  9.858   -26.100 1.00 20.02 ?  151 TYR A CA  1 
ATOM   1166 C C   . TYR A 1 177 ? -2.251  10.673  -26.285 1.00 20.07 ?  151 TYR A C   1 
ATOM   1167 O O   . TYR A 1 177 ? -2.173  11.911  -26.390 1.00 20.92 ?  151 TYR A O   1 
ATOM   1168 C CB  . TYR A 1 177 ? -0.379  10.060  -24.724 1.00 21.44 ?  151 TYR A CB  1 
ATOM   1169 C CG  . TYR A 1 177 ? -1.193  9.513   -23.591 1.00 24.28 ?  151 TYR A CG  1 
ATOM   1170 C CD1 . TYR A 1 177 ? -1.565  8.180   -23.554 1.00 26.79 ?  151 TYR A CD1 1 
ATOM   1171 C CD2 . TYR A 1 177 ? -1.539  10.308  -22.517 1.00 26.69 ?  151 TYR A CD2 1 
ATOM   1172 C CE1 . TYR A 1 177 ? -2.286  7.656   -22.495 1.00 26.89 ?  151 TYR A CE1 1 
ATOM   1173 C CE2 . TYR A 1 177 ? -2.248  9.799   -21.443 1.00 28.72 ?  151 TYR A CE2 1 
ATOM   1174 C CZ  . TYR A 1 177 ? -2.657  8.478   -21.448 1.00 25.05 ?  151 TYR A CZ  1 
ATOM   1175 O OH  . TYR A 1 177 ? -3.314  7.969   -20.371 1.00 24.87 ?  151 TYR A OH  1 
ATOM   1176 N N   . SER A 1 178 ? -3.419  10.030  -26.340 1.00 19.18 ?  152 SER A N   1 
ATOM   1177 C CA  . SER A 1 178 ? -4.609  10.759  -26.832 1.00 18.91 ?  152 SER A CA  1 
ATOM   1178 C C   . SER A 1 178 ? -5.910  10.137  -26.338 1.00 20.05 ?  152 SER A C   1 
ATOM   1179 O O   . SER A 1 178 ? -6.179  8.969   -26.669 1.00 20.51 ?  152 SER A O   1 
ATOM   1180 C CB  . SER A 1 178 ? -4.587  10.846  -28.363 1.00 19.19 ?  152 SER A CB  1 
ATOM   1181 O OG  . SER A 1 178 ? -5.841  11.303  -28.872 1.00 18.38 ?  152 SER A OG  1 
ATOM   1182 N N   . ASN A 1 179 ? -6.702  10.934  -25.635 1.00 19.62 ?  153 ASN A N   1 
ATOM   1183 C CA  . ASN A 1 179 ? -8.083  10.563  -25.242 1.00 20.24 ?  153 ASN A CA  1 
ATOM   1184 C C   . ASN A 1 179 ? -8.967  10.381  -26.467 1.00 22.30 ?  153 ASN A C   1 
ATOM   1185 O O   . ASN A 1 179 ? -9.639  9.349   -26.593 1.00 20.81 ?  153 ASN A O   1 
ATOM   1186 C CB  . ASN A 1 179 ? -8.663  11.575  -24.268 1.00 23.82 ?  153 ASN A CB  1 
ATOM   1187 C CG  . ASN A 1 179 ? -8.171  11.363  -22.851 1.00 26.66 ?  153 ASN A CG  1 
ATOM   1188 O OD1 . ASN A 1 179 ? -7.699  10.282  -22.516 1.00 31.55 ?  153 ASN A OD1 1 
ATOM   1189 N ND2 . ASN A 1 179 ? -8.269  12.396  -22.020 1.00 27.76 ?  153 ASN A ND2 1 
ATOM   1190 N N   . PRO A 1 180 ? -9.058  11.368  -27.393 1.00 18.88 ?  154 PRO A N   1 
ATOM   1191 C CA  . PRO A 1 180 ? -9.871  11.180  -28.578 1.00 21.06 ?  154 PRO A CA  1 
ATOM   1192 C C   . PRO A 1 180 ? -9.515  9.881   -29.314 1.00 19.15 ?  154 PRO A C   1 
ATOM   1193 O O   . PRO A 1 180 ? -10.395 9.312   -29.916 1.00 19.40 ?  154 PRO A O   1 
ATOM   1194 C CB  . PRO A 1 180 ? -9.610  12.441  -29.442 1.00 21.45 ?  154 PRO A CB  1 
ATOM   1195 C CG  . PRO A 1 180 ? -9.033  13.464  -28.527 1.00 21.62 ?  154 PRO A CG  1 
ATOM   1196 C CD  . PRO A 1 180 ? -8.463  12.715  -27.338 1.00 20.63 ?  154 PRO A CD  1 
ATOM   1197 N N   . SER A 1 181 ? -8.234  9.481   -29.340 1.00 18.19 ?  155 SER A N   1 
ATOM   1198 C CA  . SER A 1 181 ? -7.779  8.268   -30.068 1.00 18.01 ?  155 SER A CA  1 
ATOM   1199 C C   . SER A 1 181 ? -8.346  6.993   -29.411 1.00 19.13 ?  155 SER A C   1 
ATOM   1200 O O   . SER A 1 181 ? -9.090  6.202   -30.078 1.00 20.28 ?  155 SER A O   1 
ATOM   1201 C CB  . SER A 1 181 ? -6.253  8.277   -30.157 1.00 17.08 ?  155 SER A CB  1 
ATOM   1202 O OG  . SER A 1 181 ? -5.787  7.204   -30.957 1.00 19.60 ?  155 SER A OG  1 
ATOM   1203 N N   . ILE A 1 182 ? -7.991  6.719   -28.164 1.00 19.72 ?  156 ILE A N   1 
ATOM   1204 C CA  . ILE A 1 182 ? -8.452  5.454   -27.532 1.00 20.28 ?  156 ILE A CA  1 
ATOM   1205 C C   . ILE A 1 182 ? -9.952  5.583   -27.229 1.00 17.32 ?  156 ILE A C   1 
ATOM   1206 O O   . ILE A 1 182 ? -10.664 4.531   -27.192 1.00 19.40 ?  156 ILE A O   1 
ATOM   1207 C CB  . ILE A 1 182 ? -7.564  5.073   -26.346 1.00 21.22 ?  156 ILE A CB  1 
ATOM   1208 C CG1 . ILE A 1 182 ? -7.822  3.615   -25.936 1.00 23.64 ?  156 ILE A CG1 1 
ATOM   1209 C CG2 . ILE A 1 182 ? -7.724  6.039   -25.199 1.00 22.74 ?  156 ILE A CG2 1 
ATOM   1210 C CD1 . ILE A 1 182 ? -6.734  3.025   -25.089 1.00 25.48 ?  156 ILE A CD1 1 
ATOM   1211 N N   . GLY A 1 183 ? -10.455 6.808   -27.015 1.00 17.53 ?  157 GLY A N   1 
ATOM   1212 C CA  . GLY A 1 183 ? -11.899 7.053   -26.834 1.00 19.00 ?  157 GLY A CA  1 
ATOM   1213 C C   . GLY A 1 183 ? -12.695 6.538   -28.020 1.00 19.98 ?  157 GLY A C   1 
ATOM   1214 O O   . GLY A 1 183 ? -13.698 5.808   -27.831 1.00 20.35 ?  157 GLY A O   1 
ATOM   1215 N N   . LEU A 1 184 ? -12.297 6.932   -29.221 1.00 21.65 ?  158 LEU A N   1 
ATOM   1216 C CA  . LEU A 1 184 ? -12.973 6.483   -30.460 1.00 21.12 ?  158 LEU A CA  1 
ATOM   1217 C C   . LEU A 1 184 ? -12.823 4.971   -30.569 1.00 20.36 ?  158 LEU A C   1 
ATOM   1218 O O   . LEU A 1 184 ? -13.786 4.299   -30.929 1.00 18.03 ?  158 LEU A O   1 
ATOM   1219 C CB  . LEU A 1 184 ? -12.401 7.222   -31.670 1.00 21.41 ?  158 LEU A CB  1 
ATOM   1220 C CG  . LEU A 1 184 ? -13.034 6.810   -32.996 1.00 21.37 ?  158 LEU A CG  1 
ATOM   1221 C CD1 . LEU A 1 184 ? -14.552 7.023   -32.957 1.00 19.94 ?  158 LEU A CD1 1 
ATOM   1222 C CD2 . LEU A 1 184 ? -12.386 7.609   -34.127 1.00 22.87 ?  158 LEU A CD2 1 
ATOM   1223 N N   . PHE A 1 185 ? -11.646 4.428   -30.280 1.00 19.05 ?  159 PHE A N   1 
ATOM   1224 C CA  . PHE A 1 185 ? -11.448 2.960   -30.302 1.00 18.91 ?  159 PHE A CA  1 
ATOM   1225 C C   . PHE A 1 185 ? -12.501 2.260   -29.427 1.00 19.25 ?  159 PHE A C   1 
ATOM   1226 O O   . PHE A 1 185 ? -13.143 1.284   -29.868 1.00 20.76 ?  159 PHE A O   1 
ATOM   1227 C CB  . PHE A 1 185 ? -10.035 2.608   -29.854 1.00 19.58 ?  159 PHE A CB  1 
ATOM   1228 C CG  . PHE A 1 185 ? -9.756  1.143   -29.674 1.00 17.07 ?  159 PHE A CG  1 
ATOM   1229 C CD1 . PHE A 1 185 ? -9.646  0.304   -30.773 1.00 19.01 ?  159 PHE A CD1 1 
ATOM   1230 C CD2 . PHE A 1 185 ? -9.552  0.610   -28.419 1.00 19.68 ?  159 PHE A CD2 1 
ATOM   1231 C CE1 . PHE A 1 185 ? -9.353  -1.043  -30.599 1.00 17.65 ?  159 PHE A CE1 1 
ATOM   1232 C CE2 . PHE A 1 185 ? -9.158  -0.712  -28.254 1.00 18.84 ?  159 PHE A CE2 1 
ATOM   1233 C CZ  . PHE A 1 185 ? -9.090  -1.544  -29.343 1.00 18.74 ?  159 PHE A CZ  1 
ATOM   1234 N N   . GLY A 1 186 ? -12.752 2.743   -28.212 1.00 18.94 ?  160 GLY A N   1 
ATOM   1235 C CA  . GLY A 1 186 ? -13.743 2.074   -27.337 1.00 19.11 ?  160 GLY A CA  1 
ATOM   1236 C C   . GLY A 1 186 ? -15.153 2.293   -27.854 1.00 19.23 ?  160 GLY A C   1 
ATOM   1237 O O   . GLY A 1 186 ? -15.955 1.364   -27.760 1.00 19.21 ?  160 GLY A O   1 
ATOM   1238 N N   . TYR A 1 187 ? -15.439 3.462   -28.419 1.00 19.46 ?  161 TYR A N   1 
ATOM   1239 C CA  . TYR A 1 187 ? -16.803 3.786   -28.929 1.00 21.32 ?  161 TYR A CA  1 
ATOM   1240 C C   . TYR A 1 187 ? -17.109 2.842   -30.104 1.00 22.57 ?  161 TYR A C   1 
ATOM   1241 O O   . TYR A 1 187 ? -18.235 2.323   -30.182 1.00 21.94 ?  161 TYR A O   1 
ATOM   1242 C CB  . TYR A 1 187 ? -16.899 5.251   -29.349 1.00 20.24 ?  161 TYR A CB  1 
ATOM   1243 C CG  . TYR A 1 187 ? -18.230 5.611   -29.936 1.00 25.07 ?  161 TYR A CG  1 
ATOM   1244 C CD1 . TYR A 1 187 ? -19.403 5.306   -29.263 1.00 31.70 ?  161 TYR A CD1 1 
ATOM   1245 C CD2 . TYR A 1 187 ? -18.321 6.198   -31.183 1.00 27.87 ?  161 TYR A CD2 1 
ATOM   1246 C CE1 . TYR A 1 187 ? -20.642 5.607   -29.809 1.00 31.92 ?  161 TYR A CE1 1 
ATOM   1247 C CE2 . TYR A 1 187 ? -19.551 6.517   -31.733 1.00 31.99 ?  161 TYR A CE2 1 
ATOM   1248 C CZ  . TYR A 1 187 ? -20.714 6.223   -31.047 1.00 35.01 ?  161 TYR A CZ  1 
ATOM   1249 O OH  . TYR A 1 187 ? -21.933 6.529   -31.603 1.00 36.55 ?  161 TYR A OH  1 
ATOM   1250 N N   . LEU A 1 188 ? -16.146 2.684   -31.021 1.00 22.01 ?  162 LEU A N   1 
ATOM   1251 C CA  . LEU A 1 188 ? -16.276 1.787   -32.218 1.00 21.59 ?  162 LEU A CA  1 
ATOM   1252 C C   . LEU A 1 188 ? -16.398 0.331   -31.755 1.00 21.57 ?  162 LEU A C   1 
ATOM   1253 O O   . LEU A 1 188 ? -17.243 -0.449  -32.338 1.00 23.30 ?  162 LEU A O   1 
ATOM   1254 C CB  . LEU A 1 188 ? -15.083 1.988   -33.163 1.00 20.64 ?  162 LEU A CB  1 
ATOM   1255 C CG  . LEU A 1 188 ? -14.984 3.394   -33.783 1.00 22.35 ?  162 LEU A CG  1 
ATOM   1256 C CD1 . LEU A 1 188 ? -13.838 3.501   -34.765 1.00 23.34 ?  162 LEU A CD1 1 
ATOM   1257 C CD2 . LEU A 1 188 ? -16.247 3.843   -34.464 1.00 24.59 ?  162 LEU A CD2 1 
ATOM   1258 N N   . ALA A 1 189 ? -15.615 -0.092  -30.759 1.00 23.03 ?  163 ALA A N   1 
ATOM   1259 C CA  . ALA A 1 189 ? -15.770 -1.450  -30.197 1.00 20.43 ?  163 ALA A CA  1 
ATOM   1260 C C   . ALA A 1 189 ? -17.241 -1.635  -29.754 1.00 21.44 ?  163 ALA A C   1 
ATOM   1261 O O   . ALA A 1 189 ? -17.855 -2.726  -30.057 1.00 23.09 ?  163 ALA A O   1 
ATOM   1262 C CB  . ALA A 1 189 ? -14.813 -1.697  -29.070 1.00 22.95 ?  163 ALA A CB  1 
ATOM   1263 N N   . ALA A 1 190 ? -17.789 -0.662  -29.020 1.00 20.90 ?  164 ALA A N   1 
ATOM   1264 C CA  . ALA A 1 190 ? -19.194 -0.735  -28.519 1.00 22.61 ?  164 ALA A CA  1 
ATOM   1265 C C   . ALA A 1 190 ? -20.176 -0.792  -29.692 1.00 22.78 ?  164 ALA A C   1 
ATOM   1266 O O   . ALA A 1 190 ? -21.103 -1.619  -29.639 1.00 23.02 ?  164 ALA A O   1 
ATOM   1267 C CB  . ALA A 1 190 ? -19.493 0.432   -27.623 1.00 23.86 ?  164 ALA A CB  1 
ATOM   1268 N N   . ARG A 1 191 ? -20.001 0.056   -30.714 1.00 22.56 ?  165 ARG A N   1 
ATOM   1269 C CA  . ARG A 1 191 ? -20.857 0.033   -31.914 1.00 24.04 ?  165 ARG A CA  1 
ATOM   1270 C C   . ARG A 1 191 ? -20.780 -1.359  -32.552 1.00 24.29 ?  165 ARG A C   1 
ATOM   1271 O O   . ARG A 1 191 ? -21.825 -1.890  -32.924 1.00 26.10 ?  165 ARG A O   1 
ATOM   1272 C CB  . ARG A 1 191 ? -20.485 1.104   -32.936 1.00 22.80 ?  165 ARG A CB  1 
ATOM   1273 C CG  . ARG A 1 191 ? -20.726 2.541   -32.501 1.00 25.62 ?  165 ARG A CG  1 
ATOM   1274 C CD  . ARG A 1 191 ? -20.531 3.547   -33.640 1.00 29.33 ?  165 ARG A CD  1 
ATOM   1275 N NE  . ARG A 1 191 ? -21.485 3.255   -34.695 1.00 33.40 ?  165 ARG A NE  1 
ATOM   1276 C CZ  . ARG A 1 191 ? -22.681 3.830   -34.829 1.00 34.31 ?  165 ARG A CZ  1 
ATOM   1277 N NH1 . ARG A 1 191 ? -23.064 4.810   -34.026 1.00 32.50 ?  165 ARG A NH1 1 
ATOM   1278 N NH2 . ARG A 1 191 ? -23.461 3.471   -35.831 1.00 36.31 ?  165 ARG A NH2 1 
ATOM   1279 N N   . SER A 1 192 ? -19.597 -1.960  -32.619 1.00 23.15 ?  166 SER A N   1 
ATOM   1280 C CA  . SER A 1 192 ? -19.398 -3.306  -33.216 1.00 24.45 ?  166 SER A CA  1 
ATOM   1281 C C   . SER A 1 192 ? -20.235 -4.345  -32.450 1.00 27.31 ?  166 SER A C   1 
ATOM   1282 O O   . SER A 1 192 ? -20.590 -5.411  -33.052 1.00 27.28 ?  166 SER A O   1 
ATOM   1283 C CB  . SER A 1 192 ? -17.906 -3.672  -33.268 1.00 21.52 ?  166 SER A CB  1 
ATOM   1284 O OG  . SER A 1 192 ? -17.498 -4.403  -32.108 1.00 21.25 ?  166 SER A OG  1 
ATOM   1285 N N   . LEU A 1 193 ? -20.510 -4.092  -31.165 1.00 24.66 ?  167 LEU A N   1 
ATOM   1286 C CA  . LEU A 1 193 ? -21.303 -5.019  -30.315 1.00 27.83 ?  167 LEU A CA  1 
ATOM   1287 C C   . LEU A 1 193 ? -22.792 -4.640  -30.336 1.00 25.09 ?  167 LEU A C   1 
ATOM   1288 O O   . LEU A 1 193 ? -23.566 -5.336  -29.643 1.00 26.42 ?  167 LEU A O   1 
ATOM   1289 C CB  . LEU A 1 193 ? -20.735 -5.021  -28.887 1.00 26.81 ?  167 LEU A CB  1 
ATOM   1290 C CG  . LEU A 1 193 ? -19.414 -5.776  -28.718 1.00 27.32 ?  167 LEU A CG  1 
ATOM   1291 C CD1 . LEU A 1 193 ? -18.716 -5.393  -27.422 1.00 26.18 ?  167 LEU A CD1 1 
ATOM   1292 C CD2 . LEU A 1 193 ? -19.646 -7.276  -28.772 1.00 27.76 ?  167 LEU A CD2 1 
ATOM   1293 N N   . GLY A 1 194 ? -23.149 -3.576  -31.049 1.00 25.30 ?  168 GLY A N   1 
ATOM   1294 C CA  . GLY A 1 194 ? -24.526 -3.071  -31.216 1.00 28.17 ?  168 GLY A CA  1 
ATOM   1295 C C   . GLY A 1 194 ? -25.110 -2.435  -29.965 1.00 31.48 ?  168 GLY A C   1 
ATOM   1296 O O   . GLY A 1 194 ? -26.348 -2.348  -29.873 1.00 26.80 ?  168 GLY A O   1 
ATOM   1297 N N   . GLN A 1 195 ? -24.299 -1.920  -29.035 1.00 27.37 ?  169 GLN A N   1 
ATOM   1298 C CA  . GLN A 1 195 ? -24.876 -1.263  -27.837 1.00 24.87 ?  169 GLN A CA  1 
ATOM   1299 C C   . GLN A 1 195 ? -24.012 -0.074  -27.430 1.00 25.17 ?  169 GLN A C   1 
ATOM   1300 O O   . GLN A 1 195 ? -22.840 0.010   -27.784 1.00 24.06 ?  169 GLN A O   1 
ATOM   1301 C CB  . GLN A 1 195 ? -24.994 -2.279  -26.697 1.00 27.22 ?  169 GLN A CB  1 
ATOM   1302 C CG  . GLN A 1 195 ? -25.934 -3.444  -26.999 1.00 29.83 ?  169 GLN A CG  1 
ATOM   1303 C CD  . GLN A 1 195 ? -26.144 -4.278  -25.763 1.00 31.83 ?  169 GLN A CD  1 
ATOM   1304 O OE1 . GLN A 1 195 ? -26.376 -3.770  -24.671 1.00 36.21 ?  169 GLN A OE1 1 
ATOM   1305 N NE2 . GLN A 1 195 ? -26.019 -5.573  -25.907 1.00 34.79 ?  169 GLN A NE2 1 
ATOM   1306 N N   . PRO A 1 196 ? -24.562 0.882   -26.670 1.00 25.86 ?  170 PRO A N   1 
ATOM   1307 C CA  . PRO A 1 196 ? -23.744 1.951   -26.108 1.00 23.89 ?  170 PRO A CA  1 
ATOM   1308 C C   . PRO A 1 196 ? -22.613 1.474   -25.177 1.00 22.53 ?  170 PRO A C   1 
ATOM   1309 O O   . PRO A 1 196 ? -22.739 0.490   -24.428 1.00 20.27 ?  170 PRO A O   1 
ATOM   1310 C CB  . PRO A 1 196 ? -24.724 2.806   -25.318 1.00 28.01 ?  170 PRO A CB  1 
ATOM   1311 C CG  . PRO A 1 196 ? -26.095 2.458   -25.871 1.00 27.38 ?  170 PRO A CG  1 
ATOM   1312 C CD  . PRO A 1 196 ? -25.997 1.034   -26.364 1.00 25.63 ?  170 PRO A CD  1 
ATOM   1313 N N   . PHE A 1 197 ? -21.522 2.233   -25.183 1.00 21.67 ?  171 PHE A N   1 
ATOM   1314 C CA  . PHE A 1 197 ? -20.289 1.857   -24.463 1.00 22.29 ?  171 PHE A CA  1 
ATOM   1315 C C   . PHE A 1 197 ? -20.633 1.686   -22.977 1.00 18.56 ?  171 PHE A C   1 
ATOM   1316 O O   . PHE A 1 197 ? -20.346 0.671   -22.355 1.00 20.12 ?  171 PHE A O   1 
ATOM   1317 C CB  . PHE A 1 197 ? -19.207 2.908   -24.715 1.00 21.26 ?  171 PHE A CB  1 
ATOM   1318 C CG  . PHE A 1 197 ? -17.945 2.645   -23.937 1.00 21.31 ?  171 PHE A CG  1 
ATOM   1319 C CD1 . PHE A 1 197 ? -16.958 1.812   -24.436 1.00 21.74 ?  171 PHE A CD1 1 
ATOM   1320 C CD2 . PHE A 1 197 ? -17.768 3.181   -22.662 1.00 23.18 ?  171 PHE A CD2 1 
ATOM   1321 C CE1 . PHE A 1 197 ? -15.817 1.538   -23.691 1.00 20.51 ?  171 PHE A CE1 1 
ATOM   1322 C CE2 . PHE A 1 197 ? -16.605 2.941   -21.948 1.00 21.44 ?  171 PHE A CE2 1 
ATOM   1323 C CZ  . PHE A 1 197 ? -15.667 2.077   -22.437 1.00 20.89 ?  171 PHE A CZ  1 
ATOM   1324 N N   . GLU A 1 198 ? -21.288 2.688   -22.423 1.00 18.88 ?  172 GLU A N   1 
ATOM   1325 C CA  . GLU A 1 198 ? -21.553 2.772   -20.963 1.00 20.85 ?  172 GLU A CA  1 
ATOM   1326 C C   . GLU A 1 198 ? -22.483 1.616   -20.542 1.00 19.45 ?  172 GLU A C   1 
ATOM   1327 O O   . GLU A 1 198 ? -22.250 1.047   -19.439 1.00 20.95 ?  172 GLU A O   1 
ATOM   1328 C CB  . GLU A 1 198 ? -22.111 4.158   -20.610 1.00 24.33 ?  172 GLU A CB  1 
ATOM   1329 C CG  . GLU A 1 198 ? -21.188 5.290   -21.060 1.00 28.31 ?  172 GLU A CG  1 
ATOM   1330 C CD  . GLU A 1 198 ? -21.450 5.865   -22.456 1.00 35.07 ?  172 GLU A CD  1 
ATOM   1331 O OE1 . GLU A 1 198 ? -22.153 5.187   -23.316 1.00 31.17 ?  172 GLU A OE1 1 
ATOM   1332 O OE2 . GLU A 1 198 ? -21.000 7.030   -22.683 1.00 41.33 ?  172 GLU A OE2 1 
ATOM   1333 N N   . ARG A 1 199 ? -23.480 1.280   -21.360 1.00 21.24 ?  173 ARG A N   1 
ATOM   1334 C CA  . ARG A 1 199 ? -24.397 0.130   -21.086 1.00 22.36 ?  173 ARG A CA  1 
ATOM   1335 C C   . ARG A 1 199 ? -23.598 -1.180  -21.063 1.00 21.51 ?  173 ARG A C   1 
ATOM   1336 O O   . ARG A 1 199 ? -23.765 -1.978  -20.101 1.00 21.03 ?  173 ARG A O   1 
ATOM   1337 C CB  . ARG A 1 199 ? -25.569 0.067   -22.067 1.00 24.18 ?  173 ARG A CB  1 
ATOM   1338 C CG  . ARG A 1 199 ? -26.580 -1.025  -21.723 1.00 25.62 ?  173 ARG A CG  1 
ATOM   1339 C CD  . ARG A 1 199 ? -27.484 -1.458  -22.876 1.00 28.62 ?  173 ARG A CD  1 
ATOM   1340 N NE  . ARG A 1 199 ? -28.237 -0.334  -23.415 1.00 36.13 ?  173 ARG A NE  1 
ATOM   1341 C CZ  . ARG A 1 199 ? -28.761 -0.235  -24.651 1.00 39.75 ?  173 ARG A CZ  1 
ATOM   1342 N NH1 . ARG A 1 199 ? -28.620 -1.208  -25.543 1.00 37.18 ?  173 ARG A NH1 1 
ATOM   1343 N NH2 . ARG A 1 199 ? -29.411 0.871   -24.986 1.00 44.15 ?  173 ARG A NH2 1 
ATOM   1344 N N   . LEU A 1 200 ? -22.759 -1.412  -22.068 1.00 23.23 ?  174 LEU A N   1 
ATOM   1345 C CA  . LEU A 1 200 ? -21.918 -2.636  -22.141 1.00 22.80 ?  174 LEU A CA  1 
ATOM   1346 C C   . LEU A 1 200 ? -21.052 -2.739  -20.889 1.00 22.65 ?  174 LEU A C   1 
ATOM   1347 O O   . LEU A 1 200 ? -20.935 -3.847  -20.342 1.00 19.52 ?  174 LEU A O   1 
ATOM   1348 C CB  . LEU A 1 200 ? -21.057 -2.595  -23.398 1.00 22.08 ?  174 LEU A CB  1 
ATOM   1349 C CG  . LEU A 1 200 ? -21.812 -2.857  -24.689 1.00 22.11 ?  174 LEU A CG  1 
ATOM   1350 C CD1 . LEU A 1 200 ? -20.988 -2.408  -25.888 1.00 22.46 ?  174 LEU A CD1 1 
ATOM   1351 C CD2 . LEU A 1 200 ? -22.203 -4.338  -24.785 1.00 23.59 ?  174 LEU A CD2 1 
ATOM   1352 N N   . MET A 1 201 ? -20.470 -1.618  -20.436 1.00 23.02 ?  175 MET A N   1 
ATOM   1353 C CA  . MET A 1 201 ? -19.548 -1.664  -19.279 1.00 24.68 ?  175 MET A CA  1 
ATOM   1354 C C   . MET A 1 201 ? -20.336 -2.072  -18.047 1.00 21.27 ?  175 MET A C   1 
ATOM   1355 O O   . MET A 1 201 ? -19.882 -3.000  -17.364 1.00 21.23 ?  175 MET A O   1 
ATOM   1356 C CB  . MET A 1 201 ? -18.834 -0.329  -19.040 1.00 23.87 ?  175 MET A CB  1 
ATOM   1357 C CG  . MET A 1 201 ? -18.014 0.103   -20.211 1.00 29.02 ?  175 MET A CG  1 
ATOM   1358 S SD  . MET A 1 201 ? -16.572 -0.969  -20.593 1.00 36.39 ?  175 MET A SD  1 
ATOM   1359 C CE  . MET A 1 201 ? -16.033 -1.355  -18.952 1.00 20.71 ?  175 MET A CE  1 
ATOM   1360 N N   . GLU A 1 202 ? -21.502 -1.435  -17.774 1.00 22.74 ?  176 GLU A N   1 
ATOM   1361 C CA  . GLU A 1 202 ? -22.302 -1.711  -16.548 1.00 22.17 ?  176 GLU A CA  1 
ATOM   1362 C C   . GLU A 1 202 ? -22.986 -3.074  -16.627 1.00 22.13 ?  176 GLU A C   1 
ATOM   1363 O O   . GLU A 1 202 ? -23.055 -3.762  -15.582 1.00 20.51 ?  176 GLU A O   1 
ATOM   1364 C CB  . GLU A 1 202 ? -23.420 -0.694  -16.361 1.00 22.42 ?  176 GLU A CB  1 
ATOM   1365 C CG  . GLU A 1 202 ? -22.912 0.715   -16.127 1.00 23.63 ?  176 GLU A CG  1 
ATOM   1366 C CD  . GLU A 1 202 ? -24.008 1.759   -15.995 1.00 25.90 ?  176 GLU A CD  1 
ATOM   1367 O OE1 . GLU A 1 202 ? -25.182 1.459   -16.319 1.00 25.54 ?  176 GLU A OE1 1 
ATOM   1368 O OE2 . GLU A 1 202 ? -23.682 2.863   -15.569 1.00 27.48 ?  176 GLU A OE2 1 
ATOM   1369 N N   . GLN A 1 203 ? -23.493 -3.445  -17.808 1.00 21.93 ?  177 GLN A N   1 
ATOM   1370 C CA  . GLN A 1 203 ? -24.412 -4.616  -17.932 1.00 23.75 ?  177 GLN A CA  1 
ATOM   1371 C C   . GLN A 1 203 ? -23.590 -5.892  -18.196 1.00 24.29 ?  177 GLN A C   1 
ATOM   1372 O O   . GLN A 1 203 ? -24.043 -6.981  -17.772 1.00 22.31 ?  177 GLN A O   1 
ATOM   1373 C CB  . GLN A 1 203 ? -25.448 -4.404  -19.039 1.00 24.34 ?  177 GLN A CB  1 
ATOM   1374 C CG  . GLN A 1 203 ? -26.413 -3.242  -18.794 1.00 28.31 ?  177 GLN A CG  1 
ATOM   1375 C CD  . GLN A 1 203 ? -27.292 -3.487  -17.591 1.00 30.91 ?  177 GLN A CD  1 
ATOM   1376 O OE1 . GLN A 1 203 ? -27.033 -3.007  -16.481 1.00 29.63 ?  177 GLN A OE1 1 
ATOM   1377 N NE2 . GLN A 1 203 ? -28.328 -4.284  -17.787 1.00 29.57 ?  177 GLN A NE2 1 
ATOM   1378 N N   . GLN A 1 204 ? -22.422 -5.779  -18.844 1.00 23.52 ?  178 GLN A N   1 
ATOM   1379 C CA  . GLN A 1 204 ? -21.647 -6.965  -19.265 1.00 24.97 ?  178 GLN A CA  1 
ATOM   1380 C C   . GLN A 1 204 ? -20.250 -6.993  -18.648 1.00 22.60 ?  178 GLN A C   1 
ATOM   1381 O O   . GLN A 1 204 ? -19.916 -8.003  -18.048 1.00 22.37 ?  178 GLN A O   1 
ATOM   1382 C CB  . GLN A 1 204 ? -21.605 -7.043  -20.792 1.00 27.60 ?  178 GLN A CB  1 
ATOM   1383 C CG  . GLN A 1 204 ? -22.985 -7.322  -21.380 1.00 33.40 ?  178 GLN A CG  1 
ATOM   1384 C CD  . GLN A 1 204 ? -22.867 -7.962  -22.741 1.00 38.22 ?  178 GLN A CD  1 
ATOM   1385 O OE1 . GLN A 1 204 ? -23.221 -7.372  -23.754 1.00 47.66 ?  178 GLN A OE1 1 
ATOM   1386 N NE2 . GLN A 1 204 ? -22.366 -9.191  -22.768 1.00 44.76 ?  178 GLN A NE2 1 
ATOM   1387 N N   . VAL A 1 205 ? -19.446 -5.965  -18.823 1.00 20.89 ?  179 VAL A N   1 
ATOM   1388 C CA  . VAL A 1 205 ? -18.000 -6.067  -18.470 1.00 18.90 ?  179 VAL A CA  1 
ATOM   1389 C C   . VAL A 1 205 ? -17.824 -6.152  -16.953 1.00 19.85 ?  179 VAL A C   1 
ATOM   1390 O O   . VAL A 1 205 ? -17.186 -7.100  -16.470 1.00 20.86 ?  179 VAL A O   1 
ATOM   1391 C CB  . VAL A 1 205 ? -17.201 -4.904  -19.057 1.00 19.51 ?  179 VAL A CB  1 
ATOM   1392 C CG1 . VAL A 1 205 ? -15.733 -5.012  -18.674 1.00 19.48 ?  179 VAL A CG1 1 
ATOM   1393 C CG2 . VAL A 1 205 ? -17.342 -4.860  -20.558 1.00 21.05 ?  179 VAL A CG2 1 
ATOM   1394 N N   . PHE A 1 206 ? -18.380 -5.215  -16.192 1.00 19.97 ?  180 PHE A N   1 
ATOM   1395 C CA  . PHE A 1 206 ? -18.148 -5.190  -14.739 1.00 20.73 ?  180 PHE A CA  1 
ATOM   1396 C C   . PHE A 1 206 ? -18.688 -6.471  -14.112 1.00 21.35 ?  180 PHE A C   1 
ATOM   1397 O O   . PHE A 1 206 ? -17.992 -7.060  -13.304 1.00 21.50 ?  180 PHE A O   1 
ATOM   1398 C CB  . PHE A 1 206 ? -18.689 -3.904  -14.120 1.00 19.51 ?  180 PHE A CB  1 
ATOM   1399 C CG  . PHE A 1 206 ? -18.075 -2.610  -14.602 1.00 19.69 ?  180 PHE A CG  1 
ATOM   1400 C CD1 . PHE A 1 206 ? -16.753 -2.528  -15.043 1.00 19.57 ?  180 PHE A CD1 1 
ATOM   1401 C CD2 . PHE A 1 206 ? -18.804 -1.433  -14.453 1.00 20.69 ?  180 PHE A CD2 1 
ATOM   1402 C CE1 . PHE A 1 206 ? -16.217 -1.307  -15.426 1.00 22.04 ?  180 PHE A CE1 1 
ATOM   1403 C CE2 . PHE A 1 206 ? -18.266 -0.226  -14.847 1.00 19.75 ?  180 PHE A CE2 1 
ATOM   1404 C CZ  . PHE A 1 206 ? -16.963 -0.157  -15.277 1.00 22.02 ?  180 PHE A CZ  1 
ATOM   1405 N N   . PRO A 1 207 ? -19.931 -6.936  -14.409 1.00 21.66 ?  181 PRO A N   1 
ATOM   1406 C CA  . PRO A 1 207 ? -20.403 -8.199  -13.852 1.00 23.84 ?  181 PRO A CA  1 
ATOM   1407 C C   . PRO A 1 207 ? -19.550 -9.418  -14.236 1.00 23.81 ?  181 PRO A C   1 
ATOM   1408 O O   . PRO A 1 207 ? -19.330 -10.260 -13.383 1.00 24.76 ?  181 PRO A O   1 
ATOM   1409 C CB  . PRO A 1 207 ? -21.834 -8.343  -14.407 1.00 25.38 ?  181 PRO A CB  1 
ATOM   1410 C CG  . PRO A 1 207 ? -22.239 -6.932  -14.734 1.00 24.69 ?  181 PRO A CG  1 
ATOM   1411 C CD  . PRO A 1 207 ? -20.959 -6.272  -15.218 1.00 25.10 ?  181 PRO A CD  1 
ATOM   1412 N N   . ALA A 1 208 ? -19.071 -9.492  -15.476 1.00 23.12 ?  182 ALA A N   1 
ATOM   1413 C CA  . ALA A 1 208 ? -18.218 -10.613 -15.951 1.00 23.08 ?  182 ALA A CA  1 
ATOM   1414 C C   . ALA A 1 208 ? -16.919 -10.627 -15.147 1.00 24.91 ?  182 ALA A C   1 
ATOM   1415 O O   . ALA A 1 208 ? -16.379 -11.726 -14.905 1.00 25.08 ?  182 ALA A O   1 
ATOM   1416 C CB  . ALA A 1 208 ? -17.935 -10.477 -17.421 1.00 25.01 ?  182 ALA A CB  1 
ATOM   1417 N N   . LEU A 1 209 ? -16.457 -9.453  -14.690 1.00 23.66 ?  183 LEU A N   1 
ATOM   1418 C CA  . LEU A 1 209 ? -15.175 -9.333  -13.944 1.00 23.42 ?  183 LEU A CA  1 
ATOM   1419 C C   . LEU A 1 209 ? -15.425 -9.428  -12.431 1.00 23.09 ?  183 LEU A C   1 
ATOM   1420 O O   . LEU A 1 209 ? -14.447 -9.333  -11.699 1.00 25.61 ?  183 LEU A O   1 
ATOM   1421 C CB  . LEU A 1 209 ? -14.463 -8.028  -14.320 1.00 25.27 ?  183 LEU A CB  1 
ATOM   1422 C CG  . LEU A 1 209 ? -14.043 -7.897  -15.791 1.00 28.57 ?  183 LEU A CG  1 
ATOM   1423 C CD1 . LEU A 1 209 ? -13.566 -6.490  -16.143 1.00 28.77 ?  183 LEU A CD1 1 
ATOM   1424 C CD2 . LEU A 1 209 ? -12.956 -8.893  -16.143 1.00 34.08 ?  183 LEU A CD2 1 
ATOM   1425 N N   . GLY A 1 210 ? -16.675 -9.578  -11.975 1.00 24.17 ?  184 GLY A N   1 
ATOM   1426 C CA  . GLY A 1 210 ? -17.015 -9.663  -10.539 1.00 25.13 ?  184 GLY A CA  1 
ATOM   1427 C C   . GLY A 1 210 ? -16.901 -8.327  -9.817  1.00 24.23 ?  184 GLY A C   1 
ATOM   1428 O O   . GLY A 1 210 ? -16.587 -8.312  -8.609  1.00 23.72 ?  184 GLY A O   1 
ATOM   1429 N N   . LEU A 1 211 ? -17.102 -7.217  -10.526 1.00 23.39 ?  185 LEU A N   1 
ATOM   1430 C CA  . LEU A 1 211 ? -16.835 -5.858  -9.997  1.00 22.99 ?  185 LEU A CA  1 
ATOM   1431 C C   . LEU A 1 211 ? -18.165 -5.176  -9.652  1.00 22.74 ?  185 LEU A C   1 
ATOM   1432 O O   . LEU A 1 211 ? -18.822 -4.650  -10.547 1.00 26.67 ?  185 LEU A O   1 
ATOM   1433 C CB  . LEU A 1 211 ? -16.072 -5.094  -11.073 1.00 23.88 ?  185 LEU A CB  1 
ATOM   1434 C CG  . LEU A 1 211 ? -14.750 -5.714  -11.527 1.00 23.90 ?  185 LEU A CG  1 
ATOM   1435 C CD1 . LEU A 1 211 ? -14.052 -4.788  -12.504 1.00 22.86 ?  185 LEU A CD1 1 
ATOM   1436 C CD2 . LEU A 1 211 ? -13.839 -6.013  -10.358 1.00 24.74 ?  185 LEU A CD2 1 
ATOM   1437 N N   . GLU A 1 212 ? -18.513 -5.128  -8.368  1.00 23.71 ?  186 GLU A N   1 
ATOM   1438 C CA  . GLU A 1 212 ? -19.773 -4.507  -7.886  1.00 26.33 ?  186 GLU A CA  1 
ATOM   1439 C C   . GLU A 1 212 ? -19.498 -3.157  -7.201  1.00 24.63 ?  186 GLU A C   1 
ATOM   1440 O O   . GLU A 1 212 ? -20.468 -2.501  -6.848  1.00 26.17 ?  186 GLU A O   1 
ATOM   1441 C CB  . GLU A 1 212 ? -20.445 -5.472  -6.925  1.00 33.40 ?  186 GLU A CB  1 
ATOM   1442 C CG  . GLU A 1 212 ? -20.683 -6.835  -7.544  1.00 40.35 ?  186 GLU A CG  1 
ATOM   1443 C CD  . GLU A 1 212 ? -21.846 -7.570  -6.905  1.00 49.09 ?  186 GLU A CD  1 
ATOM   1444 O OE1 . GLU A 1 212 ? -21.583 -8.409  -6.010  1.00 57.00 ?  186 GLU A OE1 1 
ATOM   1445 O OE2 . GLU A 1 212 ? -23.003 -7.293  -7.295  1.00 59.39 ?  186 GLU A OE2 1 
ATOM   1446 N N   . GLN A 1 213 ? -18.242 -2.721  -7.108  1.00 21.46 ?  187 GLN A N   1 
ATOM   1447 C CA  . GLN A 1 213 ? -17.867 -1.382  -6.544  1.00 24.91 ?  187 GLN A CA  1 
ATOM   1448 C C   . GLN A 1 213 ? -17.136 -0.547  -7.607  1.00 22.89 ?  187 GLN A C   1 
ATOM   1449 O O   . GLN A 1 213 ? -16.194 0.193   -7.262  1.00 25.30 ?  187 GLN A O   1 
ATOM   1450 C CB  . GLN A 1 213 ? -16.967 -1.512  -5.308  1.00 25.99 ?  187 GLN A CB  1 
ATOM   1451 C CG  . GLN A 1 213 ? -17.530 -2.393  -4.208  1.00 31.79 ?  187 GLN A CG  1 
ATOM   1452 C CD  . GLN A 1 213 ? -16.571 -2.617  -3.057  1.00 37.79 ?  187 GLN A CD  1 
ATOM   1453 O OE1 . GLN A 1 213 ? -15.459 -2.072  -2.963  1.00 36.33 ?  187 GLN A OE1 1 
ATOM   1454 N NE2 . GLN A 1 213 ? -16.988 -3.486  -2.154  1.00 44.94 ?  187 GLN A NE2 1 
ATOM   1455 N N   . THR A 1 214 ? -17.439 -0.787  -8.887  1.00 22.55 ?  188 THR A N   1 
ATOM   1456 C CA  . THR A 1 214 ? -16.783 -0.130  -10.051 1.00 21.68 ?  188 THR A CA  1 
ATOM   1457 C C   . THR A 1 214 ? -17.856 0.536   -10.904 1.00 21.16 ?  188 THR A C   1 
ATOM   1458 O O   . THR A 1 214 ? -18.832 -0.137  -11.235 1.00 24.08 ?  188 THR A O   1 
ATOM   1459 C CB  . THR A 1 214 ? -15.960 -1.140  -10.874 1.00 21.64 ?  188 THR A CB  1 
ATOM   1460 O OG1 . THR A 1 214 ? -14.967 -1.700  -10.022 1.00 19.81 ?  188 THR A OG1 1 
ATOM   1461 C CG2 . THR A 1 214 ? -15.277 -0.523  -12.064 1.00 21.14 ?  188 THR A CG2 1 
ATOM   1462 N N   . HIS A 1 215 ? -17.738 1.834   -11.194 1.00 18.82 ?  189 HIS A N   1 
ATOM   1463 C CA  . HIS A 1 215 ? -18.861 2.630   -11.744 1.00 19.51 ?  189 HIS A CA  1 
ATOM   1464 C C   . HIS A 1 215 ? -18.332 3.553   -12.828 1.00 19.51 ?  189 HIS A C   1 
ATOM   1465 O O   . HIS A 1 215 ? -17.148 4.025   -12.728 1.00 19.96 ?  189 HIS A O   1 
ATOM   1466 C CB  . HIS A 1 215 ? -19.563 3.437   -10.633 1.00 19.92 ?  189 HIS A CB  1 
ATOM   1467 C CG  . HIS A 1 215 ? -19.823 2.646   -9.397  1.00 21.40 ?  189 HIS A CG  1 
ATOM   1468 N ND1 . HIS A 1 215 ? -20.917 1.805   -9.291  1.00 22.40 ?  189 HIS A ND1 1 
ATOM   1469 C CD2 . HIS A 1 215 ? -19.155 2.552   -8.222  1.00 20.85 ?  189 HIS A CD2 1 
ATOM   1470 C CE1 . HIS A 1 215 ? -20.911 1.261   -8.079  1.00 20.96 ?  189 HIS A CE1 1 
ATOM   1471 N NE2 . HIS A 1 215 ? -19.870 1.701   -7.420  1.00 22.67 ?  189 HIS A NE2 1 
ATOM   1472 N N   . LEU A 1 216 ? -19.149 3.822   -13.830 1.00 19.74 ?  190 LEU A N   1 
ATOM   1473 C CA  . LEU A 1 216 ? -18.940 5.010   -14.691 1.00 20.78 ?  190 LEU A CA  1 
ATOM   1474 C C   . LEU A 1 216 ? -19.747 6.180   -14.160 1.00 22.06 ?  190 LEU A C   1 
ATOM   1475 O O   . LEU A 1 216 ? -19.336 7.359   -14.339 1.00 22.58 ?  190 LEU A O   1 
ATOM   1476 C CB  . LEU A 1 216 ? -19.416 4.666   -16.094 1.00 21.34 ?  190 LEU A CB  1 
ATOM   1477 C CG  . LEU A 1 216 ? -18.578 3.618   -16.798 1.00 20.14 ?  190 LEU A CG  1 
ATOM   1478 C CD1 . LEU A 1 216 ? -19.232 3.278   -18.117 1.00 22.31 ?  190 LEU A CD1 1 
ATOM   1479 C CD2 . LEU A 1 216 ? -17.135 4.075   -16.997 1.00 20.57 ?  190 LEU A CD2 1 
ATOM   1480 N N   . ASP A 1 217 ? -20.913 5.846   -13.602 1.00 22.36 ?  191 ASP A N   1 
ATOM   1481 C CA  . ASP A 1 217 ? -21.908 6.805   -13.081 1.00 22.39 ?  191 ASP A CA  1 
ATOM   1482 C C   . ASP A 1 217 ? -22.252 6.323   -11.662 1.00 22.23 ?  191 ASP A C   1 
ATOM   1483 O O   . ASP A 1 217 ? -22.978 5.322   -11.531 1.00 21.87 ?  191 ASP A O   1 
ATOM   1484 C CB  . ASP A 1 217 ? -23.077 6.844   -14.074 1.00 25.20 ?  191 ASP A CB  1 
ATOM   1485 C CG  . ASP A 1 217 ? -24.002 8.011   -13.853 1.00 29.97 ?  191 ASP A CG  1 
ATOM   1486 O OD1 . ASP A 1 217 ? -23.798 8.693   -12.825 1.00 28.37 ?  191 ASP A OD1 1 
ATOM   1487 O OD2 . ASP A 1 217 ? -24.931 8.219   -14.702 1.00 29.47 ?  191 ASP A OD2 1 
ATOM   1488 N N   . VAL A 1 218 ? -21.696 6.952   -10.629 1.00 20.90 ?  192 VAL A N   1 
ATOM   1489 C CA  . VAL A 1 218 ? -21.770 6.364   -9.261  1.00 19.76 ?  192 VAL A CA  1 
ATOM   1490 C C   . VAL A 1 218 ? -23.229 6.402   -8.825  1.00 19.04 ?  192 VAL A C   1 
ATOM   1491 O O   . VAL A 1 218 ? -23.808 7.472   -8.861  1.00 22.13 ?  192 VAL A O   1 
ATOM   1492 C CB  . VAL A 1 218 ? -20.870 7.078   -8.256  1.00 19.96 ?  192 VAL A CB  1 
ATOM   1493 C CG1 . VAL A 1 218 ? -21.024 6.419   -6.892  1.00 20.62 ?  192 VAL A CG1 1 
ATOM   1494 C CG2 . VAL A 1 218 ? -19.392 7.039   -8.720  1.00 20.48 ?  192 VAL A CG2 1 
ATOM   1495 N N   . PRO A 1 219 ? -23.844 5.287   -8.400  1.00 19.88 ?  193 PRO A N   1 
ATOM   1496 C CA  . PRO A 1 219 ? -25.230 5.305   -7.933  1.00 22.73 ?  193 PRO A CA  1 
ATOM   1497 C C   . PRO A 1 219 ? -25.353 6.248   -6.717  1.00 22.07 ?  193 PRO A C   1 
ATOM   1498 O O   . PRO A 1 219 ? -24.401 6.429   -5.972  1.00 21.16 ?  193 PRO A O   1 
ATOM   1499 C CB  . PRO A 1 219 ? -25.521 3.845   -7.539  1.00 22.60 ?  193 PRO A CB  1 
ATOM   1500 C CG  . PRO A 1 219 ? -24.536 3.051   -8.383  1.00 22.96 ?  193 PRO A CG  1 
ATOM   1501 C CD  . PRO A 1 219 ? -23.291 3.921   -8.396  1.00 22.69 ?  193 PRO A CD  1 
ATOM   1502 N N   . GLU A 1 220 ? -26.530 6.841   -6.557  1.00 24.94 ?  194 GLU A N   1 
ATOM   1503 C CA  . GLU A 1 220 ? -26.904 7.650   -5.360  1.00 25.70 ?  194 GLU A CA  1 
ATOM   1504 C C   . GLU A 1 220 ? -26.593 6.879   -4.094  1.00 24.99 ?  194 GLU A C   1 
ATOM   1505 O O   . GLU A 1 220 ? -26.023 7.462   -3.193  1.00 26.73 ?  194 GLU A O   1 
ATOM   1506 C CB  . GLU A 1 220 ? -28.398 7.993   -5.370  1.00 32.42 ?  194 GLU A CB  1 
ATOM   1507 C CG  . GLU A 1 220 ? -28.707 9.255   -6.128  1.00 41.50 ?  194 GLU A CG  1 
ATOM   1508 C CD  . GLU A 1 220 ? -28.192 10.508  -5.459  1.00 50.78 ?  194 GLU A CD  1 
ATOM   1509 O OE1 . GLU A 1 220 ? -28.113 10.521  -4.210  1.00 52.66 ?  194 GLU A OE1 1 
ATOM   1510 O OE2 . GLU A 1 220 ? -27.859 11.445  -6.194  1.00 56.75 ?  194 GLU A OE2 1 
ATOM   1511 N N   . ALA A 1 221 ? -26.854 5.582   -4.056  1.00 27.07 ?  195 ALA A N   1 
ATOM   1512 C CA  . ALA A 1 221 ? -26.720 4.787   -2.818  1.00 32.49 ?  195 ALA A CA  1 
ATOM   1513 C C   . ALA A 1 221 ? -25.240 4.565   -2.477  1.00 32.61 ?  195 ALA A C   1 
ATOM   1514 O O   . ALA A 1 221 ? -24.961 4.164   -1.340  1.00 33.90 ?  195 ALA A O   1 
ATOM   1515 C CB  . ALA A 1 221 ? -27.458 3.481   -2.965  1.00 34.24 ?  195 ALA A CB  1 
ATOM   1516 N N   . ALA A 1 222 ? -24.325 4.747   -3.429  1.00 28.20 ?  196 ALA A N   1 
ATOM   1517 C CA  . ALA A 1 222 ? -22.871 4.548   -3.214  1.00 25.66 ?  196 ALA A CA  1 
ATOM   1518 C C   . ALA A 1 222 ? -22.128 5.885   -3.077  1.00 25.93 ?  196 ALA A C   1 
ATOM   1519 O O   . ALA A 1 222 ? -20.906 5.813   -2.842  1.00 26.29 ?  196 ALA A O   1 
ATOM   1520 C CB  . ALA A 1 222 ? -22.275 3.711   -4.297  1.00 25.80 ?  196 ALA A CB  1 
ATOM   1521 N N   . LEU A 1 223 ? -22.799 7.044   -3.138  1.00 25.77 ?  197 LEU A N   1 
ATOM   1522 C CA  . LEU A 1 223 ? -22.123 8.373   -3.134  1.00 29.18 ?  197 LEU A CA  1 
ATOM   1523 C C   . LEU A 1 223 ? -21.353 8.611   -1.837  1.00 28.29 ?  197 LEU A C   1 
ATOM   1524 O O   . LEU A 1 223 ? -20.331 9.318   -1.909  1.00 24.75 ?  197 LEU A O   1 
ATOM   1525 C CB  . LEU A 1 223 ? -23.129 9.508   -3.351  1.00 30.62 ?  197 LEU A CB  1 
ATOM   1526 C CG  . LEU A 1 223 ? -23.453 9.805   -4.804  1.00 34.10 ?  197 LEU A CG  1 
ATOM   1527 C CD1 . LEU A 1 223 ? -24.437 10.978  -4.913  1.00 36.17 ?  197 LEU A CD1 1 
ATOM   1528 C CD2 . LEU A 1 223 ? -22.168 10.072  -5.593  1.00 35.36 ?  197 LEU A CD2 1 
ATOM   1529 N N   . ALA A 1 224 ? -21.749 7.979   -0.731  1.00 26.30 ?  198 ALA A N   1 
ATOM   1530 C CA  . ALA A 1 224 ? -21.099 8.138   0.591   1.00 25.36 ?  198 ALA A CA  1 
ATOM   1531 C C   . ALA A 1 224 ? -19.656 7.599   0.528   1.00 27.26 ?  198 ALA A C   1 
ATOM   1532 O O   . ALA A 1 224 ? -18.806 8.067   1.335   1.00 25.53 ?  198 ALA A O   1 
ATOM   1533 C CB  . ALA A 1 224 ? -21.883 7.421   1.656   1.00 28.41 ?  198 ALA A CB  1 
ATOM   1534 N N   . GLN A 1 225 ? -19.384 6.651   -0.391  1.00 22.38 ?  199 GLN A N   1 
ATOM   1535 C CA  . GLN A 1 225 ? -18.039 6.037   -0.552  1.00 24.00 ?  199 GLN A CA  1 
ATOM   1536 C C   . GLN A 1 225 ? -17.125 6.866   -1.467  1.00 23.99 ?  199 GLN A C   1 
ATOM   1537 O O   . GLN A 1 225 ? -15.914 6.594   -1.470  1.00 23.56 ?  199 GLN A O   1 
ATOM   1538 C CB  . GLN A 1 225 ? -18.201 4.620   -1.092  1.00 26.94 ?  199 GLN A CB  1 
ATOM   1539 C CG  . GLN A 1 225 ? -18.981 3.708   -0.156  1.00 30.83 ?  199 GLN A CG  1 
ATOM   1540 C CD  . GLN A 1 225 ? -18.073 3.040   0.843   1.00 34.59 ?  199 GLN A CD  1 
ATOM   1541 O OE1 . GLN A 1 225 ? -18.274 1.882   1.197   1.00 47.51 ?  199 GLN A OE1 1 
ATOM   1542 N NE2 . GLN A 1 225 ? -17.007 3.713   1.245   1.00 34.15 ?  199 GLN A NE2 1 
ATOM   1543 N N   . TYR A 1 226 ? -17.633 7.868   -2.178  1.00 22.42 ?  200 TYR A N   1 
ATOM   1544 C CA  . TYR A 1 226 ? -16.875 8.609   -3.218  1.00 21.50 ?  200 TYR A CA  1 
ATOM   1545 C C   . TYR A 1 226 ? -15.990 9.629   -2.516  1.00 20.53 ?  200 TYR A C   1 
ATOM   1546 O O   . TYR A 1 226 ? -16.492 10.624  -1.952  1.00 19.25 ?  200 TYR A O   1 
ATOM   1547 C CB  . TYR A 1 226 ? -17.832 9.277   -4.196  1.00 22.99 ?  200 TYR A CB  1 
ATOM   1548 C CG  . TYR A 1 226 ? -17.282 9.803   -5.494  1.00 22.42 ?  200 TYR A CG  1 
ATOM   1549 C CD1 . TYR A 1 226 ? -15.933 10.053  -5.728  1.00 23.11 ?  200 TYR A CD1 1 
ATOM   1550 C CD2 . TYR A 1 226 ? -18.148 10.035  -6.532  1.00 21.92 ?  200 TYR A CD2 1 
ATOM   1551 C CE1 . TYR A 1 226 ? -15.505 10.570  -6.955  1.00 22.91 ?  200 TYR A CE1 1 
ATOM   1552 C CE2 . TYR A 1 226 ? -17.748 10.552  -7.746  1.00 21.59 ?  200 TYR A CE2 1 
ATOM   1553 C CZ  . TYR A 1 226 ? -16.403 10.805  -7.972  1.00 20.52 ?  200 TYR A CZ  1 
ATOM   1554 O OH  . TYR A 1 226 ? -16.059 11.328  -9.183  1.00 20.84 ?  200 TYR A OH  1 
ATOM   1555 N N   . ALA A 1 227 ? -14.687 9.426   -2.608  1.00 20.65 ?  201 ALA A N   1 
ATOM   1556 C CA  . ALA A 1 227 ? -13.716 10.349  -2.029  1.00 19.25 ?  201 ALA A CA  1 
ATOM   1557 C C   . ALA A 1 227 ? -13.842 11.730  -2.698  1.00 20.51 ?  201 ALA A C   1 
ATOM   1558 O O   . ALA A 1 227 ? -14.271 11.854  -3.855  1.00 20.43 ?  201 ALA A O   1 
ATOM   1559 C CB  . ALA A 1 227 ? -12.324 9.756   -2.145  1.00 17.88 ?  201 ALA A CB  1 
ATOM   1560 N N   . GLN A 1 228 ? -13.504 12.779  -1.940  1.00 20.48 ?  202 GLN A N   1 
ATOM   1561 C CA  . GLN A 1 228 ? -13.277 14.131  -2.478  1.00 21.03 ?  202 GLN A CA  1 
ATOM   1562 C C   . GLN A 1 228 ? -11.896 14.173  -3.145  1.00 19.72 ?  202 GLN A C   1 
ATOM   1563 O O   . GLN A 1 228 ? -10.984 13.579  -2.616  1.00 19.97 ?  202 GLN A O   1 
ATOM   1564 C CB  . GLN A 1 228 ? -13.388 15.153  -1.350  1.00 21.00 ?  202 GLN A CB  1 
ATOM   1565 C CG  . GLN A 1 228 ? -13.320 16.584  -1.839  1.00 21.78 ?  202 GLN A CG  1 
ATOM   1566 C CD  . GLN A 1 228 ? -14.491 16.912  -2.710  1.00 21.64 ?  202 GLN A CD  1 
ATOM   1567 O OE1 . GLN A 1 228 ? -15.614 17.129  -2.231  1.00 28.29 ?  202 GLN A OE1 1 
ATOM   1568 N NE2 . GLN A 1 228 ? -14.270 16.916  -4.012  1.00 21.35 ?  202 GLN A NE2 1 
ATOM   1569 N N   . GLY A 1 229 ? -11.801 14.780  -4.335  1.00 20.00 ?  203 GLY A N   1 
ATOM   1570 C CA  . GLY A 1 229 ? -10.503 15.088  -4.940  1.00 21.16 ?  203 GLY A CA  1 
ATOM   1571 C C   . GLY A 1 229 ? -10.029 16.444  -4.477  1.00 21.22 ?  203 GLY A C   1 
ATOM   1572 O O   . GLY A 1 229 ? -10.863 17.293  -4.275  1.00 21.71 ?  203 GLY A O   1 
ATOM   1573 N N   . TYR A 1 230 ? -8.729  16.657  -4.400  1.00 22.19 ?  204 TYR A N   1 
ATOM   1574 C CA  . TYR A 1 230 ? -8.138  17.964  -4.005  1.00 24.70 ?  204 TYR A CA  1 
ATOM   1575 C C   . TYR A 1 230 ? -7.113  18.422  -5.047  1.00 28.13 ?  204 TYR A C   1 
ATOM   1576 O O   . TYR A 1 230 ? -6.248  17.623  -5.393  1.00 25.08 ?  204 TYR A O   1 
ATOM   1577 C CB  . TYR A 1 230 ? -7.544  17.814  -2.614  1.00 24.63 ?  204 TYR A CB  1 
ATOM   1578 C CG  . TYR A 1 230 ? -8.589  17.533  -1.568  1.00 23.76 ?  204 TYR A CG  1 
ATOM   1579 C CD1 . TYR A 1 230 ? -9.312  18.579  -0.983  1.00 23.51 ?  204 TYR A CD1 1 
ATOM   1580 C CD2 . TYR A 1 230 ? -8.869  16.234  -1.186  1.00 22.96 ?  204 TYR A CD2 1 
ATOM   1581 C CE1 . TYR A 1 230 ? -10.283 18.324  -0.037  1.00 25.83 ?  204 TYR A CE1 1 
ATOM   1582 C CE2 . TYR A 1 230 ? -9.832  15.954  -0.241  1.00 24.00 ?  204 TYR A CE2 1 
ATOM   1583 C CZ  . TYR A 1 230 ? -10.542 17.006  0.336   1.00 24.86 ?  204 TYR A CZ  1 
ATOM   1584 O OH  . TYR A 1 230 ? -11.513 16.750  1.226   1.00 22.91 ?  204 TYR A OH  1 
ATOM   1585 N N   . GLY A 1 231 ? -7.209  19.683  -5.496  1.00 30.40 ?  205 GLY A N   1 
ATOM   1586 C CA  . GLY A 1 231 ? -6.182  20.349  -6.320  1.00 35.04 ?  205 GLY A CA  1 
ATOM   1587 C C   . GLY A 1 231 ? -5.490  21.496  -5.595  1.00 40.61 ?  205 GLY A C   1 
ATOM   1588 O O   . GLY A 1 231 ? -5.487  21.510  -4.339  1.00 36.58 ?  205 GLY A O   1 
ATOM   1589 N N   . LYS A 1 232 ? -4.978  22.467  -6.367  1.00 40.97 ?  206 LYS A N   1 
ATOM   1590 C CA  . LYS A 1 232 ? -4.277  23.679  -5.861  1.00 47.73 ?  206 LYS A CA  1 
ATOM   1591 C C   . LYS A 1 232 ? -5.157  24.415  -4.843  1.00 49.19 ?  206 LYS A C   1 
ATOM   1592 O O   . LYS A 1 232 ? -6.343  24.677  -5.156  1.00 52.52 ?  206 LYS A O   1 
ATOM   1593 C CB  . LYS A 1 232 ? -3.955  24.613  -7.028  1.00 53.05 ?  206 LYS A CB  1 
ATOM   1594 C CG  . LYS A 1 232 ? -3.348  25.954  -6.643  1.00 58.15 ?  206 LYS A CG  1 
ATOM   1595 C CD  . LYS A 1 232 ? -3.587  27.019  -7.694  1.00 63.80 ?  206 LYS A CD  1 
ATOM   1596 C CE  . LYS A 1 232 ? -2.701  28.233  -7.518  1.00 61.75 ?  206 LYS A CE  1 
ATOM   1597 N NZ  . LYS A 1 232 ? -1.304  27.917  -7.905  1.00 61.81 ?  206 LYS A NZ  1 
ATOM   1598 N N   . ASP A 1 233 ? -4.586  24.739  -3.681  1.00 50.75 ?  207 ASP A N   1 
ATOM   1599 C CA  . ASP A 1 233 ? -5.257  25.412  -2.535  1.00 52.26 ?  207 ASP A CA  1 
ATOM   1600 C C   . ASP A 1 233 ? -6.331  24.485  -1.965  1.00 49.23 ?  207 ASP A C   1 
ATOM   1601 O O   . ASP A 1 233 ? -7.283  24.994  -1.314  1.00 49.95 ?  207 ASP A O   1 
ATOM   1602 C CB  . ASP A 1 233 ? -5.861  26.766  -2.929  1.00 62.20 ?  207 ASP A CB  1 
ATOM   1603 C CG  . ASP A 1 233 ? -4.840  27.819  -3.337  1.00 65.99 ?  207 ASP A CG  1 
ATOM   1604 O OD1 . ASP A 1 233 ? -3.741  27.857  -2.717  1.00 65.63 ?  207 ASP A OD1 1 
ATOM   1605 O OD2 . ASP A 1 233 ? -5.159  28.603  -4.266  1.00 67.53 ?  207 ASP A OD2 1 
ATOM   1606 N N   . ASP A 1 234 ? -6.189  23.177  -2.203  1.00 42.44 ?  208 ASP A N   1 
ATOM   1607 C CA  . ASP A 1 234 ? -7.148  22.147  -1.745  1.00 40.19 ?  208 ASP A CA  1 
ATOM   1608 C C   . ASP A 1 234 ? -8.545  22.430  -2.306  1.00 33.21 ?  208 ASP A C   1 
ATOM   1609 O O   . ASP A 1 234 ? -9.515  22.030  -1.659  1.00 32.17 ?  208 ASP A O   1 
ATOM   1610 C CB  . ASP A 1 234 ? -7.142  22.033  -0.217  1.00 42.50 ?  208 ASP A CB  1 
ATOM   1611 C CG  . ASP A 1 234 ? -6.010  21.154  0.269   1.00 44.93 ?  208 ASP A CG  1 
ATOM   1612 O OD1 . ASP A 1 234 ? -5.078  20.880  -0.543  1.00 41.60 ?  208 ASP A OD1 1 
ATOM   1613 O OD2 . ASP A 1 234 ? -6.075  20.733  1.434   1.00 53.27 ?  208 ASP A OD2 1 
ATOM   1614 N N   . ARG A 1 235 ? -8.657  22.996  -3.506  1.00 33.34 ?  209 ARG A N   1 
ATOM   1615 C CA  . ARG A 1 235 ? -9.998  23.147  -4.123  1.00 35.21 ?  209 ARG A CA  1 
ATOM   1616 C C   . ARG A 1 235 ? -10.534 21.744  -4.412  1.00 32.23 ?  209 ARG A C   1 
ATOM   1617 O O   . ARG A 1 235 ? -9.791  20.825  -4.791  1.00 26.92 ?  209 ARG A O   1 
ATOM   1618 C CB  . ARG A 1 235 ? -9.996  24.071  -5.343  1.00 42.20 ?  209 ARG A CB  1 
ATOM   1619 C CG  . ARG A 1 235 ? -9.207  23.580  -6.543  1.00 50.54 ?  209 ARG A CG  1 
ATOM   1620 C CD  . ARG A 1 235 ? -9.389  24.550  -7.702  1.00 59.16 ?  209 ARG A CD  1 
ATOM   1621 N NE  . ARG A 1 235 ? -10.761 24.471  -8.200  1.00 63.20 ?  209 ARG A NE  1 
ATOM   1622 C CZ  . ARG A 1 235 ? -11.128 24.534  -9.480  1.00 71.17 ?  209 ARG A CZ  1 
ATOM   1623 N NH1 . ARG A 1 235 ? -10.229 24.689  -10.443 1.00 69.66 ?  209 ARG A NH1 1 
ATOM   1624 N NH2 . ARG A 1 235 ? -12.410 24.419  -9.790  1.00 71.49 ?  209 ARG A NH2 1 
ATOM   1625 N N   . PRO A 1 236 ? -11.823 21.518  -4.099  1.00 29.47 ?  210 PRO A N   1 
ATOM   1626 C CA  . PRO A 1 236 ? -12.447 20.215  -4.264  1.00 28.53 ?  210 PRO A CA  1 
ATOM   1627 C C   . PRO A 1 236 ? -12.741 19.965  -5.744  1.00 29.14 ?  210 PRO A C   1 
ATOM   1628 O O   . PRO A 1 236 ? -13.271 20.838  -6.412  1.00 27.96 ?  210 PRO A O   1 
ATOM   1629 C CB  . PRO A 1 236 ? -13.765 20.343  -3.491  1.00 30.90 ?  210 PRO A CB  1 
ATOM   1630 C CG  . PRO A 1 236 ? -14.086 21.822  -3.596  1.00 31.15 ?  210 PRO A CG  1 
ATOM   1631 C CD  . PRO A 1 236 ? -12.735 22.492  -3.470  1.00 30.81 ?  210 PRO A CD  1 
ATOM   1632 N N   . LEU A 1 237 ? -12.414 18.766  -6.215  1.00 24.52 ?  211 LEU A N   1 
ATOM   1633 C CA  . LEU A 1 237 ? -12.443 18.459  -7.665  1.00 26.91 ?  211 LEU A CA  1 
ATOM   1634 C C   . LEU A 1 237 ? -12.982 17.042  -7.829  1.00 26.78 ?  211 LEU A C   1 
ATOM   1635 O O   . LEU A 1 237 ? -12.299 16.137  -7.428  1.00 26.10 ?  211 LEU A O   1 
ATOM   1636 C CB  . LEU A 1 237 ? -11.028 18.609  -8.231  1.00 28.70 ?  211 LEU A CB  1 
ATOM   1637 C CG  . LEU A 1 237 ? -10.527 20.055  -8.247  1.00 29.85 ?  211 LEU A CG  1 
ATOM   1638 C CD1 . LEU A 1 237 ? -9.026  20.111  -8.485  1.00 29.61 ?  211 LEU A CD1 1 
ATOM   1639 C CD2 . LEU A 1 237 ? -11.285 20.894  -9.257  1.00 32.47 ?  211 LEU A CD2 1 
ATOM   1640 N N   . ARG A 1 238 ? -14.201 16.896  -8.324  1.00 26.12 ?  212 ARG A N   1 
ATOM   1641 C CA  . ARG A 1 238 ? -14.669 15.587  -8.837  1.00 26.27 ?  212 ARG A CA  1 
ATOM   1642 C C   . ARG A 1 238 ? -14.862 15.805  -10.334 1.00 26.28 ?  212 ARG A C   1 
ATOM   1643 O O   . ARG A 1 238 ? -15.238 16.907  -10.732 1.00 24.65 ?  212 ARG A O   1 
ATOM   1644 C CB  . ARG A 1 238 ? -15.917 15.091  -8.111  1.00 27.40 ?  212 ARG A CB  1 
ATOM   1645 C CG  . ARG A 1 238 ? -15.652 14.581  -6.705  1.00 25.03 ?  212 ARG A CG  1 
ATOM   1646 C CD  . ARG A 1 238 ? -16.877 13.966  -6.099  1.00 25.01 ?  212 ARG A CD  1 
ATOM   1647 N NE  . ARG A 1 238 ? -16.683 13.481  -4.739  1.00 25.24 ?  212 ARG A NE  1 
ATOM   1648 C CZ  . ARG A 1 238 ? -17.080 14.091  -3.618  1.00 28.07 ?  212 ARG A CZ  1 
ATOM   1649 N NH1 . ARG A 1 238 ? -17.676 15.273  -3.660  1.00 28.88 ?  212 ARG A NH1 1 
ATOM   1650 N NH2 . ARG A 1 238 ? -16.876 13.505  -2.449  1.00 25.38 ?  212 ARG A NH2 1 
ATOM   1651 N N   . VAL A 1 239 ? -14.609 14.780  -11.146 1.00 22.38 ?  213 VAL A N   1 
ATOM   1652 C CA  . VAL A 1 239 ? -14.566 14.955  -12.619 1.00 23.01 ?  213 VAL A CA  1 
ATOM   1653 C C   . VAL A 1 239 ? -15.972 15.305  -13.136 1.00 23.13 ?  213 VAL A C   1 
ATOM   1654 O O   . VAL A 1 239 ? -16.969 14.666  -12.727 1.00 25.07 ?  213 VAL A O   1 
ATOM   1655 C CB  . VAL A 1 239 ? -13.903 13.727  -13.299 1.00 23.13 ?  213 VAL A CB  1 
ATOM   1656 C CG1 . VAL A 1 239 ? -14.694 12.441  -13.082 1.00 22.74 ?  213 VAL A CG1 1 
ATOM   1657 C CG2 . VAL A 1 239 ? -13.672 13.991  -14.775 1.00 25.37 ?  213 VAL A CG2 1 
ATOM   1658 N N   . GLY A 1 240 ? -16.043 16.346  -13.969 1.00 25.22 ?  214 GLY A N   1 
ATOM   1659 C CA  . GLY A 1 240 ? -17.240 16.751  -14.719 1.00 25.04 ?  214 GLY A CA  1 
ATOM   1660 C C   . GLY A 1 240 ? -17.371 16.013  -16.056 1.00 26.54 ?  214 GLY A C   1 
ATOM   1661 O O   . GLY A 1 240 ? -16.468 15.289  -16.512 1.00 25.41 ?  214 GLY A O   1 
ATOM   1662 N N   . PRO A 1 241 ? -18.538 16.139  -16.703 1.00 27.22 ?  215 PRO A N   1 
ATOM   1663 C CA  . PRO A 1 241 ? -18.806 15.460  -17.971 1.00 26.60 ?  215 PRO A CA  1 
ATOM   1664 C C   . PRO A 1 241 ? -17.892 15.970  -19.080 1.00 23.96 ?  215 PRO A C   1 
ATOM   1665 O O   . PRO A 1 241 ? -17.526 17.127  -19.086 1.00 26.96 ?  215 PRO A O   1 
ATOM   1666 C CB  . PRO A 1 241 ? -20.302 15.741  -18.264 1.00 28.48 ?  215 PRO A CB  1 
ATOM   1667 C CG  . PRO A 1 241 ? -20.632 16.949  -17.405 1.00 33.33 ?  215 PRO A CG  1 
ATOM   1668 C CD  . PRO A 1 241 ? -19.707 16.895  -16.214 1.00 30.39 ?  215 PRO A CD  1 
ATOM   1669 N N   . GLY A 1 242 ? -17.550 15.072  -19.999 1.00 21.78 ?  216 GLY A N   1 
ATOM   1670 C CA  . GLY A 1 242 ? -16.763 15.408  -21.182 1.00 22.38 ?  216 GLY A CA  1 
ATOM   1671 C C   . GLY A 1 242 ? -16.968 14.374  -22.272 1.00 21.30 ?  216 GLY A C   1 
ATOM   1672 O O   . GLY A 1 242 ? -17.403 13.250  -21.996 1.00 19.85 ?  216 GLY A O   1 
ATOM   1673 N N   . PRO A 1 243 ? -16.656 14.769  -23.525 1.00 19.70 ?  217 PRO A N   1 
ATOM   1674 C CA  . PRO A 1 243 ? -16.771 13.888  -24.675 1.00 20.77 ?  217 PRO A CA  1 
ATOM   1675 C C   . PRO A 1 243 ? -15.923 12.623  -24.525 1.00 21.14 ?  217 PRO A C   1 
ATOM   1676 O O   . PRO A 1 243 ? -14.769 12.730  -24.224 1.00 20.53 ?  217 PRO A O   1 
ATOM   1677 C CB  . PRO A 1 243 ? -16.263 14.747  -25.824 1.00 22.91 ?  217 PRO A CB  1 
ATOM   1678 C CG  . PRO A 1 243 ? -15.422 15.819  -25.183 1.00 23.34 ?  217 PRO A CG  1 
ATOM   1679 C CD  . PRO A 1 243 ? -16.132 16.100  -23.883 1.00 22.67 ?  217 PRO A CD  1 
ATOM   1680 N N   . LEU A 1 244 ? -16.574 11.478  -24.688 1.00 21.73 ?  218 LEU A N   1 
ATOM   1681 C CA  . LEU A 1 244 ? -16.040 10.105  -24.506 1.00 21.54 ?  218 LEU A CA  1 
ATOM   1682 C C   . LEU A 1 244 ? -15.343 9.998   -23.148 1.00 19.77 ?  218 LEU A C   1 
ATOM   1683 O O   . LEU A 1 244 ? -14.279 9.370   -23.057 1.00 20.87 ?  218 LEU A O   1 
ATOM   1684 C CB  . LEU A 1 244 ? -15.129 9.765   -25.691 1.00 22.94 ?  218 LEU A CB  1 
ATOM   1685 C CG  . LEU A 1 244 ? -15.770 9.968   -27.065 1.00 23.31 ?  218 LEU A CG  1 
ATOM   1686 C CD1 . LEU A 1 244 ? -14.846 9.475   -28.164 1.00 24.42 ?  218 LEU A CD1 1 
ATOM   1687 C CD2 . LEU A 1 244 ? -17.146 9.283   -27.153 1.00 24.41 ?  218 LEU A CD2 1 
ATOM   1688 N N   . ASP A 1 245 ? -15.886 10.651  -22.143 1.00 18.34 ?  219 ASP A N   1 
ATOM   1689 C CA  . ASP A 1 245 ? -15.330 10.569  -20.779 1.00 20.04 ?  219 ASP A CA  1 
ATOM   1690 C C   . ASP A 1 245 ? -15.268 9.099   -20.352 1.00 19.02 ?  219 ASP A C   1 
ATOM   1691 O O   . ASP A 1 245 ? -14.265 8.693   -19.780 1.00 18.68 ?  219 ASP A O   1 
ATOM   1692 C CB  . ASP A 1 245 ? -16.039 11.486  -19.767 1.00 20.21 ?  219 ASP A CB  1 
ATOM   1693 C CG  . ASP A 1 245 ? -17.562 11.438  -19.686 1.00 20.59 ?  219 ASP A CG  1 
ATOM   1694 O OD1 . ASP A 1 245 ? -18.157 10.556  -20.271 1.00 20.59 ?  219 ASP A OD1 1 
ATOM   1695 O OD2 . ASP A 1 245 ? -18.113 12.283  -18.985 1.00 23.79 ?  219 ASP A OD2 1 
ATOM   1696 N N   . ALA A 1 246 ? -16.349 8.341   -20.547 1.00 18.12 ?  220 ALA A N   1 
ATOM   1697 C CA  . ALA A 1 246 ? -16.444 6.968   -19.999 1.00 18.96 ?  220 ALA A CA  1 
ATOM   1698 C C   . ALA A 1 246 ? -15.243 6.166   -20.540 1.00 18.84 ?  220 ALA A C   1 
ATOM   1699 O O   . ALA A 1 246 ? -14.649 5.326   -19.803 1.00 18.53 ?  220 ALA A O   1 
ATOM   1700 C CB  . ALA A 1 246 ? -17.771 6.330   -20.384 1.00 20.50 ?  220 ALA A CB  1 
ATOM   1701 N N   . GLU A 1 247 ? -14.983 6.339   -21.836 1.00 17.07 ?  221 GLU A N   1 
ATOM   1702 C CA  . GLU A 1 247 ? -13.971 5.546   -22.580 1.00 19.07 ?  221 GLU A CA  1 
ATOM   1703 C C   . GLU A 1 247 ? -12.578 5.947   -22.076 1.00 18.89 ?  221 GLU A C   1 
ATOM   1704 O O   . GLU A 1 247 ? -11.692 5.071   -22.025 1.00 18.05 ?  221 GLU A O   1 
ATOM   1705 C CB  . GLU A 1 247 ? -14.076 5.773   -24.100 1.00 18.59 ?  221 GLU A CB  1 
ATOM   1706 C CG  . GLU A 1 247 ? -15.314 5.140   -24.714 1.00 20.18 ?  221 GLU A CG  1 
ATOM   1707 C CD  . GLU A 1 247 ? -16.582 5.968   -24.745 1.00 22.17 ?  221 GLU A CD  1 
ATOM   1708 O OE1 . GLU A 1 247 ? -16.685 6.989   -24.021 1.00 21.35 ?  221 GLU A OE1 1 
ATOM   1709 O OE2 . GLU A 1 247 ? -17.453 5.631   -25.573 1.00 24.96 ?  221 GLU A OE2 1 
ATOM   1710 N N   . GLY A 1 248 ? -12.363 7.244   -21.852 1.00 18.82 ?  222 GLY A N   1 
ATOM   1711 C CA  . GLY A 1 248 ? -10.986 7.751   -21.643 1.00 18.20 ?  222 GLY A CA  1 
ATOM   1712 C C   . GLY A 1 248 ? -10.581 7.758   -20.170 1.00 20.57 ?  222 GLY A C   1 
ATOM   1713 O O   . GLY A 1 248 ? -9.394  7.454   -19.848 1.00 19.46 ?  222 GLY A O   1 
ATOM   1714 N N   . TYR A 1 249 ? -11.507 8.124   -19.292 1.00 20.01 ?  223 TYR A N   1 
ATOM   1715 C CA  . TYR A 1 249 ? -11.139 8.513   -17.911 1.00 21.12 ?  223 TYR A CA  1 
ATOM   1716 C C   . TYR A 1 249 ? -12.302 8.451   -16.925 1.00 20.22 ?  223 TYR A C   1 
ATOM   1717 O O   . TYR A 1 249 ? -12.135 8.972   -15.785 1.00 24.41 ?  223 TYR A O   1 
ATOM   1718 C CB  . TYR A 1 249 ? -10.477 9.889   -17.965 1.00 20.78 ?  223 TYR A CB  1 
ATOM   1719 C CG  . TYR A 1 249 ? -11.331 10.995  -18.527 1.00 21.55 ?  223 TYR A CG  1 
ATOM   1720 C CD1 . TYR A 1 249 ? -12.230 11.679  -17.727 1.00 22.83 ?  223 TYR A CD1 1 
ATOM   1721 C CD2 . TYR A 1 249 ? -11.208 11.395  -19.848 1.00 21.29 ?  223 TYR A CD2 1 
ATOM   1722 C CE1 . TYR A 1 249 ? -13.039 12.686  -18.235 1.00 24.11 ?  223 TYR A CE1 1 
ATOM   1723 C CE2 . TYR A 1 249 ? -11.983 12.426  -20.355 1.00 23.85 ?  223 TYR A CE2 1 
ATOM   1724 C CZ  . TYR A 1 249 ? -12.894 13.081  -19.554 1.00 23.96 ?  223 TYR A CZ  1 
ATOM   1725 O OH  . TYR A 1 249 ? -13.658 14.093  -20.101 1.00 23.36 ?  223 TYR A OH  1 
ATOM   1726 N N   . GLY A 1 250 ? -13.343 7.678   -17.201 1.00 21.98 ?  224 GLY A N   1 
ATOM   1727 C CA  . GLY A 1 250 ? -14.626 7.806   -16.474 1.00 25.10 ?  224 GLY A CA  1 
ATOM   1728 C C   . GLY A 1 250 ? -14.773 6.888   -15.247 1.00 22.23 ?  224 GLY A C   1 
ATOM   1729 O O   . GLY A 1 250 ? -15.795 6.972   -14.558 1.00 21.00 ?  224 GLY A O   1 
ATOM   1730 N N   . VAL A 1 251 ? -13.880 5.938   -15.032 1.00 18.10 ?  225 VAL A N   1 
ATOM   1731 C CA  . VAL A 1 251 ? -14.129 4.909   -13.985 1.00 17.78 ?  225 VAL A CA  1 
ATOM   1732 C C   . VAL A 1 251 ? -13.886 5.490   -12.576 1.00 16.09 ?  225 VAL A C   1 
ATOM   1733 O O   . VAL A 1 251 ? -12.810 6.051   -12.328 1.00 16.55 ?  225 VAL A O   1 
ATOM   1734 C CB  . VAL A 1 251 ? -13.329 3.624   -14.214 1.00 16.68 ?  225 VAL A CB  1 
ATOM   1735 C CG1 . VAL A 1 251 ? -13.537 2.615   -13.084 1.00 18.20 ?  225 VAL A CG1 1 
ATOM   1736 C CG2 . VAL A 1 251 ? -13.664 3.000   -15.574 1.00 20.43 ?  225 VAL A CG2 1 
ATOM   1737 N N   . LYS A 1 252 ? -14.783 5.161   -11.663 1.00 16.03 ?  226 LYS A N   1 
ATOM   1738 C CA  . LYS A 1 252 ? -14.583 5.270   -10.196 1.00 17.01 ?  226 LYS A CA  1 
ATOM   1739 C C   . LYS A 1 252 ? -14.690 3.873   -9.586  1.00 19.08 ?  226 LYS A C   1 
ATOM   1740 O O   . LYS A 1 252 ? -15.656 3.140   -9.843  1.00 18.73 ?  226 LYS A O   1 
ATOM   1741 C CB  . LYS A 1 252 ? -15.555 6.265   -9.560  1.00 18.59 ?  226 LYS A CB  1 
ATOM   1742 C CG  . LYS A 1 252 ? -15.559 7.640   -10.210 1.00 19.44 ?  226 LYS A CG  1 
ATOM   1743 C CD  . LYS A 1 252 ? -16.552 7.766   -11.300 1.00 21.25 ?  226 LYS A CD  1 
ATOM   1744 C CE  . LYS A 1 252 ? -16.339 8.986   -12.151 1.00 25.73 ?  226 LYS A CE  1 
ATOM   1745 N NZ  . LYS A 1 252 ? -17.274 9.003   -13.288 1.00 24.76 ?  226 LYS A NZ  1 
ATOM   1746 N N   . THR A 1 253 ? -13.722 3.518   -8.769  1.00 19.75 ?  227 THR A N   1 
ATOM   1747 C CA  . THR A 1 253 ? -13.650 2.179   -8.161  1.00 18.10 ?  227 THR A CA  1 
ATOM   1748 C C   . THR A 1 253 ? -12.907 2.254   -6.836  1.00 18.68 ?  227 THR A C   1 
ATOM   1749 O O   . THR A 1 253 ? -12.285 3.276   -6.531  1.00 18.87 ?  227 THR A O   1 
ATOM   1750 C CB  . THR A 1 253 ? -13.019 1.228   -9.180  1.00 18.79 ?  227 THR A CB  1 
ATOM   1751 O OG1 . THR A 1 253 ? -13.214 -0.085  -8.679  1.00 20.85 ?  227 THR A OG1 1 
ATOM   1752 C CG2 . THR A 1 253 ? -11.538 1.509   -9.331  1.00 18.60 ?  227 THR A CG2 1 
ATOM   1753 N N   . SER A 1 254 ? -12.972 1.179   -6.074  1.00 18.84 ?  228 SER A N   1 
ATOM   1754 C CA  . SER A 1 254 ? -12.276 1.026   -4.789  1.00 20.18 ?  228 SER A CA  1 
ATOM   1755 C C   . SER A 1 254 ? -10.953 0.319   -5.052  1.00 19.98 ?  228 SER A C   1 
ATOM   1756 O O   . SER A 1 254 ? -10.807 -0.320  -6.169  1.00 19.05 ?  228 SER A O   1 
ATOM   1757 C CB  . SER A 1 254 ? -13.125 0.237   -3.846  1.00 21.64 ?  228 SER A CB  1 
ATOM   1758 O OG  . SER A 1 254 ? -13.350 -1.071  -4.357  1.00 20.57 ?  228 SER A OG  1 
ATOM   1759 N N   . ALA A 1 255 ? -10.051 0.322   -4.068  1.00 19.53 ?  229 ALA A N   1 
ATOM   1760 C CA  . ALA A 1 255 ? -8.781  -0.429  -4.153  1.00 19.30 ?  229 ALA A CA  1 
ATOM   1761 C C   . ALA A 1 255 ? -9.119  -1.920  -4.214  1.00 20.03 ?  229 ALA A C   1 
ATOM   1762 O O   . ALA A 1 255 ? -8.475  -2.605  -4.994  1.00 19.23 ?  229 ALA A O   1 
ATOM   1763 C CB  . ALA A 1 255 ? -7.848  -0.107  -3.010  1.00 21.35 ?  229 ALA A CB  1 
ATOM   1764 N N   . ALA A 1 256 ? -10.118 -2.377  -3.437  1.00 20.03 ?  230 ALA A N   1 
ATOM   1765 C CA  . ALA A 1 256 ? -10.546 -3.801  -3.410  1.00 23.34 ?  230 ALA A CA  1 
ATOM   1766 C C   . ALA A 1 256 ? -10.969 -4.240  -4.823  1.00 22.69 ?  230 ALA A C   1 
ATOM   1767 O O   . ALA A 1 256 ? -10.448 -5.290  -5.305  1.00 20.53 ?  230 ALA A O   1 
ATOM   1768 C CB  . ALA A 1 256 ? -11.635 -4.021  -2.394  1.00 22.95 ?  230 ALA A CB  1 
ATOM   1769 N N   . ASP A 1 257 ? -11.870 -3.490  -5.465  1.00 20.99 ?  231 ASP A N   1 
ATOM   1770 C CA  . ASP A 1 257 ? -12.334 -3.821  -6.846  1.00 20.10 ?  231 ASP A CA  1 
ATOM   1771 C C   . ASP A 1 257 ? -11.191 -3.701  -7.847  1.00 20.05 ?  231 ASP A C   1 
ATOM   1772 O O   . ASP A 1 257 ? -11.109 -4.581  -8.750  1.00 19.29 ?  231 ASP A O   1 
ATOM   1773 C CB  . ASP A 1 257 ? -13.538 -3.019  -7.308  1.00 20.41 ?  231 ASP A CB  1 
ATOM   1774 C CG  . ASP A 1 257 ? -14.812 -3.841  -7.284  1.00 22.17 ?  231 ASP A CG  1 
ATOM   1775 O OD1 . ASP A 1 257 ? -14.884 -4.787  -6.453  1.00 22.83 ?  231 ASP A OD1 1 
ATOM   1776 O OD2 . ASP A 1 257 ? -15.738 -3.456  -8.012  1.00 22.71 ?  231 ASP A OD2 1 
ATOM   1777 N N   . LEU A 1 258 ? -10.354 -2.655  -7.786  1.00 18.99 ?  232 LEU A N   1 
ATOM   1778 C CA  . LEU A 1 258 ? -9.306  -2.523  -8.825  1.00 18.20 ?  232 LEU A CA  1 
ATOM   1779 C C   . LEU A 1 258 ? -8.326  -3.689  -8.657  1.00 17.85 ?  232 LEU A C   1 
ATOM   1780 O O   . LEU A 1 258 ? -7.859  -4.202  -9.654  1.00 18.75 ?  232 LEU A O   1 
ATOM   1781 C CB  . LEU A 1 258 ? -8.621  -1.162  -8.722  1.00 18.84 ?  232 LEU A CB  1 
ATOM   1782 C CG  . LEU A 1 258 ? -7.783  -0.745  -9.917  1.00 19.36 ?  232 LEU A CG  1 
ATOM   1783 C CD1 . LEU A 1 258 ? -8.522  -0.947  -11.225 1.00 19.10 ?  232 LEU A CD1 1 
ATOM   1784 C CD2 . LEU A 1 258 ? -7.367  0.725   -9.775  1.00 19.54 ?  232 LEU A CD2 1 
ATOM   1785 N N   . LEU A 1 259 ? -8.095  -4.181  -7.433  1.00 19.21 ?  233 LEU A N   1 
ATOM   1786 C CA  . LEU A 1 259 ? -7.204  -5.353  -7.255  1.00 18.26 ?  233 LEU A CA  1 
ATOM   1787 C C   . LEU A 1 259 ? -7.889  -6.612  -7.806  1.00 19.36 ?  233 LEU A C   1 
ATOM   1788 O O   . LEU A 1 259 ? -7.193  -7.449  -8.374  1.00 18.97 ?  233 LEU A O   1 
ATOM   1789 C CB  . LEU A 1 259 ? -6.815  -5.547  -5.788  1.00 18.28 ?  233 LEU A CB  1 
ATOM   1790 C CG  . LEU A 1 259 ? -5.688  -6.550  -5.581  1.00 19.27 ?  233 LEU A CG  1 
ATOM   1791 C CD1 . LEU A 1 259 ? -4.368  -5.999  -6.115  1.00 21.47 ?  233 LEU A CD1 1 
ATOM   1792 C CD2 . LEU A 1 259 ? -5.597  -6.982  -4.124  1.00 20.19 ?  233 LEU A CD2 1 
ATOM   1793 N N   . ARG A 1 260 ? -9.218  -6.713  -7.737  1.00 18.24 ?  234 ARG A N   1 
ATOM   1794 C CA  . ARG A 1 260 ? -9.923  -7.837  -8.398  1.00 19.40 ?  234 ARG A CA  1 
ATOM   1795 C C   . ARG A 1 260 ? -9.645  -7.826  -9.896  1.00 18.33 ?  234 ARG A C   1 
ATOM   1796 O O   . ARG A 1 260 ? -9.423  -8.911  -10.454 1.00 18.84 ?  234 ARG A O   1 
ATOM   1797 C CB  . ARG A 1 260 ? -11.438 -7.781  -8.164  1.00 20.19 ?  234 ARG A CB  1 
ATOM   1798 C CG  . ARG A 1 260 ? -11.872 -8.028  -6.727  1.00 24.45 ?  234 ARG A CG  1 
ATOM   1799 C CD  . ARG A 1 260 ? -13.387 -7.962  -6.467  1.00 29.47 ?  234 ARG A CD  1 
ATOM   1800 N NE  . ARG A 1 260 ? -13.517 -8.229  -5.034  1.00 38.34 ?  234 ARG A NE  1 
ATOM   1801 C CZ  . ARG A 1 260 ? -13.681 -7.344  -4.034  1.00 35.70 ?  234 ARG A CZ  1 
ATOM   1802 N NH1 . ARG A 1 260 ? -13.899 -6.059  -4.236  1.00 31.03 ?  234 ARG A NH1 1 
ATOM   1803 N NH2 . ARG A 1 260 ? -13.706 -7.801  -2.796  1.00 41.07 ?  234 ARG A NH2 1 
ATOM   1804 N N   . PHE A 1 261 ? -9.660  -6.638  -10.513 1.00 16.01 ?  235 PHE A N   1 
ATOM   1805 C CA  . PHE A 1 261 ? -9.404  -6.450  -11.946 1.00 15.40 ?  235 PHE A CA  1 
ATOM   1806 C C   . PHE A 1 261 ? -7.958  -6.883  -12.227 1.00 16.88 ?  235 PHE A C   1 
ATOM   1807 O O   . PHE A 1 261 ? -7.677  -7.592  -13.236 1.00 16.68 ?  235 PHE A O   1 
ATOM   1808 C CB  . PHE A 1 261 ? -9.639  -4.996  -12.300 1.00 16.10 ?  235 PHE A CB  1 
ATOM   1809 C CG  . PHE A 1 261 ? -9.419  -4.689  -13.759 1.00 16.75 ?  235 PHE A CG  1 
ATOM   1810 C CD1 . PHE A 1 261 ? -10.032 -5.451  -14.742 1.00 18.72 ?  235 PHE A CD1 1 
ATOM   1811 C CD2 . PHE A 1 261 ? -8.482  -3.740  -14.145 1.00 18.16 ?  235 PHE A CD2 1 
ATOM   1812 C CE1 . PHE A 1 261 ? -9.836  -5.162  -16.086 1.00 17.94 ?  235 PHE A CE1 1 
ATOM   1813 C CE2 . PHE A 1 261 ? -8.339  -3.420  -15.489 1.00 16.85 ?  235 PHE A CE2 1 
ATOM   1814 C CZ  . PHE A 1 261 ? -9.013  -4.117  -16.455 1.00 18.30 ?  235 PHE A CZ  1 
ATOM   1815 N N   . VAL A 1 262 ? -7.055  -6.478  -11.350 1.00 17.50 ?  236 VAL A N   1 
ATOM   1816 C CA  . VAL A 1 262 ? -5.634  -6.884  -11.493 1.00 18.62 ?  236 VAL A CA  1 
ATOM   1817 C C   . VAL A 1 262 ? -5.513  -8.409  -11.407 1.00 20.73 ?  236 VAL A C   1 
ATOM   1818 O O   . VAL A 1 262 ? -4.746  -8.948  -12.245 1.00 21.20 ?  236 VAL A O   1 
ATOM   1819 C CB  . VAL A 1 262 ? -4.692  -6.183  -10.519 1.00 19.57 ?  236 VAL A CB  1 
ATOM   1820 C CG1 . VAL A 1 262 ? -3.311  -6.836  -10.535 1.00 20.31 ?  236 VAL A CG1 1 
ATOM   1821 C CG2 . VAL A 1 262 ? -4.591  -4.709  -10.881 1.00 21.43 ?  236 VAL A CG2 1 
ATOM   1822 N N   . ASP A 1 263 ? -6.248  -9.059  -10.486 1.00 22.27 ?  237 ASP A N   1 
ATOM   1823 C CA  . ASP A 1 263 ? -6.210  -10.541 -10.325 1.00 21.67 ?  237 ASP A CA  1 
ATOM   1824 C C   . ASP A 1 263 ? -6.791  -11.240 -11.553 1.00 21.53 ?  237 ASP A C   1 
ATOM   1825 O O   . ASP A 1 263 ? -6.224  -12.283 -11.972 1.00 21.94 ?  237 ASP A O   1 
ATOM   1826 C CB  . ASP A 1 263 ? -6.871  -10.984 -9.022  1.00 24.19 ?  237 ASP A CB  1 
ATOM   1827 C CG  . ASP A 1 263 ? -5.942  -10.822 -7.830  1.00 27.37 ?  237 ASP A CG  1 
ATOM   1828 O OD1 . ASP A 1 263 ? -4.714  -10.990 -8.023  1.00 26.17 ?  237 ASP A OD1 1 
ATOM   1829 O OD2 . ASP A 1 263 ? -6.437  -10.475 -6.726  1.00 29.45 ?  237 ASP A OD2 1 
ATOM   1830 N N   . ALA A 1 264 ? -7.858  -10.690 -12.142 1.00 21.32 ?  238 ALA A N   1 
ATOM   1831 C CA  . ALA A 1 264 ? -8.387  -11.169 -13.438 1.00 20.91 ?  238 ALA A CA  1 
ATOM   1832 C C   . ALA A 1 264 ? -7.280  -11.051 -14.498 1.00 21.31 ?  238 ALA A C   1 
ATOM   1833 O O   . ALA A 1 264 ? -7.116  -11.980 -15.311 1.00 21.21 ?  238 ALA A O   1 
ATOM   1834 C CB  . ALA A 1 264 ? -9.636  -10.404 -13.807 1.00 22.68 ?  238 ALA A CB  1 
ATOM   1835 N N   . ASN A 1 265 ? -6.551  -9.925  -14.554 1.00 20.19 ?  239 ASN A N   1 
ATOM   1836 C CA  . ASN A 1 265 ? -5.433  -9.736  -15.520 1.00 19.48 ?  239 ASN A CA  1 
ATOM   1837 C C   . ASN A 1 265 ? -4.317  -10.765 -15.266 1.00 18.77 ?  239 ASN A C   1 
ATOM   1838 O O   . ASN A 1 265 ? -3.764  -11.255 -16.240 1.00 20.87 ?  239 ASN A O   1 
ATOM   1839 C CB  . ASN A 1 265 ? -4.882  -8.309  -15.481 1.00 18.83 ?  239 ASN A CB  1 
ATOM   1840 C CG  . ASN A 1 265 ? -5.638  -7.417  -16.428 1.00 19.32 ?  239 ASN A CG  1 
ATOM   1841 O OD1 . ASN A 1 265 ? -5.323  -7.341  -17.629 1.00 21.86 ?  239 ASN A OD1 1 
ATOM   1842 N ND2 . ASN A 1 265 ? -6.707  -6.809  -15.934 1.00 21.23 ?  239 ASN A ND2 1 
ATOM   1843 N N   . LEU A 1 266 ? -4.048  -11.127 -14.012 1.00 19.78 ?  240 LEU A N   1 
ATOM   1844 C CA  . LEU A 1 266 ? -2.985  -12.099 -13.665 1.00 18.68 ?  240 LEU A CA  1 
ATOM   1845 C C   . LEU A 1 266 ? -3.475  -13.527 -13.970 1.00 20.42 ?  240 LEU A C   1 
ATOM   1846 O O   . LEU A 1 266 ? -2.614  -14.409 -14.267 1.00 20.56 ?  240 LEU A O   1 
ATOM   1847 C CB  . LEU A 1 266 ? -2.611  -11.966 -12.195 1.00 20.83 ?  240 LEU A CB  1 
ATOM   1848 C CG  . LEU A 1 266 ? -1.695  -10.795 -11.851 1.00 20.34 ?  240 LEU A CG  1 
ATOM   1849 C CD1 . LEU A 1 266 ? -1.727  -10.545 -10.356 1.00 20.75 ?  240 LEU A CD1 1 
ATOM   1850 C CD2 . LEU A 1 266 ? -0.272  -11.033 -12.360 1.00 20.84 ?  240 LEU A CD2 1 
ATOM   1851 N N   . HIS A 1 267 ? -4.780  -13.776 -13.919 1.00 19.80 ?  241 HIS A N   1 
ATOM   1852 C CA  . HIS A 1 267 ? -5.364  -15.126 -14.133 1.00 21.32 ?  241 HIS A CA  1 
ATOM   1853 C C   . HIS A 1 267 ? -6.574  -15.040 -15.048 1.00 21.62 ?  241 HIS A C   1 
ATOM   1854 O O   . HIS A 1 267 ? -7.681  -15.339 -14.622 1.00 25.05 ?  241 HIS A O   1 
ATOM   1855 C CB  . HIS A 1 267 ? -5.630  -15.832 -12.781 1.00 22.14 ?  241 HIS A CB  1 
ATOM   1856 C CG  . HIS A 1 267 ? -4.366  -16.097 -12.047 1.00 22.25 ?  241 HIS A CG  1 
ATOM   1857 N ND1 . HIS A 1 267 ? -3.481  -17.089 -12.416 1.00 23.62 ?  241 HIS A ND1 1 
ATOM   1858 C CD2 . HIS A 1 267 ? -3.806  -15.433 -11.012 1.00 22.60 ?  241 HIS A CD2 1 
ATOM   1859 C CE1 . HIS A 1 267 ? -2.421  -17.012 -11.631 1.00 23.64 ?  241 HIS A CE1 1 
ATOM   1860 N NE2 . HIS A 1 267 ? -2.602  -15.982 -10.761 1.00 23.82 ?  241 HIS A NE2 1 
ATOM   1861 N N   . PRO A 1 268 ? -6.409  -14.722 -16.349 1.00 22.30 ?  242 PRO A N   1 
ATOM   1862 C CA  . PRO A 1 268 ? -7.554  -14.627 -17.245 1.00 24.86 ?  242 PRO A CA  1 
ATOM   1863 C C   . PRO A 1 268 ? -8.251  -15.996 -17.365 1.00 24.15 ?  242 PRO A C   1 
ATOM   1864 O O   . PRO A 1 268 ? -9.461  -16.011 -17.544 1.00 25.35 ?  242 PRO A O   1 
ATOM   1865 C CB  . PRO A 1 268 ? -6.983  -14.171 -18.585 1.00 24.35 ?  242 PRO A CB  1 
ATOM   1866 C CG  . PRO A 1 268 ? -5.566  -13.711 -18.279 1.00 26.17 ?  242 PRO A CG  1 
ATOM   1867 C CD  . PRO A 1 268 ? -5.135  -14.366 -16.993 1.00 24.21 ?  242 PRO A CD  1 
ATOM   1868 N N   . GLU A 1 269 ? -7.492  -17.081 -17.171 1.00 24.10 ?  243 GLU A N   1 
ATOM   1869 C CA  . GLU A 1 269 ? -8.018  -18.470 -17.324 1.00 27.13 ?  243 GLU A CA  1 
ATOM   1870 C C   . GLU A 1 269 ? -9.105  -18.780 -16.289 1.00 27.19 ?  243 GLU A C   1 
ATOM   1871 O O   . GLU A 1 269 ? -9.802  -19.794 -16.468 1.00 27.52 ?  243 GLU A O   1 
ATOM   1872 C CB  . GLU A 1 269 ? -6.881  -19.492 -17.227 1.00 26.07 ?  243 GLU A CB  1 
ATOM   1873 C CG  . GLU A 1 269 ? -6.308  -19.666 -15.818 1.00 25.66 ?  243 GLU A CG  1 
ATOM   1874 C CD  . GLU A 1 269 ? -5.287  -18.636 -15.350 1.00 22.96 ?  243 GLU A CD  1 
ATOM   1875 O OE1 . GLU A 1 269 ? -4.945  -17.713 -16.140 1.00 22.57 ?  243 GLU A OE1 1 
ATOM   1876 O OE2 . GLU A 1 269 ? -4.868  -18.751 -14.192 1.00 24.80 ?  243 GLU A OE2 1 
ATOM   1877 N N   . ARG A 1 270 ? -9.238  -18.002 -15.209 1.00 26.01 ?  244 ARG A N   1 
ATOM   1878 C CA  . ARG A 1 270 ? -10.290 -18.229 -14.190 1.00 27.92 ?  244 ARG A CA  1 
ATOM   1879 C C   . ARG A 1 270 ? -11.636 -17.672 -14.640 1.00 29.05 ?  244 ARG A C   1 
ATOM   1880 O O   . ARG A 1 270 ? -12.619 -17.967 -13.932 1.00 32.25 ?  244 ARG A O   1 
ATOM   1881 C CB  . ARG A 1 270 ? -9.917  -17.605 -12.845 1.00 29.57 ?  244 ARG A CB  1 
ATOM   1882 C CG  . ARG A 1 270 ? -8.679  -18.260 -12.250 1.00 31.53 ?  244 ARG A CG  1 
ATOM   1883 C CD  . ARG A 1 270 ? -8.269  -17.742 -10.879 1.00 31.16 ?  244 ARG A CD  1 
ATOM   1884 N NE  . ARG A 1 270 ? -6.932  -18.261 -10.553 1.00 30.07 ?  244 ARG A NE  1 
ATOM   1885 C CZ  . ARG A 1 270 ? -6.125  -17.763 -9.633  1.00 28.58 ?  244 ARG A CZ  1 
ATOM   1886 N NH1 . ARG A 1 270 ? -6.491  -16.683 -8.968  1.00 29.98 ?  244 ARG A NH1 1 
ATOM   1887 N NH2 . ARG A 1 270 ? -4.921  -18.285 -9.431  1.00 28.25 ?  244 ARG A NH2 1 
ATOM   1888 N N   . LEU A 1 271 ? -11.688 -16.873 -15.718 1.00 26.10 ?  245 LEU A N   1 
ATOM   1889 C CA  . LEU A 1 271 ? -12.941 -16.264 -16.210 1.00 28.76 ?  245 LEU A CA  1 
ATOM   1890 C C   . LEU A 1 271 ? -13.561 -17.153 -17.291 1.00 27.51 ?  245 LEU A C   1 
ATOM   1891 O O   . LEU A 1 271 ? -12.870 -17.992 -17.847 1.00 24.99 ?  245 LEU A O   1 
ATOM   1892 C CB  . LEU A 1 271 ? -12.645 -14.847 -16.709 1.00 29.71 ?  245 LEU A CB  1 
ATOM   1893 C CG  . LEU A 1 271 ? -12.273 -13.817 -15.626 1.00 36.37 ?  245 LEU A CG  1 
ATOM   1894 C CD1 . LEU A 1 271 ? -12.807 -12.437 -15.969 1.00 39.66 ?  245 LEU A CD1 1 
ATOM   1895 C CD2 . LEU A 1 271 ? -12.803 -14.184 -14.258 1.00 40.47 ?  245 LEU A CD2 1 
ATOM   1896 N N   . ASP A 1 272 ? -14.857 -16.987 -17.551 1.00 27.61 ?  246 ASP A N   1 
ATOM   1897 C CA  . ASP A 1 272 ? -15.544 -17.674 -18.668 1.00 27.47 ?  246 ASP A CA  1 
ATOM   1898 C C   . ASP A 1 272 ? -14.814 -17.274 -19.946 1.00 30.24 ?  246 ASP A C   1 
ATOM   1899 O O   . ASP A 1 272 ? -14.311 -16.120 -20.031 1.00 26.46 ?  246 ASP A O   1 
ATOM   1900 C CB  . ASP A 1 272 ? -17.043 -17.321 -18.681 1.00 30.51 ?  246 ASP A CB  1 
ATOM   1901 C CG  . ASP A 1 272 ? -17.825 -17.913 -17.520 1.00 34.39 ?  246 ASP A CG  1 
ATOM   1902 O OD1 . ASP A 1 272 ? -17.632 -19.109 -17.213 1.00 34.84 ?  246 ASP A OD1 1 
ATOM   1903 O OD2 . ASP A 1 272 ? -18.634 -17.172 -16.926 1.00 37.76 ?  246 ASP A OD2 1 
ATOM   1904 N N   . ARG A 1 273 ? -14.759 -18.175 -20.922 1.00 31.41 ?  247 ARG A N   1 
ATOM   1905 C CA  . ARG A 1 273 ? -13.722 -18.190 -21.992 1.00 35.03 ?  247 ARG A CA  1 
ATOM   1906 C C   . ARG A 1 273 ? -13.649 -16.866 -22.770 1.00 33.32 ?  247 ARG A C   1 
ATOM   1907 O O   . ARG A 1 273 ? -12.549 -16.383 -23.120 1.00 30.85 ?  247 ARG A O   1 
ATOM   1908 C CB  . ARG A 1 273 ? -14.006 -19.394 -22.902 1.00 39.45 ?  247 ARG A CB  1 
ATOM   1909 C CG  . ARG A 1 273 ? -12.879 -19.714 -23.867 1.00 45.78 ?  247 ARG A CG  1 
ATOM   1910 C CD  . ARG A 1 273 ? -12.757 -21.197 -24.191 1.00 45.86 ?  247 ARG A CD  1 
ATOM   1911 N NE  . ARG A 1 273 ? -11.376 -21.328 -24.575 1.00 46.66 ?  247 ARG A NE  1 
ATOM   1912 C CZ  . ARG A 1 273 ? -10.413 -21.919 -23.860 1.00 44.47 ?  247 ARG A CZ  1 
ATOM   1913 N NH1 . ARG A 1 273 ? -10.677 -22.585 -22.748 1.00 48.52 ?  247 ARG A NH1 1 
ATOM   1914 N NH2 . ARG A 1 273 ? -9.176  -21.884 -24.308 1.00 45.10 ?  247 ARG A NH2 1 
ATOM   1915 N N   . PRO A 1 274 ? -14.801 -16.256 -23.139 1.00 30.17 ?  248 PRO A N   1 
ATOM   1916 C CA  . PRO A 1 274 ? -14.793 -15.054 -23.963 1.00 27.59 ?  248 PRO A CA  1 
ATOM   1917 C C   . PRO A 1 274 ? -14.138 -13.875 -23.210 1.00 24.26 ?  248 PRO A C   1 
ATOM   1918 O O   . PRO A 1 274 ? -13.449 -13.095 -23.829 1.00 27.52 ?  248 PRO A O   1 
ATOM   1919 C CB  . PRO A 1 274 ? -16.284 -14.769 -24.232 1.00 30.73 ?  248 PRO A CB  1 
ATOM   1920 C CG  . PRO A 1 274 ? -16.938 -16.102 -23.991 1.00 33.11 ?  248 PRO A CG  1 
ATOM   1921 C CD  . PRO A 1 274 ? -16.169 -16.718 -22.840 1.00 31.99 ?  248 PRO A CD  1 
ATOM   1922 N N   . TRP A 1 275 ? -14.322 -13.798 -21.895 1.00 23.82 ?  249 TRP A N   1 
ATOM   1923 C CA  . TRP A 1 275 ? -13.704 -12.744 -21.040 1.00 22.13 ?  249 TRP A CA  1 
ATOM   1924 C C   . TRP A 1 275 ? -12.213 -13.037 -20.839 1.00 21.99 ?  249 TRP A C   1 
ATOM   1925 O O   . TRP A 1 275 ? -11.386 -12.081 -20.777 1.00 19.07 ?  249 TRP A O   1 
ATOM   1926 C CB  . TRP A 1 275 ? -14.478 -12.606 -19.723 1.00 22.98 ?  249 TRP A CB  1 
ATOM   1927 C CG  . TRP A 1 275 ? -15.867 -12.152 -20.020 1.00 22.33 ?  249 TRP A CG  1 
ATOM   1928 C CD1 . TRP A 1 275 ? -17.011 -12.902 -20.034 1.00 25.17 ?  249 TRP A CD1 1 
ATOM   1929 C CD2 . TRP A 1 275 ? -16.231 -10.852 -20.486 1.00 20.81 ?  249 TRP A CD2 1 
ATOM   1930 N NE1 . TRP A 1 275 ? -18.073 -12.130 -20.427 1.00 23.91 ?  249 TRP A NE1 1 
ATOM   1931 C CE2 . TRP A 1 275 ? -17.628 -10.871 -20.717 1.00 23.54 ?  249 TRP A CE2 1 
ATOM   1932 C CE3 . TRP A 1 275 ? -15.522 -9.668  -20.698 1.00 22.78 ?  249 TRP A CE3 1 
ATOM   1933 C CZ2 . TRP A 1 275 ? -18.318 -9.754  -21.180 1.00 25.94 ?  249 TRP A CZ2 1 
ATOM   1934 C CZ3 . TRP A 1 275 ? -16.219 -8.555  -21.134 1.00 24.84 ?  249 TRP A CZ3 1 
ATOM   1935 C CH2 . TRP A 1 275 ? -17.597 -8.607  -21.394 1.00 22.52 ?  249 TRP A CH2 1 
ATOM   1936 N N   . ALA A 1 276 ? -11.844 -14.325 -20.706 1.00 22.92 ?  250 ALA A N   1 
ATOM   1937 C CA  . ALA A 1 276 ? -10.426 -14.753 -20.669 1.00 23.58 ?  250 ALA A CA  1 
ATOM   1938 C C   . ALA A 1 276 ? -9.744  -14.200 -21.910 1.00 21.00 ?  250 ALA A C   1 
ATOM   1939 O O   . ALA A 1 276 ? -8.604  -13.687 -21.794 1.00 25.58 ?  250 ALA A O   1 
ATOM   1940 C CB  . ALA A 1 276 ? -10.286 -16.270 -20.586 1.00 23.92 ?  250 ALA A CB  1 
ATOM   1941 N N   . GLN A 1 277 ? -10.352 -14.387 -23.074 1.00 22.31 ?  251 GLN A N   1 
ATOM   1942 C CA  . GLN A 1 277 ? -9.773  -13.944 -24.357 1.00 22.62 ?  251 GLN A CA  1 
ATOM   1943 C C   . GLN A 1 277 ? -9.714  -12.420 -24.398 1.00 24.42 ?  251 GLN A C   1 
ATOM   1944 O O   . GLN A 1 277 ? -8.778  -11.856 -24.982 1.00 23.54 ?  251 GLN A O   1 
ATOM   1945 C CB  . GLN A 1 277 ? -10.615 -14.483 -25.507 1.00 29.56 ?  251 GLN A CB  1 
ATOM   1946 C CG  . GLN A 1 277 ? -10.485 -15.989 -25.692 1.00 32.82 ?  251 GLN A CG  1 
ATOM   1947 C CD  . GLN A 1 277 ? -11.479 -16.444 -26.745 1.00 47.23 ?  251 GLN A CD  1 
ATOM   1948 O OE1 . GLN A 1 277 ? -11.379 -16.121 -27.941 1.00 49.86 ?  251 GLN A OE1 1 
ATOM   1949 N NE2 . GLN A 1 277 ? -12.492 -17.165 -26.297 1.00 54.70 ?  251 GLN A NE2 1 
ATOM   1950 N N   . ALA A 1 278 ? -10.767 -11.767 -23.915 1.00 23.51 ?  252 ALA A N   1 
ATOM   1951 C CA  . ALA A 1 278 ? -10.823 -10.288 -23.848 1.00 22.47 ?  252 ALA A CA  1 
ATOM   1952 C C   . ALA A 1 278 ? -9.617  -9.772  -23.043 1.00 21.18 ?  252 ALA A C   1 
ATOM   1953 O O   . ALA A 1 278 ? -8.945  -8.822  -23.491 1.00 22.83 ?  252 ALA A O   1 
ATOM   1954 C CB  . ALA A 1 278 ? -12.144 -9.877  -23.272 1.00 23.19 ?  252 ALA A CB  1 
ATOM   1955 N N   . LEU A 1 279 ? -9.326  -10.364 -21.894 1.00 21.64 ?  253 LEU A N   1 
ATOM   1956 C CA  . LEU A 1 279 ? -8.212  -9.887  -21.049 1.00 21.66 ?  253 LEU A CA  1 
ATOM   1957 C C   . LEU A 1 279 ? -6.891  -10.217 -21.768 1.00 21.97 ?  253 LEU A C   1 
ATOM   1958 O O   . LEU A 1 279 ? -5.994  -9.328  -21.802 1.00 22.79 ?  253 LEU A O   1 
ATOM   1959 C CB  . LEU A 1 279 ? -8.291  -10.562 -19.680 1.00 22.55 ?  253 LEU A CB  1 
ATOM   1960 C CG  . LEU A 1 279 ? -9.368  -10.035 -18.732 1.00 26.15 ?  253 LEU A CG  1 
ATOM   1961 C CD1 . LEU A 1 279 ? -9.612  -11.037 -17.623 1.00 28.71 ?  253 LEU A CD1 1 
ATOM   1962 C CD2 . LEU A 1 279 ? -8.966  -8.694  -18.141 1.00 26.09 ?  253 LEU A CD2 1 
ATOM   1963 N N   . ASP A 1 280 ? -6.757  -11.395 -22.413 1.00 21.77 ?  254 ASP A N   1 
ATOM   1964 C CA  . ASP A 1 280 ? -5.487  -11.755 -23.124 1.00 23.08 ?  254 ASP A CA  1 
ATOM   1965 C C   . ASP A 1 280 ? -5.185  -10.743 -24.242 1.00 21.52 ?  254 ASP A C   1 
ATOM   1966 O O   . ASP A 1 280 ? -4.003  -10.432 -24.502 1.00 22.34 ?  254 ASP A O   1 
ATOM   1967 C CB  . ASP A 1 280 ? -5.522  -13.166 -23.731 1.00 29.00 ?  254 ASP A CB  1 
ATOM   1968 C CG  . ASP A 1 280 ? -5.472  -14.285 -22.701 1.00 36.52 ?  254 ASP A CG  1 
ATOM   1969 O OD1 . ASP A 1 280 ? -4.921  -14.047 -21.590 1.00 37.35 ?  254 ASP A OD1 1 
ATOM   1970 O OD2 . ASP A 1 280 ? -6.006  -15.395 -23.007 1.00 49.63 ?  254 ASP A OD2 1 
ATOM   1971 N N   . ALA A 1 281 ? -6.203  -10.159 -24.853 1.00 20.79 ?  255 ALA A N   1 
ATOM   1972 C CA  . ALA A 1 281 ? -6.030  -9.209  -25.965 1.00 19.53 ?  255 ALA A CA  1 
ATOM   1973 C C   . ALA A 1 281 ? -5.344  -7.940  -25.442 1.00 18.80 ?  255 ALA A C   1 
ATOM   1974 O O   . ALA A 1 281 ? -4.771  -7.211  -26.282 1.00 19.70 ?  255 ALA A O   1 
ATOM   1975 C CB  . ALA A 1 281 ? -7.345  -8.876  -26.625 1.00 21.28 ?  255 ALA A CB  1 
ATOM   1976 N N   . THR A 1 282 ? -5.432  -7.667  -24.126 1.00 18.43 ?  256 THR A N   1 
ATOM   1977 C CA  . THR A 1 282 ? -4.814  -6.477  -23.498 1.00 17.94 ?  256 THR A CA  1 
ATOM   1978 C C   . THR A 1 282 ? -3.348  -6.778  -23.116 1.00 20.41 ?  256 THR A C   1 
ATOM   1979 O O   . THR A 1 282 ? -2.699  -5.912  -22.494 1.00 22.58 ?  256 THR A O   1 
ATOM   1980 C CB  . THR A 1 282 ? -5.631  -5.957  -22.321 1.00 17.05 ?  256 THR A CB  1 
ATOM   1981 O OG1 . THR A 1 282 ? -5.500  -6.815  -21.185 1.00 19.01 ?  256 THR A OG1 1 
ATOM   1982 C CG2 . THR A 1 282 ? -7.087  -5.777  -22.707 1.00 19.08 ?  256 THR A CG2 1 
ATOM   1983 N N   . HIS A 1 283 ? -2.917  -8.025  -23.308 1.00 18.18 ?  257 HIS A N   1 
ATOM   1984 C CA  . HIS A 1 283 ? -1.534  -8.464  -22.991 1.00 19.87 ?  257 HIS A CA  1 
ATOM   1985 C C   . HIS A 1 283 ? -0.713  -8.766  -24.269 1.00 22.04 ?  257 HIS A C   1 
ATOM   1986 O O   . HIS A 1 283 ? 0.065   -9.735  -24.252 1.00 21.95 ?  257 HIS A O   1 
ATOM   1987 C CB  . HIS A 1 283 ? -1.608  -9.663  -22.051 1.00 21.93 ?  257 HIS A CB  1 
ATOM   1988 C CG  . HIS A 1 283 ? -2.442  -9.475  -20.834 1.00 22.30 ?  257 HIS A CG  1 
ATOM   1989 N ND1 . HIS A 1 283 ? -2.919  -10.561 -20.116 1.00 23.08 ?  257 HIS A ND1 1 
ATOM   1990 C CD2 . HIS A 1 283 ? -2.885  -8.357  -20.197 1.00 19.34 ?  257 HIS A CD2 1 
ATOM   1991 C CE1 . HIS A 1 283 ? -3.608  -10.118 -19.076 1.00 23.51 ?  257 HIS A CE1 1 
ATOM   1992 N NE2 . HIS A 1 283 ? -3.603  -8.773  -19.114 1.00 20.82 ?  257 HIS A NE2 1 
ATOM   1993 N N   . ARG A 1 284 ? -0.833  -7.935  -25.303 1.00 22.47 ?  258 ARG A N   1 
ATOM   1994 C CA  . ARG A 1 284 ? -0.144  -8.084  -26.605 1.00 24.47 ?  258 ARG A CA  1 
ATOM   1995 C C   . ARG A 1 284 ? 0.504   -6.739  -26.945 1.00 22.73 ?  258 ARG A C   1 
ATOM   1996 O O   . ARG A 1 284 ? -0.220  -5.710  -27.003 1.00 19.69 ?  258 ARG A O   1 
ATOM   1997 C CB  . ARG A 1 284 ? -1.080  -8.547  -27.732 1.00 30.84 ?  258 ARG A CB  1 
ATOM   1998 C CG  . ARG A 1 284 ? -2.139  -9.581  -27.358 1.00 37.28 ?  258 ARG A CG  1 
ATOM   1999 C CD  . ARG A 1 284 ? -1.765  -11.040 -27.495 1.00 47.92 ?  258 ARG A CD  1 
ATOM   2000 N NE  . ARG A 1 284 ? -1.257  -11.356 -28.828 1.00 56.82 ?  258 ARG A NE  1 
ATOM   2001 C CZ  . ARG A 1 284 ? -0.239  -12.192 -29.094 1.00 56.88 ?  258 ARG A CZ  1 
ATOM   2002 N NH1 . ARG A 1 284 ? 0.400   -12.829 -28.127 1.00 53.78 ?  258 ARG A NH1 1 
ATOM   2003 N NH2 . ARG A 1 284 ? 0.147   -12.375 -30.344 1.00 58.59 ?  258 ARG A NH2 1 
ATOM   2004 N N   . GLY A 1 285 ? 1.831   -6.738  -27.092 1.00 21.31 ?  259 GLY A N   1 
ATOM   2005 C CA  . GLY A 1 285 ? 2.604   -5.530  -27.423 1.00 22.67 ?  259 GLY A CA  1 
ATOM   2006 C C   . GLY A 1 285 ? 2.738   -5.368  -28.919 1.00 21.01 ?  259 GLY A C   1 
ATOM   2007 O O   . GLY A 1 285 ? 3.060   -6.351  -29.567 1.00 26.61 ?  259 GLY A O   1 
ATOM   2008 N N   . TYR A 1 286 ? 2.596   -4.153  -29.432 1.00 23.07 ?  260 TYR A N   1 
ATOM   2009 C CA  . TYR A 1 286 ? 2.608   -3.874  -30.886 1.00 22.37 ?  260 TYR A CA  1 
ATOM   2010 C C   . TYR A 1 286 ? 3.850   -3.091  -31.315 1.00 23.20 ?  260 TYR A C   1 
ATOM   2011 O O   . TYR A 1 286 ? 4.223   -3.188  -32.491 1.00 22.31 ?  260 TYR A O   1 
ATOM   2012 C CB  . TYR A 1 286 ? 1.334   -3.152  -31.276 1.00 22.47 ?  260 TYR A CB  1 
ATOM   2013 C CG  . TYR A 1 286 ? 0.174   -4.096  -31.111 1.00 22.36 ?  260 TYR A CG  1 
ATOM   2014 C CD1 . TYR A 1 286 ? -0.077  -5.064  -32.074 1.00 24.76 ?  260 TYR A CD1 1 
ATOM   2015 C CD2 . TYR A 1 286 ? -0.568  -4.119  -29.955 1.00 22.36 ?  260 TYR A CD2 1 
ATOM   2016 C CE1 . TYR A 1 286 ? -1.096  -5.980  -31.917 1.00 25.27 ?  260 TYR A CE1 1 
ATOM   2017 C CE2 . TYR A 1 286 ? -1.584  -5.048  -29.763 1.00 23.37 ?  260 TYR A CE2 1 
ATOM   2018 C CZ  . TYR A 1 286 ? -1.850  -5.972  -30.753 1.00 27.17 ?  260 TYR A CZ  1 
ATOM   2019 O OH  . TYR A 1 286 ? -2.840  -6.880  -30.598 1.00 28.42 ?  260 TYR A OH  1 
ATOM   2020 N N   . TYR A 1 287 ? 4.426   -2.302  -30.422 1.00 21.15 ?  261 TYR A N   1 
ATOM   2021 C CA  . TYR A 1 287 ? 5.595   -1.436  -30.721 1.00 21.47 ?  261 TYR A CA  1 
ATOM   2022 C C   . TYR A 1 287 ? 6.229   -0.948  -29.425 1.00 22.63 ?  261 TYR A C   1 
ATOM   2023 O O   . TYR A 1 287 ? 5.678   -1.137  -28.350 1.00 19.29 ?  261 TYR A O   1 
ATOM   2024 C CB  . TYR A 1 287 ? 5.238   -0.235  -31.607 1.00 21.60 ?  261 TYR A CB  1 
ATOM   2025 C CG  . TYR A 1 287 ? 4.358   0.802   -30.956 1.00 20.25 ?  261 TYR A CG  1 
ATOM   2026 C CD1 . TYR A 1 287 ? 4.845   1.643   -29.967 1.00 20.05 ?  261 TYR A CD1 1 
ATOM   2027 C CD2 . TYR A 1 287 ? 3.018   0.907   -31.289 1.00 19.27 ?  261 TYR A CD2 1 
ATOM   2028 C CE1 . TYR A 1 287 ? 4.056   2.622   -29.373 1.00 19.94 ?  261 TYR A CE1 1 
ATOM   2029 C CE2 . TYR A 1 287 ? 2.203   1.847   -30.680 1.00 21.54 ?  261 TYR A CE2 1 
ATOM   2030 C CZ  . TYR A 1 287 ? 2.714   2.705   -29.709 1.00 21.97 ?  261 TYR A CZ  1 
ATOM   2031 O OH  . TYR A 1 287 ? 1.926   3.646   -29.128 1.00 20.27 ?  261 TYR A OH  1 
ATOM   2032 N N   . LYS A 1 288 ? 7.481   -0.510  -29.543 1.00 22.05 ?  262 LYS A N   1 
ATOM   2033 C CA  . LYS A 1 288 ? 8.268   0.022   -28.423 1.00 23.14 ?  262 LYS A CA  1 
ATOM   2034 C C   . LYS A 1 288 ? 8.503   1.509   -28.646 1.00 22.93 ?  262 LYS A C   1 
ATOM   2035 O O   . LYS A 1 288 ? 8.647   1.985   -29.843 1.00 22.77 ?  262 LYS A O   1 
ATOM   2036 C CB  . LYS A 1 288 ? 9.614   -0.696  -28.290 1.00 24.93 ?  262 LYS A CB  1 
ATOM   2037 C CG  . LYS A 1 288 ? 9.497   -2.149  -27.890 1.00 29.34 ?  262 LYS A CG  1 
ATOM   2038 C CD  . LYS A 1 288 ? 10.847  -2.740  -27.448 1.00 35.38 ?  262 LYS A CD  1 
ATOM   2039 C CE  . LYS A 1 288 ? 10.906  -4.255  -27.544 1.00 41.78 ?  262 LYS A CE  1 
ATOM   2040 N NZ  . LYS A 1 288 ? 9.782   -4.900  -26.801 1.00 46.53 ?  262 LYS A NZ  1 
ATOM   2041 N N   . VAL A 1 289 ? 8.514   2.216   -27.527 1.00 22.23 ?  263 VAL A N   1 
ATOM   2042 C CA  . VAL A 1 289 ? 9.063   3.600   -27.429 1.00 23.77 ?  263 VAL A CA  1 
ATOM   2043 C C   . VAL A 1 289 ? 9.991   3.591   -26.224 1.00 23.08 ?  263 VAL A C   1 
ATOM   2044 O O   . VAL A 1 289 ? 9.521   3.352   -25.121 1.00 21.72 ?  263 VAL A O   1 
ATOM   2045 C CB  . VAL A 1 289 ? 7.983   4.687   -27.301 1.00 23.98 ?  263 VAL A CB  1 
ATOM   2046 C CG1 . VAL A 1 289 ? 8.626   6.044   -27.002 1.00 24.70 ?  263 VAL A CG1 1 
ATOM   2047 C CG2 . VAL A 1 289 ? 7.134   4.759   -28.540 1.00 25.56 ?  263 VAL A CG2 1 
ATOM   2048 N N   . GLY A 1 290 ? 11.298  3.747   -26.448 1.00 24.41 ?  264 GLY A N   1 
ATOM   2049 C CA  . GLY A 1 290 ? 12.279  3.588   -25.374 1.00 23.24 ?  264 GLY A CA  1 
ATOM   2050 C C   . GLY A 1 290 ? 12.153  2.234   -24.709 1.00 20.76 ?  264 GLY A C   1 
ATOM   2051 O O   . GLY A 1 290 ? 12.149  1.215   -25.394 1.00 21.07 ?  264 GLY A O   1 
ATOM   2052 N N   . ASP A 1 291 ? 11.970  2.227   -23.395 1.00 19.60 ?  265 ASP A N   1 
ATOM   2053 C CA  . ASP A 1 291 ? 11.908  0.972   -22.610 1.00 17.97 ?  265 ASP A CA  1 
ATOM   2054 C C   . ASP A 1 291 ? 10.464  0.442   -22.584 1.00 18.04 ?  265 ASP A C   1 
ATOM   2055 O O   . ASP A 1 291 ? 10.254  -0.617  -21.958 1.00 20.36 ?  265 ASP A O   1 
ATOM   2056 C CB  . ASP A 1 291 ? 12.395  1.243   -21.196 1.00 17.40 ?  265 ASP A CB  1 
ATOM   2057 C CG  . ASP A 1 291 ? 13.905  1.511   -21.128 1.00 19.23 ?  265 ASP A CG  1 
ATOM   2058 O OD1 . ASP A 1 291 ? 14.630  0.812   -21.834 1.00 23.47 ?  265 ASP A OD1 1 
ATOM   2059 O OD2 . ASP A 1 291 ? 14.316  2.419   -20.363 1.00 19.36 ?  265 ASP A OD2 1 
ATOM   2060 N N   . MET A 1 292 ? 9.524   1.178   -23.161 1.00 17.62 ?  266 MET A N   1 
ATOM   2061 C CA  . MET A 1 292 ? 8.062   0.845   -23.034 1.00 17.51 ?  266 MET A CA  1 
ATOM   2062 C C   . MET A 1 292 ? 7.560   0.052   -24.252 1.00 20.17 ?  266 MET A C   1 
ATOM   2063 O O   . MET A 1 292 ? 7.786   0.476   -25.394 1.00 20.35 ?  266 MET A O   1 
ATOM   2064 C CB  . MET A 1 292 ? 7.246   2.125   -22.850 1.00 18.43 ?  266 MET A CB  1 
ATOM   2065 C CG  . MET A 1 292 ? 5.801   1.885   -22.434 1.00 21.01 ?  266 MET A CG  1 
ATOM   2066 S SD  . MET A 1 292 ? 4.656   1.676   -23.796 1.00 21.55 ?  266 MET A SD  1 
ATOM   2067 C CE  . MET A 1 292 ? 4.632   3.359   -24.426 1.00 21.68 ?  266 MET A CE  1 
ATOM   2068 N N   . THR A 1 293 ? 6.821   -1.035  -24.009 1.00 20.73 ?  267 THR A N   1 
ATOM   2069 C CA  . THR A 1 293 ? 6.122   -1.794  -25.073 1.00 20.61 ?  267 THR A CA  1 
ATOM   2070 C C   . THR A 1 293 ? 4.617   -1.523  -24.907 1.00 19.38 ?  267 THR A C   1 
ATOM   2071 O O   . THR A 1 293 ? 4.130   -1.668  -23.798 1.00 20.65 ?  267 THR A O   1 
ATOM   2072 C CB  . THR A 1 293 ? 6.420   -3.288  -24.995 1.00 20.26 ?  267 THR A CB  1 
ATOM   2073 O OG1 . THR A 1 293 ? 7.826   -3.494  -25.186 1.00 19.79 ?  267 THR A OG1 1 
ATOM   2074 C CG2 . THR A 1 293 ? 5.649   -4.069  -26.023 1.00 20.88 ?  267 THR A CG2 1 
ATOM   2075 N N   . GLN A 1 294 ? 4.002   -0.996  -25.945 1.00 18.10 ?  268 GLN A N   1 
ATOM   2076 C CA  . GLN A 1 294 ? 2.584   -0.502  -25.953 1.00 17.22 ?  268 GLN A CA  1 
ATOM   2077 C C   . GLN A 1 294 ? 1.667   -1.665  -26.267 1.00 18.46 ?  268 GLN A C   1 
ATOM   2078 O O   . GLN A 1 294 ? 1.768   -2.234  -27.383 1.00 20.70 ?  268 GLN A O   1 
ATOM   2079 C CB  . GLN A 1 294 ? 2.360   0.633   -26.955 1.00 16.72 ?  268 GLN A CB  1 
ATOM   2080 C CG  . GLN A 1 294 ? 0.930   1.200   -26.953 1.00 17.68 ?  268 GLN A CG  1 
ATOM   2081 C CD  . GLN A 1 294 ? 0.619   1.987   -25.692 1.00 17.68 ?  268 GLN A CD  1 
ATOM   2082 O OE1 . GLN A 1 294 ? 1.244   3.016   -25.417 1.00 17.35 ?  268 GLN A OE1 1 
ATOM   2083 N NE2 . GLN A 1 294 ? -0.349  1.522   -24.903 1.00 20.36 ?  268 GLN A NE2 1 
ATOM   2084 N N   . GLY A 1 295 ? 0.749   -1.971  -25.353 1.00 19.65 ?  269 GLY A N   1 
ATOM   2085 C CA  . GLY A 1 295 ? -0.376  -2.892  -25.625 1.00 17.28 ?  269 GLY A CA  1 
ATOM   2086 C C   . GLY A 1 295 ? -1.670  -2.138  -25.720 1.00 16.75 ?  269 GLY A C   1 
ATOM   2087 O O   . GLY A 1 295 ? -1.637  -0.904  -25.955 1.00 18.51 ?  269 GLY A O   1 
ATOM   2088 N N   . LEU A 1 296 ? -2.787  -2.850  -25.661 1.00 16.24 ?  270 LEU A N   1 
ATOM   2089 C CA  . LEU A 1 296 ? -4.112  -2.209  -25.640 1.00 16.87 ?  270 LEU A CA  1 
ATOM   2090 C C   . LEU A 1 296 ? -4.372  -1.811  -24.193 1.00 16.86 ?  270 LEU A C   1 
ATOM   2091 O O   . LEU A 1 296 ? -4.536  -2.716  -23.337 1.00 17.79 ?  270 LEU A O   1 
ATOM   2092 C CB  . LEU A 1 296 ? -5.200  -3.145  -26.147 1.00 18.24 ?  270 LEU A CB  1 
ATOM   2093 C CG  . LEU A 1 296 ? -5.028  -3.746  -27.542 1.00 19.23 ?  270 LEU A CG  1 
ATOM   2094 C CD1 . LEU A 1 296 ? -6.286  -4.545  -27.846 1.00 20.41 ?  270 LEU A CD1 1 
ATOM   2095 C CD2 . LEU A 1 296 ? -4.816  -2.687  -28.608 1.00 20.65 ?  270 LEU A CD2 1 
ATOM   2096 N N   . GLY A 1 297 ? -4.301  -0.508  -23.900 1.00 17.04 ?  271 GLY A N   1 
ATOM   2097 C CA  . GLY A 1 297 ? -4.419  -0.047  -22.501 1.00 19.52 ?  271 GLY A CA  1 
ATOM   2098 C C   . GLY A 1 297 ? -3.094  -0.147  -21.759 1.00 19.70 ?  271 GLY A C   1 
ATOM   2099 O O   . GLY A 1 297 ? -2.511  0.906   -21.470 1.00 18.81 ?  271 GLY A O   1 
ATOM   2100 N N   . TRP A 1 298 ? -2.611  -1.367  -21.498 1.00 17.48 ?  272 TRP A N   1 
ATOM   2101 C CA  . TRP A 1 298 ? -1.386  -1.632  -20.700 1.00 19.68 ?  272 TRP A CA  1 
ATOM   2102 C C   . TRP A 1 298 ? -0.130  -1.209  -21.447 1.00 18.29 ?  272 TRP A C   1 
ATOM   2103 O O   . TRP A 1 298 ? -0.080  -1.293  -22.713 1.00 18.45 ?  272 TRP A O   1 
ATOM   2104 C CB  . TRP A 1 298 ? -1.304  -3.085  -20.233 1.00 17.03 ?  272 TRP A CB  1 
ATOM   2105 C CG  . TRP A 1 298 ? -2.470  -3.489  -19.388 1.00 18.63 ?  272 TRP A CG  1 
ATOM   2106 C CD1 . TRP A 1 298 ? -3.452  -4.361  -19.746 1.00 20.62 ?  272 TRP A CD1 1 
ATOM   2107 C CD2 . TRP A 1 298 ? -2.786  -3.068  -18.052 1.00 17.49 ?  272 TRP A CD2 1 
ATOM   2108 N NE1 . TRP A 1 298 ? -4.321  -4.544  -18.725 1.00 20.94 ?  272 TRP A NE1 1 
ATOM   2109 C CE2 . TRP A 1 298 ? -3.978  -3.726  -17.687 1.00 17.46 ?  272 TRP A CE2 1 
ATOM   2110 C CE3 . TRP A 1 298 ? -2.217  -2.192  -17.124 1.00 18.54 ?  272 TRP A CE3 1 
ATOM   2111 C CZ2 . TRP A 1 298 ? -4.577  -3.558  -16.452 1.00 18.82 ?  272 TRP A CZ2 1 
ATOM   2112 C CZ3 . TRP A 1 298 ? -2.817  -2.027  -15.891 1.00 18.63 ?  272 TRP A CZ3 1 
ATOM   2113 C CH2 . TRP A 1 298 ? -3.995  -2.687  -15.563 1.00 18.62 ?  272 TRP A CH2 1 
ATOM   2114 N N   . GLU A 1 299 ? 0.824   -0.698  -20.667 1.00 19.23 ?  273 GLU A N   1 
ATOM   2115 C CA  . GLU A 1 299 ? 2.199   -0.349  -21.101 1.00 18.31 ?  273 GLU A CA  1 
ATOM   2116 C C   . GLU A 1 299 ? 3.149   -1.243  -20.308 1.00 18.68 ?  273 GLU A C   1 
ATOM   2117 O O   . GLU A 1 299 ? 2.965   -1.331  -19.069 1.00 17.88 ?  273 GLU A O   1 
ATOM   2118 C CB  . GLU A 1 299 ? 2.454   1.156   -20.908 1.00 19.65 ?  273 GLU A CB  1 
ATOM   2119 C CG  . GLU A 1 299 ? 1.496   2.039   -21.691 1.00 19.00 ?  273 GLU A CG  1 
ATOM   2120 C CD  . GLU A 1 299 ? 1.551   3.529   -21.396 1.00 20.83 ?  273 GLU A CD  1 
ATOM   2121 O OE1 . GLU A 1 299 ? 2.579   3.997   -20.863 1.00 24.29 ?  273 GLU A OE1 1 
ATOM   2122 O OE2 . GLU A 1 299 ? 0.565   4.210   -21.681 1.00 21.35 ?  273 GLU A OE2 1 
ATOM   2123 N N   . ALA A 1 300 ? 4.152   -1.843  -20.965 1.00 18.07 ?  274 ALA A N   1 
ATOM   2124 C CA  . ALA A 1 300 ? 4.966   -2.917  -20.387 1.00 17.52 ?  274 ALA A CA  1 
ATOM   2125 C C   . ALA A 1 300 ? 6.443   -2.520  -20.439 1.00 16.63 ?  274 ALA A C   1 
ATOM   2126 O O   . ALA A 1 300 ? 6.876   -1.863  -21.388 1.00 17.27 ?  274 ALA A O   1 
ATOM   2127 C CB  . ALA A 1 300 ? 4.712   -4.243  -21.079 1.00 18.48 ?  274 ALA A CB  1 
ATOM   2128 N N   . TYR A 1 301 ? 7.163   -3.006  -19.461 1.00 16.15 ?  275 TYR A N   1 
ATOM   2129 C CA  . TYR A 1 301 ? 8.634   -2.872  -19.282 1.00 15.79 ?  275 TYR A CA  1 
ATOM   2130 C C   . TYR A 1 301 ? 9.211   -4.243  -18.983 1.00 18.29 ?  275 TYR A C   1 
ATOM   2131 O O   . TYR A 1 301 ? 8.566   -5.069  -18.268 1.00 19.17 ?  275 TYR A O   1 
ATOM   2132 C CB  . TYR A 1 301 ? 8.914   -1.930  -18.113 1.00 17.63 ?  275 TYR A CB  1 
ATOM   2133 C CG  . TYR A 1 301 ? 8.401   -0.545  -18.410 1.00 17.10 ?  275 TYR A CG  1 
ATOM   2134 C CD1 . TYR A 1 301 ? 7.065   -0.229  -18.193 1.00 18.06 ?  275 TYR A CD1 1 
ATOM   2135 C CD2 . TYR A 1 301 ? 9.193   0.406   -19.020 1.00 18.53 ?  275 TYR A CD2 1 
ATOM   2136 C CE1 . TYR A 1 301 ? 6.539   1.009   -18.524 1.00 19.25 ?  275 TYR A CE1 1 
ATOM   2137 C CE2 . TYR A 1 301 ? 8.693   1.671   -19.315 1.00 17.57 ?  275 TYR A CE2 1 
ATOM   2138 C CZ  . TYR A 1 301 ? 7.358   1.973   -19.087 1.00 18.05 ?  275 TYR A CZ  1 
ATOM   2139 O OH  . TYR A 1 301 ? 6.820   3.195   -19.426 1.00 18.55 ?  275 TYR A OH  1 
ATOM   2140 N N   . ASP A 1 302 ? 10.491  -4.419  -19.311 1.00 18.52 ?  276 ASP A N   1 
ATOM   2141 C CA  . ASP A 1 302 ? 11.207  -5.584  -18.745 1.00 21.32 ?  276 ASP A CA  1 
ATOM   2142 C C   . ASP A 1 302 ? 11.298  -5.418  -17.229 1.00 21.07 ?  276 ASP A C   1 
ATOM   2143 O O   . ASP A 1 302 ? 11.352  -4.248  -16.742 1.00 23.08 ?  276 ASP A O   1 
ATOM   2144 C CB  . ASP A 1 302 ? 12.587  -5.695  -19.365 1.00 24.41 ?  276 ASP A CB  1 
ATOM   2145 C CG  . ASP A 1 302 ? 12.527  -5.940  -20.870 1.00 27.76 ?  276 ASP A CG  1 
ATOM   2146 O OD1 . ASP A 1 302 ? 11.509  -6.482  -21.357 1.00 28.46 ?  276 ASP A OD1 1 
ATOM   2147 O OD2 . ASP A 1 302 ? 13.517  -5.627  -21.528 1.00 33.51 ?  276 ASP A OD2 1 
ATOM   2148 N N   . TRP A 1 303 ? 11.352  -6.536  -16.519 1.00 21.14 ?  277 TRP A N   1 
ATOM   2149 C CA  . TRP A 1 303 ? 11.431  -6.574  -15.045 1.00 23.23 ?  277 TRP A CA  1 
ATOM   2150 C C   . TRP A 1 303 ? 12.491  -7.597  -14.645 1.00 25.22 ?  277 TRP A C   1 
ATOM   2151 O O   . TRP A 1 303 ? 12.400  -8.742  -15.053 1.00 24.03 ?  277 TRP A O   1 
ATOM   2152 C CB  . TRP A 1 303 ? 10.047  -6.888  -14.452 1.00 24.61 ?  277 TRP A CB  1 
ATOM   2153 C CG  . TRP A 1 303 ? 10.017  -6.661  -12.977 1.00 23.86 ?  277 TRP A CG  1 
ATOM   2154 C CD1 . TRP A 1 303 ? 9.928   -7.615  -12.005 1.00 27.06 ?  277 TRP A CD1 1 
ATOM   2155 C CD2 . TRP A 1 303 ? 10.116  -5.395  -12.302 1.00 25.30 ?  277 TRP A CD2 1 
ATOM   2156 N NE1 . TRP A 1 303 ? 9.926   -7.022  -10.775 1.00 27.76 ?  277 TRP A NE1 1 
ATOM   2157 C CE2 . TRP A 1 303 ? 10.034  -5.664  -10.923 1.00 27.03 ?  277 TRP A CE2 1 
ATOM   2158 C CE3 . TRP A 1 303 ? 10.249  -4.071  -12.726 1.00 26.55 ?  277 TRP A CE3 1 
ATOM   2159 C CZ2 . TRP A 1 303 ? 10.121  -4.653  -9.964  1.00 28.65 ?  277 TRP A CZ2 1 
ATOM   2160 C CZ3 . TRP A 1 303 ? 10.300  -3.068  -11.778 1.00 28.98 ?  277 TRP A CZ3 1 
ATOM   2161 C CH2 . TRP A 1 303 ? 10.227  -3.365  -10.418 1.00 29.75 ?  277 TRP A CH2 1 
ATOM   2162 N N   . PRO A 1 304 ? 13.560  -7.215  -13.906 1.00 25.29 ?  278 PRO A N   1 
ATOM   2163 C CA  . PRO A 1 304 ? 13.694  -5.860  -13.355 1.00 24.68 ?  278 PRO A CA  1 
ATOM   2164 C C   . PRO A 1 304 ? 14.182  -4.774  -14.332 1.00 21.43 ?  278 PRO A C   1 
ATOM   2165 O O   . PRO A 1 304 ? 14.632  -5.053  -15.429 1.00 20.94 ?  278 PRO A O   1 
ATOM   2166 C CB  . PRO A 1 304 ? 14.706  -6.102  -12.215 1.00 27.96 ?  278 PRO A CB  1 
ATOM   2167 C CG  . PRO A 1 304 ? 15.624  -7.132  -12.796 1.00 27.42 ?  278 PRO A CG  1 
ATOM   2168 C CD  . PRO A 1 304 ? 14.721  -8.064  -13.588 1.00 27.33 ?  278 PRO A CD  1 
ATOM   2169 N N   . ILE A 1 305 ? 13.987  -3.513  -13.924 1.00 19.40 ?  279 ILE A N   1 
ATOM   2170 C CA  . ILE A 1 305 ? 14.458  -2.294  -14.629 1.00 20.25 ?  279 ILE A CA  1 
ATOM   2171 C C   . ILE A 1 305 ? 14.644  -1.241  -13.533 1.00 20.76 ?  279 ILE A C   1 
ATOM   2172 O O   . ILE A 1 305 ? 14.023  -1.391  -12.469 1.00 20.90 ?  279 ILE A O   1 
ATOM   2173 C CB  . ILE A 1 305 ? 13.487  -1.839  -15.733 1.00 22.06 ?  279 ILE A CB  1 
ATOM   2174 C CG1 . ILE A 1 305 ? 14.066  -0.742  -16.617 1.00 23.67 ?  279 ILE A CG1 1 
ATOM   2175 C CG2 . ILE A 1 305 ? 12.161  -1.407  -15.140 1.00 22.49 ?  279 ILE A CG2 1 
ATOM   2176 C CD1 . ILE A 1 305 ? 13.435  -0.634  -18.011 1.00 27.72 ?  279 ILE A CD1 1 
ATOM   2177 N N   . SER A 1 306 ? 15.507  -0.254  -13.736 1.00 19.26 ?  280 SER A N   1 
ATOM   2178 C CA  . SER A 1 306 ? 15.735  0.768   -12.691 1.00 18.72 ?  280 SER A CA  1 
ATOM   2179 C C   . SER A 1 306 ? 14.439  1.561   -12.437 1.00 18.36 ?  280 SER A C   1 
ATOM   2180 O O   . SER A 1 306 ? 13.637  1.781   -13.384 1.00 18.76 ?  280 SER A O   1 
ATOM   2181 C CB  . SER A 1 306 ? 16.841  1.696   -13.063 1.00 17.95 ?  280 SER A CB  1 
ATOM   2182 O OG  . SER A 1 306 ? 16.514  2.554   -14.156 1.00 19.14 ?  280 SER A OG  1 
ATOM   2183 N N   . LEU A 1 307 ? 14.350  2.143   -11.255 1.00 18.80 ?  281 LEU A N   1 
ATOM   2184 C CA  . LEU A 1 307 ? 13.264  3.093   -10.952 1.00 18.00 ?  281 LEU A CA  1 
ATOM   2185 C C   . LEU A 1 307 ? 13.337  4.249   -11.946 1.00 17.33 ?  281 LEU A C   1 
ATOM   2186 O O   . LEU A 1 307 ? 12.304  4.684   -12.415 1.00 18.35 ?  281 LEU A O   1 
ATOM   2187 C CB  . LEU A 1 307 ? 13.427  3.580   -9.509  1.00 17.87 ?  281 LEU A CB  1 
ATOM   2188 C CG  . LEU A 1 307 ? 12.489  4.716   -9.099  1.00 18.86 ?  281 LEU A CG  1 
ATOM   2189 C CD1 . LEU A 1 307 ? 11.026  4.339   -9.405  1.00 18.95 ?  281 LEU A CD1 1 
ATOM   2190 C CD2 . LEU A 1 307 ? 12.689  5.019   -7.639  1.00 20.21 ?  281 LEU A CD2 1 
ATOM   2191 N N   . LYS A 1 308 ? 14.511  4.828   -12.175 1.00 18.44 ?  282 LYS A N   1 
ATOM   2192 C CA  . LYS A 1 308 ? 14.637  5.998   -13.084 1.00 17.85 ?  282 LYS A CA  1 
ATOM   2193 C C   . LYS A 1 308 ? 14.090  5.696   -14.479 1.00 18.59 ?  282 LYS A C   1 
ATOM   2194 O O   . LYS A 1 308 ? 13.430  6.590   -15.062 1.00 17.88 ?  282 LYS A O   1 
ATOM   2195 C CB  . LYS A 1 308 ? 16.077  6.516   -13.120 1.00 18.37 ?  282 LYS A CB  1 
ATOM   2196 C CG  . LYS A 1 308 ? 16.391  7.321   -11.864 1.00 20.66 ?  282 LYS A CG  1 
ATOM   2197 C CD  . LYS A 1 308 ? 17.760  7.998   -11.866 1.00 23.11 ?  282 LYS A CD  1 
ATOM   2198 C CE  . LYS A 1 308 ? 17.930  8.826   -10.608 1.00 27.74 ?  282 LYS A CE  1 
ATOM   2199 N NZ  . LYS A 1 308 ? 19.363  9.119   -10.407 1.00 34.50 ?  282 LYS A NZ  1 
ATOM   2200 N N   . ARG A 1 309 ? 14.287  4.485   -14.982 1.00 18.02 ?  283 ARG A N   1 
ATOM   2201 C CA  . ARG A 1 309 ? 13.773  4.123   -16.323 1.00 16.92 ?  283 ARG A CA  1 
ATOM   2202 C C   . ARG A 1 309 ? 12.238  3.959   -16.271 1.00 17.30 ?  283 ARG A C   1 
ATOM   2203 O O   . ARG A 1 309 ? 11.576  4.425   -17.177 1.00 18.22 ?  283 ARG A O   1 
ATOM   2204 C CB  . ARG A 1 309 ? 14.443  2.850   -16.834 1.00 19.55 ?  283 ARG A CB  1 
ATOM   2205 C CG  . ARG A 1 309 ? 15.833  3.097   -17.387 1.00 19.51 ?  283 ARG A CG  1 
ATOM   2206 C CD  . ARG A 1 309 ? 16.546  1.859   -17.923 1.00 22.08 ?  283 ARG A CD  1 
ATOM   2207 N NE  . ARG A 1 309 ? 17.840  2.316   -18.400 1.00 21.99 ?  283 ARG A NE  1 
ATOM   2208 C CZ  . ARG A 1 309 ? 18.065  2.876   -19.580 1.00 23.34 ?  283 ARG A CZ  1 
ATOM   2209 N NH1 . ARG A 1 309 ? 17.126  2.909   -20.511 1.00 22.14 ?  283 ARG A NH1 1 
ATOM   2210 N NH2 . ARG A 1 309 ? 19.266  3.364   -19.846 1.00 24.35 ?  283 ARG A NH2 1 
ATOM   2211 N N   . LEU A 1 310 ? 11.688  3.395   -15.214 1.00 16.51 ?  284 LEU A N   1 
ATOM   2212 C CA  . LEU A 1 310 ? 10.220  3.246   -15.097 1.00 16.16 ?  284 LEU A CA  1 
ATOM   2213 C C   . LEU A 1 310 ? 9.579   4.625   -14.930 1.00 19.00 ?  284 LEU A C   1 
ATOM   2214 O O   . LEU A 1 310 ? 8.495   4.843   -15.527 1.00 21.02 ?  284 LEU A O   1 
ATOM   2215 C CB  . LEU A 1 310 ? 9.920   2.318   -13.922 1.00 18.27 ?  284 LEU A CB  1 
ATOM   2216 C CG  . LEU A 1 310 ? 8.449   1.942   -13.756 1.00 18.02 ?  284 LEU A CG  1 
ATOM   2217 C CD1 . LEU A 1 310 ? 7.956   1.295   -15.043 1.00 19.93 ?  284 LEU A CD1 1 
ATOM   2218 C CD2 . LEU A 1 310 ? 8.255   1.025   -12.547 1.00 20.06 ?  284 LEU A CD2 1 
ATOM   2219 N N   . GLN A 1 311 ? 10.210  5.550   -14.183 1.00 17.20 ?  285 GLN A N   1 
ATOM   2220 C CA  . GLN A 1 311 ? 9.715   6.931   -14.052 1.00 17.71 ?  285 GLN A CA  1 
ATOM   2221 C C   . GLN A 1 311 ? 9.730   7.597   -15.438 1.00 17.45 ?  285 GLN A C   1 
ATOM   2222 O O   . GLN A 1 311 ? 8.725   8.242   -15.780 1.00 17.65 ?  285 GLN A O   1 
ATOM   2223 C CB  . GLN A 1 311 ? 10.510  7.719   -12.998 1.00 18.55 ?  285 GLN A CB  1 
ATOM   2224 C CG  . GLN A 1 311 ? 10.339  7.213   -11.562 1.00 19.79 ?  285 GLN A CG  1 
ATOM   2225 C CD  . GLN A 1 311 ? 11.269  7.903   -10.599 1.00 22.10 ?  285 GLN A CD  1 
ATOM   2226 O OE1 . GLN A 1 311 ? 12.485  8.059   -10.867 1.00 22.05 ?  285 GLN A OE1 1 
ATOM   2227 N NE2 . GLN A 1 311 ? 10.716  8.322   -9.468  1.00 21.46 ?  285 GLN A NE2 1 
ATOM   2228 N N   . ALA A 1 312 ? 10.822  7.485   -16.200 1.00 18.37 ?  286 ALA A N   1 
ATOM   2229 C CA  . ALA A 1 312 ? 10.978  8.096   -17.535 1.00 19.94 ?  286 ALA A CA  1 
ATOM   2230 C C   . ALA A 1 312 ? 9.885   7.595   -18.492 1.00 22.09 ?  286 ALA A C   1 
ATOM   2231 O O   . ALA A 1 312 ? 9.337   8.434   -19.218 1.00 20.79 ?  286 ALA A O   1 
ATOM   2232 C CB  . ALA A 1 312 ? 12.354  7.851   -18.094 1.00 22.12 ?  286 ALA A CB  1 
ATOM   2233 N N   . GLY A 1 313 ? 9.534   6.304   -18.463 1.00 20.08 ?  287 GLY A N   1 
ATOM   2234 C CA  . GLY A 1 313 ? 8.468   5.753   -19.325 1.00 21.28 ?  287 GLY A CA  1 
ATOM   2235 C C   . GLY A 1 313 ? 7.099   6.343   -18.980 1.00 20.77 ?  287 GLY A C   1 
ATOM   2236 O O   . GLY A 1 313 ? 6.296   6.464   -19.871 1.00 18.86 ?  287 GLY A O   1 
ATOM   2237 N N   . ASN A 1 314 ? 6.920   6.805   -17.732 1.00 18.88 ?  288 ASN A N   1 
ATOM   2238 C CA  . ASN A 1 314 ? 5.647   7.371   -17.220 1.00 19.85 ?  288 ASN A CA  1 
ATOM   2239 C C   . ASN A 1 314 ? 5.824   8.882   -16.999 1.00 22.80 ?  288 ASN A C   1 
ATOM   2240 O O   . ASN A 1 314 ? 5.064   9.440   -16.247 1.00 21.75 ?  288 ASN A O   1 
ATOM   2241 C CB  . ASN A 1 314 ? 5.274   6.701   -15.910 1.00 20.30 ?  288 ASN A CB  1 
ATOM   2242 C CG  . ASN A 1 314 ? 4.809   5.277   -16.119 1.00 20.02 ?  288 ASN A CG  1 
ATOM   2243 O OD1 . ASN A 1 314 ? 3.718   5.082   -16.650 1.00 18.86 ?  288 ASN A OD1 1 
ATOM   2244 N ND2 . ASN A 1 314 ? 5.618   4.310   -15.708 1.00 20.49 ?  288 ASN A ND2 1 
ATOM   2245 N N   . SER A 1 315 ? 6.719   9.537   -17.722 1.00 21.85 ?  289 SER A N   1 
ATOM   2246 C CA  . SER A 1 315 ? 7.055   10.965  -17.508 1.00 24.17 ?  289 SER A CA  1 
ATOM   2247 C C   . SER A 1 315 ? 6.170   11.878  -18.356 1.00 24.15 ?  289 SER A C   1 
ATOM   2248 O O   . SER A 1 315 ? 5.505   11.402  -19.295 1.00 24.22 ?  289 SER A O   1 
ATOM   2249 C CB  . SER A 1 315 ? 8.493   11.235  -17.843 1.00 24.06 ?  289 SER A CB  1 
ATOM   2250 O OG  . SER A 1 315 ? 8.687   11.046  -19.241 1.00 25.75 ?  289 SER A OG  1 
ATOM   2251 N N   . THR A 1 316 ? 6.215   13.181  -18.062 1.00 22.48 ?  290 THR A N   1 
ATOM   2252 C CA  . THR A 1 316 ? 5.423   14.208  -18.773 1.00 24.51 ?  290 THR A CA  1 
ATOM   2253 C C   . THR A 1 316 ? 5.683   14.166  -20.282 1.00 24.54 ?  290 THR A C   1 
ATOM   2254 O O   . THR A 1 316 ? 4.713   14.161  -21.042 1.00 24.83 ?  290 THR A O   1 
ATOM   2255 C CB  . THR A 1 316 ? 5.634   15.574  -18.125 1.00 26.45 ?  290 THR A CB  1 
ATOM   2256 O OG1 . THR A 1 316 ? 5.104   15.427  -16.811 1.00 27.88 ?  290 THR A OG1 1 
ATOM   2257 C CG2 . THR A 1 316 ? 4.919   16.690  -18.833 1.00 28.71 ?  290 THR A CG2 1 
ATOM   2258 N N   . PRO A 1 317 ? 6.943   14.169  -20.779 1.00 26.58 ?  291 PRO A N   1 
ATOM   2259 C CA  . PRO A 1 317 ? 7.203   14.073  -22.221 1.00 28.42 ?  291 PRO A CA  1 
ATOM   2260 C C   . PRO A 1 317 ? 6.524   12.871  -22.912 1.00 29.75 ?  291 PRO A C   1 
ATOM   2261 O O   . PRO A 1 317 ? 6.090   13.004  -24.061 1.00 27.01 ?  291 PRO A O   1 
ATOM   2262 C CB  . PRO A 1 317 ? 8.742   13.946  -22.300 1.00 30.45 ?  291 PRO A CB  1 
ATOM   2263 C CG  . PRO A 1 317 ? 9.235   14.667  -21.079 1.00 29.67 ?  291 PRO A CG  1 
ATOM   2264 C CD  . PRO A 1 317 ? 8.194   14.368  -20.019 1.00 28.84 ?  291 PRO A CD  1 
ATOM   2265 N N   . MET A 1 318 ? 6.414   11.742  -22.203 1.00 29.10 ?  292 MET A N   1 
ATOM   2266 C CA  . MET A 1 318 ? 5.787   10.510  -22.757 1.00 29.11 ?  292 MET A CA  1 
ATOM   2267 C C   . MET A 1 318 ? 4.283   10.740  -22.925 1.00 29.82 ?  292 MET A C   1 
ATOM   2268 O O   . MET A 1 318 ? 3.681   10.199  -23.874 1.00 31.09 ?  292 MET A O   1 
ATOM   2269 C CB  . MET A 1 318 ? 6.036   9.303   -21.838 1.00 29.19 ?  292 MET A CB  1 
ATOM   2270 C CG  . MET A 1 318 ? 7.368   8.669   -22.044 1.00 26.74 ?  292 MET A CG  1 
ATOM   2271 S SD  . MET A 1 318 ? 7.595   8.083   -23.758 1.00 30.20 ?  292 MET A SD  1 
ATOM   2272 C CE  . MET A 1 318 ? 6.323   6.834   -23.854 1.00 31.26 ?  292 MET A CE  1 
ATOM   2273 N N   . ALA A 1 319 ? 3.672   11.509  -22.029 1.00 30.09 ?  293 ALA A N   1 
ATOM   2274 C CA  . ALA A 1 319 ? 2.250   11.886  -22.125 1.00 28.79 ?  293 ALA A CA  1 
ATOM   2275 C C   . ALA A 1 319 ? 2.042   12.970  -23.198 1.00 30.20 ?  293 ALA A C   1 
ATOM   2276 O O   . ALA A 1 319 ? 0.920   13.039  -23.763 1.00 30.58 ?  293 ALA A O   1 
ATOM   2277 C CB  . ALA A 1 319 ? 1.743   12.374  -20.796 1.00 30.96 ?  293 ALA A CB  1 
ATOM   2278 N N   . LEU A 1 320 ? 2.994   13.889  -23.401 1.00 27.54 ?  294 LEU A N   1 
ATOM   2279 C CA  . LEU A 1 320 ? 2.627   15.163  -24.090 1.00 27.76 ?  294 LEU A CA  1 
ATOM   2280 C C   . LEU A 1 320 ? 3.306   15.328  -25.449 1.00 26.25 ?  294 LEU A C   1 
ATOM   2281 O O   . LEU A 1 320 ? 2.830   16.178  -26.190 1.00 27.20 ?  294 LEU A O   1 
ATOM   2282 C CB  . LEU A 1 320 ? 2.939   16.383  -23.222 1.00 30.23 ?  294 LEU A CB  1 
ATOM   2283 C CG  . LEU A 1 320 ? 2.285   16.394  -21.842 1.00 32.58 ?  294 LEU A CG  1 
ATOM   2284 C CD1 . LEU A 1 320 ? 2.498   17.743  -21.165 1.00 33.06 ?  294 LEU A CD1 1 
ATOM   2285 C CD2 . LEU A 1 320 ? 0.797   16.068  -21.913 1.00 34.08 ?  294 LEU A CD2 1 
ATOM   2286 N N   . GLN A 1 321 ? 4.410   14.644  -25.720 1.00 25.07 ?  295 GLN A N   1 
ATOM   2287 C CA  . GLN A 1 321 ? 5.161   14.801  -26.984 1.00 26.42 ?  295 GLN A CA  1 
ATOM   2288 C C   . GLN A 1 321 ? 4.942   13.569  -27.854 1.00 24.54 ?  295 GLN A C   1 
ATOM   2289 O O   . GLN A 1 321 ? 4.844   12.441  -27.359 1.00 24.71 ?  295 GLN A O   1 
ATOM   2290 C CB  . GLN A 1 321 ? 6.651   14.991  -26.668 1.00 25.77 ?  295 GLN A CB  1 
ATOM   2291 C CG  . GLN A 1 321 ? 6.912   16.226  -25.826 1.00 29.37 ?  295 GLN A CG  1 
ATOM   2292 C CD  . GLN A 1 321 ? 8.376   16.339  -25.458 1.00 31.75 ?  295 GLN A CD  1 
ATOM   2293 O OE1 . GLN A 1 321 ? 8.735   16.906  -24.430 1.00 38.22 ?  295 GLN A OE1 1 
ATOM   2294 N NE2 . GLN A 1 321 ? 9.232   15.739  -26.263 1.00 31.97 ?  295 GLN A NE2 1 
ATOM   2295 N N   . PRO A 1 322 ? 4.974   13.734  -29.183 1.00 22.97 ?  296 PRO A N   1 
ATOM   2296 C CA  . PRO A 1 322 ? 4.987   12.596  -30.093 1.00 22.03 ?  296 PRO A CA  1 
ATOM   2297 C C   . PRO A 1 322 ? 6.326   11.855  -30.048 1.00 24.58 ?  296 PRO A C   1 
ATOM   2298 O O   . PRO A 1 322 ? 7.346   12.487  -29.871 1.00 25.62 ?  296 PRO A O   1 
ATOM   2299 C CB  . PRO A 1 322 ? 4.794   13.263  -31.470 1.00 23.47 ?  296 PRO A CB  1 
ATOM   2300 C CG  . PRO A 1 322 ? 5.404   14.628  -31.289 1.00 25.41 ?  296 PRO A CG  1 
ATOM   2301 C CD  . PRO A 1 322 ? 5.009   15.024  -29.890 1.00 25.47 ?  296 PRO A CD  1 
ATOM   2302 N N   . HIS A 1 323 ? 6.304   10.539  -30.243 1.00 24.21 ?  297 HIS A N   1 
ATOM   2303 C CA  . HIS A 1 323 ? 7.511   9.685   -30.275 1.00 24.87 ?  297 HIS A CA  1 
ATOM   2304 C C   . HIS A 1 323 ? 7.395   8.734   -31.451 1.00 26.20 ?  297 HIS A C   1 
ATOM   2305 O O   . HIS A 1 323 ? 6.320   8.101   -31.577 1.00 23.30 ?  297 HIS A O   1 
ATOM   2306 C CB  . HIS A 1 323 ? 7.675   8.892   -28.964 1.00 25.06 ?  297 HIS A CB  1 
ATOM   2307 C CG  . HIS A 1 323 ? 7.962   9.773   -27.803 1.00 24.76 ?  297 HIS A CG  1 
ATOM   2308 N ND1 . HIS A 1 323 ? 6.958   10.408  -27.108 1.00 28.17 ?  297 HIS A ND1 1 
ATOM   2309 C CD2 . HIS A 1 323 ? 9.133   10.168  -27.254 1.00 26.49 ?  297 HIS A CD2 1 
ATOM   2310 C CE1 . HIS A 1 323 ? 7.490   11.211  -26.191 1.00 25.32 ?  297 HIS A CE1 1 
ATOM   2311 N NE2 . HIS A 1 323 ? 8.837   11.040  -26.231 1.00 26.91 ?  297 HIS A NE2 1 
ATOM   2312 N N   . ARG A 1 324 ? 8.450   8.610   -32.261 1.00 24.68 ?  298 ARG A N   1 
ATOM   2313 C CA  . ARG A 1 324 ? 8.460   7.660   -33.388 1.00 28.09 ?  298 ARG A CA  1 
ATOM   2314 C C   . ARG A 1 324 ? 8.464   6.277   -32.768 1.00 27.03 ?  298 ARG A C   1 
ATOM   2315 O O   . ARG A 1 324 ? 9.108   6.102   -31.742 1.00 30.36 ?  298 ARG A O   1 
ATOM   2316 C CB  . ARG A 1 324 ? 9.684   7.849   -34.290 1.00 36.28 ?  298 ARG A CB  1 
ATOM   2317 C CG  . ARG A 1 324 ? 9.665   9.155   -35.070 1.00 43.95 ?  298 ARG A CG  1 
ATOM   2318 C CD  . ARG A 1 324 ? 11.024  9.461   -35.674 1.00 48.35 ?  298 ARG A CD  1 
ATOM   2319 N NE  . ARG A 1 324 ? 10.947  10.511  -36.679 1.00 55.43 ?  298 ARG A NE  1 
ATOM   2320 C CZ  . ARG A 1 324 ? 10.422  10.363  -37.896 1.00 61.33 ?  298 ARG A CZ  1 
ATOM   2321 N NH1 . ARG A 1 324 ? 9.884   9.213   -38.275 1.00 62.61 ?  298 ARG A NH1 1 
ATOM   2322 N NH2 . ARG A 1 324 ? 10.420  11.383  -38.733 1.00 65.04 ?  298 ARG A NH2 1 
ATOM   2323 N N   . ILE A 1 325 ? 7.714   5.340   -33.325 1.00 26.88 ?  299 ILE A N   1 
ATOM   2324 C CA  . ILE A 1 325 ? 7.595   3.990   -32.719 1.00 28.52 ?  299 ILE A CA  1 
ATOM   2325 C C   . ILE A 1 325 ? 8.624   3.080   -33.390 1.00 30.74 ?  299 ILE A C   1 
ATOM   2326 O O   . ILE A 1 325 ? 9.003   3.364   -34.548 1.00 29.95 ?  299 ILE A O   1 
ATOM   2327 C CB  . ILE A 1 325 ? 6.163   3.450   -32.861 1.00 28.93 ?  299 ILE A CB  1 
ATOM   2328 C CG1 . ILE A 1 325 ? 5.842   3.116   -34.322 1.00 29.23 ?  299 ILE A CG1 1 
ATOM   2329 C CG2 . ILE A 1 325 ? 5.156   4.433   -32.266 1.00 27.07 ?  299 ILE A CG2 1 
ATOM   2330 C CD1 . ILE A 1 325 ? 4.649   2.242   -34.482 1.00 30.65 ?  299 ILE A CD1 1 
ATOM   2331 N N   . ALA A 1 326 ? 9.044   2.043   -32.678 1.00 26.47 ?  300 ALA A N   1 
ATOM   2332 C CA  . ALA A 1 326 ? 9.754   0.881   -33.229 1.00 29.41 ?  300 ALA A CA  1 
ATOM   2333 C C   . ALA A 1 326 ? 8.760   -0.286  -33.306 1.00 29.33 ?  300 ALA A C   1 
ATOM   2334 O O   . ALA A 1 326 ? 8.518   -0.947  -32.270 1.00 27.56 ?  300 ALA A O   1 
ATOM   2335 C CB  . ALA A 1 326 ? 10.949  0.584   -32.369 1.00 28.89 ?  300 ALA A CB  1 
ATOM   2336 N N   . ARG A 1 327 ? 8.179   -0.515  -34.485 1.00 31.46 ?  301 ARG A N   1 
ATOM   2337 C CA  . ARG A 1 327 ? 7.096   -1.514  -34.660 1.00 33.83 ?  301 ARG A CA  1 
ATOM   2338 C C   . ARG A 1 327 ? 7.707   -2.901  -34.459 1.00 33.65 ?  301 ARG A C   1 
ATOM   2339 O O   . ARG A 1 327 ? 8.859   -3.108  -34.835 1.00 32.36 ?  301 ARG A O   1 
ATOM   2340 C CB  . ARG A 1 327 ? 6.384   -1.371  -36.012 1.00 38.41 ?  301 ARG A CB  1 
ATOM   2341 C CG  . ARG A 1 327 ? 5.066   -2.136  -36.063 1.00 42.48 ?  301 ARG A CG  1 
ATOM   2342 C CD  . ARG A 1 327 ? 4.018   -1.720  -37.080 1.00 44.15 ?  301 ARG A CD  1 
ATOM   2343 N NE  . ARG A 1 327 ? 3.324   -0.457  -36.816 1.00 52.99 ?  301 ARG A NE  1 
ATOM   2344 C CZ  . ARG A 1 327 ? 2.379   -0.214  -35.882 1.00 56.10 ?  301 ARG A CZ  1 
ATOM   2345 N NH1 . ARG A 1 327 ? 1.975   -1.139  -35.028 1.00 52.49 ?  301 ARG A NH1 1 
ATOM   2346 N NH2 . ARG A 1 327 ? 1.849   0.996   -35.792 1.00 61.11 ?  301 ARG A NH2 1 
ATOM   2347 N N   . LEU A 1 328 ? 6.996   -3.796  -33.792 1.00 32.60 ?  302 LEU A N   1 
ATOM   2348 C CA  . LEU A 1 328 ? 7.477   -5.184  -33.621 1.00 31.79 ?  302 LEU A CA  1 
ATOM   2349 C C   . LEU A 1 328 ? 7.112   -5.995  -34.869 1.00 34.27 ?  302 LEU A C   1 
ATOM   2350 O O   . LEU A 1 328 ? 6.031   -5.825  -35.432 1.00 34.90 ?  302 LEU A O   1 
ATOM   2351 C CB  . LEU A 1 328 ? 6.864   -5.779  -32.365 1.00 30.12 ?  302 LEU A CB  1 
ATOM   2352 C CG  . LEU A 1 328 ? 7.176   -5.056  -31.060 1.00 29.87 ?  302 LEU A CG  1 
ATOM   2353 C CD1 . LEU A 1 328 ? 6.401   -5.705  -29.933 1.00 32.30 ?  302 LEU A CD1 1 
ATOM   2354 C CD2 . LEU A 1 328 ? 8.681   -5.060  -30.770 1.00 32.63 ?  302 LEU A CD2 1 
ATOM   2355 N N   . PRO A 1 329 ? 7.997   -6.910  -35.316 1.00 39.10 ?  303 PRO A N   1 
ATOM   2356 C CA  . PRO A 1 329 ? 7.709   -7.765  -36.469 1.00 43.54 ?  303 PRO A CA  1 
ATOM   2357 C C   . PRO A 1 329 ? 6.402   -8.552  -36.300 1.00 43.14 ?  303 PRO A C   1 
ATOM   2358 O O   . PRO A 1 329 ? 5.705   -8.732  -37.263 1.00 38.61 ?  303 PRO A O   1 
ATOM   2359 C CB  . PRO A 1 329 ? 8.895   -8.735  -36.512 1.00 44.76 ?  303 PRO A CB  1 
ATOM   2360 C CG  . PRO A 1 329 ? 9.472   -8.681  -35.113 1.00 46.06 ?  303 PRO A CG  1 
ATOM   2361 C CD  . PRO A 1 329 ? 9.289   -7.236  -34.694 1.00 42.78 ?  303 PRO A CD  1 
ATOM   2362 N N   . ALA A 1 330 ? 6.112   -9.011  -35.077 1.00 41.97 ?  304 ALA A N   1 
ATOM   2363 C CA  . ALA A 1 330 ? 4.845   -9.691  -34.722 1.00 41.14 ?  304 ALA A CA  1 
ATOM   2364 C C   . ALA A 1 330 ? 4.411   -9.224  -33.334 1.00 39.70 ?  304 ALA A C   1 
ATOM   2365 O O   . ALA A 1 330 ? 5.266   -8.893  -32.534 1.00 40.69 ?  304 ALA A O   1 
ATOM   2366 C CB  . ALA A 1 330 ? 5.045   -11.186 -34.754 1.00 38.28 ?  304 ALA A CB  1 
ATOM   2367 N N   . PRO A 1 331 ? 3.103   -9.158  -33.007 1.00 37.64 ?  305 PRO A N   1 
ATOM   2368 C CA  . PRO A 1 331 ? 2.690   -8.803  -31.646 1.00 36.77 ?  305 PRO A CA  1 
ATOM   2369 C C   . PRO A 1 331 ? 3.367   -9.706  -30.600 1.00 36.95 ?  305 PRO A C   1 
ATOM   2370 O O   . PRO A 1 331 ? 3.397   -10.898 -30.809 1.00 36.50 ?  305 PRO A O   1 
ATOM   2371 C CB  . PRO A 1 331 ? 1.170   -9.012  -31.650 1.00 37.41 ?  305 PRO A CB  1 
ATOM   2372 C CG  . PRO A 1 331 ? 0.765   -8.906  -33.119 1.00 40.63 ?  305 PRO A CG  1 
ATOM   2373 C CD  . PRO A 1 331 ? 1.973   -9.358  -33.919 1.00 39.97 ?  305 PRO A CD  1 
ATOM   2374 N N   . GLN A 1 332 ? 3.891   -9.136  -29.509 1.00 34.65 ?  306 GLN A N   1 
ATOM   2375 C CA  . GLN A 1 332 ? 4.640   -9.871  -28.441 1.00 34.78 ?  306 GLN A CA  1 
ATOM   2376 C C   . GLN A 1 332 ? 3.729   -10.156 -27.229 1.00 29.72 ?  306 GLN A C   1 
ATOM   2377 O O   . GLN A 1 332 ? 3.030   -9.246  -26.788 1.00 26.82 ?  306 GLN A O   1 
ATOM   2378 C CB  . GLN A 1 332 ? 5.830   -9.040  -27.972 1.00 37.29 ?  306 GLN A CB  1 
ATOM   2379 C CG  . GLN A 1 332 ? 7.171   -9.503  -28.510 1.00 45.51 ?  306 GLN A CG  1 
ATOM   2380 C CD  . GLN A 1 332 ? 8.261   -8.598  -27.999 1.00 48.65 ?  306 GLN A CD  1 
ATOM   2381 O OE1 . GLN A 1 332 ? 8.057   -7.813  -27.065 1.00 47.32 ?  306 GLN A OE1 1 
ATOM   2382 N NE2 . GLN A 1 332 ? 9.416   -8.673  -28.643 1.00 53.97 ?  306 GLN A NE2 1 
ATOM   2383 N N   . ALA A 1 333 ? 3.730   -11.382 -26.719 1.00 30.26 ?  307 ALA A N   1 
ATOM   2384 C CA  . ALA A 1 333 ? 3.050   -11.774 -25.465 1.00 28.81 ?  307 ALA A CA  1 
ATOM   2385 C C   . ALA A 1 333 ? 3.607   -10.915 -24.326 1.00 27.13 ?  307 ALA A C   1 
ATOM   2386 O O   . ALA A 1 333 ? 4.842   -10.907 -24.103 1.00 27.58 ?  307 ALA A O   1 
ATOM   2387 C CB  . ALA A 1 333 ? 3.220   -13.250 -25.192 1.00 27.25 ?  307 ALA A CB  1 
ATOM   2388 N N   . LEU A 1 334 ? 2.748   -10.168 -23.634 1.00 25.62 ?  308 LEU A N   1 
ATOM   2389 C CA  . LEU A 1 334 ? 3.186   -9.370  -22.452 1.00 22.77 ?  308 LEU A CA  1 
ATOM   2390 C C   . LEU A 1 334 ? 2.969   -10.225 -21.214 1.00 23.53 ?  308 LEU A C   1 
ATOM   2391 O O   . LEU A 1 334 ? 1.923   -10.120 -20.597 1.00 23.94 ?  308 LEU A O   1 
ATOM   2392 C CB  . LEU A 1 334 ? 2.426   -8.050  -22.410 1.00 23.94 ?  308 LEU A CB  1 
ATOM   2393 C CG  . LEU A 1 334 ? 2.594   -7.193  -23.663 1.00 22.44 ?  308 LEU A CG  1 
ATOM   2394 C CD1 . LEU A 1 334 ? 1.861   -5.893  -23.495 1.00 23.29 ?  308 LEU A CD1 1 
ATOM   2395 C CD2 . LEU A 1 334 ? 4.073   -6.953  -23.981 1.00 25.21 ?  308 LEU A CD2 1 
ATOM   2396 N N   . GLU A 1 335 ? 3.937   -11.090 -20.925 1.00 23.39 ?  309 GLU A N   1 
ATOM   2397 C CA  . GLU A 1 335 ? 3.891   -12.044 -19.803 1.00 27.19 ?  309 GLU A CA  1 
ATOM   2398 C C   . GLU A 1 335 ? 5.317   -12.305 -19.313 1.00 22.53 ?  309 GLU A C   1 
ATOM   2399 O O   . GLU A 1 335 ? 6.258   -11.653 -19.793 1.00 23.14 ?  309 GLU A O   1 
ATOM   2400 C CB  . GLU A 1 335 ? 3.204   -13.311 -20.300 1.00 28.86 ?  309 GLU A CB  1 
ATOM   2401 C CG  . GLU A 1 335 ? 4.075   -14.076 -21.267 1.00 35.44 ?  309 GLU A CG  1 
ATOM   2402 C CD  . GLU A 1 335 ? 3.349   -14.987 -22.230 1.00 44.97 ?  309 GLU A CD  1 
ATOM   2403 O OE1 . GLU A 1 335 ? 2.099   -15.193 -22.039 1.00 50.31 ?  309 GLU A OE1 1 
ATOM   2404 O OE2 . GLU A 1 335 ? 4.024   -15.446 -23.202 1.00 44.07 ?  309 GLU A OE2 1 
ATOM   2405 N N   . GLY A 1 336 ? 5.478   -13.203 -18.354 1.00 22.96 ?  310 GLY A N   1 
ATOM   2406 C CA  . GLY A 1 336 ? 6.805   -13.526 -17.786 1.00 22.39 ?  310 GLY A CA  1 
ATOM   2407 C C   . GLY A 1 336 ? 7.413   -12.356 -17.002 1.00 23.53 ?  310 GLY A C   1 
ATOM   2408 O O   . GLY A 1 336 ? 6.701   -11.697 -16.228 1.00 22.50 ?  310 GLY A O   1 
ATOM   2409 N N   . GLN A 1 337 ? 8.703   -12.098 -17.213 1.00 23.50 ?  311 GLN A N   1 
ATOM   2410 C CA  . GLN A 1 337 ? 9.531   -11.113 -16.463 1.00 26.03 ?  311 GLN A CA  1 
ATOM   2411 C C   . GLN A 1 337 ? 9.242   -9.719  -17.040 1.00 23.63 ?  311 GLN A C   1 
ATOM   2412 O O   . GLN A 1 337 ? 10.107  -9.092  -17.680 1.00 22.56 ?  311 GLN A O   1 
ATOM   2413 C CB  . GLN A 1 337 ? 11.013  -11.491 -16.589 1.00 31.01 ?  311 GLN A CB  1 
ATOM   2414 C CG  . GLN A 1 337 ? 11.301  -12.992 -16.468 1.00 35.09 ?  311 GLN A CG  1 
ATOM   2415 C CD  . GLN A 1 337 ? 12.511  -13.483 -17.251 1.00 48.57 ?  311 GLN A CD  1 
ATOM   2416 O OE1 . GLN A 1 337 ? 12.455  -13.870 -18.436 1.00 47.85 ?  311 GLN A OE1 1 
ATOM   2417 N NE2 . GLN A 1 337 ? 13.642  -13.517 -16.567 1.00 49.84 ?  311 GLN A NE2 1 
ATOM   2418 N N   . ARG A 1 338 ? 8.006   -9.264  -16.890 1.00 22.50 ?  312 ARG A N   1 
ATOM   2419 C CA  . ARG A 1 338 ? 7.647   -7.913  -17.344 1.00 25.27 ?  312 ARG A CA  1 
ATOM   2420 C C   . ARG A 1 338 ? 6.774   -7.292  -16.272 1.00 22.35 ?  312 ARG A C   1 
ATOM   2421 O O   . ARG A 1 338 ? 6.033   -8.033  -15.614 1.00 19.41 ?  312 ARG A O   1 
ATOM   2422 C CB  . ARG A 1 338 ? 6.862   -7.902  -18.652 1.00 26.10 ?  312 ARG A CB  1 
ATOM   2423 C CG  . ARG A 1 338 ? 7.654   -8.371  -19.858 1.00 33.94 ?  312 ARG A CG  1 
ATOM   2424 C CD  . ARG A 1 338 ? 6.672   -8.486  -20.970 1.00 38.46 ?  312 ARG A CD  1 
ATOM   2425 N NE  . ARG A 1 338 ? 7.122   -9.343  -22.058 1.00 44.02 ?  312 ARG A NE  1 
ATOM   2426 C CZ  . ARG A 1 338 ? 7.644   -8.894  -23.179 1.00 40.68 ?  312 ARG A CZ  1 
ATOM   2427 N NH1 . ARG A 1 338 ? 7.848   -7.597  -23.327 1.00 41.33 ?  312 ARG A NH1 1 
ATOM   2428 N NH2 . ARG A 1 338 ? 7.968   -9.749  -24.138 1.00 46.95 ?  312 ARG A NH2 1 
ATOM   2429 N N   . LEU A 1 339 ? 6.804   -5.965  -16.225 1.00 21.02 ?  313 LEU A N   1 
ATOM   2430 C CA  . LEU A 1 339 ? 5.893   -5.142  -15.421 1.00 19.50 ?  313 LEU A CA  1 
ATOM   2431 C C   . LEU A 1 339 ? 4.933   -4.440  -16.373 1.00 17.38 ?  313 LEU A C   1 
ATOM   2432 O O   . LEU A 1 339 ? 5.371   -3.737  -17.293 1.00 16.22 ?  313 LEU A O   1 
ATOM   2433 C CB  . LEU A 1 339 ? 6.711   -4.151  -14.589 1.00 22.37 ?  313 LEU A CB  1 
ATOM   2434 C CG  . LEU A 1 339 ? 5.856   -3.266  -13.690 1.00 27.03 ?  313 LEU A CG  1 
ATOM   2435 C CD1 . LEU A 1 339 ? 6.405   -3.220  -12.292 1.00 34.04 ?  313 LEU A CD1 1 
ATOM   2436 C CD2 . LEU A 1 339 ? 5.756   -1.865  -14.252 1.00 32.80 ?  313 LEU A CD2 1 
ATOM   2437 N N   . LEU A 1 340 ? 3.639   -4.720  -16.246 1.00 16.58 ?  314 LEU A N   1 
ATOM   2438 C CA  . LEU A 1 340 ? 2.563   -4.018  -16.982 1.00 17.43 ?  314 LEU A CA  1 
ATOM   2439 C C   . LEU A 1 340 ? 1.996   -2.962  -16.041 1.00 16.15 ?  314 LEU A C   1 
ATOM   2440 O O   . LEU A 1 340 ? 1.825   -3.261  -14.845 1.00 19.40 ?  314 LEU A O   1 
ATOM   2441 C CB  . LEU A 1 340 ? 1.443   -4.990  -17.343 1.00 17.21 ?  314 LEU A CB  1 
ATOM   2442 C CG  . LEU A 1 340 ? 1.722   -5.775  -18.623 1.00 18.92 ?  314 LEU A CG  1 
ATOM   2443 C CD1 . LEU A 1 340 ? 2.951   -6.653  -18.460 1.00 20.74 ?  314 LEU A CD1 1 
ATOM   2444 C CD2 . LEU A 1 340 ? 0.545   -6.608  -19.023 1.00 19.86 ?  314 LEU A CD2 1 
ATOM   2445 N N   . ASN A 1 341 ? 1.727   -1.779  -16.551 1.00 16.43 ?  315 ASN A N   1 
ATOM   2446 C CA  . ASN A 1 341 ? 1.326   -0.651  -15.672 1.00 17.02 ?  315 ASN A CA  1 
ATOM   2447 C C   . ASN A 1 341 ? 0.431   0.292   -16.463 1.00 16.50 ?  315 ASN A C   1 
ATOM   2448 O O   . ASN A 1 341 ? 0.355   0.214   -17.713 1.00 14.97 ?  315 ASN A O   1 
ATOM   2449 C CB  . ASN A 1 341 ? 2.558   -0.017  -15.024 1.00 16.86 ?  315 ASN A CB  1 
ATOM   2450 C CG  . ASN A 1 341 ? 3.346   1.000   -15.824 1.00 17.01 ?  315 ASN A CG  1 
ATOM   2451 O OD1 . ASN A 1 341 ? 4.204   1.664   -15.237 1.00 19.99 ?  315 ASN A OD1 1 
ATOM   2452 N ND2 . ASN A 1 341 ? 3.132   1.145   -17.120 1.00 17.57 ?  315 ASN A ND2 1 
ATOM   2453 N N   . LYS A 1 342 ? -0.257  1.137   -15.727 1.00 16.29 ?  316 LYS A N   1 
ATOM   2454 C CA  . LYS A 1 342 ? -0.984  2.272   -16.279 1.00 15.90 ?  316 LYS A CA  1 
ATOM   2455 C C   . LYS A 1 342 ? -1.107  3.345   -15.169 1.00 15.24 ?  316 LYS A C   1 
ATOM   2456 O O   . LYS A 1 342 ? -1.470  3.029   -14.015 1.00 17.50 ?  316 LYS A O   1 
ATOM   2457 C CB  . LYS A 1 342 ? -2.360  1.890   -16.818 1.00 16.30 ?  316 LYS A CB  1 
ATOM   2458 C CG  . LYS A 1 342 ? -2.976  3.012   -17.637 1.00 17.45 ?  316 LYS A CG  1 
ATOM   2459 C CD  . LYS A 1 342 ? -2.295  3.275   -18.949 1.00 17.72 ?  316 LYS A CD  1 
ATOM   2460 C CE  . LYS A 1 342 ? -2.735  4.540   -19.649 1.00 19.50 ?  316 LYS A CE  1 
ATOM   2461 N NZ  . LYS A 1 342 ? -2.214  5.773   -18.995 1.00 21.44 ?  316 LYS A NZ  1 
ATOM   2462 N N   . THR A 1 343 ? -0.803  4.582   -15.523 1.00 15.62 ?  317 THR A N   1 
ATOM   2463 C CA  . THR A 1 343 ? -1.060  5.745   -14.659 1.00 16.73 ?  317 THR A CA  1 
ATOM   2464 C C   . THR A 1 343 ? -2.450  6.278   -15.028 1.00 17.95 ?  317 THR A C   1 
ATOM   2465 O O   . THR A 1 343 ? -2.926  6.097   -16.177 1.00 18.89 ?  317 THR A O   1 
ATOM   2466 C CB  . THR A 1 343 ? -0.048  6.863   -14.871 1.00 17.38 ?  317 THR A CB  1 
ATOM   2467 O OG1 . THR A 1 343 ? -0.086  7.182   -16.276 1.00 18.75 ?  317 THR A OG1 1 
ATOM   2468 C CG2 . THR A 1 343 ? 1.326   6.471   -14.379 1.00 18.43 ?  317 THR A CG2 1 
ATOM   2469 N N   . GLY A 1 344 ? -3.083  6.971   -14.104 1.00 17.01 ?  318 GLY A N   1 
ATOM   2470 C CA  . GLY A 1 344 ? -4.346  7.643   -14.404 1.00 17.23 ?  318 GLY A CA  1 
ATOM   2471 C C   . GLY A 1 344 ? -4.500  8.860   -13.525 1.00 17.52 ?  318 GLY A C   1 
ATOM   2472 O O   . GLY A 1 344 ? -4.306  8.759   -12.337 1.00 18.20 ?  318 GLY A O   1 
ATOM   2473 N N   . SER A 1 345 ? -4.910  9.949   -14.123 1.00 18.62 ?  319 SER A N   1 
ATOM   2474 C CA  . SER A 1 345 ? -5.029  11.258  -13.453 1.00 19.72 ?  319 SER A CA  1 
ATOM   2475 C C   . SER A 1 345 ? -6.356  11.901  -13.834 1.00 21.46 ?  319 SER A C   1 
ATOM   2476 O O   . SER A 1 345 ? -6.754  11.814  -14.998 1.00 20.21 ?  319 SER A O   1 
ATOM   2477 C CB  . SER A 1 345 ? -3.881  12.135  -13.833 1.00 22.01 ?  319 SER A CB  1 
ATOM   2478 O OG  . SER A 1 345 ? -2.641  11.477  -13.610 1.00 20.69 ?  319 SER A OG  1 
ATOM   2479 N N   . THR A 1 346 ? -6.978  12.559  -12.862 1.00 18.85 ?  320 THR A N   1 
ATOM   2480 C CA  . THR A 1 346 ? -8.005  13.582  -13.102 1.00 19.47 ?  320 THR A CA  1 
ATOM   2481 C C   . THR A 1 346 ? -7.517  14.853  -12.382 1.00 22.29 ?  320 THR A C   1 
ATOM   2482 O O   . THR A 1 346 ? -6.440  14.828  -11.812 1.00 21.31 ?  320 THR A O   1 
ATOM   2483 C CB  . THR A 1 346 ? -9.396  13.176  -12.619 1.00 18.69 ?  320 THR A CB  1 
ATOM   2484 O OG1 . THR A 1 346 ? -9.381  12.984  -11.209 1.00 20.58 ?  320 THR A OG1 1 
ATOM   2485 C CG2 . THR A 1 346 ? -9.882  11.901  -13.255 1.00 19.94 ?  320 THR A CG2 1 
ATOM   2486 N N   . ASN A 1 347 ? -8.284  15.935  -12.417 1.00 22.46 ?  321 ASN A N   1 
ATOM   2487 C CA  . ASN A 1 347 ? -7.815  17.164  -11.740 1.00 23.43 ?  321 ASN A CA  1 
ATOM   2488 C C   . ASN A 1 347 ? -7.643  16.901  -10.240 1.00 24.06 ?  321 ASN A C   1 
ATOM   2489 O O   . ASN A 1 347 ? -6.772  17.556  -9.665  1.00 22.60 ?  321 ASN A O   1 
ATOM   2490 C CB  . ASN A 1 347 ? -8.771  18.314  -11.970 1.00 25.07 ?  321 ASN A CB  1 
ATOM   2491 C CG  . ASN A 1 347 ? -8.724  18.806  -13.389 1.00 26.11 ?  321 ASN A CG  1 
ATOM   2492 O OD1 . ASN A 1 347 ? -9.752  19.202  -13.918 1.00 32.93 ?  321 ASN A OD1 1 
ATOM   2493 N ND2 . ASN A 1 347 ? -7.546  18.769  -13.996 1.00 29.59 ?  321 ASN A ND2 1 
ATOM   2494 N N   . GLY A 1 348 ? -8.414  15.989  -9.631  1.00 21.91 ?  322 GLY A N   1 
ATOM   2495 C CA  . GLY A 1 348 ? -8.365  15.778  -8.169  1.00 19.71 ?  322 GLY A CA  1 
ATOM   2496 C C   . GLY A 1 348 ? -7.735  14.486  -7.715  1.00 19.93 ?  322 GLY A C   1 
ATOM   2497 O O   . GLY A 1 348 ? -7.679  14.268  -6.504  1.00 18.72 ?  322 GLY A O   1 
ATOM   2498 N N   . PHE A 1 349 ? -7.391  13.569  -8.630  1.00 18.05 ?  323 PHE A N   1 
ATOM   2499 C CA  . PHE A 1 349 ? -7.009  12.187  -8.254  1.00 18.63 ?  323 PHE A CA  1 
ATOM   2500 C C   . PHE A 1 349 ? -5.793  11.706  -9.049  1.00 16.02 ?  323 PHE A C   1 
ATOM   2501 O O   . PHE A 1 349 ? -5.577  12.133  -10.180 1.00 18.22 ?  323 PHE A O   1 
ATOM   2502 C CB  . PHE A 1 349 ? -8.170  11.239  -8.522  1.00 18.10 ?  323 PHE A CB  1 
ATOM   2503 C CG  . PHE A 1 349 ? -9.348  11.406  -7.595  1.00 17.40 ?  323 PHE A CG  1 
ATOM   2504 C CD1 . PHE A 1 349 ? -10.328 12.349  -7.862  1.00 20.97 ?  323 PHE A CD1 1 
ATOM   2505 C CD2 . PHE A 1 349 ? -9.524  10.583  -6.499  1.00 18.24 ?  323 PHE A CD2 1 
ATOM   2506 C CE1 . PHE A 1 349 ? -11.426 12.486  -7.034  1.00 18.28 ?  323 PHE A CE1 1 
ATOM   2507 C CE2 . PHE A 1 349 ? -10.639 10.696  -5.681  1.00 17.65 ?  323 PHE A CE2 1 
ATOM   2508 C CZ  . PHE A 1 349 ? -11.595 11.644  -5.952  1.00 17.61 ?  323 PHE A CZ  1 
ATOM   2509 N N   . GLY A 1 350 ? -5.053  10.808  -8.451  1.00 18.18 ?  324 GLY A N   1 
ATOM   2510 C CA  . GLY A 1 350 ? -3.805  10.237  -8.988  1.00 18.20 ?  324 GLY A CA  1 
ATOM   2511 C C   . GLY A 1 350 ? -3.785  8.752   -8.703  1.00 17.45 ?  324 GLY A C   1 
ATOM   2512 O O   . GLY A 1 350 ? -3.741  8.376   -7.513  1.00 18.41 ?  324 GLY A O   1 
ATOM   2513 N N   . ALA A 1 351 ? -3.864  7.920   -9.738  1.00 17.62 ?  325 ALA A N   1 
ATOM   2514 C CA  . ALA A 1 351 ? -3.914  6.440   -9.588  1.00 18.42 ?  325 ALA A CA  1 
ATOM   2515 C C   . ALA A 1 351 ? -2.730  5.797   -10.317 1.00 17.74 ?  325 ALA A C   1 
ATOM   2516 O O   . ALA A 1 351 ? -2.228  6.364   -11.314 1.00 17.05 ?  325 ALA A O   1 
ATOM   2517 C CB  . ALA A 1 351 ? -5.200  5.913   -10.182 1.00 19.97 ?  325 ALA A CB  1 
ATOM   2518 N N   . TYR A 1 352 ? -2.344  4.617   -9.865  1.00 17.57 ?  326 TYR A N   1 
ATOM   2519 C CA  . TYR A 1 352 ? -1.313  3.816   -10.536 1.00 18.23 ?  326 TYR A CA  1 
ATOM   2520 C C   . TYR A 1 352 ? -1.652  2.364   -10.294 1.00 17.53 ?  326 TYR A C   1 
ATOM   2521 O O   . TYR A 1 352 ? -1.970  1.990   -9.161  1.00 18.21 ?  326 TYR A O   1 
ATOM   2522 C CB  . TYR A 1 352 ? 0.075   4.226   -10.075 1.00 19.40 ?  326 TYR A CB  1 
ATOM   2523 C CG  . TYR A 1 352 ? 1.195   3.489   -10.754 1.00 17.81 ?  326 TYR A CG  1 
ATOM   2524 C CD1 . TYR A 1 352 ? 1.436   3.647   -12.108 1.00 19.15 ?  326 TYR A CD1 1 
ATOM   2525 C CD2 . TYR A 1 352 ? 2.017   2.619   -10.052 1.00 22.43 ?  326 TYR A CD2 1 
ATOM   2526 C CE1 . TYR A 1 352 ? 2.512   3.021   -12.721 1.00 20.88 ?  326 TYR A CE1 1 
ATOM   2527 C CE2 . TYR A 1 352 ? 3.073   1.966   -10.666 1.00 22.11 ?  326 TYR A CE2 1 
ATOM   2528 C CZ  . TYR A 1 352 ? 3.313   2.146   -12.018 1.00 21.54 ?  326 TYR A CZ  1 
ATOM   2529 O OH  . TYR A 1 352 ? 4.358   1.486   -12.649 1.00 19.69 ?  326 TYR A OH  1 
ATOM   2530 N N   . VAL A 1 353 ? -1.525  1.579   -11.349 1.00 17.47 ?  327 VAL A N   1 
ATOM   2531 C CA  . VAL A 1 353 ? -1.663  0.104   -11.228 1.00 18.04 ?  327 VAL A CA  1 
ATOM   2532 C C   . VAL A 1 353 ? -0.462  -0.545  -11.923 1.00 19.02 ?  327 VAL A C   1 
ATOM   2533 O O   . VAL A 1 353 ? -0.059  -0.087  -13.027 1.00 16.76 ?  327 VAL A O   1 
ATOM   2534 C CB  . VAL A 1 353 ? -2.956  -0.377  -11.911 1.00 19.69 ?  327 VAL A CB  1 
ATOM   2535 C CG1 . VAL A 1 353 ? -3.026  -1.894  -11.845 1.00 21.35 ?  327 VAL A CG1 1 
ATOM   2536 C CG2 . VAL A 1 353 ? -4.198  0.258   -11.340 1.00 21.08 ?  327 VAL A CG2 1 
ATOM   2537 N N   . ALA A 1 354 ? 0.068   -1.621  -11.350 1.00 18.99 ?  328 ALA A N   1 
ATOM   2538 C CA  . ALA A 1 354 ? 1.190   -2.352  -11.940 1.00 18.93 ?  328 ALA A CA  1 
ATOM   2539 C C   . ALA A 1 354 ? 1.074   -3.829  -11.558 1.00 19.39 ?  328 ALA A C   1 
ATOM   2540 O O   . ALA A 1 354 ? 0.673   -4.140  -10.434 1.00 20.68 ?  328 ALA A O   1 
ATOM   2541 C CB  . ALA A 1 354 ? 2.495   -1.756  -11.515 1.00 19.99 ?  328 ALA A CB  1 
ATOM   2542 N N   . PHE A 1 355 ? 1.413   -4.723  -12.467 1.00 17.62 ?  329 PHE A N   1 
ATOM   2543 C CA  . PHE A 1 355 ? 1.476   -6.153  -12.090 1.00 19.22 ?  329 PHE A CA  1 
ATOM   2544 C C   . PHE A 1 355 ? 2.613   -6.807  -12.862 1.00 19.72 ?  329 PHE A C   1 
ATOM   2545 O O   . PHE A 1 355 ? 2.987   -6.335  -13.959 1.00 18.11 ?  329 PHE A O   1 
ATOM   2546 C CB  . PHE A 1 355 ? 0.124   -6.833  -12.307 1.00 19.39 ?  329 PHE A CB  1 
ATOM   2547 C CG  . PHE A 1 355 ? -0.440  -6.791  -13.710 1.00 19.79 ?  329 PHE A CG  1 
ATOM   2548 C CD1 . PHE A 1 355 ? -1.110  -5.672  -14.169 1.00 20.21 ?  329 PHE A CD1 1 
ATOM   2549 C CD2 . PHE A 1 355 ? -0.395  -7.901  -14.540 1.00 20.07 ?  329 PHE A CD2 1 
ATOM   2550 C CE1 . PHE A 1 355 ? -1.649  -5.638  -15.442 1.00 18.95 ?  329 PHE A CE1 1 
ATOM   2551 C CE2 . PHE A 1 355 ? -0.909  -7.849  -15.829 1.00 19.44 ?  329 PHE A CE2 1 
ATOM   2552 C CZ  . PHE A 1 355 ? -1.593  -6.742  -16.258 1.00 19.68 ?  329 PHE A CZ  1 
ATOM   2553 N N   . VAL A 1 356 ? 3.099   -7.902  -12.295 1.00 19.66 ?  330 VAL A N   1 
ATOM   2554 C CA  . VAL A 1 356 ? 4.206   -8.703  -12.867 1.00 21.64 ?  330 VAL A CA  1 
ATOM   2555 C C   . VAL A 1 356 ? 3.672   -10.110 -13.116 1.00 20.04 ?  330 VAL A C   1 
ATOM   2556 O O   . VAL A 1 356 ? 3.586   -10.881 -12.165 1.00 23.08 ?  330 VAL A O   1 
ATOM   2557 C CB  . VAL A 1 356 ? 5.430   -8.692  -11.935 1.00 22.31 ?  330 VAL A CB  1 
ATOM   2558 C CG1 . VAL A 1 356 ? 6.558   -9.507  -12.564 1.00 24.24 ?  330 VAL A CG1 1 
ATOM   2559 C CG2 . VAL A 1 356 ? 5.865   -7.261  -11.614 1.00 21.99 ?  330 VAL A CG2 1 
ATOM   2560 N N   . PRO A 1 357 ? 3.243   -10.444 -14.355 1.00 20.14 ?  331 PRO A N   1 
ATOM   2561 C CA  . PRO A 1 357 ? 2.596   -11.731 -14.622 1.00 20.75 ?  331 PRO A CA  1 
ATOM   2562 C C   . PRO A 1 357 ? 3.405   -12.930 -14.120 1.00 23.78 ?  331 PRO A C   1 
ATOM   2563 O O   . PRO A 1 357 ? 2.808   -13.825 -13.488 1.00 23.96 ?  331 PRO A O   1 
ATOM   2564 C CB  . PRO A 1 357 ? 2.420   -11.715 -16.149 1.00 23.37 ?  331 PRO A CB  1 
ATOM   2565 C CG  . PRO A 1 357 ? 2.237   -10.247 -16.451 1.00 23.53 ?  331 PRO A CG  1 
ATOM   2566 C CD  . PRO A 1 357 ? 3.249   -9.572  -15.548 1.00 22.62 ?  331 PRO A CD  1 
ATOM   2567 N N   . GLY A 1 358 ? 4.731   -12.910 -14.356 1.00 24.31 ?  332 GLY A N   1 
ATOM   2568 C CA  . GLY A 1 358 ? 5.646   -14.036 -14.087 1.00 23.89 ?  332 GLY A CA  1 
ATOM   2569 C C   . GLY A 1 358 ? 5.879   -14.221 -12.596 1.00 26.06 ?  332 GLY A C   1 
ATOM   2570 O O   . GLY A 1 358 ? 6.479   -15.195 -12.230 1.00 28.65 ?  332 GLY A O   1 
ATOM   2571 N N   . ARG A 1 359 ? 5.455   -13.281 -11.754 1.00 26.16 ?  333 ARG A N   1 
ATOM   2572 C CA  . ARG A 1 359 ? 5.625   -13.363 -10.276 1.00 26.10 ?  333 ARG A CA  1 
ATOM   2573 C C   . ARG A 1 359 ? 4.285   -13.358 -9.544  1.00 22.78 ?  333 ARG A C   1 
ATOM   2574 O O   . ARG A 1 359 ? 4.325   -13.363 -8.287  1.00 23.53 ?  333 ARG A O   1 
ATOM   2575 C CB  . ARG A 1 359 ? 6.490   -12.211 -9.768  1.00 29.18 ?  333 ARG A CB  1 
ATOM   2576 C CG  . ARG A 1 359 ? 7.913   -12.264 -10.313 1.00 34.38 ?  333 ARG A CG  1 
ATOM   2577 C CD  . ARG A 1 359 ? 8.775   -13.197 -9.481  1.00 41.87 ?  333 ARG A CD  1 
ATOM   2578 N NE  . ARG A 1 359 ? 10.109  -13.365 -10.058 1.00 44.11 ?  333 ARG A NE  1 
ATOM   2579 C CZ  . ARG A 1 359 ? 10.422  -14.221 -11.030 1.00 46.81 ?  333 ARG A CZ  1 
ATOM   2580 N NH1 . ARG A 1 359 ? 9.504   -15.016 -11.558 1.00 47.69 ?  333 ARG A NH1 1 
ATOM   2581 N NH2 . ARG A 1 359 ? 11.662  -14.268 -11.485 1.00 49.77 ?  333 ARG A NH2 1 
ATOM   2582 N N   . ASP A 1 360 ? 3.151   -13.394 -10.257 1.00 25.56 ?  334 ASP A N   1 
ATOM   2583 C CA  . ASP A 1 360 ? 1.795   -13.454 -9.631  1.00 26.18 ?  334 ASP A CA  1 
ATOM   2584 C C   . ASP A 1 360 ? 1.694   -12.319 -8.585  1.00 25.65 ?  334 ASP A C   1 
ATOM   2585 O O   . ASP A 1 360 ? 1.273   -12.564 -7.440  1.00 22.67 ?  334 ASP A O   1 
ATOM   2586 C CB  . ASP A 1 360 ? 1.521   -14.861 -9.076  1.00 27.12 ?  334 ASP A CB  1 
ATOM   2587 C CG  . ASP A 1 360 ? 0.048   -15.222 -8.995  1.00 32.55 ?  334 ASP A CG  1 
ATOM   2588 O OD1 . ASP A 1 360 ? -0.768  -14.503 -9.611  1.00 31.53 ?  334 ASP A OD1 1 
ATOM   2589 O OD2 . ASP A 1 360 ? -0.287  -16.195 -8.275  1.00 35.86 ?  334 ASP A OD2 1 
ATOM   2590 N N   . LEU A 1 361 ? 2.110   -11.105 -8.973  1.00 24.88 ?  335 LEU A N   1 
ATOM   2591 C CA  . LEU A 1 361 ? 2.280   -9.900  -8.098  1.00 26.52 ?  335 LEU A CA  1 
ATOM   2592 C C   . LEU A 1 361 ? 1.464   -8.790  -8.741  1.00 23.92 ?  335 LEU A C   1 
ATOM   2593 O O   . LEU A 1 361 ? 1.615   -8.568  -9.962  1.00 20.81 ?  335 LEU A O   1 
ATOM   2594 C CB  . LEU A 1 361 ? 3.724   -9.360  -8.073  1.00 31.79 ?  335 LEU A CB  1 
ATOM   2595 C CG  . LEU A 1 361 ? 4.782   -10.016 -7.200  1.00 37.96 ?  335 LEU A CG  1 
ATOM   2596 C CD1 . LEU A 1 361 ? 5.984   -9.074  -7.095  1.00 37.66 ?  335 LEU A CD1 1 
ATOM   2597 C CD2 . LEU A 1 361 ? 4.248   -10.372 -5.819  1.00 45.00 ?  335 LEU A CD2 1 
ATOM   2598 N N   . GLY A 1 362 ? 0.657   -8.127  -7.940  1.00 22.74 ?  336 GLY A N   1 
ATOM   2599 C CA  . GLY A 1 362 ? -0.214  -7.043  -8.394  1.00 23.41 ?  336 GLY A CA  1 
ATOM   2600 C C   . GLY A 1 362 ? -0.257  -5.941  -7.369  1.00 20.01 ?  336 GLY A C   1 
ATOM   2601 O O   . GLY A 1 362 ? -0.220  -6.241  -6.166  1.00 20.05 ?  336 GLY A O   1 
ATOM   2602 N N   . LEU A 1 363 ? -0.464  -4.728  -7.829  1.00 18.92 ?  337 LEU A N   1 
ATOM   2603 C CA  A LEU A 1 363 ? -0.426  -3.537  -6.950  0.70 20.69 ?  337 LEU A CA  1 
ATOM   2604 C CA  B LEU A 1 363 ? -0.378  -3.516  -6.978  0.30 19.39 ?  337 LEU A CA  1 
ATOM   2605 C C   . LEU A 1 363 ? -1.332  -2.440  -7.505  1.00 19.36 ?  337 LEU A C   1 
ATOM   2606 O O   . LEU A 1 363 ? -1.305  -2.180  -8.745  1.00 18.93 ?  337 LEU A O   1 
ATOM   2607 C CB  A LEU A 1 363 ? 1.038   -3.087  -6.923  0.70 27.12 ?  337 LEU A CB  1 
ATOM   2608 C CB  B LEU A 1 363 ? 1.086   -3.067  -7.043  0.30 21.01 ?  337 LEU A CB  1 
ATOM   2609 C CG  A LEU A 1 363 ? 1.386   -1.826  -6.159  0.70 32.38 ?  337 LEU A CG  1 
ATOM   2610 C CG  B LEU A 1 363 ? 1.476   -1.816  -6.275  0.30 21.81 ?  337 LEU A CG  1 
ATOM   2611 C CD1 A LEU A 1 363 ? 0.843   -1.892  -4.743  0.70 33.84 ?  337 LEU A CD1 1 
ATOM   2612 C CD1 B LEU A 1 363 ? 2.795   -2.051  -5.532  0.30 21.93 ?  337 LEU A CD1 1 
ATOM   2613 C CD2 A LEU A 1 363 ? 2.909   -1.650  -6.145  0.70 34.69 ?  337 LEU A CD2 1 
ATOM   2614 C CD2 B LEU A 1 363 ? 1.583   -0.629  -7.222  0.30 21.18 ?  337 LEU A CD2 1 
ATOM   2615 N N   . VAL A 1 364 ? -2.056  -1.781  -6.596  1.00 18.37 ?  338 VAL A N   1 
ATOM   2616 C CA  . VAL A 1 364 ? -2.990  -0.682  -6.887  1.00 17.10 ?  338 VAL A CA  1 
ATOM   2617 C C   . VAL A 1 364 ? -2.659  0.410   -5.865  1.00 17.38 ?  338 VAL A C   1 
ATOM   2618 O O   . VAL A 1 364 ? -2.543  0.077   -4.686  1.00 15.56 ?  338 VAL A O   1 
ATOM   2619 C CB  . VAL A 1 364 ? -4.447  -1.179  -6.740  1.00 17.09 ?  338 VAL A CB  1 
ATOM   2620 C CG1 . VAL A 1 364 ? -5.420  -0.061  -6.553  1.00 19.70 ?  338 VAL A CG1 1 
ATOM   2621 C CG2 . VAL A 1 364 ? -4.861  -2.096  -7.871  1.00 19.51 ?  338 VAL A CG2 1 
ATOM   2622 N N   . ILE A 1 365 ? -2.458  1.635   -6.353  1.00 17.57 ?  339 ILE A N   1 
ATOM   2623 C CA  . ILE A 1 365 ? -2.227  2.831   -5.487  1.00 16.39 ?  339 ILE A CA  1 
ATOM   2624 C C   . ILE A 1 365 ? -3.177  3.924   -5.945  1.00 15.90 ?  339 ILE A C   1 
ATOM   2625 O O   . ILE A 1 365 ? -2.992  4.422   -7.083  1.00 17.09 ?  339 ILE A O   1 
ATOM   2626 C CB  . ILE A 1 365 ? -0.770  3.317   -5.580  1.00 17.81 ?  339 ILE A CB  1 
ATOM   2627 C CG1 . ILE A 1 365 ? 0.236   2.198   -5.312  1.00 19.00 ?  339 ILE A CG1 1 
ATOM   2628 C CG2 . ILE A 1 365 ? -0.567  4.491   -4.615  1.00 19.94 ?  339 ILE A CG2 1 
ATOM   2629 C CD1 . ILE A 1 365 ? 1.668   2.547   -5.638  1.00 21.02 ?  339 ILE A CD1 1 
ATOM   2630 N N   . LEU A 1 366 ? -4.199  4.209   -5.136  1.00 17.10 ?  340 LEU A N   1 
ATOM   2631 C CA  . LEU A 1 366 ? -5.237  5.221   -5.430  1.00 15.25 ?  340 LEU A CA  1 
ATOM   2632 C C   . LEU A 1 366 ? -5.131  6.376   -4.442  1.00 15.59 ?  340 LEU A C   1 
ATOM   2633 O O   . LEU A 1 366 ? -5.164  6.115   -3.248  1.00 16.91 ?  340 LEU A O   1 
ATOM   2634 C CB  . LEU A 1 366 ? -6.608  4.558   -5.322  1.00 15.72 ?  340 LEU A CB  1 
ATOM   2635 C CG  . LEU A 1 366 ? -6.819  3.389   -6.274  1.00 16.12 ?  340 LEU A CG  1 
ATOM   2636 C CD1 . LEU A 1 366 ? -8.234  2.829   -6.137  1.00 16.87 ?  340 LEU A CD1 1 
ATOM   2637 C CD2 . LEU A 1 366 ? -6.575  3.819   -7.696  1.00 15.29 ?  340 LEU A CD2 1 
ATOM   2638 N N   . ALA A 1 367 ? -5.098  7.594   -4.940  1.00 17.29 ?  341 ALA A N   1 
ATOM   2639 C CA  . ALA A 1 367 ? -4.942  8.805   -4.105  1.00 18.01 ?  341 ALA A CA  1 
ATOM   2640 C C   . ALA A 1 367 ? -5.923  9.872   -4.551  1.00 17.57 ?  341 ALA A C   1 
ATOM   2641 O O   . ALA A 1 367 ? -6.270  9.890   -5.746  1.00 17.51 ?  341 ALA A O   1 
ATOM   2642 C CB  . ALA A 1 367 ? -3.533  9.345   -4.198  1.00 19.25 ?  341 ALA A CB  1 
ATOM   2643 N N   . ASN A 1 368 ? -6.305  10.750  -3.611  1.00 18.63 ?  342 ASN A N   1 
ATOM   2644 C CA  . ASN A 1 368 ? -7.226  11.886  -3.909  1.00 19.74 ?  342 ASN A CA  1 
ATOM   2645 C C   . ASN A 1 368 ? -6.432  13.184  -4.007  1.00 21.32 ?  342 ASN A C   1 
ATOM   2646 O O   . ASN A 1 368 ? -6.967  14.256  -3.616  1.00 20.50 ?  342 ASN A O   1 
ATOM   2647 C CB  . ASN A 1 368 ? -8.418  12.003  -2.961  1.00 20.22 ?  342 ASN A CB  1 
ATOM   2648 C CG  . ASN A 1 368 ? -8.022  12.098  -1.498  1.00 19.35 ?  342 ASN A CG  1 
ATOM   2649 O OD1 . ASN A 1 368 ? -6.842  12.042  -1.177  1.00 20.53 ?  342 ASN A OD1 1 
ATOM   2650 N ND2 . ASN A 1 368 ? -8.995  12.229  -0.621  1.00 21.68 ?  342 ASN A ND2 1 
ATOM   2651 N N   . ARG A 1 369 ? -5.231  13.084  -4.569  1.00 20.64 ?  343 ARG A N   1 
ATOM   2652 C CA  . ARG A 1 369 ? -4.553  14.231  -5.221  1.00 23.55 ?  343 ARG A CA  1 
ATOM   2653 C C   . ARG A 1 369 ? -3.906  13.788  -6.541  1.00 21.90 ?  343 ARG A C   1 
ATOM   2654 O O   . ARG A 1 369 ? -3.430  12.653  -6.602  1.00 20.49 ?  343 ARG A O   1 
ATOM   2655 C CB  . ARG A 1 369 ? -3.519  14.859  -4.280  1.00 26.09 ?  343 ARG A CB  1 
ATOM   2656 C CG  . ARG A 1 369 ? -3.027  16.181  -4.846  1.00 28.02 ?  343 ARG A CG  1 
ATOM   2657 C CD  . ARG A 1 369 ? -2.127  16.971  -3.939  1.00 31.13 ?  343 ARG A CD  1 
ATOM   2658 N NE  . ARG A 1 369 ? -2.696  17.291  -2.647  1.00 29.58 ?  343 ARG A NE  1 
ATOM   2659 C CZ  . ARG A 1 369 ? -3.512  18.305  -2.375  1.00 29.09 ?  343 ARG A CZ  1 
ATOM   2660 N NH1 . ARG A 1 369 ? -3.988  19.080  -3.329  1.00 30.26 ?  343 ARG A NH1 1 
ATOM   2661 N NH2 . ARG A 1 369 ? -3.871  18.509  -1.120  1.00 29.19 ?  343 ARG A NH2 1 
ATOM   2662 N N   . ASN A 1 370 ? -3.876  14.672  -7.538  1.00 21.15 ?  344 ASN A N   1 
ATOM   2663 C CA  . ASN A 1 370 ? -3.114  14.453  -8.793  1.00 20.67 ?  344 ASN A CA  1 
ATOM   2664 C C   . ASN A 1 370 ? -1.651  14.801  -8.498  1.00 20.98 ?  344 ASN A C   1 
ATOM   2665 O O   . ASN A 1 370 ? -1.224  15.901  -8.879  1.00 24.35 ?  344 ASN A O   1 
ATOM   2666 C CB  . ASN A 1 370 ? -3.666  15.279  -9.949  1.00 21.37 ?  344 ASN A CB  1 
ATOM   2667 C CG  . ASN A 1 370 ? -2.950  15.021  -11.262 1.00 23.85 ?  344 ASN A CG  1 
ATOM   2668 O OD1 . ASN A 1 370 ? -2.041  14.204  -11.326 1.00 24.48 ?  344 ASN A OD1 1 
ATOM   2669 N ND2 . ASN A 1 370 ? -3.264  15.774  -12.304 1.00 27.03 ?  344 ASN A ND2 1 
ATOM   2670 N N   . TYR A 1 371 ? -0.940  13.863  -7.909  1.00 17.97 ?  345 TYR A N   1 
ATOM   2671 C CA  . TYR A 1 371 ? 0.492   13.968  -7.556  1.00 19.31 ?  345 TYR A CA  1 
ATOM   2672 C C   . TYR A 1 371 ? 1.336   13.345  -8.650  1.00 20.73 ?  345 TYR A C   1 
ATOM   2673 O O   . TYR A 1 371 ? 0.869   12.552  -9.471  1.00 19.09 ?  345 TYR A O   1 
ATOM   2674 C CB  . TYR A 1 371 ? 0.737   13.447  -6.141  1.00 19.29 ?  345 TYR A CB  1 
ATOM   2675 C CG  . TYR A 1 371 ? 0.730   11.949  -5.986  1.00 19.38 ?  345 TYR A CG  1 
ATOM   2676 C CD1 . TYR A 1 371 ? -0.449  11.231  -6.094  1.00 18.58 ?  345 TYR A CD1 1 
ATOM   2677 C CD2 . TYR A 1 371 ? 1.892   11.243  -5.711  1.00 18.18 ?  345 TYR A CD2 1 
ATOM   2678 C CE1 . TYR A 1 371 ? -0.462  9.860   -5.916  1.00 17.54 ?  345 TYR A CE1 1 
ATOM   2679 C CE2 . TYR A 1 371 ? 1.891   9.871   -5.492  1.00 17.81 ?  345 TYR A CE2 1 
ATOM   2680 C CZ  . TYR A 1 371 ? 0.707   9.173   -5.636  1.00 18.60 ?  345 TYR A CZ  1 
ATOM   2681 O OH  . TYR A 1 371 ? 0.688   7.818   -5.493  1.00 19.58 ?  345 TYR A OH  1 
ATOM   2682 N N   . PRO A 1 372 ? 2.581   13.817  -8.832  1.00 21.76 ?  346 PRO A N   1 
ATOM   2683 C CA  . PRO A 1 372 ? 3.346   13.429  -10.013 1.00 20.78 ?  346 PRO A CA  1 
ATOM   2684 C C   . PRO A 1 372 ? 3.484   11.920  -10.217 1.00 18.28 ?  346 PRO A C   1 
ATOM   2685 O O   . PRO A 1 372 ? 3.686   11.154  -9.256  1.00 17.55 ?  346 PRO A O   1 
ATOM   2686 C CB  . PRO A 1 372 ? 4.713   14.078  -9.776  1.00 23.16 ?  346 PRO A CB  1 
ATOM   2687 C CG  . PRO A 1 372 ? 4.358   15.317  -8.942  1.00 24.36 ?  346 PRO A CG  1 
ATOM   2688 C CD  . PRO A 1 372 ? 3.252   14.855  -8.023  1.00 24.60 ?  346 PRO A CD  1 
ATOM   2689 N N   . ASN A 1 373 ? 3.433   11.514  -11.483 1.00 18.13 ?  347 ASN A N   1 
ATOM   2690 C CA  . ASN A 1 373 ? 3.597   10.078  -11.813 1.00 18.17 ?  347 ASN A CA  1 
ATOM   2691 C C   . ASN A 1 373 ? 4.915   9.555   -11.246 1.00 18.30 ?  347 ASN A C   1 
ATOM   2692 O O   . ASN A 1 373 ? 4.931   8.434   -10.718 1.00 18.77 ?  347 ASN A O   1 
ATOM   2693 C CB  . ASN A 1 373 ? 3.541   9.907   -13.328 1.00 18.36 ?  347 ASN A CB  1 
ATOM   2694 C CG  . ASN A 1 373 ? 2.143   10.005  -13.887 1.00 21.45 ?  347 ASN A CG  1 
ATOM   2695 O OD1 . ASN A 1 373 ? 1.174   9.919   -13.145 1.00 22.37 ?  347 ASN A OD1 1 
ATOM   2696 N ND2 . ASN A 1 373 ? 2.033   10.130  -15.203 1.00 24.23 ?  347 ASN A ND2 1 
ATOM   2697 N N   . ALA A 1 374 ? 6.000   10.350  -11.251 1.00 17.44 ?  348 ALA A N   1 
ATOM   2698 C CA  . ALA A 1 374 ? 7.297   9.877   -10.722 1.00 18.85 ?  348 ALA A CA  1 
ATOM   2699 C C   . ALA A 1 374 ? 7.153   9.395   -9.268  1.00 18.56 ?  348 ALA A C   1 
ATOM   2700 O O   . ALA A 1 374 ? 7.825   8.475   -8.846  1.00 18.73 ?  348 ALA A O   1 
ATOM   2701 C CB  . ALA A 1 374 ? 8.307   10.989  -10.798 1.00 19.64 ?  348 ALA A CB  1 
ATOM   2702 N N   . GLU A 1 375 ? 6.305   10.075  -8.493  1.00 19.00 ?  349 GLU A N   1 
ATOM   2703 C CA  . GLU A 1 375 ? 6.089   9.787   -7.065  1.00 19.26 ?  349 GLU A CA  1 
ATOM   2704 C C   . GLU A 1 375 ? 5.240   8.518   -6.913  1.00 18.03 ?  349 GLU A C   1 
ATOM   2705 O O   . GLU A 1 375 ? 5.459   7.788   -5.974  1.00 19.00 ?  349 GLU A O   1 
ATOM   2706 C CB  . GLU A 1 375 ? 5.463   11.016  -6.402  1.00 20.81 ?  349 GLU A CB  1 
ATOM   2707 C CG  . GLU A 1 375 ? 6.408   12.194  -6.366  1.00 23.31 ?  349 GLU A CG  1 
ATOM   2708 C CD  . GLU A 1 375 ? 7.517   12.070  -5.328  1.00 24.61 ?  349 GLU A CD  1 
ATOM   2709 O OE1 . GLU A 1 375 ? 7.216   11.800  -4.125  1.00 25.25 ?  349 GLU A OE1 1 
ATOM   2710 O OE2 . GLU A 1 375 ? 8.695   12.240  -5.702  1.00 26.49 ?  349 GLU A OE2 1 
ATOM   2711 N N   . ARG A 1 376 ? 4.259   8.306   -7.782  1.00 19.43 ?  350 ARG A N   1 
ATOM   2712 C CA  . ARG A 1 376 ? 3.431   7.073   -7.755  1.00 18.44 ?  350 ARG A CA  1 
ATOM   2713 C C   . ARG A 1 376 ? 4.328   5.869   -8.049  1.00 18.36 ?  350 ARG A C   1 
ATOM   2714 O O   . ARG A 1 376 ? 4.265   4.848   -7.317  1.00 17.58 ?  350 ARG A O   1 
ATOM   2715 C CB  . ARG A 1 376 ? 2.327   7.114   -8.800  1.00 18.96 ?  350 ARG A CB  1 
ATOM   2716 C CG  . ARG A 1 376 ? 1.499   8.375   -8.750  1.00 18.46 ?  350 ARG A CG  1 
ATOM   2717 C CD  . ARG A 1 376 ? 0.402   8.443   -9.798  1.00 19.37 ?  350 ARG A CD  1 
ATOM   2718 N NE  . ARG A 1 376 ? -0.014  9.814   -9.970  1.00 18.50 ?  350 ARG A NE  1 
ATOM   2719 C CZ  . ARG A 1 376 ? -0.904  10.206  -10.858 1.00 20.27 ?  350 ARG A CZ  1 
ATOM   2720 N NH1 . ARG A 1 376 ? -1.594  9.316   -11.566 1.00 19.17 ?  350 ARG A NH1 1 
ATOM   2721 N NH2 . ARG A 1 376 ? -1.156  11.496  -11.006 1.00 21.11 ?  350 ARG A NH2 1 
ATOM   2722 N N   . VAL A 1 377 ? 5.150   5.983   -9.072  1.00 19.34 ?  351 VAL A N   1 
ATOM   2723 C CA  . VAL A 1 377 ? 6.126   4.916   -9.431  1.00 21.78 ?  351 VAL A CA  1 
ATOM   2724 C C   . VAL A 1 377 ? 7.109   4.703   -8.263  1.00 21.44 ?  351 VAL A C   1 
ATOM   2725 O O   . VAL A 1 377 ? 7.410   3.537   -7.982  1.00 20.40 ?  351 VAL A O   1 
ATOM   2726 C CB  . VAL A 1 377 ? 6.805   5.254   -10.763 1.00 22.64 ?  351 VAL A CB  1 
ATOM   2727 C CG1 . VAL A 1 377 ? 7.848   4.215   -11.143 1.00 23.58 ?  351 VAL A CG1 1 
ATOM   2728 C CG2 . VAL A 1 377 ? 5.748   5.395   -11.838 1.00 24.80 ?  351 VAL A CG2 1 
ATOM   2729 N N   . LYS A 1 378 ? 7.558   5.767   -7.584  1.00 21.83 ?  352 LYS A N   1 
ATOM   2730 C CA  . LYS A 1 378 ? 8.465   5.663   -6.398  1.00 23.96 ?  352 LYS A CA  1 
ATOM   2731 C C   . LYS A 1 378 ? 7.846   4.745   -5.325  1.00 21.11 ?  352 LYS A C   1 
ATOM   2732 O O   . LYS A 1 378 ? 8.548   3.798   -4.866  1.00 20.22 ?  352 LYS A O   1 
ATOM   2733 C CB  . LYS A 1 378 ? 8.767   7.073   -5.888  1.00 24.61 ?  352 LYS A CB  1 
ATOM   2734 C CG  . LYS A 1 378 ? 9.691   7.188   -4.688  1.00 31.57 ?  352 LYS A CG  1 
ATOM   2735 C CD  . LYS A 1 378 ? 9.959   8.658   -4.397  1.00 33.93 ?  352 LYS A CD  1 
ATOM   2736 C CE  . LYS A 1 378 ? 10.834  8.904   -3.190  1.00 43.14 ?  352 LYS A CE  1 
ATOM   2737 N NZ  . LYS A 1 378 ? 11.328  10.300  -3.199  1.00 48.68 ?  352 LYS A NZ  1 
ATOM   2738 N N   . ILE A 1 379 ? 6.546   4.924   -4.988  1.00 19.73 ?  353 ILE A N   1 
ATOM   2739 C CA  . ILE A 1 379 ? 5.863   4.031   -4.009  1.00 18.53 ?  353 ILE A CA  1 
ATOM   2740 C C   . ILE A 1 379 ? 5.893   2.601   -4.527  1.00 19.92 ?  353 ILE A C   1 
ATOM   2741 O O   . ILE A 1 379 ? 6.224   1.662   -3.766  1.00 19.60 ?  353 ILE A O   1 
ATOM   2742 C CB  . ILE A 1 379 ? 4.403   4.459   -3.740  1.00 19.08 ?  353 ILE A CB  1 
ATOM   2743 C CG1 . ILE A 1 379 ? 4.348   5.874   -3.135  1.00 20.34 ?  353 ILE A CG1 1 
ATOM   2744 C CG2 . ILE A 1 379 ? 3.762   3.402   -2.842  1.00 19.88 ?  353 ILE A CG2 1 
ATOM   2745 C CD1 . ILE A 1 379 ? 2.966   6.503   -2.960  1.00 19.84 ?  353 ILE A CD1 1 
ATOM   2746 N N   . ALA A 1 380 ? 5.456   2.410   -5.766  1.00 19.25 ?  354 ALA A N   1 
ATOM   2747 C CA  . ALA A 1 380 ? 5.263   1.058   -6.328  1.00 18.56 ?  354 ALA A CA  1 
ATOM   2748 C C   . ALA A 1 380 ? 6.604   0.357   -6.331  1.00 19.29 ?  354 ALA A C   1 
ATOM   2749 O O   . ALA A 1 380 ? 6.670   -0.829  -5.965  1.00 20.56 ?  354 ALA A O   1 
ATOM   2750 C CB  . ALA A 1 380 ? 4.690   1.136   -7.725  1.00 19.70 ?  354 ALA A CB  1 
ATOM   2751 N N   . TYR A 1 381 ? 7.628   1.058   -6.785  1.00 18.10 ?  355 TYR A N   1 
ATOM   2752 C CA  . TYR A 1 381 ? 8.980   0.461   -6.895  1.00 19.34 ?  355 TYR A CA  1 
ATOM   2753 C C   . TYR A 1 381 ? 9.484   -0.050  -5.540  1.00 21.16 ?  355 TYR A C   1 
ATOM   2754 O O   . TYR A 1 381 ? 10.055  -1.192  -5.477  1.00 22.72 ?  355 TYR A O   1 
ATOM   2755 C CB  . TYR A 1 381 ? 9.943   1.450   -7.508  1.00 19.89 ?  355 TYR A CB  1 
ATOM   2756 C CG  . TYR A 1 381 ? 11.148  0.776   -8.098  1.00 19.41 ?  355 TYR A CG  1 
ATOM   2757 C CD1 . TYR A 1 381 ? 11.127  0.360   -9.422  1.00 19.75 ?  355 TYR A CD1 1 
ATOM   2758 C CD2 . TYR A 1 381 ? 12.296  0.553   -7.340  1.00 21.94 ?  355 TYR A CD2 1 
ATOM   2759 C CE1 . TYR A 1 381 ? 12.235  -0.230  -9.992  1.00 21.91 ?  355 TYR A CE1 1 
ATOM   2760 C CE2 . TYR A 1 381 ? 13.412  -0.040  -7.905  1.00 21.76 ?  355 TYR A CE2 1 
ATOM   2761 C CZ  . TYR A 1 381 ? 13.381  -0.422  -9.234  1.00 20.67 ?  355 TYR A CZ  1 
ATOM   2762 O OH  . TYR A 1 381 ? 14.468  -1.017  -9.811  1.00 23.71 ?  355 TYR A OH  1 
ATOM   2763 N N   . ALA A 1 382 ? 9.352   0.775   -4.513  1.00 21.29 ?  356 ALA A N   1 
ATOM   2764 C CA  . ALA A 1 382 ? 9.730   0.425   -3.132  1.00 23.82 ?  356 ALA A CA  1 
ATOM   2765 C C   . ALA A 1 382 ? 8.972   -0.831  -2.711  1.00 23.67 ?  356 ALA A C   1 
ATOM   2766 O O   . ALA A 1 382 ? 9.548   -1.696  -2.045  1.00 25.51 ?  356 ALA A O   1 
ATOM   2767 C CB  . ALA A 1 382 ? 9.457   1.589   -2.241  1.00 24.34 ?  356 ALA A CB  1 
ATOM   2768 N N   . ILE A 1 383 ? 7.680   -0.906  -3.019  1.00 24.27 ?  357 ILE A N   1 
ATOM   2769 C CA  . ILE A 1 383 ? 6.867   -2.084  -2.607  1.00 24.25 ?  357 ILE A CA  1 
ATOM   2770 C C   . ILE A 1 383 ? 7.357   -3.295  -3.398  1.00 24.86 ?  357 ILE A C   1 
ATOM   2771 O O   . ILE A 1 383 ? 7.662   -4.340  -2.773  1.00 25.89 ?  357 ILE A O   1 
ATOM   2772 C CB  . ILE A 1 383 ? 5.359   -1.809  -2.773  1.00 23.17 ?  357 ILE A CB  1 
ATOM   2773 C CG1 . ILE A 1 383 ? 4.913   -0.690  -1.827  1.00 22.32 ?  357 ILE A CG1 1 
ATOM   2774 C CG2 . ILE A 1 383 ? 4.564   -3.088  -2.578  1.00 25.23 ?  357 ILE A CG2 1 
ATOM   2775 C CD1 . ILE A 1 383 ? 3.541   -0.163  -2.097  1.00 23.20 ?  357 ILE A CD1 1 
ATOM   2776 N N   . LEU A 1 384 ? 7.417   -3.172  -4.715  1.00 26.09 ?  358 LEU A N   1 
ATOM   2777 C CA  . LEU A 1 384 ? 7.716   -4.337  -5.594  1.00 32.95 ?  358 LEU A CA  1 
ATOM   2778 C C   . LEU A 1 384 ? 9.117   -4.859  -5.297  1.00 35.22 ?  358 LEU A C   1 
ATOM   2779 O O   . LEU A 1 384 ? 9.266   -6.092  -5.326  1.00 39.90 ?  358 LEU A O   1 
ATOM   2780 C CB  . LEU A 1 384 ? 7.567   -3.971  -7.066  1.00 32.32 ?  358 LEU A CB  1 
ATOM   2781 C CG  . LEU A 1 384 ? 6.132   -3.728  -7.528  1.00 38.04 ?  358 LEU A CG  1 
ATOM   2782 C CD1 . LEU A 1 384 ? 6.108   -3.200  -8.955  1.00 42.22 ?  358 LEU A CD1 1 
ATOM   2783 C CD2 . LEU A 1 384 ? 5.285   -4.982  -7.412  1.00 39.27 ?  358 LEU A CD2 1 
ATOM   2784 N N   . SER A 1 385 ? 10.076  -3.974  -4.988  1.00 39.73 ?  359 SER A N   1 
ATOM   2785 C CA  . SER A 1 385 ? 11.464  -4.347  -4.596  1.00 43.02 ?  359 SER A CA  1 
ATOM   2786 C C   . SER A 1 385 ? 11.432  -5.090  -3.253  1.00 47.33 ?  359 SER A C   1 
ATOM   2787 O O   . SER A 1 385 ? 11.963  -6.219  -3.188  1.00 48.71 ?  359 SER A O   1 
ATOM   2788 C CB  . SER A 1 385 ? 12.361  -3.149  -4.547  1.00 44.84 ?  359 SER A CB  1 
ATOM   2789 O OG  . SER A 1 385 ? 12.612  -2.693  -5.864  1.00 52.74 ?  359 SER A OG  1 
ATOM   2790 N N   . GLY A 1 386 ? 10.793  -4.490  -2.243  1.00 43.95 ?  360 GLY A N   1 
ATOM   2791 C CA  . GLY A 1 386 ? 10.559  -5.103  -0.921  1.00 47.38 ?  360 GLY A CA  1 
ATOM   2792 C C   . GLY A 1 386 ? 10.084  -6.543  -1.036  1.00 49.56 ?  360 GLY A C   1 
ATOM   2793 O O   . GLY A 1 386 ? 10.665  -7.393  -0.367  1.00 54.88 ?  360 GLY A O   1 
ATOM   2794 N N   . LEU A 1 387 ? 9.060   -6.801  -1.853  1.00 50.85 ?  361 LEU A N   1 
ATOM   2795 C CA  . LEU A 1 387 ? 8.592   -8.168  -2.206  1.00 56.13 ?  361 LEU A CA  1 
ATOM   2796 C C   . LEU A 1 387 ? 9.605   -8.792  -3.182  1.00 57.26 ?  361 LEU A C   1 
ATOM   2797 O O   . LEU A 1 387 ? 10.193  -9.823  -2.873  1.00 70.48 ?  361 LEU A O   1 
ATOM   2798 C CB  . LEU A 1 387 ? 7.203   -8.096  -2.850  1.00 53.80 ?  361 LEU A CB  1 
ATOM   2799 C CG  . LEU A 1 387 ? 6.147   -7.260  -2.133  1.00 51.59 ?  361 LEU A CG  1 
ATOM   2800 C CD1 . LEU A 1 387 ? 4.909   -7.116  -3.001  1.00 50.80 ?  361 LEU A CD1 1 
ATOM   2801 C CD2 . LEU A 1 387 ? 5.783   -7.853  -0.785  1.00 54.42 ?  361 LEU A CD2 1 
HETATM 2802 B B07 . KJK B 2 .   ? -5.352  10.100  -18.258 1.00 24.52 -1 401 KJK A B07 1 
HETATM 2803 C C10 . KJK B 2 .   ? -3.232  11.136  -18.369 1.00 34.78 ?  401 KJK A C10 1 
HETATM 2804 C C11 . KJK B 2 .   ? -2.051  11.155  -17.581 1.00 39.70 ?  401 KJK A C11 1 
HETATM 2805 C C12 . KJK B 2 .   ? -1.569  9.903   -16.870 1.00 36.29 ?  401 KJK A C12 1 
HETATM 2806 C C15 . KJK B 2 .   ? -1.355  12.359  -17.473 1.00 39.90 ?  401 KJK A C15 1 
HETATM 2807 C C16 . KJK B 2 .   ? -1.800  13.509  -18.121 1.00 38.82 ?  401 KJK A C16 1 
HETATM 2808 C C17 . KJK B 2 .   ? -2.971  13.477  -18.858 1.00 37.85 ?  401 KJK A C17 1 
HETATM 2809 C C18 . KJK B 2 .   ? -3.692  12.291  -18.991 1.00 33.23 ?  401 KJK A C18 1 
HETATM 2810 C C19 . KJK B 2 .   ? -4.957  12.204  -19.785 1.00 34.12 ?  401 KJK A C19 1 
HETATM 2811 C C20 . KJK B 2 .   ? -5.985  11.388  -19.031 1.00 30.58 ?  401 KJK A C20 1 
HETATM 2812 C C22 . KJK B 2 .   ? -7.512  13.244  -18.495 1.00 38.84 ?  401 KJK A C22 1 
HETATM 2813 C C23 . KJK B 2 .   ? -7.878  14.245  -17.427 1.00 44.96 ?  401 KJK A C23 1 
HETATM 2814 C C24 . KJK B 2 .   ? -9.296  14.832  -17.489 1.00 44.32 ?  401 KJK A C24 1 
HETATM 2815 C C25 . KJK B 2 .   ? -9.575  15.582  -18.797 1.00 47.58 ?  401 KJK A C25 1 
HETATM 2816 C C26 . KJK B 2 .   ? -10.906 16.328  -18.799 1.00 46.17 ?  401 KJK A C26 1 
HETATM 2817 C C27 . KJK B 2 .   ? -11.091 17.198  -17.558 1.00 50.68 ?  401 KJK A C27 1 
HETATM 2818 C C29 . KJK B 2 .   ? -12.467 19.236  -17.965 1.00 71.43 ?  401 KJK A C29 1 
HETATM 2819 C C30 . KJK B 2 .   ? -13.526 20.050  -17.235 1.00 81.35 ?  401 KJK A C30 1 
HETATM 2820 C C32 . KJK B 2 .   ? -10.881 16.384  -16.303 1.00 49.50 ?  401 KJK A C32 1 
HETATM 2821 C C33 . KJK B 2 .   ? -9.497  15.765  -16.298 1.00 46.69 ?  401 KJK A C33 1 
HETATM 2822 N N21 . KJK B 2 .   ? -6.763  12.219  -18.110 1.00 33.06 ?  401 KJK A N21 1 
HETATM 2823 N N28 . KJK B 2 .   ? -12.414 17.847  -17.497 1.00 59.96 ?  401 KJK A N28 1 
HETATM 2824 N N31 . KJK B 2 .   ? -14.612 20.480  -18.123 1.00 84.32 ?  401 KJK A N31 1 
HETATM 2825 O O08 . KJK B 2 .   ? -5.603  10.089  -16.866 1.00 25.42 ?  401 KJK A O08 1 
HETATM 2826 O O09 . KJK B 2 .   ? -3.934  9.976   -18.492 1.00 27.67 ?  401 KJK A O09 1 
HETATM 2827 O O13 . KJK B 2 .   ? -1.256  8.916   -17.566 1.00 34.09 ?  401 KJK A O13 1 
HETATM 2828 O O14 . KJK B 2 .   ? -1.576  9.893   -15.608 1.00 38.95 -1 401 KJK A O14 1 
HETATM 2829 O O34 . KJK B 2 .   ? -7.806  13.421  -19.674 1.00 42.06 ?  401 KJK A O34 1 
HETATM 2830 O O   . HOH C 3 .   ? 9.128   13.134  -38.047 1.00 52.36 ?  501 HOH A O   1 
HETATM 2831 O O   . HOH C 3 .   ? -17.945 0.283   -46.034 1.00 36.73 ?  502 HOH A O   1 
HETATM 2832 O O   . HOH C 3 .   ? 1.068   -17.330 -22.282 1.00 34.38 ?  503 HOH A O   1 
HETATM 2833 O O   . HOH C 3 .   ? -11.307 13.217  -40.987 1.00 38.36 ?  504 HOH A O   1 
HETATM 2834 O O   . HOH C 3 .   ? -3.096  -8.670  -32.204 1.00 38.85 ?  505 HOH A O   1 
HETATM 2835 O O   . HOH C 3 .   ? -2.818  -13.042 -20.933 1.00 26.82 ?  506 HOH A O   1 
HETATM 2836 O O   . HOH C 3 .   ? -19.782 -2.137  -10.236 1.00 29.99 ?  507 HOH A O   1 
HETATM 2837 O O   . HOH C 3 .   ? -6.859  26.558  -6.633  1.00 48.07 ?  508 HOH A O   1 
HETATM 2838 O O   . HOH C 3 .   ? -2.494  17.142  -32.355 1.00 42.08 ?  509 HOH A O   1 
HETATM 2839 O O   . HOH C 3 .   ? -19.751 6.543   -25.651 1.00 26.28 ?  510 HOH A O   1 
HETATM 2840 O O   . HOH C 3 .   ? -4.025  -17.792 -18.435 1.00 35.44 ?  511 HOH A O   1 
HETATM 2841 O O   . HOH C 3 .   ? -22.398 -8.234  -25.923 1.00 43.49 ?  512 HOH A O   1 
HETATM 2842 O O   . HOH C 3 .   ? -15.273 3.114   3.137   1.00 40.38 ?  513 HOH A O   1 
HETATM 2843 O O   . HOH C 3 .   ? -0.552  -13.801 -15.502 1.00 41.84 ?  514 HOH A O   1 
HETATM 2844 O O   . HOH C 3 .   ? -19.471 -5.924  -35.637 1.00 33.57 ?  515 HOH A O   1 
HETATM 2845 O O   . HOH C 3 .   ? 3.162   -13.743 -5.537  1.00 43.79 ?  516 HOH A O   1 
HETATM 2846 O O   . HOH C 3 .   ? -26.493 10.151  -14.621 1.00 38.82 ?  517 HOH A O   1 
HETATM 2847 O O   . HOH C 3 .   ? -15.666 8.300   1.328   1.00 40.64 ?  518 HOH A O   1 
HETATM 2848 O O   . HOH C 3 .   ? 2.319   17.161  3.863   1.00 36.75 ?  519 HOH A O   1 
HETATM 2849 O O   . HOH C 3 .   ? -1.476  -12.805 -6.748  1.00 28.49 ?  520 HOH A O   1 
HETATM 2850 O O   . HOH C 3 .   ? -27.115 -0.636  -15.699 1.00 23.79 ?  521 HOH A O   1 
HETATM 2851 O O   . HOH C 3 .   ? -24.105 6.020   -30.464 1.00 40.38 ?  522 HOH A O   1 
HETATM 2852 O O   . HOH C 3 .   ? -26.462 16.707  -26.253 1.00 46.68 ?  523 HOH A O   1 
HETATM 2853 O O   . HOH C 3 .   ? -12.691 -3.862  4.368   1.00 39.57 ?  524 HOH A O   1 
HETATM 2854 O O   . HOH C 3 .   ? 9.035   11.877  -2.388  1.00 32.74 ?  525 HOH A O   1 
HETATM 2855 O O   . HOH C 3 .   ? -21.571 19.833  -33.999 1.00 32.84 ?  526 HOH A O   1 
HETATM 2856 O O   . HOH C 3 .   ? -6.482  -7.447  -37.442 1.00 45.73 ?  527 HOH A O   1 
HETATM 2857 O O   . HOH C 3 .   ? -2.515  -5.700  -25.954 1.00 23.27 ?  528 HOH A O   1 
HETATM 2858 O O   . HOH C 3 .   ? -5.689  -20.282 -12.352 1.00 30.58 ?  529 HOH A O   1 
HETATM 2859 O O   . HOH C 3 .   ? -14.116 19.131  -11.205 1.00 49.35 ?  530 HOH A O   1 
HETATM 2860 O O   . HOH C 3 .   ? 8.559   -5.731  -21.762 1.00 36.35 ?  531 HOH A O   1 
HETATM 2861 O O   . HOH C 3 .   ? -7.680  6.844   13.725  1.00 42.67 ?  532 HOH A O   1 
HETATM 2862 O O   . HOH C 3 .   ? -13.296 14.518  -22.581 1.00 24.87 ?  533 HOH A O   1 
HETATM 2863 O O   . HOH C 3 .   ? -13.787 18.968  -24.531 1.00 33.82 ?  534 HOH A O   1 
HETATM 2864 O O   . HOH C 3 .   ? -25.996 15.621  -30.363 1.00 34.15 ?  535 HOH A O   1 
HETATM 2865 O O   . HOH C 3 .   ? -10.924 2.349   -46.258 1.00 46.62 ?  536 HOH A O   1 
HETATM 2866 O O   . HOH C 3 .   ? -12.016 8.535   -13.264 1.00 18.48 ?  537 HOH A O   1 
HETATM 2867 O O   . HOH C 3 .   ? 2.091   15.766  -33.104 1.00 32.75 ?  538 HOH A O   1 
HETATM 2868 O O   . HOH C 3 .   ? -16.922 -6.342  -6.377  1.00 24.11 ?  539 HOH A O   1 
HETATM 2869 O O   . HOH C 3 .   ? 15.423  -3.956  -21.121 1.00 42.59 ?  540 HOH A O   1 
HETATM 2870 O O   . HOH C 3 .   ? -3.576  16.068  -36.712 1.00 30.08 ?  541 HOH A O   1 
HETATM 2871 O O   . HOH C 3 .   ? 7.017   18.608  -0.861  1.00 27.10 ?  542 HOH A O   1 
HETATM 2872 O O   . HOH C 3 .   ? -5.754  19.859  -10.207 1.00 41.60 ?  543 HOH A O   1 
HETATM 2873 O O   . HOH C 3 .   ? 7.838   5.180   -36.631 1.00 41.65 ?  544 HOH A O   1 
HETATM 2874 O O   . HOH C 3 .   ? -21.316 8.145   -20.351 1.00 49.35 ?  545 HOH A O   1 
HETATM 2875 O O   . HOH C 3 .   ? -4.386  13.174  5.468   1.00 38.51 ?  546 HOH A O   1 
HETATM 2876 O O   . HOH C 3 .   ? 0.295   -6.226  7.161   1.00 43.37 ?  547 HOH A O   1 
HETATM 2877 O O   . HOH C 3 .   ? -16.899 19.373  -17.496 1.00 49.83 ?  548 HOH A O   1 
HETATM 2878 O O   . HOH C 3 .   ? 12.836  4.476   -19.696 1.00 20.67 ?  549 HOH A O   1 
HETATM 2879 O O   . HOH C 3 .   ? -2.713  -16.865 -7.545  1.00 35.24 ?  550 HOH A O   1 
HETATM 2880 O O   . HOH C 3 .   ? -17.389 0.893   -2.547  1.00 28.46 ?  551 HOH A O   1 
HETATM 2881 O O   . HOH C 3 .   ? 7.910   1.317   8.040   1.00 39.75 ?  552 HOH A O   1 
HETATM 2882 O O   . HOH C 3 .   ? -13.586 23.232  -7.440  1.00 45.73 ?  553 HOH A O   1 
HETATM 2883 O O   . HOH C 3 .   ? -9.553  -7.411  -4.043  1.00 31.21 ?  554 HOH A O   1 
HETATM 2884 O O   . HOH C 3 .   ? 3.579   6.384   -20.345 1.00 32.57 ?  555 HOH A O   1 
HETATM 2885 O O   . HOH C 3 .   ? -22.149 -3.171  -13.170 1.00 32.68 ?  556 HOH A O   1 
HETATM 2886 O O   . HOH C 3 .   ? 1.193   8.186   -36.585 1.00 25.44 ?  557 HOH A O   1 
HETATM 2887 O O   . HOH C 3 .   ? -10.690 -11.046 -9.542  1.00 32.91 ?  558 HOH A O   1 
HETATM 2888 O O   . HOH C 3 .   ? -17.424 19.631  -33.100 1.00 31.00 ?  559 HOH A O   1 
HETATM 2889 O O   . HOH C 3 .   ? -1.615  3.182   -22.775 1.00 18.41 ?  560 HOH A O   1 
HETATM 2890 O O   . HOH C 3 .   ? 4.255   3.346   -18.790 1.00 17.85 ?  561 HOH A O   1 
HETATM 2891 O O   . HOH C 3 .   ? 0.336   6.139   -19.882 1.00 22.53 ?  562 HOH A O   1 
HETATM 2892 O O   . HOH C 3 .   ? -21.744 2.967   -13.766 1.00 20.29 ?  563 HOH A O   1 
HETATM 2893 O O   . HOH C 3 .   ? -9.604  -6.225  -41.145 1.00 45.90 ?  564 HOH A O   1 
HETATM 2894 O O   . HOH C 3 .   ? 11.850  -2.442  -20.883 1.00 23.64 ?  565 HOH A O   1 
HETATM 2895 O O   . HOH C 3 .   ? 10.464  5.464   4.427   1.00 36.25 ?  566 HOH A O   1 
HETATM 2896 O O   . HOH C 3 .   ? -4.715  -7.698  -28.894 1.00 24.47 ?  567 HOH A O   1 
HETATM 2897 O O   . HOH C 3 .   ? -14.839 2.243   -44.222 1.00 35.47 ?  568 HOH A O   1 
HETATM 2898 O O   . HOH C 3 .   ? -10.372 2.224   -1.871  1.00 17.36 ?  569 HOH A O   1 
HETATM 2899 O O   . HOH C 3 .   ? -18.941 -14.547 -17.223 1.00 32.84 ?  570 HOH A O   1 
HETATM 2900 O O   . HOH C 3 .   ? -0.322  14.041  -25.892 1.00 24.60 ?  571 HOH A O   1 
HETATM 2901 O O   . HOH C 3 .   ? 5.168   17.467  -15.103 1.00 44.69 ?  572 HOH A O   1 
HETATM 2902 O O   . HOH C 3 .   ? -25.351 4.182   -11.926 1.00 21.43 ?  573 HOH A O   1 
HETATM 2903 O O   . HOH C 3 .   ? -14.378 -4.887  -0.275  1.00 49.39 ?  574 HOH A O   1 
HETATM 2904 O O   . HOH C 3 .   ? 15.563  -7.155  -16.780 1.00 36.02 ?  575 HOH A O   1 
HETATM 2905 O O   . HOH C 3 .   ? -7.234  -1.107  4.865   1.00 30.58 ?  576 HOH A O   1 
HETATM 2906 O O   . HOH C 3 .   ? -16.713 12.627  -16.587 1.00 30.75 ?  577 HOH A O   1 
HETATM 2907 O O   . HOH C 3 .   ? -4.812  17.352  -7.635  1.00 23.96 ?  578 HOH A O   1 
HETATM 2908 O O   . HOH C 3 .   ? -5.317  -11.373 -4.464  1.00 29.45 ?  579 HOH A O   1 
HETATM 2909 O O   . HOH C 3 .   ? -18.875 8.632   -23.000 1.00 27.50 ?  580 HOH A O   1 
HETATM 2910 O O   . HOH C 3 .   ? -8.738  -9.618  -5.648  1.00 32.99 ?  581 HOH A O   1 
HETATM 2911 O O   . HOH C 3 .   ? 0.145   0.834   -33.656 1.00 37.97 ?  582 HOH A O   1 
HETATM 2912 O O   . HOH C 3 .   ? 15.906  -14.913 -16.919 1.00 40.68 ?  583 HOH A O   1 
HETATM 2913 O O   . HOH C 3 .   ? -7.605  18.237  -33.290 1.00 31.92 ?  584 HOH A O   1 
HETATM 2914 O O   . HOH C 3 .   ? -17.325 18.213  -39.295 1.00 40.20 ?  585 HOH A O   1 
HETATM 2915 O O   . HOH C 3 .   ? 14.385  8.007   -8.954  1.00 20.80 ?  586 HOH A O   1 
HETATM 2916 O O   . HOH C 3 .   ? -11.230 15.189  -10.159 1.00 21.52 ?  587 HOH A O   1 
HETATM 2917 O O   . HOH C 3 .   ? 2.698   11.176  -26.189 1.00 23.70 ?  588 HOH A O   1 
HETATM 2918 O O   . HOH C 3 .   ? 13.760  9.255   -14.787 1.00 26.44 ?  589 HOH A O   1 
HETATM 2919 O O   . HOH C 3 .   ? -2.565  10.559  -31.313 1.00 19.15 ?  590 HOH A O   1 
HETATM 2920 O O   . HOH C 3 .   ? -26.474 -4.702  -22.137 1.00 46.28 ?  591 HOH A O   1 
HETATM 2921 O O   . HOH C 3 .   ? 7.788   10.113  -14.068 1.00 31.60 ?  592 HOH A O   1 
HETATM 2922 O O   . HOH C 3 .   ? 18.748  3.981   -14.690 1.00 19.50 ?  593 HOH A O   1 
HETATM 2923 O O   . HOH C 3 .   ? -2.684  -0.746  -38.195 1.00 45.48 ?  594 HOH A O   1 
HETATM 2924 O O   . HOH C 3 .   ? 0.163   16.664  -26.141 1.00 32.22 ?  595 HOH A O   1 
HETATM 2925 O O   . HOH C 3 .   ? -11.489 -18.493 -29.251 1.00 53.28 ?  596 HOH A O   1 
HETATM 2926 O O   . HOH C 3 .   ? -25.332 19.436  -30.934 1.00 31.39 ?  597 HOH A O   1 
HETATM 2927 O O   . HOH C 3 .   ? 12.159  -1.647  -1.300  1.00 49.36 ?  598 HOH A O   1 
HETATM 2928 O O   . HOH C 3 .   ? 8.940   12.178  -32.870 1.00 45.43 ?  599 HOH A O   1 
HETATM 2929 O O   . HOH C 3 .   ? -4.149  6.567   -44.107 1.00 49.67 ?  600 HOH A O   1 
HETATM 2930 O O   . HOH C 3 .   ? -6.496  -8.974  3.126   1.00 45.13 ?  601 HOH A O   1 
HETATM 2931 O O   . HOH C 3 .   ? 9.340   -3.134  -22.940 1.00 21.56 ?  602 HOH A O   1 
HETATM 2932 O O   . HOH C 3 .   ? -26.129 6.225   -16.138 1.00 19.61 ?  603 HOH A O   1 
HETATM 2933 O O   . HOH C 3 .   ? 0.082   -11.632 -19.256 1.00 26.56 ?  604 HOH A O   1 
HETATM 2934 O O   . HOH C 3 .   ? -19.502 2.572   -42.221 1.00 44.80 ?  605 HOH A O   1 
HETATM 2935 O O   . HOH C 3 .   ? -13.772 2.789   -19.272 1.00 21.74 ?  606 HOH A O   1 
HETATM 2936 O O   . HOH C 3 .   ? -14.481 6.325   2.511   1.00 33.99 ?  607 HOH A O   1 
HETATM 2937 O O   . HOH C 3 .   ? -29.136 3.303   -23.755 1.00 43.77 ?  608 HOH A O   1 
HETATM 2938 O O   . HOH C 3 .   ? -7.585  -12.901 -27.217 1.00 42.51 ?  609 HOH A O   1 
HETATM 2939 O O   . HOH C 3 .   ? -3.555  -13.388 -8.669  1.00 34.48 ?  610 HOH A O   1 
HETATM 2940 O O   . HOH C 3 .   ? -1.489  6.920   -6.940  1.00 19.29 ?  611 HOH A O   1 
HETATM 2941 O O   . HOH C 3 .   ? 0.308   -13.133 0.461   1.00 43.41 ?  612 HOH A O   1 
HETATM 2942 O O   . HOH C 3 .   ? -22.490 1.176   -36.978 1.00 44.35 ?  613 HOH A O   1 
HETATM 2943 O O   . HOH C 3 .   ? 3.487   17.268  -5.428  1.00 29.36 ?  614 HOH A O   1 
HETATM 2944 O O   . HOH C 3 .   ? -17.818 12.861  -10.826 1.00 27.44 ?  615 HOH A O   1 
HETATM 2945 O O   . HOH C 3 .   ? -13.505 -10.514 -9.392  1.00 34.24 ?  616 HOH A O   1 
HETATM 2946 O O   . HOH C 3 .   ? -3.458  1.688   -25.470 1.00 26.20 ?  617 HOH A O   1 
HETATM 2947 O O   . HOH C 3 .   ? 9.637   -4.531  6.103   1.00 40.96 ?  618 HOH A O   1 
HETATM 2948 O O   . HOH C 3 .   ? -10.868 -24.783 -21.084 1.00 39.93 ?  619 HOH A O   1 
HETATM 2949 O O   . HOH C 3 .   ? 13.601  -4.547  -7.668  1.00 53.91 ?  620 HOH A O   1 
HETATM 2950 O O   . HOH C 3 .   ? 1.189   -6.904  14.280  1.00 40.17 ?  621 HOH A O   1 
HETATM 2951 O O   . HOH C 3 .   ? -11.684 -10.664 -34.108 1.00 44.68 ?  622 HOH A O   1 
HETATM 2952 O O   . HOH C 3 .   ? -7.513  5.634   6.375   1.00 24.06 ?  623 HOH A O   1 
HETATM 2953 O O   . HOH C 3 .   ? 1.104   16.583  -10.232 1.00 39.90 ?  624 HOH A O   1 
HETATM 2954 O O   . HOH C 3 .   ? -0.947  13.278  4.172   1.00 49.04 ?  625 HOH A O   1 
HETATM 2955 O O   . HOH C 3 .   ? -14.492 16.108  -18.373 1.00 32.91 ?  626 HOH A O   1 
HETATM 2956 O O   . HOH C 3 .   ? -19.642 -2.833  -36.831 1.00 40.40 ?  627 HOH A O   1 
HETATM 2957 O O   . HOH C 3 .   ? 3.705   14.819  -41.879 1.00 33.46 ?  628 HOH A O   1 
HETATM 2958 O O   . HOH C 3 .   ? -1.034  -11.499 -16.752 1.00 29.64 ?  629 HOH A O   1 
HETATM 2959 O O   . HOH C 3 .   ? -6.310  20.513  -45.700 1.00 45.41 ?  630 HOH A O   1 
HETATM 2960 O O   . HOH C 3 .   ? -16.235 18.140  -5.569  1.00 29.25 ?  631 HOH A O   1 
HETATM 2961 O O   . HOH C 3 .   ? 13.477  10.212  -12.351 1.00 36.04 ?  632 HOH A O   1 
HETATM 2962 O O   . HOH C 3 .   ? -20.069 -13.980 -23.380 1.00 37.97 ?  633 HOH A O   1 
HETATM 2963 O O   . HOH C 3 .   ? -4.862  -15.041 -7.387  1.00 39.60 ?  634 HOH A O   1 
HETATM 2964 O O   . HOH C 3 .   ? 11.298  3.955   -4.346  1.00 33.15 ?  635 HOH A O   1 
HETATM 2965 O O   . HOH C 3 .   ? -15.556 -4.917  -43.671 1.00 42.03 ?  636 HOH A O   1 
HETATM 2966 O O   . HOH C 3 .   ? -0.521  9.610   -33.569 1.00 23.05 ?  637 HOH A O   1 
HETATM 2967 O O   . HOH C 3 .   ? -3.784  8.434   -32.508 1.00 19.57 ?  638 HOH A O   1 
HETATM 2968 O O   . HOH C 3 .   ? -24.068 4.726   -17.634 1.00 25.65 ?  639 HOH A O   1 
HETATM 2969 O O   . HOH C 3 .   ? 19.488  4.285   -22.493 1.00 34.52 ?  640 HOH A O   1 
HETATM 2970 O O   . HOH C 3 .   ? -16.603 -20.190 -20.247 1.00 40.25 ?  641 HOH A O   1 
HETATM 2971 O O   . HOH C 3 .   ? -9.863  -11.232 -27.926 1.00 45.74 ?  642 HOH A O   1 
HETATM 2972 O O   . HOH C 3 .   ? -22.407 1.180   -11.608 1.00 26.53 ?  643 HOH A O   1 
HETATM 2973 O O   . HOH C 3 .   ? -6.500  8.959   -43.852 1.00 33.78 ?  644 HOH A O   1 
HETATM 2974 O O   . HOH C 3 .   ? -11.791 -19.698 -19.833 1.00 37.42 ?  645 HOH A O   1 
HETATM 2975 O O   . HOH C 3 .   ? -16.537 -14.082 -16.478 1.00 32.98 ?  646 HOH A O   1 
HETATM 2976 O O   . HOH C 3 .   ? -8.301  26.052  1.114   1.00 48.17 ?  647 HOH A O   1 
HETATM 2977 O O   . HOH C 3 .   ? 14.412  -7.337  -23.610 1.00 43.38 ?  648 HOH A O   1 
HETATM 2978 O O   . HOH C 3 .   ? -19.453 1.060   -4.685  1.00 25.85 ?  649 HOH A O   1 
HETATM 2979 O O   . HOH C 3 .   ? -11.434 12.347  -46.240 1.00 48.56 ?  650 HOH A O   1 
HETATM 2980 O O   . HOH C 3 .   ? -26.240 -7.227  -15.987 1.00 35.87 ?  651 HOH A O   1 
HETATM 2981 O O   . HOH C 3 .   ? -7.136  18.320  -38.076 1.00 26.79 ?  652 HOH A O   1 
HETATM 2982 O O   . HOH C 3 .   ? 9.574   0.534   1.436   1.00 32.27 ?  653 HOH A O   1 
HETATM 2983 O O   . HOH C 3 .   ? 2.401   7.515   -17.626 1.00 30.91 ?  654 HOH A O   1 
HETATM 2984 O O   . HOH C 3 .   ? -21.427 -10.423 -18.067 1.00 32.75 ?  655 HOH A O   1 
HETATM 2985 O O   . HOH C 3 .   ? -17.965 21.389  -31.036 1.00 50.21 ?  656 HOH A O   1 
HETATM 2986 O O   . HOH C 3 .   ? 4.379   9.161   -27.003 1.00 30.31 ?  657 HOH A O   1 
HETATM 2987 O O   . HOH C 3 .   ? -21.216 -5.762  -11.668 1.00 35.34 ?  658 HOH A O   1 
HETATM 2988 O O   . HOH C 3 .   ? -1.782  16.794  -27.915 1.00 32.62 ?  659 HOH A O   1 
HETATM 2989 O O   . HOH C 3 .   ? -6.915  7.590   -7.634  1.00 18.95 ?  660 HOH A O   1 
HETATM 2990 O O   . HOH C 3 .   ? 3.219   -5.092  -34.393 1.00 48.80 ?  661 HOH A O   1 
HETATM 2991 O O   . HOH C 3 .   ? -9.515  2.369   7.246   1.00 34.92 ?  662 HOH A O   1 
HETATM 2992 O O   . HOH C 3 .   ? -28.683 -6.244  -19.862 1.00 39.12 ?  663 HOH A O   1 
HETATM 2993 O O   . HOH C 3 .   ? -5.174  -6.814  4.286   1.00 28.77 ?  664 HOH A O   1 
HETATM 2994 O O   . HOH C 3 .   ? -14.328 20.659  8.973   1.00 35.01 ?  665 HOH A O   1 
HETATM 2995 O O   . HOH C 3 .   ? -11.159 16.059  -12.517 1.00 34.96 ?  666 HOH A O   1 
HETATM 2996 O O   . HOH C 3 .   ? 5.532   -13.114 -28.157 1.00 35.04 ?  667 HOH A O   1 
HETATM 2997 O O   . HOH C 3 .   ? -7.287  -5.616  -18.918 1.00 24.11 ?  668 HOH A O   1 
HETATM 2998 O O   . HOH C 3 .   ? -19.441 11.063  -24.728 1.00 25.55 ?  669 HOH A O   1 
HETATM 2999 O O   . HOH C 3 .   ? 7.055   -12.615 -24.864 1.00 41.02 ?  670 HOH A O   1 
HETATM 3000 O O   . HOH C 3 .   ? -13.860 18.031  -14.861 1.00 32.44 ?  671 HOH A O   1 
HETATM 3001 O O   . HOH C 3 .   ? 5.934   10.440  -39.083 1.00 40.29 ?  672 HOH A O   1 
HETATM 3002 O O   . HOH C 3 .   ? -15.850 19.260  -7.988  1.00 30.41 ?  673 HOH A O   1 
HETATM 3003 O O   . HOH C 3 .   ? -3.742  7.276   8.288   1.00 37.20 ?  674 HOH A O   1 
HETATM 3004 O O   . HOH C 3 .   ? -22.654 -2.192  -8.733  1.00 40.81 ?  675 HOH A O   1 
HETATM 3005 O O   . HOH C 3 .   ? 8.115   -9.326  -32.179 1.00 49.60 ?  676 HOH A O   1 
HETATM 3006 O O   . HOH C 3 .   ? 3.646   -15.046 -17.056 1.00 25.79 ?  677 HOH A O   1 
HETATM 3007 O O   . HOH C 3 .   ? 9.130   0.700   -36.951 1.00 36.46 ?  678 HOH A O   1 
HETATM 3008 O O   . HOH C 3 .   ? -16.307 10.242  -15.737 1.00 39.16 ?  679 HOH A O   1 
HETATM 3009 O O   . HOH C 3 .   ? 0.913   16.782  -4.996  1.00 36.29 ?  680 HOH A O   1 
HETATM 3010 O O   . HOH C 3 .   ? -28.555 5.945   -8.453  1.00 21.66 ?  681 HOH A O   1 
HETATM 3011 O O   . HOH C 3 .   ? 2.466   13.584  -13.296 1.00 27.13 ?  682 HOH A O   1 
HETATM 3012 O O   . HOH C 3 .   ? -14.337 7.073   8.680   1.00 40.34 ?  683 HOH A O   1 
HETATM 3013 O O   . HOH C 3 .   ? -6.869  19.858  -27.748 1.00 36.75 ?  684 HOH A O   1 
HETATM 3014 O O   . HOH C 3 .   ? 1.102   4.523   -17.828 1.00 20.30 ?  685 HOH A O   1 
HETATM 3015 O O   . HOH C 3 .   ? -25.400 13.349  -27.202 1.00 36.08 ?  686 HOH A O   1 
HETATM 3016 O O   . HOH C 3 .   ? -28.731 4.605   -6.080  1.00 27.12 ?  687 HOH A O   1 
HETATM 3017 O O   . HOH C 3 .   ? 8.173   13.992  -16.038 1.00 29.57 ?  688 HOH A O   1 
HETATM 3018 O O   . HOH C 3 .   ? -19.029 -0.134  -0.805  1.00 50.03 ?  689 HOH A O   1 
HETATM 3019 O O   . HOH C 3 .   ? -14.803 18.248  -20.027 1.00 44.69 ?  690 HOH A O   1 
HETATM 3020 O O   . HOH C 3 .   ? 6.332   12.475  -13.262 1.00 24.59 ?  691 HOH A O   1 
HETATM 3021 O O   . HOH C 3 .   ? 9.152   5.358   -22.987 1.00 48.07 ?  692 HOH A O   1 
HETATM 3022 O O   . HOH C 3 .   ? 2.217   7.689   -22.199 1.00 27.17 ?  693 HOH A O   1 
HETATM 3023 O O   . HOH C 3 .   ? -19.582 14.018  -13.966 1.00 49.69 ?  694 HOH A O   1 
HETATM 3024 O O   . HOH C 3 .   ? -23.832 -9.934  -17.599 1.00 44.03 ?  695 HOH A O   1 
HETATM 3025 O O   . HOH C 3 .   ? -21.033 -12.323 -20.419 1.00 46.88 ?  696 HOH A O   1 
HETATM 3026 O O   . HOH C 3 .   ? -15.772 5.419   -47.038 1.00 43.60 ?  697 HOH A O   1 
HETATM 3027 O O   . HOH C 3 .   ? 0.533   8.668   -19.925 1.00 36.82 ?  698 HOH A O   1 
HETATM 3028 O O   . HOH C 3 .   ? 12.835  1.220   -28.286 1.00 42.60 ?  699 HOH A O   1 
HETATM 3029 O O   . HOH C 3 .   ? 11.461  4.842   -22.076 1.00 33.59 ?  700 HOH A O   1 
HETATM 3030 O O   . HOH C 3 .   ? 10.921  12.098  -24.385 1.00 45.06 ?  701 HOH A O   1 
HETATM 3031 O O   . HOH C 3 .   ? 9.074   6.427   -0.764  1.00 37.49 ?  702 HOH A O   1 
HETATM 3032 O O   . HOH C 3 .   ? -18.771 16.471  -1.154  1.00 35.04 ?  703 HOH A O   1 
HETATM 3033 O O   . HOH C 3 .   ? -7.556  -8.542  -34.718 1.00 28.76 ?  704 HOH A O   1 
HETATM 3034 O O   . HOH C 3 .   ? -17.056 14.241  0.442   1.00 36.05 ?  705 HOH A O   1 
HETATM 3035 O O   . HOH C 3 .   ? 6.743   17.618  -22.295 1.00 30.91 ?  706 HOH A O   1 
HETATM 3036 O O   . HOH C 3 .   ? -1.731  15.631  -14.887 1.00 39.49 ?  707 HOH A O   1 
HETATM 3037 O O   . HOH C 3 .   ? -2.389  2.623   7.906   1.00 41.36 ?  708 HOH A O   1 
HETATM 3038 O O   . HOH C 3 .   ? -18.245 25.036  -27.127 1.00 47.91 ?  709 HOH A O   1 
HETATM 3039 O O   . HOH C 3 .   ? -6.963  -0.121  0.736   1.00 22.73 ?  710 HOH A O   1 
HETATM 3040 O O   . HOH C 3 .   ? -8.885  23.599  -26.151 1.00 32.17 ?  711 HOH A O   1 
HETATM 3041 O O   . HOH C 3 .   ? -16.452 -16.306 -15.019 1.00 41.81 ?  712 HOH A O   1 
HETATM 3042 O O   . HOH C 3 .   ? -18.214 17.441  -10.603 1.00 46.55 ?  713 HOH A O   1 
HETATM 3043 O O   . HOH C 3 .   ? -19.570 18.603  -21.690 1.00 41.12 ?  714 HOH A O   1 
HETATM 3044 O O   . HOH C 3 .   ? -4.412  -12.132 3.229   1.00 47.71 ?  715 HOH A O   1 
HETATM 3045 O O   . HOH C 3 .   ? 11.245  -10.561 -9.927  1.00 48.51 ?  716 HOH A O   1 
HETATM 3046 O O   . HOH C 3 .   ? -11.177 24.102  -30.960 1.00 41.73 ?  717 HOH A O   1 
HETATM 3047 O O   . HOH C 3 .   ? -21.749 4.923   -26.556 1.00 23.46 ?  718 HOH A O   1 
HETATM 3048 O O   . HOH C 3 .   ? -18.636 17.094  -5.886  1.00 26.83 ?  719 HOH A O   1 
HETATM 3049 O O   . HOH C 3 .   ? -8.976  -4.042  -43.277 1.00 49.07 ?  720 HOH A O   1 
HETATM 3050 O O   . HOH C 3 .   ? 9.806   -13.259 -19.796 1.00 28.46 ?  721 HOH A O   1 
HETATM 3051 O O   . HOH C 3 .   ? -5.947  22.321  -9.249  1.00 35.23 ?  722 HOH A O   1 
HETATM 3052 O O   . HOH C 3 .   ? -20.205 9.591   -10.937 1.00 26.81 ?  723 HOH A O   1 
HETATM 3053 O O   . HOH C 3 .   ? 16.598  1.792   -9.223  1.00 21.92 ?  724 HOH A O   1 
HETATM 3054 O O   . HOH C 3 .   ? -0.389  16.901  -33.987 1.00 42.24 ?  725 HOH A O   1 
HETATM 3055 O O   . HOH C 3 .   ? 16.981  4.284   -10.419 1.00 18.22 ?  726 HOH A O   1 
HETATM 3056 O O   . HOH C 3 .   ? -0.110  13.585  -13.654 1.00 41.41 ?  727 HOH A O   1 
HETATM 3057 O O   . HOH C 3 .   ? 13.213  -8.689  -1.569  1.00 53.99 ?  728 HOH A O   1 
HETATM 3058 O O   . HOH C 3 .   ? -0.127  -14.096 -20.178 1.00 35.09 ?  729 HOH A O   1 
HETATM 3059 O O   . HOH C 3 .   ? -4.900  18.496  -26.240 1.00 26.50 ?  730 HOH A O   1 
HETATM 3060 O O   . HOH C 3 .   ? -26.287 13.450  -4.385  1.00 54.40 ?  731 HOH A O   1 
HETATM 3061 O O   . HOH C 3 .   ? -11.913 11.448  -24.176 1.00 38.10 ?  732 HOH A O   1 
HETATM 3062 O O   . HOH C 3 .   ? 4.295   11.452  -42.477 1.00 47.24 ?  733 HOH A O   1 
HETATM 3063 O O   . HOH C 3 .   ? 9.938   -12.753 -13.696 1.00 50.35 ?  734 HOH A O   1 
HETATM 3064 O O   . HOH C 3 .   ? -19.521 -10.159 -7.682  1.00 56.39 ?  735 HOH A O   1 
HETATM 3065 O O   . HOH C 3 .   ? 12.426  3.707   -29.438 1.00 39.49 ?  736 HOH A O   1 
HETATM 3066 O O   . HOH C 3 .   ? 2.228   10.214  6.072   1.00 40.35 ?  737 HOH A O   1 
HETATM 3067 O O   . HOH C 3 .   ? -13.023 -11.916 -36.417 1.00 53.56 ?  738 HOH A O   1 
HETATM 3068 O O   . HOH C 3 .   ? 0.256   -19.096 -5.240  1.00 51.14 ?  739 HOH A O   1 
HETATM 3069 O O   . HOH C 3 .   ? -18.558 -13.170 -12.207 1.00 46.56 ?  740 HOH A O   1 
HETATM 3070 O O   . HOH C 3 .   ? 4.222   12.827  -15.098 1.00 40.17 ?  741 HOH A O   1 
HETATM 3071 O O   . HOH C 3 .   ? -20.043 8.781   -18.072 1.00 38.35 ?  742 HOH A O   1 
HETATM 3072 O O   . HOH C 3 .   ? -10.490 14.626  -23.678 1.00 19.41 ?  743 HOH A O   1 
HETATM 3073 O O   . HOH C 3 .   ? -17.880 8.463   -17.023 1.00 30.50 ?  744 HOH A O   1 
HETATM 3074 O O   . HOH C 3 .   ? -13.717 -4.462  -41.947 1.00 52.05 ?  745 HOH A O   1 
HETATM 3075 O O   . HOH C 3 .   ? -6.831  -15.698 -26.143 1.00 35.90 ?  746 HOH A O   1 
HETATM 3076 O O   . HOH C 3 .   ? 11.930  11.151  -8.403  1.00 42.68 ?  747 HOH A O   1 
HETATM 3077 O O   . HOH C 3 .   ? -11.603 -3.118  -42.967 1.00 32.15 ?  748 HOH A O   1 
HETATM 3078 O O   . HOH C 3 .   ? -24.011 9.584   -35.895 1.00 31.88 ?  749 HOH A O   1 
HETATM 3079 O O   . HOH C 3 .   ? -6.851  -17.836 -20.966 1.00 47.29 ?  750 HOH A O   1 
HETATM 3080 O O   . HOH C 3 .   ? -20.545 -9.596  -10.352 1.00 56.07 ?  751 HOH A O   1 
HETATM 3081 O O   . HOH C 3 .   ? -23.583 19.104  -23.979 1.00 44.47 ?  752 HOH A O   1 
HETATM 3082 O O   . HOH C 3 .   ? 11.649  -3.946  -23.744 1.00 35.74 ?  753 HOH A O   1 
HETATM 3083 O O   . HOH C 3 .   ? -22.552 -7.943  -10.604 1.00 42.44 ?  754 HOH A O   1 
HETATM 3084 O O   . HOH C 3 .   ? -2.827  19.296  -6.587  1.00 51.60 ?  755 HOH A O   1 
HETATM 3085 O O   . HOH C 3 .   ? 7.213   9.932   6.594   1.00 40.47 ?  756 HOH A O   1 
HETATM 3086 O O   . HOH C 3 .   ? 16.188  6.870   -17.169 1.00 25.96 ?  757 HOH A O   1 
HETATM 3087 O O   . HOH C 3 .   ? -22.804 9.412   -24.485 1.00 50.56 ?  758 HOH A O   1 
HETATM 3088 O O   . HOH C 3 .   ? 11.846  10.861  -15.865 1.00 34.88 ?  759 HOH A O   1 
HETATM 3089 O O   . HOH C 3 .   ? -5.336  18.287  -36.317 1.00 38.24 ?  760 HOH A O   1 
HETATM 3090 O O   . HOH C 3 .   ? -8.271  -18.122 -23.121 1.00 44.09 ?  761 HOH A O   1 
HETATM 3091 O O   . HOH C 3 .   ? 11.011  9.834   -22.023 1.00 55.44 ?  762 HOH A O   1 
HETATM 3092 O O   . HOH C 3 .   ? -12.953 0.290   -45.974 1.00 35.39 ?  763 HOH A O   1 
HETATM 3093 O O   . HOH C 3 .   ? 17.734  11.394  -12.666 1.00 45.23 ?  764 HOH A O   1 
HETATM 3094 O O   . HOH C 3 .   ? 12.809  1.583   -3.809  1.00 33.50 ?  765 HOH A O   1 
HETATM 3095 O O   . HOH C 3 .   ? -8.160  8.090   -46.128 1.00 48.36 ?  766 HOH A O   1 
HETATM 3096 O O   . HOH C 3 .   ? -7.697  5.499   -46.967 1.00 54.03 ?  767 HOH A O   1 
HETATM 3097 O O   . HOH C 3 .   ? -9.941  -11.577 -6.911  1.00 39.35 ?  768 HOH A O   1 
HETATM 3098 O O   . HOH C 3 .   ? -20.634 -14.585 -19.418 1.00 43.14 ?  769 HOH A O   1 
HETATM 3099 O O   . HOH C 3 .   ? 10.933  2.747   0.812   1.00 37.35 ?  770 HOH A O   1 
HETATM 3100 O O   . HOH C 3 .   ? 14.931  0.148   -4.796  1.00 34.55 ?  771 HOH A O   1 
HETATM 3101 O O   . HOH C 3 .   ? 18.292  -0.182  -10.138 1.00 28.92 ?  772 HOH A O   1 
HETATM 3102 O O   . HOH C 3 .   ? 15.872  9.400   -16.445 1.00 27.32 ?  773 HOH A O   1 
HETATM 3103 O O   . HOH C 3 .   ? 12.446  11.776  -18.123 1.00 38.93 ?  774 HOH A O   1 
HETATM 3104 O O   . HOH C 3 .   ? -4.692  15.971  4.773   1.00 51.06 ?  775 HOH A O   1 
HETATM 3105 O O   . HOH C 3 .   ? -25.368 0.882   -38.243 1.00 50.53 ?  776 HOH A O   1 
HETATM 3106 O O   . HOH C 3 .   ? 0.699   12.000  5.650   1.00 44.13 ?  777 HOH A O   1 
HETATM 3107 O O   . HOH C 3 .   ? 9.794   11.881  -14.418 1.00 36.54 ?  778 HOH A O   1 
HETATM 3108 O O   . HOH C 3 .   ? 11.538  11.880  -11.914 1.00 49.28 ?  779 HOH A O   1 
HETATM 3109 O O   . HOH C 3 .   ? 13.255  8.037   -6.259  1.00 34.32 ?  780 HOH A O   1 
HETATM 3110 O O   . HOH C 3 .   ? 15.086  6.428   -19.503 1.00 26.95 ?  781 HOH A O   1 
HETATM 3111 O O   . HOH C 3 .   ? 11.195  7.290   -22.791 1.00 49.74 ?  782 HOH A O   1 
HETATM 3112 O O   . HOH C 3 .   ? -13.547 9.683   -49.902 1.00 44.61 ?  783 HOH A O   1 
HETATM 3113 O O   . HOH C 3 .   ? 19.787  1.304   -11.661 1.00 32.85 ?  784 HOH A O   1 
HETATM 3114 O O   . HOH C 3 .   ? -31.165 5.782   -4.571  1.00 34.32 ?  785 HOH A O   1 
HETATM 3115 O O   . HOH C 3 .   ? 10.515  -4.407  8.684   1.00 48.73 ?  786 HOH A O   1 
HETATM 3116 O O   . HOH C 3 .   ? -19.517 14.112  -9.092  1.00 44.50 ?  787 HOH A O   1 
HETATM 3117 O O   . HOH C 3 .   ? -19.398 17.023  7.990   1.00 35.83 ?  788 HOH A O   1 
HETATM 3118 O O   . HOH C 3 .   ? -22.292 6.529   -18.448 1.00 43.15 ?  789 HOH A O   1 
HETATM 3119 O O   . HOH C 3 .   ? 4.211   15.999  -12.468 1.00 49.56 ?  790 HOH A O   1 
HETATM 3120 O O   . HOH C 3 .   ? 1.994   17.573  -30.429 1.00 33.63 ?  791 HOH A O   1 
HETATM 3121 O O   . HOH C 3 .   ? 7.831   14.503  -11.645 1.00 48.71 ?  792 HOH A O   1 
HETATM 3122 O O   . HOH C 3 .   ? 10.834  14.740  -17.474 1.00 51.10 ?  793 HOH A O   1 
HETATM 3123 O O   . HOH C 3 .   ? -25.852 1.055   -5.800  1.00 42.57 ?  794 HOH A O   1 
HETATM 3124 O O   . HOH C 3 .   ? -19.250 16.763  -8.274  1.00 46.18 ?  795 HOH A O   1 
HETATM 3125 O O   . HOH C 3 .   ? -5.605  -9.843  -32.993 1.00 39.99 ?  796 HOH A O   1 
HETATM 3126 O O   . HOH C 3 .   ? -28.400 1.940   -6.642  1.00 31.38 ?  797 HOH A O   1 
HETATM 3127 O O   . HOH C 3 .   ? 13.293  -0.933  -29.652 1.00 44.18 ?  798 HOH A O   1 
HETATM 3128 O O   . HOH C 3 .   ? 14.839  8.808   -20.411 1.00 39.51 ?  799 HOH A O   1 
HETATM 3129 O O   . HOH C 3 .   ? 15.071  10.850  -18.503 1.00 38.15 ?  800 HOH A O   1 
# 
