data_9F31
# 
_entry.id   9F31 
# 
_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   9F31         pdb_00009f31 10.2210/pdb9f31/pdb 
WWPDB D_1292137756 ?            ?                   
# 
_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       2025-03-05 
_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                        9F31 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-24 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 knapp@pharmchem.uni-frankfurt.de    Stefan   Knapp     ? 'principal investigator/group leader' 0000-0001-5995-6494 
3 matthias.gehringer@uni-tuebingen.de Matthias Gehringer ? 'principal investigator/group leader' 0000-0003-0163-3419 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Wang, G.Q.'                           1 0000-0003-2896-3928 
'Seidler, N.'                          2 0009-0007-4405-2397 
'Gehringer, M.'                        3 0000-0003-0163-3419 
'Knapp, S.'                            4 0000-0001-5995-6494 
'Structural Genomics Consortium (SGC)' 5 ?                   
# 
_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                   GE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Angew.Chem.Int.Ed.Engl. 
_citation.journal_id_ASTM           ACIEAY 
_citation.journal_id_CSD            0179 
_citation.journal_id_ISSN           1521-3773 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            64 
_citation.language                  ? 
_citation.page_first                e202419736 
_citation.page_last                 e202419736 
_citation.title                     
;Probing the Protein Kinases' Cysteinome by Covalent Fragments.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/anie.202419736 
_citation.pdbx_database_id_PubMed   39716901 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Wang, G.'            1  ?                   
primary 'Seidler, N.J.'       2  0009-0007-4405-2397 
primary 'Rohm, S.'            3  0000-0003-3999-712X 
primary 'Pan, Y.'             4  ?                   
primary 'Liang, X.J.'         5  ?                   
primary 'Haarer, L.'          6  ?                   
primary 'Berger, B.T.'        7  0000-0002-3314-2617 
primary 'Sivashanmugam, S.A.' 8  ?                   
primary 'Wydra, V.R.'         9  0009-0004-3295-0526 
primary 'Forster, M.'         10 ?                   
primary 'Laufer, S.A.'        11 0000-0001-6952-1486 
primary 'Chaikuad, A.'        12 0000-0003-1120-2209 
primary 'Gehringer, M.'       13 0000-0003-0163-3419 
primary 'Knapp, S.'           14 0000-0001-5995-6494 
# 
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 'Maternal embryonic leucine zipper kinase' 40259.633 1   2.7.11.1,2.7.10.2 ? ? ? 
2 non-polymer syn 'N-[4-(1H-indazol-5-yl)phenyl]propanamide' 265.310   1   ?                 ? ? ? 
3 water       nat water                                      18.015    123 ?                 ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'hMELK,Protein kinase Eg3,pEg3 kinase,Protein kinase PK38,hPK38,Tyrosine-protein kinase MELK' 
# 
_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       
;SMKDYDELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETA
NKIFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKG
NKDYHLQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILL
LQQMLQVDPKKRISMKNLLNHPWIMQDYNYPVEWQSKNPFIHLDDDCVTELSVHHRNNRQTMEDLISLWQYDHLTATYLL
LLAKKARGKPVRLRLSSFSCGQASATPFT
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMKDYDELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETA
NKIFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKG
NKDYHLQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILL
LQQMLQVDPKKRISMKNLLNHPWIMQDYNYPVEWQSKNPFIHLDDDCVTELSVHHRNNRQTMEDLISLWQYDHLTATYLL
LLAKKARGKPVRLRLSSFSCGQASATPFT
;
_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 'N-[4-(1H-indazol-5-yl)phenyl]propanamide' A1H9M 
3 water                                      HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   LYS n 
1 4   ASP n 
1 5   TYR n 
1 6   ASP n 
1 7   GLU n 
1 8   LEU n 
1 9   LEU n 
1 10  LYS n 
1 11  TYR n 
1 12  TYR n 
1 13  GLU n 
1 14  LEU n 
1 15  HIS n 
1 16  GLU n 
1 17  THR n 
1 18  ILE n 
1 19  GLY n 
1 20  THR n 
1 21  GLY n 
1 22  GLY n 
1 23  PHE n 
1 24  ALA n 
1 25  LYS n 
1 26  VAL n 
1 27  LYS n 
1 28  LEU n 
1 29  ALA n 
1 30  CYS n 
1 31  HIS n 
1 32  ILE n 
1 33  LEU n 
1 34  THR n 
1 35  GLY n 
1 36  GLU n 
1 37  MET n 
1 38  VAL n 
1 39  ALA n 
1 40  ILE n 
1 41  LYS n 
1 42  ILE n 
1 43  MET n 
1 44  ASP n 
1 45  LYS n 
1 46  ASN n 
1 47  THR n 
1 48  LEU n 
1 49  GLY n 
1 50  SER n 
1 51  ASP n 
1 52  LEU n 
1 53  PRO n 
1 54  ARG n 
1 55  ILE n 
1 56  LYS n 
1 57  THR n 
1 58  GLU n 
1 59  ILE n 
1 60  GLU n 
1 61  ALA n 
1 62  LEU n 
1 63  LYS n 
1 64  ASN n 
1 65  LEU n 
1 66  ARG n 
1 67  HIS n 
1 68  GLN n 
1 69  HIS n 
1 70  ILE n 
1 71  CYS n 
1 72  GLN n 
1 73  LEU n 
1 74  TYR n 
1 75  HIS n 
1 76  VAL n 
1 77  LEU n 
1 78  GLU n 
1 79  THR n 
1 80  ALA n 
1 81  ASN n 
1 82  LYS n 
1 83  ILE n 
1 84  PHE n 
1 85  MET n 
1 86  VAL n 
1 87  LEU n 
1 88  GLU n 
1 89  TYR n 
1 90  CYS n 
1 91  PRO n 
1 92  GLY n 
1 93  GLY n 
1 94  GLU n 
1 95  LEU n 
1 96  PHE n 
1 97  ASP n 
1 98  TYR n 
1 99  ILE n 
1 100 ILE n 
1 101 SER n 
1 102 GLN n 
1 103 ASP n 
1 104 ARG n 
1 105 LEU n 
1 106 SER n 
1 107 GLU n 
1 108 GLU n 
1 109 GLU n 
1 110 THR n 
1 111 ARG n 
1 112 VAL n 
1 113 VAL n 
1 114 PHE n 
1 115 ARG n 
1 116 GLN n 
1 117 ILE n 
1 118 VAL n 
1 119 SER n 
1 120 ALA n 
1 121 VAL n 
1 122 ALA n 
1 123 TYR n 
1 124 VAL n 
1 125 HIS n 
1 126 SER n 
1 127 GLN n 
1 128 GLY n 
1 129 TYR n 
1 130 ALA n 
1 131 HIS n 
1 132 ARG n 
1 133 ASP n 
1 134 LEU n 
1 135 LYS n 
1 136 PRO n 
1 137 GLU n 
1 138 ASN n 
1 139 LEU n 
1 140 LEU n 
1 141 PHE n 
1 142 ASP n 
1 143 GLU n 
1 144 TYR n 
1 145 HIS n 
1 146 LYS n 
1 147 LEU n 
1 148 LYS n 
1 149 LEU n 
1 150 ILE n 
1 151 ASP n 
1 152 PHE n 
1 153 GLY n 
1 154 LEU n 
1 155 CYS n 
1 156 ALA n 
1 157 LYS n 
1 158 PRO n 
1 159 LYS n 
1 160 GLY n 
1 161 ASN n 
1 162 LYS n 
1 163 ASP n 
1 164 TYR n 
1 165 HIS n 
1 166 LEU n 
1 167 GLN n 
1 168 THR n 
1 169 CYS n 
1 170 CYS n 
1 171 GLY n 
1 172 SER n 
1 173 LEU n 
1 174 ALA n 
1 175 TYR n 
1 176 ALA n 
1 177 ALA n 
1 178 PRO n 
1 179 GLU n 
1 180 LEU n 
1 181 ILE n 
1 182 GLN n 
1 183 GLY n 
1 184 LYS n 
1 185 SER n 
1 186 TYR n 
1 187 LEU n 
1 188 GLY n 
1 189 SER n 
1 190 GLU n 
1 191 ALA n 
1 192 ASP n 
1 193 VAL n 
1 194 TRP n 
1 195 SER n 
1 196 MET n 
1 197 GLY n 
1 198 ILE n 
1 199 LEU n 
1 200 LEU n 
1 201 TYR n 
1 202 VAL n 
1 203 LEU n 
1 204 MET n 
1 205 CYS n 
1 206 GLY n 
1 207 PHE n 
1 208 LEU n 
1 209 PRO n 
1 210 PHE n 
1 211 ASP n 
1 212 ASP n 
1 213 ASP n 
1 214 ASN n 
1 215 VAL n 
1 216 MET n 
1 217 ALA n 
1 218 LEU n 
1 219 TYR n 
1 220 LYS n 
1 221 LYS n 
1 222 ILE n 
1 223 MET n 
1 224 ARG n 
1 225 GLY n 
1 226 LYS n 
1 227 TYR n 
1 228 ASP n 
1 229 VAL n 
1 230 PRO n 
1 231 LYS n 
1 232 TRP n 
1 233 LEU n 
1 234 SER n 
1 235 PRO n 
1 236 SER n 
1 237 SER n 
1 238 ILE n 
1 239 LEU n 
1 240 LEU n 
1 241 LEU n 
1 242 GLN n 
1 243 GLN n 
1 244 MET n 
1 245 LEU n 
1 246 GLN n 
1 247 VAL n 
1 248 ASP n 
1 249 PRO n 
1 250 LYS n 
1 251 LYS n 
1 252 ARG n 
1 253 ILE n 
1 254 SER n 
1 255 MET n 
1 256 LYS n 
1 257 ASN n 
1 258 LEU n 
1 259 LEU n 
1 260 ASN n 
1 261 HIS n 
1 262 PRO n 
1 263 TRP n 
1 264 ILE n 
1 265 MET n 
1 266 GLN n 
1 267 ASP n 
1 268 TYR n 
1 269 ASN n 
1 270 TYR n 
1 271 PRO n 
1 272 VAL n 
1 273 GLU n 
1 274 TRP n 
1 275 GLN n 
1 276 SER n 
1 277 LYS n 
1 278 ASN n 
1 279 PRO n 
1 280 PHE n 
1 281 ILE n 
1 282 HIS n 
1 283 LEU n 
1 284 ASP n 
1 285 ASP n 
1 286 ASP n 
1 287 CYS n 
1 288 VAL n 
1 289 THR n 
1 290 GLU n 
1 291 LEU n 
1 292 SER n 
1 293 VAL n 
1 294 HIS n 
1 295 HIS n 
1 296 ARG n 
1 297 ASN n 
1 298 ASN n 
1 299 ARG n 
1 300 GLN n 
1 301 THR n 
1 302 MET n 
1 303 GLU n 
1 304 ASP n 
1 305 LEU n 
1 306 ILE n 
1 307 SER n 
1 308 LEU n 
1 309 TRP n 
1 310 GLN n 
1 311 TYR n 
1 312 ASP n 
1 313 HIS n 
1 314 LEU n 
1 315 THR n 
1 316 ALA n 
1 317 THR n 
1 318 TYR n 
1 319 LEU n 
1 320 LEU n 
1 321 LEU n 
1 322 LEU n 
1 323 ALA n 
1 324 LYS n 
1 325 LYS n 
1 326 ALA n 
1 327 ARG n 
1 328 GLY n 
1 329 LYS n 
1 330 PRO n 
1 331 VAL n 
1 332 ARG n 
1 333 LEU n 
1 334 ARG n 
1 335 LEU n 
1 336 SER n 
1 337 SER n 
1 338 PHE n 
1 339 SER n 
1 340 CYS n 
1 341 GLY n 
1 342 GLN n 
1 343 ALA n 
1 344 SER n 
1 345 ALA n 
1 346 THR n 
1 347 PRO n 
1 348 PHE n 
1 349 THR 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                   349 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'MELK, KIAA0175' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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 
A1H9M non-polymer         . 'N-[4-(1H-indazol-5-yl)phenyl]propanamide' 
'N-[4-(1H-indazol-5-yl)phenyl]prop-2-enamide (covalently bound)' 'C16 H15 N3 O'   265.310 
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 
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   SER 1   0   ?   ?   ?   A . n 
A 1 2   MET 2   1   1   MET MET A . n 
A 1 3   LYS 3   2   2   LYS LYS A . n 
A 1 4   ASP 4   3   3   ASP ASP A . n 
A 1 5   TYR 5   4   4   TYR TYR A . n 
A 1 6   ASP 6   5   5   ASP ASP A . n 
A 1 7   GLU 7   6   6   GLU GLU A . n 
A 1 8   LEU 8   7   7   LEU LEU A . n 
A 1 9   LEU 9   8   8   LEU LEU A . n 
A 1 10  LYS 10  9   9   LYS LYS A . n 
A 1 11  TYR 11  10  10  TYR TYR A . n 
A 1 12  TYR 12  11  11  TYR TYR A . n 
A 1 13  GLU 13  12  12  GLU GLU A . n 
A 1 14  LEU 14  13  13  LEU LEU A . n 
A 1 15  HIS 15  14  14  HIS HIS A . n 
A 1 16  GLU 16  15  15  GLU GLU A . n 
A 1 17  THR 17  16  16  THR THR A . n 
A 1 18  ILE 18  17  17  ILE ILE A . n 
A 1 19  GLY 19  18  18  GLY GLY A . n 
A 1 20  THR 20  19  19  THR THR A . n 
A 1 21  GLY 21  20  20  GLY GLY A . n 
A 1 22  GLY 22  21  21  GLY GLY A . n 
A 1 23  PHE 23  22  22  PHE PHE A . n 
A 1 24  ALA 24  23  23  ALA ALA A . n 
A 1 25  LYS 25  24  24  LYS LYS A . n 
A 1 26  VAL 26  25  25  VAL VAL A . n 
A 1 27  LYS 27  26  26  LYS LYS A . n 
A 1 28  LEU 28  27  27  LEU LEU A . n 
A 1 29  ALA 29  28  28  ALA ALA A . n 
A 1 30  CYS 30  29  29  CYS CYS A . n 
A 1 31  HIS 31  30  30  HIS HIS A . n 
A 1 32  ILE 32  31  31  ILE ILE A . n 
A 1 33  LEU 33  32  32  LEU LEU A . n 
A 1 34  THR 34  33  33  THR THR A . n 
A 1 35  GLY 35  34  34  GLY GLY A . n 
A 1 36  GLU 36  35  35  GLU GLU A . n 
A 1 37  MET 37  36  36  MET MET A . n 
A 1 38  VAL 38  37  37  VAL VAL A . n 
A 1 39  ALA 39  38  38  ALA ALA A . n 
A 1 40  ILE 40  39  39  ILE ILE A . n 
A 1 41  LYS 41  40  40  LYS LYS A . n 
A 1 42  ILE 42  41  41  ILE ILE A . n 
A 1 43  MET 43  42  42  MET MET A . n 
A 1 44  ASP 44  43  43  ASP ASP A . n 
A 1 45  LYS 45  44  44  LYS LYS A . n 
A 1 46  ASN 46  45  45  ASN ASN A . n 
A 1 47  THR 47  46  46  THR THR A . n 
A 1 48  LEU 48  47  47  LEU LEU A . n 
A 1 49  GLY 49  48  48  GLY GLY A . n 
A 1 50  SER 50  49  49  SER SER A . n 
A 1 51  ASP 51  50  50  ASP ASP A . n 
A 1 52  LEU 52  51  51  LEU LEU A . n 
A 1 53  PRO 53  52  52  PRO PRO A . n 
A 1 54  ARG 54  53  53  ARG ARG A . n 
A 1 55  ILE 55  54  54  ILE ILE A . n 
A 1 56  LYS 56  55  55  LYS LYS A . n 
A 1 57  THR 57  56  56  THR THR A . n 
A 1 58  GLU 58  57  57  GLU GLU A . n 
A 1 59  ILE 59  58  58  ILE ILE A . n 
A 1 60  GLU 60  59  59  GLU GLU A . n 
A 1 61  ALA 61  60  60  ALA ALA A . n 
A 1 62  LEU 62  61  61  LEU LEU A . n 
A 1 63  LYS 63  62  62  LYS LYS A . n 
A 1 64  ASN 64  63  63  ASN ASN A . n 
A 1 65  LEU 65  64  64  LEU LEU A . n 
A 1 66  ARG 66  65  65  ARG ARG A . n 
A 1 67  HIS 67  66  66  HIS HIS A . n 
A 1 68  GLN 68  67  67  GLN GLN A . n 
A 1 69  HIS 69  68  68  HIS HIS A . n 
A 1 70  ILE 70  69  69  ILE ILE A . n 
A 1 71  CYS 71  70  70  CYS CYS A . n 
A 1 72  GLN 72  71  71  GLN GLN A . n 
A 1 73  LEU 73  72  72  LEU LEU A . n 
A 1 74  TYR 74  73  73  TYR TYR A . n 
A 1 75  HIS 75  74  74  HIS HIS A . n 
A 1 76  VAL 76  75  75  VAL VAL A . n 
A 1 77  LEU 77  76  76  LEU LEU A . n 
A 1 78  GLU 78  77  77  GLU GLU A . n 
A 1 79  THR 79  78  78  THR THR A . n 
A 1 80  ALA 80  79  79  ALA ALA A . n 
A 1 81  ASN 81  80  80  ASN ASN A . n 
A 1 82  LYS 82  81  81  LYS LYS A . n 
A 1 83  ILE 83  82  82  ILE ILE A . n 
A 1 84  PHE 84  83  83  PHE PHE A . n 
A 1 85  MET 85  84  84  MET MET A . n 
A 1 86  VAL 86  85  85  VAL VAL A . n 
A 1 87  LEU 87  86  86  LEU LEU A . n 
A 1 88  GLU 88  87  87  GLU GLU A . n 
A 1 89  TYR 89  88  88  TYR TYR A . n 
A 1 90  CYS 90  89  89  CYS CYS A . n 
A 1 91  PRO 91  90  90  PRO PRO A . n 
A 1 92  GLY 92  91  91  GLY GLY A . n 
A 1 93  GLY 93  92  92  GLY GLY A . n 
A 1 94  GLU 94  93  93  GLU GLU A . n 
A 1 95  LEU 95  94  94  LEU LEU A . n 
A 1 96  PHE 96  95  95  PHE PHE A . n 
A 1 97  ASP 97  96  96  ASP ASP A . n 
A 1 98  TYR 98  97  97  TYR TYR A . n 
A 1 99  ILE 99  98  98  ILE ILE A . n 
A 1 100 ILE 100 99  99  ILE ILE A . n 
A 1 101 SER 101 100 100 SER SER A . n 
A 1 102 GLN 102 101 101 GLN GLN A . n 
A 1 103 ASP 103 102 102 ASP ASP A . n 
A 1 104 ARG 104 103 103 ARG ARG A . n 
A 1 105 LEU 105 104 104 LEU LEU A . n 
A 1 106 SER 106 105 105 SER SER A . n 
A 1 107 GLU 107 106 106 GLU GLU A . n 
A 1 108 GLU 108 107 107 GLU GLU A . n 
A 1 109 GLU 109 108 108 GLU GLU A . n 
A 1 110 THR 110 109 109 THR THR A . n 
A 1 111 ARG 111 110 110 ARG ARG A . n 
A 1 112 VAL 112 111 111 VAL VAL A . n 
A 1 113 VAL 113 112 112 VAL VAL A . n 
A 1 114 PHE 114 113 113 PHE PHE A . n 
A 1 115 ARG 115 114 114 ARG ARG A . n 
A 1 116 GLN 116 115 115 GLN GLN A . n 
A 1 117 ILE 117 116 116 ILE ILE A . n 
A 1 118 VAL 118 117 117 VAL VAL A . n 
A 1 119 SER 119 118 118 SER SER A . n 
A 1 120 ALA 120 119 119 ALA ALA A . n 
A 1 121 VAL 121 120 120 VAL VAL A . n 
A 1 122 ALA 122 121 121 ALA ALA A . n 
A 1 123 TYR 123 122 122 TYR TYR A . n 
A 1 124 VAL 124 123 123 VAL VAL A . n 
A 1 125 HIS 125 124 124 HIS HIS A . n 
A 1 126 SER 126 125 125 SER SER A . n 
A 1 127 GLN 127 126 126 GLN GLN A . n 
A 1 128 GLY 128 127 127 GLY GLY A . n 
A 1 129 TYR 129 128 128 TYR TYR A . n 
A 1 130 ALA 130 129 129 ALA ALA A . n 
A 1 131 HIS 131 130 130 HIS HIS A . n 
A 1 132 ARG 132 131 131 ARG ARG A . n 
A 1 133 ASP 133 132 132 ASP ASP A . n 
A 1 134 LEU 134 133 133 LEU LEU A . n 
A 1 135 LYS 135 134 134 LYS LYS A . n 
A 1 136 PRO 136 135 135 PRO PRO A . n 
A 1 137 GLU 137 136 136 GLU GLU A . n 
A 1 138 ASN 138 137 137 ASN ASN A . n 
A 1 139 LEU 139 138 138 LEU LEU A . n 
A 1 140 LEU 140 139 139 LEU LEU A . n 
A 1 141 PHE 141 140 140 PHE PHE A . n 
A 1 142 ASP 142 141 141 ASP ASP A . n 
A 1 143 GLU 143 142 142 GLU GLU A . n 
A 1 144 TYR 144 143 143 TYR TYR A . n 
A 1 145 HIS 145 144 144 HIS HIS A . n 
A 1 146 LYS 146 145 145 LYS LYS A . n 
A 1 147 LEU 147 146 146 LEU LEU A . n 
A 1 148 LYS 148 147 147 LYS LYS A . n 
A 1 149 LEU 149 148 148 LEU LEU A . n 
A 1 150 ILE 150 149 149 ILE ILE A . n 
A 1 151 ASP 151 150 150 ASP ASP A . n 
A 1 152 PHE 152 151 151 PHE PHE A . n 
A 1 153 GLY 153 152 152 GLY GLY A . n 
A 1 154 LEU 154 153 153 LEU LEU A . n 
A 1 155 CYS 155 154 154 CYS CYS A . n 
A 1 156 ALA 156 155 155 ALA ALA A . n 
A 1 157 LYS 157 156 ?   ?   ?   A . n 
A 1 158 PRO 158 157 ?   ?   ?   A . n 
A 1 159 LYS 159 158 ?   ?   ?   A . n 
A 1 160 GLY 160 159 ?   ?   ?   A . n 
A 1 161 ASN 161 160 ?   ?   ?   A . n 
A 1 162 LYS 162 161 ?   ?   ?   A . n 
A 1 163 ASP 163 162 ?   ?   ?   A . n 
A 1 164 TYR 164 163 ?   ?   ?   A . n 
A 1 165 HIS 165 164 ?   ?   ?   A . n 
A 1 166 LEU 166 165 ?   ?   ?   A . n 
A 1 167 GLN 167 166 ?   ?   ?   A . n 
A 1 168 THR 168 167 ?   ?   ?   A . n 
A 1 169 CYS 169 168 ?   ?   ?   A . n 
A 1 170 CYS 170 169 ?   ?   ?   A . n 
A 1 171 GLY 171 170 ?   ?   ?   A . n 
A 1 172 SER 172 171 171 SER SER A . n 
A 1 173 LEU 173 172 172 LEU LEU A . n 
A 1 174 ALA 174 173 173 ALA ALA A . n 
A 1 175 TYR 175 174 174 TYR TYR A . n 
A 1 176 ALA 176 175 175 ALA ALA A . n 
A 1 177 ALA 177 176 176 ALA ALA A . n 
A 1 178 PRO 178 177 177 PRO PRO A . n 
A 1 179 GLU 179 178 178 GLU GLU A . n 
A 1 180 LEU 180 179 179 LEU LEU A . n 
A 1 181 ILE 181 180 180 ILE ILE A . n 
A 1 182 GLN 182 181 181 GLN GLN A . n 
A 1 183 GLY 183 182 182 GLY GLY A . n 
A 1 184 LYS 184 183 183 LYS LYS A . n 
A 1 185 SER 185 184 184 SER SER A . n 
A 1 186 TYR 186 185 185 TYR TYR A . n 
A 1 187 LEU 187 186 186 LEU LEU A . n 
A 1 188 GLY 188 187 187 GLY GLY A . n 
A 1 189 SER 189 188 188 SER SER A . n 
A 1 190 GLU 190 189 189 GLU GLU A . n 
A 1 191 ALA 191 190 190 ALA ALA A . n 
A 1 192 ASP 192 191 191 ASP ASP A . n 
A 1 193 VAL 193 192 192 VAL VAL A . n 
A 1 194 TRP 194 193 193 TRP TRP A . n 
A 1 195 SER 195 194 194 SER SER A . n 
A 1 196 MET 196 195 195 MET MET A . n 
A 1 197 GLY 197 196 196 GLY GLY A . n 
A 1 198 ILE 198 197 197 ILE ILE A . n 
A 1 199 LEU 199 198 198 LEU LEU A . n 
A 1 200 LEU 200 199 199 LEU LEU A . n 
A 1 201 TYR 201 200 200 TYR TYR A . n 
A 1 202 VAL 202 201 201 VAL VAL A . n 
A 1 203 LEU 203 202 202 LEU LEU A . n 
A 1 204 MET 204 203 203 MET MET A . n 
A 1 205 CYS 205 204 204 CYS CYS A . n 
A 1 206 GLY 206 205 205 GLY GLY A . n 
A 1 207 PHE 207 206 206 PHE PHE A . n 
A 1 208 LEU 208 207 207 LEU LEU A . n 
A 1 209 PRO 209 208 208 PRO PRO A . n 
A 1 210 PHE 210 209 209 PHE PHE A . n 
A 1 211 ASP 211 210 210 ASP ASP A . n 
A 1 212 ASP 212 211 211 ASP ASP A . n 
A 1 213 ASP 213 212 212 ASP ASP A . n 
A 1 214 ASN 214 213 213 ASN ASN A . n 
A 1 215 VAL 215 214 214 VAL VAL A . n 
A 1 216 MET 216 215 215 MET MET A . n 
A 1 217 ALA 217 216 216 ALA ALA A . n 
A 1 218 LEU 218 217 217 LEU LEU A . n 
A 1 219 TYR 219 218 218 TYR TYR A . n 
A 1 220 LYS 220 219 219 LYS LYS A . n 
A 1 221 LYS 221 220 220 LYS LYS A . n 
A 1 222 ILE 222 221 221 ILE ILE A . n 
A 1 223 MET 223 222 222 MET MET A . n 
A 1 224 ARG 224 223 223 ARG ARG A . n 
A 1 225 GLY 225 224 224 GLY GLY A . n 
A 1 226 LYS 226 225 225 LYS LYS A . n 
A 1 227 TYR 227 226 226 TYR TYR A . n 
A 1 228 ASP 228 227 227 ASP ASP A . n 
A 1 229 VAL 229 228 228 VAL VAL A . n 
A 1 230 PRO 230 229 229 PRO PRO A . n 
A 1 231 LYS 231 230 230 LYS LYS A . n 
A 1 232 TRP 232 231 231 TRP TRP A . n 
A 1 233 LEU 233 232 232 LEU LEU A . n 
A 1 234 SER 234 233 233 SER SER A . n 
A 1 235 PRO 235 234 234 PRO PRO A . n 
A 1 236 SER 236 235 235 SER SER A . n 
A 1 237 SER 237 236 236 SER SER A . n 
A 1 238 ILE 238 237 237 ILE ILE A . n 
A 1 239 LEU 239 238 238 LEU LEU A . n 
A 1 240 LEU 240 239 239 LEU LEU A . n 
A 1 241 LEU 241 240 240 LEU LEU A . n 
A 1 242 GLN 242 241 241 GLN GLN A . n 
A 1 243 GLN 243 242 242 GLN GLN A . n 
A 1 244 MET 244 243 243 MET MET A . n 
A 1 245 LEU 245 244 244 LEU LEU A . n 
A 1 246 GLN 246 245 245 GLN GLN A . n 
A 1 247 VAL 247 246 246 VAL VAL A . n 
A 1 248 ASP 248 247 247 ASP ASP A . n 
A 1 249 PRO 249 248 248 PRO PRO A . n 
A 1 250 LYS 250 249 249 LYS LYS A . n 
A 1 251 LYS 251 250 250 LYS LYS A . n 
A 1 252 ARG 252 251 251 ARG ARG A . n 
A 1 253 ILE 253 252 252 ILE ILE A . n 
A 1 254 SER 254 253 253 SER SER A . n 
A 1 255 MET 255 254 254 MET MET A . n 
A 1 256 LYS 256 255 255 LYS LYS A . n 
A 1 257 ASN 257 256 256 ASN ASN A . n 
A 1 258 LEU 258 257 257 LEU LEU A . n 
A 1 259 LEU 259 258 258 LEU LEU A . n 
A 1 260 ASN 260 259 259 ASN ASN A . n 
A 1 261 HIS 261 260 260 HIS HIS A . n 
A 1 262 PRO 262 261 261 PRO PRO A . n 
A 1 263 TRP 263 262 262 TRP TRP A . n 
A 1 264 ILE 264 263 263 ILE ILE A . n 
A 1 265 MET 265 264 264 MET MET A . n 
A 1 266 GLN 266 265 265 GLN GLN A . n 
A 1 267 ASP 267 266 266 ASP ASP A . n 
A 1 268 TYR 268 267 267 TYR TYR A . n 
A 1 269 ASN 269 268 268 ASN ASN A . n 
A 1 270 TYR 270 269 269 TYR TYR A . n 
A 1 271 PRO 271 270 270 PRO PRO A . n 
A 1 272 VAL 272 271 271 VAL VAL A . n 
A 1 273 GLU 273 272 272 GLU GLU A . n 
A 1 274 TRP 274 273 273 TRP TRP A . n 
A 1 275 GLN 275 274 274 GLN GLN A . n 
A 1 276 SER 276 275 275 SER SER A . n 
A 1 277 LYS 277 276 276 LYS LYS A . n 
A 1 278 ASN 278 277 277 ASN ASN A . n 
A 1 279 PRO 279 278 278 PRO PRO A . n 
A 1 280 PHE 280 279 279 PHE PHE A . n 
A 1 281 ILE 281 280 280 ILE ILE A . n 
A 1 282 HIS 282 281 281 HIS HIS A . n 
A 1 283 LEU 283 282 282 LEU LEU A . n 
A 1 284 ASP 284 283 283 ASP ASP A . n 
A 1 285 ASP 285 284 284 ASP ASP A . n 
A 1 286 ASP 286 285 285 ASP ASP A . n 
A 1 287 CYS 287 286 286 CYS CYS A . n 
A 1 288 VAL 288 287 287 VAL VAL A . n 
A 1 289 THR 289 288 288 THR THR A . n 
A 1 290 GLU 290 289 289 GLU GLU A . n 
A 1 291 LEU 291 290 290 LEU LEU A . n 
A 1 292 SER 292 291 291 SER SER A . n 
A 1 293 VAL 293 292 292 VAL VAL A . n 
A 1 294 HIS 294 293 293 HIS HIS A . n 
A 1 295 HIS 295 294 294 HIS HIS A . n 
A 1 296 ARG 296 295 295 ARG ARG A . n 
A 1 297 ASN 297 296 296 ASN ASN A . n 
A 1 298 ASN 298 297 297 ASN ASN A . n 
A 1 299 ARG 299 298 298 ARG ARG A . n 
A 1 300 GLN 300 299 299 GLN GLN A . n 
A 1 301 THR 301 300 300 THR THR A . n 
A 1 302 MET 302 301 301 MET MET A . n 
A 1 303 GLU 303 302 302 GLU GLU A . n 
A 1 304 ASP 304 303 303 ASP ASP A . n 
A 1 305 LEU 305 304 304 LEU LEU A . n 
A 1 306 ILE 306 305 305 ILE ILE A . n 
A 1 307 SER 307 306 306 SER SER A . n 
A 1 308 LEU 308 307 307 LEU LEU A . n 
A 1 309 TRP 309 308 308 TRP TRP A . n 
A 1 310 GLN 310 309 309 GLN GLN A . n 
A 1 311 TYR 311 310 310 TYR TYR A . n 
A 1 312 ASP 312 311 311 ASP ASP A . n 
A 1 313 HIS 313 312 312 HIS HIS A . n 
A 1 314 LEU 314 313 313 LEU LEU A . n 
A 1 315 THR 315 314 314 THR THR A . n 
A 1 316 ALA 316 315 315 ALA ALA A . n 
A 1 317 THR 317 316 316 THR THR A . n 
A 1 318 TYR 318 317 317 TYR TYR A . n 
A 1 319 LEU 319 318 318 LEU LEU A . n 
A 1 320 LEU 320 319 319 LEU LEU A . n 
A 1 321 LEU 321 320 320 LEU LEU A . n 
A 1 322 LEU 322 321 321 LEU LEU A . n 
A 1 323 ALA 323 322 322 ALA ALA A . n 
A 1 324 LYS 324 323 323 LYS LYS A . n 
A 1 325 LYS 325 324 324 LYS LYS A . n 
A 1 326 ALA 326 325 325 ALA ALA A . n 
A 1 327 ARG 327 326 326 ARG ARG A . n 
A 1 328 GLY 328 327 327 GLY GLY A . n 
A 1 329 LYS 329 328 328 LYS LYS A . n 
A 1 330 PRO 330 329 329 PRO PRO A . n 
A 1 331 VAL 331 330 330 VAL VAL A . n 
A 1 332 ARG 332 331 331 ARG ARG A . n 
A 1 333 LEU 333 332 332 LEU LEU A . n 
A 1 334 ARG 334 333 333 ARG ARG A . n 
A 1 335 LEU 335 334 334 LEU LEU A . n 
A 1 336 SER 336 335 335 SER SER A . n 
A 1 337 SER 337 336 ?   ?   ?   A . n 
A 1 338 PHE 338 337 ?   ?   ?   A . n 
A 1 339 SER 339 338 ?   ?   ?   A . n 
A 1 340 CYS 340 339 ?   ?   ?   A . n 
A 1 341 GLY 341 340 ?   ?   ?   A . n 
A 1 342 GLN 342 341 ?   ?   ?   A . n 
A 1 343 ALA 343 342 ?   ?   ?   A . n 
A 1 344 SER 344 343 ?   ?   ?   A . n 
A 1 345 ALA 345 344 ?   ?   ?   A . n 
A 1 346 THR 346 345 ?   ?   ?   A . n 
A 1 347 PRO 347 346 ?   ?   ?   A . n 
A 1 348 PHE 348 347 ?   ?   ?   A . n 
A 1 349 THR 349 348 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1H9M 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1H9M 
_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 A1H9M 1   401 401 A1H9M a17 A . 
C 3 HOH   1   501 62  HOH   HOH A . 
C 3 HOH   2   502 74  HOH   HOH A . 
C 3 HOH   3   503 49  HOH   HOH A . 
C 3 HOH   4   504 81  HOH   HOH A . 
C 3 HOH   5   505 84  HOH   HOH A . 
C 3 HOH   6   506 72  HOH   HOH A . 
C 3 HOH   7   507 46  HOH   HOH A . 
C 3 HOH   8   508 36  HOH   HOH A . 
C 3 HOH   9   509 21  HOH   HOH A . 
C 3 HOH   10  510 10  HOH   HOH A . 
C 3 HOH   11  511 52  HOH   HOH A . 
C 3 HOH   12  512 116 HOH   HOH A . 
C 3 HOH   13  513 120 HOH   HOH A . 
C 3 HOH   14  514 91  HOH   HOH A . 
C 3 HOH   15  515 55  HOH   HOH A . 
C 3 HOH   16  516 97  HOH   HOH A . 
C 3 HOH   17  517 48  HOH   HOH A . 
C 3 HOH   18  518 105 HOH   HOH A . 
C 3 HOH   19  519 76  HOH   HOH A . 
C 3 HOH   20  520 124 HOH   HOH A . 
C 3 HOH   21  521 32  HOH   HOH A . 
C 3 HOH   22  522 104 HOH   HOH A . 
C 3 HOH   23  523 27  HOH   HOH A . 
C 3 HOH   24  524 45  HOH   HOH A . 
C 3 HOH   25  525 107 HOH   HOH A . 
C 3 HOH   26  526 50  HOH   HOH A . 
C 3 HOH   27  527 18  HOH   HOH A . 
C 3 HOH   28  528 57  HOH   HOH A . 
C 3 HOH   29  529 56  HOH   HOH A . 
C 3 HOH   30  530 40  HOH   HOH A . 
C 3 HOH   31  531 134 HOH   HOH A . 
C 3 HOH   32  532 19  HOH   HOH A . 
C 3 HOH   33  533 8   HOH   HOH A . 
C 3 HOH   34  534 28  HOH   HOH A . 
C 3 HOH   35  535 70  HOH   HOH A . 
C 3 HOH   36  536 23  HOH   HOH A . 
C 3 HOH   37  537 15  HOH   HOH A . 
C 3 HOH   38  538 66  HOH   HOH A . 
C 3 HOH   39  539 3   HOH   HOH A . 
C 3 HOH   40  540 14  HOH   HOH A . 
C 3 HOH   41  541 89  HOH   HOH A . 
C 3 HOH   42  542 68  HOH   HOH A . 
C 3 HOH   43  543 54  HOH   HOH A . 
C 3 HOH   44  544 26  HOH   HOH A . 
C 3 HOH   45  545 13  HOH   HOH A . 
C 3 HOH   46  546 131 HOH   HOH A . 
C 3 HOH   47  547 6   HOH   HOH A . 
C 3 HOH   48  548 7   HOH   HOH A . 
C 3 HOH   49  549 139 HOH   HOH A . 
C 3 HOH   50  550 44  HOH   HOH A . 
C 3 HOH   51  551 31  HOH   HOH A . 
C 3 HOH   52  552 35  HOH   HOH A . 
C 3 HOH   53  553 24  HOH   HOH A . 
C 3 HOH   54  554 33  HOH   HOH A . 
C 3 HOH   55  555 133 HOH   HOH A . 
C 3 HOH   56  556 63  HOH   HOH A . 
C 3 HOH   57  557 17  HOH   HOH A . 
C 3 HOH   58  558 64  HOH   HOH A . 
C 3 HOH   59  559 25  HOH   HOH A . 
C 3 HOH   60  560 102 HOH   HOH A . 
C 3 HOH   61  561 90  HOH   HOH A . 
C 3 HOH   62  562 16  HOH   HOH A . 
C 3 HOH   63  563 12  HOH   HOH A . 
C 3 HOH   64  564 109 HOH   HOH A . 
C 3 HOH   65  565 47  HOH   HOH A . 
C 3 HOH   66  566 51  HOH   HOH A . 
C 3 HOH   67  567 30  HOH   HOH A . 
C 3 HOH   68  568 65  HOH   HOH A . 
C 3 HOH   69  569 39  HOH   HOH A . 
C 3 HOH   70  570 94  HOH   HOH A . 
C 3 HOH   71  571 9   HOH   HOH A . 
C 3 HOH   72  572 38  HOH   HOH A . 
C 3 HOH   73  573 98  HOH   HOH A . 
C 3 HOH   74  574 125 HOH   HOH A . 
C 3 HOH   75  575 41  HOH   HOH A . 
C 3 HOH   76  576 2   HOH   HOH A . 
C 3 HOH   77  577 100 HOH   HOH A . 
C 3 HOH   78  578 67  HOH   HOH A . 
C 3 HOH   79  579 29  HOH   HOH A . 
C 3 HOH   80  580 96  HOH   HOH A . 
C 3 HOH   81  581 58  HOH   HOH A . 
C 3 HOH   82  582 79  HOH   HOH A . 
C 3 HOH   83  583 99  HOH   HOH A . 
C 3 HOH   84  584 93  HOH   HOH A . 
C 3 HOH   85  585 101 HOH   HOH A . 
C 3 HOH   86  586 4   HOH   HOH A . 
C 3 HOH   87  587 61  HOH   HOH A . 
C 3 HOH   88  588 42  HOH   HOH A . 
C 3 HOH   89  589 5   HOH   HOH A . 
C 3 HOH   90  590 88  HOH   HOH A . 
C 3 HOH   91  591 95  HOH   HOH A . 
C 3 HOH   92  592 37  HOH   HOH A . 
C 3 HOH   93  593 136 HOH   HOH A . 
C 3 HOH   94  594 11  HOH   HOH A . 
C 3 HOH   95  595 126 HOH   HOH A . 
C 3 HOH   96  596 59  HOH   HOH A . 
C 3 HOH   97  597 83  HOH   HOH A . 
C 3 HOH   98  598 108 HOH   HOH A . 
C 3 HOH   99  599 80  HOH   HOH A . 
C 3 HOH   100 600 128 HOH   HOH A . 
C 3 HOH   101 601 22  HOH   HOH A . 
C 3 HOH   102 602 111 HOH   HOH A . 
C 3 HOH   103 603 135 HOH   HOH A . 
C 3 HOH   104 604 117 HOH   HOH A . 
C 3 HOH   105 605 1   HOH   HOH A . 
C 3 HOH   106 606 115 HOH   HOH A . 
C 3 HOH   107 607 71  HOH   HOH A . 
C 3 HOH   108 608 106 HOH   HOH A . 
C 3 HOH   109 609 77  HOH   HOH A . 
C 3 HOH   110 610 69  HOH   HOH A . 
C 3 HOH   111 611 73  HOH   HOH A . 
C 3 HOH   112 612 60  HOH   HOH A . 
C 3 HOH   113 613 127 HOH   HOH A . 
C 3 HOH   114 614 113 HOH   HOH A . 
C 3 HOH   115 615 43  HOH   HOH A . 
C 3 HOH   116 616 110 HOH   HOH A . 
C 3 HOH   117 617 87  HOH   HOH A . 
C 3 HOH   118 618 122 HOH   HOH A . 
C 3 HOH   119 619 34  HOH   HOH A . 
C 3 HOH   120 620 119 HOH   HOH A . 
C 3 HOH   121 621 118 HOH   HOH A . 
C 3 HOH   122 622 78  HOH   HOH A . 
C 3 HOH   123 623 130 HOH   HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A MET 1   ? CG  ? A MET 2   CG  
2  1 Y 1 A MET 1   ? SD  ? A MET 2   SD  
3  1 Y 1 A MET 1   ? CE  ? A MET 2   CE  
4  1 Y 1 A LYS 2   ? CG  ? A LYS 3   CG  
5  1 Y 1 A LYS 2   ? CD  ? A LYS 3   CD  
6  1 Y 1 A LYS 2   ? CE  ? A LYS 3   CE  
7  1 Y 1 A LYS 2   ? NZ  ? A LYS 3   NZ  
8  1 Y 1 A PHE 22  ? CG  ? A PHE 23  CG  
9  1 Y 1 A PHE 22  ? CD1 ? A PHE 23  CD1 
10 1 Y 1 A PHE 22  ? CD2 ? A PHE 23  CD2 
11 1 Y 1 A PHE 22  ? CE1 ? A PHE 23  CE1 
12 1 Y 1 A PHE 22  ? CE2 ? A PHE 23  CE2 
13 1 Y 1 A PHE 22  ? CZ  ? A PHE 23  CZ  
14 1 Y 1 A PHE 279 ? CG  ? A PHE 280 CG  
15 1 Y 1 A PHE 279 ? CD1 ? A PHE 280 CD1 
16 1 Y 1 A PHE 279 ? CD2 ? A PHE 280 CD2 
17 1 Y 1 A PHE 279 ? CE1 ? A PHE 280 CE1 
18 1 Y 1 A PHE 279 ? CE2 ? A PHE 280 CE2 
19 1 Y 1 A PHE 279 ? CZ  ? A PHE 280 CZ  
20 1 Y 1 A HIS 281 ? CG  ? A HIS 282 CG  
21 1 Y 1 A HIS 281 ? ND1 ? A HIS 282 ND1 
22 1 Y 1 A HIS 281 ? CD2 ? A HIS 282 CD2 
23 1 Y 1 A HIS 281 ? CE1 ? A HIS 282 CE1 
24 1 Y 1 A HIS 281 ? NE2 ? A HIS 282 NE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0425 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9F31 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     168.734 
_cell.length_a_esd                 ? 
_cell.length_b                     168.734 
_cell.length_b_esd                 ? 
_cell.length_c                     168.734 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        48 
_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                         9F31 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                214 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'I 41 3 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9F31 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.49 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          50.52 
_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              ? 
_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    '14% PEG 3350--10% ethylene glycol--0.2M potassium thiocyanate--0.1M bis-tris propane pH 7.1' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-12-16 
_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   0.999998 
_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                        'SLS BEAMLINE X06SA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.999998 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X06SA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9F31 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2 
_reflns.d_resolution_low                               48.76 
_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                                     27915 
_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                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                81.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          29.7 
_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                                   1 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.0 
_reflns_shell.d_res_low                                     2.05 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.2 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2017 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.802 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.00 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            0.00 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               52.349 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.967 
_refine.correlation_coeff_Fo_to_Fc_free          0.944 
_refine.details                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT' 
_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                                 9F31 
_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                            2.00 
_refine.ls_d_res_low                             48.76 
_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                     26503 
_refine.ls_number_reflns_R_free                  1386 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.97 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.19067 
_refine.ls_R_factor_R_free                       0.23278 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.18853 
_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                          ? 
_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                       0.123 
_refine.pdbx_overall_ESU_R_Free                  0.152 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_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                             0.001 
_refine.overall_SU_ML                            0.000 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.00 
_refine_hist.d_res_low                        48.76 
_refine_hist.number_atoms_solvent             123 
_refine_hist.number_atoms_total               2731 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2588 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         20 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.000 
_refine_ls_shell.d_res_low                        2.052 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             104 
_refine_ls_shell.number_reflns_R_work             1908 
_refine_ls_shell.percent_reflns_obs               99.85 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.272 
_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                  0.332 
# 
_struct.entry_id                     9F31 
_struct.title                        'Crystal structure of MELK with a covalent compound GCL 99' 
_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        9F31 
_struct_keywords.text            
'Kinase, Covalent, inhibitor, MAP2K6, Structural Genomics, Structural Genomics Consortium, SGC, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
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                    MELK_HUMAN 
_struct_ref.pdbx_db_accession          Q14680 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MKDYDELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETAN
KIFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGN
KDYHLQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLL
QQMLQVDPKKRISMKNLLNHPWIMQDYNYPVEWQSKNPFIHLDDDCVTELSVHHRNNRQTMEDLISLWQYDHLTATYLLL
LAKKARGKPVRLRLSSFSCGQASATPFT
;
_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              9F31 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 2 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 349 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q14680 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  348 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       348 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             9F31 
_struct_ref_seq_dif.mon_id                       SER 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      1 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   Q14680 
_struct_ref_seq_dif.db_mon_id                    ? 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          ? 
_struct_ref_seq_dif.details                      'expression tag' 
_struct_ref_seq_dif.pdbx_auth_seq_num            0 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_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)'  14950 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 TYR A 5   ? LYS A 10  ? TYR A 4   LYS A 9   1 ? 6  
HELX_P HELX_P2  AA2 LYS A 45  ? GLY A 49  ? LYS A 44  GLY A 48  1 ? 5  
HELX_P HELX_P3  AA3 ASP A 51  ? ASN A 64  ? ASP A 50  ASN A 63  1 ? 14 
HELX_P HELX_P4  AA4 GLU A 94  ? ASP A 103 ? GLU A 93  ASP A 102 1 ? 10 
HELX_P HELX_P5  AA5 SER A 106 ? GLN A 127 ? SER A 105 GLN A 126 1 ? 22 
HELX_P HELX_P6  AA6 LYS A 135 ? GLU A 137 ? LYS A 134 GLU A 136 5 ? 3  
HELX_P HELX_P7  AA7 SER A 172 ? ALA A 176 ? SER A 171 ALA A 175 5 ? 5  
HELX_P HELX_P8  AA8 ALA A 177 ? GLN A 182 ? ALA A 176 GLN A 181 1 ? 6  
HELX_P HELX_P9  AA9 LEU A 187 ? GLY A 206 ? LEU A 186 GLY A 205 1 ? 20 
HELX_P HELX_P10 AB1 ASN A 214 ? GLY A 225 ? ASN A 213 GLY A 224 1 ? 12 
HELX_P HELX_P11 AB2 SER A 234 ? LEU A 245 ? SER A 233 LEU A 244 1 ? 12 
HELX_P HELX_P12 AB3 ASP A 248 ? ARG A 252 ? ASP A 247 ARG A 251 5 ? 5  
HELX_P HELX_P13 AB4 SER A 254 ? ASN A 260 ? SER A 253 ASN A 259 1 ? 7  
HELX_P HELX_P14 AB5 HIS A 261 ? GLN A 266 ? HIS A 260 GLN A 265 1 ? 6  
HELX_P HELX_P15 AB6 ASP A 284 ? ARG A 296 ? ASP A 283 ARG A 295 1 ? 13 
HELX_P HELX_P16 AB7 ASN A 298 ? SER A 307 ? ASN A 297 SER A 306 1 ? 10 
HELX_P HELX_P17 AB8 ASP A 312 ? ARG A 327 ? ASP A 311 ARG A 326 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           CYS 
_struct_conn.ptnr1_label_seq_id            155 
_struct_conn.ptnr1_label_atom_id           SG 
_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           A1H9M 
_struct_conn.ptnr2_label_seq_id            . 
_struct_conn.ptnr2_label_atom_id           C1 
_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            CYS 
_struct_conn.ptnr1_auth_seq_id             154 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            A1H9M 
_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               1.747 
_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                      A1H9M 
_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     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      155 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       A1H9M 
_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      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       154 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               C1 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                CYS 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        A1H9M 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Covalent chemical modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 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 
AA2 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 TYR A 12  ? GLY A 19  ? TYR A 11  GLY A 18  
AA1 2 ALA A 24  ? HIS A 31  ? ALA A 23  HIS A 30  
AA1 3 GLU A 36  ? ASP A 44  ? GLU A 35  ASP A 43  
AA1 4 LYS A 82  ? GLU A 88  ? LYS A 81  GLU A 87  
AA1 5 LEU A 73  ? GLU A 78  ? LEU A 72  GLU A 77  
AA2 1 LEU A 139 ? PHE A 141 ? LEU A 138 PHE A 140 
AA2 2 LEU A 147 ? LEU A 149 ? LEU A 146 LEU A 148 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N HIS A 15  ? N HIS A 14  O LEU A 28  ? O LEU A 27  
AA1 2 3 N LYS A 27  ? N LYS A 26  O ILE A 40  ? O ILE A 39  
AA1 3 4 N ALA A 39  ? N ALA A 38  O LEU A 87  ? O LEU A 86  
AA1 4 5 O VAL A 86  ? O VAL A 85  N TYR A 74  ? N TYR A 73  
AA2 1 2 N LEU A 140 ? N LEU A 139 O LYS A 148 ? O LYS A 147 
# 
_pdbx_entry_details.entry_id                   9F31 
_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 LYS A 2   ? ? 72.77   -11.28  
2  1 HIS A 14  ? ? -110.93 -137.54 
3  1 PHE A 22  ? ? 80.06   -28.12  
4  1 LEU A 64  ? ? -108.68 65.12   
5  1 ASP A 102 ? ? 69.66   -63.76  
6  1 ARG A 131 ? ? 79.03   -5.96   
7  1 ASP A 132 ? ? -142.99 50.50   
8  1 ASP A 150 ? ? 71.52   65.71   
9  1 LEU A 153 ? ? 66.58   -40.42  
10 1 ASP A 266 ? ? 81.77   4.66    
11 1 LYS A 276 ? ? -77.94  42.76   
12 1 ILE A 280 ? ? -134.91 -38.56  
13 1 HIS A 281 ? ? -9.05   98.82   
14 1 LEU A 334 ? ? -145.60 48.34   
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 251 ? ? 0.118 'SIDE CHAIN' 
2 1 ARG A 326 ? ? 0.090 'SIDE CHAIN' 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     573 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   C 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       623 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   7.81 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A SER 0   ? A SER 1   
2  1 Y 1 A LYS 156 ? A LYS 157 
3  1 Y 1 A PRO 157 ? A PRO 158 
4  1 Y 1 A LYS 158 ? A LYS 159 
5  1 Y 1 A GLY 159 ? A GLY 160 
6  1 Y 1 A ASN 160 ? A ASN 161 
7  1 Y 1 A LYS 161 ? A LYS 162 
8  1 Y 1 A ASP 162 ? A ASP 163 
9  1 Y 1 A TYR 163 ? A TYR 164 
10 1 Y 1 A HIS 164 ? A HIS 165 
11 1 Y 1 A LEU 165 ? A LEU 166 
12 1 Y 1 A GLN 166 ? A GLN 167 
13 1 Y 1 A THR 167 ? A THR 168 
14 1 Y 1 A CYS 168 ? A CYS 169 
15 1 Y 1 A CYS 169 ? A CYS 170 
16 1 Y 1 A GLY 170 ? A GLY 171 
17 1 Y 1 A SER 336 ? A SER 337 
18 1 Y 1 A PHE 337 ? A PHE 338 
19 1 Y 1 A SER 338 ? A SER 339 
20 1 Y 1 A CYS 339 ? A CYS 340 
21 1 Y 1 A GLY 340 ? A GLY 341 
22 1 Y 1 A GLN 341 ? A GLN 342 
23 1 Y 1 A ALA 342 ? A ALA 343 
24 1 Y 1 A SER 343 ? A SER 344 
25 1 Y 1 A ALA 344 ? A ALA 345 
26 1 Y 1 A THR 345 ? A THR 346 
27 1 Y 1 A PRO 346 ? A PRO 347 
28 1 Y 1 A PHE 347 ? A PHE 348 
29 1 Y 1 A THR 348 ? A THR 349 
# 
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 
A1H9M C1   C N N 1   
A1H9M C2   C N N 2   
A1H9M C3   C N N 3   
A1H9M O1   O N N 4   
A1H9M N1   N N N 5   
A1H9M C4   C Y N 6   
A1H9M C5   C Y N 7   
A1H9M C6   C Y N 8   
A1H9M C7   C Y N 9   
A1H9M C8   C Y N 10  
A1H9M C9   C Y N 11  
A1H9M C10  C Y N 12  
A1H9M C11  C Y N 13  
A1H9M N2   N Y N 14  
A1H9M N3   N Y N 15  
A1H9M C12  C Y N 16  
A1H9M C13  C Y N 17  
A1H9M C14  C Y N 18  
A1H9M C15  C Y N 19  
A1H9M C16  C Y N 20  
A1H9M H1   H N N 21  
A1H9M H2   H N N 22  
A1H9M H4   H N N 23  
A1H9M H6   H N N 24  
A1H9M H7   H N N 25  
A1H9M H8   H N N 26  
A1H9M H9   H N N 27  
A1H9M H10  H N N 28  
A1H9M H11  H N N 29  
A1H9M H12  H N N 30  
A1H9M H13  H N N 31  
A1H9M H14  H N N 32  
A1H9M H15  H N N 33  
A1H9M H3   H N N 34  
A1H9M H5   H N N 35  
ALA   N    N N N 36  
ALA   CA   C N S 37  
ALA   C    C N N 38  
ALA   O    O N N 39  
ALA   CB   C N N 40  
ALA   OXT  O N N 41  
ALA   H    H N N 42  
ALA   H2   H N N 43  
ALA   HA   H N N 44  
ALA   HB1  H N N 45  
ALA   HB2  H N N 46  
ALA   HB3  H N N 47  
ALA   HXT  H N N 48  
ARG   N    N N N 49  
ARG   CA   C N S 50  
ARG   C    C N N 51  
ARG   O    O N N 52  
ARG   CB   C N N 53  
ARG   CG   C N N 54  
ARG   CD   C N N 55  
ARG   NE   N N N 56  
ARG   CZ   C N N 57  
ARG   NH1  N N N 58  
ARG   NH2  N N N 59  
ARG   OXT  O N N 60  
ARG   H    H N N 61  
ARG   H2   H N N 62  
ARG   HA   H N N 63  
ARG   HB2  H N N 64  
ARG   HB3  H N N 65  
ARG   HG2  H N N 66  
ARG   HG3  H N N 67  
ARG   HD2  H N N 68  
ARG   HD3  H N N 69  
ARG   HE   H N N 70  
ARG   HH11 H N N 71  
ARG   HH12 H N N 72  
ARG   HH21 H N N 73  
ARG   HH22 H N N 74  
ARG   HXT  H N N 75  
ASN   N    N N N 76  
ASN   CA   C N S 77  
ASN   C    C N N 78  
ASN   O    O N N 79  
ASN   CB   C N N 80  
ASN   CG   C N N 81  
ASN   OD1  O N N 82  
ASN   ND2  N N N 83  
ASN   OXT  O N N 84  
ASN   H    H N N 85  
ASN   H2   H N N 86  
ASN   HA   H N N 87  
ASN   HB2  H N N 88  
ASN   HB3  H N N 89  
ASN   HD21 H N N 90  
ASN   HD22 H N N 91  
ASN   HXT  H N N 92  
ASP   N    N N N 93  
ASP   CA   C N S 94  
ASP   C    C N N 95  
ASP   O    O N N 96  
ASP   CB   C N N 97  
ASP   CG   C N N 98  
ASP   OD1  O N N 99  
ASP   OD2  O N N 100 
ASP   OXT  O N N 101 
ASP   H    H N N 102 
ASP   H2   H N N 103 
ASP   HA   H N N 104 
ASP   HB2  H N N 105 
ASP   HB3  H N N 106 
ASP   HD2  H N N 107 
ASP   HXT  H N N 108 
CYS   N    N N N 109 
CYS   CA   C N R 110 
CYS   C    C N N 111 
CYS   O    O N N 112 
CYS   CB   C N N 113 
CYS   SG   S N N 114 
CYS   OXT  O N N 115 
CYS   H    H N N 116 
CYS   H2   H N N 117 
CYS   HA   H N N 118 
CYS   HB2  H N N 119 
CYS   HB3  H N N 120 
CYS   HG   H N N 121 
CYS   HXT  H N N 122 
GLN   N    N N N 123 
GLN   CA   C N S 124 
GLN   C    C N N 125 
GLN   O    O N N 126 
GLN   CB   C N N 127 
GLN   CG   C N N 128 
GLN   CD   C N N 129 
GLN   OE1  O N N 130 
GLN   NE2  N N N 131 
GLN   OXT  O N N 132 
GLN   H    H N N 133 
GLN   H2   H N N 134 
GLN   HA   H N N 135 
GLN   HB2  H N N 136 
GLN   HB3  H N N 137 
GLN   HG2  H N N 138 
GLN   HG3  H N N 139 
GLN   HE21 H N N 140 
GLN   HE22 H N N 141 
GLN   HXT  H N N 142 
GLU   N    N N N 143 
GLU   CA   C N S 144 
GLU   C    C N N 145 
GLU   O    O N N 146 
GLU   CB   C N N 147 
GLU   CG   C N N 148 
GLU   CD   C N N 149 
GLU   OE1  O N N 150 
GLU   OE2  O N N 151 
GLU   OXT  O N N 152 
GLU   H    H N N 153 
GLU   H2   H N N 154 
GLU   HA   H N N 155 
GLU   HB2  H N N 156 
GLU   HB3  H N N 157 
GLU   HG2  H N N 158 
GLU   HG3  H N N 159 
GLU   HE2  H N N 160 
GLU   HXT  H N N 161 
GLY   N    N N N 162 
GLY   CA   C N N 163 
GLY   C    C N N 164 
GLY   O    O N N 165 
GLY   OXT  O N N 166 
GLY   H    H N N 167 
GLY   H2   H N N 168 
GLY   HA2  H N N 169 
GLY   HA3  H N N 170 
GLY   HXT  H N N 171 
HIS   N    N N N 172 
HIS   CA   C N S 173 
HIS   C    C N N 174 
HIS   O    O N N 175 
HIS   CB   C N N 176 
HIS   CG   C Y N 177 
HIS   ND1  N Y N 178 
HIS   CD2  C Y N 179 
HIS   CE1  C Y N 180 
HIS   NE2  N Y N 181 
HIS   OXT  O N N 182 
HIS   H    H N N 183 
HIS   H2   H N N 184 
HIS   HA   H N N 185 
HIS   HB2  H N N 186 
HIS   HB3  H N N 187 
HIS   HD1  H N N 188 
HIS   HD2  H N N 189 
HIS   HE1  H N N 190 
HIS   HE2  H N N 191 
HIS   HXT  H N N 192 
HOH   O    O N N 193 
HOH   H1   H N N 194 
HOH   H2   H N N 195 
ILE   N    N N N 196 
ILE   CA   C N S 197 
ILE   C    C N N 198 
ILE   O    O N N 199 
ILE   CB   C N S 200 
ILE   CG1  C N N 201 
ILE   CG2  C N N 202 
ILE   CD1  C N N 203 
ILE   OXT  O N N 204 
ILE   H    H N N 205 
ILE   H2   H N N 206 
ILE   HA   H N N 207 
ILE   HB   H N N 208 
ILE   HG12 H N N 209 
ILE   HG13 H N N 210 
ILE   HG21 H N N 211 
ILE   HG22 H N N 212 
ILE   HG23 H N N 213 
ILE   HD11 H N N 214 
ILE   HD12 H N N 215 
ILE   HD13 H N N 216 
ILE   HXT  H N N 217 
LEU   N    N N N 218 
LEU   CA   C N S 219 
LEU   C    C N N 220 
LEU   O    O N N 221 
LEU   CB   C N N 222 
LEU   CG   C N N 223 
LEU   CD1  C N N 224 
LEU   CD2  C N N 225 
LEU   OXT  O N N 226 
LEU   H    H N N 227 
LEU   H2   H N N 228 
LEU   HA   H N N 229 
LEU   HB2  H N N 230 
LEU   HB3  H N N 231 
LEU   HG   H N N 232 
LEU   HD11 H N N 233 
LEU   HD12 H N N 234 
LEU   HD13 H N N 235 
LEU   HD21 H N N 236 
LEU   HD22 H N N 237 
LEU   HD23 H N N 238 
LEU   HXT  H N N 239 
LYS   N    N N N 240 
LYS   CA   C N S 241 
LYS   C    C N N 242 
LYS   O    O N N 243 
LYS   CB   C N N 244 
LYS   CG   C N N 245 
LYS   CD   C N N 246 
LYS   CE   C N N 247 
LYS   NZ   N N N 248 
LYS   OXT  O N N 249 
LYS   H    H N N 250 
LYS   H2   H N N 251 
LYS   HA   H N N 252 
LYS   HB2  H N N 253 
LYS   HB3  H N N 254 
LYS   HG2  H N N 255 
LYS   HG3  H N N 256 
LYS   HD2  H N N 257 
LYS   HD3  H N N 258 
LYS   HE2  H N N 259 
LYS   HE3  H N N 260 
LYS   HZ1  H N N 261 
LYS   HZ2  H N N 262 
LYS   HZ3  H N N 263 
LYS   HXT  H N N 264 
MET   N    N N N 265 
MET   CA   C N S 266 
MET   C    C N N 267 
MET   O    O N N 268 
MET   CB   C N N 269 
MET   CG   C N N 270 
MET   SD   S N N 271 
MET   CE   C N N 272 
MET   OXT  O N N 273 
MET   H    H N N 274 
MET   H2   H N N 275 
MET   HA   H N N 276 
MET   HB2  H N N 277 
MET   HB3  H N N 278 
MET   HG2  H N N 279 
MET   HG3  H N N 280 
MET   HE1  H N N 281 
MET   HE2  H N N 282 
MET   HE3  H N N 283 
MET   HXT  H N N 284 
PHE   N    N N N 285 
PHE   CA   C N S 286 
PHE   C    C N N 287 
PHE   O    O N N 288 
PHE   CB   C N N 289 
PHE   CG   C Y N 290 
PHE   CD1  C Y N 291 
PHE   CD2  C Y N 292 
PHE   CE1  C Y N 293 
PHE   CE2  C Y N 294 
PHE   CZ   C Y N 295 
PHE   OXT  O N N 296 
PHE   H    H N N 297 
PHE   H2   H N N 298 
PHE   HA   H N N 299 
PHE   HB2  H N N 300 
PHE   HB3  H N N 301 
PHE   HD1  H N N 302 
PHE   HD2  H N N 303 
PHE   HE1  H N N 304 
PHE   HE2  H N N 305 
PHE   HZ   H N N 306 
PHE   HXT  H N N 307 
PRO   N    N N N 308 
PRO   CA   C N S 309 
PRO   C    C N N 310 
PRO   O    O N N 311 
PRO   CB   C N N 312 
PRO   CG   C N N 313 
PRO   CD   C N N 314 
PRO   OXT  O N N 315 
PRO   H    H N N 316 
PRO   HA   H N N 317 
PRO   HB2  H N N 318 
PRO   HB3  H N N 319 
PRO   HG2  H N N 320 
PRO   HG3  H N N 321 
PRO   HD2  H N N 322 
PRO   HD3  H N N 323 
PRO   HXT  H N N 324 
SER   N    N N N 325 
SER   CA   C N S 326 
SER   C    C N N 327 
SER   O    O N N 328 
SER   CB   C N N 329 
SER   OG   O N N 330 
SER   OXT  O N N 331 
SER   H    H N N 332 
SER   H2   H N N 333 
SER   HA   H N N 334 
SER   HB2  H N N 335 
SER   HB3  H N N 336 
SER   HG   H N N 337 
SER   HXT  H N N 338 
THR   N    N N N 339 
THR   CA   C N S 340 
THR   C    C N N 341 
THR   O    O N N 342 
THR   CB   C N R 343 
THR   OG1  O N N 344 
THR   CG2  C N N 345 
THR   OXT  O N N 346 
THR   H    H N N 347 
THR   H2   H N N 348 
THR   HA   H N N 349 
THR   HB   H N N 350 
THR   HG1  H N N 351 
THR   HG21 H N N 352 
THR   HG22 H N N 353 
THR   HG23 H N N 354 
THR   HXT  H N N 355 
TRP   N    N N N 356 
TRP   CA   C N S 357 
TRP   C    C N N 358 
TRP   O    O N N 359 
TRP   CB   C N N 360 
TRP   CG   C Y N 361 
TRP   CD1  C Y N 362 
TRP   CD2  C Y N 363 
TRP   NE1  N Y N 364 
TRP   CE2  C Y N 365 
TRP   CE3  C Y N 366 
TRP   CZ2  C Y N 367 
TRP   CZ3  C Y N 368 
TRP   CH2  C Y N 369 
TRP   OXT  O N N 370 
TRP   H    H N N 371 
TRP   H2   H N N 372 
TRP   HA   H N N 373 
TRP   HB2  H N N 374 
TRP   HB3  H N N 375 
TRP   HD1  H N N 376 
TRP   HE1  H N N 377 
TRP   HE3  H N N 378 
TRP   HZ2  H N N 379 
TRP   HZ3  H N N 380 
TRP   HH2  H N N 381 
TRP   HXT  H N N 382 
TYR   N    N N N 383 
TYR   CA   C N S 384 
TYR   C    C N N 385 
TYR   O    O N N 386 
TYR   CB   C N N 387 
TYR   CG   C Y N 388 
TYR   CD1  C Y N 389 
TYR   CD2  C Y N 390 
TYR   CE1  C Y N 391 
TYR   CE2  C Y N 392 
TYR   CZ   C Y N 393 
TYR   OH   O N N 394 
TYR   OXT  O N N 395 
TYR   H    H N N 396 
TYR   H2   H N N 397 
TYR   HA   H N N 398 
TYR   HB2  H N N 399 
TYR   HB3  H N N 400 
TYR   HD1  H N N 401 
TYR   HD2  H N N 402 
TYR   HE1  H N N 403 
TYR   HE2  H N N 404 
TYR   HH   H N N 405 
TYR   HXT  H N N 406 
VAL   N    N N N 407 
VAL   CA   C N S 408 
VAL   C    C N N 409 
VAL   O    O N N 410 
VAL   CB   C N N 411 
VAL   CG1  C N N 412 
VAL   CG2  C N N 413 
VAL   OXT  O N N 414 
VAL   H    H N N 415 
VAL   H2   H N N 416 
VAL   HA   H N N 417 
VAL   HB   H N N 418 
VAL   HG11 H N N 419 
VAL   HG12 H N N 420 
VAL   HG13 H N N 421 
VAL   HG21 H N N 422 
VAL   HG22 H N N 423 
VAL   HG23 H N N 424 
VAL   HXT  H N N 425 
# 
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 
A1H9M C1  C2   sing N N 1   
A1H9M C2  C3   sing N N 2   
A1H9M C3  O1   doub N N 3   
A1H9M C3  N1   sing N N 4   
A1H9M N1  C4   sing N N 5   
A1H9M C4  C16  doub Y N 6   
A1H9M C4  C5   sing Y N 7   
A1H9M C16 C15  sing Y N 8   
A1H9M C5  C6   doub Y N 9   
A1H9M C15 C7   doub Y N 10  
A1H9M C6  C7   sing Y N 11  
A1H9M C7  C8   sing N N 12  
A1H9M C8  C9   sing Y N 13  
A1H9M C8  C14  doub Y N 14  
A1H9M C9  C10  doub Y N 15  
A1H9M C14 C13  sing Y N 16  
A1H9M C10 C11  sing Y N 17  
A1H9M C13 C11  doub Y N 18  
A1H9M C13 C12  sing Y N 19  
A1H9M C11 N2   sing Y N 20  
A1H9M C12 N3   doub Y N 21  
A1H9M N2  N3   sing Y N 22  
A1H9M C1  H1   sing N N 23  
A1H9M C1  H2   sing N N 24  
A1H9M C2  H4   sing N N 25  
A1H9M N1  H6   sing N N 26  
A1H9M C5  H7   sing N N 27  
A1H9M C6  H8   sing N N 28  
A1H9M C9  H9   sing N N 29  
A1H9M C10 H10  sing N N 30  
A1H9M N2  H11  sing N N 31  
A1H9M C12 H12  sing N N 32  
A1H9M C14 H13  sing N N 33  
A1H9M C15 H14  sing N N 34  
A1H9M C16 H15  sing N N 35  
A1H9M C1  H3   sing N N 36  
A1H9M C2  H5   sing N N 37  
ALA   N   CA   sing N N 38  
ALA   N   H    sing N N 39  
ALA   N   H2   sing N N 40  
ALA   CA  C    sing N N 41  
ALA   CA  CB   sing N N 42  
ALA   CA  HA   sing N N 43  
ALA   C   O    doub N N 44  
ALA   C   OXT  sing N N 45  
ALA   CB  HB1  sing N N 46  
ALA   CB  HB2  sing N N 47  
ALA   CB  HB3  sing N N 48  
ALA   OXT HXT  sing N N 49  
ARG   N   CA   sing N N 50  
ARG   N   H    sing N N 51  
ARG   N   H2   sing N N 52  
ARG   CA  C    sing N N 53  
ARG   CA  CB   sing N N 54  
ARG   CA  HA   sing N N 55  
ARG   C   O    doub N N 56  
ARG   C   OXT  sing N N 57  
ARG   CB  CG   sing N N 58  
ARG   CB  HB2  sing N N 59  
ARG   CB  HB3  sing N N 60  
ARG   CG  CD   sing N N 61  
ARG   CG  HG2  sing N N 62  
ARG   CG  HG3  sing N N 63  
ARG   CD  NE   sing N N 64  
ARG   CD  HD2  sing N N 65  
ARG   CD  HD3  sing N N 66  
ARG   NE  CZ   sing N N 67  
ARG   NE  HE   sing N N 68  
ARG   CZ  NH1  sing N N 69  
ARG   CZ  NH2  doub N N 70  
ARG   NH1 HH11 sing N N 71  
ARG   NH1 HH12 sing N N 72  
ARG   NH2 HH21 sing N N 73  
ARG   NH2 HH22 sing N N 74  
ARG   OXT HXT  sing N N 75  
ASN   N   CA   sing N N 76  
ASN   N   H    sing N N 77  
ASN   N   H2   sing N N 78  
ASN   CA  C    sing N N 79  
ASN   CA  CB   sing N N 80  
ASN   CA  HA   sing N N 81  
ASN   C   O    doub N N 82  
ASN   C   OXT  sing N N 83  
ASN   CB  CG   sing N N 84  
ASN   CB  HB2  sing N N 85  
ASN   CB  HB3  sing N N 86  
ASN   CG  OD1  doub N N 87  
ASN   CG  ND2  sing N N 88  
ASN   ND2 HD21 sing N N 89  
ASN   ND2 HD22 sing N N 90  
ASN   OXT HXT  sing N N 91  
ASP   N   CA   sing N N 92  
ASP   N   H    sing N N 93  
ASP   N   H2   sing N N 94  
ASP   CA  C    sing N N 95  
ASP   CA  CB   sing N N 96  
ASP   CA  HA   sing N N 97  
ASP   C   O    doub N N 98  
ASP   C   OXT  sing N N 99  
ASP   CB  CG   sing N N 100 
ASP   CB  HB2  sing N N 101 
ASP   CB  HB3  sing N N 102 
ASP   CG  OD1  doub N N 103 
ASP   CG  OD2  sing N N 104 
ASP   OD2 HD2  sing N N 105 
ASP   OXT HXT  sing N N 106 
CYS   N   CA   sing N N 107 
CYS   N   H    sing N N 108 
CYS   N   H2   sing N N 109 
CYS   CA  C    sing N N 110 
CYS   CA  CB   sing N N 111 
CYS   CA  HA   sing N N 112 
CYS   C   O    doub N N 113 
CYS   C   OXT  sing N N 114 
CYS   CB  SG   sing N N 115 
CYS   CB  HB2  sing N N 116 
CYS   CB  HB3  sing N N 117 
CYS   SG  HG   sing N N 118 
CYS   OXT HXT  sing N N 119 
GLN   N   CA   sing N N 120 
GLN   N   H    sing N N 121 
GLN   N   H2   sing N N 122 
GLN   CA  C    sing N N 123 
GLN   CA  CB   sing N N 124 
GLN   CA  HA   sing N N 125 
GLN   C   O    doub N N 126 
GLN   C   OXT  sing N N 127 
GLN   CB  CG   sing N N 128 
GLN   CB  HB2  sing N N 129 
GLN   CB  HB3  sing N N 130 
GLN   CG  CD   sing N N 131 
GLN   CG  HG2  sing N N 132 
GLN   CG  HG3  sing N N 133 
GLN   CD  OE1  doub N N 134 
GLN   CD  NE2  sing N N 135 
GLN   NE2 HE21 sing N N 136 
GLN   NE2 HE22 sing N N 137 
GLN   OXT HXT  sing N N 138 
GLU   N   CA   sing N N 139 
GLU   N   H    sing N N 140 
GLU   N   H2   sing N N 141 
GLU   CA  C    sing N N 142 
GLU   CA  CB   sing N N 143 
GLU   CA  HA   sing N N 144 
GLU   C   O    doub N N 145 
GLU   C   OXT  sing N N 146 
GLU   CB  CG   sing N N 147 
GLU   CB  HB2  sing N N 148 
GLU   CB  HB3  sing N N 149 
GLU   CG  CD   sing N N 150 
GLU   CG  HG2  sing N N 151 
GLU   CG  HG3  sing N N 152 
GLU   CD  OE1  doub N N 153 
GLU   CD  OE2  sing N N 154 
GLU   OE2 HE2  sing N N 155 
GLU   OXT HXT  sing N N 156 
GLY   N   CA   sing N N 157 
GLY   N   H    sing N N 158 
GLY   N   H2   sing N N 159 
GLY   CA  C    sing N N 160 
GLY   CA  HA2  sing N N 161 
GLY   CA  HA3  sing N N 162 
GLY   C   O    doub N N 163 
GLY   C   OXT  sing N N 164 
GLY   OXT HXT  sing N N 165 
HIS   N   CA   sing N N 166 
HIS   N   H    sing N N 167 
HIS   N   H2   sing N N 168 
HIS   CA  C    sing N N 169 
HIS   CA  CB   sing N N 170 
HIS   CA  HA   sing N N 171 
HIS   C   O    doub N N 172 
HIS   C   OXT  sing N N 173 
HIS   CB  CG   sing N N 174 
HIS   CB  HB2  sing N N 175 
HIS   CB  HB3  sing N N 176 
HIS   CG  ND1  sing Y N 177 
HIS   CG  CD2  doub Y N 178 
HIS   ND1 CE1  doub Y N 179 
HIS   ND1 HD1  sing N N 180 
HIS   CD2 NE2  sing Y N 181 
HIS   CD2 HD2  sing N N 182 
HIS   CE1 NE2  sing Y N 183 
HIS   CE1 HE1  sing N N 184 
HIS   NE2 HE2  sing N N 185 
HIS   OXT HXT  sing N N 186 
HOH   O   H1   sing N N 187 
HOH   O   H2   sing N N 188 
ILE   N   CA   sing N N 189 
ILE   N   H    sing N N 190 
ILE   N   H2   sing N N 191 
ILE   CA  C    sing N N 192 
ILE   CA  CB   sing N N 193 
ILE   CA  HA   sing N N 194 
ILE   C   O    doub N N 195 
ILE   C   OXT  sing N N 196 
ILE   CB  CG1  sing N N 197 
ILE   CB  CG2  sing N N 198 
ILE   CB  HB   sing N N 199 
ILE   CG1 CD1  sing N N 200 
ILE   CG1 HG12 sing N N 201 
ILE   CG1 HG13 sing N N 202 
ILE   CG2 HG21 sing N N 203 
ILE   CG2 HG22 sing N N 204 
ILE   CG2 HG23 sing N N 205 
ILE   CD1 HD11 sing N N 206 
ILE   CD1 HD12 sing N N 207 
ILE   CD1 HD13 sing N N 208 
ILE   OXT HXT  sing N N 209 
LEU   N   CA   sing N N 210 
LEU   N   H    sing N N 211 
LEU   N   H2   sing N N 212 
LEU   CA  C    sing N N 213 
LEU   CA  CB   sing N N 214 
LEU   CA  HA   sing N N 215 
LEU   C   O    doub N N 216 
LEU   C   OXT  sing N N 217 
LEU   CB  CG   sing N N 218 
LEU   CB  HB2  sing N N 219 
LEU   CB  HB3  sing N N 220 
LEU   CG  CD1  sing N N 221 
LEU   CG  CD2  sing N N 222 
LEU   CG  HG   sing N N 223 
LEU   CD1 HD11 sing N N 224 
LEU   CD1 HD12 sing N N 225 
LEU   CD1 HD13 sing N N 226 
LEU   CD2 HD21 sing N N 227 
LEU   CD2 HD22 sing N N 228 
LEU   CD2 HD23 sing N N 229 
LEU   OXT HXT  sing N N 230 
LYS   N   CA   sing N N 231 
LYS   N   H    sing N N 232 
LYS   N   H2   sing N N 233 
LYS   CA  C    sing N N 234 
LYS   CA  CB   sing N N 235 
LYS   CA  HA   sing N N 236 
LYS   C   O    doub N N 237 
LYS   C   OXT  sing N N 238 
LYS   CB  CG   sing N N 239 
LYS   CB  HB2  sing N N 240 
LYS   CB  HB3  sing N N 241 
LYS   CG  CD   sing N N 242 
LYS   CG  HG2  sing N N 243 
LYS   CG  HG3  sing N N 244 
LYS   CD  CE   sing N N 245 
LYS   CD  HD2  sing N N 246 
LYS   CD  HD3  sing N N 247 
LYS   CE  NZ   sing N N 248 
LYS   CE  HE2  sing N N 249 
LYS   CE  HE3  sing N N 250 
LYS   NZ  HZ1  sing N N 251 
LYS   NZ  HZ2  sing N N 252 
LYS   NZ  HZ3  sing N N 253 
LYS   OXT HXT  sing N N 254 
MET   N   CA   sing N N 255 
MET   N   H    sing N N 256 
MET   N   H2   sing N N 257 
MET   CA  C    sing N N 258 
MET   CA  CB   sing N N 259 
MET   CA  HA   sing N N 260 
MET   C   O    doub N N 261 
MET   C   OXT  sing N N 262 
MET   CB  CG   sing N N 263 
MET   CB  HB2  sing N N 264 
MET   CB  HB3  sing N N 265 
MET   CG  SD   sing N N 266 
MET   CG  HG2  sing N N 267 
MET   CG  HG3  sing N N 268 
MET   SD  CE   sing N N 269 
MET   CE  HE1  sing N N 270 
MET   CE  HE2  sing N N 271 
MET   CE  HE3  sing N N 272 
MET   OXT HXT  sing N N 273 
PHE   N   CA   sing N N 274 
PHE   N   H    sing N N 275 
PHE   N   H2   sing N N 276 
PHE   CA  C    sing N N 277 
PHE   CA  CB   sing N N 278 
PHE   CA  HA   sing N N 279 
PHE   C   O    doub N N 280 
PHE   C   OXT  sing N N 281 
PHE   CB  CG   sing N N 282 
PHE   CB  HB2  sing N N 283 
PHE   CB  HB3  sing N N 284 
PHE   CG  CD1  doub Y N 285 
PHE   CG  CD2  sing Y N 286 
PHE   CD1 CE1  sing Y N 287 
PHE   CD1 HD1  sing N N 288 
PHE   CD2 CE2  doub Y N 289 
PHE   CD2 HD2  sing N N 290 
PHE   CE1 CZ   doub Y N 291 
PHE   CE1 HE1  sing N N 292 
PHE   CE2 CZ   sing Y N 293 
PHE   CE2 HE2  sing N N 294 
PHE   CZ  HZ   sing N N 295 
PHE   OXT HXT  sing N N 296 
PRO   N   CA   sing N N 297 
PRO   N   CD   sing N N 298 
PRO   N   H    sing N N 299 
PRO   CA  C    sing N N 300 
PRO   CA  CB   sing N N 301 
PRO   CA  HA   sing N N 302 
PRO   C   O    doub N N 303 
PRO   C   OXT  sing N N 304 
PRO   CB  CG   sing N N 305 
PRO   CB  HB2  sing N N 306 
PRO   CB  HB3  sing N N 307 
PRO   CG  CD   sing N N 308 
PRO   CG  HG2  sing N N 309 
PRO   CG  HG3  sing N N 310 
PRO   CD  HD2  sing N N 311 
PRO   CD  HD3  sing N N 312 
PRO   OXT HXT  sing N N 313 
SER   N   CA   sing N N 314 
SER   N   H    sing N N 315 
SER   N   H2   sing N N 316 
SER   CA  C    sing N N 317 
SER   CA  CB   sing N N 318 
SER   CA  HA   sing N N 319 
SER   C   O    doub N N 320 
SER   C   OXT  sing N N 321 
SER   CB  OG   sing N N 322 
SER   CB  HB2  sing N N 323 
SER   CB  HB3  sing N N 324 
SER   OG  HG   sing N N 325 
SER   OXT HXT  sing N N 326 
THR   N   CA   sing N N 327 
THR   N   H    sing N N 328 
THR   N   H2   sing N N 329 
THR   CA  C    sing N N 330 
THR   CA  CB   sing N N 331 
THR   CA  HA   sing N N 332 
THR   C   O    doub N N 333 
THR   C   OXT  sing N N 334 
THR   CB  OG1  sing N N 335 
THR   CB  CG2  sing N N 336 
THR   CB  HB   sing N N 337 
THR   OG1 HG1  sing N N 338 
THR   CG2 HG21 sing N N 339 
THR   CG2 HG22 sing N N 340 
THR   CG2 HG23 sing N N 341 
THR   OXT HXT  sing N N 342 
TRP   N   CA   sing N N 343 
TRP   N   H    sing N N 344 
TRP   N   H2   sing N N 345 
TRP   CA  C    sing N N 346 
TRP   CA  CB   sing N N 347 
TRP   CA  HA   sing N N 348 
TRP   C   O    doub N N 349 
TRP   C   OXT  sing N N 350 
TRP   CB  CG   sing N N 351 
TRP   CB  HB2  sing N N 352 
TRP   CB  HB3  sing N N 353 
TRP   CG  CD1  doub Y N 354 
TRP   CG  CD2  sing Y N 355 
TRP   CD1 NE1  sing Y N 356 
TRP   CD1 HD1  sing N N 357 
TRP   CD2 CE2  doub Y N 358 
TRP   CD2 CE3  sing Y N 359 
TRP   NE1 CE2  sing Y N 360 
TRP   NE1 HE1  sing N N 361 
TRP   CE2 CZ2  sing Y N 362 
TRP   CE3 CZ3  doub Y N 363 
TRP   CE3 HE3  sing N N 364 
TRP   CZ2 CH2  doub Y N 365 
TRP   CZ2 HZ2  sing N N 366 
TRP   CZ3 CH2  sing Y N 367 
TRP   CZ3 HZ3  sing N N 368 
TRP   CH2 HH2  sing N N 369 
TRP   OXT HXT  sing N N 370 
TYR   N   CA   sing N N 371 
TYR   N   H    sing N N 372 
TYR   N   H2   sing N N 373 
TYR   CA  C    sing N N 374 
TYR   CA  CB   sing N N 375 
TYR   CA  HA   sing N N 376 
TYR   C   O    doub N N 377 
TYR   C   OXT  sing N N 378 
TYR   CB  CG   sing N N 379 
TYR   CB  HB2  sing N N 380 
TYR   CB  HB3  sing N N 381 
TYR   CG  CD1  doub Y N 382 
TYR   CG  CD2  sing Y N 383 
TYR   CD1 CE1  sing Y N 384 
TYR   CD1 HD1  sing N N 385 
TYR   CD2 CE2  doub Y N 386 
TYR   CD2 HD2  sing N N 387 
TYR   CE1 CZ   doub Y N 388 
TYR   CE1 HE1  sing N N 389 
TYR   CE2 CZ   sing Y N 390 
TYR   CE2 HE2  sing N N 391 
TYR   CZ  OH   sing N N 392 
TYR   OH  HH   sing N N 393 
TYR   OXT HXT  sing N N 394 
VAL   N   CA   sing N N 395 
VAL   N   H    sing N N 396 
VAL   N   H2   sing N N 397 
VAL   CA  C    sing N N 398 
VAL   CA  CB   sing N N 399 
VAL   CA  HA   sing N N 400 
VAL   C   O    doub N N 401 
VAL   C   OXT  sing N N 402 
VAL   CB  CG1  sing N N 403 
VAL   CB  CG2  sing N N 404 
VAL   CB  HB   sing N N 405 
VAL   CG1 HG11 sing N N 406 
VAL   CG1 HG12 sing N N 407 
VAL   CG1 HG13 sing N N 408 
VAL   CG2 HG21 sing N N 409 
VAL   CG2 HG22 sing N N 410 
VAL   CG2 HG23 sing N N 411 
VAL   OXT HXT  sing N N 412 
# 
_pdbx_audit_support.funding_organization   'The Structural Genomics Consortium (SGC)' 
_pdbx_audit_support.country                Canada 
_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   4BKY 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9F31 
_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]   0.005926 
_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]   0.005926 
_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]   0.005926 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
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   . MET   A 1 2   ? -24.788 -18.745 -8.633  1.00 81.13  ? 1   MET   A N   1 
ATOM   2    C CA  . MET   A 1 2   ? -24.265 -19.190 -9.952  1.00 78.65  ? 1   MET   A CA  1 
ATOM   3    C C   . MET   A 1 2   ? -24.563 -20.673 -10.137 1.00 91.26  ? 1   MET   A C   1 
ATOM   4    O O   . MET   A 1 2   ? -24.077 -21.250 -11.105 1.00 107.90 ? 1   MET   A O   1 
ATOM   5    C CB  . MET   A 1 2   ? -22.749 -18.963 -10.086 1.00 70.47  ? 1   MET   A CB  1 
ATOM   6    N N   . LYS   A 1 3   ? -25.354 -21.281 -9.227  1.00 70.83  ? 2   LYS   A N   1 
ATOM   7    C CA  . LYS   A 1 3   ? -25.497 -22.734 -9.154  1.00 69.45  ? 2   LYS   A CA  1 
ATOM   8    C C   . LYS   A 1 3   ? -24.224 -23.354 -8.578  1.00 72.59  ? 2   LYS   A C   1 
ATOM   9    O O   . LYS   A 1 3   ? -24.205 -24.534 -8.242  1.00 82.17  ? 2   LYS   A O   1 
ATOM   10   C CB  . LYS   A 1 3   ? -25.764 -23.468 -10.479 1.00 59.95  ? 2   LYS   A CB  1 
ATOM   11   N N   . ASP   A 1 4   ? -23.154 -22.560 -8.465  1.00 71.11  ? 3   ASP   A N   1 
ATOM   12   C CA  . ASP   A 1 4   ? -21.968 -22.973 -7.741  1.00 65.98  ? 3   ASP   A CA  1 
ATOM   13   C C   . ASP   A 1 4   ? -22.220 -22.977 -6.243  1.00 65.68  ? 3   ASP   A C   1 
ATOM   14   O O   . ASP   A 1 4   ? -21.409 -23.514 -5.509  1.00 63.81  ? 3   ASP   A O   1 
ATOM   15   C CB  . ASP   A 1 4   ? -20.821 -22.032 -8.027  1.00 67.59  ? 3   ASP   A CB  1 
ATOM   16   C CG  . ASP   A 1 4   ? -20.285 -22.189 -9.429  1.00 68.65  ? 3   ASP   A CG  1 
ATOM   17   O OD1 . ASP   A 1 4   ? -19.905 -23.331 -9.761  1.00 71.79  ? 3   ASP   A OD1 1 
ATOM   18   O OD2 . ASP   A 1 4   ? -20.289 -21.182 -10.161 1.00 84.60  ? 3   ASP   A OD2 1 
ATOM   19   N N   . TYR   A 1 5   ? -23.311 -22.330 -5.812  1.00 61.33  ? 4   TYR   A N   1 
ATOM   20   C CA  . TYR   A 1 5   ? -23.627 -22.172 -4.407  1.00 61.99  ? 4   TYR   A CA  1 
ATOM   21   C C   . TYR   A 1 5   ? -24.721 -23.140 -3.973  1.00 64.03  ? 4   TYR   A C   1 
ATOM   22   O O   . TYR   A 1 5   ? -25.050 -23.187 -2.797  1.00 60.39  ? 4   TYR   A O   1 
ATOM   23   C CB  . TYR   A 1 5   ? -24.051 -20.723 -4.198  1.00 60.29  ? 4   TYR   A CB  1 
ATOM   24   C CG  . TYR   A 1 5   ? -22.885 -19.766 -4.374  1.00 58.67  ? 4   TYR   A CG  1 
ATOM   25   C CD1 . TYR   A 1 5   ? -22.488 -19.336 -5.635  1.00 69.63  ? 4   TYR   A CD1 1 
ATOM   26   C CD2 . TYR   A 1 5   ? -22.146 -19.337 -3.285  1.00 58.78  ? 4   TYR   A CD2 1 
ATOM   27   C CE1 . TYR   A 1 5   ? -21.400 -18.490 -5.804  1.00 63.67  ? 4   TYR   A CE1 1 
ATOM   28   C CE2 . TYR   A 1 5   ? -21.067 -18.476 -3.440  1.00 63.52  ? 4   TYR   A CE2 1 
ATOM   29   C CZ  . TYR   A 1 5   ? -20.686 -18.059 -4.701  1.00 60.22  ? 4   TYR   A CZ  1 
ATOM   30   O OH  . TYR   A 1 5   ? -19.629 -17.194 -4.818  1.00 69.30  ? 4   TYR   A OH  1 
ATOM   31   N N   . ASP   A 1 6   ? -25.252 -23.927 -4.913  1.00 63.02  ? 5   ASP   A N   1 
ATOM   32   C CA  . ASP   A 1 6   ? -26.372 -24.795 -4.605  1.00 66.17  ? 5   ASP   A CA  1 
ATOM   33   C C   . ASP   A 1 6   ? -25.950 -25.799 -3.549  1.00 58.34  ? 5   ASP   A C   1 
ATOM   34   O O   . ASP   A 1 6   ? -26.511 -25.789 -2.464  1.00 58.92  ? 5   ASP   A O   1 
ATOM   35   C CB  . ASP   A 1 6   ? -26.939 -25.469 -5.843  1.00 75.50  ? 5   ASP   A CB  1 
ATOM   36   C CG  . ASP   A 1 6   ? -27.806 -24.557 -6.697  1.00 80.97  ? 5   ASP   A CG  1 
ATOM   37   O OD1 . ASP   A 1 6   ? -27.999 -23.391 -6.291  1.00 78.43  ? 5   ASP   A OD1 1 
ATOM   38   O OD2 . ASP   A 1 6   ? -28.288 -25.022 -7.748  1.00 87.74  ? 5   ASP   A OD2 1 
ATOM   39   N N   . GLU   A 1 7   ? -24.946 -26.623 -3.870  1.00 55.58  ? 6   GLU   A N   1 
ATOM   40   C CA  . GLU   A 1 7   ? -24.479 -27.642 -2.944  1.00 56.73  ? 6   GLU   A CA  1 
ATOM   41   C C   . GLU   A 1 7   ? -24.109 -26.980 -1.608  1.00 53.33  ? 6   GLU   A C   1 
ATOM   42   O O   . GLU   A 1 7   ? -24.601 -27.396 -0.560  1.00 50.78  ? 6   GLU   A O   1 
ATOM   43   C CB  . GLU   A 1 7   ? -23.357 -28.443 -3.610  1.00 65.54  ? 6   GLU   A CB  1 
ATOM   44   C CG  . GLU   A 1 7   ? -22.793 -29.587 -2.764  1.00 76.37  ? 6   GLU   A CG  1 
ATOM   45   C CD  . GLU   A 1 7   ? -23.603 -30.872 -2.668  1.00 88.00  ? 6   GLU   A CD  1 
ATOM   46   O OE1 . GLU   A 1 7   ? -24.684 -30.924 -3.313  1.00 94.35  ? 6   GLU   A OE1 1 
ATOM   47   O OE2 . GLU   A 1 7   ? -23.154 -31.818 -1.962  1.00 73.73  ? 6   GLU   A OE2 1 
ATOM   48   N N   . LEU   A 1 8   ? -23.294 -25.912 -1.643  1.00 46.31  ? 7   LEU   A N   1 
ATOM   49   C CA  . LEU   A 1 8   ? -22.798 -25.287 -0.418  1.00 46.36  ? 7   LEU   A CA  1 
ATOM   50   C C   . LEU   A 1 8   ? -23.944 -24.933 0.532   1.00 45.72  ? 7   LEU   A C   1 
ATOM   51   O O   . LEU   A 1 8   ? -23.836 -25.124 1.746   1.00 40.53  ? 7   LEU   A O   1 
ATOM   52   C CB  . LEU   A 1 8   ? -21.973 -24.038 -0.723  1.00 43.27  ? 7   LEU   A CB  1 
ATOM   53   C CG  . LEU   A 1 8   ? -21.290 -23.383 0.485   1.00 44.07  ? 7   LEU   A CG  1 
ATOM   54   C CD1 . LEU   A 1 8   ? -20.047 -24.181 0.829   1.00 42.24  ? 7   LEU   A CD1 1 
ATOM   55   C CD2 . LEU   A 1 8   ? -20.952 -21.918 0.266   1.00 45.11  ? 7   LEU   A CD2 1 
ATOM   56   N N   . LEU   A 1 9   ? -25.013 -24.368 -0.037  1.00 43.89  ? 8   LEU   A N   1 
ATOM   57   C CA  . LEU   A 1 9   ? -26.117 -23.818 0.724   1.00 48.83  ? 8   LEU   A CA  1 
ATOM   58   C C   . LEU   A 1 9   ? -27.059 -24.912 1.235   1.00 47.19  ? 8   LEU   A C   1 
ATOM   59   O O   . LEU   A 1 9   ? -27.965 -24.627 2.005   1.00 46.13  ? 8   LEU   A O   1 
ATOM   60   C CB  . LEU   A 1 9   ? -26.841 -22.827 -0.187  1.00 53.00  ? 8   LEU   A CB  1 
ATOM   61   C CG  . LEU   A 1 9   ? -26.058 -21.551 -0.525  1.00 59.75  ? 8   LEU   A CG  1 
ATOM   62   C CD1 . LEU   A 1 9   ? -26.796 -20.716 -1.571  1.00 59.16  ? 8   LEU   A CD1 1 
ATOM   63   C CD2 . LEU   A 1 9   ? -25.798 -20.718 0.722   1.00 59.79  ? 8   LEU   A CD2 1 
ATOM   64   N N   . LYS   A 1 10  ? -26.835 -26.168 0.862   1.00 47.93  ? 9   LYS   A N   1 
ATOM   65   C CA  . LYS   A 1 10  ? -27.472 -27.261 1.580   1.00 48.63  ? 9   LYS   A CA  1 
ATOM   66   C C   . LYS   A 1 10  ? -26.826 -27.443 2.952   1.00 46.99  ? 9   LYS   A C   1 
ATOM   67   O O   . LYS   A 1 10  ? -27.412 -28.087 3.804   1.00 45.46  ? 9   LYS   A O   1 
ATOM   68   C CB  . LYS   A 1 10  ? -27.333 -28.610 0.868   1.00 53.31  ? 9   LYS   A CB  1 
ATOM   69   C CG  . LYS   A 1 10  ? -27.996 -28.725 -0.483  1.00 56.71  ? 9   LYS   A CG  1 
ATOM   70   C CD  . LYS   A 1 10  ? -27.592 -30.000 -1.213  1.00 62.34  ? 9   LYS   A CD  1 
ATOM   71   C CE  . LYS   A 1 10  ? -27.997 -29.961 -2.647  1.00 74.47  ? 9   LYS   A CE  1 
ATOM   72   N NZ  . LYS   A 1 10  ? -27.277 -30.995 -3.399  1.00 82.70  ? 9   LYS   A NZ  1 
ATOM   73   N N   . TYR   A 1 11  ? -25.615 -26.912 3.183   1.00 43.00  ? 10  TYR   A N   1 
ATOM   74   C CA  . TYR   A 1 11  ? -24.920 -27.261 4.414   1.00 39.16  ? 10  TYR   A CA  1 
ATOM   75   C C   . TYR   A 1 11  ? -24.601 -26.032 5.248   1.00 37.86  ? 10  TYR   A C   1 
ATOM   76   O O   . TYR   A 1 11  ? -24.468 -26.165 6.469   1.00 39.11  ? 10  TYR   A O   1 
ATOM   77   C CB  . TYR   A 1 11  ? -23.609 -28.009 4.153   1.00 40.95  ? 10  TYR   A CB  1 
ATOM   78   C CG  . TYR   A 1 11  ? -23.768 -29.183 3.206   1.00 39.38  ? 10  TYR   A CG  1 
ATOM   79   C CD1 . TYR   A 1 11  ? -24.626 -30.242 3.473   1.00 43.26  ? 10  TYR   A CD1 1 
ATOM   80   C CD2 . TYR   A 1 11  ? -23.089 -29.181 2.001   1.00 49.68  ? 10  TYR   A CD2 1 
ATOM   81   C CE1 . TYR   A 1 11  ? -24.770 -31.300 2.580   1.00 50.56  ? 10  TYR   A CE1 1 
ATOM   82   C CE2 . TYR   A 1 11  ? -23.190 -30.242 1.120   1.00 52.07  ? 10  TYR   A CE2 1 
ATOM   83   C CZ  . TYR   A 1 11  ? -24.042 -31.295 1.397   1.00 54.01  ? 10  TYR   A CZ  1 
ATOM   84   O OH  . TYR   A 1 11  ? -24.119 -32.249 0.425   1.00 65.68  ? 10  TYR   A OH  1 
ATOM   85   N N   . TYR   A 1 12  ? -24.483 -24.863 4.591   1.00 35.51  ? 11  TYR   A N   1 
ATOM   86   C CA  . TYR   A 1 12  ? -24.053 -23.646 5.260   1.00 38.78  ? 11  TYR   A CA  1 
ATOM   87   C C   . TYR   A 1 12  ? -25.024 -22.507 4.934   1.00 41.29  ? 11  TYR   A C   1 
ATOM   88   O O   . TYR   A 1 12  ? -25.613 -22.462 3.852   1.00 41.24  ? 11  TYR   A O   1 
ATOM   89   C CB  . TYR   A 1 12  ? -22.632 -23.264 4.845   1.00 36.78  ? 11  TYR   A CB  1 
ATOM   90   C CG  . TYR   A 1 12  ? -21.631 -24.366 5.134   1.00 32.85  ? 11  TYR   A CG  1 
ATOM   91   C CD1 . TYR   A 1 12  ? -21.021 -24.472 6.384   1.00 35.13  ? 11  TYR   A CD1 1 
ATOM   92   C CD2 . TYR   A 1 12  ? -21.330 -25.325 4.183   1.00 35.19  ? 11  TYR   A CD2 1 
ATOM   93   C CE1 . TYR   A 1 12  ? -20.143 -25.500 6.681   1.00 32.39  ? 11  TYR   A CE1 1 
ATOM   94   C CE2 . TYR   A 1 12  ? -20.428 -26.345 4.462   1.00 36.59  ? 11  TYR   A CE2 1 
ATOM   95   C CZ  . TYR   A 1 12  ? -19.850 -26.444 5.719   1.00 32.44  ? 11  TYR   A CZ  1 
ATOM   96   O OH  . TYR   A 1 12  ? -18.985 -27.456 6.021   1.00 35.98  ? 11  TYR   A OH  1 
ATOM   97   N N   . GLU   A 1 13  ? -25.160 -21.607 5.912   1.00 41.25  ? 12  GLU   A N   1 
ATOM   98   C CA  . GLU   A 1 13  ? -25.788 -20.307 5.729   1.00 46.06  ? 12  GLU   A CA  1 
ATOM   99   C C   . GLU   A 1 13  ? -24.665 -19.270 5.763   1.00 42.24  ? 12  GLU   A C   1 
ATOM   100  O O   . GLU   A 1 13  ? -23.907 -19.204 6.729   1.00 40.49  ? 12  GLU   A O   1 
ATOM   101  C CB  . GLU   A 1 13  ? -26.898 -20.175 6.778   1.00 50.53  ? 12  GLU   A CB  1 
ATOM   102  C CG  . GLU   A 1 13  ? -27.514 -18.786 6.883   1.00 68.02  ? 12  GLU   A CG  1 
ATOM   103  C CD  . GLU   A 1 13  ? -28.387 -18.582 8.119   1.00 84.00  ? 12  GLU   A CD  1 
ATOM   104  O OE1 . GLU   A 1 13  ? -27.902 -18.672 9.296   1.00 67.73  ? 12  GLU   A OE1 1 
ATOM   105  O OE2 . GLU   A 1 13  ? -29.578 -18.283 7.862   1.00 87.06  ? 12  GLU   A OE2 1 
ATOM   106  N N   . LEU   A 1 14  ? -24.563 -18.502 4.669   1.00 42.58  ? 13  LEU   A N   1 
ATOM   107  C CA  . LEU   A 1 14  ? -23.510 -17.528 4.453   1.00 43.24  ? 13  LEU   A CA  1 
ATOM   108  C C   . LEU   A 1 14  ? -23.814 -16.227 5.173   1.00 47.84  ? 13  LEU   A C   1 
ATOM   109  O O   . LEU   A 1 14  ? -24.927 -15.734 5.073   1.00 49.91  ? 13  LEU   A O   1 
ATOM   110  C CB  . LEU   A 1 14  ? -23.396 -17.321 2.945   1.00 51.14  ? 13  LEU   A CB  1 
ATOM   111  C CG  . LEU   A 1 14  ? -22.710 -18.447 2.159   1.00 54.52  ? 13  LEU   A CG  1 
ATOM   112  C CD1 . LEU   A 1 14  ? -22.558 -18.033 0.707   1.00 56.01  ? 13  LEU   A CD1 1 
ATOM   113  C CD2 . LEU   A 1 14  ? -21.353 -18.834 2.763   1.00 52.71  ? 13  LEU   A CD2 1 
ATOM   114  N N   . HIS   A 1 15  ? -22.822 -15.687 5.888   1.00 43.11  ? 14  HIS   A N   1 
ATOM   115  C CA  . HIS   A 1 15  ? -22.973 -14.394 6.533   1.00 49.66  ? 14  HIS   A CA  1 
ATOM   116  C C   . HIS   A 1 15  ? -22.068 -13.399 5.812   1.00 44.53  ? 14  HIS   A C   1 
ATOM   117  O O   . HIS   A 1 15  ? -21.944 -13.469 4.597   1.00 53.46  ? 14  HIS   A O   1 
ATOM   118  C CB  . HIS   A 1 15  ? -22.752 -14.520 8.044   1.00 47.58  ? 14  HIS   A CB  1 
ATOM   119  C CG  . HIS   A 1 15  ? -23.803 -15.334 8.696   1.00 52.97  ? 14  HIS   A CG  1 
ATOM   120  N ND1 . HIS   A 1 15  ? -23.549 -16.297 9.648   1.00 59.53  ? 14  HIS   A ND1 1 
ATOM   121  C CD2 . HIS   A 1 15  ? -25.116 -15.361 8.485   1.00 62.10  ? 14  HIS   A CD2 1 
ATOM   122  C CE1 . HIS   A 1 15  ? -24.683 -16.892 9.980   1.00 55.96  ? 14  HIS   A CE1 1 
ATOM   123  N NE2 . HIS   A 1 15  ? -25.637 -16.343 9.279   1.00 60.07  ? 14  HIS   A NE2 1 
ATOM   124  N N   . GLU   A 1 16  ? -21.372 -12.547 6.571   1.00 48.37  ? 15  GLU   A N   1 
ATOM   125  C CA  . GLU   A 1 16  ? -20.637 -11.425 6.016   1.00 49.96  ? 15  GLU   A CA  1 
ATOM   126  C C   . GLU   A 1 16  ? -19.259 -11.850 5.527   1.00 51.64  ? 15  GLU   A C   1 
ATOM   127  O O   . GLU   A 1 16  ? -18.628 -12.751 6.095   1.00 51.39  ? 15  GLU   A O   1 
ATOM   128  C CB  . GLU   A 1 16  ? -20.505 -10.294 7.032   1.00 53.70  ? 15  GLU   A CB  1 
ATOM   129  C CG  . GLU   A 1 16  ? -19.561 -10.568 8.205   1.00 51.42  ? 15  GLU   A CG  1 
ATOM   130  C CD  . GLU   A 1 16  ? -20.239 -11.088 9.443   1.00 57.75  ? 15  GLU   A CD  1 
ATOM   131  O OE1 . GLU   A 1 16  ? -21.155 -11.918 9.257   1.00 61.57  ? 15  GLU   A OE1 1 
ATOM   132  O OE2 . GLU   A 1 16  ? -19.848 -10.701 10.568  1.00 57.84  ? 15  GLU   A OE2 1 
ATOM   133  N N   . THR   A 1 17  ? -18.815 -11.163 4.465   1.00 50.74  ? 16  THR   A N   1 
ATOM   134  C CA  . THR   A 1 17  ? -17.470 -11.277 3.934   1.00 46.30  ? 16  THR   A CA  1 
ATOM   135  C C   . THR   A 1 17  ? -16.531 -10.753 5.001   1.00 49.36  ? 16  THR   A C   1 
ATOM   136  O O   . THR   A 1 17  ? -16.873 -9.801  5.662   1.00 64.94  ? 16  THR   A O   1 
ATOM   137  C CB  . THR   A 1 17  ? -17.358 -10.522 2.610   1.00 52.21  ? 16  THR   A CB  1 
ATOM   138  O OG1 . THR   A 1 17  ? -18.249 -11.186 1.710   1.00 52.68  ? 16  THR   A OG1 1 
ATOM   139  C CG2 . THR   A 1 17  ? -15.947 -10.506 2.049   1.00 56.33  ? 16  THR   A CG2 1 
ATOM   140  N N   . ILE   A 1 18  ? -15.414 -11.440 5.264   1.00 50.69  ? 17  ILE   A N   1 
ATOM   141  C CA  . ILE   A 1 18  ? -14.453 -10.942 6.237   1.00 55.80  ? 17  ILE   A CA  1 
ATOM   142  C C   . ILE   A 1 18  ? -13.073 -10.789 5.603   1.00 56.67  ? 17  ILE   A C   1 
ATOM   143  O O   . ILE   A 1 18  ? -12.122 -10.450 6.292   1.00 68.06  ? 17  ILE   A O   1 
ATOM   144  C CB  . ILE   A 1 18  ? -14.369 -11.825 7.494   1.00 53.61  ? 17  ILE   A CB  1 
ATOM   145  C CG1 . ILE   A 1 18  ? -13.997 -13.257 7.172   1.00 59.36  ? 17  ILE   A CG1 1 
ATOM   146  C CG2 . ILE   A 1 18  ? -15.663 -11.737 8.290   1.00 60.85  ? 17  ILE   A CG2 1 
ATOM   147  C CD1 . ILE   A 1 18  ? -13.576 -14.050 8.390   1.00 66.31  ? 17  ILE   A CD1 1 
ATOM   148  N N   . GLY   A 1 19  ? -12.957 -11.029 4.301   1.00 58.40  ? 18  GLY   A N   1 
ATOM   149  C CA  . GLY   A 1 19  ? -11.669 -10.967 3.635   1.00 61.00  ? 18  GLY   A CA  1 
ATOM   150  C C   . GLY   A 1 19  ? -11.834 -11.163 2.135   1.00 66.83  ? 18  GLY   A C   1 
ATOM   151  O O   . GLY   A 1 19  ? -12.655 -11.966 1.695   1.00 59.74  ? 18  GLY   A O   1 
ATOM   152  N N   . THR   A 1 20  ? -11.082 -10.382 1.355   1.00 79.12  ? 19  THR   A N   1 
ATOM   153  C CA  . THR   A 1 20  ? -11.084 -10.532 -0.092  1.00 85.16  ? 19  THR   A CA  1 
ATOM   154  C C   . THR   A 1 20  ? -9.640  -10.491 -0.576  1.00 86.44  ? 19  THR   A C   1 
ATOM   155  O O   . THR   A 1 20  ? -8.722  -10.306 0.219   1.00 86.68  ? 19  THR   A O   1 
ATOM   156  C CB  . THR   A 1 20  ? -11.994 -9.473  -0.710  1.00 82.54  ? 19  THR   A CB  1 
ATOM   157  O OG1 . THR   A 1 20  ? -13.288 -9.836  -0.231  1.00 85.48  ? 19  THR   A OG1 1 
ATOM   158  C CG2 . THR   A 1 20  ? -12.017 -9.476  -2.227  1.00 80.24  ? 19  THR   A CG2 1 
ATOM   159  N N   . GLY   A 1 21  ? -9.449  -10.793 -1.860  1.00 90.85  ? 20  GLY   A N   1 
ATOM   160  C CA  . GLY   A 1 21  ? -8.127  -10.927 -2.446  1.00 87.04  ? 20  GLY   A CA  1 
ATOM   161  C C   . GLY   A 1 21  ? -8.254  -11.474 -3.865  1.00 87.38  ? 20  GLY   A C   1 
ATOM   162  O O   . GLY   A 1 21  ? -9.319  -11.944 -4.258  1.00 98.67  ? 20  GLY   A O   1 
ATOM   163  N N   . GLY   A 1 22  ? -7.175  -11.392 -4.644  1.00 84.67  ? 21  GLY   A N   1 
ATOM   164  C CA  . GLY   A 1 22  ? -7.133  -12.089 -5.916  1.00 90.49  ? 21  GLY   A CA  1 
ATOM   165  C C   . GLY   A 1 22  ? -7.348  -13.585 -5.696  1.00 93.19  ? 21  GLY   A C   1 
ATOM   166  O O   . GLY   A 1 22  ? -6.817  -14.167 -4.746  1.00 101.01 ? 21  GLY   A O   1 
ATOM   167  N N   . PHE   A 1 23  ? -8.195  -14.183 -6.534  1.00 93.61  ? 22  PHE   A N   1 
ATOM   168  C CA  . PHE   A 1 23  ? -8.417  -15.627 -6.531  1.00 100.44 ? 22  PHE   A CA  1 
ATOM   169  C C   . PHE   A 1 23  ? -9.377  -16.089 -5.422  1.00 89.17  ? 22  PHE   A C   1 
ATOM   170  O O   . PHE   A 1 23  ? -10.052 -17.090 -5.663  1.00 78.46  ? 22  PHE   A O   1 
ATOM   171  C CB  . PHE   A 1 23  ? -7.086  -16.387 -6.464  1.00 91.45  ? 22  PHE   A CB  1 
ATOM   172  N N   . ALA   A 1 24  ? -9.472  -15.368 -4.268  1.00 82.34  ? 23  ALA   A N   1 
ATOM   173  C CA  . ALA   A 1 24  ? -10.148 -15.840 -3.051  1.00 77.77  ? 23  ALA   A CA  1 
ATOM   174  C C   . ALA   A 1 24  ? -10.997 -14.779 -2.317  1.00 67.28  ? 23  ALA   A C   1 
ATOM   175  O O   . ALA   A 1 24  ? -10.602 -13.639 -2.137  1.00 68.37  ? 23  ALA   A O   1 
ATOM   176  C CB  . ALA   A 1 24  ? -9.107  -16.399 -2.104  1.00 77.08  ? 23  ALA   A CB  1 
ATOM   177  N N   . LYS   A 1 25  ? -12.163 -15.192 -1.812  1.00 58.35  ? 24  LYS   A N   1 
ATOM   178  C CA  . LYS   A 1 25  ? -12.939 -14.431 -0.840  1.00 54.00  ? 24  LYS   A CA  1 
ATOM   179  C C   . LYS   A 1 25  ? -13.149 -15.274 0.431   1.00 50.94  ? 24  LYS   A C   1 
ATOM   180  O O   . LYS   A 1 25  ? -13.400 -16.471 0.322   1.00 51.83  ? 24  LYS   A O   1 
ATOM   181  C CB  . LYS   A 1 25  ? -14.277 -14.095 -1.515  1.00 60.39  ? 24  LYS   A CB  1 
ATOM   182  C CG  . LYS   A 1 25  ? -15.161 -13.112 -0.765  1.00 63.66  ? 24  LYS   A CG  1 
ATOM   183  C CD  . LYS   A 1 25  ? -16.601 -12.956 -1.257  1.00 72.04  ? 24  LYS   A CD  1 
ATOM   184  C CE  . LYS   A 1 25  ? -16.775 -12.146 -2.499  1.00 79.12  ? 24  LYS   A CE  1 
ATOM   185  N NZ  . LYS   A 1 25  ? -16.796 -12.995 -3.687  1.00 88.15  ? 24  LYS   A NZ  1 
ATOM   186  N N   . VAL   A 1 26  ? -13.088 -14.665 1.630   1.00 43.04  ? 25  VAL   A N   1 
ATOM   187  C CA  . VAL   A 1 26  ? -13.412 -15.357 2.870   1.00 45.32  ? 25  VAL   A CA  1 
ATOM   188  C C   . VAL   A 1 26  ? -14.709 -14.810 3.482   1.00 50.40  ? 25  VAL   A C   1 
ATOM   189  O O   . VAL   A 1 26  ? -14.842 -13.607 3.732   1.00 52.00  ? 25  VAL   A O   1 
ATOM   190  C CB  . VAL   A 1 26  ? -12.254 -15.364 3.888   1.00 43.67  ? 25  VAL   A CB  1 
ATOM   191  C CG1 . VAL   A 1 26  ? -12.601 -16.184 5.121   1.00 47.62  ? 25  VAL   A CG1 1 
ATOM   192  C CG2 . VAL   A 1 26  ? -10.979 -15.922 3.270   1.00 45.48  ? 25  VAL   A CG2 1 
ATOM   193  N N   . LYS   A 1 27  ? -15.661 -15.726 3.717   1.00 46.92  ? 26  LYS   A N   1 
ATOM   194  C CA  . LYS   A 1 27  ? -16.961 -15.422 4.312   1.00 47.65  ? 26  LYS   A CA  1 
ATOM   195  C C   . LYS   A 1 27  ? -17.140 -16.161 5.639   1.00 50.08  ? 26  LYS   A C   1 
ATOM   196  O O   . LYS   A 1 27  ? -16.681 -17.297 5.806   1.00 45.18  ? 26  LYS   A O   1 
ATOM   197  C CB  . LYS   A 1 27  ? -18.086 -15.786 3.338   1.00 51.07  ? 26  LYS   A CB  1 
ATOM   198  C CG  . LYS   A 1 27  ? -18.512 -14.667 2.383   1.00 52.11  ? 26  LYS   A CG  1 
ATOM   199  C CD  . LYS   A 1 27  ? -19.943 -14.879 1.896   1.00 58.86  ? 26  LYS   A CD  1 
ATOM   200  C CE  . LYS   A 1 27  ? -20.495 -13.747 1.075   1.00 61.72  ? 26  LYS   A CE  1 
ATOM   201  N NZ  . LYS   A 1 27  ? -20.591 -12.513 1.848   1.00 67.09  ? 26  LYS   A NZ  1 
ATOM   202  N N   . LEU   A 1 28  ? -17.750 -15.476 6.610   1.00 46.75  ? 27  LEU   A N   1 
ATOM   203  C CA  . LEU   A 1 28  ? -18.345 -16.102 7.784   1.00 46.19  ? 27  LEU   A CA  1 
ATOM   204  C C   . LEU   A 1 28  ? -19.575 -16.899 7.366   1.00 44.93  ? 27  LEU   A C   1 
ATOM   205  O O   . LEU   A 1 28  ? -20.339 -16.482 6.487   1.00 39.90  ? 27  LEU   A O   1 
ATOM   206  C CB  . LEU   A 1 28  ? -18.747 -15.092 8.857   1.00 54.03  ? 27  LEU   A CB  1 
ATOM   207  C CG  . LEU   A 1 28  ? -17.845 -15.033 10.082  1.00 70.93  ? 27  LEU   A CG  1 
ATOM   208  C CD1 . LEU   A 1 28  ? -18.015 -16.313 10.872  1.00 74.84  ? 27  LEU   A CD1 1 
ATOM   209  C CD2 . LEU   A 1 28  ? -16.407 -14.847 9.664   1.00 73.42  ? 27  LEU   A CD2 1 
ATOM   210  N N   . ALA   A 1 29  ? -19.783 -18.049 8.035   1.00 36.18  ? 28  ALA   A N   1 
ATOM   211  C CA  . ALA   A 1 29  ? -20.931 -18.870 7.720   1.00 35.25  ? 28  ALA   A CA  1 
ATOM   212  C C   . ALA   A 1 29  ? -21.271 -19.751 8.910   1.00 35.51  ? 28  ALA   A C   1 
ATOM   213  O O   . ALA   A 1 29  ? -20.518 -19.827 9.878   1.00 35.75  ? 28  ALA   A O   1 
ATOM   214  C CB  . ALA   A 1 29  ? -20.704 -19.669 6.463   1.00 38.92  ? 28  ALA   A CB  1 
ATOM   215  N N   . CYS   A 1 30  ? -22.477 -20.298 8.832   1.00 39.66  ? 29  CYS   A N   1 
ATOM   216  C CA  . CYS   A 1 30  ? -22.993 -21.156 9.868   1.00 41.40  ? 29  CYS   A CA  1 
ATOM   217  C C   . CYS   A 1 30  ? -23.234 -22.518 9.234   1.00 39.40  ? 29  CYS   A C   1 
ATOM   218  O O   . CYS   A 1 30  ? -23.908 -22.619 8.214   1.00 37.85  ? 29  CYS   A O   1 
ATOM   219  C CB  . CYS   A 1 30  ? -24.302 -20.619 10.443  1.00 44.73  ? 29  CYS   A CB  1 
ATOM   220  S SG  . CYS   A 1 30  ? -24.753 -21.520 11.949  1.00 55.84  ? 29  CYS   A SG  1 
ATOM   221  N N   . HIS   A 1 31  ? -22.626 -23.540 9.821   1.00 39.40  ? 30  HIS   A N   1 
ATOM   222  C CA  . HIS   A 1 31  ? -22.939 -24.921 9.458   1.00 37.74  ? 30  HIS   A CA  1 
ATOM   223  C C   . HIS   A 1 31  ? -24.276 -25.292 10.108  1.00 36.23  ? 30  HIS   A C   1 
ATOM   224  O O   . HIS   A 1 31  ? -24.377 -25.305 11.319  1.00 36.61  ? 30  HIS   A O   1 
ATOM   225  C CB  . HIS   A 1 31  ? -21.782 -25.802 9.935   1.00 35.93  ? 30  HIS   A CB  1 
ATOM   226  C CG  . HIS   A 1 31  ? -21.956 -27.276 9.780   1.00 37.11  ? 30  HIS   A CG  1 
ATOM   227  N ND1 . HIS   A 1 31  ? -22.456 -28.093 10.777  1.00 35.18  ? 30  HIS   A ND1 1 
ATOM   228  C CD2 . HIS   A 1 31  ? -21.586 -28.078 8.774   1.00 37.64  ? 30  HIS   A CD2 1 
ATOM   229  C CE1 . HIS   A 1 31  ? -22.397 -29.354 10.359  1.00 39.89  ? 30  HIS   A CE1 1 
ATOM   230  N NE2 . HIS   A 1 31  ? -21.895 -29.384 9.141   1.00 37.63  ? 30  HIS   A NE2 1 
ATOM   231  N N   . ILE   A 1 32  ? -25.262 -25.591 9.274   1.00 36.84  ? 31  ILE   A N   1 
ATOM   232  C CA  . ILE   A 1 32  ? -26.657 -25.707 9.670   1.00 44.00  ? 31  ILE   A CA  1 
ATOM   233  C C   . ILE   A 1 32  ? -26.850 -26.825 10.691  1.00 44.69  ? 31  ILE   A C   1 
ATOM   234  O O   . ILE   A 1 32  ? -27.512 -26.624 11.699  1.00 44.40  ? 31  ILE   A O   1 
ATOM   235  C CB  . ILE   A 1 32  ? -27.551 -25.881 8.425   1.00 41.23  ? 31  ILE   A CB  1 
ATOM   236  C CG1 . ILE   A 1 32  ? -27.452 -24.643 7.517   1.00 43.56  ? 31  ILE   A CG1 1 
ATOM   237  C CG2 . ILE   A 1 32  ? -28.999 -26.146 8.828   1.00 44.55  ? 31  ILE   A CG2 1 
ATOM   238  C CD1 . ILE   A 1 32  ? -27.997 -24.857 6.116   1.00 47.94  ? 31  ILE   A CD1 1 
ATOM   239  N N   . LEU   A 1 33  ? -26.253 -27.986 10.463  1.00 41.01  ? 32  LEU   A N   1 
ATOM   240  C CA  . LEU   A 1 33  ? -26.518 -29.135 11.323  1.00 41.31  ? 32  LEU   A CA  1 
ATOM   241  C C   . LEU   A 1 33  ? -26.022 -28.952 12.758  1.00 40.85  ? 32  LEU   A C   1 
ATOM   242  O O   . LEU   A 1 33  ? -26.627 -29.467 13.692  1.00 42.07  ? 32  LEU   A O   1 
ATOM   243  C CB  . LEU   A 1 33  ? -25.902 -30.376 10.704  1.00 44.60  ? 32  LEU   A CB  1 
ATOM   244  C CG  . LEU   A 1 33  ? -26.863 -31.324 10.004  1.00 48.45  ? 32  LEU   A CG  1 
ATOM   245  C CD1 . LEU   A 1 33  ? -26.048 -32.570 9.610   1.00 50.29  ? 32  LEU   A CD1 1 
ATOM   246  C CD2 . LEU   A 1 33  ? -28.006 -31.685 10.935  1.00 50.73  ? 32  LEU   A CD2 1 
ATOM   247  N N   . THR   A 1 34  ? -24.913 -28.248 12.952  1.00 37.14  ? 33  THR   A N   1 
ATOM   248  C CA  . THR   A 1 34  ? -24.376 -28.054 14.286  1.00 38.50  ? 33  THR   A CA  1 
ATOM   249  C C   . THR   A 1 34  ? -24.748 -26.674 14.827  1.00 39.44  ? 33  THR   A C   1 
ATOM   250  O O   . THR   A 1 34  ? -24.641 -26.462 16.021  1.00 40.81  ? 33  THR   A O   1 
ATOM   251  C CB  . THR   A 1 34  ? -22.857 -28.233 14.310  1.00 39.66  ? 33  THR   A CB  1 
ATOM   252  O OG1 . THR   A 1 34  ? -22.286 -27.318 13.378  1.00 34.42  ? 33  THR   A OG1 1 
ATOM   253  C CG2 . THR   A 1 34  ? -22.428 -29.630 13.906  1.00 43.36  ? 33  THR   A CG2 1 
ATOM   254  N N   . GLY   A 1 35  ? -25.079 -25.721 13.950  1.00 41.19  ? 34  GLY   A N   1 
ATOM   255  C CA  . GLY   A 1 35  ? -25.180 -24.314 14.316  1.00 45.80  ? 34  GLY   A CA  1 
ATOM   256  C C   . GLY   A 1 35  ? -23.816 -23.675 14.587  1.00 45.66  ? 34  GLY   A C   1 
ATOM   257  O O   . GLY   A 1 35  ? -23.735 -22.584 15.123  1.00 50.80  ? 34  GLY   A O   1 
ATOM   258  N N   . GLU   A 1 36  ? -22.712 -24.326 14.219  1.00 43.48  ? 35  GLU   A N   1 
ATOM   259  C CA  . GLU   A 1 36  ? -21.405 -23.747 14.487  1.00 42.79  ? 35  GLU   A CA  1 
ATOM   260  C C   . GLU   A 1 36  ? -20.996 -22.771 13.384  1.00 38.20  ? 35  GLU   A C   1 
ATOM   261  O O   . GLU   A 1 36  ? -21.257 -23.000 12.208  1.00 37.26  ? 35  GLU   A O   1 
ATOM   262  C CB  . GLU   A 1 36  ? -20.355 -24.838 14.660  1.00 43.34  ? 35  GLU   A CB  1 
ATOM   263  C CG  . GLU   A 1 36  ? -20.548 -25.638 15.941  1.00 50.28  ? 35  GLU   A CG  1 
ATOM   264  C CD  . GLU   A 1 36  ? -20.145 -24.926 17.220  1.00 57.34  ? 35  GLU   A CD  1 
ATOM   265  O OE1 . GLU   A 1 36  ? -18.941 -24.665 17.398  1.00 64.97  ? 35  GLU   A OE1 1 
ATOM   266  O OE2 . GLU   A 1 36  ? -21.028 -24.661 18.050  1.00 67.40  ? 35  GLU   A OE2 1 
ATOM   267  N N   . MET   A 1 37  ? -20.354 -21.677 13.800  1.00 39.55  ? 36  MET   A N   1 
ATOM   268  C CA  . MET   A 1 37  ? -19.798 -20.704 12.878  1.00 39.74  ? 36  MET   A CA  1 
ATOM   269  C C   . MET   A 1 37  ? -18.509 -21.286 12.287  1.00 36.92  ? 36  MET   A C   1 
ATOM   270  O O   . MET   A 1 37  ? -17.762 -21.950 12.975  1.00 39.42  ? 36  MET   A O   1 
ATOM   271  C CB  . MET   A 1 37  ? -19.464 -19.386 13.591  1.00 40.73  ? 36  MET   A CB  1 
ATOM   272  C CG  . MET   A 1 37  ? -20.685 -18.575 14.072  1.00 44.35  ? 36  MET   A CG  1 
ATOM   273  S SD  . MET   A 1 37  ? -21.974 -18.355 12.822  1.00 51.14  ? 36  MET   A SD  1 
ATOM   274  C CE  . MET   A 1 37  ? -21.035 -17.362 11.654  1.00 48.55  ? 36  MET   A CE  1 
ATOM   275  N N   . VAL   A 1 38  ? -18.300 -21.071 10.993  1.00 37.96  ? 37  VAL   A N   1 
ATOM   276  C CA  . VAL   A 1 38  ? -17.073 -21.417 10.301  1.00 36.35  ? 37  VAL   A CA  1 
ATOM   277  C C   . VAL   A 1 38  ? -16.647 -20.240 9.430   1.00 42.52  ? 37  VAL   A C   1 
ATOM   278  O O   . VAL   A 1 38  ? -17.422 -19.310 9.231   1.00 39.64  ? 37  VAL   A O   1 
ATOM   279  C CB  . VAL   A 1 38  ? -17.344 -22.648 9.425   1.00 33.50  ? 37  VAL   A CB  1 
ATOM   280  C CG1 . VAL   A 1 38  ? -17.750 -23.882 10.241  1.00 33.16  ? 37  VAL   A CG1 1 
ATOM   281  C CG2 . VAL   A 1 38  ? -18.398 -22.369 8.375   1.00 34.75  ? 37  VAL   A CG2 1 
ATOM   282  N N   . ALA   A 1 39  ? -15.447 -20.345 8.857   1.00 37.21  ? 38  ALA   A N   1 
ATOM   283  C CA  . ALA   A 1 39  ? -14.977 -19.440 7.821   1.00 35.64  ? 38  ALA   A CA  1 
ATOM   284  C C   . ALA   A 1 39  ? -14.889 -20.201 6.510   1.00 39.67  ? 38  ALA   A C   1 
ATOM   285  O O   . ALA   A 1 39  ? -14.358 -21.295 6.473   1.00 43.04  ? 38  ALA   A O   1 
ATOM   286  C CB  . ALA   A 1 39  ? -13.628 -18.899 8.189   1.00 39.55  ? 38  ALA   A CB  1 
ATOM   287  N N   . ILE   A 1 40  ? -15.401 -19.626 5.430   1.00 36.92  ? 39  ILE   A N   1 
ATOM   288  C CA  . ILE   A 1 40  ? -15.343 -20.286 4.148   1.00 35.51  ? 39  ILE   A CA  1 
ATOM   289  C C   . ILE   A 1 40  ? -14.541 -19.427 3.182   1.00 39.68  ? 39  ILE   A C   1 
ATOM   290  O O   . ILE   A 1 40  ? -14.905 -18.273 2.920   1.00 38.16  ? 39  ILE   A O   1 
ATOM   291  C CB  . ILE   A 1 40  ? -16.746 -20.557 3.632   1.00 35.90  ? 39  ILE   A CB  1 
ATOM   292  C CG1 . ILE   A 1 40  ? -17.615 -21.241 4.717   1.00 36.10  ? 39  ILE   A CG1 1 
ATOM   293  C CG2 . ILE   A 1 40  ? -16.654 -21.331 2.316   1.00 38.07  ? 39  ILE   A CG2 1 
ATOM   294  C CD1 . ILE   A 1 40  ? -18.912 -21.809 4.181   1.00 38.62  ? 39  ILE   A CD1 1 
ATOM   295  N N   . LYS   A 1 41  ? -13.447 -20.027 2.705   1.00 38.64  ? 40  LYS   A N   1 
ATOM   296  C CA  . LYS   A 1 41  ? -12.587 -19.484 1.669   1.00 44.16  ? 40  LYS   A CA  1 
ATOM   297  C C   . LYS   A 1 41  ? -13.126 -19.988 0.346   1.00 43.62  ? 40  LYS   A C   1 
ATOM   298  O O   . LYS   A 1 41  ? -13.280 -21.208 0.148   1.00 41.80  ? 40  LYS   A O   1 
ATOM   299  C CB  . LYS   A 1 41  ? -11.139 -19.900 1.945   1.00 47.40  ? 40  LYS   A CB  1 
ATOM   300  C CG  . LYS   A 1 41  ? -10.117 -19.420 0.940   1.00 60.65  ? 40  LYS   A CG  1 
ATOM   301  C CD  . LYS   A 1 41  ? -8.707  -19.445 1.510   1.00 68.94  ? 40  LYS   A CD  1 
ATOM   302  C CE  . LYS   A 1 41  ? -7.629  -19.258 0.492   1.00 85.30  ? 40  LYS   A CE  1 
ATOM   303  N NZ  . LYS   A 1 41  ? -6.416  -18.902 1.228   1.00 97.32  ? 40  LYS   A NZ  1 
ATOM   304  N N   . ILE   A 1 42  ? -13.555 -19.026 -0.483  1.00 43.57  ? 41  ILE   A N   1 
ATOM   305  C CA  . ILE   A 1 42  ? -14.139 -19.293 -1.787  1.00 42.31  ? 41  ILE   A CA  1 
ATOM   306  C C   . ILE   A 1 42  ? -13.122 -18.913 -2.863  1.00 47.93  ? 41  ILE   A C   1 
ATOM   307  O O   . ILE   A 1 42  ? -12.757 -17.745 -2.946  1.00 46.83  ? 41  ILE   A O   1 
ATOM   308  C CB  . ILE   A 1 42  ? -15.439 -18.499 -1.961  1.00 45.72  ? 41  ILE   A CB  1 
ATOM   309  C CG1 . ILE   A 1 42  ? -16.405 -18.733 -0.789  1.00 51.78  ? 41  ILE   A CG1 1 
ATOM   310  C CG2 . ILE   A 1 42  ? -16.081 -18.830 -3.308  1.00 50.75  ? 41  ILE   A CG2 1 
ATOM   311  C CD1 . ILE   A 1 42  ? -17.425 -17.631 -0.597  1.00 61.96  ? 41  ILE   A CD1 1 
ATOM   312  N N   . MET   A 1 43  ? -12.744 -19.884 -3.702  1.00 52.43  ? 42  MET   A N   1 
ATOM   313  C CA  . MET   A 1 43  ? -11.748 -19.707 -4.752  1.00 55.84  ? 42  MET   A CA  1 
ATOM   314  C C   . MET   A 1 43  ? -12.347 -20.002 -6.125  1.00 59.29  ? 42  MET   A C   1 
ATOM   315  O O   . MET   A 1 43  ? -13.024 -21.006 -6.309  1.00 52.49  ? 42  MET   A O   1 
ATOM   316  C CB  . MET   A 1 43  ? -10.558 -20.634 -4.523  1.00 56.92  ? 42  MET   A CB  1 
ATOM   317  C CG  . MET   A 1 43  ? -9.659  -20.171 -3.400  1.00 63.05  ? 42  MET   A CG  1 
ATOM   318  S SD  . MET   A 1 43  ? -8.428  -21.397 -2.928  1.00 70.15  ? 42  MET   A SD  1 
ATOM   319  C CE  . MET   A 1 43  ? -9.532  -22.797 -2.705  1.00 70.48  ? 42  MET   A CE  1 
ATOM   320  N N   . ASP   A 1 44  ? -12.108 -19.107 -7.098  1.00 64.87  ? 43  ASP   A N   1 
ATOM   321  C CA  . ASP   A 1 44  ? -12.633 -19.311 -8.439  1.00 65.18  ? 43  ASP   A CA  1 
ATOM   322  C C   . ASP   A 1 44  ? -11.589 -20.054 -9.269  1.00 62.87  ? 43  ASP   A C   1 
ATOM   323  O O   . ASP   A 1 44  ? -10.436 -19.627 -9.332  1.00 57.79  ? 43  ASP   A O   1 
ATOM   324  C CB  . ASP   A 1 44  ? -13.060 -18.017 -9.118  1.00 69.23  ? 43  ASP   A CB  1 
ATOM   325  C CG  . ASP   A 1 44  ? -13.706 -18.256 -10.474 1.00 72.12  ? 43  ASP   A CG  1 
ATOM   326  O OD1 . ASP   A 1 44  ? -12.953 -18.515 -11.429 1.00 76.56  ? 43  ASP   A OD1 1 
ATOM   327  O OD2 . ASP   A 1 44  ? -14.952 -18.298 -10.538 1.00 69.02  ? 43  ASP   A OD2 1 
ATOM   328  N N   . LYS   A 1 45  ? -12.014 -21.149 -9.911  1.00 61.16  ? 44  LYS   A N   1 
ATOM   329  C CA  . LYS   A 1 45  ? -11.089 -22.016 -10.628 1.00 64.51  ? 44  LYS   A CA  1 
ATOM   330  C C   . LYS   A 1 45  ? -10.567 -21.317 -11.883 1.00 62.88  ? 44  LYS   A C   1 
ATOM   331  O O   . LYS   A 1 45  ? -9.417  -21.512 -12.263 1.00 53.93  ? 44  LYS   A O   1 
ATOM   332  C CB  . LYS   A 1 45  ? -11.725 -23.379 -10.906 1.00 59.99  ? 44  LYS   A CB  1 
ATOM   333  C CG  . LYS   A 1 45  ? -11.854 -24.232 -9.659  1.00 52.42  ? 44  LYS   A CG  1 
ATOM   334  C CD  . LYS   A 1 45  ? -12.166 -25.695 -9.891  1.00 50.98  ? 44  LYS   A CD  1 
ATOM   335  C CE  . LYS   A 1 45  ? -13.593 -25.929 -10.197 1.00 53.89  ? 44  LYS   A CE  1 
ATOM   336  N NZ  . LYS   A 1 45  ? -13.793 -27.323 -10.562 1.00 53.16  ? 44  LYS   A NZ  1 
ATOM   337  N N   . ASN   A 1 46  ? -11.389 -20.448 -12.474 1.00 64.27  ? 45  ASN   A N   1 
ATOM   338  C CA  . ASN   A 1 46  ? -11.047 -19.784 -13.728 1.00 67.10  ? 45  ASN   A CA  1 
ATOM   339  C C   . ASN   A 1 46  ? -9.911  -18.806 -13.479 1.00 66.87  ? 45  ASN   A C   1 
ATOM   340  O O   . ASN   A 1 46  ? -8.937  -18.805 -14.216 1.00 74.04  ? 45  ASN   A O   1 
ATOM   341  C CB  . ASN   A 1 46  ? -12.279 -19.160 -14.371 1.00 68.06  ? 45  ASN   A CB  1 
ATOM   342  C CG  . ASN   A 1 46  ? -13.378 -20.194 -14.451 1.00 69.92  ? 45  ASN   A CG  1 
ATOM   343  O OD1 . ASN   A 1 46  ? -14.378 -20.113 -13.723 1.00 81.15  ? 45  ASN   A OD1 1 
ATOM   344  N ND2 . ASN   A 1 46  ? -13.144 -21.239 -15.230 1.00 68.94  ? 45  ASN   A ND2 1 
ATOM   345  N N   . THR   A 1 47  ? -10.030 -18.036 -12.393 1.00 64.56  ? 46  THR   A N   1 
ATOM   346  C CA  . THR   A 1 47  ? -9.002  -17.122 -11.916 1.00 57.69  ? 46  THR   A CA  1 
ATOM   347  C C   . THR   A 1 47  ? -7.700  -17.857 -11.608 1.00 64.50  ? 46  THR   A C   1 
ATOM   348  O O   . THR   A 1 47  ? -6.607  -17.368 -11.867 1.00 67.20  ? 46  THR   A O   1 
ATOM   349  C CB  . THR   A 1 47  ? -9.563  -16.473 -10.652 1.00 62.90  ? 46  THR   A CB  1 
ATOM   350  O OG1 . THR   A 1 47  ? -10.911 -16.117 -10.970 1.00 62.04  ? 46  THR   A OG1 1 
ATOM   351  C CG2 . THR   A 1 47  ? -8.713  -15.317 -10.162 1.00 59.90  ? 46  THR   A CG2 1 
ATOM   352  N N   . LEU   A 1 48  ? -7.810  -19.017 -10.969 1.00 65.27  ? 47  LEU   A N   1 
ATOM   353  C CA  . LEU   A 1 48  ? -6.623  -19.766 -10.632 1.00 61.46  ? 47  LEU   A CA  1 
ATOM   354  C C   . LEU   A 1 48  ? -5.994  -20.205 -11.944 1.00 55.46  ? 47  LEU   A C   1 
ATOM   355  O O   . LEU   A 1 48  ? -4.816  -20.001 -12.151 1.00 65.91  ? 47  LEU   A O   1 
ATOM   356  C CB  . LEU   A 1 48  ? -6.995  -20.938 -9.721  1.00 61.26  ? 47  LEU   A CB  1 
ATOM   357  C CG  . LEU   A 1 48  ? -7.476  -20.557 -8.310  1.00 58.12  ? 47  LEU   A CG  1 
ATOM   358  C CD1 . LEU   A 1 48  ? -7.992  -21.755 -7.563  1.00 53.62  ? 47  LEU   A CD1 1 
ATOM   359  C CD2 . LEU   A 1 48  ? -6.350  -19.906 -7.540  1.00 56.75  ? 47  LEU   A CD2 1 
ATOM   360  N N   . GLY   A 1 49  ? -6.805  -20.803 -12.810 1.00 59.59  ? 48  GLY   A N   1 
ATOM   361  C CA  . GLY   A 1 49  ? -6.338  -21.334 -14.078 1.00 57.48  ? 48  GLY   A CA  1 
ATOM   362  C C   . GLY   A 1 49  ? -5.171  -22.295 -13.875 1.00 58.74  ? 48  GLY   A C   1 
ATOM   363  O O   . GLY   A 1 49  ? -5.310  -23.319 -13.223 1.00 67.98  ? 48  GLY   A O   1 
ATOM   364  N N   . SER   A 1 50  ? -4.015  -21.895 -14.402 1.00 57.59  ? 49  SER   A N   1 
ATOM   365  C CA  . SER   A 1 50  ? -2.776  -22.664 -14.408 1.00 62.89  ? 49  SER   A CA  1 
ATOM   366  C C   . SER   A 1 50  ? -2.276  -23.039 -13.008 1.00 58.97  ? 49  SER   A C   1 
ATOM   367  O O   . SER   A 1 50  ? -1.548  -24.020 -12.855 1.00 60.14  ? 49  SER   A O   1 
ATOM   368  C CB  . SER   A 1 50  ? -1.706  -21.863 -15.137 1.00 63.33  ? 49  SER   A CB  1 
ATOM   369  O OG  . SER   A 1 50  ? -1.653  -20.529 -14.624 1.00 69.87  ? 49  SER   A OG  1 
ATOM   370  N N   . ASP   A 1 51  ? -2.612  -22.241 -11.986 1.00 64.82  ? 50  ASP   A N   1 
ATOM   371  C CA  . ASP   A 1 51  ? -2.172  -22.509 -10.615 1.00 69.55  ? 50  ASP   A CA  1 
ATOM   372  C C   . ASP   A 1 51  ? -3.102  -23.473 -9.860  1.00 67.02  ? 50  ASP   A C   1 
ATOM   373  O O   . ASP   A 1 51  ? -2.789  -23.881 -8.736  1.00 60.99  ? 50  ASP   A O   1 
ATOM   374  C CB  . ASP   A 1 51  ? -2.071  -21.227 -9.813  1.00 67.82  ? 50  ASP   A CB  1 
ATOM   375  C CG  . ASP   A 1 51  ? -1.298  -20.109 -10.489 1.00 72.05  ? 50  ASP   A CG  1 
ATOM   376  O OD1 . ASP   A 1 51  ? -1.817  -19.543 -11.474 1.00 85.06  ? 50  ASP   A OD1 1 
ATOM   377  O OD2 . ASP   A 1 51  ? -0.200  -19.812 -9.997  1.00 68.97  ? 50  ASP   A OD2 1 
ATOM   378  N N   . LEU   A 1 52  ? -4.221  -23.878 -10.478 1.00 62.60  ? 51  LEU   A N   1 
ATOM   379  C CA  . LEU   A 1 52  ? -5.185  -24.744 -9.817  1.00 62.06  ? 51  LEU   A CA  1 
ATOM   380  C C   . LEU   A 1 52  ? -4.505  -25.994 -9.241  1.00 69.76  ? 51  LEU   A C   1 
ATOM   381  O O   . LEU   A 1 52  ? -4.820  -26.402 -8.122  1.00 64.44  ? 51  LEU   A O   1 
ATOM   382  C CB  . LEU   A 1 52  ? -6.352  -25.093 -10.741 1.00 56.97  ? 51  LEU   A CB  1 
ATOM   383  C CG  . LEU   A 1 52  ? -7.398  -26.039 -10.143 1.00 56.23  ? 51  LEU   A CG  1 
ATOM   384  C CD1 . LEU   A 1 52  ? -8.060  -25.411 -8.913  1.00 61.44  ? 51  LEU   A CD1 1 
ATOM   385  C CD2 . LEU   A 1 52  ? -8.448  -26.437 -11.148 1.00 55.18  ? 51  LEU   A CD2 1 
ATOM   386  N N   . PRO   A 1 53  ? -3.559  -26.664 -9.947  1.00 69.65  ? 52  PRO   A N   1 
ATOM   387  C CA  . PRO   A 1 53  ? -2.896  -27.847 -9.392  1.00 64.98  ? 52  PRO   A CA  1 
ATOM   388  C C   . PRO   A 1 53  ? -2.117  -27.550 -8.119  1.00 63.18  ? 52  PRO   A C   1 
ATOM   389  O O   . PRO   A 1 53  ? -2.074  -28.373 -7.215  1.00 60.35  ? 52  PRO   A O   1 
ATOM   390  C CB  . PRO   A 1 53  ? -1.968  -28.290 -10.513 1.00 63.80  ? 52  PRO   A CB  1 
ATOM   391  C CG  . PRO   A 1 53  ? -2.611  -27.715 -11.736 1.00 63.98  ? 52  PRO   A CG  1 
ATOM   392  C CD  . PRO   A 1 53  ? -3.094  -26.356 -11.305 1.00 65.22  ? 52  PRO   A CD  1 
ATOM   393  N N   . ARG   A 1 54  ? -1.522  -26.360 -8.053  1.00 64.74  ? 53  ARG   A N   1 
ATOM   394  C CA  . ARG   A 1 54  ? -0.754  -25.963 -6.886  1.00 70.95  ? 53  ARG   A CA  1 
ATOM   395  C C   . ARG   A 1 54  ? -1.684  -25.862 -5.674  1.00 64.49  ? 53  ARG   A C   1 
ATOM   396  O O   . ARG   A 1 54  ? -1.328  -26.312 -4.587  1.00 66.15  ? 53  ARG   A O   1 
ATOM   397  C CB  . ARG   A 1 54  ? -0.040  -24.622 -7.110  1.00 78.85  ? 53  ARG   A CB  1 
ATOM   398  C CG  . ARG   A 1 54  ? 1.373   -24.557 -6.545  1.00 83.77  ? 53  ARG   A CG  1 
ATOM   399  C CD  . ARG   A 1 54  ? 1.877   -23.115 -6.454  1.00 88.55  ? 53  ARG   A CD  1 
ATOM   400  N NE  . ARG   A 1 54  ? 1.236   -22.439 -5.316  1.00 95.40  ? 53  ARG   A NE  1 
ATOM   401  C CZ  . ARG   A 1 54  ? 0.493   -21.337 -5.344  1.00 87.11  ? 53  ARG   A CZ  1 
ATOM   402  N NH1 . ARG   A 1 54  ? 0.334   -20.674 -6.472  1.00 78.62  ? 53  ARG   A NH1 1 
ATOM   403  N NH2 . ARG   A 1 54  ? -0.078  -20.894 -4.229  1.00 85.53  ? 53  ARG   A NH2 1 
ATOM   404  N N   . ILE   A 1 55  ? -2.860  -25.251 -5.869  1.00 53.66  ? 54  ILE   A N   1 
ATOM   405  C CA  . ILE   A 1 55  ? -3.822  -25.074 -4.792  1.00 57.59  ? 54  ILE   A CA  1 
ATOM   406  C C   . ILE   A 1 55  ? -4.309  -26.443 -4.288  1.00 52.47  ? 54  ILE   A C   1 
ATOM   407  O O   . ILE   A 1 55  ? -4.413  -26.652 -3.091  1.00 55.08  ? 54  ILE   A O   1 
ATOM   408  C CB  . ILE   A 1 55  ? -4.970  -24.150 -5.245  1.00 61.86  ? 54  ILE   A CB  1 
ATOM   409  C CG1 . ILE   A 1 55  ? -4.580  -22.687 -5.080  1.00 67.67  ? 54  ILE   A CG1 1 
ATOM   410  C CG2 . ILE   A 1 55  ? -6.282  -24.443 -4.510  1.00 63.29  ? 54  ILE   A CG2 1 
ATOM   411  C CD1 . ILE   A 1 55  ? -3.216  -22.336 -5.642  1.00 66.81  ? 54  ILE   A CD1 1 
ATOM   412  N N   . LYS   A 1 56  ? -4.590  -27.379 -5.195  1.00 45.16  ? 55  LYS   A N   1 
ATOM   413  C CA  . LYS   A 1 56  ? -5.031  -28.701 -4.809  1.00 51.60  ? 55  LYS   A CA  1 
ATOM   414  C C   . LYS   A 1 56  ? -3.994  -29.369 -3.924  1.00 58.29  ? 55  LYS   A C   1 
ATOM   415  O O   . LYS   A 1 56  ? -4.339  -29.937 -2.899  1.00 63.08  ? 55  LYS   A O   1 
ATOM   416  C CB  . LYS   A 1 56  ? -5.362  -29.481 -6.074  1.00 51.74  ? 55  LYS   A CB  1 
ATOM   417  C CG  . LYS   A 1 56  ? -6.609  -28.934 -6.725  1.00 55.46  ? 55  LYS   A CG  1 
ATOM   418  C CD  . LYS   A 1 56  ? -7.287  -29.883 -7.694  1.00 60.74  ? 55  LYS   A CD  1 
ATOM   419  C CE  . LYS   A 1 56  ? -8.746  -29.584 -7.863  1.00 74.81  ? 55  LYS   A CE  1 
ATOM   420  N NZ  . LYS   A 1 56  ? -9.423  -30.606 -8.676  1.00 81.83  ? 55  LYS   A NZ  1 
ATOM   421  N N   . THR   A 1 57  ? -2.729  -29.276 -4.328  1.00 63.39  ? 56  THR   A N   1 
ATOM   422  C CA  . THR   A 1 57  ? -1.599  -29.739 -3.535  1.00 65.97  ? 56  THR   A CA  1 
ATOM   423  C C   . THR   A 1 57  ? -1.606  -29.098 -2.144  1.00 72.66  ? 56  THR   A C   1 
ATOM   424  O O   . THR   A 1 57  ? -1.530  -29.815 -1.147  1.00 77.94  ? 56  THR   A O   1 
ATOM   425  C CB  . THR   A 1 57  ? -0.298  -29.443 -4.292  1.00 69.45  ? 56  THR   A CB  1 
ATOM   426  O OG1 . THR   A 1 57  ? -0.311  -30.406 -5.336  1.00 59.31  ? 56  THR   A OG1 1 
ATOM   427  C CG2 . THR   A 1 57  ? 0.959   -29.634 -3.463  1.00 73.89  ? 56  THR   A CG2 1 
ATOM   428  N N   . GLU   A 1 58  ? -1.669  -27.758 -2.070  1.00 66.87  ? 57  GLU   A N   1 
ATOM   429  C CA  . GLU   A 1 58  ? -1.706  -27.062 -0.787  1.00 69.43  ? 57  GLU   A CA  1 
ATOM   430  C C   . GLU   A 1 58  ? -2.942  -27.464 0.041   1.00 55.88  ? 57  GLU   A C   1 
ATOM   431  O O   . GLU   A 1 58  ? -2.881  -27.466 1.267   1.00 52.19  ? 57  GLU   A O   1 
ATOM   432  C CB  . GLU   A 1 58  ? -1.703  -25.543 -0.964  1.00 68.79  ? 57  GLU   A CB  1 
ATOM   433  C CG  . GLU   A 1 58  ? -0.427  -24.991 -1.594  1.00 80.82  ? 57  GLU   A CG  1 
ATOM   434  C CD  . GLU   A 1 58  ? -0.545  -23.496 -1.836  1.00 90.27  ? 57  GLU   A CD  1 
ATOM   435  O OE1 . GLU   A 1 58  ? -1.597  -23.086 -2.366  1.00 91.04  ? 57  GLU   A OE1 1 
ATOM   436  O OE2 . GLU   A 1 58  ? 0.392   -22.740 -1.498  1.00 101.40 ? 57  GLU   A OE2 1 
ATOM   437  N N   . ILE   A 1 59  ? -4.064  -27.777 -0.620  1.00 46.48  ? 58  ILE   A N   1 
ATOM   438  C CA  . ILE   A 1 59  ? -5.244  -28.244 0.096   1.00 46.25  ? 58  ILE   A CA  1 
ATOM   439  C C   . ILE   A 1 59  ? -4.890  -29.559 0.787   1.00 54.03  ? 58  ILE   A C   1 
ATOM   440  O O   . ILE   A 1 59  ? -5.180  -29.720 1.964   1.00 45.48  ? 58  ILE   A O   1 
ATOM   441  C CB  . ILE   A 1 59  ? -6.492  -28.328 -0.800  1.00 46.75  ? 58  ILE   A CB  1 
ATOM   442  C CG1 . ILE   A 1 59  ? -7.006  -26.920 -1.121  1.00 46.83  ? 58  ILE   A CG1 1 
ATOM   443  C CG2 . ILE   A 1 59  ? -7.595  -29.180 -0.151  1.00 49.55  ? 58  ILE   A CG2 1 
ATOM   444  C CD1 . ILE   A 1 59  ? -8.109  -26.888 -2.156  1.00 49.07  ? 58  ILE   A CD1 1 
ATOM   445  N N   . GLU   A 1 60  ? -4.179  -30.451 0.080   1.00 55.55  ? 59  GLU   A N   1 
ATOM   446  C CA  . GLU   A 1 60  ? -3.832  -31.757 0.623   1.00 54.50  ? 59  GLU   A CA  1 
ATOM   447  C C   . GLU   A 1 60  ? -2.863  -31.614 1.788   1.00 49.39  ? 59  GLU   A C   1 
ATOM   448  O O   . GLU   A 1 60  ? -3.010  -32.299 2.790   1.00 58.59  ? 59  GLU   A O   1 
ATOM   449  C CB  . GLU   A 1 60  ? -3.276  -32.616 -0.502  1.00 55.38  ? 59  GLU   A CB  1 
ATOM   450  C CG  . GLU   A 1 60  ? -4.356  -32.930 -1.533  1.00 55.81  ? 59  GLU   A CG  1 
ATOM   451  C CD  . GLU   A 1 60  ? -5.490  -33.759 -0.958  1.00 59.08  ? 59  GLU   A CD  1 
ATOM   452  O OE1 . GLU   A 1 60  ? -5.205  -34.735 -0.228  1.00 62.80  ? 59  GLU   A OE1 1 
ATOM   453  O OE2 . GLU   A 1 60  ? -6.654  -33.434 -1.244  1.00 57.50  ? 59  GLU   A OE2 1 
ATOM   454  N N   . ALA   A 1 61  ? -1.921  -30.679 1.684   1.00 48.52  ? 60  ALA   A N   1 
ATOM   455  C CA  . ALA   A 1 61  ? -1.009  -30.392 2.782   1.00 53.51  ? 60  ALA   A CA  1 
ATOM   456  C C   . ALA   A 1 61  ? -1.792  -29.995 4.039   1.00 58.41  ? 60  ALA   A C   1 
ATOM   457  O O   . ALA   A 1 61  ? -1.455  -30.408 5.157   1.00 54.04  ? 60  ALA   A O   1 
ATOM   458  C CB  . ALA   A 1 61  ? -0.031  -29.303 2.393   1.00 53.22  ? 60  ALA   A CB  1 
ATOM   459  N N   . LEU   A 1 62  ? -2.849  -29.194 3.841   1.00 49.23  ? 61  LEU   A N   1 
ATOM   460  C CA  . LEU   A 1 62  ? -3.611  -28.662 4.957   1.00 48.26  ? 61  LEU   A CA  1 
ATOM   461  C C   . LEU   A 1 62  ? -4.463  -29.757 5.619   1.00 46.47  ? 61  LEU   A C   1 
ATOM   462  O O   . LEU   A 1 62  ? -4.691  -29.718 6.822   1.00 46.10  ? 61  LEU   A O   1 
ATOM   463  C CB  . LEU   A 1 62  ? -4.443  -27.507 4.418   1.00 45.23  ? 61  LEU   A CB  1 
ATOM   464  C CG  . LEU   A 1 62  ? -5.261  -26.735 5.446   1.00 47.59  ? 61  LEU   A CG  1 
ATOM   465  C CD1 . LEU   A 1 62  ? -4.452  -26.146 6.616   1.00 52.83  ? 61  LEU   A CD1 1 
ATOM   466  C CD2 . LEU   A 1 62  ? -5.998  -25.666 4.689   1.00 54.21  ? 61  LEU   A CD2 1 
ATOM   467  N N   . LYS   A 1 63  ? -4.905  -30.755 4.853   1.00 48.24  ? 62  LYS   A N   1 
ATOM   468  C CA  . LYS   A 1 63  ? -5.547  -31.923 5.439   1.00 52.67  ? 62  LYS   A CA  1 
ATOM   469  C C   . LYS   A 1 63  ? -4.658  -32.672 6.430   1.00 54.86  ? 62  LYS   A C   1 
ATOM   470  O O   . LYS   A 1 63  ? -5.202  -33.288 7.335   1.00 57.75  ? 62  LYS   A O   1 
ATOM   471  C CB  . LYS   A 1 63  ? -5.991  -32.934 4.389   1.00 45.99  ? 62  LYS   A CB  1 
ATOM   472  C CG  . LYS   A 1 63  ? -7.101  -32.413 3.540   1.00 41.40  ? 62  LYS   A CG  1 
ATOM   473  C CD  . LYS   A 1 63  ? -7.511  -33.415 2.469   1.00 45.40  ? 62  LYS   A CD  1 
ATOM   474  C CE  . LYS   A 1 63  ? -8.484  -32.810 1.529   1.00 46.77  ? 62  LYS   A CE  1 
ATOM   475  N NZ  . LYS   A 1 63  ? -8.919  -33.702 0.453   1.00 45.66  ? 62  LYS   A NZ  1 
ATOM   476  N N   . ASN   A 1 64  ? -3.326  -32.592 6.285   1.00 55.77  ? 63  ASN   A N   1 
ATOM   477  C CA  . ASN   A 1 64  ? -2.391  -33.213 7.218   1.00 53.34  ? 63  ASN   A CA  1 
ATOM   478  C C   . ASN   A 1 64  ? -1.857  -32.257 8.277   1.00 61.19  ? 63  ASN   A C   1 
ATOM   479  O O   . ASN   A 1 64  ? -0.886  -32.578 8.961   1.00 70.78  ? 63  ASN   A O   1 
ATOM   480  C CB  . ASN   A 1 64  ? -1.118  -33.703 6.538   1.00 67.47  ? 63  ASN   A CB  1 
ATOM   481  C CG  . ASN   A 1 64  ? -1.409  -34.677 5.425   1.00 69.61  ? 63  ASN   A CG  1 
ATOM   482  O OD1 . ASN   A 1 64  ? -2.271  -35.551 5.571   1.00 74.67  ? 63  ASN   A OD1 1 
ATOM   483  N ND2 . ASN   A 1 64  ? -0.729  -34.508 4.302   1.00 81.90  ? 63  ASN   A ND2 1 
ATOM   484  N N   . LEU   A 1 65  ? -2.444  -31.070 8.399   1.00 52.73  ? 64  LEU   A N   1 
ATOM   485  C CA  . LEU   A 1 65  ? -2.000  -30.115 9.398   1.00 54.16  ? 64  LEU   A CA  1 
ATOM   486  C C   . LEU   A 1 65  ? -3.052  -30.018 10.496  1.00 61.53  ? 64  LEU   A C   1 
ATOM   487  O O   . LEU   A 1 65  ? -3.662  -28.960 10.693  1.00 60.35  ? 64  LEU   A O   1 
ATOM   488  C CB  . LEU   A 1 65  ? -1.719  -28.752 8.777   1.00 58.33  ? 64  LEU   A CB  1 
ATOM   489  C CG  . LEU   A 1 65  ? -0.411  -28.627 7.998   1.00 57.88  ? 64  LEU   A CG  1 
ATOM   490  C CD1 . LEU   A 1 65  ? -0.136  -27.150 7.774   1.00 64.64  ? 64  LEU   A CD1 1 
ATOM   491  C CD2 . LEU   A 1 65  ? 0.742   -29.281 8.722   1.00 68.15  ? 64  LEU   A CD2 1 
ATOM   492  N N   . ARG   A 1 66  ? -3.223  -31.139 11.206  1.00 52.32  ? 65  ARG   A N   1 
ATOM   493  C CA  . ARG   A 1 66  ? -4.152  -31.232 12.314  1.00 52.09  ? 65  ARG   A CA  1 
ATOM   494  C C   . ARG   A 1 66  ? -3.373  -30.949 13.597  1.00 51.31  ? 65  ARG   A C   1 
ATOM   495  O O   . ARG   A 1 66  ? -2.540  -31.735 14.027  1.00 54.74  ? 65  ARG   A O   1 
ATOM   496  C CB  . ARG   A 1 66  ? -4.840  -32.603 12.255  1.00 59.15  ? 65  ARG   A CB  1 
ATOM   497  C CG  . ARG   A 1 66  ? -5.692  -32.831 11.009  1.00 70.45  ? 65  ARG   A CG  1 
ATOM   498  C CD  . ARG   A 1 66  ? -5.880  -34.328 10.708  1.00 79.85  ? 65  ARG   A CD  1 
ATOM   499  N NE  . ARG   A 1 66  ? -7.002  -34.666 9.820   1.00 100.70 ? 65  ARG   A NE  1 
ATOM   500  C CZ  . ARG   A 1 66  ? -8.018  -35.501 10.092  1.00 108.00 ? 65  ARG   A CZ  1 
ATOM   501  N NH1 . ARG   A 1 66  ? -8.125  -36.064 11.284  1.00 108.86 ? 65  ARG   A NH1 1 
ATOM   502  N NH2 . ARG   A 1 66  ? -8.938  -35.770 9.171   1.00 96.40  ? 65  ARG   A NH2 1 
ATOM   503  N N   . HIS   A 1 67  ? -3.643  -29.797 14.211  1.00 48.50  ? 66  HIS   A N   1 
ATOM   504  C CA  . HIS   A 1 67  ? -2.855  -29.350 15.346  1.00 44.31  ? 66  HIS   A CA  1 
ATOM   505  C C   . HIS   A 1 67  ? -3.651  -28.297 16.109  1.00 41.89  ? 66  HIS   A C   1 
ATOM   506  O O   . HIS   A 1 67  ? -4.403  -27.486 15.551  1.00 47.26  ? 66  HIS   A O   1 
ATOM   507  C CB  . HIS   A 1 67  ? -1.451  -28.941 14.872  1.00 44.43  ? 66  HIS   A CB  1 
ATOM   508  C CG  . HIS   A 1 67  ? -0.512  -28.436 15.914  1.00 40.60  ? 66  HIS   A CG  1 
ATOM   509  N ND1 . HIS   A 1 67  ? -0.694  -27.233 16.553  1.00 42.11  ? 66  HIS   A ND1 1 
ATOM   510  C CD2 . HIS   A 1 67  ? 0.622   -28.951 16.421  1.00 40.44  ? 66  HIS   A CD2 1 
ATOM   511  C CE1 . HIS   A 1 67  ? 0.310   -27.036 17.412  1.00 46.85  ? 66  HIS   A CE1 1 
ATOM   512  N NE2 . HIS   A 1 67  ? 1.131   -28.070 17.338  1.00 39.41  ? 66  HIS   A NE2 1 
ATOM   513  N N   . GLN   A 1 68  ? -3.447  -28.308 17.419  1.00 44.68  ? 67  GLN   A N   1 
ATOM   514  C CA  . GLN   A 1 68  ? -4.211  -27.475 18.333  1.00 51.78  ? 67  GLN   A CA  1 
ATOM   515  C C   . GLN   A 1 68  ? -3.977  -25.975 18.117  1.00 45.83  ? 67  GLN   A C   1 
ATOM   516  O O   . GLN   A 1 68  ? -4.802  -25.180 18.542  1.00 42.06  ? 67  GLN   A O   1 
ATOM   517  C CB  . GLN   A 1 68  ? -3.948  -27.942 19.771  1.00 56.24  ? 67  GLN   A CB  1 
ATOM   518  C CG  . GLN   A 1 68  ? -2.478  -28.071 20.177  1.00 66.57  ? 67  GLN   A CG  1 
ATOM   519  C CD  . GLN   A 1 68  ? -1.756  -29.321 19.691  1.00 66.54  ? 67  GLN   A CD  1 
ATOM   520  O OE1 . GLN   A 1 68  ? -2.309  -30.184 19.005  1.00 66.15  ? 67  GLN   A OE1 1 
ATOM   521  N NE2 . GLN   A 1 68  ? -0.475  -29.428 20.019  1.00 65.70  ? 67  GLN   A NE2 1 
ATOM   522  N N   . HIS   A 1 69  ? -2.867  -25.569 17.476  1.00 43.01  ? 68  HIS   A N   1 
ATOM   523  C CA  . HIS   A 1 69  ? -2.618  -24.147 17.244  1.00 45.54  ? 68  HIS   A CA  1 
ATOM   524  C C   . HIS   A 1 69  ? -2.646  -23.794 15.758  1.00 43.40  ? 68  HIS   A C   1 
ATOM   525  O O   . HIS   A 1 69  ? -2.134  -22.743 15.363  1.00 40.38  ? 68  HIS   A O   1 
ATOM   526  C CB  . HIS   A 1 69  ? -1.301  -23.675 17.873  1.00 38.99  ? 68  HIS   A CB  1 
ATOM   527  C CG  . HIS   A 1 69  ? -1.374  -23.707 19.350  1.00 41.75  ? 68  HIS   A CG  1 
ATOM   528  N ND1 . HIS   A 1 69  ? -2.352  -23.039 20.052  1.00 41.22  ? 68  HIS   A ND1 1 
ATOM   529  C CD2 . HIS   A 1 69  ? -0.665  -24.396 20.246  1.00 42.23  ? 68  HIS   A CD2 1 
ATOM   530  C CE1 . HIS   A 1 69  ? -2.218  -23.325 21.336  1.00 44.70  ? 68  HIS   A CE1 1 
ATOM   531  N NE2 . HIS   A 1 69  ? -1.168  -24.126 21.470  1.00 42.66  ? 68  HIS   A NE2 1 
ATOM   532  N N   . ILE   A 1 70  ? -3.237  -24.677 14.948  1.00 40.11  ? 69  ILE   A N   1 
ATOM   533  C CA  . ILE   A 1 70  ? -3.432  -24.429 13.540  1.00 39.48  ? 69  ILE   A CA  1 
ATOM   534  C C   . ILE   A 1 70  ? -4.916  -24.480 13.256  1.00 40.62  ? 69  ILE   A C   1 
ATOM   535  O O   . ILE   A 1 70  ? -5.585  -25.431 13.626  1.00 40.91  ? 69  ILE   A O   1 
ATOM   536  C CB  . ILE   A 1 70  ? -2.678  -25.450 12.680  1.00 40.43  ? 69  ILE   A CB  1 
ATOM   537  C CG1 . ILE   A 1 70  ? -1.203  -25.395 13.029  1.00 39.26  ? 69  ILE   A CG1 1 
ATOM   538  C CG2 . ILE   A 1 70  ? -2.961  -25.242 11.186  1.00 39.54  ? 69  ILE   A CG2 1 
ATOM   539  C CD1 . ILE   A 1 70  ? -0.328  -26.201 12.115  1.00 41.38  ? 69  ILE   A CD1 1 
ATOM   540  N N   . CYS   A 1 71  ? -5.379  -23.460 12.541  1.00 39.13  ? 70  CYS   A N   1 
ATOM   541  C CA  . CYS   A 1 71  ? -6.761  -23.334 12.135  1.00 44.12  ? 70  CYS   A CA  1 
ATOM   542  C C   . CYS   A 1 71  ? -7.111  -24.524 11.247  1.00 43.15  ? 70  CYS   A C   1 
ATOM   543  O O   . CYS   A 1 71  ? -6.417  -24.808 10.277  1.00 39.51  ? 70  CYS   A O   1 
ATOM   544  C CB  . CYS   A 1 71  ? -6.970  -21.964 11.496  1.00 47.93  ? 70  CYS   A CB  1 
ATOM   545  S SG  . CYS   A 1 71  ? -8.613  -21.802 10.771  1.00 58.66  ? 70  CYS   A SG  1 
ATOM   546  N N   . GLN   A 1 72  ? -8.149  -25.274 11.621  1.00 39.73  ? 71  GLN   A N   1 
ATOM   547  C CA  . GLN   A 1 72  ? -8.353  -26.575 11.014  1.00 40.73  ? 71  GLN   A CA  1 
ATOM   548  C C   . GLN   A 1 72  ? -9.286  -26.493 9.811   1.00 40.41  ? 71  GLN   A C   1 
ATOM   549  O O   . GLN   A 1 72  ? -10.245 -25.733 9.801   1.00 38.27  ? 71  GLN   A O   1 
ATOM   550  C CB  . GLN   A 1 72  ? -8.847  -27.616 12.016  1.00 48.89  ? 71  GLN   A CB  1 
ATOM   551  C CG  . GLN   A 1 72  ? -8.482  -29.020 11.539  1.00 68.43  ? 71  GLN   A CG  1 
ATOM   552  C CD  . GLN   A 1 72  ? -9.147  -30.140 12.302  1.00 72.88  ? 71  GLN   A CD  1 
ATOM   553  O OE1 . GLN   A 1 72  ? -9.869  -29.931 13.291  1.00 70.17  ? 71  GLN   A OE1 1 
ATOM   554  N NE2 . GLN   A 1 72  ? -8.933  -31.342 11.785  1.00 63.39  ? 71  GLN   A NE2 1 
ATOM   555  N N   . LEU   A 1 73  ? -8.973  -27.325 8.815   1.00 34.15  ? 72  LEU   A N   1 
ATOM   556  C CA  . LEU   A 1 73  ? -9.795  -27.518 7.646   1.00 36.29  ? 72  LEU   A CA  1 
ATOM   557  C C   . LEU   A 1 73  ? -10.882 -28.554 7.943   1.00 35.15  ? 72  LEU   A C   1 
ATOM   558  O O   . LEU   A 1 73  ? -10.594 -29.643 8.438   1.00 33.20  ? 72  LEU   A O   1 
ATOM   559  C CB  . LEU   A 1 73  ? -8.889  -27.970 6.504   1.00 35.87  ? 72  LEU   A CB  1 
ATOM   560  C CG  . LEU   A 1 73  ? -9.597  -28.300 5.184   1.00 37.53  ? 72  LEU   A CG  1 
ATOM   561  C CD1 . LEU   A 1 73  ? -10.278 -27.080 4.630   1.00 37.81  ? 72  LEU   A CD1 1 
ATOM   562  C CD2 . LEU   A 1 73  ? -8.612  -28.883 4.161   1.00 40.87  ? 72  LEU   A CD2 1 
ATOM   563  N N   . TYR   A 1 74  ? -12.115 -28.253 7.518   1.00 29.86  ? 73  TYR   A N   1 
ATOM   564  C CA  . TYR   A 1 74  ? -13.255 -29.107 7.816   1.00 33.78  ? 73  TYR   A CA  1 
ATOM   565  C C   . TYR   A 1 74  ? -13.860 -29.743 6.573   1.00 35.31  ? 73  TYR   A C   1 
ATOM   566  O O   . TYR   A 1 74  ? -14.415 -30.857 6.634   1.00 35.18  ? 73  TYR   A O   1 
ATOM   567  C CB  . TYR   A 1 74  ? -14.351 -28.316 8.511   1.00 32.71  ? 73  TYR   A CB  1 
ATOM   568  C CG  . TYR   A 1 74  ? -13.994 -27.795 9.890   1.00 36.94  ? 73  TYR   A CG  1 
ATOM   569  C CD1 . TYR   A 1 74  ? -13.130 -28.498 10.695  1.00 36.14  ? 73  TYR   A CD1 1 
ATOM   570  C CD2 . TYR   A 1 74  ? -14.547 -26.612 10.384  1.00 39.18  ? 73  TYR   A CD2 1 
ATOM   571  C CE1 . TYR   A 1 74  ? -12.857 -28.074 11.980  1.00 40.12  ? 73  TYR   A CE1 1 
ATOM   572  C CE2 . TYR   A 1 74  ? -14.284 -26.183 11.676  1.00 41.66  ? 73  TYR   A CE2 1 
ATOM   573  C CZ  . TYR   A 1 74  ? -13.437 -26.926 12.480  1.00 41.72  ? 73  TYR   A CZ  1 
ATOM   574  O OH  . TYR   A 1 74  ? -13.086 -26.608 13.769  1.00 37.54  ? 73  TYR   A OH  1 
ATOM   575  N N   . HIS   A 1 75  ? -13.785 -29.037 5.449   1.00 30.97  ? 74  HIS   A N   1 
ATOM   576  C CA  . HIS   A 1 75  ? -14.640 -29.400 4.330   1.00 33.37  ? 74  HIS   A CA  1 
ATOM   577  C C   . HIS   A 1 75  ? -14.036 -28.799 3.068   1.00 36.86  ? 74  HIS   A C   1 
ATOM   578  O O   . HIS   A 1 75  ? -13.685 -27.632 3.088   1.00 34.25  ? 74  HIS   A O   1 
ATOM   579  C CB  . HIS   A 1 75  ? -16.054 -28.845 4.545   1.00 34.14  ? 74  HIS   A CB  1 
ATOM   580  C CG  . HIS   A 1 75  ? -17.116 -29.424 3.677   1.00 32.40  ? 74  HIS   A CG  1 
ATOM   581  N ND1 . HIS   A 1 75  ? -18.429 -29.119 3.950   1.00 35.63  ? 74  HIS   A ND1 1 
ATOM   582  C CD2 . HIS   A 1 75  ? -17.147 -30.193 2.577   1.00 36.09  ? 74  HIS   A CD2 1 
ATOM   583  C CE1 . HIS   A 1 75  ? -19.223 -29.703 3.046   1.00 32.55  ? 74  HIS   A CE1 1 
ATOM   584  N NE2 . HIS   A 1 75  ? -18.481 -30.363 2.207   1.00 31.18  ? 74  HIS   A NE2 1 
ATOM   585  N N   . VAL   A 1 76  ? -13.956 -29.584 1.989   1.00 39.84  ? 75  VAL   A N   1 
ATOM   586  C CA  . VAL   A 1 76  ? -13.554 -29.076 0.691   1.00 40.87  ? 75  VAL   A CA  1 
ATOM   587  C C   . VAL   A 1 76  ? -14.659 -29.467 -0.272  1.00 43.52  ? 75  VAL   A C   1 
ATOM   588  O O   . VAL   A 1 76  ? -14.944 -30.642 -0.429  1.00 42.74  ? 75  VAL   A O   1 
ATOM   589  C CB  . VAL   A 1 76  ? -12.207 -29.634 0.201   1.00 42.65  ? 75  VAL   A CB  1 
ATOM   590  C CG1 . VAL   A 1 76  ? -11.748 -28.967 -1.098  1.00 45.81  ? 75  VAL   A CG1 1 
ATOM   591  C CG2 . VAL   A 1 76  ? -11.151 -29.503 1.266   1.00 38.89  ? 75  VAL   A CG2 1 
ATOM   592  N N   . LEU   A 1 77  ? -15.276 -28.467 -0.882  1.00 39.39  ? 76  LEU   A N   1 
ATOM   593  C CA  . LEU   A 1 77  ? -16.334 -28.682 -1.845  1.00 44.17  ? 76  LEU   A CA  1 
ATOM   594  C C   . LEU   A 1 77  ? -15.956 -27.994 -3.156  1.00 49.24  ? 76  LEU   A C   1 
ATOM   595  O O   . LEU   A 1 77  ? -15.743 -26.777 -3.176  1.00 49.79  ? 76  LEU   A O   1 
ATOM   596  C CB  . LEU   A 1 77  ? -17.583 -28.103 -1.194  1.00 43.94  ? 76  LEU   A CB  1 
ATOM   597  C CG  . LEU   A 1 77  ? -18.869 -28.241 -1.989  1.00 53.16  ? 76  LEU   A CG  1 
ATOM   598  C CD1 . LEU   A 1 77  ? -19.118 -29.714 -2.376  1.00 65.80  ? 76  LEU   A CD1 1 
ATOM   599  C CD2 . LEU   A 1 77  ? -19.992 -27.673 -1.136  1.00 57.88  ? 76  LEU   A CD2 1 
ATOM   600  N N   . GLU   A 1 78  ? -15.811 -28.804 -4.215  1.00 46.66  ? 77  GLU   A N   1 
ATOM   601  C CA  . GLU   A 1 78  ? -15.467 -28.339 -5.544  1.00 48.77  ? 77  GLU   A CA  1 
ATOM   602  C C   . GLU   A 1 78  ? -16.711 -28.401 -6.412  1.00 46.55  ? 77  GLU   A C   1 
ATOM   603  O O   . GLU   A 1 78  ? -17.418 -29.396 -6.381  1.00 54.15  ? 77  GLU   A O   1 
ATOM   604  C CB  . GLU   A 1 78  ? -14.400 -29.229 -6.170  1.00 50.77  ? 77  GLU   A CB  1 
ATOM   605  C CG  . GLU   A 1 78  ? -13.900 -28.732 -7.525  1.00 51.28  ? 77  GLU   A CG  1 
ATOM   606  C CD  . GLU   A 1 78  ? -12.666 -29.462 -8.052  1.00 57.12  ? 77  GLU   A CD  1 
ATOM   607  O OE1 . GLU   A 1 78  ? -12.122 -30.372 -7.391  1.00 61.99  ? 77  GLU   A OE1 1 
ATOM   608  O OE2 . GLU   A 1 78  ? -12.228 -29.093 -9.142  1.00 64.11  ? 77  GLU   A OE2 1 
ATOM   609  N N   . THR   A 1 79  ? -16.992 -27.314 -7.134  1.00 51.43  ? 78  THR   A N   1 
ATOM   610  C CA  . THR   A 1 79  ? -18.065 -27.287 -8.119  1.00 51.88  ? 78  THR   A CA  1 
ATOM   611  C C   . THR   A 1 79  ? -17.414 -27.020 -9.470  1.00 55.81  ? 78  THR   A C   1 
ATOM   612  O O   . THR   A 1 79  ? -16.193 -26.917 -9.551  1.00 58.59  ? 78  THR   A O   1 
ATOM   613  C CB  . THR   A 1 79  ? -19.093 -26.211 -7.774  1.00 56.20  ? 78  THR   A CB  1 
ATOM   614  O OG1 . THR   A 1 79  ? -18.447 -24.949 -7.957  1.00 53.53  ? 78  THR   A OG1 1 
ATOM   615  C CG2 . THR   A 1 79  ? -19.629 -26.335 -6.360  1.00 57.35  ? 78  THR   A CG2 1 
ATOM   616  N N   . ALA   A 1 80  ? -18.234 -26.853 -10.515 1.00 62.78  ? 79  ALA   A N   1 
ATOM   617  C CA  . ALA   A 1 80  ? -17.709 -26.578 -11.844 1.00 59.72  ? 79  ALA   A CA  1 
ATOM   618  C C   . ALA   A 1 80  ? -16.774 -25.368 -11.833 1.00 64.12  ? 79  ALA   A C   1 
ATOM   619  O O   . ALA   A 1 80  ? -15.769 -25.395 -12.525 1.00 69.81  ? 79  ALA   A O   1 
ATOM   620  C CB  . ALA   A 1 80  ? -18.856 -26.404 -12.812 1.00 64.87  ? 79  ALA   A CB  1 
ATOM   621  N N   . ASN   A 1 81  ? -17.068 -24.319 -11.045 1.00 58.49  ? 80  ASN   A N   1 
ATOM   622  C CA  . ASN   A 1 81  ? -16.302 -23.082 -11.128 1.00 57.30  ? 80  ASN   A CA  1 
ATOM   623  C C   . ASN   A 1 81  ? -15.585 -22.682 -9.850  1.00 55.16  ? 80  ASN   A C   1 
ATOM   624  O O   . ASN   A 1 81  ? -14.823 -21.715 -9.888  1.00 51.35  ? 80  ASN   A O   1 
ATOM   625  C CB  . ASN   A 1 81  ? -17.183 -21.893 -11.474 1.00 60.78  ? 80  ASN   A CB  1 
ATOM   626  C CG  . ASN   A 1 81  ? -17.792 -22.091 -12.837 1.00 65.07  ? 80  ASN   A CG  1 
ATOM   627  O OD1 . ASN   A 1 81  ? -17.058 -22.162 -13.834 1.00 68.40  ? 80  ASN   A OD1 1 
ATOM   628  N ND2 . ASN   A 1 81  ? -19.108 -22.245 -12.883 1.00 61.67  ? 80  ASN   A ND2 1 
ATOM   629  N N   . LYS   A 1 82  ? -15.829 -23.396 -8.740  1.00 47.64  ? 81  LYS   A N   1 
ATOM   630  C CA  . LYS   A 1 82  ? -15.381 -22.933 -7.433  1.00 48.77  ? 81  LYS   A CA  1 
ATOM   631  C C   . LYS   A 1 82  ? -14.750 -24.070 -6.624  1.00 45.77  ? 81  LYS   A C   1 
ATOM   632  O O   . LYS   A 1 82  ? -15.061 -25.247 -6.817  1.00 50.65  ? 81  LYS   A O   1 
ATOM   633  C CB  . LYS   A 1 82  ? -16.554 -22.345 -6.631  1.00 52.71  ? 81  LYS   A CB  1 
ATOM   634  C CG  . LYS   A 1 82  ? -17.354 -21.224 -7.301  1.00 49.01  ? 81  LYS   A CG  1 
ATOM   635  C CD  . LYS   A 1 82  ? -16.576 -19.926 -7.441  1.00 54.05  ? 81  LYS   A CD  1 
ATOM   636  C CE  . LYS   A 1 82  ? -17.378 -18.877 -8.201  1.00 59.98  ? 81  LYS   A CE  1 
ATOM   637  N NZ  . LYS   A 1 82  ? -16.671 -17.595 -8.278  1.00 63.02  ? 81  LYS   A NZ  1 
ATOM   638  N N   . ILE   A 1 83  ? -13.851 -23.696 -5.713  1.00 42.21  ? 82  ILE   A N   1 
ATOM   639  C CA  . ILE   A 1 83  ? -13.474 -24.562 -4.615  1.00 46.61  ? 82  ILE   A CA  1 
ATOM   640  C C   . ILE   A 1 83  ? -13.759 -23.779 -3.344  1.00 46.99  ? 82  ILE   A C   1 
ATOM   641  O O   . ILE   A 1 83  ? -13.369 -22.617 -3.216  1.00 44.54  ? 82  ILE   A O   1 
ATOM   642  C CB  . ILE   A 1 83  ? -12.014 -25.032 -4.683  1.00 50.02  ? 82  ILE   A CB  1 
ATOM   643  C CG1 . ILE   A 1 83  ? -11.720 -25.812 -5.951  1.00 57.12  ? 82  ILE   A CG1 1 
ATOM   644  C CG2 . ILE   A 1 83  ? -11.671 -25.853 -3.438  1.00 53.92  ? 82  ILE   A CG2 1 
ATOM   645  C CD1 . ILE   A 1 83  ? -10.260 -26.195 -6.100  1.00 57.71  ? 82  ILE   A CD1 1 
ATOM   646  N N   . PHE   A 1 84  ? -14.545 -24.409 -2.471  1.00 44.66  ? 83  PHE   A N   1 
ATOM   647  C CA  . PHE   A 1 84  ? -14.848 -23.876 -1.158  1.00 40.99  ? 83  PHE   A CA  1 
ATOM   648  C C   . PHE   A 1 84  ? -14.058 -24.674 -0.131  1.00 40.16  ? 83  PHE   A C   1 
ATOM   649  O O   . PHE   A 1 84  ? -14.109 -25.897 -0.109  1.00 40.91  ? 83  PHE   A O   1 
ATOM   650  C CB  . PHE   A 1 84  ? -16.345 -24.013 -0.894  1.00 43.30  ? 83  PHE   A CB  1 
ATOM   651  C CG  . PHE   A 1 84  ? -17.275 -23.341 -1.895  1.00 43.35  ? 83  PHE   A CG  1 
ATOM   652  C CD1 . PHE   A 1 84  ? -17.578 -21.991 -1.782  1.00 46.16  ? 83  PHE   A CD1 1 
ATOM   653  C CD2 . PHE   A 1 84  ? -17.884 -24.063 -2.905  1.00 48.17  ? 83  PHE   A CD2 1 
ATOM   654  C CE1 . PHE   A 1 84  ? -18.451 -21.391 -2.664  1.00 40.72  ? 83  PHE   A CE1 1 
ATOM   655  C CE2 . PHE   A 1 84  ? -18.721 -23.439 -3.809  1.00 45.04  ? 83  PHE   A CE2 1 
ATOM   656  C CZ  . PHE   A 1 84  ? -19.004 -22.111 -3.675  1.00 42.79  ? 83  PHE   A CZ  1 
ATOM   657  N N   . MET   A 1 85  ? -13.339 -23.974 0.731   1.00 40.09  ? 84  MET   A N   1 
ATOM   658  C CA  . MET   A 1 85  ? -12.670 -24.577 1.862   1.00 40.13  ? 84  MET   A CA  1 
ATOM   659  C C   . MET   A 1 85  ? -13.294 -24.023 3.127   1.00 40.76  ? 84  MET   A C   1 
ATOM   660  O O   . MET   A 1 85  ? -13.257 -22.815 3.375   1.00 38.46  ? 84  MET   A O   1 
ATOM   661  C CB  . MET   A 1 85  ? -11.180 -24.247 1.857   1.00 40.95  ? 84  MET   A CB  1 
ATOM   662  C CG  . MET   A 1 85  ? -10.437 -24.846 0.677   1.00 49.48  ? 84  MET   A CG  1 
ATOM   663  S SD  . MET   A 1 85  ? -8.812  -24.066 0.566   1.00 55.67  ? 84  MET   A SD  1 
ATOM   664  C CE  . MET   A 1 85  ? -8.029  -24.565 2.106   1.00 47.68  ? 84  MET   A CE  1 
ATOM   665  N N   . VAL   A 1 86  ? -13.861 -24.925 3.926   1.00 39.24  ? 85  VAL   A N   1 
ATOM   666  C CA  . VAL   A 1 86  ? -14.492 -24.542 5.171   1.00 32.68  ? 85  VAL   A CA  1 
ATOM   667  C C   . VAL   A 1 86  ? -13.489 -24.752 6.277   1.00 35.72  ? 85  VAL   A C   1 
ATOM   668  O O   . VAL   A 1 86  ? -12.958 -25.844 6.417   1.00 36.31  ? 85  VAL   A O   1 
ATOM   669  C CB  . VAL   A 1 86  ? -15.760 -25.363 5.417   1.00 34.14  ? 85  VAL   A CB  1 
ATOM   670  C CG1 . VAL   A 1 86  ? -16.378 -25.040 6.762   1.00 36.56  ? 85  VAL   A CG1 1 
ATOM   671  C CG2 . VAL   A 1 86  ? -16.770 -25.177 4.308   1.00 41.44  ? 85  VAL   A CG2 1 
ATOM   672  N N   . LEU   A 1 87  ? -13.312 -23.726 7.106   1.00 32.58  ? 86  LEU   A N   1 
ATOM   673  C CA  . LEU   A 1 87  ? -12.277 -23.720 8.110   1.00 31.07  ? 86  LEU   A CA  1 
ATOM   674  C C   . LEU   A 1 87  ? -12.850 -23.342 9.459   1.00 32.67  ? 86  LEU   A C   1 
ATOM   675  O O   . LEU   A 1 87  ? -13.911 -22.710 9.592   1.00 33.26  ? 86  LEU   A O   1 
ATOM   676  C CB  . LEU   A 1 87  ? -11.205 -22.713 7.697   1.00 39.81  ? 86  LEU   A CB  1 
ATOM   677  C CG  . LEU   A 1 87  ? -10.560 -22.972 6.334   1.00 41.88  ? 86  LEU   A CG  1 
ATOM   678  C CD1 . LEU   A 1 87  ? -10.289 -21.661 5.616   1.00 44.59  ? 86  LEU   A CD1 1 
ATOM   679  C CD2 . LEU   A 1 87  ? -9.296  -23.726 6.546   1.00 41.79  ? 86  LEU   A CD2 1 
ATOM   680  N N   . GLU   A 1 88  ? -12.067 -23.696 10.468  1.00 35.07  ? 87  GLU   A N   1 
ATOM   681  C CA  . GLU   A 1 88  ? -12.408 -23.390 11.838  1.00 38.39  ? 87  GLU   A CA  1 
ATOM   682  C C   . GLU   A 1 88  ? -12.509 -21.885 12.023  1.00 40.45  ? 87  GLU   A C   1 
ATOM   683  O O   . GLU   A 1 88  ? -11.602 -21.152 11.604  1.00 38.20  ? 87  GLU   A O   1 
ATOM   684  C CB  . GLU   A 1 88  ? -11.253 -23.912 12.674  1.00 41.06  ? 87  GLU   A CB  1 
ATOM   685  C CG  . GLU   A 1 88  ? -11.320 -23.491 14.135  1.00 41.21  ? 87  GLU   A CG  1 
ATOM   686  C CD  . GLU   A 1 88  ? -10.139 -24.065 14.882  1.00 39.79  ? 87  GLU   A CD  1 
ATOM   687  O OE1 . GLU   A 1 88  ? -9.290  -24.734 14.283  1.00 39.49  ? 87  GLU   A OE1 1 
ATOM   688  O OE2 . GLU   A 1 88  ? -10.079 -23.811 16.073  1.00 42.02  ? 87  GLU   A OE2 1 
ATOM   689  N N   . TYR   A 1 89  ? -13.595 -21.450 12.682  1.00 44.13  ? 88  TYR   A N   1 
ATOM   690  C CA  . TYR   A 1 89  ? -13.788 -20.028 12.961  1.00 41.23  ? 88  TYR   A CA  1 
ATOM   691  C C   . TYR   A 1 89  ? -13.028 -19.685 14.235  1.00 38.01  ? 88  TYR   A C   1 
ATOM   692  O O   . TYR   A 1 89  ? -13.132 -20.392 15.228  1.00 40.51  ? 88  TYR   A O   1 
ATOM   693  C CB  . TYR   A 1 89  ? -15.282 -19.684 13.039  1.00 44.42  ? 88  TYR   A CB  1 
ATOM   694  C CG  . TYR   A 1 89  ? -15.593 -18.226 13.399  1.00 44.65  ? 88  TYR   A CG  1 
ATOM   695  C CD1 . TYR   A 1 89  ? -15.026 -17.150 12.711  1.00 52.55  ? 88  TYR   A CD1 1 
ATOM   696  C CD2 . TYR   A 1 89  ? -16.389 -17.940 14.498  1.00 49.25  ? 88  TYR   A CD2 1 
ATOM   697  C CE1 . TYR   A 1 89  ? -15.300 -15.833 13.075  1.00 58.73  ? 88  TYR   A CE1 1 
ATOM   698  C CE2 . TYR   A 1 89  ? -16.654 -16.637 14.888  1.00 53.75  ? 88  TYR   A CE2 1 
ATOM   699  C CZ  . TYR   A 1 89  ? -16.119 -15.584 14.172  1.00 56.39  ? 88  TYR   A CZ  1 
ATOM   700  O OH  . TYR   A 1 89  ? -16.450 -14.336 14.624  1.00 77.07  ? 88  TYR   A OH  1 
ATOM   701  N N   . CYS   A 1 90  ? -12.231 -18.613 14.208  1.00 36.68  ? 89  CYS   A N   1 
ATOM   702  C CA  . CYS   A 1 90  ? -11.517 -18.180 15.392  1.00 37.93  ? 89  CYS   A CA  1 
ATOM   703  C C   . CYS   A 1 90  ? -12.133 -16.883 15.913  1.00 51.24  ? 89  CYS   A C   1 
ATOM   704  O O   . CYS   A 1 90  ? -11.912 -15.827 15.334  1.00 44.85  ? 89  CYS   A O   1 
ATOM   705  C CB  . CYS   A 1 90  ? -10.049 -17.970 15.065  1.00 46.93  ? 89  CYS   A CB  1 
ATOM   706  S SG  . CYS   A 1 90  ? -9.239  -19.504 14.532  1.00 47.02  ? 89  CYS   A SG  1 
ATOM   707  N N   . PRO   A 1 91  ? -12.982 -16.905 16.958  1.00 49.08  ? 90  PRO   A N   1 
ATOM   708  C CA  . PRO   A 1 91  ? -13.704 -15.684 17.345  1.00 53.00  ? 90  PRO   A CA  1 
ATOM   709  C C   . PRO   A 1 91  ? -12.962 -14.587 18.119  1.00 55.22  ? 90  PRO   A C   1 
ATOM   710  O O   . PRO   A 1 91  ? -13.470 -13.472 18.224  1.00 57.30  ? 90  PRO   A O   1 
ATOM   711  C CB  . PRO   A 1 91  ? -14.876 -16.281 18.159  1.00 53.19  ? 90  PRO   A CB  1 
ATOM   712  C CG  . PRO   A 1 91  ? -14.297 -17.531 18.805  1.00 54.06  ? 90  PRO   A CG  1 
ATOM   713  C CD  . PRO   A 1 91  ? -13.371 -18.093 17.733  1.00 54.78  ? 90  PRO   A CD  1 
ATOM   714  N N   . GLY   A 1 92  ? -11.752 -14.860 18.625  1.00 52.73  ? 91  GLY   A N   1 
ATOM   715  C CA  . GLY   A 1 92  ? -11.019 -13.882 19.428  1.00 52.46  ? 91  GLY   A CA  1 
ATOM   716  C C   . GLY   A 1 92  ? -10.313 -12.773 18.640  1.00 49.89  ? 91  GLY   A C   1 
ATOM   717  O O   . GLY   A 1 92  ? -9.584  -11.980 19.211  1.00 54.77  ? 91  GLY   A O   1 
ATOM   718  N N   . GLY   A 1 93  ? -10.436 -12.716 17.324  1.00 56.61  ? 92  GLY   A N   1 
ATOM   719  C CA  . GLY   A 1 93  ? -9.717  -11.695 16.572  1.00 57.51  ? 92  GLY   A CA  1 
ATOM   720  C C   . GLY   A 1 93  ? -8.194  -11.882 16.588  1.00 56.15  ? 92  GLY   A C   1 
ATOM   721  O O   . GLY   A 1 93  ? -7.668  -12.850 17.130  1.00 57.55  ? 92  GLY   A O   1 
ATOM   722  N N   . GLU   A 1 94  ? -7.486  -10.935 15.960  1.00 56.24  ? 93  GLU   A N   1 
ATOM   723  C CA  . GLU   A 1 94  ? -6.094  -11.134 15.605  1.00 50.65  ? 93  GLU   A CA  1 
ATOM   724  C C   . GLU   A 1 94  ? -5.218  -10.771 16.796  1.00 51.08  ? 93  GLU   A C   1 
ATOM   725  O O   . GLU   A 1 94  ? -5.543  -9.898  17.586  1.00 51.07  ? 93  GLU   A O   1 
ATOM   726  C CB  . GLU   A 1 94  ? -5.605  -10.280 14.434  1.00 54.80  ? 93  GLU   A CB  1 
ATOM   727  C CG  . GLU   A 1 94  ? -6.429  -10.380 13.151  1.00 60.95  ? 93  GLU   A CG  1 
ATOM   728  C CD  . GLU   A 1 94  ? -6.060  -9.320  12.119  1.00 59.53  ? 93  GLU   A CD  1 
ATOM   729  O OE1 . GLU   A 1 94  ? -5.104  -8.559  12.383  1.00 63.10  ? 93  GLU   A OE1 1 
ATOM   730  O OE2 . GLU   A 1 94  ? -6.718  -9.234  11.063  1.00 68.05  ? 93  GLU   A OE2 1 
ATOM   731  N N   . LEU   A 1 95  ? -4.070  -11.438 16.873  1.00 44.96  ? 94  LEU   A N   1 
ATOM   732  C CA  . LEU   A 1 95  ? -2.992  -11.048 17.756  1.00 43.85  ? 94  LEU   A CA  1 
ATOM   733  C C   . LEU   A 1 95  ? -2.653  -9.563  17.575  1.00 36.97  ? 94  LEU   A C   1 
ATOM   734  O O   . LEU   A 1 95  ? -2.303  -8.903  18.542  1.00 40.07  ? 94  LEU   A O   1 
ATOM   735  C CB  . LEU   A 1 95  ? -1.793  -11.923 17.409  1.00 44.67  ? 94  LEU   A CB  1 
ATOM   736  C CG  . LEU   A 1 95  ? -0.573  -11.714 18.299  1.00 43.53  ? 94  LEU   A CG  1 
ATOM   737  C CD1 . LEU   A 1 95  ? -0.931  -11.849 19.777  1.00 44.60  ? 94  LEU   A CD1 1 
ATOM   738  C CD2 . LEU   A 1 95  ? 0.518   -12.682 17.881  1.00 50.39  ? 94  LEU   A CD2 1 
ATOM   739  N N   . PHE   A 1 96  ? -2.670  -9.106  16.327  1.00 42.30  ? 95  PHE   A N   1 
ATOM   740  C CA  . PHE   A 1 96  ? -2.399  -7.717  15.981  1.00 41.45  ? 95  PHE   A CA  1 
ATOM   741  C C   . PHE   A 1 96  ? -3.245  -6.774  16.854  1.00 43.07  ? 95  PHE   A C   1 
ATOM   742  O O   . PHE   A 1 96  ? -2.717  -5.897  17.520  1.00 44.46  ? 95  PHE   A O   1 
ATOM   743  C CB  . PHE   A 1 96  ? -2.671  -7.576  14.479  1.00 43.42  ? 95  PHE   A CB  1 
ATOM   744  C CG  . PHE   A 1 96  ? -2.407  -6.165  13.961  1.00 53.02  ? 95  PHE   A CG  1 
ATOM   745  C CD1 . PHE   A 1 96  ? -1.110  -5.738  13.704  1.00 45.21  ? 95  PHE   A CD1 1 
ATOM   746  C CD2 . PHE   A 1 96  ? -3.454  -5.257  13.819  1.00 53.17  ? 95  PHE   A CD2 1 
ATOM   747  C CE1 . PHE   A 1 96  ? -0.875  -4.446  13.265  1.00 54.17  ? 95  PHE   A CE1 1 
ATOM   748  C CE2 . PHE   A 1 96  ? -3.205  -3.970  13.386  1.00 59.27  ? 95  PHE   A CE2 1 
ATOM   749  C CZ  . PHE   A 1 96  ? -1.917  -3.572  13.110  1.00 52.95  ? 95  PHE   A CZ  1 
ATOM   750  N N   . ASP   A 1 97  ? -4.558  -7.016  16.875  1.00 51.48  ? 96  ASP   A N   1 
ATOM   751  C CA  . ASP   A 1 97  ? -5.497  -6.239  17.667  1.00 54.13  ? 96  ASP   A CA  1 
ATOM   752  C C   . ASP   A 1 97  ? -5.127  -6.342  19.142  1.00 54.87  ? 96  ASP   A C   1 
ATOM   753  O O   . ASP   A 1 97  ? -5.146  -5.362  19.880  1.00 53.39  ? 96  ASP   A O   1 
ATOM   754  C CB  . ASP   A 1 97  ? -6.933  -6.625  17.338  1.00 56.37  ? 96  ASP   A CB  1 
ATOM   755  C CG  . ASP   A 1 97  ? -7.325  -6.535  15.865  1.00 62.13  ? 96  ASP   A CG  1 
ATOM   756  O OD1 . ASP   A 1 97  ? -6.931  -5.550  15.207  1.00 58.30  ? 96  ASP   A OD1 1 
ATOM   757  O OD2 . ASP   A 1 97  ? -8.011  -7.463  15.371  1.00 71.94  ? 96  ASP   A OD2 1 
ATOM   758  N N   . TYR   A 1 98  ? -4.693  -7.512  19.584  1.00 52.48  ? 97  TYR   A N   1 
ATOM   759  C CA  . TYR   A 1 98  ? -4.414  -7.671  20.999  1.00 49.13  ? 97  TYR   A CA  1 
ATOM   760  C C   . TYR   A 1 98  ? -3.213  -6.823  21.411  1.00 49.77  ? 97  TYR   A C   1 
ATOM   761  O O   . TYR   A 1 98  ? -3.257  -6.115  22.420  1.00 53.04  ? 97  TYR   A O   1 
ATOM   762  C CB  . TYR   A 1 98  ? -4.234  -9.162  21.309  1.00 53.00  ? 97  TYR   A CB  1 
ATOM   763  C CG  . TYR   A 1 98  ? -4.032  -9.392  22.789  1.00 54.18  ? 97  TYR   A CG  1 
ATOM   764  C CD1 . TYR   A 1 98  ? -5.052  -9.088  23.680  1.00 59.06  ? 97  TYR   A CD1 1 
ATOM   765  C CD2 . TYR   A 1 98  ? -2.830  -9.867  23.293  1.00 58.18  ? 97  TYR   A CD2 1 
ATOM   766  C CE1 . TYR   A 1 98  ? -4.890  -9.267  25.040  1.00 60.15  ? 97  TYR   A CE1 1 
ATOM   767  C CE2 . TYR   A 1 98  ? -2.661  -10.061 24.652  1.00 64.22  ? 97  TYR   A CE2 1 
ATOM   768  C CZ  . TYR   A 1 98  ? -3.695  -9.757  25.523  1.00 63.99  ? 97  TYR   A CZ  1 
ATOM   769  O OH  . TYR   A 1 98  ? -3.573  -9.910  26.866  1.00 68.45  ? 97  TYR   A OH  1 
ATOM   770  N N   . ILE   A 1 99  ? -2.133  -6.888  20.631  1.00 46.93  ? 98  ILE   A N   1 
ATOM   771  C CA  . ILE   A 1 99  ? -0.917  -6.162  20.960  1.00 46.53  ? 98  ILE   A CA  1 
ATOM   772  C C   . ILE   A 1 99  ? -1.216  -4.660  21.115  1.00 54.09  ? 98  ILE   A C   1 
ATOM   773  O O   . ILE   A 1 99  ? -0.664  -4.029  22.006  1.00 47.18  ? 98  ILE   A O   1 
ATOM   774  C CB  . ILE   A 1 99  ? 0.198   -6.382  19.916  1.00 51.05  ? 98  ILE   A CB  1 
ATOM   775  C CG1 . ILE   A 1 99  ? 0.658   -7.850  19.842  1.00 60.65  ? 98  ILE   A CG1 1 
ATOM   776  C CG2 . ILE   A 1 99  ? 1.385   -5.459  20.219  1.00 48.71  ? 98  ILE   A CG2 1 
ATOM   777  C CD1 . ILE   A 1 99  ? 1.476   -8.170  18.596  1.00 56.17  ? 98  ILE   A CD1 1 
ATOM   778  N N   . ILE   A 1 100 ? -2.008  -4.087  20.200  1.00 49.30  ? 99  ILE   A N   1 
ATOM   779  C CA  . ILE   A 1 100 ? -2.319  -2.666  20.241  1.00 58.29  ? 99  ILE   A CA  1 
ATOM   780  C C   . ILE   A 1 100 ? -3.127  -2.306  21.495  1.00 52.95  ? 99  ILE   A C   1 
ATOM   781  O O   . ILE   A 1 100 ? -2.826  -1.361  22.215  1.00 65.11  ? 99  ILE   A O   1 
ATOM   782  C CB  . ILE   A 1 100 ? -3.079  -2.271  18.973  1.00 54.98  ? 99  ILE   A CB  1 
ATOM   783  C CG1 . ILE   A 1 100 ? -2.185  -2.317  17.769  1.00 55.51  ? 99  ILE   A CG1 1 
ATOM   784  C CG2 . ILE   A 1 100 ? -3.684  -0.885  19.182  1.00 63.03  ? 99  ILE   A CG2 1 
ATOM   785  C CD1 . ILE   A 1 100 ? -2.939  -2.189  16.469  1.00 52.02  ? 99  ILE   A CD1 1 
ATOM   786  N N   . SER   A 1 101 ? -4.150  -3.091  21.774  1.00 61.64  ? 100 SER   A N   1 
ATOM   787  C CA  . SER   A 1 101 ? -4.980  -2.874  22.950  1.00 63.34  ? 100 SER   A CA  1 
ATOM   788  C C   . SER   A 1 101 ? -4.151  -2.900  24.233  1.00 68.16  ? 100 SER   A C   1 
ATOM   789  O O   . SER   A 1 101 ? -4.432  -2.146  25.157  1.00 66.41  ? 100 SER   A O   1 
ATOM   790  C CB  . SER   A 1 101 ? -6.088  -3.888  23.021  1.00 56.35  ? 100 SER   A CB  1 
ATOM   791  O OG  . SER   A 1 101 ? -5.621  -5.113  23.568  1.00 64.03  ? 100 SER   A OG  1 
ATOM   792  N N   . GLN   A 1 102 ? -3.124  -3.759  24.292  1.00 70.17  ? 101 GLN   A N   1 
ATOM   793  C CA  . GLN   A 1 102 ? -2.295  -3.868  25.479  1.00 54.08  ? 101 GLN   A CA  1 
ATOM   794  C C   . GLN   A 1 102 ? -1.089  -2.930  25.438  1.00 52.55  ? 101 GLN   A C   1 
ATOM   795  O O   . GLN   A 1 102 ? -0.386  -2.851  26.449  1.00 51.99  ? 101 GLN   A O   1 
ATOM   796  C CB  . GLN   A 1 102 ? -1.793  -5.298  25.636  1.00 64.07  ? 101 GLN   A CB  1 
ATOM   797  C CG  . GLN   A 1 102 ? -2.895  -6.319  25.865  1.00 67.11  ? 101 GLN   A CG  1 
ATOM   798  C CD  . GLN   A 1 102 ? -3.445  -6.298  27.274  1.00 69.45  ? 101 GLN   A CD  1 
ATOM   799  O OE1 . GLN   A 1 102 ? -2.706  -6.386  28.260  1.00 74.11  ? 101 GLN   A OE1 1 
ATOM   800  N NE2 . GLN   A 1 102 ? -4.761  -6.243  27.377  1.00 67.73  ? 101 GLN   A NE2 1 
ATOM   801  N N   . ASP   A 1 103 ? -0.855  -2.230  24.309  1.00 45.92  ? 102 ASP   A N   1 
ATOM   802  C CA  . ASP   A 1 103 ? 0.363   -1.443  24.071  1.00 48.81  ? 102 ASP   A CA  1 
ATOM   803  C C   . ASP   A 1 103 ? 1.681   -2.241  23.863  1.00 54.37  ? 102 ASP   A C   1 
ATOM   804  O O   . ASP   A 1 103 ? 2.370   -2.066  22.869  1.00 53.72  ? 102 ASP   A O   1 
ATOM   805  C CB  . ASP   A 1 103 ? 0.701   -0.488  25.192  1.00 46.17  ? 102 ASP   A CB  1 
ATOM   806  C CG  . ASP   A 1 103 ? 1.927   0.341   24.870  1.00 59.51  ? 102 ASP   A CG  1 
ATOM   807  O OD1 . ASP   A 1 103 ? 2.185   0.569   23.661  1.00 68.18  ? 102 ASP   A OD1 1 
ATOM   808  O OD2 . ASP   A 1 103 ? 2.610   0.750   25.821  1.00 82.77  ? 102 ASP   A OD2 1 
ATOM   809  N N   . ARG   A 1 104 ? 2.154   -2.986  24.866  1.00 47.50  ? 103 ARG   A N   1 
ATOM   810  C CA  . ARG   A 1 104 ? 3.107   -4.068  24.650  1.00 47.10  ? 103 ARG   A CA  1 
ATOM   811  C C   . ARG   A 1 104 ? 2.809   -5.150  25.677  1.00 48.80  ? 103 ARG   A C   1 
ATOM   812  O O   . ARG   A 1 104 ? 2.194   -4.845  26.673  1.00 38.95  ? 103 ARG   A O   1 
ATOM   813  C CB  . ARG   A 1 104 ? 4.536   -3.544  24.790  1.00 44.40  ? 103 ARG   A CB  1 
ATOM   814  C CG  . ARG   A 1 104 ? 4.922   -3.183  26.210  1.00 44.96  ? 103 ARG   A CG  1 
ATOM   815  C CD  . ARG   A 1 104 ? 6.214   -2.410  26.181  1.00 46.61  ? 103 ARG   A CD  1 
ATOM   816  N NE  . ARG   A 1 104 ? 6.662   -2.016  27.520  1.00 57.26  ? 103 ARG   A NE  1 
ATOM   817  C CZ  . ARG   A 1 104 ? 7.170   -0.833  27.869  1.00 69.81  ? 103 ARG   A CZ  1 
ATOM   818  N NH1 . ARG   A 1 104 ? 7.069   0.231   27.081  1.00 71.73  ? 103 ARG   A NH1 1 
ATOM   819  N NH2 . ARG   A 1 104 ? 7.775   -0.720  29.040  1.00 77.01  ? 103 ARG   A NH2 1 
ATOM   820  N N   . LEU   A 1 105 ? 3.206   -6.403  25.431  1.00 39.76  ? 104 LEU   A N   1 
ATOM   821  C CA  . LEU   A 1 105 ? 2.990   -7.466  26.400  1.00 41.19  ? 104 LEU   A CA  1 
ATOM   822  C C   . LEU   A 1 105 ? 4.226   -7.576  27.285  1.00 42.42  ? 104 LEU   A C   1 
ATOM   823  O O   . LEU   A 1 105 ? 5.344   -7.327  26.828  1.00 41.58  ? 104 LEU   A O   1 
ATOM   824  C CB  . LEU   A 1 105 ? 2.694   -8.815  25.753  1.00 40.89  ? 104 LEU   A CB  1 
ATOM   825  C CG  . LEU   A 1 105 ? 1.623   -8.810  24.666  1.00 45.03  ? 104 LEU   A CG  1 
ATOM   826  C CD1 . LEU   A 1 105 ? 1.237   -10.224 24.356  1.00 49.22  ? 104 LEU   A CD1 1 
ATOM   827  C CD2 . LEU   A 1 105 ? 0.428   -8.004  25.071  1.00 47.24  ? 104 LEU   A CD2 1 
ATOM   828  N N   . SER   A 1 106 ? 3.996   -7.968  28.549  1.00 39.90  ? 105 SER   A N   1 
ATOM   829  C CA  . SER   A 1 106 ? 5.049   -8.335  29.480  1.00 39.97  ? 105 SER   A CA  1 
ATOM   830  C C   . SER   A 1 106 ? 5.836   -9.514  28.899  1.00 36.63  ? 105 SER   A C   1 
ATOM   831  O O   . SER   A 1 106 ? 5.347   -10.260 28.036  1.00 36.29  ? 105 SER   A O   1 
ATOM   832  C CB  . SER   A 1 106 ? 4.446   -8.669  30.855  1.00 38.89  ? 105 SER   A CB  1 
ATOM   833  O OG  . SER   A 1 106 ? 3.764   -9.926  30.850  1.00 34.99  ? 105 SER   A OG  1 
ATOM   834  N N   . GLU   A 1 107 ? 7.057   -9.704  29.380  1.00 36.86  ? 106 GLU   A N   1 
ATOM   835  C CA  . GLU   A 1 107 ? 7.840   -10.880 28.997  1.00 39.53  ? 106 GLU   A CA  1 
ATOM   836  C C   . GLU   A 1 107 ? 7.034   -12.151 29.290  1.00 43.78  ? 106 GLU   A C   1 
ATOM   837  O O   . GLU   A 1 107 ? 7.029   -13.117 28.501  1.00 40.70  ? 106 GLU   A O   1 
ATOM   838  C CB  . GLU   A 1 107 ? 9.228   -10.842 29.667  1.00 39.57  ? 106 GLU   A CB  1 
ATOM   839  C CG  . GLU   A 1 107 ? 10.109  -12.027 29.308  1.00 39.89  ? 106 GLU   A CG  1 
ATOM   840  C CD  . GLU   A 1 107 ? 11.477  -12.093 29.965  1.00 40.89  ? 106 GLU   A CD  1 
ATOM   841  O OE1 . GLU   A 1 107 ? 12.104  -11.082 30.242  1.00 46.85  ? 106 GLU   A OE1 1 
ATOM   842  O OE2 . GLU   A 1 107 ? 11.989  -13.204 30.090  1.00 52.57  ? 106 GLU   A OE2 1 
ATOM   843  N N   . GLU   A 1 108 ? 6.334   -12.151 30.434  1.00 41.80  ? 107 GLU   A N   1 
ATOM   844  C CA  . GLU   A 1 108 ? 5.644   -13.346 30.894  1.00 44.92  ? 107 GLU   A CA  1 
ATOM   845  C C   . GLU   A 1 108 ? 4.503   -13.671 29.932  1.00 38.59  ? 107 GLU   A C   1 
ATOM   846  O O   . GLU   A 1 108 ? 4.311   -14.817 29.514  1.00 43.66  ? 107 GLU   A O   1 
ATOM   847  C CB  . GLU   A 1 108 ? 5.021   -13.242 32.298  1.00 46.95  ? 107 GLU   A CB  1 
ATOM   848  C CG  . GLU   A 1 108 ? 6.009   -12.908 33.415  1.00 56.72  ? 107 GLU   A CG  1 
ATOM   849  C CD  . GLU   A 1 108 ? 6.978   -11.736 33.281  1.00 66.76  ? 107 GLU   A CD  1 
ATOM   850  O OE1 . GLU   A 1 108 ? 6.639   -10.587 32.864  1.00 51.57  ? 107 GLU   A OE1 1 
ATOM   851  O OE2 . GLU   A 1 108 ? 8.155   -12.000 33.643  1.00 75.82  ? 107 GLU   A OE2 1 
ATOM   852  N N   . GLU   A 1 109 ? 3.713   -12.658 29.593  1.00 37.67  ? 108 GLU   A N   1 
ATOM   853  C CA  . GLU   A 1 109 ? 2.590   -12.917 28.715  1.00 44.20  ? 108 GLU   A CA  1 
ATOM   854  C C   . GLU   A 1 109 ? 3.065   -13.147 27.268  1.00 36.20  ? 108 GLU   A C   1 
ATOM   855  O O   . GLU   A 1 109 ? 2.471   -13.931 26.544  1.00 38.25  ? 108 GLU   A O   1 
ATOM   856  C CB  . GLU   A 1 109 ? 1.583   -11.778 28.790  1.00 48.47  ? 108 GLU   A CB  1 
ATOM   857  C CG  . GLU   A 1 109 ? 0.336   -12.167 28.005  1.00 57.71  ? 108 GLU   A CG  1 
ATOM   858  C CD  . GLU   A 1 109 ? -0.666  -11.048 27.896  1.00 61.01  ? 108 GLU   A CD  1 
ATOM   859  O OE1 . GLU   A 1 109 ? -0.386  -9.941  28.419  1.00 62.23  ? 108 GLU   A OE1 1 
ATOM   860  O OE2 . GLU   A 1 109 ? -1.711  -11.345 27.287  1.00 54.03  ? 108 GLU   A OE2 1 
ATOM   861  N N   . THR   A 1 110 ? 4.140   -12.460 26.863  1.00 36.37  ? 109 THR   A N   1 
ATOM   862  C CA  . THR   A 1 110 ? 4.738   -12.744 25.569  1.00 34.94  ? 109 THR   A CA  1 
ATOM   863  C C   . THR   A 1 110 ? 5.021   -14.243 25.498  1.00 36.56  ? 109 THR   A C   1 
ATOM   864  O O   . THR   A 1 110 ? 4.684   -14.897 24.523  1.00 36.34  ? 109 THR   A O   1 
ATOM   865  C CB  . THR   A 1 110 ? 6.009   -11.937 25.327  1.00 36.39  ? 109 THR   A CB  1 
ATOM   866  O OG1 . THR   A 1 110 ? 5.684   -10.541 25.271  1.00 34.74  ? 109 THR   A OG1 1 
ATOM   867  C CG2 . THR   A 1 110 ? 6.699   -12.402 24.052  1.00 35.76  ? 109 THR   A CG2 1 
ATOM   868  N N   . ARG   A 1 111 ? 5.646   -14.779 26.548  1.00 36.06  ? 110 ARG   A N   1 
ATOM   869  C CA  . ARG   A 1 111 ? 6.023   -16.186 26.589  1.00 34.84  ? 110 ARG   A CA  1 
ATOM   870  C C   . ARG   A 1 111 ? 4.812   -17.093 26.444  1.00 34.59  ? 110 ARG   A C   1 
ATOM   871  O O   . ARG   A 1 111 ? 4.869   -18.099 25.744  1.00 38.69  ? 110 ARG   A O   1 
ATOM   872  C CB  . ARG   A 1 111 ? 6.781   -16.469 27.889  1.00 39.69  ? 110 ARG   A CB  1 
ATOM   873  C CG  . ARG   A 1 111 ? 7.245   -17.914 27.987  1.00 41.79  ? 110 ARG   A CG  1 
ATOM   874  C CD  . ARG   A 1 111 ? 8.087   -18.083 29.224  1.00 41.21  ? 110 ARG   A CD  1 
ATOM   875  N NE  . ARG   A 1 111 ? 9.338   -17.356 29.077  1.00 39.71  ? 110 ARG   A NE  1 
ATOM   876  C CZ  . ARG   A 1 111 ? 9.734   -16.283 29.755  1.00 37.03  ? 110 ARG   A CZ  1 
ATOM   877  N NH1 . ARG   A 1 111 ? 8.930   -15.698 30.611  1.00 43.07  ? 110 ARG   A NH1 1 
ATOM   878  N NH2 . ARG   A 1 111 ? 10.936  -15.763 29.511  1.00 40.91  ? 110 ARG   A NH2 1 
ATOM   879  N N   . VAL   A 1 112 ? 3.702   -16.789 27.136  1.00 41.00  ? 111 VAL   A N   1 
ATOM   880  C CA  . VAL   A 1 112 ? 2.525   -17.638 26.992  1.00 38.64  ? 111 VAL   A CA  1 
ATOM   881  C C   . VAL   A 1 112 ? 2.168   -17.730 25.499  1.00 39.54  ? 111 VAL   A C   1 
ATOM   882  O O   . VAL   A 1 112 ? 1.914   -18.806 24.942  1.00 42.95  ? 111 VAL   A O   1 
ATOM   883  C CB  . VAL   A 1 112 ? 1.322   -17.123 27.798  1.00 45.08  ? 111 VAL   A CB  1 
ATOM   884  C CG1 . VAL   A 1 112 ? 0.118   -18.012 27.610  1.00 50.38  ? 111 VAL   A CG1 1 
ATOM   885  C CG2 . VAL   A 1 112 ? 1.611   -16.940 29.277  1.00 45.62  ? 111 VAL   A CG2 1 
ATOM   886  N N   . VAL   A 1 113 ? 2.108   -16.559 24.847  1.00 39.02  ? 112 VAL   A N   1 
ATOM   887  C CA  . VAL   A 1 113 ? 1.633   -16.444 23.476  1.00 36.58  ? 112 VAL   A CA  1 
ATOM   888  C C   . VAL   A 1 113 ? 2.658   -17.076 22.541  1.00 35.74  ? 112 VAL   A C   1 
ATOM   889  O O   . VAL   A 1 113 ? 2.313   -17.889 21.691  1.00 40.78  ? 112 VAL   A O   1 
ATOM   890  C CB  . VAL   A 1 113 ? 1.371   -14.948 23.166  1.00 44.05  ? 112 VAL   A CB  1 
ATOM   891  C CG1 . VAL   A 1 113 ? 1.448   -14.624 21.691  1.00 45.25  ? 112 VAL   A CG1 1 
ATOM   892  C CG2 . VAL   A 1 113 ? 0.011   -14.507 23.709  1.00 47.99  ? 112 VAL   A CG2 1 
ATOM   893  N N   . PHE   A 1 114 ? 3.931   -16.752 22.759  1.00 35.25  ? 113 PHE   A N   1 
ATOM   894  C CA  . PHE   A 1 114 ? 4.982   -17.172 21.855  1.00 34.67  ? 113 PHE   A CA  1 
ATOM   895  C C   . PHE   A 1 114 ? 5.165   -18.684 21.851  1.00 35.80  ? 113 PHE   A C   1 
ATOM   896  O O   . PHE   A 1 114 ? 5.518   -19.258 20.822  1.00 37.41  ? 113 PHE   A O   1 
ATOM   897  C CB  . PHE   A 1 114 ? 6.313   -16.512 22.219  1.00 34.23  ? 113 PHE   A CB  1 
ATOM   898  C CG  . PHE   A 1 114 ? 7.327   -16.449 21.102  1.00 35.16  ? 113 PHE   A CG  1 
ATOM   899  C CD1 . PHE   A 1 114 ? 7.068   -15.683 19.962  1.00 37.66  ? 113 PHE   A CD1 1 
ATOM   900  C CD2 . PHE   A 1 114 ? 8.550   -17.087 21.199  1.00 35.82  ? 113 PHE   A CD2 1 
ATOM   901  C CE1 . PHE   A 1 114 ? 8.004   -15.581 18.938  1.00 34.78  ? 113 PHE   A CE1 1 
ATOM   902  C CE2 . PHE   A 1 114 ? 9.483   -16.993 20.168  1.00 35.27  ? 113 PHE   A CE2 1 
ATOM   903  C CZ  . PHE   A 1 114 ? 9.210   -16.256 19.044  1.00 34.98  ? 113 PHE   A CZ  1 
ATOM   904  N N   . ARG   A 1 115 ? 4.978   -19.350 22.994  1.00 36.14  ? 114 ARG   A N   1 
ATOM   905  C CA  . ARG   A 1 115 ? 5.183   -20.787 23.034  1.00 36.94  ? 114 ARG   A CA  1 
ATOM   906  C C   . ARG   A 1 115 ? 4.168   -21.464 22.114  1.00 38.14  ? 114 ARG   A C   1 
ATOM   907  O O   . ARG   A 1 115 ? 4.431   -22.517 21.563  1.00 37.16  ? 114 ARG   A O   1 
ATOM   908  C CB  . ARG   A 1 115 ? 5.078   -21.332 24.469  1.00 36.07  ? 114 ARG   A CB  1 
ATOM   909  C CG  . ARG   A 1 115 ? 6.320   -21.078 25.308  1.00 38.62  ? 114 ARG   A CG  1 
ATOM   910  C CD  . ARG   A 1 115 ? 6.119   -21.465 26.786  1.00 37.97  ? 114 ARG   A CD  1 
ATOM   911  N NE  . ARG   A 1 115 ? 5.864   -22.902 26.937  1.00 38.56  ? 114 ARG   A NE  1 
ATOM   912  C CZ  . ARG   A 1 115 ? 6.770   -23.818 27.302  1.00 45.05  ? 114 ARG   A CZ  1 
ATOM   913  N NH1 . ARG   A 1 115 ? 7.996   -23.478 27.673  1.00 44.56  ? 114 ARG   A NH1 1 
ATOM   914  N NH2 . ARG   A 1 115 ? 6.450   -25.093 27.259  1.00 45.33  ? 114 ARG   A NH2 1 
ATOM   915  N N   . GLN   A 1 116 ? 2.976   -20.880 22.015  1.00 37.72  ? 115 GLN   A N   1 
ATOM   916  C CA  . GLN   A 1 116 ? 1.926   -21.419 21.171  1.00 38.79  ? 115 GLN   A CA  1 
ATOM   917  C C   . GLN   A 1 116 ? 2.297   -21.276 19.702  1.00 41.43  ? 115 GLN   A C   1 
ATOM   918  O O   . GLN   A 1 116 ? 2.083   -22.190 18.906  1.00 40.00  ? 115 GLN   A O   1 
ATOM   919  C CB  . GLN   A 1 116 ? 0.596   -20.725 21.451  1.00 43.80  ? 115 GLN   A CB  1 
ATOM   920  C CG  . GLN   A 1 116 ? 0.130   -20.836 22.902  1.00 42.34  ? 115 GLN   A CG  1 
ATOM   921  C CD  . GLN   A 1 116 ? -1.140  -20.064 23.163  1.00 48.96  ? 115 GLN   A CD  1 
ATOM   922  O OE1 . GLN   A 1 116 ? -2.162  -20.287 22.509  1.00 52.91  ? 115 GLN   A OE1 1 
ATOM   923  N NE2 . GLN   A 1 116 ? -1.095  -19.144 24.116  1.00 55.68  ? 115 GLN   A NE2 1 
ATOM   924  N N   . ILE   A 1 117 ? 2.848   -20.113 19.344  1.00 39.23  ? 116 ILE   A N   1 
ATOM   925  C CA  . ILE   A 1 117 ? 3.304   -19.890 17.987  1.00 41.29  ? 116 ILE   A CA  1 
ATOM   926  C C   . ILE   A 1 117 ? 4.400   -20.903 17.625  1.00 36.84  ? 116 ILE   A C   1 
ATOM   927  O O   . ILE   A 1 117 ? 4.442   -21.448 16.515  1.00 37.31  ? 116 ILE   A O   1 
ATOM   928  C CB  . ILE   A 1 117 ? 3.789   -18.429 17.804  1.00 41.88  ? 116 ILE   A CB  1 
ATOM   929  C CG1 . ILE   A 1 117 ? 2.674   -17.413 18.027  1.00 46.24  ? 116 ILE   A CG1 1 
ATOM   930  C CG2 . ILE   A 1 117 ? 4.423   -18.224 16.438  1.00 44.30  ? 116 ILE   A CG2 1 
ATOM   931  C CD1 . ILE   A 1 117 ? 3.177   -15.978 18.132  1.00 45.78  ? 116 ILE   A CD1 1 
ATOM   932  N N   . VAL   A 1 118 ? 5.361   -21.067 18.532  1.00 35.44  ? 117 VAL   A N   1 
ATOM   933  C CA  . VAL   A 1 118 ? 6.484   -21.941 18.283  1.00 41.70  ? 117 VAL   A CA  1 
ATOM   934  C C   . VAL   A 1 118 ? 5.973   -23.365 18.081  1.00 35.61  ? 117 VAL   A C   1 
ATOM   935  O O   . VAL   A 1 118 ? 6.402   -24.052 17.168  1.00 36.71  ? 117 VAL   A O   1 
ATOM   936  C CB  . VAL   A 1 118 ? 7.487   -21.830 19.447  1.00 42.58  ? 117 VAL   A CB  1 
ATOM   937  C CG1 . VAL   A 1 118 ? 8.593   -22.861 19.329  1.00 45.91  ? 117 VAL   A CG1 1 
ATOM   938  C CG2 . VAL   A 1 118 ? 8.100   -20.440 19.502  1.00 42.62  ? 117 VAL   A CG2 1 
ATOM   939  N N   . SER   A 1 119 ? 4.946   -23.720 18.837  1.00 38.33  ? 118 SER   A N   1 
ATOM   940  C CA  . SER   A 1 119 ? 4.352   -25.042 18.740  1.00 41.79  ? 118 SER   A CA  1 
ATOM   941  C C   . SER   A 1 119 ? 3.797   -25.269 17.339  1.00 44.44  ? 118 SER   A C   1 
ATOM   942  O O   . SER   A 1 119 ? 4.129   -26.284 16.696  1.00 40.48  ? 118 SER   A O   1 
ATOM   943  C CB  . SER   A 1 119 ? 3.280   -25.201 19.806  1.00 46.96  ? 118 SER   A CB  1 
ATOM   944  O OG  . SER   A 1 119 ? 2.461   -26.335 19.584  1.00 48.86  ? 118 SER   A OG  1 
ATOM   945  N N   . ALA   A 1 120 ? 2.938   -24.336 16.883  1.00 41.31  ? 119 ALA   A N   1 
ATOM   946  C CA  . ALA   A 1 120 ? 2.359   -24.416 15.544  1.00 43.05  ? 119 ALA   A CA  1 
ATOM   947  C C   . ALA   A 1 120 ? 3.459   -24.504 14.490  1.00 40.55  ? 119 ALA   A C   1 
ATOM   948  O O   . ALA   A 1 120 ? 3.410   -25.320 13.566  1.00 38.55  ? 119 ALA   A O   1 
ATOM   949  C CB  . ALA   A 1 120 ? 1.495   -23.222 15.250  1.00 47.87  ? 119 ALA   A CB  1 
ATOM   950  N N   . VAL   A 1 121 ? 4.428   -23.602 14.593  1.00 36.45  ? 120 VAL   A N   1 
ATOM   951  C CA  . VAL   A 1 121 ? 5.391   -23.457 13.526  1.00 39.00  ? 120 VAL   A CA  1 
ATOM   952  C C   . VAL   A 1 121 ? 6.363   -24.640 13.540  1.00 37.37  ? 120 VAL   A C   1 
ATOM   953  O O   . VAL   A 1 121 ? 6.734   -25.129 12.477  1.00 35.49  ? 120 VAL   A O   1 
ATOM   954  C CB  . VAL   A 1 121 ? 6.116   -22.106 13.611  1.00 39.33  ? 120 VAL   A CB  1 
ATOM   955  C CG1 . VAL   A 1 121 ? 7.286   -22.005 12.641  1.00 35.38  ? 120 VAL   A CG1 1 
ATOM   956  C CG2 . VAL   A 1 121 ? 5.115   -20.975 13.403  1.00 42.89  ? 120 VAL   A CG2 1 
ATOM   957  N N   . ALA   A 1 122 ? 6.736   -25.104 14.734  1.00 34.76  ? 121 ALA   A N   1 
ATOM   958  C CA  . ALA   A 1 122 ? 7.539   -26.321 14.794  1.00 42.73  ? 121 ALA   A CA  1 
ATOM   959  C C   . ALA   A 1 122 ? 6.784   -27.477 14.137  1.00 37.47  ? 121 ALA   A C   1 
ATOM   960  O O   . ALA   A 1 122 ? 7.348   -28.230 13.360  1.00 41.72  ? 121 ALA   A O   1 
ATOM   961  C CB  . ALA   A 1 122 ? 7.929   -26.624 16.219  1.00 41.07  ? 121 ALA   A CB  1 
ATOM   962  N N   . TYR   A 1 123 ? 5.480   -27.605 14.390  1.00 42.99  ? 122 TYR   A N   1 
ATOM   963  C CA  . TYR   A 1 123 ? 4.731   -28.695 13.784  1.00 41.56  ? 122 TYR   A CA  1 
ATOM   964  C C   . TYR   A 1 123 ? 4.723   -28.599 12.260  1.00 43.02  ? 122 TYR   A C   1 
ATOM   965  O O   . TYR   A 1 123 ? 4.874   -29.588 11.558  1.00 41.59  ? 122 TYR   A O   1 
ATOM   966  C CB  . TYR   A 1 123 ? 3.321   -28.746 14.352  1.00 45.85  ? 122 TYR   A CB  1 
ATOM   967  C CG  . TYR   A 1 123 ? 2.468   -29.800 13.670  1.00 49.79  ? 122 TYR   A CG  1 
ATOM   968  C CD1 . TYR   A 1 123 ? 2.553   -31.154 14.005  1.00 56.79  ? 122 TYR   A CD1 1 
ATOM   969  C CD2 . TYR   A 1 123 ? 1.591   -29.429 12.670  1.00 47.32  ? 122 TYR   A CD2 1 
ATOM   970  C CE1 . TYR   A 1 123 ? 1.764   -32.105 13.371  1.00 53.83  ? 122 TYR   A CE1 1 
ATOM   971  C CE2 . TYR   A 1 123 ? 0.802   -30.359 12.039  1.00 55.26  ? 122 TYR   A CE2 1 
ATOM   972  C CZ  . TYR   A 1 123 ? 0.887   -31.694 12.381  1.00 59.16  ? 122 TYR   A CZ  1 
ATOM   973  O OH  . TYR   A 1 123 ? 0.048   -32.503 11.678  1.00 74.46  ? 122 TYR   A OH  1 
ATOM   974  N N   . VAL   A 1 124 ? 4.487   -27.416 11.719  1.00 37.01  ? 123 VAL   A N   1 
ATOM   975  C CA  . VAL   A 1 124 ? 4.489   -27.221 10.285  1.00 39.35  ? 123 VAL   A CA  1 
ATOM   976  C C   . VAL   A 1 124 ? 5.822   -27.681 9.692   1.00 38.46  ? 123 VAL   A C   1 
ATOM   977  O O   . VAL   A 1 124 ? 5.848   -28.376 8.686   1.00 38.85  ? 123 VAL   A O   1 
ATOM   978  C CB  . VAL   A 1 124 ? 4.223   -25.725 10.003  1.00 41.78  ? 123 VAL   A CB  1 
ATOM   979  C CG1 . VAL   A 1 124 ? 4.534   -25.370 8.576   1.00 41.09  ? 123 VAL   A CG1 1 
ATOM   980  C CG2 . VAL   A 1 124 ? 2.797   -25.341 10.383  1.00 43.99  ? 123 VAL   A CG2 1 
ATOM   981  N N   . HIS   A 1 125 ? 6.927   -27.234 10.293  1.00 38.21  ? 124 HIS   A N   1 
ATOM   982  C CA  . HIS   A 1 125 ? 8.266   -27.524 9.799   1.00 40.37  ? 124 HIS   A CA  1 
ATOM   983  C C   . HIS   A 1 125 ? 8.520   -29.037 9.866   1.00 45.37  ? 124 HIS   A C   1 
ATOM   984  O O   . HIS   A 1 125 ? 9.118   -29.603 8.959   1.00 44.92  ? 124 HIS   A O   1 
ATOM   985  C CB  . HIS   A 1 125 ? 9.306   -26.747 10.627  1.00 42.33  ? 124 HIS   A CB  1 
ATOM   986  C CG  . HIS   A 1 125 ? 9.276   -25.270 10.381  1.00 44.21  ? 124 HIS   A CG  1 
ATOM   987  N ND1 . HIS   A 1 125 ? 10.183  -24.373 10.921  1.00 41.60  ? 124 HIS   A ND1 1 
ATOM   988  C CD2 . HIS   A 1 125 ? 8.427   -24.531 9.625   1.00 43.03  ? 124 HIS   A CD2 1 
ATOM   989  C CE1 . HIS   A 1 125 ? 9.890   -23.148 10.482  1.00 40.90  ? 124 HIS   A CE1 1 
ATOM   990  N NE2 . HIS   A 1 125 ? 8.823   -23.212 9.717   1.00 41.77  ? 124 HIS   A NE2 1 
ATOM   991  N N   . SER   A 1 126 ? 8.027   -29.685 10.924  1.00 44.89  ? 125 SER   A N   1 
ATOM   992  C CA  . SER   A 1 126 ? 8.251   -31.107 11.109  1.00 54.19  ? 125 SER   A CA  1 
ATOM   993  C C   . SER   A 1 126 ? 7.544   -31.899 10.015  1.00 54.05  ? 125 SER   A C   1 
ATOM   994  O O   . SER   A 1 126 ? 7.940   -33.016 9.736   1.00 55.42  ? 125 SER   A O   1 
ATOM   995  C CB  . SER   A 1 126 ? 7.811   -31.565 12.455  1.00 43.12  ? 125 SER   A CB  1 
ATOM   996  O OG  . SER   A 1 126 ? 6.403   -31.723 12.434  1.00 47.32  ? 125 SER   A OG  1 
ATOM   997  N N   . GLN   A 1 127 ? 6.499   -31.332 9.399   1.00 50.63  ? 126 GLN   A N   1 
ATOM   998  C CA  . GLN   A 1 127 ? 5.785   -32.020 8.333   1.00 46.32  ? 126 GLN   A CA  1 
ATOM   999  C C   . GLN   A 1 127 ? 6.408   -31.676 6.991   1.00 42.89  ? 126 GLN   A C   1 
ATOM   1000 O O   . GLN   A 1 127 ? 5.859   -31.975 5.954   1.00 51.35  ? 126 GLN   A O   1 
ATOM   1001 C CB  . GLN   A 1 127 ? 4.294   -31.674 8.363   1.00 47.81  ? 126 GLN   A CB  1 
ATOM   1002 C CG  . GLN   A 1 127 ? 3.642   -32.006 9.693   1.00 51.76  ? 126 GLN   A CG  1 
ATOM   1003 C CD  . GLN   A 1 127 ? 3.399   -33.493 9.862   1.00 59.54  ? 126 GLN   A CD  1 
ATOM   1004 O OE1 . GLN   A 1 127 ? 4.110   -34.180 10.598  1.00 57.94  ? 126 GLN   A OE1 1 
ATOM   1005 N NE2 . GLN   A 1 127 ? 2.384   -34.000 9.182   1.00 64.70  ? 126 GLN   A NE2 1 
ATOM   1006 N N   . GLY   A 1 128 ? 7.526   -30.971 7.013   1.00 43.21  ? 127 GLY   A N   1 
ATOM   1007 C CA  . GLY   A 1 128 ? 8.209   -30.624 5.787   1.00 50.17  ? 127 GLY   A CA  1 
ATOM   1008 C C   . GLY   A 1 128 ? 7.596   -29.407 5.099   1.00 53.33  ? 127 GLY   A C   1 
ATOM   1009 O O   . GLY   A 1 128 ? 7.858   -29.188 3.913   1.00 45.85  ? 127 GLY   A O   1 
ATOM   1010 N N   . TYR   A 1 129 ? 6.842   -28.584 5.845   1.00 52.29  ? 128 TYR   A N   1 
ATOM   1011 C CA  . TYR   A 1 129 ? 6.312   -27.363 5.254   1.00 50.87  ? 128 TYR   A CA  1 
ATOM   1012 C C   . TYR   A 1 129 ? 6.851   -26.135 5.994   1.00 54.93  ? 128 TYR   A C   1 
ATOM   1013 O O   . TYR   A 1 129 ? 7.500   -26.252 7.032   1.00 51.45  ? 128 TYR   A O   1 
ATOM   1014 C CB  . TYR   A 1 129 ? 4.784   -27.360 5.240   1.00 51.09  ? 128 TYR   A CB  1 
ATOM   1015 C CG  . TYR   A 1 129 ? 4.082   -28.629 4.778   1.00 48.86  ? 128 TYR   A CG  1 
ATOM   1016 C CD1 . TYR   A 1 129 ? 4.160   -29.109 3.472   1.00 55.59  ? 128 TYR   A CD1 1 
ATOM   1017 C CD2 . TYR   A 1 129 ? 3.248   -29.292 5.660   1.00 56.50  ? 128 TYR   A CD2 1 
ATOM   1018 C CE1 . TYR   A 1 129 ? 3.464   -30.251 3.079   1.00 54.57  ? 128 TYR   A CE1 1 
ATOM   1019 C CE2 . TYR   A 1 129 ? 2.550   -30.426 5.290   1.00 61.04  ? 128 TYR   A CE2 1 
ATOM   1020 C CZ  . TYR   A 1 129 ? 2.658   -30.910 4.001   1.00 59.77  ? 128 TYR   A CZ  1 
ATOM   1021 O OH  . TYR   A 1 129 ? 1.892   -32.022 3.785   1.00 63.22  ? 128 TYR   A OH  1 
ATOM   1022 N N   . ALA   A 1 130 ? 6.566   -24.944 5.444   1.00 56.65  ? 129 ALA   A N   1 
ATOM   1023 C CA  . ALA   A 1 130 ? 6.850   -23.682 6.119   1.00 55.07  ? 129 ALA   A CA  1 
ATOM   1024 C C   . ALA   A 1 130 ? 5.624   -22.781 5.981   1.00 62.70  ? 129 ALA   A C   1 
ATOM   1025 O O   . ALA   A 1 130 ? 4.741   -23.079 5.172   1.00 55.73  ? 129 ALA   A O   1 
ATOM   1026 C CB  . ALA   A 1 130 ? 8.094   -23.057 5.546   1.00 51.55  ? 129 ALA   A CB  1 
ATOM   1027 N N   . HIS   A 1 131 ? 5.544   -21.697 6.774   1.00 51.71  ? 130 HIS   A N   1 
ATOM   1028 C CA  . HIS   A 1 131 ? 4.376   -20.834 6.677   1.00 46.92  ? 130 HIS   A CA  1 
ATOM   1029 C C   . HIS   A 1 131 ? 4.664   -19.752 5.646   1.00 46.37  ? 130 HIS   A C   1 
ATOM   1030 O O   . HIS   A 1 131 ? 3.824   -19.505 4.787   1.00 53.38  ? 130 HIS   A O   1 
ATOM   1031 C CB  . HIS   A 1 131 ? 3.910   -20.337 8.045   1.00 46.44  ? 130 HIS   A CB  1 
ATOM   1032 C CG  . HIS   A 1 131 ? 2.706   -19.477 7.944   1.00 43.72  ? 130 HIS   A CG  1 
ATOM   1033 N ND1 . HIS   A 1 131 ? 2.768   -18.159 7.525   1.00 44.88  ? 130 HIS   A ND1 1 
ATOM   1034 C CD2 . HIS   A 1 131 ? 1.417   -19.744 8.188   1.00 47.50  ? 130 HIS   A CD2 1 
ATOM   1035 C CE1 . HIS   A 1 131 ? 1.543   -17.652 7.541   1.00 49.80  ? 130 HIS   A CE1 1 
ATOM   1036 N NE2 . HIS   A 1 131 ? 0.702   -18.601 7.955   1.00 46.34  ? 130 HIS   A NE2 1 
ATOM   1037 N N   . ARG   A 1 132 ? 5.830   -19.104 5.780   1.00 44.91  ? 131 ARG   A N   1 
ATOM   1038 C CA  . ARG   A 1 132 ? 6.390   -18.147 4.827   1.00 50.85  ? 131 ARG   A CA  1 
ATOM   1039 C C   . ARG   A 1 132 ? 5.753   -16.759 4.938   1.00 46.40  ? 131 ARG   A C   1 
ATOM   1040 O O   . ARG   A 1 132 ? 6.225   -15.825 4.289   1.00 50.80  ? 131 ARG   A O   1 
ATOM   1041 C CB  . ARG   A 1 132 ? 6.299   -18.550 3.353   1.00 56.03  ? 131 ARG   A CB  1 
ATOM   1042 C CG  . ARG   A 1 132 ? 6.913   -19.903 3.071   1.00 64.75  ? 131 ARG   A CG  1 
ATOM   1043 C CD  . ARG   A 1 132 ? 7.121   -20.099 1.578   1.00 70.68  ? 131 ARG   A CD  1 
ATOM   1044 N NE  . ARG   A 1 132 ? 7.889   -21.334 1.382   1.00 73.73  ? 131 ARG   A NE  1 
ATOM   1045 C CZ  . ARG   A 1 132 ? 7.379   -22.529 1.644   1.00 67.46  ? 131 ARG   A CZ  1 
ATOM   1046 N NH1 . ARG   A 1 132 ? 6.089   -22.618 1.905   1.00 71.31  ? 131 ARG   A NH1 1 
ATOM   1047 N NH2 . ARG   A 1 132 ? 8.132   -23.619 1.626   1.00 64.65  ? 131 ARG   A NH2 1 
ATOM   1048 N N   . ASP   A 1 133 ? 4.715   -16.608 5.766   1.00 46.10  ? 132 ASP   A N   1 
ATOM   1049 C CA  . ASP   A 1 133 ? 4.114   -15.296 5.956   1.00 54.29  ? 132 ASP   A CA  1 
ATOM   1050 C C   . ASP   A 1 133 ? 3.681   -15.106 7.409   1.00 47.26  ? 132 ASP   A C   1 
ATOM   1051 O O   . ASP   A 1 133 ? 2.564   -14.683 7.684   1.00 47.33  ? 132 ASP   A O   1 
ATOM   1052 C CB  . ASP   A 1 133 ? 2.995   -15.061 4.945   1.00 59.33  ? 132 ASP   A CB  1 
ATOM   1053 C CG  . ASP   A 1 133 ? 2.417   -13.651 4.961   1.00 67.40  ? 132 ASP   A CG  1 
ATOM   1054 O OD1 . ASP   A 1 133 ? 3.213   -12.706 5.141   1.00 52.15  ? 132 ASP   A OD1 1 
ATOM   1055 O OD2 . ASP   A 1 133 ? 1.178   -13.511 4.805   1.00 66.65  ? 132 ASP   A OD2 1 
ATOM   1056 N N   . LEU   A 1 134 ? 4.576   -15.371 8.364   1.00 41.78  ? 133 LEU   A N   1 
ATOM   1057 C CA  . LEU   A 1 134 ? 4.176   -15.203 9.753   1.00 40.68  ? 133 LEU   A CA  1 
ATOM   1058 C C   . LEU   A 1 134 ? 4.114   -13.712 10.066  1.00 46.68  ? 133 LEU   A C   1 
ATOM   1059 O O   . LEU   A 1 134 ? 5.020   -12.943 9.686   1.00 42.05  ? 133 LEU   A O   1 
ATOM   1060 C CB  . LEU   A 1 134 ? 5.138   -15.941 10.682  1.00 39.40  ? 133 LEU   A CB  1 
ATOM   1061 C CG  . LEU   A 1 134 ? 5.103   -17.466 10.492  1.00 40.78  ? 133 LEU   A CG  1 
ATOM   1062 C CD1 . LEU   A 1 134 ? 6.334   -18.122 11.074  1.00 44.37  ? 133 LEU   A CD1 1 
ATOM   1063 C CD2 . LEU   A 1 134 ? 3.823   -18.018 11.101  1.00 41.48  ? 133 LEU   A CD2 1 
ATOM   1064 N N   . LYS   A 1 135 ? 3.016   -13.338 10.734  1.00 44.19  ? 134 LYS   A N   1 
ATOM   1065 C CA  . LYS   A 1 135 ? 2.790   -11.967 11.167  1.00 44.08  ? 134 LYS   A CA  1 
ATOM   1066 C C   . LYS   A 1 135 ? 1.565   -11.992 12.064  1.00 43.11  ? 134 LYS   A C   1 
ATOM   1067 O O   . LYS   A 1 135 ? 0.847   -12.995 12.053  1.00 40.36  ? 134 LYS   A O   1 
ATOM   1068 C CB  . LYS   A 1 135 ? 2.673   -11.009 9.984   1.00 47.94  ? 134 LYS   A CB  1 
ATOM   1069 C CG  . LYS   A 1 135 ? 1.531   -11.253 9.027   1.00 53.42  ? 134 LYS   A CG  1 
ATOM   1070 C CD  . LYS   A 1 135 ? 1.787   -10.645 7.652   1.00 60.26  ? 134 LYS   A CD  1 
ATOM   1071 C CE  . LYS   A 1 135 ? 0.506   -10.465 6.917   1.00 70.54  ? 134 LYS   A CE  1 
ATOM   1072 N NZ  . LYS   A 1 135 ? 0.730   -10.524 5.474   1.00 79.96  ? 134 LYS   A NZ  1 
ATOM   1073 N N   . PRO   A 1 136 ? 1.353   -10.950 12.908  1.00 47.15  ? 135 PRO   A N   1 
ATOM   1074 C CA  . PRO   A 1 136 ? 0.304   -10.962 13.929  1.00 44.36  ? 135 PRO   A CA  1 
ATOM   1075 C C   . PRO   A 1 136 ? -1.109  -11.022 13.359  1.00 43.45  ? 135 PRO   A C   1 
ATOM   1076 O O   . PRO   A 1 136 ? -2.042  -11.432 14.045  1.00 44.49  ? 135 PRO   A O   1 
ATOM   1077 C CB  . PRO   A 1 136 ? 0.517   -9.690  14.754  1.00 48.06  ? 135 PRO   A CB  1 
ATOM   1078 C CG  . PRO   A 1 136 ? 1.824   -9.107  14.274  1.00 48.51  ? 135 PRO   A CG  1 
ATOM   1079 C CD  . PRO   A 1 136 ? 2.162   -9.723  12.953  1.00 45.14  ? 135 PRO   A CD  1 
ATOM   1080 N N   . GLU   A 1 137 ? -1.244  -10.619 12.099  1.00 41.30  ? 136 GLU   A N   1 
ATOM   1081 C CA  . GLU   A 1 137 ? -2.499  -10.720 11.388  1.00 44.97  ? 136 GLU   A CA  1 
ATOM   1082 C C   . GLU   A 1 137 ? -2.839  -12.181 11.081  1.00 45.66  ? 136 GLU   A C   1 
ATOM   1083 O O   . GLU   A 1 137 ? -3.991  -12.495 10.810  1.00 46.77  ? 136 GLU   A O   1 
ATOM   1084 C CB  . GLU   A 1 137 ? -2.437  -9.916  10.086  1.00 55.14  ? 136 GLU   A CB  1 
ATOM   1085 C CG  . GLU   A 1 137 ? -2.256  -8.409  10.283  1.00 60.08  ? 136 GLU   A CG  1 
ATOM   1086 C CD  . GLU   A 1 137 ? -0.832  -7.859  10.333  1.00 65.08  ? 136 GLU   A CD  1 
ATOM   1087 O OE1 . GLU   A 1 137 ? 0.120   -8.649  10.511  1.00 55.60  ? 136 GLU   A OE1 1 
ATOM   1088 O OE2 . GLU   A 1 137 ? -0.664  -6.617  10.177  1.00 60.98  ? 136 GLU   A OE2 1 
ATOM   1089 N N   . ASN   A 1 138 ? -1.842  -13.075 11.066  1.00 45.17  ? 137 ASN   A N   1 
ATOM   1090 C CA  . ASN   A 1 138 ? -2.084  -14.457 10.681  1.00 42.46  ? 137 ASN   A CA  1 
ATOM   1091 C C   . ASN   A 1 138 ? -2.221  -15.330 11.915  1.00 41.63  ? 137 ASN   A C   1 
ATOM   1092 O O   . ASN   A 1 138 ? -2.137  -16.549 11.821  1.00 43.89  ? 137 ASN   A O   1 
ATOM   1093 C CB  . ASN   A 1 138 ? -0.988  -15.004 9.782   1.00 42.61  ? 137 ASN   A CB  1 
ATOM   1094 C CG  . ASN   A 1 138 ? -1.164  -14.520 8.367   1.00 52.27  ? 137 ASN   A CG  1 
ATOM   1095 O OD1 . ASN   A 1 138 ? -2.299  -14.388 7.902   1.00 57.40  ? 137 ASN   A OD1 1 
ATOM   1096 N ND2 . ASN   A 1 138 ? -0.071  -14.251 7.673   1.00 57.18  ? 137 ASN   A ND2 1 
ATOM   1097 N N   . LEU   A 1 139 ? -2.359  -14.691 13.076  1.00 41.62  ? 138 LEU   A N   1 
ATOM   1098 C CA  . LEU   A 1 139 ? -2.504  -15.420 14.317  1.00 39.89  ? 138 LEU   A CA  1 
ATOM   1099 C C   . LEU   A 1 139 ? -3.761  -14.907 15.000  1.00 46.76  ? 138 LEU   A C   1 
ATOM   1100 O O   . LEU   A 1 139 ? -3.855  -13.719 15.344  1.00 44.69  ? 138 LEU   A O   1 
ATOM   1101 C CB  . LEU   A 1 139 ? -1.227  -15.233 15.142  1.00 45.67  ? 138 LEU   A CB  1 
ATOM   1102 C CG  . LEU   A 1 139 ? 0.033   -15.906 14.577  1.00 44.10  ? 138 LEU   A CG  1 
ATOM   1103 C CD1 . LEU   A 1 139 ? 1.267   -15.178 15.057  1.00 45.87  ? 138 LEU   A CD1 1 
ATOM   1104 C CD2 . LEU   A 1 139 ? 0.054   -17.364 15.046  1.00 52.65  ? 138 LEU   A CD2 1 
ATOM   1105 N N   . LEU   A 1 140 ? -4.728  -15.815 15.130  1.00 42.32  ? 139 LEU   A N   1 
ATOM   1106 C CA  . LEU   A 1 140 ? -6.033  -15.510 15.677  1.00 42.54  ? 139 LEU   A CA  1 
ATOM   1107 C C   . LEU   A 1 140 ? -6.212  -16.263 16.975  1.00 42.03  ? 139 LEU   A C   1 
ATOM   1108 O O   . LEU   A 1 140 ? -5.624  -17.312 17.191  1.00 49.91  ? 139 LEU   A O   1 
ATOM   1109 C CB  . LEU   A 1 140 ? -7.133  -15.887 14.698  1.00 44.07  ? 139 LEU   A CB  1 
ATOM   1110 C CG  . LEU   A 1 140 ? -6.939  -15.455 13.246  1.00 45.24  ? 139 LEU   A CG  1 
ATOM   1111 C CD1 . LEU   A 1 140 ? -8.154  -15.929 12.435  1.00 55.88  ? 139 LEU   A CD1 1 
ATOM   1112 C CD2 . LEU   A 1 140 ? -6.751  -13.975 13.093  1.00 47.12  ? 139 LEU   A CD2 1 
ATOM   1113 N N   . PHE   A 1 141 ? -7.032  -15.686 17.841  1.00 43.35  ? 140 PHE   A N   1 
ATOM   1114 C CA  . PHE   A 1 141 ? -7.398  -16.314 19.089  1.00 43.99  ? 140 PHE   A CA  1 
ATOM   1115 C C   . PHE   A 1 141 ? -8.732  -17.032 18.917  1.00 46.28  ? 140 PHE   A C   1 
ATOM   1116 O O   . PHE   A 1 141 ? -9.599  -16.543 18.215  1.00 43.44  ? 140 PHE   A O   1 
ATOM   1117 C CB  . PHE   A 1 141 ? -7.538  -15.266 20.188  1.00 49.28  ? 140 PHE   A CB  1 
ATOM   1118 C CG  . PHE   A 1 141 ? -6.216  -14.718 20.694  1.00 44.56  ? 140 PHE   A CG  1 
ATOM   1119 C CD1 . PHE   A 1 141 ? -5.404  -15.503 21.501  1.00 46.35  ? 140 PHE   A CD1 1 
ATOM   1120 C CD2 . PHE   A 1 141 ? -5.830  -13.424 20.388  1.00 47.17  ? 140 PHE   A CD2 1 
ATOM   1121 C CE1 . PHE   A 1 141 ? -4.212  -14.996 21.984  1.00 55.49  ? 140 PHE   A CE1 1 
ATOM   1122 C CE2 . PHE   A 1 141 ? -4.637  -12.926 20.859  1.00 49.66  ? 140 PHE   A CE2 1 
ATOM   1123 C CZ  . PHE   A 1 141 ? -3.830  -13.707 21.654  1.00 56.22  ? 140 PHE   A CZ  1 
ATOM   1124 N N   . ASP   A 1 142 ? -8.879  -18.165 19.601  1.00 49.07  ? 141 ASP   A N   1 
ATOM   1125 C CA  . ASP   A 1 142 ? -10.132 -18.894 19.649  1.00 54.33  ? 141 ASP   A CA  1 
ATOM   1126 C C   . ASP   A 1 142 ? -10.927 -18.346 20.837  1.00 57.98  ? 141 ASP   A C   1 
ATOM   1127 O O   . ASP   A 1 142 ? -10.492 -17.388 21.469  1.00 56.88  ? 141 ASP   A O   1 
ATOM   1128 C CB  . ASP   A 1 142 ? -9.869  -20.394 19.664  1.00 56.91  ? 141 ASP   A CB  1 
ATOM   1129 C CG  . ASP   A 1 142 ? -9.269  -20.991 20.935  1.00 57.08  ? 141 ASP   A CG  1 
ATOM   1130 O OD1 . ASP   A 1 142 ? -9.293  -20.343 21.993  1.00 60.82  ? 141 ASP   A OD1 1 
ATOM   1131 O OD2 . ASP   A 1 142 ? -8.747  -22.111 20.856  1.00 61.72  ? 141 ASP   A OD2 1 
ATOM   1132 N N   . GLU   A 1 143 ? -12.068 -18.986 21.134  1.00 77.01  ? 142 GLU   A N   1 
ATOM   1133 C CA  . GLU   A 1 143 ? -12.916 -18.678 22.278  1.00 78.42  ? 142 GLU   A CA  1 
ATOM   1134 C C   . GLU   A 1 143 ? -12.123 -18.519 23.576  1.00 69.67  ? 142 GLU   A C   1 
ATOM   1135 O O   . GLU   A 1 143 ? -12.529 -17.741 24.433  1.00 64.94  ? 142 GLU   A O   1 
ATOM   1136 C CB  . GLU   A 1 143 ? -13.898 -19.820 22.547  1.00 88.24  ? 142 GLU   A CB  1 
ATOM   1137 C CG  . GLU   A 1 143 ? -15.037 -19.958 21.544  1.00 91.95  ? 142 GLU   A CG  1 
ATOM   1138 C CD  . GLU   A 1 143 ? -16.230 -20.657 22.183  1.00 104.28 ? 142 GLU   A CD  1 
ATOM   1139 O OE1 . GLU   A 1 143 ? -16.003 -21.633 22.929  1.00 113.26 ? 142 GLU   A OE1 1 
ATOM   1140 O OE2 . GLU   A 1 143 ? -17.383 -20.228 21.960  1.00 109.79 ? 142 GLU   A OE2 1 
ATOM   1141 N N   . TYR   A 1 144 ? -11.009 -19.257 23.712  1.00 67.27  ? 143 TYR   A N   1 
ATOM   1142 C CA  . TYR   A 1 144 ? -10.294 -19.422 24.974  1.00 74.18  ? 143 TYR   A CA  1 
ATOM   1143 C C   . TYR   A 1 144 ? -8.956  -18.684 24.997  1.00 65.74  ? 143 TYR   A C   1 
ATOM   1144 O O   . TYR   A 1 144 ? -8.060  -19.051 25.757  1.00 62.11  ? 143 TYR   A O   1 
ATOM   1145 C CB  . TYR   A 1 144 ? -10.046 -20.919 25.188  1.00 73.57  ? 143 TYR   A CB  1 
ATOM   1146 C CG  . TYR   A 1 144 ? -11.335 -21.705 25.348  1.00 88.78  ? 143 TYR   A CG  1 
ATOM   1147 C CD1 . TYR   A 1 144 ? -12.423 -21.147 26.019  1.00 94.37  ? 143 TYR   A CD1 1 
ATOM   1148 C CD2 . TYR   A 1 144 ? -11.470 -22.990 24.831  1.00 100.23 ? 143 TYR   A CD2 1 
ATOM   1149 C CE1 . TYR   A 1 144 ? -13.610 -21.836 26.169  1.00 94.84  ? 143 TYR   A CE1 1 
ATOM   1150 C CE2 . TYR   A 1 144 ? -12.652 -23.696 24.990  1.00 101.76 ? 143 TYR   A CE2 1 
ATOM   1151 C CZ  . TYR   A 1 144 ? -13.722 -23.110 25.651  1.00 99.67  ? 143 TYR   A CZ  1 
ATOM   1152 O OH  . TYR   A 1 144 ? -14.911 -23.741 25.831  1.00 108.83 ? 143 TYR   A OH  1 
ATOM   1153 N N   . HIS   A 1 145 ? -8.827  -17.655 24.159  1.00 66.34  ? 144 HIS   A N   1 
ATOM   1154 C CA  . HIS   A 1 145 ? -7.580  -16.921 24.013  1.00 68.58  ? 144 HIS   A CA  1 
ATOM   1155 C C   . HIS   A 1 145 ? -6.415  -17.880 23.699  1.00 56.09  ? 144 HIS   A C   1 
ATOM   1156 O O   . HIS   A 1 145 ? -5.296  -17.676 24.167  1.00 52.03  ? 144 HIS   A O   1 
ATOM   1157 C CB  . HIS   A 1 145 ? -7.371  -16.031 25.252  1.00 66.79  ? 144 HIS   A CB  1 
ATOM   1158 C CG  . HIS   A 1 145 ? -6.742  -14.698 24.962  1.00 75.93  ? 144 HIS   A CG  1 
ATOM   1159 N ND1 . HIS   A 1 145 ? -7.257  -13.760 24.080  1.00 74.44  ? 144 HIS   A ND1 1 
ATOM   1160 C CD2 . HIS   A 1 145 ? -5.652  -14.135 25.507  1.00 76.94  ? 144 HIS   A CD2 1 
ATOM   1161 C CE1 . HIS   A 1 145 ? -6.492  -12.678 24.092  1.00 73.31  ? 144 HIS   A CE1 1 
ATOM   1162 N NE2 . HIS   A 1 145 ? -5.506  -12.889 24.946  1.00 79.09  ? 144 HIS   A NE2 1 
ATOM   1163 N N   . LYS   A 1 146 ? -6.666  -18.923 22.896  1.00 52.99  ? 145 LYS   A N   1 
ATOM   1164 C CA  . LYS   A 1 146 ? -5.598  -19.746 22.335  1.00 60.99  ? 145 LYS   A CA  1 
ATOM   1165 C C   . LYS   A 1 146 ? -5.354  -19.356 20.869  1.00 47.27  ? 145 LYS   A C   1 
ATOM   1166 O O   . LYS   A 1 146 ? -6.307  -19.188 20.105  1.00 43.77  ? 145 LYS   A O   1 
ATOM   1167 C CB  . LYS   A 1 146 ? -5.923  -21.243 22.473  1.00 72.13  ? 145 LYS   A CB  1 
ATOM   1168 C CG  . LYS   A 1 146 ? -5.095  -22.028 23.494  1.00 87.18  ? 145 LYS   A CG  1 
ATOM   1169 C CD  . LYS   A 1 146 ? -5.109  -21.467 24.913  1.00 91.21  ? 145 LYS   A CD  1 
ATOM   1170 C CE  . LYS   A 1 146 ? -3.966  -21.955 25.738  1.00 94.23  ? 145 LYS   A CE  1 
ATOM   1171 N NZ  . LYS   A 1 146 ? -3.827  -21.122 26.933  1.00 98.28  ? 145 LYS   A NZ  1 
ATOM   1172 N N   . LEU   A 1 147 ? -4.074  -19.322 20.472  1.00 45.19  ? 146 LEU   A N   1 
ATOM   1173 C CA  . LEU   A 1 147 ? -3.667  -18.936 19.127  1.00 43.31  ? 146 LEU   A CA  1 
ATOM   1174 C C   . LEU   A 1 147 ? -3.864  -20.055 18.111  1.00 43.90  ? 146 LEU   A C   1 
ATOM   1175 O O   . LEU   A 1 147 ? -3.573  -21.219 18.360  1.00 43.43  ? 146 LEU   A O   1 
ATOM   1176 C CB  . LEU   A 1 147 ? -2.215  -18.459 19.125  1.00 50.00  ? 146 LEU   A CB  1 
ATOM   1177 C CG  . LEU   A 1 147 ? -2.020  -17.035 19.657  1.00 55.09  ? 146 LEU   A CG  1 
ATOM   1178 C CD1 . LEU   A 1 147 ? -0.570  -16.623 19.660  1.00 61.84  ? 146 LEU   A CD1 1 
ATOM   1179 C CD2 . LEU   A 1 147 ? -2.849  -16.065 18.816  1.00 55.39  ? 146 LEU   A CD2 1 
ATOM   1180 N N   . LYS   A 1 148 ? -4.350  -19.649 16.936  1.00 37.31  ? 147 LYS   A N   1 
ATOM   1181 C CA  . LYS   A 1 148 ? -4.453  -20.499 15.773  1.00 42.65  ? 147 LYS   A CA  1 
ATOM   1182 C C   . LYS   A 1 148 ? -3.806  -19.796 14.590  1.00 43.75  ? 147 LYS   A C   1 
ATOM   1183 O O   . LYS   A 1 148 ? -4.177  -18.667 14.264  1.00 41.80  ? 147 LYS   A O   1 
ATOM   1184 C CB  . LYS   A 1 148 ? -5.936  -20.678 15.444  1.00 48.54  ? 147 LYS   A CB  1 
ATOM   1185 C CG  . LYS   A 1 148 ? -6.789  -21.191 16.580  1.00 49.61  ? 147 LYS   A CG  1 
ATOM   1186 C CD  . LYS   A 1 148 ? -6.620  -22.680 16.779  1.00 52.94  ? 147 LYS   A CD  1 
ATOM   1187 C CE  . LYS   A 1 148 ? -7.507  -23.189 17.880  1.00 61.07  ? 147 LYS   A CE  1 
ATOM   1188 N NZ  . LYS   A 1 148 ? -7.451  -24.654 17.909  1.00 60.39  ? 147 LYS   A NZ  1 
ATOM   1189 N N   . LEU   A 1 149 ? -2.899  -20.504 13.924  1.00 39.35  ? 148 LEU   A N   1 
ATOM   1190 C CA  . LEU   A 1 149 ? -2.226  -20.000 12.751  1.00 39.16  ? 148 LEU   A CA  1 
ATOM   1191 C C   . LEU   A 1 149 ? -3.162  -20.157 11.560  1.00 42.88  ? 148 LEU   A C   1 
ATOM   1192 O O   . LEU   A 1 149 ? -3.816  -21.189 11.405  1.00 40.32  ? 148 LEU   A O   1 
ATOM   1193 C CB  . LEU   A 1 149 ? -0.914  -20.783 12.651  1.00 40.38  ? 148 LEU   A CB  1 
ATOM   1194 C CG  . LEU   A 1 149 ? 0.057   -20.383 11.535  1.00 49.03  ? 148 LEU   A CG  1 
ATOM   1195 C CD1 . LEU   A 1 149 ? 0.551   -18.939 11.656  1.00 46.78  ? 148 LEU   A CD1 1 
ATOM   1196 C CD2 . LEU   A 1 149 ? 1.228   -21.346 11.462  1.00 49.64  ? 148 LEU   A CD2 1 
ATOM   1197 N N   . ILE   A 1 150 ? -3.271  -19.110 10.743  1.00 39.00  ? 149 ILE   A N   1 
ATOM   1198 C CA  . ILE   A 1 150 ? -4.042  -19.198 9.512   1.00 46.09  ? 149 ILE   A CA  1 
ATOM   1199 C C   . ILE   A 1 150 ? -3.135  -18.926 8.321   1.00 51.11  ? 149 ILE   A C   1 
ATOM   1200 O O   . ILE   A 1 150 ? -1.997  -18.489 8.500   1.00 46.63  ? 149 ILE   A O   1 
ATOM   1201 C CB  . ILE   A 1 150 ? -5.228  -18.220 9.523   1.00 44.31  ? 149 ILE   A CB  1 
ATOM   1202 C CG1 . ILE   A 1 150 ? -4.764  -16.747 9.533   1.00 52.36  ? 149 ILE   A CG1 1 
ATOM   1203 C CG2 . ILE   A 1 150 ? -6.140  -18.506 10.713  1.00 45.79  ? 149 ILE   A CG2 1 
ATOM   1204 C CD1 . ILE   A 1 150 ? -5.893  -15.739 9.398   1.00 52.19  ? 149 ILE   A CD1 1 
ATOM   1205 N N   . ASP   A 1 151 ? -3.693  -19.175 7.124   1.00 63.73  ? 150 ASP   A N   1 
ATOM   1206 C CA  . ASP   A 1 151 ? -3.304  -18.550 5.859   1.00 75.61  ? 150 ASP   A CA  1 
ATOM   1207 C C   . ASP   A 1 151 ? -1.947  -19.069 5.397   1.00 83.88  ? 150 ASP   A C   1 
ATOM   1208 O O   . ASP   A 1 151 ? -1.001  -18.302 5.249   1.00 87.34  ? 150 ASP   A O   1 
ATOM   1209 C CB  . ASP   A 1 151 ? -3.370  -17.024 5.919   1.00 81.43  ? 150 ASP   A CB  1 
ATOM   1210 C CG  . ASP   A 1 151 ? -3.306  -16.270 4.591   1.00 86.57  ? 150 ASP   A CG  1 
ATOM   1211 O OD1 . ASP   A 1 151 ? -2.959  -16.890 3.562   1.00 93.07  ? 150 ASP   A OD1 1 
ATOM   1212 O OD2 . ASP   A 1 151 ? -3.620  -15.060 4.589   1.00 79.59  ? 150 ASP   A OD2 1 
ATOM   1213 N N   . PHE   A 1 152 ? -1.886  -20.357 5.068   1.00 93.73  ? 151 PHE   A N   1 
ATOM   1214 C CA  . PHE   A 1 152 ? -0.618  -20.984 4.725   1.00 103.66 ? 151 PHE   A CA  1 
ATOM   1215 C C   . PHE   A 1 152 ? -0.104  -20.507 3.371   1.00 109.95 ? 151 PHE   A C   1 
ATOM   1216 O O   . PHE   A 1 152 ? 0.956   -19.889 3.287   1.00 106.77 ? 151 PHE   A O   1 
ATOM   1217 C CB  . PHE   A 1 152 ? -0.814  -22.498 4.813   1.00 98.45  ? 151 PHE   A CB  1 
ATOM   1218 C CG  . PHE   A 1 152 ? -0.724  -22.823 6.287   1.00 86.81  ? 151 PHE   A CG  1 
ATOM   1219 C CD1 . PHE   A 1 152 ? -1.826  -22.605 7.104   1.00 79.79  ? 151 PHE   A CD1 1 
ATOM   1220 C CD2 . PHE   A 1 152 ? 0.496   -23.174 6.856   1.00 73.85  ? 151 PHE   A CD2 1 
ATOM   1221 C CE1 . PHE   A 1 152 ? -1.737  -22.811 8.461   1.00 70.75  ? 151 PHE   A CE1 1 
ATOM   1222 C CE2 . PHE   A 1 152 ? 0.579   -23.391 8.215   1.00 78.30  ? 151 PHE   A CE2 1 
ATOM   1223 C CZ  . PHE   A 1 152 ? -0.542  -23.221 9.014   1.00 74.80  ? 151 PHE   A CZ  1 
ATOM   1224 N N   . GLY   A 1 153 ? -0.845  -20.860 2.323   1.00 113.94 ? 152 GLY   A N   1 
ATOM   1225 C CA  . GLY   A 1 153 ? -0.560  -20.395 0.981   1.00 117.95 ? 152 GLY   A CA  1 
ATOM   1226 C C   . GLY   A 1 153 ? -1.871  -19.966 0.345   1.00 126.46 ? 152 GLY   A C   1 
ATOM   1227 O O   . GLY   A 1 153 ? -2.675  -19.305 1.007   1.00 128.09 ? 152 GLY   A O   1 
ATOM   1228 N N   . LEU   A 1 154 ? -2.051  -20.357 -0.923  1.00 131.07 ? 153 LEU   A N   1 
ATOM   1229 C CA  . LEU   A 1 154 ? -3.275  -20.129 -1.671  1.00 126.85 ? 153 LEU   A CA  1 
ATOM   1230 C C   . LEU   A 1 154 ? -3.433  -18.613 -1.889  1.00 128.48 ? 153 LEU   A C   1 
ATOM   1231 O O   . LEU   A 1 154 ? -3.672  -18.193 -3.021  1.00 112.35 ? 153 LEU   A O   1 
ATOM   1232 C CB  . LEU   A 1 154 ? -4.465  -20.857 -1.012  1.00 116.92 ? 153 LEU   A CB  1 
ATOM   1233 C CG  . LEU   A 1 154 ? -4.210  -22.298 -0.530  1.00 100.34 ? 153 LEU   A CG  1 
ATOM   1234 C CD1 . LEU   A 1 154 ? -4.393  -22.451 0.973   1.00 96.53  ? 153 LEU   A CD1 1 
ATOM   1235 C CD2 . LEU   A 1 154 ? -5.048  -23.316 -1.258  1.00 96.88  ? 153 LEU   A CD2 1 
ATOM   1236 N N   . CYS   A 1 155 ? -3.114  -17.800 -0.857  1.00 142.26 ? 154 CYS   A N   1 
ATOM   1237 C CA  . CYS   A 1 155 ? -3.413  -16.374 -0.799  1.00 146.48 ? 154 CYS   A CA  1 
ATOM   1238 C C   . CYS   A 1 155 ? -2.172  -15.558 -0.422  1.00 153.85 ? 154 CYS   A C   1 
ATOM   1239 O O   . CYS   A 1 155 ? -1.100  -16.109 -0.182  1.00 176.26 ? 154 CYS   A O   1 
ATOM   1240 C CB  . CYS   A 1 155 ? -4.501  -16.094 0.231   1.00 145.85 ? 154 CYS   A CB  1 
ATOM   1241 S SG  . CYS   A 1 155 ? -4.969  -14.354 0.276   1.00 160.71 ? 154 CYS   A SG  1 
ATOM   1242 N N   . ALA   A 1 156 ? -2.332  -14.230 -0.351  1.00 143.44 ? 155 ALA   A N   1 
ATOM   1243 C CA  . ALA   A 1 156 ? -1.218  -13.324 -0.112  1.00 124.88 ? 155 ALA   A CA  1 
ATOM   1244 C C   . ALA   A 1 156 ? -0.182  -13.491 -1.230  1.00 110.54 ? 155 ALA   A C   1 
ATOM   1245 O O   . ALA   A 1 156 ? 0.721   -12.633 -1.339  1.00 110.84 ? 155 ALA   A O   1 
ATOM   1246 C CB  . ALA   A 1 156 ? -0.606  -13.563 1.263   1.00 118.40 ? 155 ALA   A CB  1 
ATOM   1247 N N   . SER   A 1 172 ? 3.797   -5.747  5.810   1.00 76.78  ? 171 SER   A N   1 
ATOM   1248 C CA  . SER   A 1 172 ? 4.008   -7.223  5.816   1.00 72.94  ? 171 SER   A CA  1 
ATOM   1249 C C   . SER   A 1 172 ? 5.438   -7.589  5.410   1.00 75.50  ? 171 SER   A C   1 
ATOM   1250 O O   . SER   A 1 172 ? 5.957   -8.647  5.810   1.00 62.81  ? 171 SER   A O   1 
ATOM   1251 C CB  . SER   A 1 172 ? 3.023   -7.918  4.933   1.00 79.98  ? 171 SER   A CB  1 
ATOM   1252 O OG  . SER   A 1 172 ? 3.158   -9.331  5.059   1.00 78.36  ? 171 SER   A OG  1 
ATOM   1253 N N   . LEU   A 1 173 ? 6.077   -6.706  4.628   1.00 62.05  ? 172 LEU   A N   1 
ATOM   1254 C CA  . LEU   A 1 173 ? 7.504   -6.795  4.386   1.00 58.63  ? 172 LEU   A CA  1 
ATOM   1255 C C   . LEU   A 1 173 ? 8.274   -6.561  5.677   1.00 42.21  ? 172 LEU   A C   1 
ATOM   1256 O O   . LEU   A 1 173 ? 9.375   -7.071  5.828   1.00 45.34  ? 172 LEU   A O   1 
ATOM   1257 C CB  . LEU   A 1 173 ? 7.923   -5.851  3.262   1.00 75.37  ? 172 LEU   A CB  1 
ATOM   1258 C CG  . LEU   A 1 173 ? 7.351   -6.249  1.893   1.00 93.53  ? 172 LEU   A CG  1 
ATOM   1259 C CD1 . LEU   A 1 173 ? 7.655   -5.235  0.799   1.00 99.51  ? 172 LEU   A CD1 1 
ATOM   1260 C CD2 . LEU   A 1 173 ? 7.829   -7.654  1.491   1.00 90.83  ? 172 LEU   A CD2 1 
ATOM   1261 N N   . ALA   A 1 174 ? 7.661   -5.913  6.668   1.00 39.28  ? 173 ALA   A N   1 
ATOM   1262 C CA  . ALA   A 1 174 ? 8.355   -5.694  7.930   1.00 36.08  ? 173 ALA   A CA  1 
ATOM   1263 C C   . ALA   A 1 174 ? 8.771   -7.016  8.617   1.00 36.41  ? 173 ALA   A C   1 
ATOM   1264 O O   . ALA   A 1 174 ? 9.744   -7.031  9.374   1.00 39.71  ? 173 ALA   A O   1 
ATOM   1265 C CB  . ALA   A 1 174 ? 7.463   -4.883  8.797   1.00 37.77  ? 173 ALA   A CB  1 
ATOM   1266 N N   . TYR   A 1 175 ? 8.062   -8.119  8.321   1.00 35.43  ? 174 TYR   A N   1 
ATOM   1267 C CA  . TYR   A 1 175 ? 8.256   -9.403  8.972   1.00 36.55  ? 174 TYR   A CA  1 
ATOM   1268 C C   . TYR   A 1 175 ? 9.064   -10.340 8.072   1.00 40.42  ? 174 TYR   A C   1 
ATOM   1269 O O   . TYR   A 1 175 ? 9.351   -11.461 8.477   1.00 40.30  ? 174 TYR   A O   1 
ATOM   1270 C CB  . TYR   A 1 175 ? 6.905   -10.041 9.302   1.00 34.94  ? 174 TYR   A CB  1 
ATOM   1271 C CG  . TYR   A 1 175 ? 6.167   -9.335  10.428  1.00 38.76  ? 174 TYR   A CG  1 
ATOM   1272 C CD1 . TYR   A 1 175 ? 5.439   -8.183  10.179  1.00 37.66  ? 174 TYR   A CD1 1 
ATOM   1273 C CD2 . TYR   A 1 175 ? 6.268   -9.759  11.748  1.00 35.69  ? 174 TYR   A CD2 1 
ATOM   1274 C CE1 . TYR   A 1 175 ? 4.822   -7.489  11.197  1.00 37.12  ? 174 TYR   A CE1 1 
ATOM   1275 C CE2 . TYR   A 1 175 ? 5.653   -9.071  12.778  1.00 39.61  ? 174 TYR   A CE2 1 
ATOM   1276 C CZ  . TYR   A 1 175 ? 4.910   -7.940  12.501  1.00 41.41  ? 174 TYR   A CZ  1 
ATOM   1277 O OH  . TYR   A 1 175 ? 4.254   -7.239  13.487  1.00 44.43  ? 174 TYR   A OH  1 
ATOM   1278 N N   . ALA   A 1 176 ? 9.431   -9.887  6.862   1.00 36.29  ? 175 ALA   A N   1 
ATOM   1279 C CA  . ALA   A 1 176 ? 10.091  -10.730 5.881   1.00 37.89  ? 175 ALA   A CA  1 
ATOM   1280 C C   . ALA   A 1 176 ? 11.603  -10.802 6.093   1.00 36.25  ? 175 ALA   A C   1 
ATOM   1281 O O   . ALA   A 1 176 ? 12.305  -9.822  6.355   1.00 33.51  ? 175 ALA   A O   1 
ATOM   1282 C CB  . ALA   A 1 176 ? 9.773   -10.266 4.486   1.00 46.63  ? 175 ALA   A CB  1 
ATOM   1283 N N   . ALA   A 1 177 ? 12.128  -12.010 5.902   1.00 34.22  ? 176 ALA   A N   1 
ATOM   1284 C CA  . ALA   A 1 177 ? 13.545  -12.262 6.137   1.00 36.82  ? 176 ALA   A CA  1 
ATOM   1285 C C   . ALA   A 1 177 ? 14.355  -11.582 5.036   1.00 34.80  ? 176 ALA   A C   1 
ATOM   1286 O O   . ALA   A 1 177 ? 13.882  -11.469 3.910   1.00 39.15  ? 176 ALA   A O   1 
ATOM   1287 C CB  . ALA   A 1 177 ? 13.819  -13.773 6.164   1.00 37.30  ? 176 ALA   A CB  1 
ATOM   1288 N N   . PRO   A 1 178 ? 15.602  -11.183 5.323   1.00 36.03  ? 177 PRO   A N   1 
ATOM   1289 C CA  . PRO   A 1 178 ? 16.501  -10.569 4.343   1.00 45.93  ? 177 PRO   A CA  1 
ATOM   1290 C C   . PRO   A 1 178 ? 16.727  -11.292 3.022   1.00 49.59  ? 177 PRO   A C   1 
ATOM   1291 O O   . PRO   A 1 178 ? 16.949  -10.621 2.024   1.00 50.99  ? 177 PRO   A O   1 
ATOM   1292 C CB  . PRO   A 1 178 ? 17.845  -10.446 5.059   1.00 42.20  ? 177 PRO   A CB  1 
ATOM   1293 C CG  . PRO   A 1 178 ? 17.533  -10.593 6.512   1.00 39.46  ? 177 PRO   A CG  1 
ATOM   1294 C CD  . PRO   A 1 178 ? 16.213  -11.280 6.655   1.00 41.07  ? 177 PRO   A CD  1 
ATOM   1295 N N   . GLU   A 1 179 ? 16.718  -12.635 3.041   1.00 40.92  ? 178 GLU   A N   1 
ATOM   1296 C CA  . GLU   A 1 179 ? 17.032  -13.403 1.852   1.00 39.76  ? 178 GLU   A CA  1 
ATOM   1297 C C   . GLU   A 1 179 ? 15.752  -13.501 1.033   1.00 42.71  ? 178 GLU   A C   1 
ATOM   1298 O O   . GLU   A 1 179 ? 15.785  -13.645 -0.178  1.00 51.51  ? 178 GLU   A O   1 
ATOM   1299 C CB  . GLU   A 1 179 ? 17.677  -14.740 2.219   1.00 45.33  ? 178 GLU   A CB  1 
ATOM   1300 C CG  . GLU   A 1 179 ? 16.734  -15.752 2.890   1.00 47.15  ? 178 GLU   A CG  1 
ATOM   1301 C CD  . GLU   A 1 179 ? 16.606  -15.697 4.424   1.00 41.05  ? 178 GLU   A CD  1 
ATOM   1302 O OE1 . GLU   A 1 179 ? 17.063  -14.692 5.003   1.00 40.76  ? 178 GLU   A OE1 1 
ATOM   1303 O OE2 . GLU   A 1 179 ? 16.060  -16.656 5.020   1.00 39.21  ? 178 GLU   A OE2 1 
ATOM   1304 N N   . LEU   A 1 180 ? 14.601  -13.435 1.693   1.00 39.81  ? 179 LEU   A N   1 
ATOM   1305 C CA  . LEU   A 1 180 ? 13.360  -13.510 0.970   1.00 42.38  ? 179 LEU   A CA  1 
ATOM   1306 C C   . LEU   A 1 180 ? 13.181  -12.206 0.187   1.00 51.51  ? 179 LEU   A C   1 
ATOM   1307 O O   . LEU   A 1 180 ? 12.807  -12.213 -0.980  1.00 56.37  ? 179 LEU   A O   1 
ATOM   1308 C CB  . LEU   A 1 180 ? 12.257  -13.791 1.977   1.00 47.48  ? 179 LEU   A CB  1 
ATOM   1309 C CG  . LEU   A 1 180 ? 10.912  -14.209 1.392   1.00 53.48  ? 179 LEU   A CG  1 
ATOM   1310 C CD1 . LEU   A 1 180 ? 10.070  -14.976 2.405   1.00 62.01  ? 179 LEU   A CD1 1 
ATOM   1311 C CD2 . LEU   A 1 180 ? 10.172  -12.955 0.958   1.00 61.11  ? 179 LEU   A CD2 1 
ATOM   1312 N N   . ILE   A 1 181 ? 13.509  -11.084 0.810   1.00 48.25  ? 180 ILE   A N   1 
ATOM   1313 C CA  . ILE   A 1 181 ? 13.210  -9.791  0.223   1.00 54.53  ? 180 ILE   A CA  1 
ATOM   1314 C C   . ILE   A 1 181 ? 14.187  -9.527  -0.911  1.00 57.73  ? 180 ILE   A C   1 
ATOM   1315 O O   . ILE   A 1 181 ? 13.803  -8.916  -1.895  1.00 74.46  ? 180 ILE   A O   1 
ATOM   1316 C CB  . ILE   A 1 181 ? 13.198  -8.637  1.247   1.00 46.77  ? 180 ILE   A CB  1 
ATOM   1317 C CG1 . ILE   A 1 181 ? 14.515  -8.476  1.978   1.00 51.01  ? 180 ILE   A CG1 1 
ATOM   1318 C CG2 . ILE   A 1 181 ? 12.038  -8.785  2.218   1.00 48.11  ? 180 ILE   A CG2 1 
ATOM   1319 C CD1 . ILE   A 1 181 ? 14.627  -7.175  2.742   1.00 60.88  ? 180 ILE   A CD1 1 
ATOM   1320 N N   . GLN   A 1 182 ? 15.418  -10.026 -0.799  1.00 61.22  ? 181 GLN   A N   1 
ATOM   1321 C CA  . GLN   A 1 182 ? 16.352  -9.967  -1.910  1.00 58.73  ? 181 GLN   A CA  1 
ATOM   1322 C C   . GLN   A 1 182 ? 16.000  -10.932 -3.042  1.00 59.35  ? 181 GLN   A C   1 
ATOM   1323 O O   . GLN   A 1 182 ? 16.833  -11.139 -3.913  1.00 75.22  ? 181 GLN   A O   1 
ATOM   1324 C CB  . GLN   A 1 182 ? 17.744  -10.381 -1.461  1.00 65.47  ? 181 GLN   A CB  1 
ATOM   1325 C CG  . GLN   A 1 182 ? 18.419  -9.377  -0.547  1.00 73.10  ? 181 GLN   A CG  1 
ATOM   1326 C CD  . GLN   A 1 182 ? 19.777  -9.879  -0.129  1.00 80.63  ? 181 GLN   A CD  1 
ATOM   1327 O OE1 . GLN   A 1 182 ? 19.895  -10.937 0.502   1.00 103.91 ? 181 GLN   A OE1 1 
ATOM   1328 N NE2 . GLN   A 1 182 ? 20.814  -9.157  -0.527  1.00 89.95  ? 181 GLN   A NE2 1 
ATOM   1329 N N   . GLY   A 1 183 ? 14.826  -11.581 -3.000  1.00 58.86  ? 182 GLY   A N   1 
ATOM   1330 C CA  . GLY   A 1 183 ? 14.351  -12.473 -4.050  1.00 59.89  ? 182 GLY   A CA  1 
ATOM   1331 C C   . GLY   A 1 183 ? 15.180  -13.750 -4.278  1.00 68.76  ? 182 GLY   A C   1 
ATOM   1332 O O   . GLY   A 1 183 ? 14.845  -14.535 -5.167  1.00 70.08  ? 182 GLY   A O   1 
ATOM   1333 N N   . LYS   A 1 184 ? 16.244  -13.976 -3.492  1.00 73.10  ? 183 LYS   A N   1 
ATOM   1334 C CA  . LYS   A 1 184 ? 17.060  -15.185 -3.590  1.00 67.91  ? 183 LYS   A CA  1 
ATOM   1335 C C   . LYS   A 1 184 ? 16.212  -16.374 -3.158  1.00 69.15  ? 183 LYS   A C   1 
ATOM   1336 O O   . LYS   A 1 184 ? 15.167  -16.181 -2.528  1.00 70.11  ? 183 LYS   A O   1 
ATOM   1337 C CB  . LYS   A 1 184 ? 18.276  -15.155 -2.660  1.00 68.37  ? 183 LYS   A CB  1 
ATOM   1338 C CG  . LYS   A 1 184 ? 18.731  -13.761 -2.299  1.00 75.05  ? 183 LYS   A CG  1 
ATOM   1339 C CD  . LYS   A 1 184 ? 19.578  -13.722 -1.047  1.00 84.23  ? 183 LYS   A CD  1 
ATOM   1340 C CE  . LYS   A 1 184 ? 21.015  -13.627 -1.446  1.00 92.67  ? 183 LYS   A CE  1 
ATOM   1341 N NZ  . LYS   A 1 184 ? 21.801  -14.548 -0.635  1.00 100.82 ? 183 LYS   A NZ  1 
ATOM   1342 N N   . SER   A 1 185 ? 16.645  -17.610 -3.458  1.00 68.57  ? 184 SER   A N   1 
ATOM   1343 C CA  . SER   A 1 185 ? 15.886  -18.720 -2.894  1.00 66.43  ? 184 SER   A CA  1 
ATOM   1344 C C   . SER   A 1 185 ? 16.208  -18.753 -1.402  1.00 49.11  ? 184 SER   A C   1 
ATOM   1345 O O   . SER   A 1 185 ? 17.145  -18.126 -0.896  1.00 46.90  ? 184 SER   A O   1 
ATOM   1346 C CB  . SER   A 1 185 ? 15.986  -20.092 -3.611  1.00 69.16  ? 184 SER   A CB  1 
ATOM   1347 O OG  . SER   A 1 185 ? 17.315  -20.501 -3.909  1.00 79.97  ? 184 SER   A OG  1 
ATOM   1348 N N   . TYR   A 1 186 ? 15.275  -19.321 -0.665  1.00 54.55  ? 185 TYR   A N   1 
ATOM   1349 C CA  . TYR   A 1 186 ? 15.323  -19.187 0.774   1.00 51.37  ? 185 TYR   A CA  1 
ATOM   1350 C C   . TYR   A 1 186 ? 14.659  -20.445 1.269   1.00 43.52  ? 185 TYR   A C   1 
ATOM   1351 O O   . TYR   A 1 186 ? 13.831  -20.983 0.550   1.00 44.92  ? 185 TYR   A O   1 
ATOM   1352 C CB  . TYR   A 1 186 ? 14.652  -17.880 1.191   1.00 49.05  ? 185 TYR   A CB  1 
ATOM   1353 C CG  . TYR   A 1 186 ? 13.159  -17.901 0.906   1.00 54.66  ? 185 TYR   A CG  1 
ATOM   1354 C CD1 . TYR   A 1 186 ? 12.288  -18.485 1.814   1.00 58.23  ? 185 TYR   A CD1 1 
ATOM   1355 C CD2 . TYR   A 1 186 ? 12.632  -17.392 -0.275  1.00 56.91  ? 185 TYR   A CD2 1 
ATOM   1356 C CE1 . TYR   A 1 186 ? 10.923  -18.532 1.584   1.00 66.23  ? 185 TYR   A CE1 1 
ATOM   1357 C CE2 . TYR   A 1 186 ? 11.269  -17.434 -0.524  1.00 64.82  ? 185 TYR   A CE2 1 
ATOM   1358 C CZ  . TYR   A 1 186 ? 10.414  -18.001 0.413   1.00 78.78  ? 185 TYR   A CZ  1 
ATOM   1359 O OH  . TYR   A 1 186 ? 9.061   -18.061 0.246   1.00 84.86  ? 185 TYR   A OH  1 
ATOM   1360 N N   . LEU   A 1 187 ? 15.075  -20.936 2.443   1.00 44.59  ? 186 LEU   A N   1 
ATOM   1361 C CA  . LEU   A 1 187 ? 14.378  -22.037 3.069   1.00 43.28  ? 186 LEU   A CA  1 
ATOM   1362 C C   . LEU   A 1 187 ? 13.238  -21.485 3.899   1.00 45.33  ? 186 LEU   A C   1 
ATOM   1363 O O   . LEU   A 1 187 ? 13.495  -20.717 4.813   1.00 46.58  ? 186 LEU   A O   1 
ATOM   1364 C CB  . LEU   A 1 187 ? 15.321  -22.795 3.998   1.00 44.51  ? 186 LEU   A CB  1 
ATOM   1365 C CG  . LEU   A 1 187 ? 15.991  -24.018 3.396   1.00 50.24  ? 186 LEU   A CG  1 
ATOM   1366 C CD1 . LEU   A 1 187 ? 16.884  -24.614 4.478   1.00 45.92  ? 186 LEU   A CD1 1 
ATOM   1367 C CD2 . LEU   A 1 187 ? 14.912  -24.970 2.858   1.00 47.24  ? 186 LEU   A CD2 1 
ATOM   1368 N N   . GLY   A 1 188 ? 12.044  -21.999 3.656   1.00 47.86  ? 187 GLY   A N   1 
ATOM   1369 C CA  . GLY   A 1 188 ? 10.860  -21.550 4.350   1.00 57.04  ? 187 GLY   A CA  1 
ATOM   1370 C C   . GLY   A 1 188 ? 11.074  -21.595 5.855   1.00 54.08  ? 187 GLY   A C   1 
ATOM   1371 O O   . GLY   A 1 188 ? 10.744  -20.655 6.553   1.00 46.06  ? 187 GLY   A O   1 
ATOM   1372 N N   . SER   A 1 189 ? 11.668  -22.687 6.333   1.00 45.91  ? 188 SER   A N   1 
ATOM   1373 C CA  . SER   A 1 189 ? 11.830  -22.901 7.752   1.00 41.02  ? 188 SER   A CA  1 
ATOM   1374 C C   . SER   A 1 189 ? 12.695  -21.794 8.328   1.00 38.64  ? 188 SER   A C   1 
ATOM   1375 O O   . SER   A 1 189 ? 12.401  -21.300 9.406   1.00 38.62  ? 188 SER   A O   1 
ATOM   1376 C CB  . SER   A 1 189 ? 12.445  -24.279 8.065   1.00 39.17  ? 188 SER   A CB  1 
ATOM   1377 O OG  . SER   A 1 189 ? 13.735  -24.300 7.473   1.00 40.11  ? 188 SER   A OG  1 
ATOM   1378 N N   . GLU   A 1 190 ? 13.804  -21.459 7.658   1.00 38.99  ? 189 GLU   A N   1 
ATOM   1379 C CA  . GLU   A 1 190 ? 14.701  -20.432 8.159   1.00 32.87  ? 189 GLU   A CA  1 
ATOM   1380 C C   . GLU   A 1 190 ? 14.052  -19.031 8.140   1.00 34.54  ? 189 GLU   A C   1 
ATOM   1381 O O   . GLU   A 1 190 ? 14.373  -18.186 8.972   1.00 33.67  ? 189 GLU   A O   1 
ATOM   1382 C CB  . GLU   A 1 190 ? 16.038  -20.371 7.412   1.00 37.19  ? 189 GLU   A CB  1 
ATOM   1383 C CG  . GLU   A 1 190 ? 16.842  -21.668 7.495   1.00 42.09  ? 189 GLU   A CG  1 
ATOM   1384 C CD  . GLU   A 1 190 ? 18.027  -21.747 6.541   1.00 46.46  ? 189 GLU   A CD  1 
ATOM   1385 O OE1 . GLU   A 1 190 ? 18.069  -20.983 5.535   1.00 39.26  ? 189 GLU   A OE1 1 
ATOM   1386 O OE2 . GLU   A 1 190 ? 18.947  -22.540 6.815   1.00 40.19  ? 189 GLU   A OE2 1 
ATOM   1387 N N   . ALA   A 1 191 ? 13.234  -18.743 7.135   1.00 36.22  ? 190 ALA   A N   1 
ATOM   1388 C CA  . ALA   A 1 191 ? 12.595  -17.447 6.996   1.00 37.07  ? 190 ALA   A CA  1 
ATOM   1389 C C   . ALA   A 1 191 ? 11.538  -17.295 8.088   1.00 39.18  ? 190 ALA   A C   1 
ATOM   1390 O O   . ALA   A 1 191 ? 11.385  -16.229 8.658   1.00 35.98  ? 190 ALA   A O   1 
ATOM   1391 C CB  . ALA   A 1 191 ? 11.968  -17.350 5.633   1.00 40.36  ? 190 ALA   A CB  1 
ATOM   1392 N N   . ASP   A 1 192 ? 10.879  -18.409 8.413   1.00 35.17  ? 191 ASP   A N   1 
ATOM   1393 C CA  . ASP   A 1 192 ? 9.954   -18.471 9.519   1.00 36.45  ? 191 ASP   A CA  1 
ATOM   1394 C C   . ASP   A 1 192 ? 10.629  -18.094 10.838  1.00 34.25  ? 191 ASP   A C   1 
ATOM   1395 O O   . ASP   A 1 192 ? 10.032  -17.439 11.678  1.00 33.27  ? 191 ASP   A O   1 
ATOM   1396 C CB  . ASP   A 1 192 ? 9.323   -19.840 9.585   1.00 34.25  ? 191 ASP   A CB  1 
ATOM   1397 C CG  . ASP   A 1 192 ? 8.186   -20.066 8.612   1.00 40.18  ? 191 ASP   A CG  1 
ATOM   1398 O OD1 . ASP   A 1 192 ? 7.826   -19.109 7.904   1.00 35.95  ? 191 ASP   A OD1 1 
ATOM   1399 O OD2 . ASP   A 1 192 ? 7.682   -21.207 8.571   1.00 38.25  ? 191 ASP   A OD2 1 
ATOM   1400 N N   . VAL   A 1 193 ? 11.863  -18.542 11.069  1.00 35.58  ? 192 VAL   A N   1 
ATOM   1401 C CA  . VAL   A 1 193 ? 12.541  -18.215 12.313  1.00 32.05  ? 192 VAL   A CA  1 
ATOM   1402 C C   . VAL   A 1 193 ? 12.764  -16.704 12.416  1.00 32.73  ? 192 VAL   A C   1 
ATOM   1403 O O   . VAL   A 1 193 ? 12.555  -16.122 13.457  1.00 28.92  ? 192 VAL   A O   1 
ATOM   1404 C CB  . VAL   A 1 193 ? 13.834  -19.005 12.499  1.00 32.89  ? 192 VAL   A CB  1 
ATOM   1405 C CG1 . VAL   A 1 193 ? 14.670  -18.454 13.637  1.00 34.98  ? 192 VAL   A CG1 1 
ATOM   1406 C CG2 . VAL   A 1 193 ? 13.526  -20.506 12.693  1.00 31.53  ? 192 VAL   A CG2 1 
ATOM   1407 N N   . TRP   A 1 194 ? 13.249  -16.092 11.354  1.00 32.56  ? 193 TRP   A N   1 
ATOM   1408 C CA  . TRP   A 1 194 ? 13.375  -14.644 11.288  1.00 32.31  ? 193 TRP   A CA  1 
ATOM   1409 C C   . TRP   A 1 194 ? 12.040  -13.988 11.635  1.00 27.13  ? 193 TRP   A C   1 
ATOM   1410 O O   . TRP   A 1 194 ? 11.982  -13.121 12.479  1.00 28.22  ? 193 TRP   A O   1 
ATOM   1411 C CB  . TRP   A 1 194 ? 13.865  -14.208 9.885   1.00 32.98  ? 193 TRP   A CB  1 
ATOM   1412 C CG  . TRP   A 1 194 ? 13.871  -12.710 9.736   1.00 29.04  ? 193 TRP   A CG  1 
ATOM   1413 C CD1 . TRP   A 1 194 ? 12.839  -11.888 9.354   1.00 29.05  ? 193 TRP   A CD1 1 
ATOM   1414 C CD2 . TRP   A 1 194 ? 14.991  -11.858 9.987   1.00 29.77  ? 193 TRP   A CD2 1 
ATOM   1415 N NE1 . TRP   A 1 194 ? 13.248  -10.582 9.411   1.00 30.19  ? 193 TRP   A NE1 1 
ATOM   1416 C CE2 . TRP   A 1 194 ? 14.562  -10.530 9.748   1.00 29.19  ? 193 TRP   A CE2 1 
ATOM   1417 C CE3 . TRP   A 1 194 ? 16.327  -12.091 10.328  1.00 31.06  ? 193 TRP   A CE3 1 
ATOM   1418 C CZ2 . TRP   A 1 194 ? 15.402  -9.441  9.909   1.00 31.97  ? 193 TRP   A CZ2 1 
ATOM   1419 C CZ3 . TRP   A 1 194 ? 17.149  -11.005 10.482  1.00 31.55  ? 193 TRP   A CZ3 1 
ATOM   1420 C CH2 . TRP   A 1 194 ? 16.686  -9.698  10.311  1.00 32.02  ? 193 TRP   A CH2 1 
ATOM   1421 N N   . SER   A 1 195 ? 10.977  -14.354 10.910  1.00 31.70  ? 194 SER   A N   1 
ATOM   1422 C CA  . SER   A 1 195 ? 9.692   -13.715 11.100  1.00 32.49  ? 194 SER   A CA  1 
ATOM   1423 C C   . SER   A 1 195 ? 9.259   -13.839 12.558  1.00 34.33  ? 194 SER   A C   1 
ATOM   1424 O O   . SER   A 1 195 ? 8.610   -12.953 13.117  1.00 28.76  ? 194 SER   A O   1 
ATOM   1425 C CB  . SER   A 1 195 ? 8.687   -14.299 10.188  1.00 30.27  ? 194 SER   A CB  1 
ATOM   1426 O OG  . SER   A 1 195 ? 9.086   -14.081 8.845   1.00 36.80  ? 194 SER   A OG  1 
ATOM   1427 N N   . MET   A 1 196 ? 9.522   -15.007 13.146  1.00 29.29  ? 195 MET   A N   1 
ATOM   1428 C CA  . MET   A 1 196 ? 9.155   -15.220 14.528  1.00 29.67  ? 195 MET   A CA  1 
ATOM   1429 C C   . MET   A 1 196 ? 9.965   -14.322 15.451  1.00 27.13  ? 195 MET   A C   1 
ATOM   1430 O O   . MET   A 1 196 ? 9.486   -13.940 16.508  1.00 29.22  ? 195 MET   A O   1 
ATOM   1431 C CB  . MET   A 1 196 ? 9.283   -16.700 14.913  1.00 30.21  ? 195 MET   A CB  1 
ATOM   1432 C CG  . MET   A 1 196 ? 8.092   -17.560 14.467  1.00 32.73  ? 195 MET   A CG  1 
ATOM   1433 S SD  . MET   A 1 196 ? 8.366   -19.244 15.093  1.00 49.94  ? 195 MET   A SD  1 
ATOM   1434 C CE  . MET   A 1 196 ? 10.031  -19.530 14.469  1.00 56.38  ? 195 MET   A CE  1 
ATOM   1435 N N   . GLY   A 1 197 ? 11.209  -14.018 15.090  1.00 25.69  ? 196 GLY   A N   1 
ATOM   1436 C CA  . GLY   A 1 197 ? 11.975  -13.063 15.860  1.00 30.80  ? 196 GLY   A CA  1 
ATOM   1437 C C   . GLY   A 1 197 ? 11.374  -11.654 15.805  1.00 34.34  ? 196 GLY   A C   1 
ATOM   1438 O O   . GLY   A 1 197 ? 11.354  -10.932 16.814  1.00 32.93  ? 196 GLY   A O   1 
ATOM   1439 N N   . ILE   A 1 198 ? 10.929  -11.242 14.615  1.00 31.43  ? 197 ILE   A N   1 
ATOM   1440 C CA  . ILE   A 1 198 ? 10.273  -9.954  14.500  1.00 33.09  ? 197 ILE   A CA  1 
ATOM   1441 C C   . ILE   A 1 198 ? 9.036   -9.966  15.408  1.00 33.18  ? 197 ILE   A C   1 
ATOM   1442 O O   . ILE   A 1 198 ? 8.792   -9.008  16.115  1.00 32.22  ? 197 ILE   A O   1 
ATOM   1443 C CB  . ILE   A 1 198 ? 9.890   -9.659  13.029  1.00 33.30  ? 197 ILE   A CB  1 
ATOM   1444 C CG1 . ILE   A 1 198 ? 11.072  -9.790  12.053  1.00 29.72  ? 197 ILE   A CG1 1 
ATOM   1445 C CG2 . ILE   A 1 198 ? 9.221   -8.287  12.919  1.00 32.97  ? 197 ILE   A CG2 1 
ATOM   1446 C CD1 . ILE   A 1 198 ? 12.169  -8.763  12.230  1.00 33.19  ? 197 ILE   A CD1 1 
ATOM   1447 N N   . LEU   A 1 199 ? 8.215   -11.019 15.306  1.00 33.12  ? 198 LEU   A N   1 
ATOM   1448 C CA  . LEU   A 1 199 ? 7.034   -11.207 16.138  1.00 33.26  ? 198 LEU   A CA  1 
ATOM   1449 C C   . LEU   A 1 199 ? 7.353   -11.086 17.615  1.00 34.19  ? 198 LEU   A C   1 
ATOM   1450 O O   . LEU   A 1 199 ? 6.664   -10.374 18.333  1.00 34.04  ? 198 LEU   A O   1 
ATOM   1451 C CB  . LEU   A 1 199 ? 6.383   -12.556 15.889  1.00 35.01  ? 198 LEU   A CB  1 
ATOM   1452 C CG  . LEU   A 1 199 ? 5.280   -12.564 14.841  1.00 48.86  ? 198 LEU   A CG  1 
ATOM   1453 C CD1 . LEU   A 1 199 ? 4.991   -13.998 14.463  1.00 55.55  ? 198 LEU   A CD1 1 
ATOM   1454 C CD2 . LEU   A 1 199 ? 4.032   -11.873 15.385  1.00 53.55  ? 198 LEU   A CD2 1 
ATOM   1455 N N   . LEU   A 1 200 ? 8.419   -11.758 18.042  1.00 34.42  ? 199 LEU   A N   1 
ATOM   1456 C CA  . LEU   A 1 200 ? 8.878   -11.683 19.425  1.00 32.83  ? 199 LEU   A CA  1 
ATOM   1457 C C   . LEU   A 1 200 ? 9.142   -10.229 19.817  1.00 31.45  ? 199 LEU   A C   1 
ATOM   1458 O O   . LEU   A 1 200 ? 8.762   -9.793  20.901  1.00 28.71  ? 199 LEU   A O   1 
ATOM   1459 C CB  . LEU   A 1 200 ? 10.154  -12.504 19.584  1.00 29.31  ? 199 LEU   A CB  1 
ATOM   1460 C CG  . LEU   A 1 200 ? 10.664  -12.628 21.015  1.00 31.32  ? 199 LEU   A CG  1 
ATOM   1461 C CD1 . LEU   A 1 200 ? 9.614   -13.236 21.946  1.00 33.90  ? 199 LEU   A CD1 1 
ATOM   1462 C CD2 . LEU   A 1 200 ? 11.913  -13.463 21.017  1.00 30.77  ? 199 LEU   A CD2 1 
ATOM   1463 N N   . TYR   A 1 201 ? 9.892   -9.518  18.973  1.00 29.76  ? 200 TYR   A N   1 
ATOM   1464 C CA  . TYR   A 1 201 ? 10.222  -8.135  19.251  1.00 31.33  ? 200 TYR   A CA  1 
ATOM   1465 C C   . TYR   A 1 201 ? 8.941   -7.295  19.365  1.00 33.24  ? 200 TYR   A C   1 
ATOM   1466 O O   . TYR   A 1 201 ? 8.778   -6.514  20.308  1.00 32.68  ? 200 TYR   A O   1 
ATOM   1467 C CB  . TYR   A 1 201 ? 11.115  -7.615  18.133  1.00 32.06  ? 200 TYR   A CB  1 
ATOM   1468 C CG  . TYR   A 1 201 ? 11.648  -6.212  18.366  1.00 32.41  ? 200 TYR   A CG  1 
ATOM   1469 C CD1 . TYR   A 1 201 ? 10.845  -5.097  18.140  1.00 33.88  ? 200 TYR   A CD1 1 
ATOM   1470 C CD2 . TYR   A 1 201 ? 12.958  -6.000  18.736  1.00 32.48  ? 200 TYR   A CD2 1 
ATOM   1471 C CE1 . TYR   A 1 201 ? 11.354  -3.811  18.273  1.00 35.09  ? 200 TYR   A CE1 1 
ATOM   1472 C CE2 . TYR   A 1 201 ? 13.474  -4.728  18.879  1.00 35.25  ? 200 TYR   A CE2 1 
ATOM   1473 C CZ  . TYR   A 1 201 ? 12.648  -3.632  18.710  1.00 33.86  ? 200 TYR   A CZ  1 
ATOM   1474 O OH  . TYR   A 1 201 ? 13.178  -2.392  18.827  1.00 36.64  ? 200 TYR   A OH  1 
ATOM   1475 N N   . VAL   A 1 202 ? 8.007   -7.491  18.431  1.00 29.01  ? 201 VAL   A N   1 
ATOM   1476 C CA  . VAL   A 1 202 ? 6.796   -6.677  18.426  1.00 33.94  ? 201 VAL   A CA  1 
ATOM   1477 C C   . VAL   A 1 202 ? 5.948   -6.971  19.660  1.00 34.08  ? 201 VAL   A C   1 
ATOM   1478 O O   . VAL   A 1 202 ? 5.390   -6.056  20.258  1.00 33.31  ? 201 VAL   A O   1 
ATOM   1479 C CB  . VAL   A 1 202 ? 6.017   -6.877  17.114  1.00 35.28  ? 201 VAL   A CB  1 
ATOM   1480 C CG1 . VAL   A 1 202 ? 4.575   -6.352  17.181  1.00 35.92  ? 201 VAL   A CG1 1 
ATOM   1481 C CG2 . VAL   A 1 202 ? 6.811   -6.223  15.978  1.00 38.83  ? 201 VAL   A CG2 1 
ATOM   1482 N N   . LEU   A 1 203 ? 5.839   -8.229  20.049  1.00 31.53  ? 202 LEU   A N   1 
ATOM   1483 C CA  . LEU   A 1 203 ? 5.064   -8.603  21.231  1.00 34.84  ? 202 LEU   A CA  1 
ATOM   1484 C C   . LEU   A 1 203 ? 5.571   -7.880  22.473  1.00 36.82  ? 202 LEU   A C   1 
ATOM   1485 O O   . LEU   A 1 203 ? 4.775   -7.406  23.297  1.00 35.87  ? 202 LEU   A O   1 
ATOM   1486 C CB  . LEU   A 1 203 ? 5.132   -10.108 21.438  1.00 37.01  ? 202 LEU   A CB  1 
ATOM   1487 C CG  . LEU   A 1 203 ? 4.342   -10.950 20.444  1.00 39.34  ? 202 LEU   A CG  1 
ATOM   1488 C CD1 . LEU   A 1 203 ? 4.781   -12.424 20.466  1.00 41.25  ? 202 LEU   A CD1 1 
ATOM   1489 C CD2 . LEU   A 1 203 ? 2.873   -10.767 20.729  1.00 39.97  ? 202 LEU   A CD2 1 
ATOM   1490 N N   . MET   A 1 204 ? 6.894   -7.802  22.610  1.00 32.71  ? 203 MET   A N   1 
ATOM   1491 C CA  . MET   A 1 204 ? 7.490   -7.287  23.825  1.00 34.39  ? 203 MET   A CA  1 
ATOM   1492 C C   . MET   A 1 204 ? 7.762   -5.792  23.744  1.00 37.76  ? 203 MET   A C   1 
ATOM   1493 O O   . MET   A 1 204 ? 8.057   -5.191  24.773  1.00 37.39  ? 203 MET   A O   1 
ATOM   1494 C CB  . MET   A 1 204 ? 8.814   -7.995  24.146  1.00 36.02  ? 203 MET   A CB  1 
ATOM   1495 C CG  . MET   A 1 204 ? 8.595   -9.392  24.706  1.00 42.83  ? 203 MET   A CG  1 
ATOM   1496 S SD  . MET   A 1 204 ? 10.095  -10.146 25.363  1.00 45.19  ? 203 MET   A SD  1 
ATOM   1497 C CE  . MET   A 1 204 ? 11.156  -10.110 23.916  1.00 43.90  ? 203 MET   A CE  1 
ATOM   1498 N N   . CYS   A 1 205 ? 7.732   -5.205  22.531  1.00 35.29  ? 204 CYS   A N   1 
ATOM   1499 C CA  . CYS   A 1 205 ? 8.075   -3.801  22.364  1.00 36.87  ? 204 CYS   A CA  1 
ATOM   1500 C C   . CYS   A 1 205 ? 6.857   -2.946  21.976  1.00 35.66  ? 204 CYS   A C   1 
ATOM   1501 O O   . CYS   A 1 205 ? 6.831   -1.772  22.274  1.00 38.65  ? 204 CYS   A O   1 
ATOM   1502 C CB  . CYS   A 1 205 ? 9.228   -3.611  21.399  1.00 35.64  ? 204 CYS   A CB  1 
ATOM   1503 S SG  . CYS   A 1 205 ? 10.794  -4.345  21.944  1.00 40.29  ? 204 CYS   A SG  1 
ATOM   1504 N N   . GLY   A 1 206 ? 5.899   -3.522  21.267  1.00 35.09  ? 205 GLY   A N   1 
ATOM   1505 C CA  . GLY   A 1 206 ? 4.729   -2.810  20.784  1.00 38.58  ? 205 GLY   A CA  1 
ATOM   1506 C C   . GLY   A 1 206 ? 4.994   -1.926  19.561  1.00 36.74  ? 205 GLY   A C   1 
ATOM   1507 O O   . GLY   A 1 206 ? 4.122   -1.083  19.227  1.00 35.49  ? 205 GLY   A O   1 
ATOM   1508 N N   . PHE   A 1 207 ? 6.134   -2.183  18.889  1.00 36.70  ? 206 PHE   A N   1 
ATOM   1509 C CA  . PHE   A 1 207 ? 6.503   -1.555  17.627  1.00 34.89  ? 206 PHE   A CA  1 
ATOM   1510 C C   . PHE   A 1 207 ? 7.528   -2.406  16.855  1.00 36.99  ? 206 PHE   A C   1 
ATOM   1511 O O   . PHE   A 1 207 ? 8.196   -3.280  17.403  1.00 32.02  ? 206 PHE   A O   1 
ATOM   1512 C CB  . PHE   A 1 207 ? 7.085   -0.165  17.892  1.00 35.58  ? 206 PHE   A CB  1 
ATOM   1513 C CG  . PHE   A 1 207 ? 8.188   -0.069  18.927  1.00 33.01  ? 206 PHE   A CG  1 
ATOM   1514 C CD1 . PHE   A 1 207 ? 9.499   -0.368  18.592  1.00 35.45  ? 206 PHE   A CD1 1 
ATOM   1515 C CD2 . PHE   A 1 207 ? 7.908   0.391   20.224  1.00 32.65  ? 206 PHE   A CD2 1 
ATOM   1516 C CE1 . PHE   A 1 207 ? 10.515  -0.284  19.545  1.00 37.99  ? 206 PHE   A CE1 1 
ATOM   1517 C CE2 . PHE   A 1 207 ? 8.920   0.504   21.159  1.00 36.49  ? 206 PHE   A CE2 1 
ATOM   1518 C CZ  . PHE   A 1 207 ? 10.231  0.170   20.820  1.00 34.45  ? 206 PHE   A CZ  1 
ATOM   1519 N N   . LEU   A 1 208 ? 7.664   -2.123  15.565  1.00 35.45  ? 207 LEU   A N   1 
ATOM   1520 C CA  . LEU   A 1 208 ? 8.537   -2.880  14.669  1.00 33.94  ? 207 LEU   A CA  1 
ATOM   1521 C C   . LEU   A 1 208 ? 9.992   -2.598  14.988  1.00 34.49  ? 207 LEU   A C   1 
ATOM   1522 O O   . LEU   A 1 208 ? 10.346  -1.487  15.393  1.00 35.84  ? 207 LEU   A O   1 
ATOM   1523 C CB  . LEU   A 1 208 ? 8.276   -2.559  13.200  1.00 34.11  ? 207 LEU   A CB  1 
ATOM   1524 C CG  . LEU   A 1 208 ? 6.868   -2.840  12.684  1.00 37.19  ? 207 LEU   A CG  1 
ATOM   1525 C CD1 . LEU   A 1 208 ? 6.672   -2.309  11.270  1.00 38.39  ? 207 LEU   A CD1 1 
ATOM   1526 C CD2 . LEU   A 1 208 ? 6.614   -4.310  12.752  1.00 39.78  ? 207 LEU   A CD2 1 
ATOM   1527 N N   . PRO   A 1 209 ? 10.881  -3.611  14.826  1.00 30.88  ? 208 PRO   A N   1 
ATOM   1528 C CA  . PRO   A 1 209 ? 12.310  -3.377  14.938  1.00 32.22  ? 208 PRO   A CA  1 
ATOM   1529 C C   . PRO   A 1 209 ? 12.868  -2.614  13.742  1.00 34.10  ? 208 PRO   A C   1 
ATOM   1530 O O   . PRO   A 1 209 ? 13.886  -1.919  13.866  1.00 36.71  ? 208 PRO   A O   1 
ATOM   1531 C CB  . PRO   A 1 209 ? 12.906  -4.818  15.051  1.00 32.92  ? 208 PRO   A CB  1 
ATOM   1532 C CG  . PRO   A 1 209 ? 11.909  -5.707  14.434  1.00 30.55  ? 208 PRO   A CG  1 
ATOM   1533 C CD  . PRO   A 1 209 ? 10.546  -5.012  14.540  1.00 32.01  ? 208 PRO   A CD  1 
ATOM   1534 N N   . PHE   A 1 210 ? 12.251  -2.845  12.578  1.00 39.15  ? 209 PHE   A N   1 
ATOM   1535 C CA  . PHE   A 1 210 ? 12.675  -2.188  11.352  1.00 41.49  ? 209 PHE   A CA  1 
ATOM   1536 C C   . PHE   A 1 210 ? 11.454  -1.554  10.713  1.00 38.31  ? 209 PHE   A C   1 
ATOM   1537 O O   . PHE   A 1 210 ? 10.467  -2.234  10.466  1.00 35.76  ? 209 PHE   A O   1 
ATOM   1538 C CB  . PHE   A 1 210 ? 13.290  -3.137  10.327  1.00 38.82  ? 209 PHE   A CB  1 
ATOM   1539 C CG  . PHE   A 1 210 ? 14.305  -4.100  10.900  1.00 34.39  ? 209 PHE   A CG  1 
ATOM   1540 C CD1 . PHE   A 1 210 ? 15.599  -3.700  11.130  1.00 36.26  ? 209 PHE   A CD1 1 
ATOM   1541 C CD2 . PHE   A 1 210 ? 13.966  -5.431  11.152  1.00 37.26  ? 209 PHE   A CD2 1 
ATOM   1542 C CE1 . PHE   A 1 210 ? 16.532  -4.605  11.638  1.00 37.56  ? 209 PHE   A CE1 1 
ATOM   1543 C CE2 . PHE   A 1 210 ? 14.902  -6.322  11.659  1.00 34.39  ? 209 PHE   A CE2 1 
ATOM   1544 C CZ  . PHE   A 1 210 ? 16.179  -5.917  11.884  1.00 32.95  ? 209 PHE   A CZ  1 
ATOM   1545 N N   . ASP   A 1 211 ? 11.526  -0.251  10.468  1.00 36.80  ? 210 ASP   A N   1 
ATOM   1546 C CA  . ASP   A 1 211 ? 10.441  0.437   9.791   1.00 37.17  ? 210 ASP   A CA  1 
ATOM   1547 C C   . ASP   A 1 211 ? 11.011  1.571   8.945   1.00 38.35  ? 210 ASP   A C   1 
ATOM   1548 O O   . ASP   A 1 211 ? 12.086  2.114   9.217   1.00 36.09  ? 210 ASP   A O   1 
ATOM   1549 C CB  . ASP   A 1 211 ? 9.452   1.031   10.785  1.00 42.75  ? 210 ASP   A CB  1 
ATOM   1550 C CG  . ASP   A 1 211 ? 10.052  2.185   11.575  1.00 46.53  ? 210 ASP   A CG  1 
ATOM   1551 O OD1 . ASP   A 1 211 ? 10.076  3.338   11.064  1.00 52.21  ? 210 ASP   A OD1 1 
ATOM   1552 O OD2 . ASP   A 1 211 ? 10.620  1.905   12.635  1.00 46.72  ? 210 ASP   A OD2 1 
ATOM   1553 N N   . ASP   A 1 212 ? 10.261  1.929   7.900   1.00 39.74  ? 211 ASP   A N   1 
ATOM   1554 C CA  . ASP   A 1 212 ? 10.642  3.078   7.109   1.00 39.95  ? 211 ASP   A CA  1 
ATOM   1555 C C   . ASP   A 1 212 ? 9.460   3.510   6.256   1.00 38.10  ? 211 ASP   A C   1 
ATOM   1556 O O   . ASP   A 1 212 ? 8.444   2.820   6.198   1.00 37.08  ? 211 ASP   A O   1 
ATOM   1557 C CB  . ASP   A 1 212 ? 11.869  2.776   6.261   1.00 40.01  ? 211 ASP   A CB  1 
ATOM   1558 C CG  . ASP   A 1 212 ? 12.762  3.994   6.125   1.00 42.46  ? 211 ASP   A CG  1 
ATOM   1559 O OD1 . ASP   A 1 212 ? 12.315  4.959   5.457   1.00 47.96  ? 211 ASP   A OD1 1 
ATOM   1560 O OD2 . ASP   A 1 212 ? 13.819  3.984   6.758   1.00 48.49  ? 211 ASP   A OD2 1 
ATOM   1561 N N   . ASP   A 1 213 ? 9.615   4.605   5.506   1.00 42.01  ? 212 ASP   A N   1 
ATOM   1562 C CA  . ASP   A 1 213 ? 8.459   5.114   4.779   1.00 45.13  ? 212 ASP   A CA  1 
ATOM   1563 C C   . ASP   A 1 213 ? 8.547   4.797   3.290   1.00 45.13  ? 212 ASP   A C   1 
ATOM   1564 O O   . ASP   A 1 213 ? 7.771   5.331   2.494   1.00 46.26  ? 212 ASP   A O   1 
ATOM   1565 C CB  . ASP   A 1 213 ? 8.280   6.591   5.035   1.00 46.18  ? 212 ASP   A CB  1 
ATOM   1566 C CG  . ASP   A 1 213 ? 9.349   7.451   4.397   1.00 50.10  ? 212 ASP   A CG  1 
ATOM   1567 O OD1 . ASP   A 1 213 ? 10.276  6.870   3.730   1.00 41.53  ? 212 ASP   A OD1 1 
ATOM   1568 O OD2 . ASP   A 1 213 ? 9.238   8.690   4.566   1.00 52.40  ? 212 ASP   A OD2 1 
ATOM   1569 N N   . ASN   A 1 214 ? 9.503   3.945   2.904   1.00 41.00  ? 213 ASN   A N   1 
ATOM   1570 C CA  . ASN   A 1 214 ? 9.576   3.494   1.517   1.00 40.90  ? 213 ASN   A CA  1 
ATOM   1571 C C   . ASN   A 1 214 ? 10.321  2.164   1.501   1.00 36.71  ? 213 ASN   A C   1 
ATOM   1572 O O   . ASN   A 1 214 ? 11.197  1.967   2.331   1.00 36.68  ? 213 ASN   A O   1 
ATOM   1573 C CB  . ASN   A 1 214 ? 10.205  4.555   0.595   1.00 39.45  ? 213 ASN   A CB  1 
ATOM   1574 C CG  . ASN   A 1 214 ? 11.677  4.801   0.826   1.00 38.62  ? 213 ASN   A CG  1 
ATOM   1575 O OD1 . ASN   A 1 214 ? 12.536  4.185   0.171   1.00 41.12  ? 213 ASN   A OD1 1 
ATOM   1576 N ND2 . ASN   A 1 214 ? 11.998  5.671   1.770   1.00 36.89  ? 213 ASN   A ND2 1 
ATOM   1577 N N   . VAL   A 1 215 ? 9.987   1.310   0.535   1.00 38.19  ? 214 VAL   A N   1 
ATOM   1578 C CA  . VAL   A 1 215 ? 10.442  -0.076  0.456   1.00 49.34  ? 214 VAL   A CA  1 
ATOM   1579 C C   . VAL   A 1 215 ? 11.973  -0.168  0.417   1.00 44.55  ? 214 VAL   A C   1 
ATOM   1580 O O   . VAL   A 1 215 ? 12.590  -1.012  1.082   1.00 40.61  ? 214 VAL   A O   1 
ATOM   1581 C CB  . VAL   A 1 215 ? 9.802   -0.775  -0.765  1.00 54.05  ? 214 VAL   A CB  1 
ATOM   1582 C CG1 . VAL   A 1 215 ? 10.386  -2.158  -1.032  1.00 63.60  ? 214 VAL   A CG1 1 
ATOM   1583 C CG2 . VAL   A 1 215 ? 8.298   -0.909  -0.612  1.00 60.50  ? 214 VAL   A CG2 1 
ATOM   1584 N N   . MET   A 1 216 ? 12.610  0.670   -0.405  1.00 43.95  ? 215 MET   A N   1 
ATOM   1585 C CA  . MET   A 1 216 ? 14.049  0.557   -0.575  1.00 43.59  ? 215 MET   A CA  1 
ATOM   1586 C C   . MET   A 1 216 ? 14.724  0.816   0.766   1.00 39.07  ? 215 MET   A C   1 
ATOM   1587 O O   . MET   A 1 216 ? 15.662  0.106   1.129   1.00 38.29  ? 215 MET   A O   1 
ATOM   1588 C CB  . MET   A 1 216 ? 14.605  1.535   -1.619  1.00 45.25  ? 215 MET   A CB  1 
ATOM   1589 C CG  . MET   A 1 216 ? 16.091  1.410   -1.792  1.00 51.93  ? 215 MET   A CG  1 
ATOM   1590 S SD  . MET   A 1 216 ? 16.791  2.459   -3.089  1.00 52.29  ? 215 MET   A SD  1 
ATOM   1591 C CE  . MET   A 1 216 ? 16.201  1.487   -4.488  1.00 64.65  ? 215 MET   A CE  1 
ATOM   1592 N N   . ALA   A 1 217 ? 14.274  1.843   1.488   1.00 34.53  ? 216 ALA   A N   1 
ATOM   1593 C CA  . ALA   A 1 217 ? 14.913  2.164   2.759   1.00 37.60  ? 216 ALA   A CA  1 
ATOM   1594 C C   . ALA   A 1 217 ? 14.675  1.070   3.813   1.00 33.24  ? 216 ALA   A C   1 
ATOM   1595 O O   . ALA   A 1 217 ? 15.521  0.841   4.675   1.00 36.83  ? 216 ALA   A O   1 
ATOM   1596 C CB  . ALA   A 1 217 ? 14.429  3.504   3.271   1.00 39.25  ? 216 ALA   A CB  1 
ATOM   1597 N N   . LEU   A 1 218 ? 13.481  0.489   3.801   1.00 35.57  ? 217 LEU   A N   1 
ATOM   1598 C CA  . LEU   A 1 218 ? 13.141  -0.572  4.745   1.00 38.15  ? 217 LEU   A CA  1 
ATOM   1599 C C   . LEU   A 1 218 ? 13.990  -1.811  4.447   1.00 38.56  ? 217 LEU   A C   1 
ATOM   1600 O O   . LEU   A 1 218 ? 14.556  -2.406  5.351   1.00 32.75  ? 217 LEU   A O   1 
ATOM   1601 C CB  . LEU   A 1 218 ? 11.665  -0.917  4.635   1.00 38.19  ? 217 LEU   A CB  1 
ATOM   1602 C CG  . LEU   A 1 218 ? 11.188  -2.079  5.503   1.00 40.27  ? 217 LEU   A CG  1 
ATOM   1603 C CD1 . LEU   A 1 218 ? 11.444  -1.780  6.954   1.00 41.29  ? 217 LEU   A CD1 1 
ATOM   1604 C CD2 . LEU   A 1 218 ? 9.731   -2.361  5.205   1.00 47.10  ? 217 LEU   A CD2 1 
ATOM   1605 N N   . TYR   A 1 219 ? 14.042  -2.185  3.177   1.00 38.64  ? 218 TYR   A N   1 
ATOM   1606 C CA  . TYR   A 1 219 ? 14.849  -3.303  2.719   1.00 43.69  ? 218 TYR   A CA  1 
ATOM   1607 C C   . TYR   A 1 219 ? 16.286  -3.126  3.163   1.00 40.83  ? 218 TYR   A C   1 
ATOM   1608 O O   . TYR   A 1 219 ? 16.900  -4.039  3.695   1.00 40.59  ? 218 TYR   A O   1 
ATOM   1609 C CB  . TYR   A 1 219 ? 14.839  -3.429  1.197   1.00 47.36  ? 218 TYR   A CB  1 
ATOM   1610 C CG  . TYR   A 1 219 ? 13.639  -4.157  0.624   1.00 55.48  ? 218 TYR   A CG  1 
ATOM   1611 C CD1 . TYR   A 1 219 ? 12.451  -4.277  1.340   1.00 66.34  ? 218 TYR   A CD1 1 
ATOM   1612 C CD2 . TYR   A 1 219 ? 13.715  -4.748  -0.630  1.00 65.57  ? 218 TYR   A CD2 1 
ATOM   1613 C CE1 . TYR   A 1 219 ? 11.362  -4.948  0.811   1.00 80.11  ? 218 TYR   A CE1 1 
ATOM   1614 C CE2 . TYR   A 1 219 ? 12.623  -5.396  -1.182  1.00 76.20  ? 218 TYR   A CE2 1 
ATOM   1615 C CZ  . TYR   A 1 219 ? 11.446  -5.494  -0.461  1.00 81.34  ? 218 TYR   A CZ  1 
ATOM   1616 O OH  . TYR   A 1 219 ? 10.393  -6.162  -1.015  1.00 97.54  ? 218 TYR   A OH  1 
ATOM   1617 N N   . LYS   A 1 220 ? 16.836  -1.940  2.973   1.00 36.70  ? 219 LYS   A N   1 
ATOM   1618 C CA  . LYS   A 1 220 ? 18.188  -1.746  3.447   1.00 37.45  ? 219 LYS   A CA  1 
ATOM   1619 C C   . LYS   A 1 220 ? 18.314  -1.991  4.942   1.00 41.05  ? 219 LYS   A C   1 
ATOM   1620 O O   . LYS   A 1 220 ? 19.332  -2.509  5.379   1.00 37.28  ? 219 LYS   A O   1 
ATOM   1621 C CB  . LYS   A 1 220 ? 18.692  -0.359  3.065   1.00 44.11  ? 219 LYS   A CB  1 
ATOM   1622 C CG  . LYS   A 1 220 ? 19.003  -0.329  1.561   1.00 46.18  ? 219 LYS   A CG  1 
ATOM   1623 C CD  . LYS   A 1 220 ? 19.742  0.929   1.141   1.00 42.45  ? 219 LYS   A CD  1 
ATOM   1624 C CE  . LYS   A 1 220 ? 20.102  0.817   -0.304  1.00 42.86  ? 219 LYS   A CE  1 
ATOM   1625 N NZ  . LYS   A 1 220 ? 20.829  2.047   -0.573  1.00 40.23  ? 219 LYS   A NZ  1 
ATOM   1626 N N   . LYS   A 1 221 ? 17.349  -1.505  5.728   1.00 42.72  ? 220 LYS   A N   1 
ATOM   1627 C CA  . LYS   A 1 221 ? 17.427  -1.611  7.177   1.00 42.36  ? 220 LYS   A CA  1 
ATOM   1628 C C   . LYS   A 1 221 ? 17.386  -3.084  7.607   1.00 35.26  ? 220 LYS   A C   1 
ATOM   1629 O O   . LYS   A 1 221 ? 18.154  -3.506  8.457   1.00 40.31  ? 220 LYS   A O   1 
ATOM   1630 C CB  . LYS   A 1 221 ? 16.275  -0.818  7.803   1.00 46.95  ? 220 LYS   A CB  1 
ATOM   1631 C CG  . LYS   A 1 221 ? 16.633  0.609   8.121   1.00 50.23  ? 220 LYS   A CG  1 
ATOM   1632 C CD  . LYS   A 1 221 ? 15.436  1.386   8.648   1.00 54.04  ? 220 LYS   A CD  1 
ATOM   1633 C CE  . LYS   A 1 221 ? 15.792  2.744   9.122   1.00 50.38  ? 220 LYS   A CE  1 
ATOM   1634 N NZ  . LYS   A 1 221 ? 14.572  3.413   9.572   1.00 57.88  ? 220 LYS   A NZ  1 
ATOM   1635 N N   . ILE   A 1 222 ? 16.465  -3.842  7.022   1.00 36.61  ? 221 ILE   A N   1 
ATOM   1636 C CA  . ILE   A 1 222 ? 16.335  -5.260  7.288   1.00 38.31  ? 221 ILE   A CA  1 
ATOM   1637 C C   . ILE   A 1 222 ? 17.635  -5.993  6.954   1.00 48.00  ? 221 ILE   A C   1 
ATOM   1638 O O   . ILE   A 1 222 ? 18.119  -6.768  7.779   1.00 44.40  ? 221 ILE   A O   1 
ATOM   1639 C CB  . ILE   A 1 222 ? 15.140  -5.822  6.523   1.00 34.20  ? 221 ILE   A CB  1 
ATOM   1640 C CG1 . ILE   A 1 222 ? 13.844  -5.329  7.151   1.00 33.51  ? 221 ILE   A CG1 1 
ATOM   1641 C CG2 . ILE   A 1 222 ? 15.190  -7.355  6.477   1.00 37.75  ? 221 ILE   A CG2 1 
ATOM   1642 C CD1 . ILE   A 1 222 ? 12.640  -5.507  6.277   1.00 37.28  ? 221 ILE   A CD1 1 
ATOM   1643 N N   . MET   A 1 223 ? 18.227  -5.710  5.781   1.00 39.67  ? 222 MET   A N   1 
ATOM   1644 C CA  . MET   A 1 223 ? 19.447  -6.389  5.372   1.00 42.97  ? 222 MET   A CA  1 
ATOM   1645 C C   . MET   A 1 223 ? 20.643  -6.014  6.237   1.00 42.78  ? 222 MET   A C   1 
ATOM   1646 O O   . MET   A 1 223 ? 21.580  -6.806  6.376   1.00 41.91  ? 222 MET   A O   1 
ATOM   1647 C CB  . MET   A 1 223 ? 19.741  -6.117  3.902   1.00 48.74  ? 222 MET   A CB  1 
ATOM   1648 C CG  . MET   A 1 223 ? 18.863  -6.944  2.983   1.00 59.98  ? 222 MET   A CG  1 
ATOM   1649 S SD  . MET   A 1 223 ? 18.892  -6.098  1.398   1.00 71.82  ? 222 MET   A SD  1 
ATOM   1650 C CE  . MET   A 1 223 ? 20.634  -6.313  0.985   1.00 86.61  ? 222 MET   A CE  1 
ATOM   1651 N N   . ARG   A 1 224 ? 20.622  -4.809  6.814   1.00 41.75  ? 223 ARG   A N   1 
ATOM   1652 C CA  . ARG   A 1 224 ? 21.672  -4.387  7.717   1.00 45.18  ? 223 ARG   A CA  1 
ATOM   1653 C C   . ARG   A 1 224 ? 21.498  -5.113  9.061   1.00 51.99  ? 223 ARG   A C   1 
ATOM   1654 O O   . ARG   A 1 224 ? 22.476  -5.342  9.764   1.00 45.74  ? 223 ARG   A O   1 
ATOM   1655 C CB  . ARG   A 1 224 ? 21.635  -2.858  7.837   1.00 52.96  ? 223 ARG   A CB  1 
ATOM   1656 C CG  . ARG   A 1 224 ? 22.878  -2.193  8.409   1.00 71.37  ? 223 ARG   A CG  1 
ATOM   1657 C CD  . ARG   A 1 224 ? 22.759  -0.679  8.713   1.00 77.43  ? 223 ARG   A CD  1 
ATOM   1658 N NE  . ARG   A 1 224 ? 22.022  0.097   7.699   1.00 83.76  ? 223 ARG   A NE  1 
ATOM   1659 C CZ  . ARG   A 1 224 ? 20.799  0.661   7.881   1.00 83.46  ? 223 ARG   A CZ  1 
ATOM   1660 N NH1 . ARG   A 1 224 ? 20.204  0.588   9.072   1.00 66.06  ? 223 ARG   A NH1 1 
ATOM   1661 N NH2 . ARG   A 1 224 ? 20.156  1.281   6.880   1.00 67.91  ? 223 ARG   A NH2 1 
ATOM   1662 N N   . GLY   A 1 225 ? 20.242  -5.397  9.454   1.00 46.69  ? 224 GLY   A N   1 
ATOM   1663 C CA  . GLY   A 1 225 ? 19.954  -6.186  10.641  1.00 45.34  ? 224 GLY   A CA  1 
ATOM   1664 C C   . GLY   A 1 225 ? 20.177  -5.453  11.963  1.00 43.35  ? 224 GLY   A C   1 
ATOM   1665 O O   . GLY   A 1 225 ? 20.210  -6.101  13.003  1.00 45.57  ? 224 GLY   A O   1 
ATOM   1666 N N   . LYS   A 1 226 ? 20.260  -4.116  11.968  1.00 41.15  ? 225 LYS   A N   1 
ATOM   1667 C CA  . LYS   A 1 226 ? 20.457  -3.397  13.214  1.00 42.13  ? 225 LYS   A CA  1 
ATOM   1668 C C   . LYS   A 1 226 ? 19.112  -2.828  13.673  1.00 41.03  ? 225 LYS   A C   1 
ATOM   1669 O O   . LYS   A 1 226 ? 18.344  -2.324  12.853  1.00 36.66  ? 225 LYS   A O   1 
ATOM   1670 C CB  . LYS   A 1 226 ? 21.446  -2.228  13.114  1.00 49.75  ? 225 LYS   A CB  1 
ATOM   1671 C CG  . LYS   A 1 226 ? 22.557  -2.360  12.102  1.00 62.04  ? 225 LYS   A CG  1 
ATOM   1672 C CD  . LYS   A 1 226 ? 23.684  -3.315  12.470  1.00 77.44  ? 225 LYS   A CD  1 
ATOM   1673 C CE  . LYS   A 1 226 ? 24.814  -3.153  11.480  1.00 92.51  ? 225 LYS   A CE  1 
ATOM   1674 N NZ  . LYS   A 1 226 ? 25.802  -4.228  11.565  1.00 101.76 ? 225 LYS   A NZ  1 
ATOM   1675 N N   . TYR   A 1 227 ? 18.847  -2.919  14.975  1.00 39.21  ? 226 TYR   A N   1 
ATOM   1676 C CA  . TYR   A 1 227 ? 17.607  -2.436  15.562  1.00 42.88  ? 226 TYR   A CA  1 
ATOM   1677 C C   . TYR   A 1 227 ? 17.900  -1.947  16.976  1.00 41.88  ? 226 TYR   A C   1 
ATOM   1678 O O   . TYR   A 1 227 ? 18.877  -2.356  17.588  1.00 41.01  ? 226 TYR   A O   1 
ATOM   1679 C CB  . TYR   A 1 227 ? 16.504  -3.496  15.641  1.00 40.68  ? 226 TYR   A CB  1 
ATOM   1680 C CG  . TYR   A 1 227 ? 16.972  -4.830  16.211  1.00 37.49  ? 226 TYR   A CG  1 
ATOM   1681 C CD1 . TYR   A 1 227 ? 16.953  -5.068  17.581  1.00 39.40  ? 226 TYR   A CD1 1 
ATOM   1682 C CD2 . TYR   A 1 227 ? 17.431  -5.852  15.380  1.00 35.41  ? 226 TYR   A CD2 1 
ATOM   1683 C CE1 . TYR   A 1 227 ? 17.357  -6.289  18.114  1.00 38.04  ? 226 TYR   A CE1 1 
ATOM   1684 C CE2 . TYR   A 1 227 ? 17.838  -7.078  15.898  1.00 39.95  ? 226 TYR   A CE2 1 
ATOM   1685 C CZ  . TYR   A 1 227 ? 17.799  -7.294  17.266  1.00 37.91  ? 226 TYR   A CZ  1 
ATOM   1686 O OH  . TYR   A 1 227 ? 18.217  -8.451  17.806  1.00 35.14  ? 226 TYR   A OH  1 
ATOM   1687 N N   . ASP   A 1 228 ? 17.024  -1.102  17.512  1.00 48.62  ? 227 ASP   A N   1 
ATOM   1688 C CA  . ASP   A 1 228 ? 17.204  -0.681  18.888  1.00 52.91  ? 227 ASP   A CA  1 
ATOM   1689 C C   . ASP   A 1 228 ? 16.595  -1.743  19.791  1.00 52.09  ? 227 ASP   A C   1 
ATOM   1690 O O   . ASP   A 1 228 ? 15.650  -2.447  19.434  1.00 46.83  ? 227 ASP   A O   1 
ATOM   1691 C CB  . ASP   A 1 228 ? 16.576  0.664   19.214  1.00 61.41  ? 227 ASP   A CB  1 
ATOM   1692 C CG  . ASP   A 1 228 ? 16.862  1.808   18.252  1.00 65.93  ? 227 ASP   A CG  1 
ATOM   1693 O OD1 . ASP   A 1 228 ? 18.047  1.965   17.855  1.00 60.35  ? 227 ASP   A OD1 1 
ATOM   1694 O OD2 . ASP   A 1 228 ? 15.885  2.526   17.918  1.00 71.62  ? 227 ASP   A OD2 1 
ATOM   1695 N N   . VAL   A 1 229 ? 17.146  -1.796  20.995  1.00 49.97  ? 228 VAL   A N   1 
ATOM   1696 C CA  . VAL   A 1 229 ? 16.703  -2.719  22.020  1.00 54.82  ? 228 VAL   A CA  1 
ATOM   1697 C C   . VAL   A 1 229 ? 16.230  -1.869  23.186  1.00 45.69  ? 228 VAL   A C   1 
ATOM   1698 O O   . VAL   A 1 229 ? 17.067  -1.367  23.904  1.00 51.68  ? 228 VAL   A O   1 
ATOM   1699 C CB  . VAL   A 1 229 ? 17.937  -3.584  22.353  1.00 59.36  ? 228 VAL   A CB  1 
ATOM   1700 C CG1 . VAL   A 1 229 ? 17.880  -4.230  23.732  1.00 56.72  ? 228 VAL   A CG1 1 
ATOM   1701 C CG2 . VAL   A 1 229 ? 18.170  -4.640  21.279  1.00 68.29  ? 228 VAL   A CG2 1 
ATOM   1702 N N   . PRO   A 1 230 ? 14.919  -1.666  23.404  1.00 47.99  ? 229 PRO   A N   1 
ATOM   1703 C CA  . PRO   A 1 230 ? 14.424  -0.897  24.553  1.00 50.27  ? 229 PRO   A CA  1 
ATOM   1704 C C   . PRO   A 1 230 ? 14.901  -1.400  25.923  1.00 54.11  ? 229 PRO   A C   1 
ATOM   1705 O O   . PRO   A 1 230 ? 15.202  -2.572  26.102  1.00 44.10  ? 229 PRO   A O   1 
ATOM   1706 C CB  . PRO   A 1 230 ? 12.901  -1.004  24.447  1.00 48.82  ? 229 PRO   A CB  1 
ATOM   1707 C CG  . PRO   A 1 230 ? 12.642  -1.377  23.014  1.00 50.00  ? 229 PRO   A CG  1 
ATOM   1708 C CD  . PRO   A 1 230 ? 13.832  -2.175  22.565  1.00 53.08  ? 229 PRO   A CD  1 
ATOM   1709 N N   . LYS   A 1 231 ? 14.851  -0.501  26.912  1.00 60.66  ? 230 LYS   A N   1 
ATOM   1710 C CA  . LYS   A 1 231 ? 15.513  -0.674  28.190  1.00 56.84  ? 230 LYS   A CA  1 
ATOM   1711 C C   . LYS   A 1 231 ? 14.783  -1.746  28.986  1.00 48.69  ? 230 LYS   A C   1 
ATOM   1712 O O   . LYS   A 1 231 ? 15.356  -2.334  29.876  1.00 55.23  ? 230 LYS   A O   1 
ATOM   1713 C CB  . LYS   A 1 231 ? 15.464  0.628   29.005  1.00 64.97  ? 230 LYS   A CB  1 
ATOM   1714 C CG  . LYS   A 1 231 ? 16.084  1.876   28.393  1.00 72.26  ? 230 LYS   A CG  1 
ATOM   1715 C CD  . LYS   A 1 231 ? 15.434  2.433   27.124  1.00 89.41  ? 230 LYS   A CD  1 
ATOM   1716 C CE  . LYS   A 1 231 ? 13.956  2.730   27.244  1.00 91.62  ? 230 LYS   A CE  1 
ATOM   1717 N NZ  . LYS   A 1 231 ? 13.327  2.961   25.940  1.00 86.37  ? 230 LYS   A NZ  1 
ATOM   1718 N N   . TRP   A 1 232 ? 13.504  -1.988  28.682  1.00 46.34  ? 231 TRP   A N   1 
ATOM   1719 C CA  . TRP   A 1 232 ? 12.699  -2.909  29.458  1.00 41.53  ? 231 TRP   A CA  1 
ATOM   1720 C C   . TRP   A 1 232 ? 12.899  -4.380  29.072  1.00 42.01  ? 231 TRP   A C   1 
ATOM   1721 O O   . TRP   A 1 232 ? 12.404  -5.254  29.769  1.00 43.19  ? 231 TRP   A O   1 
ATOM   1722 C CB  . TRP   A 1 232 ? 11.230  -2.495  29.365  1.00 43.36  ? 231 TRP   A CB  1 
ATOM   1723 C CG  . TRP   A 1 232 ? 10.662  -2.476  27.976  1.00 50.31  ? 231 TRP   A CG  1 
ATOM   1724 C CD1 . TRP   A 1 232 ? 10.230  -3.546  27.249  1.00 47.77  ? 231 TRP   A CD1 1 
ATOM   1725 C CD2 . TRP   A 1 232 ? 10.405  -1.311  27.167  1.00 50.50  ? 231 TRP   A CD2 1 
ATOM   1726 N NE1 . TRP   A 1 232 ? 9.757   -3.138  26.035  1.00 49.19  ? 231 TRP   A NE1 1 
ATOM   1727 C CE2 . TRP   A 1 232 ? 9.837   -1.775  25.956  1.00 52.94  ? 231 TRP   A CE2 1 
ATOM   1728 C CE3 . TRP   A 1 232 ? 10.611  0.061   27.333  1.00 52.39  ? 231 TRP   A CE3 1 
ATOM   1729 C CZ2 . TRP   A 1 232 ? 9.459   -0.906  24.933  1.00 52.73  ? 231 TRP   A CZ2 1 
ATOM   1730 C CZ3 . TRP   A 1 232 ? 10.247  0.921   26.314  1.00 63.13  ? 231 TRP   A CZ3 1 
ATOM   1731 C CH2 . TRP   A 1 232 ? 9.669   0.444   25.131  1.00 56.58  ? 231 TRP   A CH2 1 
ATOM   1732 N N   . LEU   A 1 233 ? 13.629  -4.676  27.994  1.00 39.46  ? 232 LEU   A N   1 
ATOM   1733 C CA  . LEU   A 1 233 ? 13.840  -6.063  27.592  1.00 42.89  ? 232 LEU   A CA  1 
ATOM   1734 C C   . LEU   A 1 233 ? 14.845  -6.733  28.532  1.00 44.15  ? 232 LEU   A C   1 
ATOM   1735 O O   . LEU   A 1 233 ? 15.905  -6.190  28.804  1.00 42.18  ? 232 LEU   A O   1 
ATOM   1736 C CB  . LEU   A 1 233 ? 14.349  -6.117  26.153  1.00 38.05  ? 232 LEU   A CB  1 
ATOM   1737 C CG  . LEU   A 1 233 ? 13.378  -5.633  25.064  1.00 39.96  ? 232 LEU   A CG  1 
ATOM   1738 C CD1 . LEU   A 1 233 ? 13.983  -5.880  23.681  1.00 39.16  ? 232 LEU   A CD1 1 
ATOM   1739 C CD2 . LEU   A 1 233 ? 11.991  -6.283  25.206  1.00 43.70  ? 232 LEU   A CD2 1 
ATOM   1740 N N   . SER   A 1 234 ? 14.533  -7.937  28.999  1.00 41.43  ? 233 SER   A N   1 
ATOM   1741 C CA  . SER   A 1 234 ? 15.492  -8.654  29.829  1.00 39.42  ? 233 SER   A CA  1 
ATOM   1742 C C   . SER   A 1 234 ? 16.724  -9.043  29.006  1.00 49.05  ? 233 SER   A C   1 
ATOM   1743 O O   . SER   A 1 234 ? 16.684  -9.104  27.774  1.00 42.94  ? 233 SER   A O   1 
ATOM   1744 C CB  . SER   A 1 234 ? 14.850  -9.836  30.457  1.00 38.43  ? 233 SER   A CB  1 
ATOM   1745 O OG  . SER   A 1 234 ? 14.396  -10.769 29.488  1.00 37.14  ? 233 SER   A OG  1 
ATOM   1746 N N   . PRO   A 1 235 ? 17.886  -9.281  29.655  1.00 50.30  ? 234 PRO   A N   1 
ATOM   1747 C CA  . PRO   A 1 235 ? 19.039  -9.847  28.963  1.00 45.95  ? 234 PRO   A CA  1 
ATOM   1748 C C   . PRO   A 1 235 ? 18.679  -11.096 28.173  1.00 43.39  ? 234 PRO   A C   1 
ATOM   1749 O O   . PRO   A 1 235 ? 19.095  -11.247 27.036  1.00 40.51  ? 234 PRO   A O   1 
ATOM   1750 C CB  . PRO   A 1 235 ? 20.007  -10.149 30.137  1.00 57.30  ? 234 PRO   A CB  1 
ATOM   1751 C CG  . PRO   A 1 235 ? 19.684  -9.057  31.149  1.00 55.05  ? 234 PRO   A CG  1 
ATOM   1752 C CD  . PRO   A 1 235 ? 18.159  -8.973  31.076  1.00 55.48  ? 234 PRO   A CD  1 
ATOM   1753 N N   . SER   A 1 236 ? 17.873  -11.967 28.770  1.00 37.69  ? 235 SER   A N   1 
ATOM   1754 C CA  . SER   A 1 236 ? 17.518  -13.218 28.134  1.00 40.44  ? 235 SER   A CA  1 
ATOM   1755 C C   . SER   A 1 236 ? 16.681  -12.986 26.862  1.00 41.21  ? 235 SER   A C   1 
ATOM   1756 O O   . SER   A 1 236 ? 16.869  -13.655 25.850  1.00 37.36  ? 235 SER   A O   1 
ATOM   1757 C CB  . SER   A 1 236 ? 16.792  -14.032 29.149  1.00 41.90  ? 235 SER   A CB  1 
ATOM   1758 O OG  . SER   A 1 236 ? 16.169  -15.172 28.598  1.00 47.21  ? 235 SER   A OG  1 
ATOM   1759 N N   . SER   A 1 237 ? 15.741  -12.036 26.923  1.00 41.42  ? 236 SER   A N   1 
ATOM   1760 C CA  . SER   A 1 237 ? 14.982  -11.583 25.758  1.00 39.00  ? 236 SER   A CA  1 
ATOM   1761 C C   . SER   A 1 237 ? 15.904  -11.126 24.636  1.00 30.84  ? 236 SER   A C   1 
ATOM   1762 O O   . SER   A 1 237 ? 15.719  -11.500 23.483  1.00 33.47  ? 236 SER   A O   1 
ATOM   1763 C CB  . SER   A 1 237 ? 14.021  -10.438 26.134  1.00 32.76  ? 236 SER   A CB  1 
ATOM   1764 O OG  . SER   A 1 237 ? 12.820  -10.993 26.646  1.00 36.98  ? 236 SER   A OG  1 
ATOM   1765 N N   . ILE   A 1 238 ? 16.822  -10.239 24.990  1.00 30.97  ? 237 ILE   A N   1 
ATOM   1766 C CA  . ILE   A 1 238 ? 17.751  -9.637  24.074  1.00 35.88  ? 237 ILE   A CA  1 
ATOM   1767 C C   . ILE   A 1 238 ? 18.559  -10.744 23.408  1.00 43.98  ? 237 ILE   A C   1 
ATOM   1768 O O   . ILE   A 1 238 ? 18.787  -10.712 22.198  1.00 40.08  ? 237 ILE   A O   1 
ATOM   1769 C CB  . ILE   A 1 238 ? 18.635  -8.620  24.809  1.00 41.73  ? 237 ILE   A CB  1 
ATOM   1770 C CG1 . ILE   A 1 238 ? 17.794  -7.429  25.297  1.00 44.37  ? 237 ILE   A CG1 1 
ATOM   1771 C CG2 . ILE   A 1 238 ? 19.803  -8.180  23.925  1.00 39.48  ? 237 ILE   A CG2 1 
ATOM   1772 C CD1 . ILE   A 1 238 ? 18.569  -6.427  26.144  1.00 47.25  ? 237 ILE   A CD1 1 
ATOM   1773 N N   . LEU   A 1 239 ? 18.926  -11.747 24.204  1.00 41.82  ? 238 LEU   A N   1 
ATOM   1774 C CA  . LEU   A 1 239 ? 19.754  -12.822 23.696  1.00 41.84  ? 238 LEU   A CA  1 
ATOM   1775 C C   . LEU   A 1 239 ? 18.965  -13.708 22.750  1.00 34.86  ? 238 LEU   A C   1 
ATOM   1776 O O   . LEU   A 1 239 ? 19.528  -14.020 21.708  1.00 37.40  ? 238 LEU   A O   1 
ATOM   1777 C CB  . LEU   A 1 239 ? 20.470  -13.568 24.821  1.00 44.70  ? 238 LEU   A CB  1 
ATOM   1778 C CG  . LEU   A 1 239 ? 21.535  -12.698 25.528  1.00 52.27  ? 238 LEU   A CG  1 
ATOM   1779 C CD1 . LEU   A 1 239 ? 21.759  -13.044 26.989  1.00 55.86  ? 238 LEU   A CD1 1 
ATOM   1780 C CD2 . LEU   A 1 239 ? 22.895  -12.662 24.796  1.00 46.63  ? 238 LEU   A CD2 1 
ATOM   1781 N N   . LEU   A 1 240 ? 17.696  -14.075 23.052  1.00 32.93  ? 239 LEU   A N   1 
ATOM   1782 C CA  . LEU   A 1 240 ? 16.930  -14.877 22.107  1.00 37.61  ? 239 LEU   A CA  1 
ATOM   1783 C C   . LEU   A 1 240 ? 16.669  -14.122 20.782  1.00 38.18  ? 239 LEU   A C   1 
ATOM   1784 O O   . LEU   A 1 240 ? 16.746  -14.708 19.693  1.00 32.38  ? 239 LEU   A O   1 
ATOM   1785 C CB  . LEU   A 1 240 ? 15.625  -15.299 22.744  1.00 38.09  ? 239 LEU   A CB  1 
ATOM   1786 C CG  . LEU   A 1 240 ? 14.657  -16.037 21.829  1.00 37.61  ? 239 LEU   A CG  1 
ATOM   1787 C CD1 . LEU   A 1 240 ? 15.289  -17.294 21.229  1.00 42.81  ? 239 LEU   A CD1 1 
ATOM   1788 C CD2 . LEU   A 1 240 ? 13.381  -16.374 22.617  1.00 39.53  ? 239 LEU   A CD2 1 
ATOM   1789 N N   . LEU   A 1 241 ? 16.384  -12.820 20.869  1.00 32.82  ? 240 LEU   A N   1 
ATOM   1790 C CA  . LEU   A 1 241 ? 16.230  -11.999 19.666  1.00 36.20  ? 240 LEU   A CA  1 
ATOM   1791 C C   . LEU   A 1 241 ? 17.475  -12.055 18.777  1.00 34.33  ? 240 LEU   A C   1 
ATOM   1792 O O   . LEU   A 1 241 ? 17.361  -12.183 17.562  1.00 36.46  ? 240 LEU   A O   1 
ATOM   1793 C CB  . LEU   A 1 241 ? 15.918  -10.564 20.071  1.00 31.94  ? 240 LEU   A CB  1 
ATOM   1794 C CG  . LEU   A 1 241 ? 14.489  -10.357 20.552  1.00 32.21  ? 240 LEU   A CG  1 
ATOM   1795 C CD1 . LEU   A 1 241 ? 14.404  -9.027  21.269  1.00 34.95  ? 240 LEU   A CD1 1 
ATOM   1796 C CD2 . LEU   A 1 241 ? 13.531  -10.440 19.375  1.00 33.81  ? 240 LEU   A CD2 1 
ATOM   1797 N N   . GLN   A 1 242 ? 18.668  -11.968 19.388  1.00 37.86  ? 241 GLN   A N   1 
ATOM   1798 C CA  . GLN   A 1 242 ? 19.923  -11.972 18.638  1.00 40.31  ? 241 GLN   A CA  1 
ATOM   1799 C C   . GLN   A 1 242 ? 20.157  -13.306 17.942  1.00 36.42  ? 241 GLN   A C   1 
ATOM   1800 O O   . GLN   A 1 242 ? 20.757  -13.353 16.863  1.00 37.22  ? 241 GLN   A O   1 
ATOM   1801 C CB  . GLN   A 1 242 ? 21.166  -11.808 19.500  1.00 39.79  ? 241 GLN   A CB  1 
ATOM   1802 C CG  . GLN   A 1 242 ? 21.326  -10.455 20.151  1.00 52.87  ? 241 GLN   A CG  1 
ATOM   1803 C CD  . GLN   A 1 242 ? 22.659  -10.334 20.855  1.00 53.09  ? 241 GLN   A CD  1 
ATOM   1804 O OE1 . GLN   A 1 242 ? 22.711  -10.157 22.068  1.00 71.12  ? 241 GLN   A OE1 1 
ATOM   1805 N NE2 . GLN   A 1 242 ? 23.742  -10.493 20.104  1.00 61.69  ? 241 GLN   A NE2 1 
ATOM   1806 N N   . GLN   A 1 243 ? 19.687  -14.390 18.560  1.00 32.59  ? 242 GLN   A N   1 
ATOM   1807 C CA  . GLN   A 1 243 ? 19.796  -15.717 17.965  1.00 38.74  ? 242 GLN   A CA  1 
ATOM   1808 C C   . GLN   A 1 243 ? 18.788  -15.935 16.840  1.00 34.54  ? 242 GLN   A C   1 
ATOM   1809 O O   . GLN   A 1 243 ? 18.983  -16.793 15.968  1.00 38.86  ? 242 GLN   A O   1 
ATOM   1810 C CB  . GLN   A 1 243 ? 19.590  -16.806 19.021  1.00 35.03  ? 242 GLN   A CB  1 
ATOM   1811 C CG  . GLN   A 1 243 ? 20.665  -16.767 20.100  1.00 38.25  ? 242 GLN   A CG  1 
ATOM   1812 C CD  . GLN   A 1 243 ? 20.609  -17.932 21.068  1.00 38.57  ? 242 GLN   A CD  1 
ATOM   1813 O OE1 . GLN   A 1 243 ? 19.739  -18.066 21.936  1.00 44.98  ? 242 GLN   A OE1 1 
ATOM   1814 N NE2 . GLN   A 1 243 ? 21.587  -18.797 20.934  1.00 45.69  ? 242 GLN   A NE2 1 
ATOM   1815 N N   . MET   A 1 244 ? 17.657  -15.244 16.887  1.00 33.89  ? 243 MET   A N   1 
ATOM   1816 C CA  . MET   A 1 244 ? 16.664  -15.407 15.835  1.00 32.04  ? 243 MET   A CA  1 
ATOM   1817 C C   . MET   A 1 244 ? 16.890  -14.424 14.686  1.00 33.35  ? 243 MET   A C   1 
ATOM   1818 O O   . MET   A 1 244 ? 16.689  -14.798 13.536  1.00 36.95  ? 243 MET   A O   1 
ATOM   1819 C CB  . MET   A 1 244 ? 15.239  -15.245 16.368  1.00 34.70  ? 243 MET   A CB  1 
ATOM   1820 C CG  . MET   A 1 244 ? 14.892  -16.382 17.294  1.00 39.56  ? 243 MET   A CG  1 
ATOM   1821 S SD  . MET   A 1 244 ? 13.271  -16.225 18.053  1.00 35.09  ? 243 MET   A SD  1 
ATOM   1822 C CE  . MET   A 1 244 ? 12.360  -17.112 16.791  1.00 35.27  ? 243 MET   A CE  1 
ATOM   1823 N N   . LEU   A 1 245 ? 17.224  -13.174 15.006  1.00 33.46  ? 244 LEU   A N   1 
ATOM   1824 C CA  . LEU   A 1 245 ? 17.306  -12.106 14.017  1.00 34.67  ? 244 LEU   A CA  1 
ATOM   1825 C C   . LEU   A 1 245 ? 18.746  -11.987 13.503  1.00 33.18  ? 244 LEU   A C   1 
ATOM   1826 O O   . LEU   A 1 245 ? 19.459  -11.064 13.837  1.00 35.98  ? 244 LEU   A O   1 
ATOM   1827 C CB  . LEU   A 1 245 ? 16.810  -10.808 14.657  1.00 30.51  ? 244 LEU   A CB  1 
ATOM   1828 C CG  . LEU   A 1 245 ? 15.321  -10.754 14.985  1.00 31.77  ? 244 LEU   A CG  1 
ATOM   1829 C CD1 . LEU   A 1 245 ? 14.928  -9.411  15.599  1.00 35.89  ? 244 LEU   A CD1 1 
ATOM   1830 C CD2 . LEU   A 1 245 ? 14.441  -11.071 13.803  1.00 32.29  ? 244 LEU   A CD2 1 
ATOM   1831 N N   . GLN   A 1 246 ? 19.153  -12.993 12.743  1.00 35.63  ? 245 GLN   A N   1 
ATOM   1832 C CA  . GLN   A 1 246 ? 20.449  -13.093 12.107  1.00 37.84  ? 245 GLN   A CA  1 
ATOM   1833 C C   . GLN   A 1 246 ? 20.207  -12.958 10.610  1.00 32.66  ? 245 GLN   A C   1 
ATOM   1834 O O   . GLN   A 1 246 ? 19.409  -13.720 10.052  1.00 35.79  ? 245 GLN   A O   1 
ATOM   1835 C CB  . GLN   A 1 246 ? 21.033  -14.486 12.378  1.00 43.56  ? 245 GLN   A CB  1 
ATOM   1836 C CG  . GLN   A 1 246 ? 21.644  -14.627 13.767  1.00 46.63  ? 245 GLN   A CG  1 
ATOM   1837 C CD  . GLN   A 1 246 ? 22.769  -13.643 13.960  1.00 51.22  ? 245 GLN   A CD  1 
ATOM   1838 O OE1 . GLN   A 1 246 ? 23.782  -13.715 13.268  1.00 52.12  ? 245 GLN   A OE1 1 
ATOM   1839 N NE2 . GLN   A 1 246 ? 22.568  -12.661 14.829  1.00 55.75  ? 245 GLN   A NE2 1 
ATOM   1840 N N   . VAL   A 1 247 ? 20.842  -11.956 9.992   1.00 37.33  ? 246 VAL   A N   1 
ATOM   1841 C CA  . VAL   A 1 247 ? 20.538  -11.661 8.599   1.00 37.97  ? 246 VAL   A CA  1 
ATOM   1842 C C   . VAL   A 1 247 ? 20.941  -12.861 7.750   1.00 35.88  ? 246 VAL   A C   1 
ATOM   1843 O O   . VAL   A 1 247 ? 20.267  -13.190 6.772   1.00 37.02  ? 246 VAL   A O   1 
ATOM   1844 C CB  . VAL   A 1 247 ? 21.168  -10.358 8.060   1.00 42.85  ? 246 VAL   A CB  1 
ATOM   1845 C CG1 . VAL   A 1 247 ? 20.689  -9.141  8.849   1.00 43.36  ? 246 VAL   A CG1 1 
ATOM   1846 C CG2 . VAL   A 1 247 ? 22.683  -10.406 8.071   1.00 56.68  ? 246 VAL   A CG2 1 
ATOM   1847 N N   . ASP   A 1 248 ? 22.009  -13.530 8.185   1.00 37.57  ? 247 ASP   A N   1 
ATOM   1848 C CA  . ASP   A 1 248 ? 22.472  -14.729 7.518   1.00 39.82  ? 247 ASP   A CA  1 
ATOM   1849 C C   . ASP   A 1 248 ? 21.653  -15.898 8.023   1.00 40.27  ? 247 ASP   A C   1 
ATOM   1850 O O   . ASP   A 1 248 ? 21.740  -16.260 9.193   1.00 39.36  ? 247 ASP   A O   1 
ATOM   1851 C CB  . ASP   A 1 248 ? 23.964  -14.897 7.708   1.00 43.97  ? 247 ASP   A CB  1 
ATOM   1852 C CG  . ASP   A 1 248 ? 24.549  -16.157 7.086   1.00 51.29  ? 247 ASP   A CG  1 
ATOM   1853 O OD1 . ASP   A 1 248 ? 23.777  -17.016 6.562   1.00 41.30  ? 247 ASP   A OD1 1 
ATOM   1854 O OD2 . ASP   A 1 248 ? 25.774  -16.261 7.164   1.00 53.63  ? 247 ASP   A OD2 1 
ATOM   1855 N N   . PRO   A 1 249 ? 20.835  -16.521 7.150   1.00 36.45  ? 248 PRO   A N   1 
ATOM   1856 C CA  . PRO   A 1 249 ? 19.892  -17.546 7.559   1.00 36.71  ? 248 PRO   A CA  1 
ATOM   1857 C C   . PRO   A 1 249 ? 20.570  -18.758 8.179   1.00 48.18  ? 248 PRO   A C   1 
ATOM   1858 O O   . PRO   A 1 249 ? 19.979  -19.448 8.995   1.00 41.19  ? 248 PRO   A O   1 
ATOM   1859 C CB  . PRO   A 1 249 ? 19.171  -17.946 6.287   1.00 37.15  ? 248 PRO   A CB  1 
ATOM   1860 C CG  . PRO   A 1 249 ? 20.017  -17.418 5.178   1.00 40.03  ? 248 PRO   A CG  1 
ATOM   1861 C CD  . PRO   A 1 249 ? 20.806  -16.263 5.705   1.00 40.62  ? 248 PRO   A CD  1 
ATOM   1862 N N   . LYS   A 1 250 ? 21.790  -19.022 7.711   1.00 46.83  ? 249 LYS   A N   1 
ATOM   1863 C CA  . LYS   A 1 250 ? 22.538  -20.155 8.197   1.00 53.19  ? 249 LYS   A CA  1 
ATOM   1864 C C   . LYS   A 1 250 ? 22.856  -19.960 9.670   1.00 49.02  ? 249 LYS   A C   1 
ATOM   1865 O O   . LYS   A 1 250 ? 22.968  -20.950 10.354  1.00 48.81  ? 249 LYS   A O   1 
ATOM   1866 C CB  . LYS   A 1 250 ? 23.864  -20.300 7.447   1.00 53.31  ? 249 LYS   A CB  1 
ATOM   1867 C CG  . LYS   A 1 250 ? 23.747  -20.463 5.950   1.00 61.08  ? 249 LYS   A CG  1 
ATOM   1868 C CD  . LYS   A 1 250 ? 25.118  -20.641 5.319   1.00 65.63  ? 249 LYS   A CD  1 
ATOM   1869 C CE  . LYS   A 1 250 ? 25.966  -19.400 5.398   1.00 67.11  ? 249 LYS   A CE  1 
ATOM   1870 N NZ  . LYS   A 1 250 ? 27.384  -19.763 5.432   1.00 67.07  ? 249 LYS   A NZ  1 
ATOM   1871 N N   . LYS   A 1 251 ? 23.010  -18.711 10.135  1.00 46.04  ? 250 LYS   A N   1 
ATOM   1872 C CA  . LYS   A 1 251 ? 23.387  -18.430 11.509  1.00 47.34  ? 250 LYS   A CA  1 
ATOM   1873 C C   . LYS   A 1 251 ? 22.197  -18.380 12.459  1.00 47.27  ? 250 LYS   A C   1 
ATOM   1874 O O   . LYS   A 1 251 ? 22.387  -18.146 13.648  1.00 48.73  ? 250 LYS   A O   1 
ATOM   1875 C CB  . LYS   A 1 251 ? 24.097  -17.088 11.620  1.00 46.95  ? 250 LYS   A CB  1 
ATOM   1876 C CG  . LYS   A 1 251 ? 25.446  -17.115 10.939  1.00 50.09  ? 250 LYS   A CG  1 
ATOM   1877 C CD  . LYS   A 1 251 ? 26.268  -15.845 11.061  1.00 52.22  ? 250 LYS   A CD  1 
ATOM   1878 C CE  . LYS   A 1 251 ? 27.514  -16.042 10.243  1.00 61.49  ? 250 LYS   A CE  1 
ATOM   1879 N NZ  . LYS   A 1 251 ? 28.283  -14.797 10.180  1.00 68.70  ? 250 LYS   A NZ  1 
ATOM   1880 N N   . ARG   A 1 252 ? 20.991  -18.582 11.932  1.00 50.75  ? 251 ARG   A N   1 
ATOM   1881 C CA  . ARG   A 1 252 ? 19.797  -18.471 12.742  1.00 48.71  ? 251 ARG   A CA  1 
ATOM   1882 C C   . ARG   A 1 252 ? 19.580  -19.779 13.490  1.00 49.94  ? 251 ARG   A C   1 
ATOM   1883 O O   . ARG   A 1 252 ? 19.690  -20.868 12.922  1.00 44.34  ? 251 ARG   A O   1 
ATOM   1884 C CB  . ARG   A 1 252 ? 18.502  -18.184 11.953  1.00 44.74  ? 251 ARG   A CB  1 
ATOM   1885 C CG  . ARG   A 1 252 ? 18.376  -16.762 11.441  1.00 42.17  ? 251 ARG   A CG  1 
ATOM   1886 C CD  . ARG   A 1 252 ? 17.205  -16.686 10.503  1.00 38.07  ? 251 ARG   A CD  1 
ATOM   1887 N NE  . ARG   A 1 252 ? 17.386  -15.526 9.626   1.00 35.61  ? 251 ARG   A NE  1 
ATOM   1888 C CZ  . ARG   A 1 252 ? 17.142  -15.529 8.334   1.00 31.61  ? 251 ARG   A CZ  1 
ATOM   1889 N NH1 . ARG   A 1 252 ? 16.283  -16.362 7.824   1.00 34.82  ? 251 ARG   A NH1 1 
ATOM   1890 N NH2 . ARG   A 1 252 ? 17.761  -14.645 7.571   1.00 38.73  ? 251 ARG   A NH2 1 
ATOM   1891 N N   . ILE   A 1 253 ? 19.162  -19.628 14.739  1.00 44.86  ? 252 ILE   A N   1 
ATOM   1892 C CA  . ILE   A 1 253 ? 18.715  -20.755 15.505  1.00 42.04  ? 252 ILE   A CA  1 
ATOM   1893 C C   . ILE   A 1 253 ? 17.739  -21.577 14.686  1.00 48.54  ? 252 ILE   A C   1 
ATOM   1894 O O   . ILE   A 1 253 ? 16.902  -21.105 13.916  1.00 45.88  ? 252 ILE   A O   1 
ATOM   1895 C CB  . ILE   A 1 253 ? 18.164  -20.259 16.853  1.00 52.62  ? 252 ILE   A CB  1 
ATOM   1896 C CG1 . ILE   A 1 253 ? 18.454  -21.245 17.962  1.00 50.14  ? 252 ILE   A CG1 1 
ATOM   1897 C CG2 . ILE   A 1 253 ? 16.684  -19.869 16.756  1.00 52.44  ? 252 ILE   A CG2 1 
ATOM   1898 C CD1 . ILE   A 1 253 ? 18.066  -20.726 19.336  1.00 48.95  ? 252 ILE   A CD1 1 
ATOM   1899 N N   . SER   A 1 254 ? 17.888  -22.867 14.912  1.00 50.61  ? 253 SER   A N   1 
ATOM   1900 C CA  . SER   A 1 254 ? 17.058  -23.901 14.362  1.00 56.71  ? 253 SER   A CA  1 
ATOM   1901 C C   . SER   A 1 254 ? 15.779  -23.899 15.166  1.00 58.21  ? 253 SER   A C   1 
ATOM   1902 O O   . SER   A 1 254 ? 15.793  -23.478 16.329  1.00 51.80  ? 253 SER   A O   1 
ATOM   1903 C CB  . SER   A 1 254 ? 17.833  -25.228 14.501  1.00 65.35  ? 253 SER   A CB  1 
ATOM   1904 O OG  . SER   A 1 254 ? 18.561  -25.241 15.734  1.00 46.63  ? 253 SER   A OG  1 
ATOM   1905 N N   . MET   A 1 255 ? 14.720  -24.466 14.601  1.00 59.89  ? 254 MET   A N   1 
ATOM   1906 C CA  . MET   A 1 255 ? 13.464  -24.509 15.324  1.00 64.49  ? 254 MET   A CA  1 
ATOM   1907 C C   . MET   A 1 255 ? 13.615  -25.376 16.575  1.00 80.25  ? 254 MET   A C   1 
ATOM   1908 O O   . MET   A 1 255 ? 12.774  -25.337 17.492  1.00 61.46  ? 254 MET   A O   1 
ATOM   1909 C CB  . MET   A 1 255 ? 12.344  -25.174 14.526  1.00 72.17  ? 254 MET   A CB  1 
ATOM   1910 C CG  . MET   A 1 255 ? 10.983  -24.746 15.027  1.00 73.70  ? 254 MET   A CG  1 
ATOM   1911 S SD  . MET   A 1 255 ? 10.691  -23.058 14.480  1.00 86.14  ? 254 MET   A SD  1 
ATOM   1912 C CE  . MET   A 1 255 ? 9.339   -22.633 15.589  1.00 87.84  ? 254 MET   A CE  1 
ATOM   1913 N N   . LYS   A 1 256 ? 14.668  -26.205 16.577  1.00 67.84  ? 255 LYS   A N   1 
ATOM   1914 C CA  . LYS   A 1 256 ? 14.731  -27.256 17.564  1.00 70.12  ? 255 LYS   A CA  1 
ATOM   1915 C C   . LYS   A 1 256 ? 15.623  -26.809 18.704  1.00 61.00  ? 255 LYS   A C   1 
ATOM   1916 O O   . LYS   A 1 256 ? 15.335  -27.180 19.836  1.00 62.42  ? 255 LYS   A O   1 
ATOM   1917 C CB  . LYS   A 1 256 ? 15.018  -28.577 16.850  1.00 79.07  ? 255 LYS   A CB  1 
ATOM   1918 C CG  . LYS   A 1 256 ? 13.808  -28.986 15.985  1.00 75.02  ? 255 LYS   A CG  1 
ATOM   1919 C CD  . LYS   A 1 256 ? 13.740  -30.446 15.566  1.00 79.24  ? 255 LYS   A CD  1 
ATOM   1920 C CE  . LYS   A 1 256 ? 13.499  -31.326 16.744  1.00 78.89  ? 255 LYS   A CE  1 
ATOM   1921 N NZ  . LYS   A 1 256 ? 14.158  -32.622 16.551  1.00 87.17  ? 255 LYS   A NZ  1 
ATOM   1922 N N   . ASN   A 1 257 ? 16.602  -25.929 18.438  1.00 52.84  ? 256 ASN   A N   1 
ATOM   1923 C CA  . ASN   A 1 257 ? 17.227  -25.234 19.551  1.00 65.02  ? 256 ASN   A CA  1 
ATOM   1924 C C   . ASN   A 1 257 ? 16.222  -24.259 20.200  1.00 63.44  ? 256 ASN   A C   1 
ATOM   1925 O O   . ASN   A 1 257 ? 16.468  -23.834 21.331  1.00 46.97  ? 256 ASN   A O   1 
ATOM   1926 C CB  . ASN   A 1 257 ? 18.618  -24.690 19.198  1.00 64.80  ? 256 ASN   A CB  1 
ATOM   1927 C CG  . ASN   A 1 257 ? 19.741  -25.715 19.304  1.00 60.00  ? 256 ASN   A CG  1 
ATOM   1928 O OD1 . ASN   A 1 257 ? 19.656  -26.713 20.028  1.00 62.75  ? 256 ASN   A OD1 1 
ATOM   1929 N ND2 . ASN   A 1 257 ? 20.830  -25.493 18.595  1.00 51.31  ? 256 ASN   A ND2 1 
ATOM   1930 N N   . LEU   A 1 258 ? 15.069  -23.966 19.552  1.00 52.08  ? 257 LEU   A N   1 
ATOM   1931 C CA  . LEU   A 1 258 ? 14.138  -22.950 20.033  1.00 47.66  ? 257 LEU   A CA  1 
ATOM   1932 C C   . LEU   A 1 258 ? 13.104  -23.545 20.992  1.00 46.31  ? 257 LEU   A C   1 
ATOM   1933 O O   . LEU   A 1 258 ? 12.709  -22.939 21.990  1.00 41.82  ? 257 LEU   A O   1 
ATOM   1934 C CB  . LEU   A 1 258 ? 13.512  -22.273 18.807  1.00 49.92  ? 257 LEU   A CB  1 
ATOM   1935 C CG  . LEU   A 1 258 ? 12.491  -21.159 19.053  1.00 46.64  ? 257 LEU   A CG  1 
ATOM   1936 C CD1 . LEU   A 1 258 ? 13.093  -20.002 19.814  1.00 47.14  ? 257 LEU   A CD1 1 
ATOM   1937 C CD2 . LEU   A 1 258 ? 11.962  -20.653 17.708  1.00 49.57  ? 257 LEU   A CD2 1 
ATOM   1938 N N   . LEU   A 1 259 ? 12.662  -24.780 20.732  1.00 43.64  ? 258 LEU   A N   1 
ATOM   1939 C CA  . LEU   A 1 259 ? 11.731  -25.440 21.629  1.00 45.83  ? 258 LEU   A CA  1 
ATOM   1940 C C   . LEU   A 1 259 ? 12.338  -25.585 23.031  1.00 43.01  ? 258 LEU   A C   1 
ATOM   1941 O O   . LEU   A 1 259 ? 11.603  -25.666 24.014  1.00 43.19  ? 258 LEU   A O   1 
ATOM   1942 C CB  . LEU   A 1 259 ? 11.419  -26.828 21.070  1.00 48.42  ? 258 LEU   A CB  1 
ATOM   1943 C CG  . LEU   A 1 259 ? 10.726  -26.847 19.713  1.00 48.70  ? 258 LEU   A CG  1 
ATOM   1944 C CD1 . LEU   A 1 259 ? 10.958  -28.169 19.031  1.00 55.37  ? 258 LEU   A CD1 1 
ATOM   1945 C CD2 . LEU   A 1 259 ? 9.273   -26.588 19.946  1.00 45.42  ? 258 LEU   A CD2 1 
ATOM   1946 N N   . ASN   A 1 260 ? 13.675  -25.669 23.075  1.00 41.96  ? 259 ASN   A N   1 
ATOM   1947 C CA  . ASN   A 1 260 ? 14.422  -25.997 24.283  1.00 49.65  ? 259 ASN   A CA  1 
ATOM   1948 C C   . ASN   A 1 260 ? 15.084  -24.761 24.876  1.00 50.57  ? 259 ASN   A C   1 
ATOM   1949 O O   . ASN   A 1 260 ? 15.824  -24.876 25.864  1.00 45.37  ? 259 ASN   A O   1 
ATOM   1950 C CB  . ASN   A 1 260 ? 15.521  -27.013 23.970  1.00 51.97  ? 259 ASN   A CB  1 
ATOM   1951 C CG  . ASN   A 1 260 ? 14.933  -28.327 23.507  1.00 58.80  ? 259 ASN   A CG  1 
ATOM   1952 O OD1 . ASN   A 1 260 ? 14.037  -28.877 24.169  1.00 59.60  ? 259 ASN   A OD1 1 
ATOM   1953 N ND2 . ASN   A 1 260 ? 15.402  -28.825 22.370  1.00 50.94  ? 259 ASN   A ND2 1 
ATOM   1954 N N   . HIS   A 1 261 ? 14.810  -23.590 24.266  1.00 44.54  ? 260 HIS   A N   1 
ATOM   1955 C CA  . HIS   A 1 261 ? 15.591  -22.400 24.547  1.00 38.96  ? 260 HIS   A CA  1 
ATOM   1956 C C   . HIS   A 1 261 ? 15.329  -21.975 25.985  1.00 35.78  ? 260 HIS   A C   1 
ATOM   1957 O O   . HIS   A 1 261 ? 14.194  -22.016 26.472  1.00 37.94  ? 260 HIS   A O   1 
ATOM   1958 C CB  . HIS   A 1 261 ? 15.329  -21.298 23.506  1.00 36.82  ? 260 HIS   A CB  1 
ATOM   1959 C CG  . HIS   A 1 261 ? 16.300  -20.195 23.593  1.00 33.32  ? 260 HIS   A CG  1 
ATOM   1960 N ND1 . HIS   A 1 261 ? 16.221  -19.256 24.590  1.00 33.12  ? 260 HIS   A ND1 1 
ATOM   1961 C CD2 . HIS   A 1 261 ? 17.368  -19.866 22.845  1.00 35.35  ? 260 HIS   A CD2 1 
ATOM   1962 C CE1 . HIS   A 1 261 ? 17.193  -18.367 24.424  1.00 32.24  ? 260 HIS   A CE1 1 
ATOM   1963 N NE2 . HIS   A 1 261 ? 17.923  -18.732 23.403  1.00 34.31  ? 260 HIS   A NE2 1 
ATOM   1964 N N   . PRO   A 1 262 ? 16.382  -21.568 26.723  1.00 34.60  ? 261 PRO   A N   1 
ATOM   1965 C CA  . PRO   A 1 262 ? 16.217  -21.085 28.094  1.00 37.06  ? 261 PRO   A CA  1 
ATOM   1966 C C   . PRO   A 1 262 ? 15.124  -20.044 28.257  1.00 37.52  ? 261 PRO   A C   1 
ATOM   1967 O O   . PRO   A 1 262 ? 14.367  -20.109 29.219  1.00 39.72  ? 261 PRO   A O   1 
ATOM   1968 C CB  . PRO   A 1 262 ? 17.571  -20.519 28.449  1.00 38.49  ? 261 PRO   A CB  1 
ATOM   1969 C CG  . PRO   A 1 262 ? 18.510  -21.434 27.667  1.00 43.53  ? 261 PRO   A CG  1 
ATOM   1970 C CD  . PRO   A 1 262 ? 17.785  -21.604 26.317  1.00 39.14  ? 261 PRO   A CD  1 
ATOM   1971 N N   . TRP   A 1 263 ? 15.004  -19.123 27.303  1.00 35.31  ? 262 TRP   A N   1 
ATOM   1972 C CA  . TRP   A 1 263 ? 14.004  -18.081 27.441  1.00 36.43  ? 262 TRP   A CA  1 
ATOM   1973 C C   . TRP   A 1 263 ? 12.606  -18.688 27.355  1.00 37.38  ? 262 TRP   A C   1 
ATOM   1974 O O   . TRP   A 1 263 ? 11.698  -18.283 28.068  1.00 38.44  ? 262 TRP   A O   1 
ATOM   1975 C CB  . TRP   A 1 263 ? 14.227  -16.977 26.394  1.00 36.94  ? 262 TRP   A CB  1 
ATOM   1976 C CG  . TRP   A 1 263 ? 13.217  -15.867 26.466  1.00 39.53  ? 262 TRP   A CG  1 
ATOM   1977 C CD1 . TRP   A 1 263 ? 13.384  -14.655 27.066  1.00 38.16  ? 262 TRP   A CD1 1 
ATOM   1978 C CD2 . TRP   A 1 263 ? 11.873  -15.873 25.925  1.00 34.00  ? 262 TRP   A CD2 1 
ATOM   1979 N NE1 . TRP   A 1 263 ? 12.256  -13.904 26.905  1.00 38.82  ? 262 TRP   A NE1 1 
ATOM   1980 C CE2 . TRP   A 1 263 ? 11.307  -14.617 26.238  1.00 35.91  ? 262 TRP   A CE2 1 
ATOM   1981 C CE3 . TRP   A 1 263 ? 11.101  -16.799 25.225  1.00 35.50  ? 262 TRP   A CE3 1 
ATOM   1982 C CZ2 . TRP   A 1 263 ? 10.005  -14.276 25.880  1.00 35.60  ? 262 TRP   A CZ2 1 
ATOM   1983 C CZ3 . TRP   A 1 263 ? 9.801   -16.474 24.886  1.00 34.84  ? 262 TRP   A CZ3 1 
ATOM   1984 C CH2 . TRP   A 1 263 ? 9.268   -15.225 25.211  1.00 36.74  ? 262 TRP   A CH2 1 
ATOM   1985 N N   . ILE   A 1 264 ? 12.464  -19.685 26.500  1.00 35.09  ? 263 ILE   A N   1 
ATOM   1986 C CA  . ILE   A 1 264 ? 11.206  -20.355 26.258  1.00 39.53  ? 263 ILE   A CA  1 
ATOM   1987 C C   . ILE   A 1 264 ? 10.812  -21.164 27.486  1.00 44.83  ? 263 ILE   A C   1 
ATOM   1988 O O   . ILE   A 1 264 ? 9.620   -21.332 27.728  1.00 40.30  ? 263 ILE   A O   1 
ATOM   1989 C CB  . ILE   A 1 264 ? 11.357  -21.225 24.996  1.00 38.24  ? 263 ILE   A CB  1 
ATOM   1990 C CG1 . ILE   A 1 264 ? 11.302  -20.370 23.725  1.00 41.98  ? 263 ILE   A CG1 1 
ATOM   1991 C CG2 . ILE   A 1 264 ? 10.335  -22.362 24.908  1.00 42.83  ? 263 ILE   A CG2 1 
ATOM   1992 C CD1 . ILE   A 1 264 ? 9.874   -20.037 23.321  1.00 41.26  ? 263 ILE   A CD1 1 
ATOM   1993 N N   . MET   A 1 265 ? 11.805  -21.664 28.220  1.00 45.72  ? 264 MET   A N   1 
ATOM   1994 C CA  . MET   A 1 265 ? 11.551  -22.568 29.371  1.00 47.10  ? 264 MET   A CA  1 
ATOM   1995 C C   . MET   A 1 265 ? 11.327  -21.802 30.688  1.00 52.70  ? 264 MET   A C   1 
ATOM   1996 O O   . MET   A 1 265 ? 10.701  -22.380 31.586  1.00 53.00  ? 264 MET   A O   1 
ATOM   1997 C CB  . MET   A 1 265 ? 12.745  -23.503 29.560  1.00 47.06  ? 264 MET   A CB  1 
ATOM   1998 C CG  . MET   A 1 265 ? 13.127  -24.261 28.327  1.00 48.23  ? 264 MET   A CG  1 
ATOM   1999 S SD  . MET   A 1 265 ? 12.201  -25.801 28.308  1.00 76.29  ? 264 MET   A SD  1 
ATOM   2000 C CE  . MET   A 1 265 ? 13.562  -26.918 27.949  1.00 64.70  ? 264 MET   A CE  1 
ATOM   2001 N N   . GLN   A 1 266 ? 11.836  -20.578 30.812  1.00 50.22  ? 265 GLN   A N   1 
ATOM   2002 C CA  . GLN   A 1 266 ? 11.670  -19.839 32.058  1.00 55.14  ? 265 GLN   A CA  1 
ATOM   2003 C C   . GLN   A 1 266 ? 10.212  -19.888 32.515  1.00 60.29  ? 265 GLN   A C   1 
ATOM   2004 O O   . GLN   A 1 266 ? 9.311   -19.498 31.770  1.00 52.94  ? 265 GLN   A O   1 
ATOM   2005 C CB  . GLN   A 1 266 ? 12.182  -18.404 31.970  1.00 58.15  ? 265 GLN   A CB  1 
ATOM   2006 C CG  . GLN   A 1 266 ? 13.644  -18.263 32.384  1.00 76.45  ? 265 GLN   A CG  1 
ATOM   2007 C CD  . GLN   A 1 266 ? 14.325  -17.076 31.729  1.00 88.28  ? 265 GLN   A CD  1 
ATOM   2008 O OE1 . GLN   A 1 266 ? 15.335  -17.202 31.015  1.00 78.78  ? 265 GLN   A OE1 1 
ATOM   2009 N NE2 . GLN   A 1 266 ? 13.748  -15.902 31.947  1.00 84.87  ? 265 GLN   A NE2 1 
ATOM   2010 N N   . ASP   A 1 267 ? 10.007  -20.403 33.743  1.00 56.71  ? 266 ASP   A N   1 
ATOM   2011 C CA  . ASP   A 1 267 ? 8.731   -20.363 34.452  1.00 61.06  ? 266 ASP   A CA  1 
ATOM   2012 C C   . ASP   A 1 267 ? 7.780   -21.471 34.009  1.00 62.04  ? 266 ASP   A C   1 
ATOM   2013 O O   . ASP   A 1 267 ? 6.639   -21.481 34.448  1.00 80.88  ? 266 ASP   A O   1 
ATOM   2014 C CB  . ASP   A 1 267 ? 8.011   -19.032 34.317  1.00 60.84  ? 266 ASP   A CB  1 
ATOM   2015 C CG  . ASP   A 1 267 ? 8.834   -17.838 34.771  1.00 72.84  ? 266 ASP   A CG  1 
ATOM   2016 O OD1 . ASP   A 1 267 ? 10.027  -18.041 35.093  1.00 85.29  ? 266 ASP   A OD1 1 
ATOM   2017 O OD2 . ASP   A 1 267 ? 8.285   -16.725 34.781  1.00 77.82  ? 266 ASP   A OD2 1 
ATOM   2018 N N   . TYR   A 1 268 ? 8.246   -22.366 33.135  1.00 55.43  ? 267 TYR   A N   1 
ATOM   2019 C CA  . TYR   A 1 268 ? 7.496   -23.519 32.667  1.00 58.51  ? 267 TYR   A CA  1 
ATOM   2020 C C   . TYR   A 1 268 ? 8.260   -24.769 33.076  1.00 58.04  ? 267 TYR   A C   1 
ATOM   2021 O O   . TYR   A 1 268 ? 7.676   -25.723 33.580  1.00 66.25  ? 267 TYR   A O   1 
ATOM   2022 C CB  . TYR   A 1 268 ? 7.317   -23.503 31.141  1.00 55.97  ? 267 TYR   A CB  1 
ATOM   2023 C CG  . TYR   A 1 268 ? 6.241   -22.522 30.698  1.00 53.67  ? 267 TYR   A CG  1 
ATOM   2024 C CD1 . TYR   A 1 268 ? 6.498   -21.157 30.661  1.00 55.79  ? 267 TYR   A CD1 1 
ATOM   2025 C CD2 . TYR   A 1 268 ? 4.950   -22.955 30.416  1.00 56.09  ? 267 TYR   A CD2 1 
ATOM   2026 C CE1 . TYR   A 1 268 ? 5.520   -20.249 30.288  1.00 53.35  ? 267 TYR   A CE1 1 
ATOM   2027 C CE2 . TYR   A 1 268 ? 3.964   -22.059 30.041  1.00 59.88  ? 267 TYR   A CE2 1 
ATOM   2028 C CZ  . TYR   A 1 268 ? 4.252   -20.704 29.981  1.00 52.30  ? 267 TYR   A CZ  1 
ATOM   2029 O OH  . TYR   A 1 268 ? 3.272   -19.833 29.629  1.00 61.89  ? 267 TYR   A OH  1 
ATOM   2030 N N   . ASN   A 1 269 ? 9.567   -24.740 32.785  1.00 72.05  ? 268 ASN   A N   1 
ATOM   2031 C CA  . ASN   A 1 269 ? 10.506  -25.780 33.160  1.00 75.43  ? 268 ASN   A CA  1 
ATOM   2032 C C   . ASN   A 1 269 ? 10.234  -27.034 32.329  1.00 81.05  ? 268 ASN   A C   1 
ATOM   2033 O O   . ASN   A 1 269 ? 10.709  -28.110 32.682  1.00 78.99  ? 268 ASN   A O   1 
ATOM   2034 C CB  . ASN   A 1 269 ? 10.492  -26.017 34.669  1.00 75.20  ? 268 ASN   A CB  1 
ATOM   2035 C CG  . ASN   A 1 269 ? 10.494  -24.724 35.455  1.00 79.88  ? 268 ASN   A CG  1 
ATOM   2036 O OD1 . ASN   A 1 269 ? 9.538   -24.437 36.186  1.00 81.36  ? 268 ASN   A OD1 1 
ATOM   2037 N ND2 . ASN   A 1 269 ? 11.536  -23.917 35.298  1.00 81.62  ? 268 ASN   A ND2 1 
ATOM   2038 N N   . TYR   A 1 270 ? 9.499   -26.898 31.211  1.00 80.50  ? 269 TYR   A N   1 
ATOM   2039 C CA  . TYR   A 1 270 ? 9.376   -27.991 30.257  1.00 72.18  ? 269 TYR   A CA  1 
ATOM   2040 C C   . TYR   A 1 270 ? 9.259   -27.430 28.848  1.00 70.37  ? 269 TYR   A C   1 
ATOM   2041 O O   . TYR   A 1 270 ? 8.657   -26.375 28.660  1.00 68.35  ? 269 TYR   A O   1 
ATOM   2042 C CB  . TYR   A 1 270 ? 8.185   -28.910 30.530  1.00 69.31  ? 269 TYR   A CB  1 
ATOM   2043 C CG  . TYR   A 1 270 ? 6.837   -28.222 30.482  1.00 71.95  ? 269 TYR   A CG  1 
ATOM   2044 C CD1 . TYR   A 1 270 ? 6.319   -27.583 31.606  1.00 78.57  ? 269 TYR   A CD1 1 
ATOM   2045 C CD2 . TYR   A 1 270 ? 6.086   -28.209 29.315  1.00 68.62  ? 269 TYR   A CD2 1 
ATOM   2046 C CE1 . TYR   A 1 270 ? 5.083   -26.952 31.572  1.00 72.62  ? 269 TYR   A CE1 1 
ATOM   2047 C CE2 . TYR   A 1 270 ? 4.845   -27.592 29.270  1.00 67.73  ? 269 TYR   A CE2 1 
ATOM   2048 C CZ  . TYR   A 1 270 ? 4.347   -26.961 30.399  1.00 70.92  ? 269 TYR   A CZ  1 
ATOM   2049 O OH  . TYR   A 1 270 ? 3.142   -26.330 30.347  1.00 73.46  ? 269 TYR   A OH  1 
ATOM   2050 N N   . PRO   A 1 271 ? 9.791   -28.136 27.821  1.00 74.90  ? 270 PRO   A N   1 
ATOM   2051 C CA  . PRO   A 1 271 ? 9.886   -27.580 26.471  1.00 71.83  ? 270 PRO   A CA  1 
ATOM   2052 C C   . PRO   A 1 271 ? 8.511   -27.437 25.823  1.00 62.46  ? 270 PRO   A C   1 
ATOM   2053 O O   . PRO   A 1 271 ? 7.509   -27.993 26.284  1.00 52.21  ? 270 PRO   A O   1 
ATOM   2054 C CB  . PRO   A 1 271 ? 10.802  -28.550 25.691  1.00 72.56  ? 270 PRO   A CB  1 
ATOM   2055 C CG  . PRO   A 1 271 ? 11.232  -29.609 26.703  1.00 73.62  ? 270 PRO   A CG  1 
ATOM   2056 C CD  . PRO   A 1 271 ? 10.282  -29.522 27.881  1.00 73.44  ? 270 PRO   A CD  1 
ATOM   2057 N N   . VAL   A 1 272 ? 8.468   -26.677 24.732  1.00 60.71  ? 271 VAL   A N   1 
ATOM   2058 C CA  . VAL   A 1 272 ? 7.216   -26.554 24.007  1.00 49.73  ? 271 VAL   A CA  1 
ATOM   2059 C C   . VAL   A 1 272 ? 6.862   -27.926 23.458  1.00 54.75  ? 271 VAL   A C   1 
ATOM   2060 O O   . VAL   A 1 272 ? 7.669   -28.484 22.719  1.00 45.14  ? 271 VAL   A O   1 
ATOM   2061 C CB  . VAL   A 1 272 ? 7.340   -25.572 22.840  1.00 50.05  ? 271 VAL   A CB  1 
ATOM   2062 C CG1 . VAL   A 1 272 ? 6.054   -25.563 22.010  1.00 47.67  ? 271 VAL   A CG1 1 
ATOM   2063 C CG2 . VAL   A 1 272 ? 7.730   -24.187 23.335  1.00 50.44  ? 271 VAL   A CG2 1 
ATOM   2064 N N   . GLU   A 1 273 ? 5.658   -28.414 23.793  1.00 65.06  ? 272 GLU   A N   1 
ATOM   2065 C CA  . GLU   A 1 273 ? 5.100   -29.611 23.182  1.00 74.35  ? 272 GLU   A CA  1 
ATOM   2066 C C   . GLU   A 1 273 ? 4.494   -29.242 21.830  1.00 64.51  ? 272 GLU   A C   1 
ATOM   2067 O O   . GLU   A 1 273 ? 3.399   -28.684 21.757  1.00 64.27  ? 272 GLU   A O   1 
ATOM   2068 C CB  . GLU   A 1 273 ? 4.008   -30.225 24.060  1.00 87.53  ? 272 GLU   A CB  1 
ATOM   2069 C CG  . GLU   A 1 273 ? 4.547   -30.870 25.331  1.00 103.98 ? 272 GLU   A CG  1 
ATOM   2070 C CD  . GLU   A 1 273 ? 3.484   -31.085 26.385  1.00 117.38 ? 272 GLU   A CD  1 
ATOM   2071 O OE1 . GLU   A 1 273 ? 2.287   -31.016 26.043  1.00 133.98 ? 272 GLU   A OE1 1 
ATOM   2072 O OE2 . GLU   A 1 273 ? 3.878   -31.281 27.555  1.00 119.19 ? 272 GLU   A OE2 1 
ATOM   2073 N N   . TRP   A 1 274 ? 5.234   -29.537 20.764  1.00 62.54  ? 273 TRP   A N   1 
ATOM   2074 C CA  . TRP   A 1 274 ? 4.840   -29.122 19.428  1.00 61.89  ? 273 TRP   A CA  1 
ATOM   2075 C C   . TRP   A 1 274 ? 4.041   -30.205 18.709  1.00 62.30  ? 273 TRP   A C   1 
ATOM   2076 O O   . TRP   A 1 274 ? 3.376   -29.916 17.735  1.00 50.43  ? 273 TRP   A O   1 
ATOM   2077 C CB  . TRP   A 1 274 ? 6.077   -28.754 18.611  1.00 64.54  ? 273 TRP   A CB  1 
ATOM   2078 C CG  . TRP   A 1 274 ? 7.089   -29.861 18.515  1.00 70.37  ? 273 TRP   A CG  1 
ATOM   2079 C CD1 . TRP   A 1 274 ? 8.112   -30.120 19.378  1.00 71.04  ? 273 TRP   A CD1 1 
ATOM   2080 C CD2 . TRP   A 1 274 ? 7.161   -30.872 17.491  1.00 77.24  ? 273 TRP   A CD2 1 
ATOM   2081 N NE1 . TRP   A 1 274 ? 8.831   -31.206 18.951  1.00 74.51  ? 273 TRP   A NE1 1 
ATOM   2082 C CE2 . TRP   A 1 274 ? 8.274   -31.690 17.798  1.00 80.34  ? 273 TRP   A CE2 1 
ATOM   2083 C CE3 . TRP   A 1 274 ? 6.399   -31.163 16.358  1.00 78.33  ? 273 TRP   A CE3 1 
ATOM   2084 C CZ2 . TRP   A 1 274 ? 8.643   -32.778 17.011  1.00 79.38  ? 273 TRP   A CZ2 1 
ATOM   2085 C CZ3 . TRP   A 1 274 ? 6.765   -32.242 15.582  1.00 87.82  ? 273 TRP   A CZ3 1 
ATOM   2086 C CH2 . TRP   A 1 274 ? 7.868   -33.038 15.904  1.00 82.14  ? 273 TRP   A CH2 1 
ATOM   2087 N N   . GLN   A 1 275 ? 4.140   -31.453 19.168  1.00 65.95  ? 274 GLN   A N   1 
ATOM   2088 C CA  . GLN   A 1 275 ? 3.489   -32.583 18.530  1.00 61.76  ? 274 GLN   A CA  1 
ATOM   2089 C C   . GLN   A 1 275 ? 1.991   -32.385 18.710  1.00 61.90  ? 274 GLN   A C   1 
ATOM   2090 O O   . GLN   A 1 275 ? 1.572   -31.846 19.730  1.00 54.73  ? 274 GLN   A O   1 
ATOM   2091 C CB  . GLN   A 1 275 ? 3.923   -33.905 19.180  1.00 66.43  ? 274 GLN   A CB  1 
ATOM   2092 C CG  . GLN   A 1 275 ? 5.424   -34.045 19.446  1.00 76.98  ? 274 GLN   A CG  1 
ATOM   2093 C CD  . GLN   A 1 275 ? 5.973   -33.172 20.571  1.00 90.37  ? 274 GLN   A CD  1 
ATOM   2094 O OE1 . GLN   A 1 275 ? 5.260   -32.638 21.439  1.00 71.16  ? 274 GLN   A OE1 1 
ATOM   2095 N NE2 . GLN   A 1 275 ? 7.290   -33.020 20.575  1.00 96.81  ? 274 GLN   A NE2 1 
ATOM   2096 N N   . SER   A 1 276 ? 1.193   -32.831 17.728  1.00 71.88  ? 275 SER   A N   1 
ATOM   2097 C CA  . SER   A 1 276 ? -0.256  -32.660 17.771  1.00 81.21  ? 275 SER   A CA  1 
ATOM   2098 C C   . SER   A 1 276 ? -0.876  -33.552 18.849  1.00 84.97  ? 275 SER   A C   1 
ATOM   2099 O O   . SER   A 1 276 ? -0.706  -34.766 18.828  1.00 83.73  ? 275 SER   A O   1 
ATOM   2100 C CB  . SER   A 1 276 ? -0.888  -32.894 16.408  1.00 77.10  ? 275 SER   A CB  1 
ATOM   2101 O OG  . SER   A 1 276 ? -0.075  -33.721 15.594  1.00 76.79  ? 275 SER   A OG  1 
ATOM   2102 N N   . LYS   A 1 277 ? -1.602  -32.932 19.787  1.00 84.91  ? 276 LYS   A N   1 
ATOM   2103 C CA  . LYS   A 1 277 ? -2.384  -33.655 20.771  1.00 82.71  ? 276 LYS   A CA  1 
ATOM   2104 C C   . LYS   A 1 277 ? -3.654  -34.126 20.079  1.00 97.27  ? 276 LYS   A C   1 
ATOM   2105 O O   . LYS   A 1 277 ? -4.732  -33.988 20.638  1.00 101.94 ? 276 LYS   A O   1 
ATOM   2106 C CB  . LYS   A 1 277 ? -2.756  -32.737 21.940  1.00 81.90  ? 276 LYS   A CB  1 
ATOM   2107 C CG  . LYS   A 1 277 ? -1.600  -31.985 22.582  1.00 96.43  ? 276 LYS   A CG  1 
ATOM   2108 C CD  . LYS   A 1 277 ? -0.407  -32.843 23.012  1.00 104.12 ? 276 LYS   A CD  1 
ATOM   2109 C CE  . LYS   A 1 277 ? 0.779   -32.057 23.514  1.00 104.10 ? 276 LYS   A CE  1 
ATOM   2110 N NZ  . LYS   A 1 277 ? 0.432   -31.180 24.636  1.00 101.69 ? 276 LYS   A NZ  1 
ATOM   2111 N N   . ASN   A 1 278 ? -3.512  -34.629 18.843  1.00 111.96 ? 277 ASN   A N   1 
ATOM   2112 C CA  . ASN   A 1 278 ? -4.645  -34.925 17.977  1.00 119.98 ? 277 ASN   A CA  1 
ATOM   2113 C C   . ASN   A 1 278 ? -4.617  -36.423 17.658  1.00 113.91 ? 277 ASN   A C   1 
ATOM   2114 O O   . ASN   A 1 278 ? -3.557  -36.974 17.364  1.00 103.29 ? 277 ASN   A O   1 
ATOM   2115 C CB  . ASN   A 1 278 ? -4.649  -34.040 16.726  1.00 123.46 ? 277 ASN   A CB  1 
ATOM   2116 C CG  . ASN   A 1 278 ? -5.084  -32.599 16.954  1.00 116.72 ? 277 ASN   A CG  1 
ATOM   2117 O OD1 . ASN   A 1 278 ? -4.526  -31.873 17.792  1.00 83.81  ? 277 ASN   A OD1 1 
ATOM   2118 N ND2 . ASN   A 1 278 ? -6.069  -32.143 16.188  1.00 108.11 ? 277 ASN   A ND2 1 
ATOM   2119 N N   . PRO   A 1 279 ? -5.769  -37.138 17.713  1.00 121.69 ? 278 PRO   A N   1 
ATOM   2120 C CA  . PRO   A 1 279 ? -5.771  -38.590 17.542  1.00 122.06 ? 278 PRO   A CA  1 
ATOM   2121 C C   . PRO   A 1 279 ? -5.436  -38.896 16.089  1.00 120.01 ? 278 PRO   A C   1 
ATOM   2122 O O   . PRO   A 1 279 ? -6.116  -38.390 15.201  1.00 119.06 ? 278 PRO   A O   1 
ATOM   2123 C CB  . PRO   A 1 279 ? -7.208  -39.014 17.926  1.00 122.43 ? 278 PRO   A CB  1 
ATOM   2124 C CG  . PRO   A 1 279 ? -8.050  -37.784 17.632  1.00 120.41 ? 278 PRO   A CG  1 
ATOM   2125 C CD  . PRO   A 1 279 ? -7.129  -36.595 17.895  1.00 125.21 ? 278 PRO   A CD  1 
ATOM   2126 N N   . PHE   A 1 280 ? -4.382  -39.693 15.862  1.00 119.11 ? 279 PHE   A N   1 
ATOM   2127 C CA  . PHE   A 1 280 ? -4.033  -40.165 14.527  1.00 111.05 ? 279 PHE   A CA  1 
ATOM   2128 C C   . PHE   A 1 280 ? -5.320  -40.459 13.743  1.00 120.70 ? 279 PHE   A C   1 
ATOM   2129 O O   . PHE   A 1 280 ? -5.579  -39.820 12.727  1.00 131.15 ? 279 PHE   A O   1 
ATOM   2130 C CB  . PHE   A 1 280 ? -3.060  -41.346 14.608  1.00 81.12  ? 279 PHE   A CB  1 
ATOM   2131 N N   . ILE   A 1 281 ? -6.141  -41.412 14.201  1.00 114.97 ? 280 ILE   A N   1 
ATOM   2132 C CA  . ILE   A 1 281 ? -7.504  -41.529 13.694  1.00 111.06 ? 280 ILE   A CA  1 
ATOM   2133 C C   . ILE   A 1 281 ? -8.455  -41.731 14.876  1.00 109.17 ? 280 ILE   A C   1 
ATOM   2134 O O   . ILE   A 1 281 ? -9.541  -41.150 14.865  1.00 130.20 ? 280 ILE   A O   1 
ATOM   2135 C CB  . ILE   A 1 281 ? -7.637  -42.608 12.592  1.00 100.47 ? 280 ILE   A CB  1 
ATOM   2136 C CG1 . ILE   A 1 281 ? -8.925  -42.421 11.725  1.00 86.36  ? 280 ILE   A CG1 1 
ATOM   2137 C CG2 . ILE   A 1 281 ? -7.489  -44.024 13.170  1.00 99.32  ? 280 ILE   A CG2 1 
ATOM   2138 C CD1 . ILE   A 1 281 ? -10.045 -43.433 11.961  1.00 81.65  ? 280 ILE   A CD1 1 
ATOM   2139 N N   . HIS   A 1 282 ? -8.051  -42.512 15.901  1.00 77.85  ? 281 HIS   A N   1 
ATOM   2140 C CA  . HIS   A 1 282 ? -8.891  -42.789 17.060  1.00 67.15  ? 281 HIS   A CA  1 
ATOM   2141 C C   . HIS   A 1 282 ? -10.160 -41.915 17.060  1.00 61.69  ? 281 HIS   A C   1 
ATOM   2142 O O   . HIS   A 1 282 ? -10.104 -40.752 17.469  1.00 62.76  ? 281 HIS   A O   1 
ATOM   2143 C CB  . HIS   A 1 282 ? -8.068  -42.583 18.335  1.00 59.50  ? 281 HIS   A CB  1 
ATOM   2144 N N   . LEU   A 1 283 ? -11.309 -42.465 16.603  1.00 50.01  ? 282 LEU   A N   1 
ATOM   2145 C CA  . LEU   A 1 283 ? -12.544 -41.689 16.521  1.00 45.59  ? 282 LEU   A CA  1 
ATOM   2146 C C   . LEU   A 1 283 ? -13.092 -41.419 17.916  1.00 47.11  ? 282 LEU   A C   1 
ATOM   2147 O O   . LEU   A 1 283 ? -12.911 -42.218 18.821  1.00 45.72  ? 282 LEU   A O   1 
ATOM   2148 C CB  . LEU   A 1 283 ? -13.624 -42.372 15.695  1.00 41.92  ? 282 LEU   A CB  1 
ATOM   2149 C CG  . LEU   A 1 283 ? -13.310 -42.558 14.218  1.00 39.82  ? 282 LEU   A CG  1 
ATOM   2150 C CD1 . LEU   A 1 283 ? -14.445 -43.275 13.581  1.00 43.98  ? 282 LEU   A CD1 1 
ATOM   2151 C CD2 . LEU   A 1 283 ? -13.022 -41.226 13.582  1.00 45.42  ? 282 LEU   A CD2 1 
ATOM   2152 N N   . ASP   A 1 284 ? -13.814 -40.303 18.056  1.00 46.09  ? 283 ASP   A N   1 
ATOM   2153 C CA  . ASP   A 1 284 ? -14.462 -39.943 19.305  1.00 43.79  ? 283 ASP   A CA  1 
ATOM   2154 C C   . ASP   A 1 284 ? -15.822 -40.618 19.384  1.00 40.70  ? 283 ASP   A C   1 
ATOM   2155 O O   . ASP   A 1 284 ? -16.687 -40.367 18.550  1.00 39.05  ? 283 ASP   A O   1 
ATOM   2156 C CB  . ASP   A 1 284 ? -14.709 -38.444 19.434  1.00 46.31  ? 283 ASP   A CB  1 
ATOM   2157 C CG  . ASP   A 1 284 ? -15.372 -38.079 20.751  1.00 46.59  ? 283 ASP   A CG  1 
ATOM   2158 O OD1 . ASP   A 1 284 ? -14.651 -38.018 21.752  1.00 52.52  ? 283 ASP   A OD1 1 
ATOM   2159 O OD2 . ASP   A 1 284 ? -16.604 -37.976 20.784  1.00 43.83  ? 283 ASP   A OD2 1 
ATOM   2160 N N   . ASP   A 1 285 ? -16.050 -41.401 20.439  1.00 42.70  ? 284 ASP   A N   1 
ATOM   2161 C CA  . ASP   A 1 285 ? -17.276 -42.187 20.555  1.00 39.09  ? 284 ASP   A CA  1 
ATOM   2162 C C   . ASP   A 1 285 ? -18.514 -41.303 20.604  1.00 37.57  ? 284 ASP   A C   1 
ATOM   2163 O O   . ASP   A 1 285 ? -19.530 -41.660 20.004  1.00 39.68  ? 284 ASP   A O   1 
ATOM   2164 C CB  . ASP   A 1 285 ? -17.208 -43.212 21.682  1.00 50.26  ? 284 ASP   A CB  1 
ATOM   2165 C CG  . ASP   A 1 285 ? -16.065 -44.205 21.513  1.00 52.08  ? 284 ASP   A CG  1 
ATOM   2166 O OD1 . ASP   A 1 285 ? -15.795 -44.610 20.343  1.00 52.54  ? 284 ASP   A OD1 1 
ATOM   2167 O OD2 . ASP   A 1 285 ? -15.419 -44.520 22.518  1.00 65.68  ? 284 ASP   A OD2 1 
ATOM   2168 N N   . ASP   A 1 286 ? -18.471 -40.170 21.318  1.00 35.25  ? 285 ASP   A N   1 
ATOM   2169 C CA  . ASP   A 1 286 ? -19.666 -39.347 21.433  1.00 37.25  ? 285 ASP   A CA  1 
ATOM   2170 C C   . ASP   A 1 286 ? -20.055 -38.726 20.085  1.00 33.94  ? 285 ASP   A C   1 
ATOM   2171 O O   . ASP   A 1 286 ? -21.227 -38.628 19.718  1.00 33.52  ? 285 ASP   A O   1 
ATOM   2172 C CB  . ASP   A 1 286 ? -19.496 -38.257 22.474  1.00 44.64  ? 285 ASP   A CB  1 
ATOM   2173 C CG  . ASP   A 1 286 ? -19.271 -38.805 23.872  1.00 48.92  ? 285 ASP   A CG  1 
ATOM   2174 O OD1 . ASP   A 1 286 ? -20.012 -39.733 24.230  1.00 54.60  ? 285 ASP   A OD1 1 
ATOM   2175 O OD2 . ASP   A 1 286 ? -18.342 -38.341 24.537  1.00 52.10  ? 285 ASP   A OD2 1 
ATOM   2176 N N   . CYS   A 1 287 ? -19.058 -38.300 19.330  1.00 35.69  ? 286 CYS   A N   1 
ATOM   2177 C CA  . CYS   A 1 287 ? -19.311 -37.793 17.992  1.00 36.04  ? 286 CYS   A CA  1 
ATOM   2178 C C   . CYS   A 1 287 ? -19.895 -38.872 17.073  1.00 30.39  ? 286 CYS   A C   1 
ATOM   2179 O O   . CYS   A 1 287 ? -20.796 -38.590 16.291  1.00 32.14  ? 286 CYS   A O   1 
ATOM   2180 C CB  . CYS   A 1 287 ? -18.023 -37.190 17.441  1.00 40.18  ? 286 CYS   A CB  1 
ATOM   2181 S SG  . CYS   A 1 287 ? -17.466 -35.748 18.399  1.00 40.87  ? 286 CYS   A SG  1 
ATOM   2182 N N   . VAL   A 1 288 ? -19.325 -40.074 17.123  1.00 33.28  ? 287 VAL   A N   1 
ATOM   2183 C CA  . VAL   A 1 288 ? -19.815 -41.168 16.294  1.00 36.34  ? 287 VAL   A CA  1 
ATOM   2184 C C   . VAL   A 1 288 ? -21.255 -41.489 16.675  1.00 33.85  ? 287 VAL   A C   1 
ATOM   2185 O O   . VAL   A 1 288 ? -22.115 -41.633 15.802  1.00 34.10  ? 287 VAL   A O   1 
ATOM   2186 C CB  . VAL   A 1 288 ? -18.919 -42.406 16.450  1.00 35.27  ? 287 VAL   A CB  1 
ATOM   2187 C CG1 . VAL   A 1 288 ? -19.566 -43.603 15.783  1.00 34.88  ? 287 VAL   A CG1 1 
ATOM   2188 C CG2 . VAL   A 1 288 ? -17.497 -42.147 15.940  1.00 36.96  ? 287 VAL   A CG2 1 
ATOM   2189 N N   . THR   A 1 289 ? -21.547 -41.495 17.992  1.00 33.20  ? 288 THR   A N   1 
ATOM   2190 C CA  . THR   A 1 289 ? -22.901 -41.828 18.429  1.00 34.31  ? 288 THR   A CA  1 
ATOM   2191 C C   . THR   A 1 289 ? -23.864 -40.819 17.826  1.00 31.93  ? 288 THR   A C   1 
ATOM   2192 O O   . THR   A 1 289 ? -24.900 -41.173 17.260  1.00 35.19  ? 288 THR   A O   1 
ATOM   2193 C CB  . THR   A 1 289 ? -23.046 -41.847 19.957  1.00 31.47  ? 288 THR   A CB  1 
ATOM   2194 O OG1 . THR   A 1 289 ? -22.099 -42.698 20.589  1.00 35.48  ? 288 THR   A OG1 1 
ATOM   2195 C CG2 . THR   A 1 289 ? -24.468 -42.150 20.370  1.00 37.13  ? 288 THR   A CG2 1 
ATOM   2196 N N   . GLU   A 1 290 ? -23.541 -39.534 17.953  1.00 37.05  ? 289 GLU   A N   1 
ATOM   2197 C CA  . GLU   A 1 290 ? -24.482 -38.517 17.495  1.00 37.40  ? 289 GLU   A CA  1 
ATOM   2198 C C   . GLU   A 1 290 ? -24.748 -38.661 15.992  1.00 36.19  ? 289 GLU   A C   1 
ATOM   2199 O O   . GLU   A 1 290 ? -25.887 -38.528 15.529  1.00 37.24  ? 289 GLU   A O   1 
ATOM   2200 C CB  . GLU   A 1 290 ? -23.956 -37.137 17.911  1.00 43.25  ? 289 GLU   A CB  1 
ATOM   2201 C CG  . GLU   A 1 290 ? -24.951 -36.000 17.650  1.00 49.57  ? 289 GLU   A CG  1 
ATOM   2202 C CD  . GLU   A 1 290 ? -26.200 -35.999 18.544  1.00 57.85  ? 289 GLU   A CD  1 
ATOM   2203 O OE1 . GLU   A 1 290 ? -26.268 -36.876 19.465  1.00 50.98  ? 289 GLU   A OE1 1 
ATOM   2204 O OE2 . GLU   A 1 290 ? -27.110 -35.135 18.297  1.00 51.52  ? 289 GLU   A OE2 1 
ATOM   2205 N N   . LEU   A 1 291 ? -23.682 -38.890 15.210  1.00 34.59  ? 290 LEU   A N   1 
ATOM   2206 C CA  . LEU   A 1 291 ? -23.845 -39.093 13.781  1.00 32.95  ? 290 LEU   A CA  1 
ATOM   2207 C C   . LEU   A 1 291 ? -24.646 -40.367 13.518  1.00 33.06  ? 290 LEU   A C   1 
ATOM   2208 O O   . LEU   A 1 291 ? -25.433 -40.395 12.587  1.00 32.17  ? 290 LEU   A O   1 
ATOM   2209 C CB  . LEU   A 1 291 ? -22.484 -39.090 13.088  1.00 35.51  ? 290 LEU   A CB  1 
ATOM   2210 C CG  . LEU   A 1 291 ? -21.839 -37.707 12.944  1.00 34.07  ? 290 LEU   A CG  1 
ATOM   2211 C CD1 . LEU   A 1 291 ? -20.341 -37.676 12.739  1.00 33.77  ? 290 LEU   A CD1 1 
ATOM   2212 C CD2 . LEU   A 1 291 ? -22.494 -37.006 11.797  1.00 36.15  ? 290 LEU   A CD2 1 
ATOM   2213 N N   . SER   A 1 292 ? -24.391 -41.447 14.270  1.00 37.39  ? 291 SER   A N   1 
ATOM   2214 C CA  . SER   A 1 292 ? -25.103 -42.706 14.067  1.00 37.38  ? 291 SER   A CA  1 
ATOM   2215 C C   . SER   A 1 292 ? -26.598 -42.514 14.265  1.00 36.63  ? 291 SER   A C   1 
ATOM   2216 O O   . SER   A 1 292 ? -27.411 -42.959 13.442  1.00 37.46  ? 291 SER   A O   1 
ATOM   2217 C CB  . SER   A 1 292 ? -24.607 -43.795 14.994  1.00 38.09  ? 291 SER   A CB  1 
ATOM   2218 O OG  . SER   A 1 292 ? -23.278 -44.185 14.707  1.00 39.44  ? 291 SER   A OG  1 
ATOM   2219 N N   . VAL   A 1 293 ? -26.944 -41.826 15.368  1.00 40.31  ? 292 VAL   A N   1 
ATOM   2220 C CA  . VAL   A 1 293 ? -28.334 -41.430 15.598  1.00 42.17  ? 292 VAL   A CA  1 
ATOM   2221 C C   . VAL   A 1 293 ? -28.877 -40.650 14.405  1.00 40.64  ? 292 VAL   A C   1 
ATOM   2222 O O   . VAL   A 1 293 ? -29.917 -40.990 13.864  1.00 43.33  ? 292 VAL   A O   1 
ATOM   2223 C CB  . VAL   A 1 293 ? -28.516 -40.592 16.873  1.00 44.93  ? 292 VAL   A CB  1 
ATOM   2224 C CG1 . VAL   A 1 293 ? -29.950 -40.091 16.974  1.00 50.37  ? 292 VAL   A CG1 1 
ATOM   2225 C CG2 . VAL   A 1 293 ? -28.124 -41.389 18.113  1.00 44.48  ? 292 VAL   A CG2 1 
ATOM   2226 N N   . HIS   A 1 294 ? -28.183 -39.579 14.006  1.00 41.67  ? 293 HIS   A N   1 
ATOM   2227 C CA  . HIS   A 1 294 ? -28.696 -38.714 12.965  1.00 40.83  ? 293 HIS   A CA  1 
ATOM   2228 C C   . HIS   A 1 294 ? -28.884 -39.457 11.653  1.00 43.85  ? 293 HIS   A C   1 
ATOM   2229 O O   . HIS   A 1 294 ? -29.860 -39.208 10.976  1.00 46.93  ? 293 HIS   A O   1 
ATOM   2230 C CB  . HIS   A 1 294 ? -27.732 -37.571 12.649  1.00 46.71  ? 293 HIS   A CB  1 
ATOM   2231 C CG  . HIS   A 1 294 ? -28.240 -36.612 11.620  1.00 50.45  ? 293 HIS   A CG  1 
ATOM   2232 N ND1 . HIS   A 1 294 ? -27.691 -36.437 10.362  1.00 51.51  ? 293 HIS   A ND1 1 
ATOM   2233 C CD2 . HIS   A 1 294 ? -29.252 -35.738 11.719  1.00 47.13  ? 293 HIS   A CD2 1 
ATOM   2234 C CE1 . HIS   A 1 294 ? -28.357 -35.486 9.730   1.00 51.75  ? 293 HIS   A CE1 1 
ATOM   2235 N NE2 . HIS   A 1 294 ? -29.318 -35.057 10.536  1.00 50.81  ? 293 HIS   A NE2 1 
ATOM   2236 N N   . HIS   A 1 295 ? -27.896 -40.282 11.265  1.00 41.99  ? 294 HIS   A N   1 
ATOM   2237 C CA  . HIS   A 1 295 ? -27.952 -41.025 10.023  1.00 41.33  ? 294 HIS   A CA  1 
ATOM   2238 C C   . HIS   A 1 295 ? -28.681 -42.366 10.167  1.00 47.31  ? 294 HIS   A C   1 
ATOM   2239 O O   . HIS   A 1 295 ? -28.824 -43.075 9.187   1.00 41.74  ? 294 HIS   A O   1 
ATOM   2240 C CB  . HIS   A 1 295 ? -26.536 -41.225 9.475   1.00 43.14  ? 294 HIS   A CB  1 
ATOM   2241 C CG  . HIS   A 1 295 ? -25.906 -39.953 8.960   1.00 45.48  ? 294 HIS   A CG  1 
ATOM   2242 N ND1 . HIS   A 1 295 ? -26.305 -39.351 7.785   1.00 50.37  ? 294 HIS   A ND1 1 
ATOM   2243 C CD2 . HIS   A 1 295 ? -24.946 -39.155 9.474   1.00 44.24  ? 294 HIS   A CD2 1 
ATOM   2244 C CE1 . HIS   A 1 295 ? -25.595 -38.245 7.594   1.00 54.41  ? 294 HIS   A CE1 1 
ATOM   2245 N NE2 . HIS   A 1 295 ? -24.765 -38.104 8.619   1.00 48.59  ? 294 HIS   A NE2 1 
ATOM   2246 N N   . ARG   A 1 296 ? -29.143 -42.745 11.365  1.00 47.63  ? 295 ARG   A N   1 
ATOM   2247 C CA  . ARG   A 1 296 ? -29.864 -44.007 11.520  1.00 50.63  ? 295 ARG   A CA  1 
ATOM   2248 C C   . ARG   A 1 296 ? -28.962 -45.183 11.150  1.00 51.06  ? 295 ARG   A C   1 
ATOM   2249 O O   . ARG   A 1 296 ? -29.413 -46.143 10.542  1.00 43.46  ? 295 ARG   A O   1 
ATOM   2250 C CB  . ARG   A 1 296 ? -31.163 -43.998 10.701  1.00 60.02  ? 295 ARG   A CB  1 
ATOM   2251 C CG  . ARG   A 1 296 ? -32.266 -43.195 11.384  1.00 70.24  ? 295 ARG   A CG  1 
ATOM   2252 C CD  . ARG   A 1 296 ? -33.357 -42.676 10.438  1.00 79.03  ? 295 ARG   A CD  1 
ATOM   2253 N NE  . ARG   A 1 296 ? -34.717 -42.851 10.965  1.00 90.83  ? 295 ARG   A NE  1 
ATOM   2254 C CZ  . ARG   A 1 296 ? -35.137 -42.584 12.206  1.00 104.23 ? 295 ARG   A CZ  1 
ATOM   2255 N NH1 . ARG   A 1 296 ? -34.312 -42.081 13.108  1.00 110.64 ? 295 ARG   A NH1 1 
ATOM   2256 N NH2 . ARG   A 1 296 ? -36.389 -42.834 12.555  1.00 105.29 ? 295 ARG   A NH2 1 
ATOM   2257 N N   . ASN   A 1 297 ? -27.687 -45.108 11.566  1.00 42.50  ? 296 ASN   A N   1 
ATOM   2258 C CA  . ASN   A 1 297 ? -26.705 -46.149 11.311  1.00 41.39  ? 296 ASN   A CA  1 
ATOM   2259 C C   . ASN   A 1 297 ? -26.325 -46.845 12.604  1.00 42.24  ? 296 ASN   A C   1 
ATOM   2260 O O   . ASN   A 1 297 ? -26.387 -46.265 13.683  1.00 45.66  ? 296 ASN   A O   1 
ATOM   2261 C CB  . ASN   A 1 297 ? -25.402 -45.579 10.760  1.00 41.36  ? 296 ASN   A CB  1 
ATOM   2262 C CG  . ASN   A 1 297 ? -25.510 -45.361 9.281   1.00 45.42  ? 296 ASN   A CG  1 
ATOM   2263 O OD1 . ASN   A 1 297 ? -26.304 -46.043 8.638   1.00 50.16  ? 296 ASN   A OD1 1 
ATOM   2264 N ND2 . ASN   A 1 297 ? -24.729 -44.451 8.727   1.00 47.39  ? 296 ASN   A ND2 1 
ATOM   2265 N N   . ASN   A 1 298 ? -25.876 -48.090 12.467  1.00 37.65  ? 297 ASN   A N   1 
ATOM   2266 C CA  . ASN   A 1 298 ? -25.199 -48.755 13.543  1.00 35.99  ? 297 ASN   A CA  1 
ATOM   2267 C C   . ASN   A 1 298 ? -23.807 -48.139 13.610  1.00 38.41  ? 297 ASN   A C   1 
ATOM   2268 O O   . ASN   A 1 298 ? -23.304 -47.589 12.620  1.00 43.04  ? 297 ASN   A O   1 
ATOM   2269 C CB  . ASN   A 1 298 ? -25.258 -50.269 13.387  1.00 43.39  ? 297 ASN   A CB  1 
ATOM   2270 C CG  . ASN   A 1 298 ? -24.356 -50.770 12.276  1.00 52.66  ? 297 ASN   A CG  1 
ATOM   2271 O OD1 . ASN   A 1 298 ? -23.122 -50.763 12.426  1.00 50.90  ? 297 ASN   A OD1 1 
ATOM   2272 N ND2 . ASN   A 1 298 ? -24.950 -51.218 11.174  1.00 51.94  ? 297 ASN   A ND2 1 
ATOM   2273 N N   . ARG   A 1 299 ? -23.194 -48.288 14.781  1.00 39.00  ? 298 ARG   A N   1 
ATOM   2274 C CA  . ARG   A 1 299 ? -21.959 -47.618 15.138  1.00 38.96  ? 298 ARG   A CA  1 
ATOM   2275 C C   . ARG   A 1 299 ? -20.846 -47.962 14.141  1.00 41.93  ? 298 ARG   A C   1 
ATOM   2276 O O   . ARG   A 1 299 ? -20.143 -47.069 13.687  1.00 37.82  ? 298 ARG   A O   1 
ATOM   2277 C CB  . ARG   A 1 299 ? -21.574 -48.019 16.564  1.00 34.76  ? 298 ARG   A CB  1 
ATOM   2278 C CG  . ARG   A 1 299 ? -20.307 -47.347 17.073  1.00 34.33  ? 298 ARG   A CG  1 
ATOM   2279 C CD  . ARG   A 1 299 ? -20.048 -47.639 18.525  1.00 37.39  ? 298 ARG   A CD  1 
ATOM   2280 N NE  . ARG   A 1 299 ? -21.167 -47.122 19.336  1.00 38.51  ? 298 ARG   A NE  1 
ATOM   2281 C CZ  . ARG   A 1 299 ? -21.323 -45.853 19.744  1.00 41.80  ? 298 ARG   A CZ  1 
ATOM   2282 N NH1 . ARG   A 1 299 ? -20.373 -44.948 19.534  1.00 38.60  ? 298 ARG   A NH1 1 
ATOM   2283 N NH2 . ARG   A 1 299 ? -22.462 -45.482 20.325  1.00 36.56  ? 298 ARG   A NH2 1 
ATOM   2284 N N   . GLN   A 1 300 ? -20.689 -49.248 13.812  1.00 46.70  ? 299 GLN   A N   1 
ATOM   2285 C CA  . GLN   A 1 300 ? -19.577 -49.696 12.979  1.00 45.44  ? 299 GLN   A CA  1 
ATOM   2286 C C   . GLN   A 1 300 ? -19.690 -49.074 11.584  1.00 38.69  ? 299 GLN   A C   1 
ATOM   2287 O O   . GLN   A 1 300 ? -18.710 -48.564 11.039  1.00 38.71  ? 299 GLN   A O   1 
ATOM   2288 C CB  . GLN   A 1 300 ? -19.477 -51.224 12.935  1.00 44.80  ? 299 GLN   A CB  1 
ATOM   2289 C CG  . GLN   A 1 300 ? -18.243 -51.731 12.181  1.00 49.50  ? 299 GLN   A CG  1 
ATOM   2290 C CD  . GLN   A 1 300 ? -16.937 -51.370 12.858  1.00 56.31  ? 299 GLN   A CD  1 
ATOM   2291 O OE1 . GLN   A 1 300 ? -16.512 -52.005 13.827  1.00 66.83  ? 299 GLN   A OE1 1 
ATOM   2292 N NE2 . GLN   A 1 300 ? -16.280 -50.330 12.376  1.00 56.55  ? 299 GLN   A NE2 1 
ATOM   2293 N N   . THR   A 1 301 ? -20.897 -49.077 11.036  1.00 37.63  ? 300 THR   A N   1 
ATOM   2294 C CA  . THR   A 1 301 ? -21.106 -48.504 9.729   1.00 38.16  ? 300 THR   A CA  1 
ATOM   2295 C C   . THR   A 1 301 ? -20.745 -47.020 9.747   1.00 43.48  ? 300 THR   A C   1 
ATOM   2296 O O   . THR   A 1 301 ? -20.079 -46.530 8.835   1.00 37.27  ? 300 THR   A O   1 
ATOM   2297 C CB  . THR   A 1 301 ? -22.514 -48.759 9.242   1.00 39.28  ? 300 THR   A CB  1 
ATOM   2298 O OG1 . THR   A 1 301 ? -22.657 -50.156 9.013   1.00 38.46  ? 300 THR   A OG1 1 
ATOM   2299 C CG2 . THR   A 1 301 ? -22.807 -48.049 7.936   1.00 38.47  ? 300 THR   A CG2 1 
ATOM   2300 N N   . MET   A 1 302 ? -21.171 -46.308 10.796  1.00 37.21  ? 301 MET   A N   1 
ATOM   2301 C CA  . MET   A 1 302 ? -20.906 -44.894 10.892  1.00 35.36  ? 301 MET   A CA  1 
ATOM   2302 C C   . MET   A 1 302 ? -19.410 -44.636 11.002  1.00 32.59  ? 301 MET   A C   1 
ATOM   2303 O O   . MET   A 1 302 ? -18.881 -43.690 10.396  1.00 35.85  ? 301 MET   A O   1 
ATOM   2304 C CB  . MET   A 1 302 ? -21.615 -44.282 12.115  1.00 36.97  ? 301 MET   A CB  1 
ATOM   2305 C CG  . MET   A 1 302 ? -21.674 -42.803 12.066  1.00 35.13  ? 301 MET   A CG  1 
ATOM   2306 S SD  . MET   A 1 302 ? -22.841 -42.182 10.848  1.00 37.92  ? 301 MET   A SD  1 
ATOM   2307 C CE  . MET   A 1 302 ? -21.741 -41.677 9.507   1.00 40.02  ? 301 MET   A CE  1 
ATOM   2308 N N   . GLU   A 1 303 ? -18.712 -45.447 11.809  1.00 32.48  ? 302 GLU   A N   1 
ATOM   2309 C CA  . GLU   A 1 303 ? -17.272 -45.297 11.959  1.00 33.71  ? 302 GLU   A CA  1 
ATOM   2310 C C   . GLU   A 1 303 ? -16.526 -45.543 10.648  1.00 36.21  ? 302 GLU   A C   1 
ATOM   2311 O O   . GLU   A 1 303 ? -15.522 -44.865 10.362  1.00 33.91  ? 302 GLU   A O   1 
ATOM   2312 C CB  . GLU   A 1 303 ? -16.692 -46.292 12.964  1.00 38.78  ? 302 GLU   A CB  1 
ATOM   2313 C CG  . GLU   A 1 303 ? -17.144 -46.024 14.395  1.00 38.67  ? 302 GLU   A CG  1 
ATOM   2314 C CD  . GLU   A 1 303 ? -16.553 -47.023 15.386  1.00 44.64  ? 302 GLU   A CD  1 
ATOM   2315 O OE1 . GLU   A 1 303 ? -15.746 -47.870 14.978  1.00 50.36  ? 302 GLU   A OE1 1 
ATOM   2316 O OE2 . GLU   A 1 303 ? -16.864 -46.934 16.577  1.00 45.28  ? 302 GLU   A OE2 1 
ATOM   2317 N N   . ASP   A 1 304 ? -16.971 -46.557 9.895   1.00 36.91  ? 303 ASP   A N   1 
ATOM   2318 C CA  . ASP   A 1 304 ? -16.425 -46.858 8.579   1.00 39.01  ? 303 ASP   A CA  1 
ATOM   2319 C C   . ASP   A 1 304 ? -16.607 -45.685 7.601   1.00 41.09  ? 303 ASP   A C   1 
ATOM   2320 O O   . ASP   A 1 304 ? -15.688 -45.377 6.859   1.00 39.75  ? 303 ASP   A O   1 
ATOM   2321 C CB  . ASP   A 1 304 ? -17.043 -48.124 7.997   1.00 40.13  ? 303 ASP   A CB  1 
ATOM   2322 C CG  . ASP   A 1 304 ? -16.631 -49.421 8.682   1.00 40.90  ? 303 ASP   A CG  1 
ATOM   2323 O OD1 . ASP   A 1 304 ? -15.697 -49.370 9.475   1.00 40.76  ? 303 ASP   A OD1 1 
ATOM   2324 O OD2 . ASP   A 1 304 ? -17.291 -50.446 8.449   1.00 42.82  ? 303 ASP   A OD2 1 
ATOM   2325 N N   . LEU   A 1 305 ? -17.791 -45.052 7.568   1.00 34.88  ? 304 LEU   A N   1 
ATOM   2326 C CA  . LEU   A 1 305 ? -18.015 -43.901 6.705   1.00 36.00  ? 304 LEU   A CA  1 
ATOM   2327 C C   . LEU   A 1 305 ? -17.151 -42.700 7.112   1.00 39.38  ? 304 LEU   A C   1 
ATOM   2328 O O   . LEU   A 1 305 ? -16.595 -42.019 6.239   1.00 41.71  ? 304 LEU   A O   1 
ATOM   2329 C CB  . LEU   A 1 305 ? -19.499 -43.575 6.746   1.00 39.70  ? 304 LEU   A CB  1 
ATOM   2330 C CG  . LEU   A 1 305 ? -20.422 -44.577 6.052   1.00 40.71  ? 304 LEU   A CG  1 
ATOM   2331 C CD1 . LEU   A 1 305 ? -21.847 -44.175 6.170   1.00 38.82  ? 304 LEU   A CD1 1 
ATOM   2332 C CD2 . LEU   A 1 305 ? -20.047 -44.692 4.585   1.00 50.69  ? 304 LEU   A CD2 1 
ATOM   2333 N N   . ILE   A 1 306 ? -17.052 -42.411 8.424   1.00 35.46  ? 305 ILE   A N   1 
ATOM   2334 C CA  . ILE   A 1 306 ? -16.263 -41.281 8.884   1.00 33.17  ? 305 ILE   A CA  1 
ATOM   2335 C C   . ILE   A 1 306 ? -14.816 -41.526 8.476   1.00 33.09  ? 305 ILE   A C   1 
ATOM   2336 O O   . ILE   A 1 306 ? -14.125 -40.614 8.051   1.00 37.81  ? 305 ILE   A O   1 
ATOM   2337 C CB  . ILE   A 1 306 ? -16.380 -41.072 10.396  1.00 34.42  ? 305 ILE   A CB  1 
ATOM   2338 C CG1 . ILE   A 1 306 ? -17.806 -40.657 10.779  1.00 34.38  ? 305 ILE   A CG1 1 
ATOM   2339 C CG2 . ILE   A 1 306 ? -15.351 -40.060 10.886  1.00 35.17  ? 305 ILE   A CG2 1 
ATOM   2340 C CD1 . ILE   A 1 306 ? -18.147 -40.949 12.211  1.00 33.05  ? 305 ILE   A CD1 1 
ATOM   2341 N N   . SER   A 1 307 ? -14.360 -42.764 8.650   1.00 41.80  ? 306 SER   A N   1 
ATOM   2342 C CA  . SER   A 1 307 ? -12.966 -43.132 8.437   1.00 41.17  ? 306 SER   A CA  1 
ATOM   2343 C C   . SER   A 1 307 ? -12.536 -43.000 6.971   1.00 39.94  ? 306 SER   A C   1 
ATOM   2344 O O   . SER   A 1 307 ? -11.376 -43.060 6.681   1.00 41.43  ? 306 SER   A O   1 
ATOM   2345 C CB  . SER   A 1 307 ? -12.712 -44.503 8.919   1.00 40.07  ? 306 SER   A CB  1 
ATOM   2346 O OG  . SER   A 1 307 ? -12.836 -44.522 10.322  1.00 43.70  ? 306 SER   A OG  1 
ATOM   2347 N N   . LEU   A 1 308 ? -13.452 -42.836 6.039   1.00 39.55  ? 307 LEU   A N   1 
ATOM   2348 C CA  . LEU   A 1 308 ? -13.070 -42.473 4.690   1.00 43.58  ? 307 LEU   A CA  1 
ATOM   2349 C C   . LEU   A 1 308 ? -12.471 -41.070 4.619   1.00 48.67  ? 307 LEU   A C   1 
ATOM   2350 O O   . LEU   A 1 308 ? -11.719 -40.809 3.701   1.00 47.63  ? 307 LEU   A O   1 
ATOM   2351 C CB  . LEU   A 1 308 ? -14.295 -42.598 3.798   1.00 39.86  ? 307 LEU   A CB  1 
ATOM   2352 C CG  . LEU   A 1 308 ? -14.828 -44.022 3.677   1.00 47.28  ? 307 LEU   A CG  1 
ATOM   2353 C CD1 . LEU   A 1 308 ? -15.961 -44.035 2.671   1.00 39.11  ? 307 LEU   A CD1 1 
ATOM   2354 C CD2 . LEU   A 1 308 ? -13.673 -44.992 3.307   1.00 46.57  ? 307 LEU   A CD2 1 
ATOM   2355 N N   . TRP   A 1 309 ? -12.805 -40.151 5.539   1.00 40.13  ? 308 TRP   A N   1 
ATOM   2356 C CA  . TRP   A 1 309 ? -12.127 -38.859 5.593   1.00 38.72  ? 308 TRP   A CA  1 
ATOM   2357 C C   . TRP   A 1 309 ? -12.100 -38.198 4.233   1.00 39.53  ? 308 TRP   A C   1 
ATOM   2358 O O   . TRP   A 1 309 ? -11.050 -37.787 3.775   1.00 43.49  ? 308 TRP   A O   1 
ATOM   2359 C CB  . TRP   A 1 309 ? -10.680 -38.993 6.075   1.00 40.57  ? 308 TRP   A CB  1 
ATOM   2360 C CG  . TRP   A 1 309 ? -10.637 -39.319 7.523   1.00 48.32  ? 308 TRP   A CG  1 
ATOM   2361 C CD1 . TRP   A 1 309 ? -10.260 -40.499 8.094   1.00 56.74  ? 308 TRP   A CD1 1 
ATOM   2362 C CD2 . TRP   A 1 309 ? -11.142 -38.481 8.581   1.00 49.62  ? 308 TRP   A CD2 1 
ATOM   2363 N NE1 . TRP   A 1 309 ? -10.413 -40.421 9.455   1.00 59.08  ? 308 TRP   A NE1 1 
ATOM   2364 C CE2 . TRP   A 1 309 ? -10.991 -39.212 9.779   1.00 60.70  ? 308 TRP   A CE2 1 
ATOM   2365 C CE3 . TRP   A 1 309 ? -11.700 -37.205 8.639   1.00 61.00  ? 308 TRP   A CE3 1 
ATOM   2366 C CZ2 . TRP   A 1 309 ? -11.381 -38.690 11.017  1.00 61.40  ? 308 TRP   A CZ2 1 
ATOM   2367 C CZ3 . TRP   A 1 309 ? -12.092 -36.702 9.862   1.00 59.46  ? 308 TRP   A CZ3 1 
ATOM   2368 C CH2 . TRP   A 1 309 ? -11.960 -37.441 11.030  1.00 53.58  ? 308 TRP   A CH2 1 
ATOM   2369 N N   . GLN   A 1 310 ? -13.267 -38.057 3.623   1.00 38.70  ? 309 GLN   A N   1 
ATOM   2370 C CA  . GLN   A 1 310 ? -13.344 -37.471 2.308   1.00 44.30  ? 309 GLN   A CA  1 
ATOM   2371 C C   . GLN   A 1 310 ? -13.374 -35.944 2.351   1.00 42.30  ? 309 GLN   A C   1 
ATOM   2372 O O   . GLN   A 1 310 ? -13.476 -35.342 1.300   1.00 43.86  ? 309 GLN   A O   1 
ATOM   2373 C CB  . GLN   A 1 310 ? -14.604 -37.996 1.644   1.00 42.93  ? 309 GLN   A CB  1 
ATOM   2374 C CG  . GLN   A 1 310 ? -14.684 -39.515 1.702   1.00 47.59  ? 309 GLN   A CG  1 
ATOM   2375 C CD  . GLN   A 1 310 ? -15.610 -40.036 0.641   1.00 51.35  ? 309 GLN   A CD  1 
ATOM   2376 O OE1 . GLN   A 1 310 ? -16.783 -40.338 0.877   1.00 58.02  ? 309 GLN   A OE1 1 
ATOM   2377 N NE2 . GLN   A 1 310 ? -15.094 -40.047 -0.572  1.00 62.36  ? 309 GLN   A NE2 1 
ATOM   2378 N N   . TYR   A 1 311 ? -13.331 -35.312 3.524   1.00 41.09  ? 310 TYR   A N   1 
ATOM   2379 C CA  . TYR   A 1 311 ? -13.514 -33.865 3.618   1.00 38.83  ? 310 TYR   A CA  1 
ATOM   2380 C C   . TYR   A 1 311 ? -14.770 -33.457 2.864   1.00 38.62  ? 310 TYR   A C   1 
ATOM   2381 O O   . TYR   A 1 311 ? -14.834 -32.403 2.230   1.00 36.35  ? 310 TYR   A O   1 
ATOM   2382 C CB  . TYR   A 1 311 ? -12.246 -33.138 3.161   1.00 41.58  ? 310 TYR   A CB  1 
ATOM   2383 C CG  . TYR   A 1 311 ? -11.199 -33.204 4.249   1.00 35.01  ? 310 TYR   A CG  1 
ATOM   2384 C CD1 . TYR   A 1 311 ? -10.387 -34.318 4.405   1.00 40.45  ? 310 TYR   A CD1 1 
ATOM   2385 C CD2 . TYR   A 1 311 ? -11.098 -32.197 5.192   1.00 37.99  ? 310 TYR   A CD2 1 
ATOM   2386 C CE1 . TYR   A 1 311 ? -9.498  -34.411 5.461   1.00 40.12  ? 310 TYR   A CE1 1 
ATOM   2387 C CE2 . TYR   A 1 311 ? -10.219 -32.284 6.254   1.00 41.50  ? 310 TYR   A CE2 1 
ATOM   2388 C CZ  . TYR   A 1 311 ? -9.422  -33.408 6.408   1.00 41.12  ? 310 TYR   A CZ  1 
ATOM   2389 O OH  . TYR   A 1 311 ? -8.536  -33.455 7.470   1.00 45.67  ? 310 TYR   A OH  1 
ATOM   2390 N N   . ASP   A 1 312 ? -15.805 -34.287 2.995   1.00 34.93  ? 311 ASP   A N   1 
ATOM   2391 C CA  . ASP   A 1 312 ? -17.140 -33.942 2.570   1.00 35.38  ? 311 ASP   A CA  1 
ATOM   2392 C C   . ASP   A 1 312 ? -17.922 -33.439 3.790   1.00 36.01  ? 311 ASP   A C   1 
ATOM   2393 O O   . ASP   A 1 312 ? -17.318 -33.078 4.811   1.00 35.64  ? 311 ASP   A O   1 
ATOM   2394 C CB  . ASP   A 1 312 ? -17.788 -35.119 1.879   1.00 35.85  ? 311 ASP   A CB  1 
ATOM   2395 C CG  . ASP   A 1 312 ? -17.922 -36.333 2.785   1.00 40.03  ? 311 ASP   A CG  1 
ATOM   2396 O OD1 . ASP   A 1 312 ? -17.350 -36.293 3.896   1.00 34.54  ? 311 ASP   A OD1 1 
ATOM   2397 O OD2 . ASP   A 1 312 ? -18.555 -37.303 2.348   1.00 48.21  ? 311 ASP   A OD2 1 
ATOM   2398 N N   . HIS   A 1 313 ? -19.254 -33.408 3.663   1.00 35.32  ? 312 HIS   A N   1 
ATOM   2399 C CA  . HIS   A 1 313 ? -20.102 -32.856 4.713   1.00 37.36  ? 312 HIS   A CA  1 
ATOM   2400 C C   . HIS   A 1 313 ? -19.998 -33.692 5.998   1.00 41.44  ? 312 HIS   A C   1 
ATOM   2401 O O   . HIS   A 1 313 ? -20.046 -33.153 7.117   1.00 36.44  ? 312 HIS   A O   1 
ATOM   2402 C CB  . HIS   A 1 313 ? -21.544 -32.685 4.236   1.00 38.34  ? 312 HIS   A CB  1 
ATOM   2403 C CG  . HIS   A 1 313 ? -22.405 -31.996 5.264   1.00 39.35  ? 312 HIS   A CG  1 
ATOM   2404 N ND1 . HIS   A 1 313 ? -23.600 -32.494 5.736   1.00 43.67  ? 312 HIS   A ND1 1 
ATOM   2405 C CD2 . HIS   A 1 313 ? -22.213 -30.839 5.934   1.00 42.90  ? 312 HIS   A CD2 1 
ATOM   2406 C CE1 . HIS   A 1 313 ? -24.098 -31.656 6.643   1.00 44.03  ? 312 HIS   A CE1 1 
ATOM   2407 N NE2 . HIS   A 1 313 ? -23.279 -30.640 6.770   1.00 42.25  ? 312 HIS   A NE2 1 
ATOM   2408 N N   . LEU   A 1 314 ? -19.786 -35.006 5.842   1.00 35.98  ? 313 LEU   A N   1 
ATOM   2409 C CA  . LEU   A 1 314 ? -19.625 -35.879 6.994   1.00 35.20  ? 313 LEU   A CA  1 
ATOM   2410 C C   . LEU   A 1 314 ? -18.352 -35.551 7.785   1.00 34.31  ? 313 LEU   A C   1 
ATOM   2411 O O   . LEU   A 1 314 ? -18.405 -35.407 9.028   1.00 31.95  ? 313 LEU   A O   1 
ATOM   2412 C CB  . LEU   A 1 314 ? -19.681 -37.334 6.529   1.00 35.51  ? 313 LEU   A CB  1 
ATOM   2413 C CG  . LEU   A 1 314 ? -19.321 -38.361 7.605   1.00 38.37  ? 313 LEU   A CG  1 
ATOM   2414 C CD1 . LEU   A 1 314 ? -20.279 -38.148 8.797   1.00 35.10  ? 313 LEU   A CD1 1 
ATOM   2415 C CD2 . LEU   A 1 314 ? -19.357 -39.768 7.071   1.00 41.96  ? 313 LEU   A CD2 1 
ATOM   2416 N N   . THR   A 1 315 ? -17.211 -35.378 7.083   1.00 31.03  ? 314 THR   A N   1 
ATOM   2417 C CA  . THR   A 1 315 ? -15.978 -34.996 7.737   1.00 29.99  ? 314 THR   A CA  1 
ATOM   2418 C C   . THR   A 1 315 ? -16.191 -33.695 8.516   1.00 31.70  ? 314 THR   A C   1 
ATOM   2419 O O   . THR   A 1 315 ? -15.694 -33.488 9.620   1.00 31.44  ? 314 THR   A O   1 
ATOM   2420 C CB  . THR   A 1 315 ? -14.865 -34.784 6.708   1.00 33.19  ? 314 THR   A CB  1 
ATOM   2421 O OG1 . THR   A 1 315 ? -14.677 -35.993 5.983   1.00 33.45  ? 314 THR   A OG1 1 
ATOM   2422 C CG2 . THR   A 1 315 ? -13.593 -34.327 7.387   1.00 36.21  ? 314 THR   A CG2 1 
ATOM   2423 N N   . ALA   A 1 316 ? -16.838 -32.745 7.866   1.00 30.26  ? 315 ALA   A N   1 
ATOM   2424 C CA  . ALA   A 1 316 ? -17.052 -31.444 8.479   1.00 32.53  ? 315 ALA   A CA  1 
ATOM   2425 C C   . ALA   A 1 316 ? -17.920 -31.557 9.741   1.00 31.43  ? 315 ALA   A C   1 
ATOM   2426 O O   . ALA   A 1 316 ? -17.573 -31.013 10.785  1.00 32.00  ? 315 ALA   A O   1 
ATOM   2427 C CB  . ALA   A 1 316 ? -17.706 -30.539 7.443   1.00 36.37  ? 315 ALA   A CB  1 
ATOM   2428 N N   . THR   A 1 317 ? -19.021 -32.311 9.669   1.00 33.47  ? 316 THR   A N   1 
ATOM   2429 C CA  . THR   A 1 317 ? -19.929 -32.412 10.812  1.00 33.78  ? 316 THR   A CA  1 
ATOM   2430 C C   . THR   A 1 317 ? -19.204 -33.091 11.968  1.00 36.85  ? 316 THR   A C   1 
ATOM   2431 O O   . THR   A 1 317 ? -19.263 -32.621 13.103  1.00 37.07  ? 316 THR   A O   1 
ATOM   2432 C CB  . THR   A 1 317 ? -21.194 -33.140 10.399  1.00 38.74  ? 316 THR   A CB  1 
ATOM   2433 O OG1 . THR   A 1 317 ? -21.772 -32.332 9.374   1.00 34.64  ? 316 THR   A OG1 1 
ATOM   2434 C CG2 . THR   A 1 317 ? -22.174 -33.349 11.547  1.00 39.05  ? 316 THR   A CG2 1 
ATOM   2435 N N   . TYR   A 1 318 ? -18.456 -34.150 11.636  1.00 31.69  ? 317 TYR   A N   1 
ATOM   2436 C CA  . TYR   A 1 318 ? -17.653 -34.886 12.587  1.00 31.31  ? 317 TYR   A CA  1 
ATOM   2437 C C   . TYR   A 1 318 ? -16.663 -33.953 13.285  1.00 35.69  ? 317 TYR   A C   1 
ATOM   2438 O O   . TYR   A 1 318 ? -16.569 -33.943 14.511  1.00 35.85  ? 317 TYR   A O   1 
ATOM   2439 C CB  . TYR   A 1 318 ? -16.984 -36.107 11.943  1.00 32.16  ? 317 TYR   A CB  1 
ATOM   2440 C CG  . TYR   A 1 318 ? -16.077 -36.769 12.970  1.00 35.02  ? 317 TYR   A CG  1 
ATOM   2441 C CD1 . TYR   A 1 318 ? -16.585 -37.627 13.917  1.00 34.87  ? 317 TYR   A CD1 1 
ATOM   2442 C CD2 . TYR   A 1 318 ? -14.723 -36.467 13.022  1.00 36.82  ? 317 TYR   A CD2 1 
ATOM   2443 C CE1 . TYR   A 1 318 ? -15.768 -38.188 14.871  1.00 37.82  ? 317 TYR   A CE1 1 
ATOM   2444 C CE2 . TYR   A 1 318 ? -13.893 -37.000 13.989  1.00 40.74  ? 317 TYR   A CE2 1 
ATOM   2445 C CZ  . TYR   A 1 318 ? -14.427 -37.878 14.905  1.00 38.45  ? 317 TYR   A CZ  1 
ATOM   2446 O OH  . TYR   A 1 318 ? -13.672 -38.409 15.874  1.00 38.75  ? 317 TYR   A OH  1 
ATOM   2447 N N   . LEU   A 1 319 ? -15.906 -33.170 12.504  1.00 37.24  ? 318 LEU   A N   1 
ATOM   2448 C CA  . LEU   A 1 319 ? -14.834 -32.344 13.053  1.00 35.37  ? 318 LEU   A CA  1 
ATOM   2449 C C   . LEU   A 1 319 ? -15.429 -31.232 13.903  1.00 36.07  ? 318 LEU   A C   1 
ATOM   2450 O O   . LEU   A 1 319 ? -14.890 -30.937 14.963  1.00 38.64  ? 318 LEU   A O   1 
ATOM   2451 C CB  . LEU   A 1 319 ? -13.915 -31.815 11.948  1.00 35.72  ? 318 LEU   A CB  1 
ATOM   2452 C CG  . LEU   A 1 319 ? -13.060 -32.914 11.300  1.00 39.67  ? 318 LEU   A CG  1 
ATOM   2453 C CD1 . LEU   A 1 319 ? -12.257 -32.402 10.136  1.00 40.68  ? 318 LEU   A CD1 1 
ATOM   2454 C CD2 . LEU   A 1 319 ? -12.181 -33.549 12.384  1.00 41.69  ? 318 LEU   A CD2 1 
ATOM   2455 N N   . LEU   A 1 320 ? -16.584 -30.701 13.482  1.00 33.64  ? 319 LEU   A N   1 
ATOM   2456 C CA  . LEU   A 1 320 ? -17.269 -29.675 14.251  1.00 38.58  ? 319 LEU   A CA  1 
ATOM   2457 C C   . LEU   A 1 320 ? -17.802 -30.202 15.584  1.00 40.96  ? 319 LEU   A C   1 
ATOM   2458 O O   . LEU   A 1 320 ? -17.617 -29.569 16.624  1.00 40.26  ? 319 LEU   A O   1 
ATOM   2459 C CB  . LEU   A 1 320 ? -18.355 -29.037 13.407  1.00 34.83  ? 319 LEU   A CB  1 
ATOM   2460 C CG  . LEU   A 1 320 ? -17.834 -28.080 12.330  1.00 35.97  ? 319 LEU   A CG  1 
ATOM   2461 C CD1 . LEU   A 1 320 ? -18.928 -27.829 11.327  1.00 36.44  ? 319 LEU   A CD1 1 
ATOM   2462 C CD2 . LEU   A 1 320 ? -17.296 -26.758 12.928  1.00 36.60  ? 319 LEU   A CD2 1 
ATOM   2463 N N   . LEU   A 1 321 ? -18.434 -31.369 15.572  1.00 40.43  ? 320 LEU   A N   1 
ATOM   2464 C CA  . LEU   A 1 321 ? -18.844 -31.989 16.820  1.00 37.88  ? 320 LEU   A CA  1 
ATOM   2465 C C   . LEU   A 1 321 ? -17.635 -32.214 17.732  1.00 43.84  ? 320 LEU   A C   1 
ATOM   2466 O O   . LEU   A 1 321 ? -17.759 -32.068 18.932  1.00 49.67  ? 320 LEU   A O   1 
ATOM   2467 C CB  . LEU   A 1 321 ? -19.563 -33.303 16.539  1.00 36.52  ? 320 LEU   A CB  1 
ATOM   2468 C CG  . LEU   A 1 321 ? -20.898 -33.203 15.807  1.00 40.02  ? 320 LEU   A CG  1 
ATOM   2469 C CD1 . LEU   A 1 321 ? -21.451 -34.575 15.443  1.00 39.08  ? 320 LEU   A CD1 1 
ATOM   2470 C CD2 . LEU   A 1 321 ? -21.895 -32.470 16.679  1.00 49.51  ? 320 LEU   A CD2 1 
ATOM   2471 N N   . LEU   A 1 322 ? -16.496 -32.625 17.172  1.00 45.48  ? 321 LEU   A N   1 
ATOM   2472 C CA  . LEU   A 1 322 ? -15.296 -32.931 17.942  1.00 53.21  ? 321 LEU   A CA  1 
ATOM   2473 C C   . LEU   A 1 322 ? -14.739 -31.653 18.565  1.00 62.06  ? 321 LEU   A C   1 
ATOM   2474 O O   . LEU   A 1 322 ? -14.146 -31.672 19.643  1.00 55.68  ? 321 LEU   A O   1 
ATOM   2475 C CB  . LEU   A 1 322 ? -14.270 -33.599 17.037  1.00 50.67  ? 321 LEU   A CB  1 
ATOM   2476 C CG  . LEU   A 1 322 ? -12.964 -34.039 17.695  1.00 56.18  ? 321 LEU   A CG  1 
ATOM   2477 C CD1 . LEU   A 1 322 ? -13.169 -35.238 18.602  1.00 52.71  ? 321 LEU   A CD1 1 
ATOM   2478 C CD2 . LEU   A 1 322 ? -11.959 -34.346 16.608  1.00 56.10  ? 321 LEU   A CD2 1 
ATOM   2479 N N   . ALA   A 1 323 ? -14.935 -30.533 17.878  1.00 60.79  ? 322 ALA   A N   1 
ATOM   2480 C CA  . ALA   A 1 323 ? -14.521 -29.254 18.414  1.00 63.41  ? 322 ALA   A CA  1 
ATOM   2481 C C   . ALA   A 1 323 ? -15.548 -28.777 19.441  1.00 59.93  ? 322 ALA   A C   1 
ATOM   2482 O O   . ALA   A 1 323 ? -15.197 -28.132 20.421  1.00 73.62  ? 322 ALA   A O   1 
ATOM   2483 C CB  . ALA   A 1 323 ? -14.330 -28.280 17.275  1.00 66.97  ? 322 ALA   A CB  1 
ATOM   2484 N N   . LYS   A 1 324 ? -16.823 -29.103 19.236  1.00 55.10  ? 323 LYS   A N   1 
ATOM   2485 C CA  . LYS   A 1 324 ? -17.822 -28.885 20.263  1.00 52.21  ? 323 LYS   A CA  1 
ATOM   2486 C C   . LYS   A 1 324 ? -17.430 -29.632 21.532  1.00 73.85  ? 323 LYS   A C   1 
ATOM   2487 O O   . LYS   A 1 324 ? -17.630 -29.129 22.635  1.00 82.41  ? 323 LYS   A O   1 
ATOM   2488 C CB  . LYS   A 1 324 ? -19.224 -29.345 19.880  1.00 59.18  ? 323 LYS   A CB  1 
ATOM   2489 C CG  . LYS   A 1 324 ? -20.058 -28.286 19.221  1.00 58.18  ? 323 LYS   A CG  1 
ATOM   2490 C CD  . LYS   A 1 324 ? -21.442 -28.778 18.838  1.00 67.45  ? 323 LYS   A CD  1 
ATOM   2491 C CE  . LYS   A 1 324 ? -22.402 -27.645 18.600  1.00 73.81  ? 323 LYS   A CE  1 
ATOM   2492 N NZ  . LYS   A 1 324 ? -23.701 -28.122 18.121  1.00 72.94  ? 323 LYS   A NZ  1 
ATOM   2493 N N   . LYS   A 1 325 ? -16.878 -30.838 21.373  1.00 71.02  ? 324 LYS   A N   1 
ATOM   2494 C CA  . LYS   A 1 325 ? -16.522 -31.647 22.525  1.00 73.96  ? 324 LYS   A CA  1 
ATOM   2495 C C   . LYS   A 1 325 ? -15.289 -31.041 23.194  1.00 72.62  ? 324 LYS   A C   1 
ATOM   2496 O O   . LYS   A 1 325 ? -15.337 -30.721 24.374  1.00 87.98  ? 324 LYS   A O   1 
ATOM   2497 C CB  . LYS   A 1 325 ? -16.315 -33.120 22.159  1.00 63.43  ? 324 LYS   A CB  1 
ATOM   2498 C CG  . LYS   A 1 325 ? -15.911 -33.971 23.345  1.00 64.32  ? 324 LYS   A CG  1 
ATOM   2499 C CD  . LYS   A 1 325 ? -16.318 -35.430 23.306  1.00 65.62  ? 324 LYS   A CD  1 
ATOM   2500 C CE  . LYS   A 1 325 ? -15.377 -36.272 24.120  1.00 69.53  ? 324 LYS   A CE  1 
ATOM   2501 N NZ  . LYS   A 1 325 ? -15.831 -37.668 24.185  1.00 65.37  ? 324 LYS   A NZ  1 
ATOM   2502 N N   . ALA   A 1 326 ? -14.213 -30.847 22.423  1.00 74.28  ? 325 ALA   A N   1 
ATOM   2503 C CA  . ALA   A 1 326 ? -12.942 -30.369 22.946  1.00 72.78  ? 325 ALA   A CA  1 
ATOM   2504 C C   . ALA   A 1 326 ? -13.126 -29.066 23.717  1.00 84.05  ? 325 ALA   A C   1 
ATOM   2505 O O   . ALA   A 1 326 ? -12.277 -28.730 24.539  1.00 95.63  ? 325 ALA   A O   1 
ATOM   2506 C CB  . ALA   A 1 326 ? -11.950 -30.196 21.829  1.00 66.13  ? 325 ALA   A CB  1 
ATOM   2507 N N   . ARG   A 1 327 ? -14.239 -28.361 23.461  1.00 85.91  ? 326 ARG   A N   1 
ATOM   2508 C CA  . ARG   A 1 327 ? -14.547 -27.096 24.117  1.00 88.47  ? 326 ARG   A CA  1 
ATOM   2509 C C   . ARG   A 1 327 ? -15.657 -27.311 25.149  1.00 87.63  ? 326 ARG   A C   1 
ATOM   2510 O O   . ARG   A 1 327 ? -16.405 -26.391 25.456  1.00 86.57  ? 326 ARG   A O   1 
ATOM   2511 C CB  . ARG   A 1 327 ? -14.933 -26.019 23.092  1.00 84.16  ? 326 ARG   A CB  1 
ATOM   2512 C CG  . ARG   A 1 327 ? -13.775 -25.607 22.191  1.00 90.53  ? 326 ARG   A CG  1 
ATOM   2513 C CD  . ARG   A 1 327 ? -14.079 -24.427 21.264  1.00 92.86  ? 326 ARG   A CD  1 
ATOM   2514 N NE  . ARG   A 1 327 ? -14.781 -24.872 20.058  1.00 90.71  ? 326 ARG   A NE  1 
ATOM   2515 C CZ  . ARG   A 1 327 ? -16.074 -24.708 19.808  1.00 95.88  ? 326 ARG   A CZ  1 
ATOM   2516 N NH1 . ARG   A 1 327 ? -16.770 -23.789 20.450  1.00 106.91 ? 326 ARG   A NH1 1 
ATOM   2517 N NH2 . ARG   A 1 327 ? -16.660 -25.450 18.885  1.00 80.24  ? 326 ARG   A NH2 1 
ATOM   2518 N N   . GLY   A 1 328 ? -15.763 -28.538 25.673  1.00 77.45  ? 327 GLY   A N   1 
ATOM   2519 C CA  . GLY   A 1 328 ? -16.662 -28.849 26.770  1.00 71.35  ? 327 GLY   A CA  1 
ATOM   2520 C C   . GLY   A 1 328 ? -18.138 -28.654 26.439  1.00 71.30  ? 327 GLY   A C   1 
ATOM   2521 O O   . GLY   A 1 328 ? -18.977 -28.857 27.310  1.00 87.30  ? 327 GLY   A O   1 
ATOM   2522 N N   . LYS   A 1 329 ? -18.472 -28.300 25.192  1.00 77.56  ? 328 LYS   A N   1 
ATOM   2523 C CA  . LYS   A 1 329 ? -19.856 -28.015 24.830  1.00 77.34  ? 328 LYS   A CA  1 
ATOM   2524 C C   . LYS   A 1 329 ? -20.538 -29.331 24.453  1.00 69.02  ? 328 LYS   A C   1 
ATOM   2525 O O   . LYS   A 1 329 ? -19.870 -30.351 24.274  1.00 72.44  ? 328 LYS   A O   1 
ATOM   2526 C CB  . LYS   A 1 329 ? -19.927 -26.970 23.706  1.00 80.88  ? 328 LYS   A CB  1 
ATOM   2527 C CG  . LYS   A 1 329 ? -19.311 -25.606 24.010  1.00 83.44  ? 328 LYS   A CG  1 
ATOM   2528 C CD  . LYS   A 1 329 ? -18.989 -24.772 22.774  1.00 91.73  ? 328 LYS   A CD  1 
ATOM   2529 C CE  . LYS   A 1 329 ? -20.206 -24.283 22.040  1.00 93.81  ? 328 LYS   A CE  1 
ATOM   2530 N NZ  . LYS   A 1 329 ? -19.884 -23.639 20.760  1.00 97.24  ? 328 LYS   A NZ  1 
ATOM   2531 N N   . PRO   A 1 330 ? -21.884 -29.367 24.348  1.00 57.15  ? 329 PRO   A N   1 
ATOM   2532 C CA  . PRO   A 1 330 ? -22.596 -30.608 24.070  1.00 52.67  ? 329 PRO   A CA  1 
ATOM   2533 C C   . PRO   A 1 330 ? -22.445 -31.074 22.615  1.00 57.67  ? 329 PRO   A C   1 
ATOM   2534 O O   . PRO   A 1 330 ? -22.383 -30.283 21.675  1.00 51.67  ? 329 PRO   A O   1 
ATOM   2535 C CB  . PRO   A 1 330 ? -24.060 -30.320 24.430  1.00 58.55  ? 329 PRO   A CB  1 
ATOM   2536 C CG  . PRO   A 1 330 ? -24.070 -28.912 24.975  1.00 63.13  ? 329 PRO   A CG  1 
ATOM   2537 C CD  . PRO   A 1 330 ? -22.788 -28.233 24.536  1.00 62.36  ? 329 PRO   A CD  1 
ATOM   2538 N N   . VAL   A 1 331 ? -22.413 -32.394 22.457  1.00 54.84  ? 330 VAL   A N   1 
ATOM   2539 C CA  . VAL   A 1 331 ? -22.120 -33.031 21.194  1.00 51.74  ? 330 VAL   A CA  1 
ATOM   2540 C C   . VAL   A 1 331 ? -23.469 -33.395 20.596  1.00 51.38  ? 330 VAL   A C   1 
ATOM   2541 O O   . VAL   A 1 331 ? -24.007 -34.490 20.786  1.00 60.33  ? 330 VAL   A O   1 
ATOM   2542 C CB  . VAL   A 1 331 ? -21.164 -34.222 21.352  1.00 51.86  ? 330 VAL   A CB  1 
ATOM   2543 C CG1 . VAL   A 1 331 ? -21.018 -35.000 20.052  1.00 53.48  ? 330 VAL   A CG1 1 
ATOM   2544 C CG2 . VAL   A 1 331 ? -19.800 -33.773 21.844  1.00 54.39  ? 330 VAL   A CG2 1 
ATOM   2545 N N   . ARG   A 1 332 ? -24.028 -32.395 19.925  1.00 45.55  ? 331 ARG   A N   1 
ATOM   2546 C CA  . ARG   A 1 332 ? -25.407 -32.433 19.498  1.00 46.81  ? 331 ARG   A CA  1 
ATOM   2547 C C   . ARG   A 1 332 ? -25.525 -31.762 18.144  1.00 43.61  ? 331 ARG   A C   1 
ATOM   2548 O O   . ARG   A 1 332 ? -24.893 -30.740 17.904  1.00 50.36  ? 331 ARG   A O   1 
ATOM   2549 C CB  . ARG   A 1 332 ? -26.319 -31.681 20.479  1.00 59.53  ? 331 ARG   A CB  1 
ATOM   2550 C CG  . ARG   A 1 332 ? -27.161 -32.601 21.353  1.00 73.80  ? 331 ARG   A CG  1 
ATOM   2551 C CD  . ARG   A 1 332 ? -26.380 -33.406 22.382  1.00 79.69  ? 331 ARG   A CD  1 
ATOM   2552 N NE  . ARG   A 1 332 ? -27.233 -34.410 23.028  1.00 94.37  ? 331 ARG   A NE  1 
ATOM   2553 C CZ  . ARG   A 1 332 ? -26.830 -35.374 23.854  1.00 101.65 ? 331 ARG   A CZ  1 
ATOM   2554 N NH1 . ARG   A 1 332 ? -25.542 -35.573 24.062  1.00 107.17 ? 331 ARG   A NH1 1 
ATOM   2555 N NH2 . ARG   A 1 332 ? -27.717 -36.150 24.457  1.00 104.94 ? 331 ARG   A NH2 1 
ATOM   2556 N N   . LEU   A 1 333 ? -26.441 -32.306 17.345  1.00 42.89  ? 332 LEU   A N   1 
ATOM   2557 C CA  . LEU   A 1 333 ? -26.764 -31.725 16.027  1.00 50.50  ? 332 LEU   A CA  1 
ATOM   2558 C C   . LEU   A 1 333 ? -28.161 -31.097 16.129  1.00 66.21  ? 332 LEU   A C   1 
ATOM   2559 O O   . LEU   A 1 333 ? -29.094 -31.810 16.530  1.00 71.78  ? 332 LEU   A O   1 
ATOM   2560 C CB  . LEU   A 1 333 ? -26.744 -32.840 14.989  1.00 47.43  ? 332 LEU   A CB  1 
ATOM   2561 C CG  . LEU   A 1 333 ? -25.387 -33.496 14.733  1.00 51.06  ? 332 LEU   A CG  1 
ATOM   2562 C CD1 . LEU   A 1 333 ? -25.530 -34.728 13.862  1.00 57.61  ? 332 LEU   A CD1 1 
ATOM   2563 C CD2 . LEU   A 1 333 ? -24.502 -32.480 14.062  1.00 50.68  ? 332 LEU   A CD2 1 
ATOM   2564 N N   . ARG   A 1 334 ? -28.293 -29.818 15.792  1.00 69.26  ? 333 ARG   A N   1 
ATOM   2565 C CA  . ARG   A 1 334 ? -29.601 -29.117 15.827  1.00 74.70  ? 333 ARG   A CA  1 
ATOM   2566 C C   . ARG   A 1 334 ? -30.530 -29.719 14.766  1.00 73.14  ? 333 ARG   A C   1 
ATOM   2567 O O   . ARG   A 1 334 ? -30.107 -29.790 13.599  1.00 70.30  ? 333 ARG   A O   1 
ATOM   2568 C CB  . ARG   A 1 334 ? -29.308 -27.632 15.600  1.00 80.03  ? 333 ARG   A CB  1 
ATOM   2569 C CG  . ARG   A 1 334 ? -27.999 -27.163 16.213  1.00 79.72  ? 333 ARG   A CG  1 
ATOM   2570 C CD  . ARG   A 1 334 ? -28.243 -26.304 17.437  1.00 78.32  ? 333 ARG   A CD  1 
ATOM   2571 N NE  . ARG   A 1 334 ? -27.049 -25.545 17.820  1.00 80.08  ? 333 ARG   A NE  1 
ATOM   2572 C CZ  . ARG   A 1 334 ? -26.893 -24.246 17.621  1.00 72.99  ? 333 ARG   A CZ  1 
ATOM   2573 N NH1 . ARG   A 1 334 ? -25.924 -23.598 18.242  1.00 75.78  ? 333 ARG   A NH1 1 
ATOM   2574 N NH2 . ARG   A 1 334 ? -27.705 -23.600 16.804  1.00 73.45  ? 333 ARG   A NH2 1 
ATOM   2575 N N   . LEU   A 1 335 ? -31.760 -30.086 15.138  1.00 78.76  ? 334 LEU   A N   1 
ATOM   2576 C CA  . LEU   A 1 335 ? -32.628 -30.783 14.194  1.00 95.55  ? 334 LEU   A CA  1 
ATOM   2577 C C   . LEU   A 1 335 ? -34.119 -30.439 14.334  1.00 98.41  ? 334 LEU   A C   1 
ATOM   2578 O O   . LEU   A 1 335 ? -34.941 -31.355 14.311  1.00 114.16 ? 334 LEU   A O   1 
ATOM   2579 C CB  . LEU   A 1 335 ? -32.411 -32.284 14.399  1.00 95.61  ? 334 LEU   A CB  1 
ATOM   2580 C CG  . LEU   A 1 335 ? -31.162 -32.880 13.749  1.00 95.50  ? 334 LEU   A CG  1 
ATOM   2581 C CD1 . LEU   A 1 335 ? -30.915 -34.288 14.290  1.00 92.80  ? 334 LEU   A CD1 1 
ATOM   2582 C CD2 . LEU   A 1 335 ? -31.315 -32.899 12.225  1.00 100.41 ? 334 LEU   A CD2 1 
ATOM   2583 N N   . SER   A 1 336 ? -34.484 -29.145 14.405  1.00 91.87  ? 335 SER   A N   1 
ATOM   2584 C CA  . SER   A 1 336 ? -35.879 -28.725 14.280  1.00 86.15  ? 335 SER   A CA  1 
ATOM   2585 C C   . SER   A 1 336 ? -35.949 -27.218 13.988  1.00 82.23  ? 335 SER   A C   1 
ATOM   2586 O O   . SER   A 1 336 ? -37.084 -26.727 13.815  1.00 88.94  ? 335 SER   A O   1 
ATOM   2587 C CB  . SER   A 1 336 ? -36.697 -29.097 15.507  1.00 85.96  ? 335 SER   A CB  1 
ATOM   2588 O OG  . SER   A 1 336 ? -38.060 -28.711 15.392  1.00 75.95  ? 335 SER   A OG  1 
HETATM 2589 C C1  . A1H9M B 2 .   ? -6.684  -14.445 -0.043  1.00 132.32 ? 401 A1H9M A C1  1 
HETATM 2590 C C2  . A1H9M B 2 .   ? -7.679  -13.562 0.611   1.00 120.45 ? 401 A1H9M A C2  1 
HETATM 2591 C C3  . A1H9M B 2 .   ? -7.702  -13.255 2.069   1.00 112.28 ? 401 A1H9M A C3  1 
HETATM 2592 O O1  . A1H9M B 2 .   ? -8.191  -12.199 2.503   1.00 90.52  ? 401 A1H9M A O1  1 
HETATM 2593 N N1  . A1H9M B 2 .   ? -7.174  -14.213 2.876   1.00 106.15 ? 401 A1H9M A N1  1 
HETATM 2594 C C4  . A1H9M B 2 .   ? -7.690  -14.749 4.088   1.00 92.30  ? 401 A1H9M A C4  1 
HETATM 2595 C C5  . A1H9M B 2 .   ? -8.597  -14.063 4.901   1.00 93.56  ? 401 A1H9M A C5  1 
HETATM 2596 C C6  . A1H9M B 2 .   ? -9.092  -14.649 6.057   1.00 85.08  ? 401 A1H9M A C6  1 
HETATM 2597 C C7  . A1H9M B 2 .   ? -8.720  -15.940 6.444   1.00 72.80  ? 401 A1H9M A C7  1 
HETATM 2598 C C8  . A1H9M B 2 .   ? -9.308  -16.603 7.651   1.00 57.24  ? 401 A1H9M A C8  1 
HETATM 2599 C C9  . A1H9M B 2 .   ? -9.277  -18.015 7.730   1.00 55.30  ? 401 A1H9M A C9  1 
HETATM 2600 C C10 . A1H9M B 2 .   ? -9.826  -18.711 8.793   1.00 59.88  ? 401 A1H9M A C10 1 
HETATM 2601 C C11 . A1H9M B 2 .   ? -10.449 -17.983 9.809   1.00 51.35  ? 401 A1H9M A C11 1 
HETATM 2602 N N2  . A1H9M B 2 .   ? -11.047 -18.376 10.959  1.00 44.78  ? 401 A1H9M A N2  1 
HETATM 2603 N N3  . A1H9M B 2 .   ? -11.504 -17.309 11.671  1.00 44.89  ? 401 A1H9M A N3  1 
HETATM 2604 C C12 . A1H9M B 2 .   ? -11.203 -16.237 10.956  1.00 51.50  ? 401 A1H9M A C12 1 
HETATM 2605 C C13 . A1H9M B 2 .   ? -10.509 -16.583 9.762   1.00 52.31  ? 401 A1H9M A C13 1 
HETATM 2606 C C14 . A1H9M B 2 .   ? -9.948  -15.893 8.673   1.00 54.19  ? 401 A1H9M A C14 1 
HETATM 2607 C C15 . A1H9M B 2 .   ? -7.837  -16.624 5.597   1.00 71.68  ? 401 A1H9M A C15 1 
HETATM 2608 C C16 . A1H9M B 2 .   ? -7.327  -16.047 4.447   1.00 82.60  ? 401 A1H9M A C16 1 
HETATM 2609 O O   . HOH   C 3 .   ? 19.116  -2.125  10.060  1.00 43.36  ? 501 HOH   A O   1 
HETATM 2610 O O   . HOH   C 3 .   ? 9.531   -13.565 32.520  1.00 58.64  ? 502 HOH   A O   1 
HETATM 2611 O O   . HOH   C 3 .   ? 18.222  -27.313 21.822  1.00 57.43  ? 503 HOH   A O   1 
HETATM 2612 O O   . HOH   C 3 .   ? 7.138   -4.020  28.869  1.00 51.74  ? 504 HOH   A O   1 
HETATM 2613 O O   . HOH   C 3 .   ? -21.496 -41.934 22.860  1.00 57.09  ? 505 HOH   A O   1 
HETATM 2614 O O   . HOH   C 3 .   ? 14.047  -13.479 31.489  1.00 58.89  ? 506 HOH   A O   1 
HETATM 2615 O O   . HOH   C 3 .   ? -3.003  -17.378 25.111  1.00 52.44  ? 507 HOH   A O   1 
HETATM 2616 O O   . HOH   C 3 .   ? -11.216 -38.090 16.231  1.00 54.34  ? 508 HOH   A O   1 
HETATM 2617 O O   . HOH   C 3 .   ? 17.579  2.233   5.028   1.00 35.19  ? 509 HOH   A O   1 
HETATM 2618 O O   . HOH   C 3 .   ? 1.064   -8.105  29.332  1.00 44.49  ? 510 HOH   A O   1 
HETATM 2619 O O   . HOH   C 3 .   ? 20.161  -8.834  12.899  1.00 51.88  ? 511 HOH   A O   1 
HETATM 2620 O O   . HOH   C 3 .   ? -11.156 -27.859 14.806  1.00 54.57  ? 512 HOH   A O   1 
HETATM 2621 O O   . HOH   C 3 .   ? 24.659  -10.372 23.668  1.00 70.85  ? 513 HOH   A O   1 
HETATM 2622 O O   . HOH   C 3 .   ? -22.043 -25.453 -3.794  1.00 61.59  ? 514 HOH   A O   1 
HETATM 2623 O O   . HOH   C 3 .   ? -13.776 -46.974 6.363   1.00 49.40  ? 515 HOH   A O   1 
HETATM 2624 O O   . HOH   C 3 .   ? 2.300   -10.396 32.879  1.00 69.86  ? 516 HOH   A O   1 
HETATM 2625 O O   . HOH   C 3 .   ? -10.800 -15.028 22.479  1.00 64.26  ? 517 HOH   A O   1 
HETATM 2626 O O   . HOH   C 3 .   ? -28.149 -22.406 3.328   1.00 50.01  ? 518 HOH   A O   1 
HETATM 2627 O O   . HOH   C 3 .   ? 5.930   -12.636 7.277   1.00 54.86  ? 519 HOH   A O   1 
HETATM 2628 O O   . HOH   C 3 .   ? 12.562  2.698   23.468  1.00 66.06  ? 520 HOH   A O   1 
HETATM 2629 O O   . HOH   C 3 .   ? -15.148 -38.138 7.395   1.00 40.73  ? 521 HOH   A O   1 
HETATM 2630 O O   . HOH   C 3 .   ? -19.498 -39.478 3.472   1.00 53.58  ? 522 HOH   A O   1 
HETATM 2631 O O   . HOH   C 3 .   ? 9.370   0.847   14.689  1.00 38.00  ? 523 HOH   A O   1 
HETATM 2632 O O   . HOH   C 3 .   ? -14.783 -25.327 15.312  1.00 46.30  ? 524 HOH   A O   1 
HETATM 2633 O O   . HOH   C 3 .   ? -18.275 -32.037 25.510  1.00 73.30  ? 525 HOH   A O   1 
HETATM 2634 O O   . HOH   C 3 .   ? -15.955 -51.721 6.567   1.00 43.38  ? 526 HOH   A O   1 
HETATM 2635 O O   . HOH   C 3 .   ? 7.704   -6.159  27.205  1.00 37.34  ? 527 HOH   A O   1 
HETATM 2636 O O   . HOH   C 3 .   ? -7.241  -26.029 15.663  1.00 44.86  ? 528 HOH   A O   1 
HETATM 2637 O O   . HOH   C 3 .   ? 2.813   -5.085  12.968  1.00 55.30  ? 529 HOH   A O   1 
HETATM 2638 O O   . HOH   C 3 .   ? 21.811  -17.783 16.206  1.00 53.62  ? 530 HOH   A O   1 
HETATM 2639 O O   . HOH   C 3 .   ? 14.584  -0.470  15.970  1.00 45.10  ? 531 HOH   A O   1 
HETATM 2640 O O   . HOH   C 3 .   ? -17.456 -40.806 4.027   1.00 39.49  ? 532 HOH   A O   1 
HETATM 2641 O O   . HOH   C 3 .   ? 11.957  -8.266  8.493   1.00 33.79  ? 533 HOH   A O   1 
HETATM 2642 O O   . HOH   C 3 .   ? -17.689 -45.095 18.334  1.00 37.94  ? 534 HOH   A O   1 
HETATM 2643 O O   . HOH   C 3 .   ? 19.084  -21.658 10.211  1.00 47.74  ? 535 HOH   A O   1 
HETATM 2644 O O   . HOH   C 3 .   ? -15.426 -23.281 13.360  1.00 35.99  ? 536 HOH   A O   1 
HETATM 2645 O O   . HOH   C 3 .   ? 16.722  -25.191 28.366  1.00 53.20  ? 537 HOH   A O   1 
HETATM 2646 O O   . HOH   C 3 .   ? -12.249 -30.685 15.352  1.00 42.28  ? 538 HOH   A O   1 
HETATM 2647 O O   . HOH   C 3 .   ? 14.918  5.376   -0.153  1.00 38.52  ? 539 HOH   A O   1 
HETATM 2648 O O   . HOH   C 3 .   ? -10.856 -32.652 -1.088  1.00 48.43  ? 540 HOH   A O   1 
HETATM 2649 O O   . HOH   C 3 .   ? -11.739 -31.725 -5.086  1.00 74.58  ? 541 HOH   A O   1 
HETATM 2650 O O   . HOH   C 3 .   ? 17.223  -3.992  27.935  1.00 57.19  ? 542 HOH   A O   1 
HETATM 2651 O O   . HOH   C 3 .   ? 16.145  -0.773  12.532  1.00 45.56  ? 543 HOH   A O   1 
HETATM 2652 O O   . HOH   C 3 .   ? -8.475  -31.229 9.028   1.00 47.10  ? 544 HOH   A O   1 
HETATM 2653 O O   . HOH   C 3 .   ? 1.678   -21.151 26.289  1.00 44.42  ? 545 HOH   A O   1 
HETATM 2654 O O   . HOH   C 3 .   ? -18.733 -38.697 27.202  1.00 67.90  ? 546 HOH   A O   1 
HETATM 2655 O O   . HOH   C 3 .   ? -29.498 -45.688 7.861   1.00 53.70  ? 547 HOH   A O   1 
HETATM 2656 O O   . HOH   C 3 .   ? 10.365  -4.833  11.268  1.00 34.41  ? 548 HOH   A O   1 
HETATM 2657 O O   . HOH   C 3 .   ? 20.952  -28.912 19.078  1.00 55.92  ? 549 HOH   A O   1 
HETATM 2658 O O   . HOH   C 3 .   ? 20.029  -9.716  16.137  1.00 51.14  ? 550 HOH   A O   1 
HETATM 2659 O O   . HOH   C 3 .   ? 12.081  -9.037  28.407  1.00 39.87  ? 551 HOH   A O   1 
HETATM 2660 O O   . HOH   C 3 .   ? -16.882 -32.465 -1.073  1.00 46.05  ? 552 HOH   A O   1 
HETATM 2661 O O   . HOH   C 3 .   ? 10.275  -14.498 6.408   1.00 35.20  ? 553 HOH   A O   1 
HETATM 2662 O O   . HOH   C 3 .   ? -13.998 -47.767 10.916  1.00 48.45  ? 554 HOH   A O   1 
HETATM 2663 O O   . HOH   C 3 .   ? -19.315 -32.118 0.265   1.00 49.15  ? 555 HOH   A O   1 
HETATM 2664 O O   . HOH   C 3 .   ? -5.508  -28.057 12.519  1.00 49.84  ? 556 HOH   A O   1 
HETATM 2665 O O   . HOH   C 3 .   ? 3.751   0.559   17.051  1.00 34.14  ? 557 HOH   A O   1 
HETATM 2666 O O   . HOH   C 3 .   ? -11.469 -21.675 17.128  1.00 54.02  ? 558 HOH   A O   1 
HETATM 2667 O O   . HOH   C 3 .   ? 16.741  -19.088 3.909   1.00 37.53  ? 559 HOH   A O   1 
HETATM 2668 O O   . HOH   C 3 .   ? 12.777  -21.460 35.097  1.00 61.90  ? 560 HOH   A O   1 
HETATM 2669 O O   . HOH   C 3 .   ? -13.777 -48.520 13.144  1.00 57.21  ? 561 HOH   A O   1 
HETATM 2670 O O   . HOH   C 3 .   ? -24.968 -28.533 7.837   1.00 35.16  ? 562 HOH   A O   1 
HETATM 2671 O O   . HOH   C 3 .   ? 18.022  -25.008 7.708   1.00 42.46  ? 563 HOH   A O   1 
HETATM 2672 O O   . HOH   C 3 .   ? -27.350 -29.222 6.353   1.00 50.51  ? 564 HOH   A O   1 
HETATM 2673 O O   . HOH   C 3 .   ? 12.220  5.065   10.568  1.00 63.27  ? 565 HOH   A O   1 
HETATM 2674 O O   . HOH   C 3 .   ? 11.820  -25.004 4.771   1.00 50.36  ? 566 HOH   A O   1 
HETATM 2675 O O   . HOH   C 3 .   ? 23.772  -12.950 10.566  1.00 41.02  ? 567 HOH   A O   1 
HETATM 2676 O O   . HOH   C 3 .   ? -20.071 -21.200 16.574  1.00 49.04  ? 568 HOH   A O   1 
HETATM 2677 O O   . HOH   C 3 .   ? 20.638  -12.913 3.978   1.00 50.84  ? 569 HOH   A O   1 
HETATM 2678 O O   . HOH   C 3 .   ? 1.946   -24.544 28.497  1.00 67.07  ? 570 HOH   A O   1 
HETATM 2679 O O   . HOH   C 3 .   ? -16.103 -38.715 4.685   1.00 39.50  ? 571 HOH   A O   1 
HETATM 2680 O O   . HOH   C 3 .   ? 18.587  -8.335  20.617  1.00 42.25  ? 572 HOH   A O   1 
HETATM 2681 O O   . HOH   C 3 .   ? -21.101 -52.267 10.100  0.50 44.46  ? 573 HOH   A O   1 
HETATM 2682 O O   . HOH   C 3 .   ? 21.285  -14.943 2.135   1.00 66.72  ? 574 HOH   A O   1 
HETATM 2683 O O   . HOH   C 3 .   ? -13.354 -33.014 -0.390  1.00 45.64  ? 575 HOH   A O   1 
HETATM 2684 O O   . HOH   C 3 .   ? 22.297  -10.252 11.775  1.00 43.59  ? 576 HOH   A O   1 
HETATM 2685 O O   . HOH   C 3 .   ? 0.056   -5.781  28.718  1.00 62.69  ? 577 HOH   A O   1 
HETATM 2686 O O   . HOH   C 3 .   ? 18.647  -23.785 23.192  1.00 50.37  ? 578 HOH   A O   1 
HETATM 2687 O O   . HOH   C 3 .   ? -6.613  -29.109 8.875   1.00 42.05  ? 579 HOH   A O   1 
HETATM 2688 O O   . HOH   C 3 .   ? -26.809 -18.205 2.894   1.00 56.07  ? 580 HOH   A O   1 
HETATM 2689 O O   . HOH   C 3 .   ? -25.396 -44.101 5.947   1.00 60.14  ? 581 HOH   A O   1 
HETATM 2690 O O   . HOH   C 3 .   ? 7.932   -13.829 5.474   1.00 47.24  ? 582 HOH   A O   1 
HETATM 2691 O O   . HOH   C 3 .   ? 8.230   -7.725  31.118  1.00 46.43  ? 583 HOH   A O   1 
HETATM 2692 O O   . HOH   C 3 .   ? 5.097   -14.041 2.323   1.00 73.88  ? 584 HOH   A O   1 
HETATM 2693 O O   . HOH   C 3 .   ? 3.145   -23.669 26.297  1.00 57.48  ? 585 HOH   A O   1 
HETATM 2694 O O   . HOH   C 3 .   ? 11.225  -24.227 1.979   1.00 55.24  ? 586 HOH   A O   1 
HETATM 2695 O O   . HOH   C 3 .   ? 13.877  0.987   11.646  1.00 45.44  ? 587 HOH   A O   1 
HETATM 2696 O O   . HOH   C 3 .   ? 7.341   -16.246 7.763   1.00 37.24  ? 588 HOH   A O   1 
HETATM 2697 O O   . HOH   C 3 .   ? 16.612  -21.684 11.080  1.00 45.96  ? 589 HOH   A O   1 
HETATM 2698 O O   . HOH   C 3 .   ? -9.945  -36.308 1.281   1.00 50.30  ? 590 HOH   A O   1 
HETATM 2699 O O   . HOH   C 3 .   ? -1.363  1.167   22.161  1.00 69.32  ? 591 HOH   A O   1 
HETATM 2700 O O   . HOH   C 3 .   ? -21.824 -51.547 15.227  1.00 51.95  ? 592 HOH   A O   1 
HETATM 2701 O O   . HOH   C 3 .   ? -28.829 -37.934 20.433  1.00 70.43  ? 593 HOH   A O   1 
HETATM 2702 O O   . HOH   C 3 .   ? 7.612   0.646   8.036   1.00 43.67  ? 594 HOH   A O   1 
HETATM 2703 O O   . HOH   C 3 .   ? -31.607 -47.250 8.850   1.00 60.82  ? 595 HOH   A O   1 
HETATM 2704 O O   . HOH   C 3 .   ? 19.553  -0.051  21.291  1.00 55.27  ? 596 HOH   A O   1 
HETATM 2705 O O   . HOH   C 3 .   ? -2.789  -13.774 25.843  1.00 73.11  ? 597 HOH   A O   1 
HETATM 2706 O O   . HOH   C 3 .   ? 18.799  -25.057 26.282  1.00 57.81  ? 598 HOH   A O   1 
HETATM 2707 O O   . HOH   C 3 .   ? -16.689 -31.671 -3.900  1.00 56.77  ? 599 HOH   A O   1 
HETATM 2708 O O   . HOH   C 3 .   ? -13.765 -41.892 22.358  1.00 57.87  ? 600 HOH   A O   1 
HETATM 2709 O O   . HOH   C 3 .   ? 14.806  6.809   2.019   1.00 42.80  ? 601 HOH   A O   1 
HETATM 2710 O O   . HOH   C 3 .   ? 7.642   2.332   -1.129  1.00 49.94  ? 602 HOH   A O   1 
HETATM 2711 O O   . HOH   C 3 .   ? 5.666   -16.875 31.372  1.00 59.87  ? 603 HOH   A O   1 
HETATM 2712 O O   . HOH   C 3 .   ? 23.400  -8.517  24.607  1.00 67.03  ? 604 HOH   A O   1 
HETATM 2713 O O   . HOH   C 3 .   ? -23.386 -35.330 8.398   1.00 30.84  ? 605 HOH   A O   1 
HETATM 2714 O O   . HOH   C 3 .   ? -21.353 -27.019 -10.354 1.00 63.34  ? 606 HOH   A O   1 
HETATM 2715 O O   . HOH   C 3 .   ? 16.929  -12.288 31.744  1.00 58.53  ? 607 HOH   A O   1 
HETATM 2716 O O   . HOH   C 3 .   ? 3.775   -26.372 25.264  1.00 57.73  ? 608 HOH   A O   1 
HETATM 2717 O O   . HOH   C 3 .   ? -29.428 -46.498 14.659  1.00 58.92  ? 609 HOH   A O   1 
HETATM 2718 O O   . HOH   C 3 .   ? 11.704  2.836   -2.630  1.00 47.02  ? 610 HOH   A O   1 
HETATM 2719 O O   . HOH   C 3 .   ? 18.827  -18.648 1.837   1.00 56.76  ? 611 HOH   A O   1 
HETATM 2720 O O   . HOH   C 3 .   ? 9.794   -7.260  28.706  1.00 43.36  ? 612 HOH   A O   1 
HETATM 2721 O O   . HOH   C 3 .   ? 16.088  -28.078 13.877  1.00 50.19  ? 613 HOH   A O   1 
HETATM 2722 O O   . HOH   C 3 .   ? -20.707 -44.404 23.464  1.00 72.30  ? 614 HOH   A O   1 
HETATM 2723 O O   . HOH   C 3 .   ? 20.654  4.198   2.396   1.00 51.45  ? 615 HOH   A O   1 
HETATM 2724 O O   . HOH   C 3 .   ? 22.391  0.081   3.961   1.00 69.56  ? 616 HOH   A O   1 
HETATM 2725 O O   . HOH   C 3 .   ? -10.915 -30.862 17.613  1.00 55.96  ? 617 HOH   A O   1 
HETATM 2726 O O   . HOH   C 3 .   ? 10.119  3.636   23.783  1.00 72.30  ? 618 HOH   A O   1 
HETATM 2727 O O   . HOH   C 3 .   ? 4.156   2.828   18.285  1.00 45.68  ? 619 HOH   A O   1 
HETATM 2728 O O   . HOH   C 3 .   ? -5.993  -36.983 4.715   1.00 66.01  ? 620 HOH   A O   1 
HETATM 2729 O O   . HOH   C 3 .   ? -28.011 -31.807 5.899   1.00 71.39  ? 621 HOH   A O   1 
HETATM 2730 O O   . HOH   C 3 .   ? 16.649  6.327   3.674   1.00 51.41  ? 622 HOH   A O   1 
HETATM 2731 O O   . HOH   C 3 .   ? 18.839  9.343   4.108   1.00 70.09  ? 623 HOH   A O   1 
# 
