data_9DTK
# 
_entry.id   9DTK 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   9DTK         pdb_00009dtk 10.2210/pdb9dtk/pdb 
WWPDB D_1000282825 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-22 
# 
_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                        9DTK 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-01 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
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 
4 mmartine@unizar.es Marta    Martinez-Julvez M 'principal investigator/group leader' 0000-0001-9047-0046 
5 mmedina@unizar.es  Milagros Medina          ? 'principal investigator/group leader' 0000-0001-8743-0182 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Martinez-Julvez, M.' 1 0000-0001-9047-0046 
'Medina, M.'          2 0000-0001-8743-0182 
'Minjarez-Saenz, M.'  3 0000-0001-7947-8813 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Arch.Biochem.Biophys. 
_citation.journal_id_ASTM           ABBIA4 
_citation.journal_id_CSD            0158 
_citation.journal_id_ISSN           1096-0384 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            765 
_citation.language                  ? 
_citation.page_first                110288 
_citation.page_last                 110288 
_citation.title                     
'Structural and functional insights into UDP-N-acetylglucosamine-enolpyruvate reductase (MurB) from Brucella ovis.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.abb.2025.110288 
_citation.pdbx_database_id_PubMed   39761724 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Minjarez-Saenz, M.'  1  ? 
primary 'Rivero, M.'          2  ? 
primary 'Correa-Perez, V.'    3  ? 
primary 'Boneta, S.'          4  ? 
primary 'Suarez, P.'          5  ? 
primary 'Polo, V.'            6  ? 
primary 'Sadeghi, S.J.'       7  ? 
primary 'Yruela, I.'          8  ? 
primary 'Martinez-Julvez, M.' 9  ? 
primary 'Medina, M.'          10 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'UDP-N-acetylenolpyruvoylglucosamine reductase'            34938.605 1  1.3.1.98 ? ? ? 
2 non-polymer syn 'SULFATE ION'                                              96.063    1  ?        ? ? ? 
3 non-polymer syn 'FLAVIN-ADENINE DINUCLEOTIDE'                              785.550   1  ?        ? ? ? 
4 non-polymer syn 'URIDINE-DIPHOSPHATE-2(N-ACETYLGLUCOSAMINYL) BUTYRIC ACID' 677.400   1  ?        ? ? ? 
5 water       nat water                                                      18.015    94 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'UDP-N-acetylmuramate dehydrogenase' 
# 
_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       
;MMESGEALLKKLDGRLSGLRGRLTPDTGMDKITWFRAGGPAQVLFQPSDEEDLSAFLKAVPEEIPLLVVGIGSNLLVRDG
GVPGFVVRLSAKGFGEVEQVCDTQLRAGAAAPDKRVAAAALEAGLAGFHFYHGIPGGIGGALRMNAGANGVETRERVVEV
RALDRKGEVHVLSNADMGYAYRHSSASPDLIFTSVLFEGVPGERDDIRRAMDEVQHHRETVQPVREKTGGSTFKNPEGTS
AWKEIDKAGCRGLRVGGAQMSEMHCNFMINTGNATGHDLETLGETVRARVFENSGIRLHWEIKRLGLFREGEQIEEFLGK
IV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MMESGEALLKKLDGRLSGLRGRLTPDTGMDKITWFRAGGPAQVLFQPSDEEDLSAFLKAVPEEIPLLVVGIGSNLLVRDG
GVPGFVVRLSAKGFGEVEQVCDTQLRAGAAAPDKRVAAAALEAGLAGFHFYHGIPGGIGGALRMNAGANGVETRERVVEV
RALDRKGEVHVLSNADMGYAYRHSSASPDLIFTSVLFEGVPGERDDIRRAMDEVQHHRETVQPVREKTGGSTFKNPEGTS
AWKEIDKAGCRGLRVGGAQMSEMHCNFMINTGNATGHDLETLGETVRARVFENSGIRLHWEIKRLGLFREGEQIEEFLGK
IV
;
_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 'SULFATE ION'                                              SO4 
3 'FLAVIN-ADENINE DINUCLEOTIDE'                              FAD 
4 'URIDINE-DIPHOSPHATE-2(N-ACETYLGLUCOSAMINYL) BUTYRIC ACID' EPU 
5 water                                                      HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   MET n 
1 3   GLU n 
1 4   SER n 
1 5   GLY n 
1 6   GLU n 
1 7   ALA n 
1 8   LEU n 
1 9   LEU n 
1 10  LYS n 
1 11  LYS n 
1 12  LEU n 
1 13  ASP n 
1 14  GLY n 
1 15  ARG n 
1 16  LEU n 
1 17  SER n 
1 18  GLY n 
1 19  LEU n 
1 20  ARG n 
1 21  GLY n 
1 22  ARG n 
1 23  LEU n 
1 24  THR n 
1 25  PRO n 
1 26  ASP n 
1 27  THR n 
1 28  GLY n 
1 29  MET n 
1 30  ASP n 
1 31  LYS n 
1 32  ILE n 
1 33  THR n 
1 34  TRP n 
1 35  PHE n 
1 36  ARG n 
1 37  ALA n 
1 38  GLY n 
1 39  GLY n 
1 40  PRO n 
1 41  ALA n 
1 42  GLN n 
1 43  VAL n 
1 44  LEU n 
1 45  PHE n 
1 46  GLN n 
1 47  PRO n 
1 48  SER n 
1 49  ASP n 
1 50  GLU n 
1 51  GLU n 
1 52  ASP n 
1 53  LEU n 
1 54  SER n 
1 55  ALA n 
1 56  PHE n 
1 57  LEU n 
1 58  LYS n 
1 59  ALA n 
1 60  VAL n 
1 61  PRO n 
1 62  GLU n 
1 63  GLU n 
1 64  ILE n 
1 65  PRO n 
1 66  LEU n 
1 67  LEU n 
1 68  VAL n 
1 69  VAL n 
1 70  GLY n 
1 71  ILE n 
1 72  GLY n 
1 73  SER n 
1 74  ASN n 
1 75  LEU n 
1 76  LEU n 
1 77  VAL n 
1 78  ARG n 
1 79  ASP n 
1 80  GLY n 
1 81  GLY n 
1 82  VAL n 
1 83  PRO n 
1 84  GLY n 
1 85  PHE n 
1 86  VAL n 
1 87  VAL n 
1 88  ARG n 
1 89  LEU n 
1 90  SER n 
1 91  ALA n 
1 92  LYS n 
1 93  GLY n 
1 94  PHE n 
1 95  GLY n 
1 96  GLU n 
1 97  VAL n 
1 98  GLU n 
1 99  GLN n 
1 100 VAL n 
1 101 CYS n 
1 102 ASP n 
1 103 THR n 
1 104 GLN n 
1 105 LEU n 
1 106 ARG n 
1 107 ALA n 
1 108 GLY n 
1 109 ALA n 
1 110 ALA n 
1 111 ALA n 
1 112 PRO n 
1 113 ASP n 
1 114 LYS n 
1 115 ARG n 
1 116 VAL n 
1 117 ALA n 
1 118 ALA n 
1 119 ALA n 
1 120 ALA n 
1 121 LEU n 
1 122 GLU n 
1 123 ALA n 
1 124 GLY n 
1 125 LEU n 
1 126 ALA n 
1 127 GLY n 
1 128 PHE n 
1 129 HIS n 
1 130 PHE n 
1 131 TYR n 
1 132 HIS n 
1 133 GLY n 
1 134 ILE n 
1 135 PRO n 
1 136 GLY n 
1 137 GLY n 
1 138 ILE n 
1 139 GLY n 
1 140 GLY n 
1 141 ALA n 
1 142 LEU n 
1 143 ARG n 
1 144 MET n 
1 145 ASN n 
1 146 ALA n 
1 147 GLY n 
1 148 ALA n 
1 149 ASN n 
1 150 GLY n 
1 151 VAL n 
1 152 GLU n 
1 153 THR n 
1 154 ARG n 
1 155 GLU n 
1 156 ARG n 
1 157 VAL n 
1 158 VAL n 
1 159 GLU n 
1 160 VAL n 
1 161 ARG n 
1 162 ALA n 
1 163 LEU n 
1 164 ASP n 
1 165 ARG n 
1 166 LYS n 
1 167 GLY n 
1 168 GLU n 
1 169 VAL n 
1 170 HIS n 
1 171 VAL n 
1 172 LEU n 
1 173 SER n 
1 174 ASN n 
1 175 ALA n 
1 176 ASP n 
1 177 MET n 
1 178 GLY n 
1 179 TYR n 
1 180 ALA n 
1 181 TYR n 
1 182 ARG n 
1 183 HIS n 
1 184 SER n 
1 185 SER n 
1 186 ALA n 
1 187 SER n 
1 188 PRO n 
1 189 ASP n 
1 190 LEU n 
1 191 ILE n 
1 192 PHE n 
1 193 THR n 
1 194 SER n 
1 195 VAL n 
1 196 LEU n 
1 197 PHE n 
1 198 GLU n 
1 199 GLY n 
1 200 VAL n 
1 201 PRO n 
1 202 GLY n 
1 203 GLU n 
1 204 ARG n 
1 205 ASP n 
1 206 ASP n 
1 207 ILE n 
1 208 ARG n 
1 209 ARG n 
1 210 ALA n 
1 211 MET n 
1 212 ASP n 
1 213 GLU n 
1 214 VAL n 
1 215 GLN n 
1 216 HIS n 
1 217 HIS n 
1 218 ARG n 
1 219 GLU n 
1 220 THR n 
1 221 VAL n 
1 222 GLN n 
1 223 PRO n 
1 224 VAL n 
1 225 ARG n 
1 226 GLU n 
1 227 LYS n 
1 228 THR n 
1 229 GLY n 
1 230 GLY n 
1 231 SER n 
1 232 THR n 
1 233 PHE n 
1 234 LYS n 
1 235 ASN n 
1 236 PRO n 
1 237 GLU n 
1 238 GLY n 
1 239 THR n 
1 240 SER n 
1 241 ALA n 
1 242 TRP n 
1 243 LYS n 
1 244 GLU n 
1 245 ILE n 
1 246 ASP n 
1 247 LYS n 
1 248 ALA n 
1 249 GLY n 
1 250 CYS n 
1 251 ARG n 
1 252 GLY n 
1 253 LEU n 
1 254 ARG n 
1 255 VAL n 
1 256 GLY n 
1 257 GLY n 
1 258 ALA n 
1 259 GLN n 
1 260 MET n 
1 261 SER n 
1 262 GLU n 
1 263 MET n 
1 264 HIS n 
1 265 CYS n 
1 266 ASN n 
1 267 PHE n 
1 268 MET n 
1 269 ILE n 
1 270 ASN n 
1 271 THR n 
1 272 GLY n 
1 273 ASN n 
1 274 ALA n 
1 275 THR n 
1 276 GLY n 
1 277 HIS n 
1 278 ASP n 
1 279 LEU n 
1 280 GLU n 
1 281 THR n 
1 282 LEU n 
1 283 GLY n 
1 284 GLU n 
1 285 THR n 
1 286 VAL n 
1 287 ARG n 
1 288 ALA n 
1 289 ARG n 
1 290 VAL n 
1 291 PHE n 
1 292 GLU n 
1 293 ASN n 
1 294 SER n 
1 295 GLY n 
1 296 ILE n 
1 297 ARG n 
1 298 LEU n 
1 299 HIS n 
1 300 TRP n 
1 301 GLU n 
1 302 ILE n 
1 303 LYS n 
1 304 ARG n 
1 305 LEU n 
1 306 GLY n 
1 307 LEU n 
1 308 PHE n 
1 309 ARG n 
1 310 GLU n 
1 311 GLY n 
1 312 GLU n 
1 313 GLN n 
1 314 ILE n 
1 315 GLU n 
1 316 GLU n 
1 317 PHE n 
1 318 LEU n 
1 319 GLY n 
1 320 LYS n 
1 321 ILE n 
1 322 VAL 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                   322 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'murB, BOV_1386' 
_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      'Brucella ovis ATCC 25840' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     444178 
_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 
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 
EPU non-polymer         . 'URIDINE-DIPHOSPHATE-2(N-ACETYLGLUCOSAMINYL) BUTYRIC ACID' 
ENOLPYRUVYL-URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE 'C20 H29 N3 O19 P2' 677.400 
FAD non-polymer         . 'FLAVIN-ADENINE DINUCLEOTIDE'                              ? 'C27 H33 N9 O15 P2' 785.550 
GLN 'L-peptide linking' y GLUTAMINE                                                  ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                            ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                                                    ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                                                  ? 'C6 H10 N3 O2 1'    156.162 
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 
SO4 non-polymer         . 'SULFATE ION'                                              ? 'O4 S -2'           96.063  
THR 'L-peptide linking' y THREONINE                                                  ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                 ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                                                   ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                                                     ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   1   MET MET A . n 
A 1 2   MET 2   2   2   MET MET A . n 
A 1 3   GLU 3   3   3   GLU GLU A . n 
A 1 4   SER 4   4   4   SER SER A . n 
A 1 5   GLY 5   5   5   GLY GLY A . n 
A 1 6   GLU 6   6   6   GLU GLU A . n 
A 1 7   ALA 7   7   7   ALA ALA A . n 
A 1 8   LEU 8   8   8   LEU LEU A . n 
A 1 9   LEU 9   9   9   LEU LEU A . n 
A 1 10  LYS 10  10  10  LYS LYS A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  ASP 13  13  13  ASP ASP A . n 
A 1 14  GLY 14  14  14  GLY GLY A . n 
A 1 15  ARG 15  15  15  ARG ARG A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  SER 17  17  17  SER SER A . n 
A 1 18  GLY 18  18  18  GLY GLY A . n 
A 1 19  LEU 19  19  19  LEU LEU A . n 
A 1 20  ARG 20  20  20  ARG ARG A . n 
A 1 21  GLY 21  21  21  GLY GLY A . n 
A 1 22  ARG 22  22  22  ARG ARG A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  PRO 25  25  25  PRO PRO A . n 
A 1 26  ASP 26  26  26  ASP ASP A . n 
A 1 27  THR 27  27  27  THR THR A . n 
A 1 28  GLY 28  28  28  GLY GLY A . n 
A 1 29  MET 29  29  29  MET MET A . n 
A 1 30  ASP 30  30  30  ASP ASP A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  ILE 32  32  32  ILE ILE A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  TRP 34  34  34  TRP TRP A . n 
A 1 35  PHE 35  35  35  PHE PHE A . n 
A 1 36  ARG 36  36  36  ARG ARG A . n 
A 1 37  ALA 37  37  37  ALA ALA A . n 
A 1 38  GLY 38  38  38  GLY GLY A . n 
A 1 39  GLY 39  39  39  GLY GLY A . n 
A 1 40  PRO 40  40  40  PRO PRO A . n 
A 1 41  ALA 41  41  41  ALA ALA A . n 
A 1 42  GLN 42  42  42  GLN GLN A . n 
A 1 43  VAL 43  43  43  VAL VAL A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  PHE 45  45  45  PHE PHE A . n 
A 1 46  GLN 46  46  46  GLN GLN A . n 
A 1 47  PRO 47  47  47  PRO PRO A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  ASP 49  49  49  ASP ASP A . n 
A 1 50  GLU 50  50  50  GLU GLU A . n 
A 1 51  GLU 51  51  51  GLU GLU A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  SER 54  54  54  SER SER A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  PHE 56  56  56  PHE PHE A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  LYS 58  58  58  LYS LYS A . n 
A 1 59  ALA 59  59  59  ALA ALA A . n 
A 1 60  VAL 60  60  60  VAL VAL A . n 
A 1 61  PRO 61  61  61  PRO PRO A . n 
A 1 62  GLU 62  62  62  GLU GLU A . n 
A 1 63  GLU 63  63  63  GLU GLU A . n 
A 1 64  ILE 64  64  64  ILE ILE A . n 
A 1 65  PRO 65  65  65  PRO PRO A . n 
A 1 66  LEU 66  66  66  LEU LEU A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  VAL 69  69  69  VAL VAL A . n 
A 1 70  GLY 70  70  70  GLY GLY A . n 
A 1 71  ILE 71  71  71  ILE ILE A . n 
A 1 72  GLY 72  72  72  GLY GLY A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  ASN 74  74  74  ASN ASN A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LEU 76  76  76  LEU LEU A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  ARG 78  78  78  ARG ARG A . n 
A 1 79  ASP 79  79  79  ASP ASP A . n 
A 1 80  GLY 80  80  80  GLY GLY A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  GLY 84  84  84  GLY GLY A . n 
A 1 85  PHE 85  85  85  PHE PHE A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  ARG 88  88  88  ARG ARG A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  SER 90  90  90  SER SER A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  LYS 92  92  92  LYS LYS A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  PHE 94  94  94  PHE PHE A . n 
A 1 95  GLY 95  95  95  GLY GLY A . n 
A 1 96  GLU 96  96  96  GLU GLU A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  GLU 98  98  98  GLU GLU A . n 
A 1 99  GLN 99  99  99  GLN GLN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 CYS 101 101 101 CYS CYS A . n 
A 1 102 ASP 102 102 102 ASP ASP A . n 
A 1 103 THR 103 103 103 THR THR A . n 
A 1 104 GLN 104 104 104 GLN GLN A . n 
A 1 105 LEU 105 105 105 LEU LEU A . n 
A 1 106 ARG 106 106 106 ARG ARG A . n 
A 1 107 ALA 107 107 107 ALA ALA A . n 
A 1 108 GLY 108 108 108 GLY GLY A . n 
A 1 109 ALA 109 109 109 ALA ALA A . n 
A 1 110 ALA 110 110 110 ALA ALA A . n 
A 1 111 ALA 111 111 111 ALA ALA A . n 
A 1 112 PRO 112 112 112 PRO PRO A . n 
A 1 113 ASP 113 113 113 ASP ASP A . n 
A 1 114 LYS 114 114 114 LYS LYS A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 VAL 116 116 116 VAL VAL A . n 
A 1 117 ALA 117 117 117 ALA ALA A . n 
A 1 118 ALA 118 118 118 ALA ALA A . n 
A 1 119 ALA 119 119 119 ALA ALA A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 LEU 121 121 121 LEU LEU A . n 
A 1 122 GLU 122 122 122 GLU GLU A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 GLY 124 124 124 GLY GLY A . n 
A 1 125 LEU 125 125 125 LEU LEU A . n 
A 1 126 ALA 126 126 126 ALA ALA A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 PHE 128 128 128 PHE PHE A . n 
A 1 129 HIS 129 129 129 HIS HIS A . n 
A 1 130 PHE 130 130 130 PHE PHE A . n 
A 1 131 TYR 131 131 131 TYR TYR A . n 
A 1 132 HIS 132 132 132 HIS HIS A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ILE 134 134 134 ILE ILE A . n 
A 1 135 PRO 135 135 135 PRO PRO A . n 
A 1 136 GLY 136 136 136 GLY GLY A . n 
A 1 137 GLY 137 137 137 GLY GLY A . n 
A 1 138 ILE 138 138 138 ILE ILE A . n 
A 1 139 GLY 139 139 139 GLY GLY A . n 
A 1 140 GLY 140 140 140 GLY GLY A . n 
A 1 141 ALA 141 141 141 ALA ALA A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 ARG 143 143 143 ARG ARG A . n 
A 1 144 MET 144 144 144 MET MET A . n 
A 1 145 ASN 145 145 145 ASN ASN A . n 
A 1 146 ALA 146 146 146 ALA ALA A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 ALA 148 148 148 ALA ALA A . n 
A 1 149 ASN 149 149 149 ASN ASN A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 GLU 152 152 152 GLU GLU A . n 
A 1 153 THR 153 153 153 THR THR A . n 
A 1 154 ARG 154 154 154 ARG ARG A . n 
A 1 155 GLU 155 155 155 GLU GLU A . n 
A 1 156 ARG 156 156 156 ARG ARG A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 VAL 158 158 158 VAL VAL A . n 
A 1 159 GLU 159 159 159 GLU GLU A . n 
A 1 160 VAL 160 160 160 VAL VAL A . n 
A 1 161 ARG 161 161 161 ARG ARG A . n 
A 1 162 ALA 162 162 162 ALA ALA A . n 
A 1 163 LEU 163 163 163 LEU LEU A . n 
A 1 164 ASP 164 164 164 ASP ASP A . n 
A 1 165 ARG 165 165 165 ARG ARG A . n 
A 1 166 LYS 166 166 166 LYS LYS A . n 
A 1 167 GLY 167 167 167 GLY GLY A . n 
A 1 168 GLU 168 168 168 GLU GLU A . n 
A 1 169 VAL 169 169 169 VAL VAL A . n 
A 1 170 HIS 170 170 170 HIS HIS A . n 
A 1 171 VAL 171 171 171 VAL VAL A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 SER 173 173 173 SER SER A . n 
A 1 174 ASN 174 174 174 ASN ASN A . n 
A 1 175 ALA 175 175 175 ALA ALA A . n 
A 1 176 ASP 176 176 176 ASP ASP A . n 
A 1 177 MET 177 177 177 MET MET A . n 
A 1 178 GLY 178 178 178 GLY GLY A . n 
A 1 179 TYR 179 179 179 TYR TYR A . n 
A 1 180 ALA 180 180 180 ALA ALA A . n 
A 1 181 TYR 181 181 181 TYR TYR A . n 
A 1 182 ARG 182 182 182 ARG ARG A . n 
A 1 183 HIS 183 183 183 HIS HIS A . n 
A 1 184 SER 184 184 184 SER SER A . n 
A 1 185 SER 185 185 185 SER SER A . n 
A 1 186 ALA 186 186 186 ALA ALA A . n 
A 1 187 SER 187 187 187 SER SER A . n 
A 1 188 PRO 188 188 188 PRO PRO A . n 
A 1 189 ASP 189 189 189 ASP ASP A . n 
A 1 190 LEU 190 190 190 LEU LEU A . n 
A 1 191 ILE 191 191 191 ILE ILE A . n 
A 1 192 PHE 192 192 192 PHE PHE A . n 
A 1 193 THR 193 193 193 THR THR A . n 
A 1 194 SER 194 194 194 SER SER A . n 
A 1 195 VAL 195 195 195 VAL VAL A . n 
A 1 196 LEU 196 196 196 LEU LEU A . n 
A 1 197 PHE 197 197 197 PHE PHE A . n 
A 1 198 GLU 198 198 198 GLU GLU A . n 
A 1 199 GLY 199 199 199 GLY GLY A . n 
A 1 200 VAL 200 200 200 VAL VAL A . n 
A 1 201 PRO 201 201 201 PRO PRO A . n 
A 1 202 GLY 202 202 202 GLY GLY A . n 
A 1 203 GLU 203 203 203 GLU GLU A . n 
A 1 204 ARG 204 204 204 ARG ARG A . n 
A 1 205 ASP 205 205 205 ASP ASP A . n 
A 1 206 ASP 206 206 206 ASP ASP A . n 
A 1 207 ILE 207 207 207 ILE ILE A . n 
A 1 208 ARG 208 208 208 ARG ARG A . n 
A 1 209 ARG 209 209 209 ARG ARG A . n 
A 1 210 ALA 210 210 210 ALA ALA A . n 
A 1 211 MET 211 211 211 MET MET A . n 
A 1 212 ASP 212 212 212 ASP ASP A . n 
A 1 213 GLU 213 213 213 GLU GLU A . n 
A 1 214 VAL 214 214 214 VAL VAL A . n 
A 1 215 GLN 215 215 215 GLN GLN A . n 
A 1 216 HIS 216 216 216 HIS HIS A . n 
A 1 217 HIS 217 217 217 HIS HIS A . n 
A 1 218 ARG 218 218 218 ARG ARG A . n 
A 1 219 GLU 219 219 219 GLU GLU A . n 
A 1 220 THR 220 220 220 THR THR A . n 
A 1 221 VAL 221 221 221 VAL VAL A . n 
A 1 222 GLN 222 222 222 GLN GLN A . n 
A 1 223 PRO 223 223 223 PRO PRO A . n 
A 1 224 VAL 224 224 224 VAL VAL A . n 
A 1 225 ARG 225 225 225 ARG ARG A . n 
A 1 226 GLU 226 226 226 GLU GLU A . n 
A 1 227 LYS 227 227 227 LYS LYS A . n 
A 1 228 THR 228 228 228 THR THR A . n 
A 1 229 GLY 229 229 229 GLY GLY A . n 
A 1 230 GLY 230 230 230 GLY GLY A . n 
A 1 231 SER 231 231 231 SER SER A . n 
A 1 232 THR 232 232 232 THR THR A . n 
A 1 233 PHE 233 233 233 PHE PHE A . n 
A 1 234 LYS 234 234 234 LYS LYS A . n 
A 1 235 ASN 235 235 235 ASN ASN A . n 
A 1 236 PRO 236 236 236 PRO PRO A . n 
A 1 237 GLU 237 237 237 GLU GLU A . n 
A 1 238 GLY 238 238 238 GLY GLY A . n 
A 1 239 THR 239 239 239 THR THR A . n 
A 1 240 SER 240 240 240 SER SER A . n 
A 1 241 ALA 241 241 241 ALA ALA A . n 
A 1 242 TRP 242 242 242 TRP TRP A . n 
A 1 243 LYS 243 243 243 LYS LYS A . n 
A 1 244 GLU 244 244 244 GLU GLU A . n 
A 1 245 ILE 245 245 245 ILE ILE A . n 
A 1 246 ASP 246 246 246 ASP ASP A . n 
A 1 247 LYS 247 247 247 LYS LYS A . n 
A 1 248 ALA 248 248 248 ALA ALA A . n 
A 1 249 GLY 249 249 249 GLY GLY A . n 
A 1 250 CYS 250 250 250 CYS CYS A . n 
A 1 251 ARG 251 251 251 ARG ARG A . n 
A 1 252 GLY 252 252 252 GLY GLY A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 ARG 254 254 254 ARG ARG A . n 
A 1 255 VAL 255 255 255 VAL VAL A . n 
A 1 256 GLY 256 256 256 GLY GLY A . n 
A 1 257 GLY 257 257 257 GLY GLY A . n 
A 1 258 ALA 258 258 258 ALA ALA A . n 
A 1 259 GLN 259 259 259 GLN GLN A . n 
A 1 260 MET 260 260 260 MET MET A . n 
A 1 261 SER 261 261 261 SER SER A . n 
A 1 262 GLU 262 262 262 GLU GLU A . n 
A 1 263 MET 263 263 263 MET MET A . n 
A 1 264 HIS 264 264 264 HIS HIS A . n 
A 1 265 CYS 265 265 265 CYS CYS A . n 
A 1 266 ASN 266 266 266 ASN ASN A . n 
A 1 267 PHE 267 267 267 PHE PHE A . n 
A 1 268 MET 268 268 268 MET MET A . n 
A 1 269 ILE 269 269 269 ILE ILE A . n 
A 1 270 ASN 270 270 270 ASN ASN A . n 
A 1 271 THR 271 271 271 THR THR A . n 
A 1 272 GLY 272 272 272 GLY GLY A . n 
A 1 273 ASN 273 273 273 ASN ASN A . n 
A 1 274 ALA 274 274 274 ALA ALA A . n 
A 1 275 THR 275 275 275 THR THR A . n 
A 1 276 GLY 276 276 276 GLY GLY A . n 
A 1 277 HIS 277 277 277 HIS HIS A . n 
A 1 278 ASP 278 278 278 ASP ASP A . n 
A 1 279 LEU 279 279 279 LEU LEU A . n 
A 1 280 GLU 280 280 280 GLU GLU A . n 
A 1 281 THR 281 281 281 THR THR A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 GLY 283 283 283 GLY GLY A . n 
A 1 284 GLU 284 284 284 GLU GLU A . n 
A 1 285 THR 285 285 285 THR THR A . n 
A 1 286 VAL 286 286 286 VAL VAL A . n 
A 1 287 ARG 287 287 287 ARG ARG A . n 
A 1 288 ALA 288 288 288 ALA ALA A . n 
A 1 289 ARG 289 289 289 ARG ARG A . n 
A 1 290 VAL 290 290 290 VAL VAL A . n 
A 1 291 PHE 291 291 291 PHE PHE A . n 
A 1 292 GLU 292 292 292 GLU GLU A . n 
A 1 293 ASN 293 293 293 ASN ASN A . n 
A 1 294 SER 294 294 294 SER SER A . n 
A 1 295 GLY 295 295 295 GLY GLY A . n 
A 1 296 ILE 296 296 296 ILE ILE A . n 
A 1 297 ARG 297 297 297 ARG ARG A . n 
A 1 298 LEU 298 298 298 LEU LEU A . n 
A 1 299 HIS 299 299 299 HIS HIS A . n 
A 1 300 TRP 300 300 300 TRP TRP A . n 
A 1 301 GLU 301 301 301 GLU GLU A . n 
A 1 302 ILE 302 302 302 ILE ILE A . n 
A 1 303 LYS 303 303 303 LYS LYS A . n 
A 1 304 ARG 304 304 304 ARG ARG A . n 
A 1 305 LEU 305 305 305 LEU LEU A . n 
A 1 306 GLY 306 306 306 GLY GLY A . n 
A 1 307 LEU 307 307 307 LEU LEU A . n 
A 1 308 PHE 308 308 308 PHE PHE A . n 
A 1 309 ARG 309 309 309 ARG ARG A . n 
A 1 310 GLU 310 310 310 GLU GLU A . n 
A 1 311 GLY 311 311 311 GLY GLY A . n 
A 1 312 GLU 312 312 312 GLU GLU A . n 
A 1 313 GLN 313 313 313 GLN GLN A . n 
A 1 314 ILE 314 314 314 ILE ILE A . n 
A 1 315 GLU 315 315 315 GLU GLU A . n 
A 1 316 GLU 316 316 316 GLU GLU A . n 
A 1 317 PHE 317 317 317 PHE PHE A . n 
A 1 318 LEU 318 318 318 LEU LEU A . n 
A 1 319 GLY 319 319 319 GLY GLY A . n 
A 1 320 LYS 320 320 320 LYS LYS A . n 
A 1 321 ILE 321 321 321 ILE ILE A . n 
A 1 322 VAL 322 322 322 VAL VAL A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 EPU ? ? EPU ? ? 'SUBJECT OF INVESTIGATION' ? 
2 FAD ? ? FAD ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 SO4 1  401 403 SO4 SO4 A . 
C 3 FAD 1  402 401 FAD FAD A . 
D 4 EPU 1  403 402 EPU EPU A . 
E 5 HOH 1  501 38  HOH HOH A . 
E 5 HOH 2  502 86  HOH HOH A . 
E 5 HOH 3  503 14  HOH HOH A . 
E 5 HOH 4  504 5   HOH HOH A . 
E 5 HOH 5  505 40  HOH HOH A . 
E 5 HOH 6  506 91  HOH HOH A . 
E 5 HOH 7  507 49  HOH HOH A . 
E 5 HOH 8  508 54  HOH HOH A . 
E 5 HOH 9  509 52  HOH HOH A . 
E 5 HOH 10 510 39  HOH HOH A . 
E 5 HOH 11 511 73  HOH HOH A . 
E 5 HOH 12 512 37  HOH HOH A . 
E 5 HOH 13 513 62  HOH HOH A . 
E 5 HOH 14 514 13  HOH HOH A . 
E 5 HOH 15 515 8   HOH HOH A . 
E 5 HOH 16 516 4   HOH HOH A . 
E 5 HOH 17 517 83  HOH HOH A . 
E 5 HOH 18 518 34  HOH HOH A . 
E 5 HOH 19 519 64  HOH HOH A . 
E 5 HOH 20 520 68  HOH HOH A . 
E 5 HOH 21 521 53  HOH HOH A . 
E 5 HOH 22 522 3   HOH HOH A . 
E 5 HOH 23 523 32  HOH HOH A . 
E 5 HOH 24 524 6   HOH HOH A . 
E 5 HOH 25 525 45  HOH HOH A . 
E 5 HOH 26 526 24  HOH HOH A . 
E 5 HOH 27 527 78  HOH HOH A . 
E 5 HOH 28 528 1   HOH HOH A . 
E 5 HOH 29 529 35  HOH HOH A . 
E 5 HOH 30 530 33  HOH HOH A . 
E 5 HOH 31 531 44  HOH HOH A . 
E 5 HOH 32 532 69  HOH HOH A . 
E 5 HOH 33 533 61  HOH HOH A . 
E 5 HOH 34 534 75  HOH HOH A . 
E 5 HOH 35 535 2   HOH HOH A . 
E 5 HOH 36 536 31  HOH HOH A . 
E 5 HOH 37 537 42  HOH HOH A . 
E 5 HOH 38 538 85  HOH HOH A . 
E 5 HOH 39 539 22  HOH HOH A . 
E 5 HOH 40 540 74  HOH HOH A . 
E 5 HOH 41 541 27  HOH HOH A . 
E 5 HOH 42 542 80  HOH HOH A . 
E 5 HOH 43 543 79  HOH HOH A . 
E 5 HOH 44 544 7   HOH HOH A . 
E 5 HOH 45 545 67  HOH HOH A . 
E 5 HOH 46 546 60  HOH HOH A . 
E 5 HOH 47 547 63  HOH HOH A . 
E 5 HOH 48 548 10  HOH HOH A . 
E 5 HOH 49 549 56  HOH HOH A . 
E 5 HOH 50 550 15  HOH HOH A . 
E 5 HOH 51 551 26  HOH HOH A . 
E 5 HOH 52 552 9   HOH HOH A . 
E 5 HOH 53 553 88  HOH HOH A . 
E 5 HOH 54 554 18  HOH HOH A . 
E 5 HOH 55 555 65  HOH HOH A . 
E 5 HOH 56 556 36  HOH HOH A . 
E 5 HOH 57 557 29  HOH HOH A . 
E 5 HOH 58 558 57  HOH HOH A . 
E 5 HOH 59 559 43  HOH HOH A . 
E 5 HOH 60 560 23  HOH HOH A . 
E 5 HOH 61 561 30  HOH HOH A . 
E 5 HOH 62 562 11  HOH HOH A . 
E 5 HOH 63 563 20  HOH HOH A . 
E 5 HOH 64 564 19  HOH HOH A . 
E 5 HOH 65 565 21  HOH HOH A . 
E 5 HOH 66 566 51  HOH HOH A . 
E 5 HOH 67 567 48  HOH HOH A . 
E 5 HOH 68 568 76  HOH HOH A . 
E 5 HOH 69 569 46  HOH HOH A . 
E 5 HOH 70 570 41  HOH HOH A . 
E 5 HOH 71 571 71  HOH HOH A . 
E 5 HOH 72 572 16  HOH HOH A . 
E 5 HOH 73 573 28  HOH HOH A . 
E 5 HOH 74 574 59  HOH HOH A . 
E 5 HOH 75 575 77  HOH HOH A . 
E 5 HOH 76 576 17  HOH HOH A . 
E 5 HOH 77 577 55  HOH HOH A . 
E 5 HOH 78 578 87  HOH HOH A . 
E 5 HOH 79 579 12  HOH HOH A . 
E 5 HOH 80 580 92  HOH HOH A . 
E 5 HOH 81 581 93  HOH HOH A . 
E 5 HOH 82 582 70  HOH HOH A . 
E 5 HOH 83 583 94  HOH HOH A . 
E 5 HOH 84 584 90  HOH HOH A . 
E 5 HOH 85 585 50  HOH HOH A . 
E 5 HOH 86 586 66  HOH HOH A . 
E 5 HOH 87 587 25  HOH HOH A . 
E 5 HOH 88 588 81  HOH HOH A . 
E 5 HOH 89 589 82  HOH HOH A . 
E 5 HOH 90 590 89  HOH HOH A . 
E 5 HOH 91 591 72  HOH HOH A . 
E 5 HOH 92 592 47  HOH HOH A . 
E 5 HOH 93 593 84  HOH HOH A . 
E 5 HOH 94 594 58  HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.20.1_4487: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALA  ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   91.09 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DTK 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     120.032 
_cell.length_a_esd                 ? 
_cell.length_b                     37.533 
_cell.length_b_esd                 ? 
_cell.length_c                     77.902 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9DTK 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_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                   9DTK 
_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             2.41 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.01 
_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    '16% PEG4000, 0.200 M lithium sulfate, 0.100 M Tris-HCl, pH 8.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291.15 
# 
_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 PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-05-25 
_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   0.979185 
_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                        'ALBA BEAMLINE XALOC' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979185 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   XALOC 
_diffrn_source.pdbx_synchrotron_site       ALBA 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9DTK 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.23 
_reflns.d_resolution_low                               77.89 
_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                                     15551 
_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                           94.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_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                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.075 
_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                                    2.23 
_reflns_shell.d_res_low                                     2.35 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           3.6 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1638 
_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                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          94.4 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.264 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9DTK 
_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                            2.27 
_refine.ls_d_res_low                             60.01 
_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                     15534 
_refine.ls_number_reflns_R_free                  825 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    93.93 
_refine.ls_percent_reflns_R_free                 5.31 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2473 
_refine.ls_R_factor_R_free                       0.2472 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2166 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          34.75 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       TWIN_LSQ_F 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 34.20 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.27 
_refine_hist.d_res_low                        60.01 
_refine_hist.number_atoms_solvent             94 
_refine_hist.number_atoms_total               2648 
_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        2549 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         5 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.006  ? ?   ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.768  ? ?   ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 11.129 ? 374 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.043  ? 378 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009  ? 457 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.27 2.41 . . 111 2502 91.00 . . . . .      . . . . . . . . . . . 0.3453 
'X-RAY DIFFRACTION' 2.41 2.59 . . 137 2519 93.00 . . . . 0.3398 . . . . . . . . . . . 0.3473 
'X-RAY DIFFRACTION' 2.59 2.85 . . 123 2158 79.00 . . . . 0.3067 . . . . . . . . . . . 0.3410 
'X-RAY DIFFRACTION' 2.85 3.27 . . 129 2522 93.00 . . . . 0.2711 . . . . . . . . . . . 0.3184 
'X-RAY DIFFRACTION' 3.27 4.12 . . 149 2527 91.00 . . . . 0.2178 . . . . . . . . . . . 0.2581 
'X-RAY DIFFRACTION' 4.12 5    . . 130 2527 89.00 . . . . 0.1854 . . . . . . . . . . . 0.2320 
# 
_struct.entry_id                     9DTK 
_struct.title                        'Crystal structure of UDP-N-acetylenolpyruvoylglucosamine reductase (MurB) from Brucella ovis' 
_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        9DTK 
_struct_keywords.text            
'flavoenzyme, peptidoglycan synthesis, cell wall, NADPH oxidation, Brucella ovis, OXIDOREDUCTASE, FAD' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    MURB_BRUO2 
_struct_ref.pdbx_db_accession          A5VRH5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MMESGEALLKKLDGRLSGLRGRLTPDTGMDKITWFRAGGPAQVLFQPSDEEDLSAFLKAVPEEIPLLVVGIGSNLLVRDG
GVPGFVVRLSAKGFGEVEQVCDTQLRAGAAAPDKRVAAAALEAGLAGFHFYHGIPGGIGGALRMNAGANGVETRERVVEV
RALDRKGEVHVLSNADMGYAYRHSSASPDLIFTSVLFEGVPGERDDIRRAMDEVQHHRETVQPVREKTGGSTFKNPEGTS
AWKEIDKAGCRGLRVGGAQMSEMHCNFMINTGNATGHDLETLGETVRARVFENSGIRLHWEIKRLGLFREGEQIEEFLGK
IV
;
_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              9DTK 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 322 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A5VRH5 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  322 
_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       322 
# 
_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)' 2690  ? 
1 MORE         -22   ? 
1 'SSA (A^2)'  14060 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_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 SER A 4   ? LEU A 12  ? SER A 4   LEU A 12  1 ? 9  
HELX_P HELX_P2  AA2 ASP A 30  ? ILE A 32  ? ASP A 30  ILE A 32  5 ? 3  
HELX_P HELX_P3  AA3 ASP A 49  ? VAL A 60  ? ASP A 49  VAL A 60  1 ? 12 
HELX_P HELX_P4  AA4 SER A 90  ? GLY A 95  ? SER A 90  GLY A 95  1 ? 6  
HELX_P HELX_P5  AA5 PRO A 112 ? GLU A 122 ? PRO A 112 GLU A 122 1 ? 11 
HELX_P HELX_P6  AA6 PHE A 128 ? GLY A 133 ? PHE A 128 GLY A 133 5 ? 6  
HELX_P HELX_P7  AA7 GLY A 137 ? ASN A 145 ? GLY A 137 ASN A 145 1 ? 9  
HELX_P HELX_P8  AA8 GLU A 203 ? GLN A 222 ? GLU A 203 GLN A 222 1 ? 20 
HELX_P HELX_P9  AA9 SER A 240 ? ALA A 248 ? SER A 240 ALA A 248 1 ? 9  
HELX_P HELX_P10 AB1 THR A 275 ? GLY A 295 ? THR A 275 GLY A 295 1 ? 21 
HELX_P HELX_P11 AB2 GLU A 315 ? LYS A 320 ? GLU A 315 LYS A 320 5 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 2 ? 
AA3 ? 5 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 2 ? 
AA7 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ARG A 22  ? GLY A 28  ? ARG A 22  GLY A 28  
AA1 2 PRO A 40  ? GLN A 46  ? PRO A 40  GLN A 46  
AA1 3 VAL A 82  ? VAL A 87  ? VAL A 82  VAL A 87  
AA1 4 LEU A 66  ? VAL A 68  ? LEU A 66  VAL A 68  
AA2 1 LEU A 75  ? VAL A 77  ? LEU A 75  VAL A 77  
AA2 2 LYS A 303 ? LEU A 305 ? LYS A 303 LEU A 305 
AA3 1 VAL A 97  ? GLN A 99  ? VAL A 97  GLN A 99  
AA3 2 GLN A 104 ? GLY A 108 ? GLN A 104 GLY A 108 
AA3 3 ILE A 191 ? GLU A 198 ? ILE A 191 GLU A 198 
AA3 4 VAL A 157 ? LEU A 163 ? VAL A 157 LEU A 163 
AA3 5 VAL A 169 ? SER A 173 ? VAL A 169 SER A 173 
AA4 1 LEU A 125 ? ALA A 126 ? LEU A 125 ALA A 126 
AA4 2 VAL A 200 ? PRO A 201 ? VAL A 200 PRO A 201 
AA5 1 GLY A 147 ? ALA A 148 ? GLY A 147 ALA A 148 
AA5 2 VAL A 151 ? GLU A 152 ? VAL A 151 GLU A 152 
AA6 1 TYR A 179 ? ALA A 180 ? TYR A 179 ALA A 180 
AA6 2 HIS A 183 ? SER A 184 ? HIS A 183 SER A 184 
AA7 1 ARG A 254 ? VAL A 255 ? ARG A 254 VAL A 255 
AA7 2 ALA A 258 ? MET A 260 ? ALA A 258 MET A 260 
AA7 3 MET A 268 ? ASN A 270 ? MET A 268 ASN A 270 
# 
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 THR A 24  ? N THR A 24  O LEU A 44  ? O LEU A 44  
AA1 2 3 N PHE A 45  ? N PHE A 45  O VAL A 86  ? O VAL A 86  
AA1 3 4 O VAL A 87  ? O VAL A 87  N LEU A 67  ? N LEU A 67  
AA2 1 2 N LEU A 76  ? N LEU A 76  O LYS A 303 ? O LYS A 303 
AA3 1 2 N GLU A 98  ? N GLU A 98  O ARG A 106 ? O ARG A 106 
AA3 2 3 N LEU A 105 ? N LEU A 105 O PHE A 197 ? O PHE A 197 
AA3 3 4 O LEU A 196 ? O LEU A 196 N VAL A 158 ? N VAL A 158 
AA3 4 5 N VAL A 160 ? N VAL A 160 O LEU A 172 ? O LEU A 172 
AA4 1 2 N ALA A 126 ? N ALA A 126 O VAL A 200 ? O VAL A 200 
AA5 1 2 N ALA A 148 ? N ALA A 148 O VAL A 151 ? O VAL A 151 
AA6 1 2 N ALA A 180 ? N ALA A 180 O HIS A 183 ? O HIS A 183 
AA7 1 2 N VAL A 255 ? N VAL A 255 O ALA A 258 ? O ALA A 258 
AA7 2 3 N GLN A 259 ? N GLN A 259 O ILE A 269 ? O ILE A 269 
# 
_pdbx_entry_details.entry_id                   9DTK 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A HOH 539 ? ? O A HOH 592 ? ? 2.00 
2 1 O   A HOH 570 ? ? O A HOH 589 ? ? 2.05 
3 1 O   A HOH 544 ? ? O A HOH 578 ? ? 2.06 
4 1 O   A HOH 527 ? ? O A HOH 558 ? ? 2.12 
5 1 OG  A SER 231 ? ? O A HOH 501 ? ? 2.17 
6 1 O   A HOH 559 ? ? O A HOH 580 ? ? 2.19 
7 1 O2D A EPU 403 ? ? O A HOH 502 ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     513 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     557 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   1_565 
_pdbx_validate_symm_contact.dist              2.13 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CD 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            LYS 
_pdbx_validate_rmsd_bond.auth_seq_id_1             243 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            CE 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            LYS 
_pdbx_validate_rmsd_bond.auth_seq_id_2             243 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.297 
_pdbx_validate_rmsd_bond.bond_target_value         1.508 
_pdbx_validate_rmsd_bond.bond_deviation            -0.211 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.025 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 MET A 2   ? ? 70.24   119.41  
2 1 LEU A 12  ? ? -97.21  58.23   
3 1 CYS A 101 ? ? -140.82 -124.86 
4 1 ASN A 145 ? ? 36.92   53.96   
5 1 ASN A 149 ? ? 58.47   18.36   
6 1 VAL A 158 ? ? -90.99  -75.34  
7 1 THR A 239 ? ? -161.69 -168.70 
8 1 SER A 294 ? ? -146.19 -8.20   
# 
_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     510 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   E 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N N N 1   
ALA CA     C N S 2   
ALA C      C N N 3   
ALA O      O N N 4   
ALA CB     C N N 5   
ALA OXT    O N N 6   
ALA H      H N N 7   
ALA H2     H N N 8   
ALA HA     H N N 9   
ALA HB1    H N N 10  
ALA HB2    H N N 11  
ALA HB3    H N N 12  
ALA HXT    H N N 13  
ARG N      N N N 14  
ARG CA     C N S 15  
ARG C      C N N 16  
ARG O      O N N 17  
ARG CB     C N N 18  
ARG CG     C N N 19  
ARG CD     C N N 20  
ARG NE     N N N 21  
ARG CZ     C N N 22  
ARG NH1    N N N 23  
ARG NH2    N N N 24  
ARG OXT    O N N 25  
ARG H      H N N 26  
ARG H2     H N N 27  
ARG HA     H N N 28  
ARG HB2    H N N 29  
ARG HB3    H N N 30  
ARG HG2    H N N 31  
ARG HG3    H N N 32  
ARG HD2    H N N 33  
ARG HD3    H N N 34  
ARG HE     H N N 35  
ARG HH11   H N N 36  
ARG HH12   H N N 37  
ARG HH21   H N N 38  
ARG HH22   H N N 39  
ARG HXT    H N N 40  
ASN N      N N N 41  
ASN CA     C N S 42  
ASN C      C N N 43  
ASN O      O N N 44  
ASN CB     C N N 45  
ASN CG     C N N 46  
ASN OD1    O N N 47  
ASN ND2    N N N 48  
ASN OXT    O N N 49  
ASN H      H N N 50  
ASN H2     H N N 51  
ASN HA     H N N 52  
ASN HB2    H N N 53  
ASN HB3    H N N 54  
ASN HD21   H N N 55  
ASN HD22   H N N 56  
ASN HXT    H N N 57  
ASP N      N N N 58  
ASP CA     C N S 59  
ASP C      C N N 60  
ASP O      O N N 61  
ASP CB     C N N 62  
ASP CG     C N N 63  
ASP OD1    O N N 64  
ASP OD2    O N N 65  
ASP OXT    O N N 66  
ASP H      H N N 67  
ASP H2     H N N 68  
ASP HA     H N N 69  
ASP HB2    H N N 70  
ASP HB3    H N N 71  
ASP HD2    H N N 72  
ASP HXT    H N N 73  
CYS N      N N N 74  
CYS CA     C N R 75  
CYS C      C N N 76  
CYS O      O N N 77  
CYS CB     C N N 78  
CYS SG     S N N 79  
CYS OXT    O N N 80  
CYS H      H N N 81  
CYS H2     H N N 82  
CYS HA     H N N 83  
CYS HB2    H N N 84  
CYS HB3    H N N 85  
CYS HG     H N N 86  
CYS HXT    H N N 87  
EPU N1U    N N N 88  
EPU C2U    C N N 89  
EPU N3U    N N N 90  
EPU C4U    C N N 91  
EPU C5U    C N N 92  
EPU C6U    C N N 93  
EPU O2U    O N N 94  
EPU O4U    O N N 95  
EPU C1D    C N R 96  
EPU C2D    C N R 97  
EPU O2D    O N N 98  
EPU C3D    C N S 99  
EPU C4D    C N R 100 
EPU O4D    O N N 101 
EPU O3D    O N N 102 
EPU C5D    C N N 103 
EPU O5D    O N N 104 
EPU PA     P N R 105 
EPU O1A    O N N 106 
EPU O2A    O N N 107 
EPU O3A    O N N 108 
EPU PB     P N R 109 
EPU O1B    O N N 110 
EPU O2B    O N N 111 
EPU C1     C N R 112 
EPU C2     C N R 113 
EPU C3     C N R 114 
EPU C4     C N S 115 
EPU C5     C N R 116 
EPU C6     C N N 117 
EPU C7     C N N 118 
EPU C8     C N N 119 
EPU N2     N N N 120 
EPU O1     O N N 121 
EPU O3     O N N 122 
EPU O4     O N N 123 
EPU O5     O N N 124 
EPU O6     O N N 125 
EPU O7     O N N 126 
EPU C1E    C N N 127 
EPU O1E    O N N 128 
EPU O2E    O N N 129 
EPU C2E    C N N 130 
EPU C3E    C N N 131 
EPU HN3U   H N N 132 
EPU H5U    H N N 133 
EPU H6U    H N N 134 
EPU H1D    H N N 135 
EPU H2D    H N N 136 
EPU HO2U   H N N 137 
EPU H3D    H N N 138 
EPU H4D    H N N 139 
EPU HO3U   H N N 140 
EPU "H5'1" H N N 141 
EPU "H5'2" H N N 142 
EPU HOA2   H N N 143 
EPU HOB2   H N N 144 
EPU H1     H N N 145 
EPU H2     H N N 146 
EPU H3     H N N 147 
EPU H4     H N N 148 
EPU H5     H N N 149 
EPU H61    H N N 150 
EPU H62    H N N 151 
EPU H81    H N N 152 
EPU H82    H N N 153 
EPU H83    H N N 154 
EPU HN2    H N N 155 
EPU HO4    H N N 156 
EPU HO6    H N N 157 
EPU HO2E   H N N 158 
EPU HE31   H N N 159 
EPU HE32   H N N 160 
FAD PA     P N R 161 
FAD O1A    O N N 162 
FAD O2A    O N N 163 
FAD O5B    O N N 164 
FAD C5B    C N N 165 
FAD C4B    C N R 166 
FAD O4B    O N N 167 
FAD C3B    C N S 168 
FAD O3B    O N N 169 
FAD C2B    C N R 170 
FAD O2B    O N N 171 
FAD C1B    C N R 172 
FAD N9A    N Y N 173 
FAD C8A    C Y N 174 
FAD N7A    N Y N 175 
FAD C5A    C Y N 176 
FAD C6A    C Y N 177 
FAD N6A    N N N 178 
FAD N1A    N Y N 179 
FAD C2A    C Y N 180 
FAD N3A    N Y N 181 
FAD C4A    C Y N 182 
FAD N1     N N N 183 
FAD C2     C N N 184 
FAD O2     O N N 185 
FAD N3     N N N 186 
FAD C4     C N N 187 
FAD O4     O N N 188 
FAD C4X    C N N 189 
FAD N5     N N N 190 
FAD C5X    C Y N 191 
FAD C6     C Y N 192 
FAD C7     C Y N 193 
FAD C7M    C N N 194 
FAD C8     C Y N 195 
FAD C8M    C N N 196 
FAD C9     C Y N 197 
FAD C9A    C Y N 198 
FAD N10    N N N 199 
FAD C10    C N N 200 
FAD "C1'"  C N N 201 
FAD "C2'"  C N S 202 
FAD "O2'"  O N N 203 
FAD "C3'"  C N S 204 
FAD "O3'"  O N N 205 
FAD "C4'"  C N R 206 
FAD "O4'"  O N N 207 
FAD "C5'"  C N N 208 
FAD "O5'"  O N N 209 
FAD P      P N R 210 
FAD O1P    O N N 211 
FAD O2P    O N N 212 
FAD O3P    O N N 213 
FAD HOA2   H N N 214 
FAD H51A   H N N 215 
FAD H52A   H N N 216 
FAD H4B    H N N 217 
FAD H3B    H N N 218 
FAD HO3A   H N N 219 
FAD H2B    H N N 220 
FAD HO2A   H N N 221 
FAD H1B    H N N 222 
FAD H8A    H N N 223 
FAD H61A   H N N 224 
FAD H62A   H N N 225 
FAD H2A    H N N 226 
FAD HN3    H N N 227 
FAD H6     H N N 228 
FAD HM71   H N N 229 
FAD HM72   H N N 230 
FAD HM73   H N N 231 
FAD HM81   H N N 232 
FAD HM82   H N N 233 
FAD HM83   H N N 234 
FAD H9     H N N 235 
FAD "H1'1" H N N 236 
FAD "H1'2" H N N 237 
FAD "H2'"  H N N 238 
FAD "HO2'" H N N 239 
FAD "H3'"  H N N 240 
FAD "HO3'" H N N 241 
FAD "H4'"  H N N 242 
FAD "HO4'" H N N 243 
FAD "H5'1" H N N 244 
FAD "H5'2" H N N 245 
FAD HOP2   H N N 246 
GLN N      N N N 247 
GLN CA     C N S 248 
GLN C      C N N 249 
GLN O      O N N 250 
GLN CB     C N N 251 
GLN CG     C N N 252 
GLN CD     C N N 253 
GLN OE1    O N N 254 
GLN NE2    N N N 255 
GLN OXT    O N N 256 
GLN H      H N N 257 
GLN H2     H N N 258 
GLN HA     H N N 259 
GLN HB2    H N N 260 
GLN HB3    H N N 261 
GLN HG2    H N N 262 
GLN HG3    H N N 263 
GLN HE21   H N N 264 
GLN HE22   H N N 265 
GLN HXT    H N N 266 
GLU N      N N N 267 
GLU CA     C N S 268 
GLU C      C N N 269 
GLU O      O N N 270 
GLU CB     C N N 271 
GLU CG     C N N 272 
GLU CD     C N N 273 
GLU OE1    O N N 274 
GLU OE2    O N N 275 
GLU OXT    O N N 276 
GLU H      H N N 277 
GLU H2     H N N 278 
GLU HA     H N N 279 
GLU HB2    H N N 280 
GLU HB3    H N N 281 
GLU HG2    H N N 282 
GLU HG3    H N N 283 
GLU HE2    H N N 284 
GLU HXT    H N N 285 
GLY N      N N N 286 
GLY CA     C N N 287 
GLY C      C N N 288 
GLY O      O N N 289 
GLY OXT    O N N 290 
GLY H      H N N 291 
GLY H2     H N N 292 
GLY HA2    H N N 293 
GLY HA3    H N N 294 
GLY HXT    H N N 295 
HIS N      N N N 296 
HIS CA     C N S 297 
HIS C      C N N 298 
HIS O      O N N 299 
HIS CB     C N N 300 
HIS CG     C Y N 301 
HIS ND1    N Y N 302 
HIS CD2    C Y N 303 
HIS CE1    C Y N 304 
HIS NE2    N Y N 305 
HIS OXT    O N N 306 
HIS H      H N N 307 
HIS H2     H N N 308 
HIS HA     H N N 309 
HIS HB2    H N N 310 
HIS HB3    H N N 311 
HIS HD1    H N N 312 
HIS HD2    H N N 313 
HIS HE1    H N N 314 
HIS HE2    H N N 315 
HIS HXT    H N N 316 
HOH O      O N N 317 
HOH H1     H N N 318 
HOH H2     H N N 319 
ILE N      N N N 320 
ILE CA     C N S 321 
ILE C      C N N 322 
ILE O      O N N 323 
ILE CB     C N S 324 
ILE CG1    C N N 325 
ILE CG2    C N N 326 
ILE CD1    C N N 327 
ILE OXT    O N N 328 
ILE H      H N N 329 
ILE H2     H N N 330 
ILE HA     H N N 331 
ILE HB     H N N 332 
ILE HG12   H N N 333 
ILE HG13   H N N 334 
ILE HG21   H N N 335 
ILE HG22   H N N 336 
ILE HG23   H N N 337 
ILE HD11   H N N 338 
ILE HD12   H N N 339 
ILE HD13   H N N 340 
ILE HXT    H N N 341 
LEU N      N N N 342 
LEU CA     C N S 343 
LEU C      C N N 344 
LEU O      O N N 345 
LEU CB     C N N 346 
LEU CG     C N N 347 
LEU CD1    C N N 348 
LEU CD2    C N N 349 
LEU OXT    O N N 350 
LEU H      H N N 351 
LEU H2     H N N 352 
LEU HA     H N N 353 
LEU HB2    H N N 354 
LEU HB3    H N N 355 
LEU HG     H N N 356 
LEU HD11   H N N 357 
LEU HD12   H N N 358 
LEU HD13   H N N 359 
LEU HD21   H N N 360 
LEU HD22   H N N 361 
LEU HD23   H N N 362 
LEU HXT    H N N 363 
LYS N      N N N 364 
LYS CA     C N S 365 
LYS C      C N N 366 
LYS O      O N N 367 
LYS CB     C N N 368 
LYS CG     C N N 369 
LYS CD     C N N 370 
LYS CE     C N N 371 
LYS NZ     N N N 372 
LYS OXT    O N N 373 
LYS H      H N N 374 
LYS H2     H N N 375 
LYS HA     H N N 376 
LYS HB2    H N N 377 
LYS HB3    H N N 378 
LYS HG2    H N N 379 
LYS HG3    H N N 380 
LYS HD2    H N N 381 
LYS HD3    H N N 382 
LYS HE2    H N N 383 
LYS HE3    H N N 384 
LYS HZ1    H N N 385 
LYS HZ2    H N N 386 
LYS HZ3    H N N 387 
LYS HXT    H N N 388 
MET N      N N N 389 
MET CA     C N S 390 
MET C      C N N 391 
MET O      O N N 392 
MET CB     C N N 393 
MET CG     C N N 394 
MET SD     S N N 395 
MET CE     C N N 396 
MET OXT    O N N 397 
MET H      H N N 398 
MET H2     H N N 399 
MET HA     H N N 400 
MET HB2    H N N 401 
MET HB3    H N N 402 
MET HG2    H N N 403 
MET HG3    H N N 404 
MET HE1    H N N 405 
MET HE2    H N N 406 
MET HE3    H N N 407 
MET HXT    H N N 408 
PHE N      N N N 409 
PHE CA     C N S 410 
PHE C      C N N 411 
PHE O      O N N 412 
PHE CB     C N N 413 
PHE CG     C Y N 414 
PHE CD1    C Y N 415 
PHE CD2    C Y N 416 
PHE CE1    C Y N 417 
PHE CE2    C Y N 418 
PHE CZ     C Y N 419 
PHE OXT    O N N 420 
PHE H      H N N 421 
PHE H2     H N N 422 
PHE HA     H N N 423 
PHE HB2    H N N 424 
PHE HB3    H N N 425 
PHE HD1    H N N 426 
PHE HD2    H N N 427 
PHE HE1    H N N 428 
PHE HE2    H N N 429 
PHE HZ     H N N 430 
PHE HXT    H N N 431 
PRO N      N N N 432 
PRO CA     C N S 433 
PRO C      C N N 434 
PRO O      O N N 435 
PRO CB     C N N 436 
PRO CG     C N N 437 
PRO CD     C N N 438 
PRO OXT    O N N 439 
PRO H      H N N 440 
PRO HA     H N N 441 
PRO HB2    H N N 442 
PRO HB3    H N N 443 
PRO HG2    H N N 444 
PRO HG3    H N N 445 
PRO HD2    H N N 446 
PRO HD3    H N N 447 
PRO HXT    H N N 448 
SER N      N N N 449 
SER CA     C N S 450 
SER C      C N N 451 
SER O      O N N 452 
SER CB     C N N 453 
SER OG     O N N 454 
SER OXT    O N N 455 
SER H      H N N 456 
SER H2     H N N 457 
SER HA     H N N 458 
SER HB2    H N N 459 
SER HB3    H N N 460 
SER HG     H N N 461 
SER HXT    H N N 462 
SO4 S      S N N 463 
SO4 O1     O N N 464 
SO4 O2     O N N 465 
SO4 O3     O N N 466 
SO4 O4     O N N 467 
THR N      N N N 468 
THR CA     C N S 469 
THR C      C N N 470 
THR O      O N N 471 
THR CB     C N R 472 
THR OG1    O N N 473 
THR CG2    C N N 474 
THR OXT    O N N 475 
THR H      H N N 476 
THR H2     H N N 477 
THR HA     H N N 478 
THR HB     H N N 479 
THR HG1    H N N 480 
THR HG21   H N N 481 
THR HG22   H N N 482 
THR HG23   H N N 483 
THR HXT    H N N 484 
TRP N      N N N 485 
TRP CA     C N S 486 
TRP C      C N N 487 
TRP O      O N N 488 
TRP CB     C N N 489 
TRP CG     C Y N 490 
TRP CD1    C Y N 491 
TRP CD2    C Y N 492 
TRP NE1    N Y N 493 
TRP CE2    C Y N 494 
TRP CE3    C Y N 495 
TRP CZ2    C Y N 496 
TRP CZ3    C Y N 497 
TRP CH2    C Y N 498 
TRP OXT    O N N 499 
TRP H      H N N 500 
TRP H2     H N N 501 
TRP HA     H N N 502 
TRP HB2    H N N 503 
TRP HB3    H N N 504 
TRP HD1    H N N 505 
TRP HE1    H N N 506 
TRP HE3    H N N 507 
TRP HZ2    H N N 508 
TRP HZ3    H N N 509 
TRP HH2    H N N 510 
TRP HXT    H N N 511 
TYR N      N N N 512 
TYR CA     C N S 513 
TYR C      C N N 514 
TYR O      O N N 515 
TYR CB     C N N 516 
TYR CG     C Y N 517 
TYR CD1    C Y N 518 
TYR CD2    C Y N 519 
TYR CE1    C Y N 520 
TYR CE2    C Y N 521 
TYR CZ     C Y N 522 
TYR OH     O N N 523 
TYR OXT    O N N 524 
TYR H      H N N 525 
TYR H2     H N N 526 
TYR HA     H N N 527 
TYR HB2    H N N 528 
TYR HB3    H N N 529 
TYR HD1    H N N 530 
TYR HD2    H N N 531 
TYR HE1    H N N 532 
TYR HE2    H N N 533 
TYR HH     H N N 534 
TYR HXT    H N N 535 
VAL N      N N N 536 
VAL CA     C N S 537 
VAL C      C N N 538 
VAL O      O N N 539 
VAL CB     C N N 540 
VAL CG1    C N N 541 
VAL CG2    C N N 542 
VAL OXT    O N N 543 
VAL H      H N N 544 
VAL H2     H N N 545 
VAL HA     H N N 546 
VAL HB     H N N 547 
VAL HG11   H N N 548 
VAL HG12   H N N 549 
VAL HG13   H N N 550 
VAL HG21   H N N 551 
VAL HG22   H N N 552 
VAL HG23   H N N 553 
VAL HXT    H N N 554 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
EPU N1U   C2U    sing N N 83  
EPU N1U   C6U    sing N N 84  
EPU N1U   C1D    sing N N 85  
EPU C2U   N3U    sing N N 86  
EPU C2U   O2U    doub N N 87  
EPU N3U   C4U    sing N N 88  
EPU N3U   HN3U   sing N N 89  
EPU C4U   C5U    sing N N 90  
EPU C4U   O4U    doub N N 91  
EPU C5U   C6U    doub N N 92  
EPU C5U   H5U    sing N N 93  
EPU C6U   H6U    sing N N 94  
EPU C1D   C2D    sing N N 95  
EPU C1D   O4D    sing N N 96  
EPU C1D   H1D    sing N N 97  
EPU C2D   O2D    sing N N 98  
EPU C2D   C3D    sing N N 99  
EPU C2D   H2D    sing N N 100 
EPU O2D   HO2U   sing N N 101 
EPU C3D   C4D    sing N N 102 
EPU C3D   O3D    sing N N 103 
EPU C3D   H3D    sing N N 104 
EPU C4D   O4D    sing N N 105 
EPU C4D   C5D    sing N N 106 
EPU C4D   H4D    sing N N 107 
EPU O3D   HO3U   sing N N 108 
EPU C5D   O5D    sing N N 109 
EPU C5D   "H5'1" sing N N 110 
EPU C5D   "H5'2" sing N N 111 
EPU O5D   PA     sing N N 112 
EPU PA    O1A    doub N N 113 
EPU PA    O2A    sing N N 114 
EPU PA    O3A    sing N N 115 
EPU O2A   HOA2   sing N N 116 
EPU O3A   PB     sing N N 117 
EPU PB    O1B    doub N N 118 
EPU PB    O2B    sing N N 119 
EPU PB    O1     sing N N 120 
EPU O2B   HOB2   sing N N 121 
EPU C1    C2     sing N N 122 
EPU C1    O1     sing N N 123 
EPU C1    O5     sing N N 124 
EPU C1    H1     sing N N 125 
EPU C2    C3     sing N N 126 
EPU C2    N2     sing N N 127 
EPU C2    H2     sing N N 128 
EPU C3    C4     sing N N 129 
EPU C3    O3     sing N N 130 
EPU C3    H3     sing N N 131 
EPU C4    C5     sing N N 132 
EPU C4    O4     sing N N 133 
EPU C4    H4     sing N N 134 
EPU C5    C6     sing N N 135 
EPU C5    O5     sing N N 136 
EPU C5    H5     sing N N 137 
EPU C6    O6     sing N N 138 
EPU C6    H61    sing N N 139 
EPU C6    H62    sing N N 140 
EPU C7    C8     sing N N 141 
EPU C7    N2     sing N N 142 
EPU C7    O7     doub N N 143 
EPU C8    H81    sing N N 144 
EPU C8    H82    sing N N 145 
EPU C8    H83    sing N N 146 
EPU N2    HN2    sing N N 147 
EPU O3    C2E    sing N N 148 
EPU O4    HO4    sing N N 149 
EPU O6    HO6    sing N N 150 
EPU C1E   O1E    doub N N 151 
EPU C1E   O2E    sing N N 152 
EPU C1E   C2E    sing N N 153 
EPU O2E   HO2E   sing N N 154 
EPU C2E   C3E    doub N N 155 
EPU C3E   HE31   sing N N 156 
EPU C3E   HE32   sing N N 157 
FAD PA    O1A    doub N N 158 
FAD PA    O2A    sing N N 159 
FAD PA    O5B    sing N N 160 
FAD PA    O3P    sing N N 161 
FAD O2A   HOA2   sing N N 162 
FAD O5B   C5B    sing N N 163 
FAD C5B   C4B    sing N N 164 
FAD C5B   H51A   sing N N 165 
FAD C5B   H52A   sing N N 166 
FAD C4B   O4B    sing N N 167 
FAD C4B   C3B    sing N N 168 
FAD C4B   H4B    sing N N 169 
FAD O4B   C1B    sing N N 170 
FAD C3B   O3B    sing N N 171 
FAD C3B   C2B    sing N N 172 
FAD C3B   H3B    sing N N 173 
FAD O3B   HO3A   sing N N 174 
FAD C2B   O2B    sing N N 175 
FAD C2B   C1B    sing N N 176 
FAD C2B   H2B    sing N N 177 
FAD O2B   HO2A   sing N N 178 
FAD C1B   N9A    sing N N 179 
FAD C1B   H1B    sing N N 180 
FAD N9A   C8A    sing Y N 181 
FAD N9A   C4A    sing Y N 182 
FAD C8A   N7A    doub Y N 183 
FAD C8A   H8A    sing N N 184 
FAD N7A   C5A    sing Y N 185 
FAD C5A   C6A    sing Y N 186 
FAD C5A   C4A    doub Y N 187 
FAD C6A   N6A    sing N N 188 
FAD C6A   N1A    doub Y N 189 
FAD N6A   H61A   sing N N 190 
FAD N6A   H62A   sing N N 191 
FAD N1A   C2A    sing Y N 192 
FAD C2A   N3A    doub Y N 193 
FAD C2A   H2A    sing N N 194 
FAD N3A   C4A    sing Y N 195 
FAD N1    C2     sing N N 196 
FAD N1    C10    doub N N 197 
FAD C2    O2     doub N N 198 
FAD C2    N3     sing N N 199 
FAD N3    C4     sing N N 200 
FAD N3    HN3    sing N N 201 
FAD C4    O4     doub N N 202 
FAD C4    C4X    sing N N 203 
FAD C4X   N5     doub N N 204 
FAD C4X   C10    sing N N 205 
FAD N5    C5X    sing N N 206 
FAD C5X   C6     doub Y N 207 
FAD C5X   C9A    sing Y N 208 
FAD C6    C7     sing Y N 209 
FAD C6    H6     sing N N 210 
FAD C7    C7M    sing N N 211 
FAD C7    C8     doub Y N 212 
FAD C7M   HM71   sing N N 213 
FAD C7M   HM72   sing N N 214 
FAD C7M   HM73   sing N N 215 
FAD C8    C8M    sing N N 216 
FAD C8    C9     sing Y N 217 
FAD C8M   HM81   sing N N 218 
FAD C8M   HM82   sing N N 219 
FAD C8M   HM83   sing N N 220 
FAD C9    C9A    doub Y N 221 
FAD C9    H9     sing N N 222 
FAD C9A   N10    sing N N 223 
FAD N10   C10    sing N N 224 
FAD N10   "C1'"  sing N N 225 
FAD "C1'" "C2'"  sing N N 226 
FAD "C1'" "H1'1" sing N N 227 
FAD "C1'" "H1'2" sing N N 228 
FAD "C2'" "O2'"  sing N N 229 
FAD "C2'" "C3'"  sing N N 230 
FAD "C2'" "H2'"  sing N N 231 
FAD "O2'" "HO2'" sing N N 232 
FAD "C3'" "O3'"  sing N N 233 
FAD "C3'" "C4'"  sing N N 234 
FAD "C3'" "H3'"  sing N N 235 
FAD "O3'" "HO3'" sing N N 236 
FAD "C4'" "O4'"  sing N N 237 
FAD "C4'" "C5'"  sing N N 238 
FAD "C4'" "H4'"  sing N N 239 
FAD "O4'" "HO4'" sing N N 240 
FAD "C5'" "O5'"  sing N N 241 
FAD "C5'" "H5'1" sing N N 242 
FAD "C5'" "H5'2" sing N N 243 
FAD "O5'" P      sing N N 244 
FAD P     O1P    doub N N 245 
FAD P     O2P    sing N N 246 
FAD P     O3P    sing N N 247 
FAD O2P   HOP2   sing N N 248 
GLN N     CA     sing N N 249 
GLN N     H      sing N N 250 
GLN N     H2     sing N N 251 
GLN CA    C      sing N N 252 
GLN CA    CB     sing N N 253 
GLN CA    HA     sing N N 254 
GLN C     O      doub N N 255 
GLN C     OXT    sing N N 256 
GLN CB    CG     sing N N 257 
GLN CB    HB2    sing N N 258 
GLN CB    HB3    sing N N 259 
GLN CG    CD     sing N N 260 
GLN CG    HG2    sing N N 261 
GLN CG    HG3    sing N N 262 
GLN CD    OE1    doub N N 263 
GLN CD    NE2    sing N N 264 
GLN NE2   HE21   sing N N 265 
GLN NE2   HE22   sing N N 266 
GLN OXT   HXT    sing N N 267 
GLU N     CA     sing N N 268 
GLU N     H      sing N N 269 
GLU N     H2     sing N N 270 
GLU CA    C      sing N N 271 
GLU CA    CB     sing N N 272 
GLU CA    HA     sing N N 273 
GLU C     O      doub N N 274 
GLU C     OXT    sing N N 275 
GLU CB    CG     sing N N 276 
GLU CB    HB2    sing N N 277 
GLU CB    HB3    sing N N 278 
GLU CG    CD     sing N N 279 
GLU CG    HG2    sing N N 280 
GLU CG    HG3    sing N N 281 
GLU CD    OE1    doub N N 282 
GLU CD    OE2    sing N N 283 
GLU OE2   HE2    sing N N 284 
GLU OXT   HXT    sing N N 285 
GLY N     CA     sing N N 286 
GLY N     H      sing N N 287 
GLY N     H2     sing N N 288 
GLY CA    C      sing N N 289 
GLY CA    HA2    sing N N 290 
GLY CA    HA3    sing N N 291 
GLY C     O      doub N N 292 
GLY C     OXT    sing N N 293 
GLY OXT   HXT    sing N N 294 
HIS N     CA     sing N N 295 
HIS N     H      sing N N 296 
HIS N     H2     sing N N 297 
HIS CA    C      sing N N 298 
HIS CA    CB     sing N N 299 
HIS CA    HA     sing N N 300 
HIS C     O      doub N N 301 
HIS C     OXT    sing N N 302 
HIS CB    CG     sing N N 303 
HIS CB    HB2    sing N N 304 
HIS CB    HB3    sing N N 305 
HIS CG    ND1    sing Y N 306 
HIS CG    CD2    doub Y N 307 
HIS ND1   CE1    doub Y N 308 
HIS ND1   HD1    sing N N 309 
HIS CD2   NE2    sing Y N 310 
HIS CD2   HD2    sing N N 311 
HIS CE1   NE2    sing Y N 312 
HIS CE1   HE1    sing N N 313 
HIS NE2   HE2    sing N N 314 
HIS OXT   HXT    sing N N 315 
HOH O     H1     sing N N 316 
HOH O     H2     sing N N 317 
ILE N     CA     sing N N 318 
ILE N     H      sing N N 319 
ILE N     H2     sing N N 320 
ILE CA    C      sing N N 321 
ILE CA    CB     sing N N 322 
ILE CA    HA     sing N N 323 
ILE C     O      doub N N 324 
ILE C     OXT    sing N N 325 
ILE CB    CG1    sing N N 326 
ILE CB    CG2    sing N N 327 
ILE CB    HB     sing N N 328 
ILE CG1   CD1    sing N N 329 
ILE CG1   HG12   sing N N 330 
ILE CG1   HG13   sing N N 331 
ILE CG2   HG21   sing N N 332 
ILE CG2   HG22   sing N N 333 
ILE CG2   HG23   sing N N 334 
ILE CD1   HD11   sing N N 335 
ILE CD1   HD12   sing N N 336 
ILE CD1   HD13   sing N N 337 
ILE OXT   HXT    sing N N 338 
LEU N     CA     sing N N 339 
LEU N     H      sing N N 340 
LEU N     H2     sing N N 341 
LEU CA    C      sing N N 342 
LEU CA    CB     sing N N 343 
LEU CA    HA     sing N N 344 
LEU C     O      doub N N 345 
LEU C     OXT    sing N N 346 
LEU CB    CG     sing N N 347 
LEU CB    HB2    sing N N 348 
LEU CB    HB3    sing N N 349 
LEU CG    CD1    sing N N 350 
LEU CG    CD2    sing N N 351 
LEU CG    HG     sing N N 352 
LEU CD1   HD11   sing N N 353 
LEU CD1   HD12   sing N N 354 
LEU CD1   HD13   sing N N 355 
LEU CD2   HD21   sing N N 356 
LEU CD2   HD22   sing N N 357 
LEU CD2   HD23   sing N N 358 
LEU OXT   HXT    sing N N 359 
LYS N     CA     sing N N 360 
LYS N     H      sing N N 361 
LYS N     H2     sing N N 362 
LYS CA    C      sing N N 363 
LYS CA    CB     sing N N 364 
LYS CA    HA     sing N N 365 
LYS C     O      doub N N 366 
LYS C     OXT    sing N N 367 
LYS CB    CG     sing N N 368 
LYS CB    HB2    sing N N 369 
LYS CB    HB3    sing N N 370 
LYS CG    CD     sing N N 371 
LYS CG    HG2    sing N N 372 
LYS CG    HG3    sing N N 373 
LYS CD    CE     sing N N 374 
LYS CD    HD2    sing N N 375 
LYS CD    HD3    sing N N 376 
LYS CE    NZ     sing N N 377 
LYS CE    HE2    sing N N 378 
LYS CE    HE3    sing N N 379 
LYS NZ    HZ1    sing N N 380 
LYS NZ    HZ2    sing N N 381 
LYS NZ    HZ3    sing N N 382 
LYS OXT   HXT    sing N N 383 
MET N     CA     sing N N 384 
MET N     H      sing N N 385 
MET N     H2     sing N N 386 
MET CA    C      sing N N 387 
MET CA    CB     sing N N 388 
MET CA    HA     sing N N 389 
MET C     O      doub N N 390 
MET C     OXT    sing N N 391 
MET CB    CG     sing N N 392 
MET CB    HB2    sing N N 393 
MET CB    HB3    sing N N 394 
MET CG    SD     sing N N 395 
MET CG    HG2    sing N N 396 
MET CG    HG3    sing N N 397 
MET SD    CE     sing N N 398 
MET CE    HE1    sing N N 399 
MET CE    HE2    sing N N 400 
MET CE    HE3    sing N N 401 
MET OXT   HXT    sing N N 402 
PHE N     CA     sing N N 403 
PHE N     H      sing N N 404 
PHE N     H2     sing N N 405 
PHE CA    C      sing N N 406 
PHE CA    CB     sing N N 407 
PHE CA    HA     sing N N 408 
PHE C     O      doub N N 409 
PHE C     OXT    sing N N 410 
PHE CB    CG     sing N N 411 
PHE CB    HB2    sing N N 412 
PHE CB    HB3    sing N N 413 
PHE CG    CD1    doub Y N 414 
PHE CG    CD2    sing Y N 415 
PHE CD1   CE1    sing Y N 416 
PHE CD1   HD1    sing N N 417 
PHE CD2   CE2    doub Y N 418 
PHE CD2   HD2    sing N N 419 
PHE CE1   CZ     doub Y N 420 
PHE CE1   HE1    sing N N 421 
PHE CE2   CZ     sing Y N 422 
PHE CE2   HE2    sing N N 423 
PHE CZ    HZ     sing N N 424 
PHE OXT   HXT    sing N N 425 
PRO N     CA     sing N N 426 
PRO N     CD     sing N N 427 
PRO N     H      sing N N 428 
PRO CA    C      sing N N 429 
PRO CA    CB     sing N N 430 
PRO CA    HA     sing N N 431 
PRO C     O      doub N N 432 
PRO C     OXT    sing N N 433 
PRO CB    CG     sing N N 434 
PRO CB    HB2    sing N N 435 
PRO CB    HB3    sing N N 436 
PRO CG    CD     sing N N 437 
PRO CG    HG2    sing N N 438 
PRO CG    HG3    sing N N 439 
PRO CD    HD2    sing N N 440 
PRO CD    HD3    sing N N 441 
PRO OXT   HXT    sing N N 442 
SER N     CA     sing N N 443 
SER N     H      sing N N 444 
SER N     H2     sing N N 445 
SER CA    C      sing N N 446 
SER CA    CB     sing N N 447 
SER CA    HA     sing N N 448 
SER C     O      doub N N 449 
SER C     OXT    sing N N 450 
SER CB    OG     sing N N 451 
SER CB    HB2    sing N N 452 
SER CB    HB3    sing N N 453 
SER OG    HG     sing N N 454 
SER OXT   HXT    sing N N 455 
SO4 S     O1     doub N N 456 
SO4 S     O2     doub N N 457 
SO4 S     O3     sing N N 458 
SO4 S     O4     sing N N 459 
THR N     CA     sing N N 460 
THR N     H      sing N N 461 
THR N     H2     sing N N 462 
THR CA    C      sing N N 463 
THR CA    CB     sing N N 464 
THR CA    HA     sing N N 465 
THR C     O      doub N N 466 
THR C     OXT    sing N N 467 
THR CB    OG1    sing N N 468 
THR CB    CG2    sing N N 469 
THR CB    HB     sing N N 470 
THR OG1   HG1    sing N N 471 
THR CG2   HG21   sing N N 472 
THR CG2   HG22   sing N N 473 
THR CG2   HG23   sing N N 474 
THR OXT   HXT    sing N N 475 
TRP N     CA     sing N N 476 
TRP N     H      sing N N 477 
TRP N     H2     sing N N 478 
TRP CA    C      sing N N 479 
TRP CA    CB     sing N N 480 
TRP CA    HA     sing N N 481 
TRP C     O      doub N N 482 
TRP C     OXT    sing N N 483 
TRP CB    CG     sing N N 484 
TRP CB    HB2    sing N N 485 
TRP CB    HB3    sing N N 486 
TRP CG    CD1    doub Y N 487 
TRP CG    CD2    sing Y N 488 
TRP CD1   NE1    sing Y N 489 
TRP CD1   HD1    sing N N 490 
TRP CD2   CE2    doub Y N 491 
TRP CD2   CE3    sing Y N 492 
TRP NE1   CE2    sing Y N 493 
TRP NE1   HE1    sing N N 494 
TRP CE2   CZ2    sing Y N 495 
TRP CE3   CZ3    doub Y N 496 
TRP CE3   HE3    sing N N 497 
TRP CZ2   CH2    doub Y N 498 
TRP CZ2   HZ2    sing N N 499 
TRP CZ3   CH2    sing Y N 500 
TRP CZ3   HZ3    sing N N 501 
TRP CH2   HH2    sing N N 502 
TRP OXT   HXT    sing N N 503 
TYR N     CA     sing N N 504 
TYR N     H      sing N N 505 
TYR N     H2     sing N N 506 
TYR CA    C      sing N N 507 
TYR CA    CB     sing N N 508 
TYR CA    HA     sing N N 509 
TYR C     O      doub N N 510 
TYR C     OXT    sing N N 511 
TYR CB    CG     sing N N 512 
TYR CB    HB2    sing N N 513 
TYR CB    HB3    sing N N 514 
TYR CG    CD1    doub Y N 515 
TYR CG    CD2    sing Y N 516 
TYR CD1   CE1    sing Y N 517 
TYR CD1   HD1    sing N N 518 
TYR CD2   CE2    doub Y N 519 
TYR CD2   HD2    sing N N 520 
TYR CE1   CZ     doub Y N 521 
TYR CE1   HE1    sing N N 522 
TYR CE2   CZ     sing Y N 523 
TYR CE2   HE2    sing N N 524 
TYR CZ    OH     sing N N 525 
TYR OH    HH     sing N N 526 
TYR OXT   HXT    sing N N 527 
VAL N     CA     sing N N 528 
VAL N     H      sing N N 529 
VAL N     H2     sing N N 530 
VAL CA    C      sing N N 531 
VAL CA    CB     sing N N 532 
VAL CA    HA     sing N N 533 
VAL C     O      doub N N 534 
VAL C     OXT    sing N N 535 
VAL CB    CG1    sing N N 536 
VAL CB    CG2    sing N N 537 
VAL CB    HB     sing N N 538 
VAL CG1   HG11   sing N N 539 
VAL CG1   HG12   sing N N 540 
VAL CG1   HG13   sing N N 541 
VAL CG2   HG21   sing N N 542 
VAL CG2   HG22   sing N N 543 
VAL CG2   HG23   sing N N 544 
VAL OXT   HXT    sing N N 545 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Ministry of Economy and Competitiveness (MINECO)' Spain PID2022-136369NB-I00           1 
'Other government'                                 Spain LMP13_21                       2 
'Other government'                                 Spain 'Biologia Estructural_E35_23R' 3 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   AF-A5VRH5-F1 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9DTK 
_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]   0.008331 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000159 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.026643 
_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]   0.012839 
_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 
H 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N     . MET A 1 1   ? 41.833  -2.092  30.177 1.00 73.81 ? 1   MET A N     1 
ATOM   2    C CA    . MET A 1 1   ? 40.399  -2.489  30.129 1.00 78.60 ? 1   MET A CA    1 
ATOM   3    C C     . MET A 1 1   ? 39.670  -1.454  29.284 1.00 75.29 ? 1   MET A C     1 
ATOM   4    O O     . MET A 1 1   ? 39.149  -0.478  29.819 1.00 76.00 ? 1   MET A O     1 
ATOM   5    C CB    . MET A 1 1   ? 39.797  -2.564  31.539 1.00 88.53 ? 1   MET A CB    1 
ATOM   6    C CG    . MET A 1 1   ? 40.354  -3.669  32.438 1.00 86.25 ? 1   MET A CG    1 
ATOM   7    S SD    . MET A 1 1   ? 39.236  -4.101  33.795 1.00 72.96 ? 1   MET A SD    1 
ATOM   8    C CE    . MET A 1 1   ? 37.650  -4.191  32.960 1.00 76.70 ? 1   MET A CE    1 
ATOM   9    N N     . MET A 1 2   ? 39.659  -1.658  27.965 1.00 65.87 ? 2   MET A N     1 
ATOM   10   C CA    . MET A 1 2   ? 39.096  -0.688  27.030 1.00 61.16 ? 2   MET A CA    1 
ATOM   11   C C     . MET A 1 2   ? 39.977  0.554   26.955 1.00 60.43 ? 2   MET A C     1 
ATOM   12   O O     . MET A 1 2   ? 40.186  1.238   27.962 1.00 63.84 ? 2   MET A O     1 
ATOM   13   C CB    . MET A 1 2   ? 37.667  -0.303  27.435 1.00 67.87 ? 2   MET A CB    1 
ATOM   14   C CG    . MET A 1 2   ? 37.029  0.788   26.584 1.00 67.62 ? 2   MET A CG    1 
ATOM   15   S SD    . MET A 1 2   ? 35.692  0.169   25.549 1.00 45.24 ? 2   MET A SD    1 
ATOM   16   C CE    . MET A 1 2   ? 34.506  -0.321  26.790 1.00 39.17 ? 2   MET A CE    1 
ATOM   17   N N     . GLU A 1 3   ? 40.497  0.848   25.766 1.00 59.58 ? 3   GLU A N     1 
ATOM   18   C CA    . GLU A 1 3   ? 41.198  2.106   25.550 1.00 66.11 ? 3   GLU A CA    1 
ATOM   19   C C     . GLU A 1 3   ? 40.217  3.265   25.690 1.00 59.53 ? 3   GLU A C     1 
ATOM   20   O O     . GLU A 1 3   ? 39.014  3.119   25.455 1.00 55.83 ? 3   GLU A O     1 
ATOM   21   C CB    . GLU A 1 3   ? 41.858  2.151   24.165 1.00 62.52 ? 3   GLU A CB    1 
ATOM   22   C CG    . GLU A 1 3   ? 42.217  0.801   23.535 1.00 71.92 ? 3   GLU A CG    1 
ATOM   23   C CD    . GLU A 1 3   ? 42.696  0.937   22.101 1.00 79.26 ? 3   GLU A CD    1 
ATOM   24   O OE1   . GLU A 1 3   ? 42.889  2.083   21.645 1.00 70.29 ? 3   GLU A OE1   1 
ATOM   25   O OE2   . GLU A 1 3   ? 42.880  -0.102  21.432 1.00 83.08 ? 3   GLU A OE2   1 
ATOM   26   N N     . SER A 1 4   ? 40.735  4.428   26.075 1.00 54.58 ? 4   SER A N     1 
ATOM   27   C CA    . SER A 1 4   ? 39.876  5.591   26.222 1.00 37.19 ? 4   SER A CA    1 
ATOM   28   C C     . SER A 1 4   ? 39.403  6.080   24.854 1.00 33.20 ? 4   SER A C     1 
ATOM   29   O O     . SER A 1 4   ? 39.895  5.660   23.802 1.00 44.39 ? 4   SER A O     1 
ATOM   30   C CB    . SER A 1 4   ? 40.607  6.714   26.956 1.00 39.75 ? 4   SER A CB    1 
ATOM   31   O OG    . SER A 1 4   ? 41.694  7.202   26.189 1.00 57.83 ? 4   SER A OG    1 
ATOM   32   N N     . GLY A 1 5   ? 38.420  6.982   24.878 1.00 46.08 ? 5   GLY A N     1 
ATOM   33   C CA    . GLY A 1 5   ? 37.963  7.591   23.640 1.00 49.52 ? 5   GLY A CA    1 
ATOM   34   C C     . GLY A 1 5   ? 39.020  8.482   23.018 1.00 46.60 ? 5   GLY A C     1 
ATOM   35   O O     . GLY A 1 5   ? 39.173  8.516   21.794 1.00 46.19 ? 5   GLY A O     1 
ATOM   36   N N     . GLU A 1 6   ? 39.750  9.230   23.852 1.00 48.75 ? 6   GLU A N     1 
ATOM   37   C CA    . GLU A 1 6   ? 40.939  9.946   23.406 1.00 56.50 ? 6   GLU A CA    1 
ATOM   38   C C     . GLU A 1 6   ? 41.733  9.114   22.409 1.00 55.24 ? 6   GLU A C     1 
ATOM   39   O O     . GLU A 1 6   ? 41.909  9.496   21.246 1.00 51.91 ? 6   GLU A O     1 
ATOM   40   C CB    . GLU A 1 6   ? 41.829  10.276  24.608 1.00 58.72 ? 6   GLU A CB    1 
ATOM   41   C CG    . GLU A 1 6   ? 41.413  11.469  25.444 1.00 69.81 ? 6   GLU A CG    1 
ATOM   42   C CD    . GLU A 1 6   ? 41.984  11.402  26.850 1.00 74.32 ? 6   GLU A CD    1 
ATOM   43   O OE1   . GLU A 1 6   ? 42.769  10.470  27.131 1.00 64.11 ? 6   GLU A OE1   1 
ATOM   44   O OE2   . GLU A 1 6   ? 41.654  12.280  27.673 1.00 64.64 ? 6   GLU A OE2   1 
ATOM   45   N N     . ALA A 1 7   ? 42.213  7.958   22.871 1.00 53.50 ? 7   ALA A N     1 
ATOM   46   C CA    . ALA A 1 7   ? 43.072  7.116   22.048 1.00 47.22 ? 7   ALA A CA    1 
ATOM   47   C C     . ALA A 1 7   ? 42.390  6.738   20.740 1.00 45.63 ? 7   ALA A C     1 
ATOM   48   O O     . ALA A 1 7   ? 43.047  6.630   19.697 1.00 47.10 ? 7   ALA A O     1 
ATOM   49   C CB    . ALA A 1 7   ? 43.467  5.866   22.832 1.00 47.38 ? 7   ALA A CB    1 
ATOM   50   N N     . LEU A 1 8   ? 41.074  6.528   20.774 1.00 53.02 ? 8   LEU A N     1 
ATOM   51   C CA    . LEU A 1 8   ? 40.338  6.247   19.546 1.00 48.80 ? 8   LEU A CA    1 
ATOM   52   C C     . LEU A 1 8   ? 40.357  7.454   18.618 1.00 51.29 ? 8   LEU A C     1 
ATOM   53   O O     . LEU A 1 8   ? 40.642  7.330   17.421 1.00 54.59 ? 8   LEU A O     1 
ATOM   54   C CB    . LEU A 1 8   ? 38.901  5.849   19.881 1.00 59.28 ? 8   LEU A CB    1 
ATOM   55   C CG    . LEU A 1 8   ? 38.196  4.877   18.934 1.00 52.46 ? 8   LEU A CG    1 
ATOM   56   C CD1   . LEU A 1 8   ? 36.817  4.555   19.477 1.00 58.83 ? 8   LEU A CD1   1 
ATOM   57   C CD2   . LEU A 1 8   ? 38.093  5.436   17.526 1.00 55.35 ? 8   LEU A CD2   1 
ATOM   58   N N     . LEU A 1 9   ? 40.055  8.636   19.158 1.00 55.51 ? 9   LEU A N     1 
ATOM   59   C CA    . LEU A 1 9   ? 40.053  9.844   18.343 1.00 61.69 ? 9   LEU A CA    1 
ATOM   60   C C     . LEU A 1 9   ? 41.448  10.174  17.831 1.00 66.96 ? 9   LEU A C     1 
ATOM   61   O O     . LEU A 1 9   ? 41.593  10.709  16.726 1.00 67.93 ? 9   LEU A O     1 
ATOM   62   C CB    . LEU A 1 9   ? 39.488  11.011  19.152 1.00 65.29 ? 9   LEU A CB    1 
ATOM   63   C CG    . LEU A 1 9   ? 38.029  10.831  19.577 1.00 56.82 ? 9   LEU A CG    1 
ATOM   64   C CD1   . LEU A 1 9   ? 37.671  11.758  20.729 1.00 58.30 ? 9   LEU A CD1   1 
ATOM   65   C CD2   . LEU A 1 9   ? 37.101  11.059  18.395 1.00 48.76 ? 9   LEU A CD2   1 
ATOM   66   N N     . LYS A 1 10  ? 42.484  9.858   18.610 1.00 60.23 ? 10  LYS A N     1 
ATOM   67   C CA    . LYS A 1 10  ? 43.844  10.175  18.187 1.00 63.98 ? 10  LYS A CA    1 
ATOM   68   C C     . LYS A 1 10  ? 44.279  9.295   17.022 1.00 62.06 ? 10  LYS A C     1 
ATOM   69   O O     . LYS A 1 10  ? 44.944  9.770   16.095 1.00 66.98 ? 10  LYS A O     1 
ATOM   70   C CB    . LYS A 1 10  ? 44.807  10.031  19.368 1.00 68.59 ? 10  LYS A CB    1 
ATOM   71   C CG    . LYS A 1 10  ? 44.637  11.056  20.511 1.00 78.47 ? 10  LYS A CG    1 
ATOM   72   C CD    . LYS A 1 10  ? 44.365  12.498  20.058 1.00 84.11 ? 10  LYS A CD    1 
ATOM   73   C CE    . LYS A 1 10  ? 43.425  13.211  21.015 1.00 86.49 ? 10  LYS A CE    1 
ATOM   74   N NZ    . LYS A 1 10  ? 42.012  12.777  20.830 1.00 84.99 ? 10  LYS A NZ    1 
ATOM   75   N N     . LYS A 1 11  ? 43.915  8.012   17.047 1.00 61.58 ? 11  LYS A N     1 
ATOM   76   C CA    . LYS A 1 11  ? 44.208  7.156   15.903 1.00 62.56 ? 11  LYS A CA    1 
ATOM   77   C C     . LYS A 1 11  ? 43.457  7.619   14.662 1.00 70.90 ? 11  LYS A C     1 
ATOM   78   O O     . LYS A 1 11  ? 43.937  7.431   13.538 1.00 74.52 ? 11  LYS A O     1 
ATOM   79   C CB    . LYS A 1 11  ? 43.864  5.703   16.233 1.00 63.25 ? 11  LYS A CB    1 
ATOM   80   C CG    . LYS A 1 11  ? 44.879  5.046   17.154 1.00 74.60 ? 11  LYS A CG    1 
ATOM   81   C CD    . LYS A 1 11  ? 44.565  3.585   17.432 1.00 75.22 ? 11  LYS A CD    1 
ATOM   82   C CE    . LYS A 1 11  ? 45.480  3.044   18.521 1.00 76.65 ? 11  LYS A CE    1 
ATOM   83   N NZ    . LYS A 1 11  ? 45.173  1.639   18.902 1.00 74.90 ? 11  LYS A NZ    1 
ATOM   84   N N     . LEU A 1 12  ? 42.292  8.234   14.844 1.00 75.80 ? 12  LEU A N     1 
ATOM   85   C CA    . LEU A 1 12  ? 41.499  8.766   13.736 1.00 75.11 ? 12  LEU A CA    1 
ATOM   86   C C     . LEU A 1 12  ? 41.762  10.262  13.565 1.00 87.75 ? 12  LEU A C     1 
ATOM   87   O O     . LEU A 1 12  ? 40.862  11.100  13.630 1.00 85.73 ? 12  LEU A O     1 
ATOM   88   C CB    . LEU A 1 12  ? 40.017  8.486   13.972 1.00 66.20 ? 12  LEU A CB    1 
ATOM   89   C CG    . LEU A 1 12  ? 39.491  7.174   13.391 1.00 69.75 ? 12  LEU A CG    1 
ATOM   90   C CD1   . LEU A 1 12  ? 38.282  6.688   14.175 1.00 67.35 ? 12  LEU A CD1   1 
ATOM   91   C CD2   . LEU A 1 12  ? 39.146  7.349   11.922 1.00 79.16 ? 12  LEU A CD2   1 
ATOM   92   N N     . ASP A 1 13  ? 43.031  10.591  13.340 1.00 93.28 ? 13  ASP A N     1 
ATOM   93   C CA    . ASP A 1 13  ? 43.454  11.983  13.240 1.00 90.79 ? 13  ASP A CA    1 
ATOM   94   C C     . ASP A 1 13  ? 43.056  12.552  11.882 1.00 87.67 ? 13  ASP A C     1 
ATOM   95   O O     . ASP A 1 13  ? 43.462  12.029  10.838 1.00 74.14 ? 13  ASP A O     1 
ATOM   96   C CB    . ASP A 1 13  ? 44.964  12.093  13.446 1.00 89.35 ? 13  ASP A CB    1 
ATOM   97   C CG    . ASP A 1 13  ? 45.462  13.527  13.377 1.00 94.43 ? 13  ASP A CG    1 
ATOM   98   O OD1   . ASP A 1 13  ? 44.639  14.444  13.171 1.00 95.49 ? 13  ASP A OD1   1 
ATOM   99   O OD2   . ASP A 1 13  ? 46.684  13.738  13.530 1.00 91.93 ? 13  ASP A OD2   1 
ATOM   100  N N     . GLY A 1 14  ? 42.261  13.622  11.901 1.00 80.75 ? 14  GLY A N     1 
ATOM   101  C CA    . GLY A 1 14  ? 41.942  14.373  10.707 1.00 79.89 ? 14  GLY A CA    1 
ATOM   102  C C     . GLY A 1 14  ? 40.831  13.803  9.853  1.00 72.91 ? 14  GLY A C     1 
ATOM   103  O O     . GLY A 1 14  ? 40.186  14.559  9.119  1.00 67.65 ? 14  GLY A O     1 
ATOM   104  N N     . ARG A 1 15  ? 40.590  12.492  9.914  1.00 77.33 ? 15  ARG A N     1 
ATOM   105  C CA    . ARG A 1 15  ? 39.499  11.910  9.143  1.00 75.28 ? 15  ARG A CA    1 
ATOM   106  C C     . ARG A 1 15  ? 38.138  12.262  9.726  1.00 69.39 ? 15  ARG A C     1 
ATOM   107  O O     . ARG A 1 15  ? 37.124  12.111  9.036  1.00 63.29 ? 15  ARG A O     1 
ATOM   108  C CB    . ARG A 1 15  ? 39.660  10.390  9.069  1.00 78.22 ? 15  ARG A CB    1 
ATOM   109  C CG    . ARG A 1 15  ? 40.481  9.916   7.875  1.00 83.41 ? 15  ARG A CG    1 
ATOM   110  C CD    . ARG A 1 15  ? 41.010  8.498   8.065  1.00 87.83 ? 15  ARG A CD    1 
ATOM   111  N NE    . ARG A 1 15  ? 41.899  8.382   9.216  1.00 88.02 ? 15  ARG A NE    1 
ATOM   112  C CZ    . ARG A 1 15  ? 42.357  7.235   9.698  1.00 91.92 ? 15  ARG A CZ    1 
ATOM   113  N NH1   . ARG A 1 15  ? 42.046  6.076   9.140  1.00 80.75 ? 15  ARG A NH1   1 
ATOM   114  N NH2   . ARG A 1 15  ? 43.151  7.250   10.765 1.00 92.98 ? 15  ARG A NH2   1 
ATOM   115  N N     . LEU A 1 16  ? 38.094  12.731  10.974 1.00 67.97 ? 16  LEU A N     1 
ATOM   116  C CA    . LEU A 1 16  ? 36.848  13.136  11.608 1.00 68.70 ? 16  LEU A CA    1 
ATOM   117  C C     . LEU A 1 16  ? 36.656  14.645  11.640 1.00 71.33 ? 16  LEU A C     1 
ATOM   118  O O     . LEU A 1 16  ? 35.520  15.103  11.798 1.00 70.52 ? 16  LEU A O     1 
ATOM   119  C CB    . LEU A 1 16  ? 36.780  12.592  13.039 1.00 64.68 ? 16  LEU A CB    1 
ATOM   120  C CG    . LEU A 1 16  ? 36.723  11.067  13.155 1.00 60.78 ? 16  LEU A CG    1 
ATOM   121  C CD1   . LEU A 1 16  ? 36.623  10.655  14.613 1.00 58.74 ? 16  LEU A CD1   1 
ATOM   122  C CD2   . LEU A 1 16  ? 35.561  10.493  12.355 1.00 53.30 ? 16  LEU A CD2   1 
ATOM   123  N N     . SER A 1 17  ? 37.728  15.424  11.508 1.00 81.79 ? 17  SER A N     1 
ATOM   124  C CA    . SER A 1 17  ? 37.576  16.857  11.309 1.00 74.48 ? 17  SER A CA    1 
ATOM   125  C C     . SER A 1 17  ? 36.649  17.106  10.128 1.00 66.37 ? 17  SER A C     1 
ATOM   126  O O     . SER A 1 17  ? 36.654  16.359  9.146  1.00 58.85 ? 17  SER A O     1 
ATOM   127  C CB    . SER A 1 17  ? 38.937  17.512  11.067 1.00 73.09 ? 17  SER A CB    1 
ATOM   128  O OG    . SER A 1 17  ? 39.566  16.971  9.919  1.00 77.76 ? 17  SER A OG    1 
ATOM   129  N N     . GLY A 1 18  ? 35.845  18.157  10.230 1.00 54.12 ? 18  GLY A N     1 
ATOM   130  C CA    . GLY A 1 18  ? 34.810  18.405  9.253  1.00 68.16 ? 18  GLY A CA    1 
ATOM   131  C C     . GLY A 1 18  ? 33.488  17.741  9.558  1.00 67.97 ? 18  GLY A C     1 
ATOM   132  O O     . GLY A 1 18  ? 32.618  17.699  8.679  1.00 65.95 ? 18  GLY A O     1 
ATOM   133  N N     . LEU A 1 19  ? 33.313  17.211  10.765 1.00 67.91 ? 19  LEU A N     1 
ATOM   134  C CA    . LEU A 1 19  ? 32.044  16.661  11.218 1.00 59.86 ? 19  LEU A CA    1 
ATOM   135  C C     . LEU A 1 19  ? 31.438  17.623  12.226 1.00 57.42 ? 19  LEU A C     1 
ATOM   136  O O     . LEU A 1 19  ? 32.128  18.093  13.136 1.00 63.98 ? 19  LEU A O     1 
ATOM   137  C CB    . LEU A 1 19  ? 32.221  15.279  11.845 1.00 59.83 ? 19  LEU A CB    1 
ATOM   138  C CG    . LEU A 1 19  ? 32.753  14.181  10.924 1.00 61.70 ? 19  LEU A CG    1 
ATOM   139  C CD1   . LEU A 1 19  ? 32.997  12.917  11.728 1.00 65.68 ? 19  LEU A CD1   1 
ATOM   140  C CD2   . LEU A 1 19  ? 31.797  13.915  9.771  1.00 60.44 ? 19  LEU A CD2   1 
ATOM   141  N N     . ARG A 1 20  ? 30.150  17.905  12.065 1.00 59.34 ? 20  ARG A N     1 
ATOM   142  C CA    . ARG A 1 20  ? 29.492  18.962  12.817 1.00 54.06 ? 20  ARG A CA    1 
ATOM   143  C C     . ARG A 1 20  ? 28.782  18.456  14.063 1.00 50.13 ? 20  ARG A C     1 
ATOM   144  O O     . ARG A 1 20  ? 28.600  19.226  15.012 1.00 41.32 ? 20  ARG A O     1 
ATOM   145  C CB    . ARG A 1 20  ? 28.507  19.689  11.897 1.00 58.71 ? 20  ARG A CB    1 
ATOM   146  C CG    . ARG A 1 20  ? 29.198  20.206  10.633 1.00 56.82 ? 20  ARG A CG    1 
ATOM   147  C CD    . ARG A 1 20  ? 28.261  20.875  9.643  1.00 57.25 ? 20  ARG A CD    1 
ATOM   148  N NE    . ARG A 1 20  ? 27.852  19.959  8.584  1.00 55.17 ? 20  ARG A NE    1 
ATOM   149  C CZ    . ARG A 1 20  ? 26.777  19.183  8.633  1.00 56.00 ? 20  ARG A CZ    1 
ATOM   150  N NH1   . ARG A 1 20  ? 25.937  19.227  9.654  1.00 61.38 ? 20  ARG A NH1   1 
ATOM   151  N NH2   . ARG A 1 20  ? 26.535  18.347  7.627  1.00 64.63 ? 20  ARG A NH2   1 
ATOM   152  N N     . GLY A 1 21  ? 28.397  17.183  14.091 1.00 46.26 ? 21  GLY A N     1 
ATOM   153  C CA    . GLY A 1 21  ? 27.837  16.611  15.296 1.00 39.98 ? 21  GLY A CA    1 
ATOM   154  C C     . GLY A 1 21  ? 28.882  16.402  16.375 1.00 42.05 ? 21  GLY A C     1 
ATOM   155  O O     . GLY A 1 21  ? 30.078  16.258  16.116 1.00 51.60 ? 21  GLY A O     1 
ATOM   156  N N     . ARG A 1 22  ? 28.403  16.375  17.614 1.00 36.00 ? 22  ARG A N     1 
ATOM   157  C CA    . ARG A 1 22  ? 29.284  16.336  18.773 1.00 33.52 ? 22  ARG A CA    1 
ATOM   158  C C     . ARG A 1 22  ? 29.936  14.966  18.928 1.00 46.08 ? 22  ARG A C     1 
ATOM   159  O O     . ARG A 1 22  ? 29.310  13.929  18.694 1.00 37.12 ? 22  ARG A O     1 
ATOM   160  C CB    . ARG A 1 22  ? 28.481  16.698  20.023 1.00 41.46 ? 22  ARG A CB    1 
ATOM   161  C CG    . ARG A 1 22  ? 29.248  16.683  21.338 1.00 45.06 ? 22  ARG A CG    1 
ATOM   162  C CD    . ARG A 1 22  ? 28.362  17.132  22.506 1.00 58.16 ? 22  ARG A CD    1 
ATOM   163  N NE    . ARG A 1 22  ? 27.150  17.820  22.068 1.00 61.58 ? 22  ARG A NE    1 
ATOM   164  C CZ    . ARG A 1 22  ? 27.102  19.090  21.685 1.00 66.53 ? 22  ARG A CZ    1 
ATOM   165  N NH1   . ARG A 1 22  ? 28.183  19.853  21.680 1.00 69.04 ? 22  ARG A NH1   1 
ATOM   166  N NH2   . ARG A 1 22  ? 25.941  19.603  21.286 1.00 60.83 ? 22  ARG A NH2   1 
ATOM   167  N N     . LEU A 1 23  ? 31.211  14.973  19.321 1.00 57.80 ? 23  LEU A N     1 
ATOM   168  C CA    . LEU A 1 23  ? 31.992  13.762  19.578 1.00 37.10 ? 23  LEU A CA    1 
ATOM   169  C C     . LEU A 1 23  ? 32.419  13.788  21.043 1.00 38.53 ? 23  LEU A C     1 
ATOM   170  O O     . LEU A 1 23  ? 33.332  14.532  21.413 1.00 42.77 ? 23  LEU A O     1 
ATOM   171  C CB    . LEU A 1 23  ? 33.207  13.683  18.657 1.00 28.98 ? 23  LEU A CB    1 
ATOM   172  C CG    . LEU A 1 23  ? 32.995  13.130  17.248 1.00 35.49 ? 23  LEU A CG    1 
ATOM   173  C CD1   . LEU A 1 23  ? 34.099  13.616  16.319 1.00 48.03 ? 23  LEU A CD1   1 
ATOM   174  C CD2   . LEU A 1 23  ? 32.947  11.613  17.276 1.00 41.93 ? 23  LEU A CD2   1 
ATOM   175  N N     . THR A 1 24  ? 31.769  12.974  21.875 1.00 45.01 ? 24  THR A N     1 
ATOM   176  C CA    . THR A 1 24  ? 32.036  12.964  23.309 1.00 47.48 ? 24  THR A CA    1 
ATOM   177  C C     . THR A 1 24  ? 32.687  11.649  23.712 1.00 49.65 ? 24  THR A C     1 
ATOM   178  O O     . THR A 1 24  ? 32.056  10.590  23.572 1.00 44.98 ? 24  THR A O     1 
ATOM   179  C CB    . THR A 1 24  ? 30.745  13.174  24.098 1.00 44.18 ? 24  THR A CB    1 
ATOM   180  O OG1   . THR A 1 24  ? 29.974  14.219  23.492 1.00 54.54 ? 24  THR A OG1   1 
ATOM   181  C CG2   . THR A 1 24  ? 31.063  13.547  25.539 1.00 36.15 ? 24  THR A CG2   1 
ATOM   182  N N     . PRO A 1 25  ? 33.923  11.652  24.208 1.00 64.51 ? 25  PRO A N     1 
ATOM   183  C CA    . PRO A 1 25  ? 34.547  10.399  24.645 1.00 57.10 ? 25  PRO A CA    1 
ATOM   184  C C     . PRO A 1 25  ? 34.115  9.968   26.038 1.00 41.08 ? 25  PRO A C     1 
ATOM   185  O O     . PRO A 1 25  ? 33.772  10.783  26.898 1.00 41.05 ? 25  PRO A O     1 
ATOM   186  C CB    . PRO A 1 25  ? 36.045  10.731  24.623 1.00 51.74 ? 25  PRO A CB    1 
ATOM   187  C CG    . PRO A 1 25  ? 36.095  12.196  24.870 1.00 52.23 ? 25  PRO A CG    1 
ATOM   188  C CD    . PRO A 1 25  ? 34.901  12.756  24.153 1.00 59.95 ? 25  PRO A CD    1 
ATOM   189  N N     . ASP A 1 26  ? 34.135  8.649   26.244 1.00 37.04 ? 26  ASP A N     1 
ATOM   190  C CA    . ASP A 1 26  ? 33.990  8.044   27.569 1.00 37.33 ? 26  ASP A CA    1 
ATOM   191  C C     . ASP A 1 26  ? 32.648  8.374   28.214 1.00 34.37 ? 26  ASP A C     1 
ATOM   192  O O     . ASP A 1 26  ? 32.545  8.462   29.440 1.00 30.97 ? 26  ASP A O     1 
ATOM   193  C CB    . ASP A 1 26  ? 35.133  8.471   28.494 1.00 48.72 ? 26  ASP A CB    1 
ATOM   194  C CG    . ASP A 1 26  ? 36.500  8.230   27.883 1.00 45.93 ? 26  ASP A CG    1 
ATOM   195  O OD1   . ASP A 1 26  ? 36.775  7.082   27.475 1.00 42.11 ? 26  ASP A OD1   1 
ATOM   196  O OD2   . ASP A 1 26  ? 37.299  9.187   27.813 1.00 50.08 ? 26  ASP A OD2   1 
ATOM   197  N N     . THR A 1 27  ? 31.608  8.547   27.406 1.00 38.17 ? 27  THR A N     1 
ATOM   198  C CA    . THR A 1 27  ? 30.282  8.835   27.936 1.00 44.16 ? 27  THR A CA    1 
ATOM   199  C C     . THR A 1 27  ? 29.682  7.560   28.513 1.00 43.21 ? 27  THR A C     1 
ATOM   200  O O     . THR A 1 27  ? 29.506  6.570   27.794 1.00 43.78 ? 27  THR A O     1 
ATOM   201  C CB    . THR A 1 27  ? 29.376  9.405   26.847 1.00 40.12 ? 27  THR A CB    1 
ATOM   202  O OG1   . THR A 1 27  ? 30.026  10.513  26.213 1.00 46.29 ? 27  THR A OG1   1 
ATOM   203  C CG2   . THR A 1 27  ? 28.049  9.864   27.444 1.00 38.55 ? 27  THR A CG2   1 
ATOM   204  N N     . GLY A 1 28  ? 29.378  7.579   29.807 1.00 32.34 ? 28  GLY A N     1 
ATOM   205  C CA    . GLY A 1 28  ? 28.693  6.446   30.401 1.00 36.63 ? 28  GLY A CA    1 
ATOM   206  C C     . GLY A 1 28  ? 27.398  6.160   29.663 1.00 34.91 ? 28  GLY A C     1 
ATOM   207  O O     . GLY A 1 28  ? 26.673  7.074   29.263 1.00 39.64 ? 28  GLY A O     1 
ATOM   208  N N     . MET A 1 29  ? 27.118  4.877   29.463 1.00 31.36 ? 29  MET A N     1 
ATOM   209  C CA    . MET A 1 29  ? 25.881  4.483   28.809 1.00 33.43 ? 29  MET A CA    1 
ATOM   210  C C     . MET A 1 29  ? 24.719  4.428   29.791 1.00 21.96 ? 29  MET A C     1 
ATOM   211  O O     . MET A 1 29  ? 23.570  4.265   29.367 1.00 30.85 ? 29  MET A O     1 
ATOM   212  C CB    . MET A 1 29  ? 26.082  3.139   28.102 1.00 32.11 ? 29  MET A CB    1 
ATOM   213  C CG    . MET A 1 29  ? 26.983  3.268   26.864 1.00 24.56 ? 29  MET A CG    1 
ATOM   214  S SD    . MET A 1 29  ? 26.188  3.656   25.286 1.00 42.88 ? 29  MET A SD    1 
ATOM   215  C CE    . MET A 1 29  ? 24.718  2.637   25.307 1.00 49.64 ? 29  MET A CE    1 
ATOM   216  N N     . ASP A 1 30  ? 25.003  4.578   31.087 1.00 21.45 ? 30  ASP A N     1 
ATOM   217  C CA    . ASP A 1 30  ? 23.973  4.833   32.085 1.00 22.74 ? 30  ASP A CA    1 
ATOM   218  C C     . ASP A 1 30  ? 23.370  6.226   31.953 1.00 28.96 ? 30  ASP A C     1 
ATOM   219  O O     . ASP A 1 30  ? 22.261  6.457   32.445 1.00 29.52 ? 30  ASP A O     1 
ATOM   220  C CB    . ASP A 1 30  ? 24.563  4.667   33.484 1.00 22.76 ? 30  ASP A CB    1 
ATOM   221  C CG    . ASP A 1 30  ? 25.692  5.644   33.756 1.00 30.29 ? 30  ASP A CG    1 
ATOM   222  O OD1   . ASP A 1 30  ? 26.588  5.770   32.894 1.00 28.05 ? 30  ASP A OD1   1 
ATOM   223  O OD2   . ASP A 1 30  ? 25.681  6.287   34.826 1.00 32.67 ? 30  ASP A OD2   1 
ATOM   224  N N     . LYS A 1 31  ? 24.082  7.164   31.329 1.00 32.18 ? 31  LYS A N     1 
ATOM   225  C CA    . LYS A 1 31  ? 23.531  8.486   31.066 1.00 29.70 ? 31  LYS A CA    1 
ATOM   226  C C     . LYS A 1 31  ? 22.529  8.484   29.927 1.00 28.01 ? 31  LYS A C     1 
ATOM   227  O O     . LYS A 1 31  ? 21.888  9.512   29.686 1.00 28.29 ? 31  LYS A O     1 
ATOM   228  C CB    . LYS A 1 31  ? 24.651  9.475   30.721 1.00 24.24 ? 31  LYS A CB    1 
ATOM   229  C CG    . LYS A 1 31  ? 25.729  9.620   31.773 1.00 16.35 ? 31  LYS A CG    1 
ATOM   230  C CD    . LYS A 1 31  ? 25.157  9.907   33.145 1.00 11.96 ? 31  LYS A CD    1 
ATOM   231  C CE    . LYS A 1 31  ? 26.209  9.718   34.208 1.00 19.98 ? 31  LYS A CE    1 
ATOM   232  N NZ    . LYS A 1 31  ? 25.656  9.950   35.565 1.00 25.11 ? 31  LYS A NZ    1 
ATOM   233  N N     . ILE A 1 32  ? 22.381  7.363   29.228 1.00 31.37 ? 32  ILE A N     1 
ATOM   234  C CA    . ILE A 1 32  ? 21.755  7.374   27.913 1.00 29.46 ? 32  ILE A CA    1 
ATOM   235  C C     . ILE A 1 32  ? 20.864  6.151   27.743 1.00 23.77 ? 32  ILE A C     1 
ATOM   236  O O     . ILE A 1 32  ? 20.314  5.912   26.663 1.00 20.79 ? 32  ILE A O     1 
ATOM   237  C CB    . ILE A 1 32  ? 22.844  7.454   26.827 1.00 29.83 ? 32  ILE A CB    1 
ATOM   238  C CG1   . ILE A 1 32  ? 23.500  8.835   26.865 1.00 35.93 ? 32  ILE A CG1   1 
ATOM   239  C CG2   . ILE A 1 32  ? 22.276  7.165   25.447 1.00 39.32 ? 32  ILE A CG2   1 
ATOM   240  C CD1   . ILE A 1 32  ? 24.692  8.941   26.001 1.00 31.76 ? 32  ILE A CD1   1 
ATOM   241  N N     . THR A 1 33  ? 20.692  5.376   28.807 1.00 20.73 ? 33  THR A N     1 
ATOM   242  C CA    . THR A 1 33  ? 19.787  4.239   28.770 1.00 27.31 ? 33  THR A CA    1 
ATOM   243  C C     . THR A 1 33  ? 18.802  4.343   29.922 1.00 28.43 ? 33  THR A C     1 
ATOM   244  O O     . THR A 1 33  ? 19.110  4.902   30.979 1.00 31.87 ? 33  THR A O     1 
ATOM   245  C CB    . THR A 1 33  ? 20.540  2.906   28.830 1.00 20.13 ? 33  THR A CB    1 
ATOM   246  O OG1   . THR A 1 33  ? 21.410  2.886   29.968 1.00 20.92 ? 33  THR A OG1   1 
ATOM   247  C CG2   . THR A 1 33  ? 21.354  2.713   27.558 1.00 21.01 ? 33  THR A CG2   1 
ATOM   248  N N     . TRP A 1 34  ? 17.604  3.801   29.699 1.00 26.04 ? 34  TRP A N     1 
ATOM   249  C CA    . TRP A 1 34  ? 16.540  3.940   30.684 1.00 25.16 ? 34  TRP A CA    1 
ATOM   250  C C     . TRP A 1 34  ? 16.874  3.215   31.980 1.00 21.20 ? 34  TRP A C     1 
ATOM   251  O O     . TRP A 1 34  ? 16.443  3.645   33.057 1.00 22.77 ? 34  TRP A O     1 
ATOM   252  C CB    . TRP A 1 34  ? 15.226  3.419   30.106 1.00 45.69 ? 34  TRP A CB    1 
ATOM   253  C CG    . TRP A 1 34  ? 14.262  4.504   29.744 1.00 45.21 ? 34  TRP A CG    1 
ATOM   254  C CD1   . TRP A 1 34  ? 14.408  5.438   28.759 1.00 44.30 ? 34  TRP A CD1   1 
ATOM   255  C CD2   . TRP A 1 34  ? 13.001  4.769   30.365 1.00 34.32 ? 34  TRP A CD2   1 
ATOM   256  N NE1   . TRP A 1 34  ? 13.315  6.269   28.729 1.00 42.60 ? 34  TRP A NE1   1 
ATOM   257  C CE2   . TRP A 1 34  ? 12.436  5.879   29.705 1.00 45.05 ? 34  TRP A CE2   1 
ATOM   258  C CE3   . TRP A 1 34  ? 12.294  4.176   31.414 1.00 43.27 ? 34  TRP A CE3   1 
ATOM   259  C CZ2   . TRP A 1 34  ? 11.198  6.406   30.062 1.00 43.03 ? 34  TRP A CZ2   1 
ATOM   260  C CZ3   . TRP A 1 34  ? 11.065  4.701   31.766 1.00 47.70 ? 34  TRP A CZ3   1 
ATOM   261  C CH2   . TRP A 1 34  ? 10.529  5.804   31.092 1.00 51.11 ? 34  TRP A CH2   1 
ATOM   262  N N     . PHE A 1 35  ? 17.632  2.120   31.902 1.00 28.43 ? 35  PHE A N     1 
ATOM   263  C CA    . PHE A 1 35  ? 18.057  1.425   33.112 1.00 21.45 ? 35  PHE A CA    1 
ATOM   264  C C     . PHE A 1 35  ? 18.972  2.287   33.975 1.00 15.16 ? 35  PHE A C     1 
ATOM   265  O O     . PHE A 1 35  ? 19.090  2.030   35.178 1.00 21.05 ? 35  PHE A O     1 
ATOM   266  C CB    . PHE A 1 35  ? 18.772  0.120   32.746 1.00 23.73 ? 35  PHE A CB    1 
ATOM   267  C CG    . PHE A 1 35  ? 17.868  -1.087  32.690 1.00 18.17 ? 35  PHE A CG    1 
ATOM   268  C CD1   . PHE A 1 35  ? 17.035  -1.406  33.751 1.00 23.49 ? 35  PHE A CD1   1 
ATOM   269  C CD2   . PHE A 1 35  ? 17.867  -1.912  31.577 1.00 24.06 ? 35  PHE A CD2   1 
ATOM   270  C CE1   . PHE A 1 35  ? 16.215  -2.519  33.698 1.00 19.37 ? 35  PHE A CE1   1 
ATOM   271  C CE2   . PHE A 1 35  ? 17.048  -3.025  31.519 1.00 17.91 ? 35  PHE A CE2   1 
ATOM   272  C CZ    . PHE A 1 35  ? 16.222  -3.328  32.581 1.00 21.37 ? 35  PHE A CZ    1 
ATOM   273  N N     . ARG A 1 36  ? 19.615  3.302   33.393 1.00 22.99 ? 36  ARG A N     1 
ATOM   274  C CA    . ARG A 1 36  ? 20.560  4.153   34.117 1.00 22.62 ? 36  ARG A CA    1 
ATOM   275  C C     . ARG A 1 36  ? 21.693  3.308   34.700 1.00 14.84 ? 36  ARG A C     1 
ATOM   276  O O     . ARG A 1 36  ? 22.071  3.439   35.867 1.00 16.84 ? 36  ARG A O     1 
ATOM   277  C CB    . ARG A 1 36  ? 19.849  4.961   35.205 1.00 27.93 ? 36  ARG A CB    1 
ATOM   278  C CG    . ARG A 1 36  ? 20.333  6.408   35.362 1.00 39.02 ? 36  ARG A CG    1 
ATOM   279  C CD    . ARG A 1 36  ? 19.910  7.279   34.180 1.00 43.84 ? 36  ARG A CD    1 
ATOM   280  N NE    . ARG A 1 36  ? 18.489  7.600   34.231 1.00 48.25 ? 36  ARG A NE    1 
ATOM   281  C CZ    . ARG A 1 36  ? 17.927  8.399   35.129 1.00 41.47 ? 36  ARG A CZ    1 
ATOM   282  N NH1   . ARG A 1 36  ? 18.654  9.124   35.964 1.00 39.32 ? 36  ARG A NH1   1 
ATOM   283  N NH2   . ARG A 1 36  ? 16.601  8.484   35.178 1.00 40.63 ? 36  ARG A NH2   1 
ATOM   284  N N     . ALA A 1 37  ? 22.231  2.427   33.863 1.00 19.01 ? 37  ALA A N     1 
ATOM   285  C CA    . ALA A 1 37  ? 23.323  1.548   34.246 1.00 22.24 ? 37  ALA A CA    1 
ATOM   286  C C     . ALA A 1 37  ? 24.093  1.180   32.988 1.00 22.17 ? 37  ALA A C     1 
ATOM   287  O O     . ALA A 1 37  ? 23.640  1.418   31.865 1.00 20.47 ? 37  ALA A O     1 
ATOM   288  C CB    . ALA A 1 37  ? 22.814  0.297   34.971 1.00 22.75 ? 37  ALA A CB    1 
ATOM   289  N N     . GLY A 1 38  ? 25.264  0.594   33.186 1.00 27.06 ? 38  GLY A N     1 
ATOM   290  C CA    . GLY A 1 38  ? 26.165  0.268   32.101 1.00 27.46 ? 38  GLY A CA    1 
ATOM   291  C C     . GLY A 1 38  ? 27.485  1.007   32.223 1.00 34.01 ? 38  GLY A C     1 
ATOM   292  O O     . GLY A 1 38  ? 27.675  1.879   33.069 1.00 34.27 ? 38  GLY A O     1 
ATOM   293  N N     . GLY A 1 39  ? 28.403  0.630   31.338 1.00 34.71 ? 39  GLY A N     1 
ATOM   294  C CA    . GLY A 1 39  ? 29.738  1.172   31.352 1.00 32.69 ? 39  GLY A CA    1 
ATOM   295  C C     . GLY A 1 39  ? 29.981  2.161   30.232 1.00 39.61 ? 39  GLY A C     1 
ATOM   296  O O     . GLY A 1 39  ? 29.076  2.508   29.467 1.00 36.61 ? 39  GLY A O     1 
ATOM   297  N N     . PRO A 1 40  ? 31.224  2.624   30.107 1.00 49.39 ? 40  PRO A N     1 
ATOM   298  C CA    . PRO A 1 40  ? 31.509  3.722   29.176 1.00 37.58 ? 40  PRO A CA    1 
ATOM   299  C C     . PRO A 1 40  ? 31.383  3.301   27.721 1.00 31.94 ? 40  PRO A C     1 
ATOM   300  O O     . PRO A 1 40  ? 31.775  2.198   27.332 1.00 33.79 ? 40  PRO A O     1 
ATOM   301  C CB    . PRO A 1 40  ? 32.956  4.114   29.507 1.00 44.06 ? 40  PRO A CB    1 
ATOM   302  C CG    . PRO A 1 40  ? 33.335  3.346   30.736 1.00 51.97 ? 40  PRO A CG    1 
ATOM   303  C CD    . PRO A 1 40  ? 32.428  2.170   30.822 1.00 43.11 ? 40  PRO A CD    1 
ATOM   304  N N     . ALA A 1 41  ? 30.826  4.201   26.917 1.00 32.62 ? 41  ALA A N     1 
ATOM   305  C CA    . ALA A 1 41  ? 30.949  4.131   25.470 1.00 38.29 ? 41  ALA A CA    1 
ATOM   306  C C     . ALA A 1 41  ? 32.231  4.848   25.074 1.00 45.99 ? 41  ALA A C     1 
ATOM   307  O O     . ALA A 1 41  ? 32.457  5.991   25.486 1.00 49.52 ? 41  ALA A O     1 
ATOM   308  C CB    . ALA A 1 41  ? 29.743  4.772   24.784 1.00 35.25 ? 41  ALA A CB    1 
ATOM   309  N N     . GLN A 1 42  ? 33.079  4.173   24.294 1.00 52.54 ? 42  GLN A N     1 
ATOM   310  C CA    . GLN A 1 42  ? 34.377  4.751   23.957 1.00 52.48 ? 42  GLN A CA    1 
ATOM   311  C C     . GLN A 1 42  ? 34.218  6.162   23.403 1.00 50.27 ? 42  GLN A C     1 
ATOM   312  O O     . GLN A 1 42  ? 34.826  7.111   23.911 1.00 53.68 ? 42  GLN A O     1 
ATOM   313  C CB    . GLN A 1 42  ? 35.121  3.849   22.969 1.00 49.87 ? 42  GLN A CB    1 
ATOM   314  C CG    . GLN A 1 42  ? 36.314  3.140   23.603 1.00 54.81 ? 42  GLN A CG    1 
ATOM   315  C CD    . GLN A 1 42  ? 37.311  2.606   22.593 1.00 57.20 ? 42  GLN A CD    1 
ATOM   316  O OE1   . GLN A 1 42  ? 36.944  2.192   21.494 1.00 52.09 ? 42  GLN A OE1   1 
ATOM   317  N NE2   . GLN A 1 42  ? 38.585  2.609   22.968 1.00 66.48 ? 42  GLN A NE2   1 
ATOM   318  N N     . VAL A 1 43  ? 33.392  6.326   22.371 1.00 37.05 ? 43  VAL A N     1 
ATOM   319  C CA    . VAL A 1 43  ? 33.069  7.649   21.846 1.00 47.47 ? 43  VAL A CA    1 
ATOM   320  C C     . VAL A 1 43  ? 31.602  7.683   21.439 1.00 49.65 ? 43  VAL A C     1 
ATOM   321  O O     . VAL A 1 43  ? 31.146  6.844   20.655 1.00 50.55 ? 43  VAL A O     1 
ATOM   322  C CB    . VAL A 1 43  ? 33.951  8.042   20.645 1.00 50.69 ? 43  VAL A CB    1 
ATOM   323  C CG1   . VAL A 1 43  ? 33.641  9.473   20.226 1.00 51.80 ? 43  VAL A CG1   1 
ATOM   324  C CG2   . VAL A 1 43  ? 35.425  7.890   20.980 1.00 50.11 ? 43  VAL A CG2   1 
ATOM   325  N N     . LEU A 1 44  ? 30.872  8.660   21.970 1.00 48.11 ? 44  LEU A N     1 
ATOM   326  C CA    . LEU A 1 44  ? 29.515  8.965   21.540 1.00 40.09 ? 44  LEU A CA    1 
ATOM   327  C C     . LEU A 1 44  ? 29.563  9.963   20.390 1.00 41.57 ? 44  LEU A C     1 
ATOM   328  O O     . LEU A 1 44  ? 30.235  10.995  20.489 1.00 47.15 ? 44  LEU A O     1 
ATOM   329  C CB    . LEU A 1 44  ? 28.718  9.552   22.703 1.00 40.37 ? 44  LEU A CB    1 
ATOM   330  C CG    . LEU A 1 44  ? 27.203  9.366   22.783 1.00 37.99 ? 44  LEU A CG    1 
ATOM   331  C CD1   . LEU A 1 44  ? 26.730  10.105  24.000 1.00 38.28 ? 44  LEU A CD1   1 
ATOM   332  C CD2   . LEU A 1 44  ? 26.456  9.872   21.573 1.00 36.67 ? 44  LEU A CD2   1 
ATOM   333  N N     . PHE A 1 45  ? 28.857  9.659   19.303 1.00 34.59 ? 45  PHE A N     1 
ATOM   334  C CA    . PHE A 1 45  ? 28.694  10.587  18.193 1.00 41.01 ? 45  PHE A CA    1 
ATOM   335  C C     . PHE A 1 45  ? 27.216  10.909  18.019 1.00 45.35 ? 45  PHE A C     1 
ATOM   336  O O     . PHE A 1 45  ? 26.361  10.024  18.125 1.00 42.76 ? 45  PHE A O     1 
ATOM   337  C CB    . PHE A 1 45  ? 29.267  10.018  16.887 1.00 36.45 ? 45  PHE A CB    1 
ATOM   338  C CG    . PHE A 1 45  ? 29.126  10.944  15.707 1.00 38.33 ? 45  PHE A CG    1 
ATOM   339  C CD1   . PHE A 1 45  ? 29.602  12.244  15.769 1.00 38.21 ? 45  PHE A CD1   1 
ATOM   340  C CD2   . PHE A 1 45  ? 28.526  10.512  14.536 1.00 45.27 ? 45  PHE A CD2   1 
ATOM   341  C CE1   . PHE A 1 45  ? 29.475  13.097  14.687 1.00 40.30 ? 45  PHE A CE1   1 
ATOM   342  C CE2   . PHE A 1 45  ? 28.398  11.361  13.451 1.00 47.31 ? 45  PHE A CE2   1 
ATOM   343  C CZ    . PHE A 1 45  ? 28.874  12.654  13.527 1.00 41.23 ? 45  PHE A CZ    1 
ATOM   344  N N     . GLN A 1 46  ? 26.921  12.182  17.757 1.00 41.50 ? 46  GLN A N     1 
ATOM   345  C CA    . GLN A 1 46  ? 25.551  12.668  17.590 1.00 29.74 ? 46  GLN A CA    1 
ATOM   346  C C     . GLN A 1 46  ? 25.491  13.490  16.310 1.00 30.50 ? 46  GLN A C     1 
ATOM   347  O O     . GLN A 1 46  ? 25.622  14.721  16.343 1.00 41.15 ? 46  GLN A O     1 
ATOM   348  C CB    . GLN A 1 46  ? 25.107  13.489  18.797 1.00 28.79 ? 46  GLN A CB    1 
ATOM   349  C CG    . GLN A 1 46  ? 25.204  12.735  20.108 1.00 34.91 ? 46  GLN A CG    1 
ATOM   350  C CD    . GLN A 1 46  ? 24.847  13.588  21.307 1.00 41.70 ? 46  GLN A CD    1 
ATOM   351  O OE1   . GLN A 1 46  ? 23.675  13.874  21.554 1.00 38.11 ? 46  GLN A OE1   1 
ATOM   352  N NE2   . GLN A 1 46  ? 25.858  13.993  22.067 1.00 42.59 ? 46  GLN A NE2   1 
ATOM   353  N N     . PRO A 1 47  ? 25.287  12.844  15.162 1.00 36.09 ? 47  PRO A N     1 
ATOM   354  C CA    . PRO A 1 47  ? 25.318  13.580  13.891 1.00 38.45 ? 47  PRO A CA    1 
ATOM   355  C C     . PRO A 1 47  ? 24.226  14.637  13.823 1.00 46.42 ? 47  PRO A C     1 
ATOM   356  O O     . PRO A 1 47  ? 23.113  14.443  14.316 1.00 45.77 ? 47  PRO A O     1 
ATOM   357  C CB    . PRO A 1 47  ? 25.114  12.488  12.834 1.00 40.10 ? 47  PRO A CB    1 
ATOM   358  C CG    . PRO A 1 47  ? 24.603  11.303  13.561 1.00 43.20 ? 47  PRO A CG    1 
ATOM   359  C CD    . PRO A 1 47  ? 25.010  11.409  14.985 1.00 43.77 ? 47  PRO A CD    1 
ATOM   360  N N     . SER A 1 48  ? 24.559  15.766  13.194 1.00 49.22 ? 48  SER A N     1 
ATOM   361  C CA    . SER A 1 48  ? 23.619  16.880  13.120 1.00 52.01 ? 48  SER A CA    1 
ATOM   362  C C     . SER A 1 48  ? 22.506  16.598  12.119 1.00 54.08 ? 48  SER A C     1 
ATOM   363  O O     . SER A 1 48  ? 21.329  16.849  12.399 1.00 41.49 ? 48  SER A O     1 
ATOM   364  C CB    . SER A 1 48  ? 24.362  18.165  12.754 1.00 44.56 ? 48  SER A CB    1 
ATOM   365  O OG    . SER A 1 48  ? 25.174  18.603  13.829 1.00 50.15 ? 48  SER A OG    1 
ATOM   366  N N     . ASP A 1 49  ? 22.858  16.088  10.940 1.00 57.09 ? 49  ASP A N     1 
ATOM   367  C CA    . ASP A 1 49  ? 21.874  15.723  9.931  1.00 60.01 ? 49  ASP A CA    1 
ATOM   368  C C     . ASP A 1 49  ? 22.344  14.463  9.219  1.00 58.40 ? 49  ASP A C     1 
ATOM   369  O O     . ASP A 1 49  ? 23.449  13.965  9.453  1.00 49.52 ? 49  ASP A O     1 
ATOM   370  C CB    . ASP A 1 49  ? 21.641  16.864  8.930  1.00 60.04 ? 49  ASP A CB    1 
ATOM   371  C CG    . ASP A 1 49  ? 22.922  17.573  8.540  1.00 50.99 ? 49  ASP A CG    1 
ATOM   372  O OD1   . ASP A 1 49  ? 23.891  16.885  8.155  1.00 55.32 ? 49  ASP A OD1   1 
ATOM   373  O OD2   . ASP A 1 49  ? 22.957  18.819  8.616  1.00 44.38 ? 49  ASP A OD2   1 
ATOM   374  N N     . GLU A 1 50  ? 21.479  13.942  8.343  1.00 65.04 ? 50  GLU A N     1 
ATOM   375  C CA    . GLU A 1 50  ? 21.790  12.708  7.630  1.00 59.50 ? 50  GLU A CA    1 
ATOM   376  C C     . GLU A 1 50  ? 23.150  12.772  6.957  1.00 55.98 ? 50  GLU A C     1 
ATOM   377  O O     . GLU A 1 50  ? 23.823  11.745  6.812  1.00 57.25 ? 50  GLU A O     1 
ATOM   378  C CB    . GLU A 1 50  ? 20.709  12.421  6.588  1.00 61.24 ? 50  GLU A CB    1 
ATOM   379  C CG    . GLU A 1 50  ? 20.902  11.119  5.828  1.00 65.84 ? 50  GLU A CG    1 
ATOM   380  C CD    . GLU A 1 50  ? 19.698  10.764  4.980  1.00 57.48 ? 50  GLU A CD    1 
ATOM   381  O OE1   . GLU A 1 50  ? 18.576  10.729  5.527  1.00 55.27 ? 50  GLU A OE1   1 
ATOM   382  O OE2   . GLU A 1 50  ? 19.871  10.523  3.766  1.00 49.38 ? 50  GLU A OE2   1 
ATOM   383  N N     . GLU A 1 51  ? 23.576  13.964  6.540  1.00 55.95 ? 51  GLU A N     1 
ATOM   384  C CA    . GLU A 1 51  ? 24.848  14.082  5.843  1.00 57.08 ? 51  GLU A CA    1 
ATOM   385  C C     . GLU A 1 51  ? 26.024  14.093  6.809  1.00 51.99 ? 51  GLU A C     1 
ATOM   386  O O     . GLU A 1 51  ? 27.103  13.597  6.466  1.00 50.74 ? 51  GLU A O     1 
ATOM   387  C CB    . GLU A 1 51  ? 24.841  15.338  4.969  1.00 54.96 ? 51  GLU A CB    1 
ATOM   388  C CG    . GLU A 1 51  ? 23.920  15.251  3.742  1.00 54.58 ? 51  GLU A CG    1 
ATOM   389  C CD    . GLU A 1 51  ? 23.891  13.878  3.078  1.00 60.85 ? 51  GLU A CD    1 
ATOM   390  O OE1   . GLU A 1 51  ? 22.912  13.560  2.371  1.00 66.12 ? 51  GLU A OE1   1 
ATOM   391  O OE2   . GLU A 1 51  ? 24.866  13.116  3.252  1.00 55.10 ? 51  GLU A OE2   1 
ATOM   392  N N     . ASP A 1 52  ? 25.842  14.636  8.014  1.00 51.20 ? 52  ASP A N     1 
ATOM   393  C CA    . ASP A 1 52  ? 26.853  14.458  9.051  1.00 54.83 ? 52  ASP A CA    1 
ATOM   394  C C     . ASP A 1 52  ? 27.064  12.978  9.349  1.00 52.98 ? 52  ASP A C     1 
ATOM   395  O O     . ASP A 1 52  ? 28.204  12.524  9.506  1.00 47.87 ? 52  ASP A O     1 
ATOM   396  C CB    . ASP A 1 52  ? 26.445  15.216  10.314 1.00 49.44 ? 52  ASP A CB    1 
ATOM   397  C CG    . ASP A 1 52  ? 27.637  15.698  11.118 1.00 50.31 ? 52  ASP A CG    1 
ATOM   398  O OD1   . ASP A 1 52  ? 28.560  16.294  10.522 1.00 55.49 ? 52  ASP A OD1   1 
ATOM   399  O OD2   . ASP A 1 52  ? 27.648  15.487  12.349 1.00 45.09 ? 52  ASP A OD2   1 
ATOM   400  N N     . LEU A 1 53  ? 25.976  12.208  9.423  1.00 54.54 ? 53  LEU A N     1 
ATOM   401  C CA    . LEU A 1 53  ? 26.091  10.761  9.583  1.00 46.81 ? 53  LEU A CA    1 
ATOM   402  C C     . LEU A 1 53  ? 26.809  10.136  8.393  1.00 47.24 ? 53  LEU A C     1 
ATOM   403  O O     . LEU A 1 53  ? 27.819  9.441   8.554  1.00 52.93 ? 53  LEU A O     1 
ATOM   404  C CB    . LEU A 1 53  ? 24.703  10.139  9.758  1.00 53.21 ? 53  LEU A CB    1 
ATOM   405  C CG    . LEU A 1 53  ? 24.663  8.646   10.113 1.00 67.08 ? 53  LEU A CG    1 
ATOM   406  C CD1   . LEU A 1 53  ? 25.475  8.325   11.361 1.00 64.02 ? 53  LEU A CD1   1 
ATOM   407  C CD2   . LEU A 1 53  ? 23.227  8.168   10.281 1.00 62.86 ? 53  LEU A CD2   1 
ATOM   408  N N     . SER A 1 54  ? 26.292  10.367  7.182  1.00 48.88 ? 54  SER A N     1 
ATOM   409  C CA    . SER A 1 54  ? 26.896  9.769   5.994  1.00 44.68 ? 54  SER A CA    1 
ATOM   410  C C     . SER A 1 54  ? 28.384  10.083  5.918  1.00 54.23 ? 54  SER A C     1 
ATOM   411  O O     . SER A 1 54  ? 29.198  9.208   5.601  1.00 53.00 ? 54  SER A O     1 
ATOM   412  C CB    . SER A 1 54  ? 26.182  10.264  4.735  1.00 39.65 ? 54  SER A CB    1 
ATOM   413  O OG    . SER A 1 54  ? 27.017  10.141  3.596  1.00 39.29 ? 54  SER A OG    1 
ATOM   414  N N     . ALA A 1 55  ? 28.758  11.330  6.211  1.00 56.97 ? 55  ALA A N     1 
ATOM   415  C CA    . ALA A 1 55  ? 30.170  11.695  6.220  1.00 53.08 ? 55  ALA A CA    1 
ATOM   416  C C     . ALA A 1 55  ? 30.938  10.887  7.258  1.00 56.02 ? 55  ALA A C     1 
ATOM   417  O O     . ALA A 1 55  ? 32.071  10.456  7.010  1.00 52.32 ? 55  ALA A O     1 
ATOM   418  C CB    . ALA A 1 55  ? 30.317  13.191  6.492  1.00 44.21 ? 55  ALA A CB    1 
ATOM   419  N N     . PHE A 1 56  ? 30.332  10.668  8.426  1.00 53.71 ? 56  PHE A N     1 
ATOM   420  C CA    . PHE A 1 56  ? 31.011  9.965   9.510  1.00 45.50 ? 56  PHE A CA    1 
ATOM   421  C C     . PHE A 1 56  ? 31.126  8.473   9.226  1.00 52.84 ? 56  PHE A C     1 
ATOM   422  O O     . PHE A 1 56  ? 32.037  7.814   9.741  1.00 51.91 ? 56  PHE A O     1 
ATOM   423  C CB    . PHE A 1 56  ? 30.261  10.231  10.819 1.00 48.86 ? 56  PHE A CB    1 
ATOM   424  C CG    . PHE A 1 56  ? 30.575  9.264   11.926 1.00 50.54 ? 56  PHE A CG    1 
ATOM   425  C CD1   . PHE A 1 56  ? 29.894  8.062   12.032 1.00 46.99 ? 56  PHE A CD1   1 
ATOM   426  C CD2   . PHE A 1 56  ? 31.526  9.574   12.884 1.00 52.97 ? 56  PHE A CD2   1 
ATOM   427  C CE1   . PHE A 1 56  ? 30.173  7.179   13.057 1.00 47.63 ? 56  PHE A CE1   1 
ATOM   428  C CE2   . PHE A 1 56  ? 31.807  8.695   13.913 1.00 47.10 ? 56  PHE A CE2   1 
ATOM   429  C CZ    . PHE A 1 56  ? 31.129  7.497   13.999 1.00 52.25 ? 56  PHE A CZ    1 
ATOM   430  N N     . LEU A 1 57  ? 30.222  7.923   8.413  1.00 56.00 ? 57  LEU A N     1 
ATOM   431  C CA    . LEU A 1 57  ? 30.326  6.521   8.024  1.00 58.34 ? 57  LEU A CA    1 
ATOM   432  C C     . LEU A 1 57  ? 31.377  6.328   6.939  1.00 59.47 ? 57  LEU A C     1 
ATOM   433  O O     . LEU A 1 57  ? 32.149  5.363   6.981  1.00 60.82 ? 57  LEU A O     1 
ATOM   434  C CB    . LEU A 1 57  ? 28.965  6.008   7.553  1.00 67.10 ? 57  LEU A CB    1 
ATOM   435  C CG    . LEU A 1 57  ? 27.836  6.185   8.571  1.00 59.15 ? 57  LEU A CG    1 
ATOM   436  C CD1   . LEU A 1 57  ? 26.476  5.994   7.920  1.00 58.61 ? 57  LEU A CD1   1 
ATOM   437  C CD2   . LEU A 1 57  ? 28.020  5.227   9.737  1.00 51.55 ? 57  LEU A CD2   1 
ATOM   438  N N     . LYS A 1 58  ? 31.420  7.234   5.959  1.00 57.08 ? 58  LYS A N     1 
ATOM   439  C CA    . LYS A 1 58  ? 32.498  7.206   4.977  1.00 59.65 ? 58  LYS A CA    1 
ATOM   440  C C     . LYS A 1 58  ? 33.856  7.399   5.637  1.00 53.37 ? 58  LYS A C     1 
ATOM   441  O O     . LYS A 1 58  ? 34.872  6.921   5.119  1.00 65.75 ? 58  LYS A O     1 
ATOM   442  C CB    . LYS A 1 58  ? 32.276  8.291   3.922  1.00 60.63 ? 58  LYS A CB    1 
ATOM   443  C CG    . LYS A 1 58  ? 31.168  7.993   2.925  1.00 55.00 ? 58  LYS A CG    1 
ATOM   444  C CD    . LYS A 1 58  ? 30.894  9.201   2.039  1.00 57.64 ? 58  LYS A CD    1 
ATOM   445  C CE    . LYS A 1 58  ? 29.755  8.942   1.065  1.00 63.82 ? 58  LYS A CE    1 
ATOM   446  N NZ    . LYS A 1 58  ? 30.028  7.783   0.171  1.00 63.58 ? 58  LYS A NZ    1 
ATOM   447  N N     . ALA A 1 59  ? 33.895  8.088   6.777  1.00 49.61 ? 59  ALA A N     1 
ATOM   448  C CA    . ALA A 1 59  ? 35.153  8.458   7.412  1.00 57.67 ? 59  ALA A CA    1 
ATOM   449  C C     . ALA A 1 59  ? 35.710  7.359   8.310  1.00 61.68 ? 59  ALA A C     1 
ATOM   450  O O     . ALA A 1 59  ? 36.919  7.105   8.294  1.00 59.38 ? 59  ALA A O     1 
ATOM   451  C CB    . ALA A 1 59  ? 34.969  9.742   8.226  1.00 51.55 ? 59  ALA A CB    1 
ATOM   452  N N     . VAL A 1 60  ? 34.860  6.701   9.092  1.00 60.35 ? 60  VAL A N     1 
ATOM   453  C CA    . VAL A 1 60  ? 35.317  5.702   10.056 1.00 53.26 ? 60  VAL A CA    1 
ATOM   454  C C     . VAL A 1 60  ? 35.587  4.393   9.322  1.00 53.09 ? 60  VAL A C     1 
ATOM   455  O O     . VAL A 1 60  ? 34.773  3.979   8.483  1.00 56.12 ? 60  VAL A O     1 
ATOM   456  C CB    . VAL A 1 60  ? 34.288  5.513   11.184 1.00 48.76 ? 60  VAL A CB    1 
ATOM   457  C CG1   . VAL A 1 60  ? 34.671  4.340   12.078 1.00 45.54 ? 60  VAL A CG1   1 
ATOM   458  C CG2   . VAL A 1 60  ? 34.168  6.786   12.006 1.00 49.05 ? 60  VAL A CG2   1 
ATOM   459  N N     . PRO A 1 61  ? 36.698  3.712   9.590  1.00 51.36 ? 61  PRO A N     1 
ATOM   460  C CA    . PRO A 1 61  ? 36.961  2.431   8.925  1.00 54.33 ? 61  PRO A CA    1 
ATOM   461  C C     . PRO A 1 61  ? 36.145  1.289   9.519  1.00 46.07 ? 61  PRO A C     1 
ATOM   462  O O     . PRO A 1 61  ? 35.721  1.315   10.676 1.00 48.04 ? 61  PRO A O     1 
ATOM   463  C CB    . PRO A 1 61  ? 38.463  2.210   9.142  1.00 56.85 ? 61  PRO A CB    1 
ATOM   464  C CG    . PRO A 1 61  ? 38.830  3.060   10.300 1.00 61.33 ? 61  PRO A CG    1 
ATOM   465  C CD    . PRO A 1 61  ? 37.857  4.194   10.361 1.00 56.59 ? 61  PRO A CD    1 
ATOM   466  N N     . GLU A 1 62  ? 35.948  0.261   8.689  1.00 44.06 ? 62  GLU A N     1 
ATOM   467  C CA    . GLU A 1 62  ? 34.999  -0.803  9.000  1.00 50.40 ? 62  GLU A CA    1 
ATOM   468  C C     . GLU A 1 62  ? 35.416  -1.650  10.196 1.00 54.34 ? 62  GLU A C     1 
ATOM   469  O O     . GLU A 1 62  ? 34.551  -2.259  10.834 1.00 59.13 ? 62  GLU A O     1 
ATOM   470  C CB    . GLU A 1 62  ? 34.814  -1.704  7.777  1.00 59.79 ? 62  GLU A CB    1 
ATOM   471  C CG    . GLU A 1 62  ? 33.446  -2.370  7.699  1.00 66.61 ? 62  GLU A CG    1 
ATOM   472  C CD    . GLU A 1 62  ? 33.481  -3.723  7.009  1.00 78.89 ? 62  GLU A CD    1 
ATOM   473  O OE1   . GLU A 1 62  ? 34.565  -4.135  6.544  1.00 87.19 ? 62  GLU A OE1   1 
ATOM   474  O OE2   . GLU A 1 62  ? 32.419  -4.376  6.930  1.00 77.39 ? 62  GLU A OE2   1 
ATOM   475  N N     . GLU A 1 63  ? 36.710  -1.714  10.513 1.00 58.31 ? 63  GLU A N     1 
ATOM   476  C CA    . GLU A 1 63  ? 37.160  -2.554  11.617 1.00 52.29 ? 63  GLU A CA    1 
ATOM   477  C C     . GLU A 1 63  ? 36.749  -2.011  12.979 1.00 46.37 ? 63  GLU A C     1 
ATOM   478  O O     . GLU A 1 63  ? 36.840  -2.743  13.970 1.00 45.28 ? 63  GLU A O     1 
ATOM   479  C CB    . GLU A 1 63  ? 38.681  -2.714  11.571 1.00 58.62 ? 63  GLU A CB    1 
ATOM   480  C CG    . GLU A 1 63  ? 39.444  -1.402  11.495 1.00 60.03 ? 63  GLU A CG    1 
ATOM   481  C CD    . GLU A 1 63  ? 39.959  -1.111  10.099 1.00 68.25 ? 63  GLU A CD    1 
ATOM   482  O OE1   . GLU A 1 63  ? 39.165  -1.205  9.139  1.00 69.02 ? 63  GLU A OE1   1 
ATOM   483  O OE2   . GLU A 1 63  ? 41.157  -0.788  9.962  1.00 78.33 ? 63  GLU A OE2   1 
ATOM   484  N N     . ILE A 1 64  ? 36.304  -0.761  13.053 1.00 49.67 ? 64  ILE A N     1 
ATOM   485  C CA    . ILE A 1 64  ? 35.912  -0.147  14.319 1.00 54.00 ? 64  ILE A CA    1 
ATOM   486  C C     . ILE A 1 64  ? 34.426  -0.413  14.542 1.00 51.26 ? 64  ILE A C     1 
ATOM   487  O O     . ILE A 1 64  ? 33.608  -0.105  13.663 1.00 55.01 ? 64  ILE A O     1 
ATOM   488  C CB    . ILE A 1 64  ? 36.233  1.356   14.322 1.00 50.93 ? 64  ILE A CB    1 
ATOM   489  C CG1   . ILE A 1 64  ? 37.730  1.566   14.070 1.00 45.23 ? 64  ILE A CG1   1 
ATOM   490  C CG2   . ILE A 1 64  ? 35.812  1.992   15.640 1.00 44.10 ? 64  ILE A CG2   1 
ATOM   491  C CD1   . ILE A 1 64  ? 38.129  3.005   13.835 1.00 46.82 ? 64  ILE A CD1   1 
ATOM   492  N N     . PRO A 1 65  ? 34.026  -0.987  15.680 1.00 45.46 ? 65  PRO A N     1 
ATOM   493  C CA    . PRO A 1 65  ? 32.610  -1.335  15.864 1.00 46.13 ? 65  PRO A CA    1 
ATOM   494  C C     . PRO A 1 65  ? 31.731  -0.106  16.046 1.00 50.11 ? 65  PRO A C     1 
ATOM   495  O O     . PRO A 1 65  ? 32.090  0.844   16.746 1.00 43.78 ? 65  PRO A O     1 
ATOM   496  C CB    . PRO A 1 65  ? 32.604  -2.213  17.122 1.00 55.22 ? 65  PRO A CB    1 
ATOM   497  C CG    . PRO A 1 65  ? 33.933  -2.069  17.754 1.00 56.03 ? 65  PRO A CG    1 
ATOM   498  C CD    . PRO A 1 65  ? 34.884  -1.470  16.777 1.00 54.19 ? 65  PRO A CD    1 
ATOM   499  N N     . LEU A 1 66  ? 30.562  -0.145  15.409 1.00 62.92 ? 66  LEU A N     1 
ATOM   500  C CA    . LEU A 1 66  ? 29.560  0.907   15.503 1.00 52.93 ? 66  LEU A CA    1 
ATOM   501  C C     . LEU A 1 66  ? 28.293  0.348   16.134 1.00 44.00 ? 66  LEU A C     1 
ATOM   502  O O     . LEU A 1 66  ? 27.925  -0.806  15.892 1.00 47.51 ? 66  LEU A O     1 
ATOM   503  C CB    . LEU A 1 66  ? 29.226  1.486   14.122 1.00 48.28 ? 66  LEU A CB    1 
ATOM   504  C CG    . LEU A 1 66  ? 30.374  2.075   13.301 1.00 50.31 ? 66  LEU A CG    1 
ATOM   505  C CD1   . LEU A 1 66  ? 29.851  2.595   11.973 1.00 62.36 ? 66  LEU A CD1   1 
ATOM   506  C CD2   . LEU A 1 66  ? 31.077  3.180   14.063 1.00 55.71 ? 66  LEU A CD2   1 
ATOM   507  N N     . LEU A 1 67  ? 27.628  1.171   16.943 1.00 42.57 ? 67  LEU A N     1 
ATOM   508  C CA    . LEU A 1 67  ? 26.339  0.820   17.524 1.00 43.70 ? 67  LEU A CA    1 
ATOM   509  C C     . LEU A 1 67  ? 25.438  2.042   17.482 1.00 39.37 ? 67  LEU A C     1 
ATOM   510  O O     . LEU A 1 67  ? 25.829  3.120   17.939 1.00 34.53 ? 67  LEU A O     1 
ATOM   511  C CB    . LEU A 1 67  ? 26.487  0.322   18.967 1.00 41.80 ? 67  LEU A CB    1 
ATOM   512  C CG    . LEU A 1 67  ? 25.185  0.084   19.743 1.00 46.36 ? 67  LEU A CG    1 
ATOM   513  C CD1   . LEU A 1 67  ? 24.524  -1.218  19.314 1.00 42.34 ? 67  LEU A CD1   1 
ATOM   514  C CD2   . LEU A 1 67  ? 25.449  0.086   21.239 1.00 40.58 ? 67  LEU A CD2   1 
ATOM   515  N N     . VAL A 1 68  ? 24.237  1.872   16.936 1.00 48.40 ? 68  VAL A N     1 
ATOM   516  C CA    . VAL A 1 68  ? 23.228  2.922   16.905 1.00 41.69 ? 68  VAL A CA    1 
ATOM   517  C C     . VAL A 1 68  ? 22.269  2.700   18.063 1.00 39.96 ? 68  VAL A C     1 
ATOM   518  O O     . VAL A 1 68  ? 21.806  1.575   18.291 1.00 40.37 ? 68  VAL A O     1 
ATOM   519  C CB    . VAL A 1 68  ? 22.469  2.940   15.568 1.00 34.14 ? 68  VAL A CB    1 
ATOM   520  C CG1   . VAL A 1 68  ? 21.720  4.256   15.408 1.00 34.23 ? 68  VAL A CG1   1 
ATOM   521  C CG2   . VAL A 1 68  ? 23.421  2.718   14.408 1.00 46.45 ? 68  VAL A CG2   1 
ATOM   522  N N     . VAL A 1 69  ? 21.973  3.769   18.793 1.00 42.36 ? 69  VAL A N     1 
ATOM   523  C CA    . VAL A 1 69  ? 20.973  3.744   19.849 1.00 49.74 ? 69  VAL A CA    1 
ATOM   524  C C     . VAL A 1 69  ? 20.048  4.931   19.645 1.00 46.15 ? 69  VAL A C     1 
ATOM   525  O O     . VAL A 1 69  ? 20.443  5.966   19.099 1.00 39.70 ? 69  VAL A O     1 
ATOM   526  C CB    . VAL A 1 69  ? 21.595  3.790   21.263 1.00 46.31 ? 69  VAL A CB    1 
ATOM   527  C CG1   . VAL A 1 69  ? 22.662  2.719   21.416 1.00 41.91 ? 69  VAL A CG1   1 
ATOM   528  C CG2   . VAL A 1 69  ? 22.161  5.175   21.553 1.00 46.28 ? 69  VAL A CG2   1 
ATOM   529  N N     . GLY A 1 70  ? 18.806  4.769   20.078 1.00 46.38 ? 70  GLY A N     1 
ATOM   530  C CA    . GLY A 1 70  ? 17.899  5.890   20.156 1.00 37.98 ? 70  GLY A CA    1 
ATOM   531  C C     . GLY A 1 70  ? 17.844  6.404   21.574 1.00 28.27 ? 70  GLY A C     1 
ATOM   532  O O     . GLY A 1 70  ? 18.786  7.036   22.063 1.00 36.27 ? 70  GLY A O     1 
ATOM   533  N N     . ILE A 1 71  ? 16.740  6.104   22.255 1.00 21.49 ? 71  ILE A N     1 
ATOM   534  C CA    . ILE A 1 71  ? 16.538  6.538   23.631 1.00 21.86 ? 71  ILE A CA    1 
ATOM   535  C C     . ILE A 1 71  ? 17.098  5.531   24.623 1.00 18.16 ? 71  ILE A C     1 
ATOM   536  O O     . ILE A 1 71  ? 17.154  5.823   25.828 1.00 18.69 ? 71  ILE A O     1 
ATOM   537  C CB    . ILE A 1 71  ? 15.031  6.809   23.817 1.00 25.90 ? 71  ILE A CB    1 
ATOM   538  C CG1   . ILE A 1 71  ? 14.639  8.083   23.057 1.00 26.00 ? 71  ILE A CG1   1 
ATOM   539  C CG2   . ILE A 1 71  ? 14.646  6.926   25.287 1.00 26.18 ? 71  ILE A CG2   1 
ATOM   540  C CD1   . ILE A 1 71  ? 14.532  7.913   21.545 1.00 37.77 ? 71  ILE A CD1   1 
ATOM   541  N N     . GLY A 1 72  ? 17.543  4.370   24.155 1.00 28.24 ? 72  GLY A N     1 
ATOM   542  C CA    . GLY A 1 72  ? 18.113  3.374   25.042 1.00 18.77 ? 72  GLY A CA    1 
ATOM   543  C C     . GLY A 1 72  ? 17.114  2.822   26.031 1.00 17.16 ? 72  GLY A C     1 
ATOM   544  O O     . GLY A 1 72  ? 17.440  2.661   27.214 1.00 20.77 ? 72  GLY A O     1 
ATOM   545  N N     . SER A 1 73  ? 15.896  2.537   25.577 1.00 28.02 ? 73  SER A N     1 
ATOM   546  C CA    . SER A 1 73  ? 14.858  1.964   26.421 1.00 31.13 ? 73  SER A CA    1 
ATOM   547  C C     . SER A 1 73  ? 14.745  0.454   26.265 1.00 25.15 ? 73  SER A C     1 
ATOM   548  O O     . SER A 1 73  ? 13.912  -0.163  26.937 1.00 27.71 ? 73  SER A O     1 
ATOM   549  C CB    . SER A 1 73  ? 13.509  2.623   26.115 1.00 22.85 ? 73  SER A CB    1 
ATOM   550  O OG    . SER A 1 73  ? 13.154  2.457   24.754 1.00 28.06 ? 73  SER A OG    1 
ATOM   551  N N     . ASN A 1 74  ? 15.563  -0.156  25.400 1.00 28.44 ? 74  ASN A N     1 
ATOM   552  C CA    . ASN A 1 74  ? 15.578  -1.604  25.225 1.00 32.85 ? 74  ASN A CA    1 
ATOM   553  C C     . ASN A 1 74  ? 16.984  -2.179  25.355 1.00 35.86 ? 74  ASN A C     1 
ATOM   554  O O     . ASN A 1 74  ? 17.261  -3.250  24.805 1.00 23.57 ? 74  ASN A O     1 
ATOM   555  C CB    . ASN A 1 74  ? 14.989  -1.992  23.867 1.00 24.78 ? 74  ASN A CB    1 
ATOM   556  C CG    . ASN A 1 74  ? 14.497  -3.427  23.835 1.00 27.26 ? 74  ASN A CG    1 
ATOM   557  O OD1   . ASN A 1 74  ? 13.760  -3.861  24.720 1.00 32.95 ? 74  ASN A OD1   1 
ATOM   558  N ND2   . ASN A 1 74  ? 14.909  -4.173  22.817 1.00 28.20 ? 74  ASN A ND2   1 
ATOM   559  N N     . LEU A 1 75  ? 17.878  -1.501  26.074 1.00 46.34 ? 75  LEU A N     1 
ATOM   560  C CA    . LEU A 1 75  ? 19.282  -1.885  26.142 1.00 27.73 ? 75  LEU A CA    1 
ATOM   561  C C     . LEU A 1 75  ? 19.707  -2.104  27.587 1.00 26.11 ? 75  LEU A C     1 
ATOM   562  O O     . LEU A 1 75  ? 19.469  -1.250  28.448 1.00 19.31 ? 75  LEU A O     1 
ATOM   563  C CB    . LEU A 1 75  ? 20.169  -0.819  25.493 1.00 23.35 ? 75  LEU A CB    1 
ATOM   564  C CG    . LEU A 1 75  ? 19.844  -0.466  24.039 1.00 25.28 ? 75  LEU A CG    1 
ATOM   565  C CD1   . LEU A 1 75  ? 20.856  0.530   23.496 1.00 35.82 ? 75  LEU A CD1   1 
ATOM   566  C CD2   . LEU A 1 75  ? 19.802  -1.711  23.168 1.00 28.08 ? 75  LEU A CD2   1 
ATOM   567  N N     . LEU A 1 76  ? 20.335  -3.252  27.842 1.00 30.73 ? 76  LEU A N     1 
ATOM   568  C CA    . LEU A 1 76  ? 21.008  -3.552  29.104 1.00 30.99 ? 76  LEU A CA    1 
ATOM   569  C C     . LEU A 1 76  ? 22.504  -3.562  28.808 1.00 33.53 ? 76  LEU A C     1 
ATOM   570  O O     . LEU A 1 76  ? 23.024  -4.520  28.228 1.00 35.53 ? 76  LEU A O     1 
ATOM   571  C CB    . LEU A 1 76  ? 20.542  -4.888  29.676 1.00 29.79 ? 76  LEU A CB    1 
ATOM   572  C CG    . LEU A 1 76  ? 20.844  -5.155  31.154 1.00 42.58 ? 76  LEU A CG    1 
ATOM   573  C CD1   . LEU A 1 76  ? 19.890  -6.209  31.691 1.00 36.04 ? 76  LEU A CD1   1 
ATOM   574  C CD2   . LEU A 1 76  ? 22.294  -5.584  31.366 1.00 45.93 ? 76  LEU A CD2   1 
ATOM   575  N N     . VAL A 1 77  ? 23.191  -2.496  29.201 1.00 32.62 ? 77  VAL A N     1 
ATOM   576  C CA    . VAL A 1 77  ? 24.604  -2.320  28.885 1.00 30.84 ? 77  VAL A CA    1 
ATOM   577  C C     . VAL A 1 77  ? 25.442  -2.858  30.037 1.00 24.22 ? 77  VAL A C     1 
ATOM   578  O O     . VAL A 1 77  ? 25.153  -2.589  31.209 1.00 27.22 ? 77  VAL A O     1 
ATOM   579  C CB    . VAL A 1 77  ? 24.918  -0.841  28.604 1.00 34.05 ? 77  VAL A CB    1 
ATOM   580  C CG1   . VAL A 1 77  ? 26.397  -0.649  28.294 1.00 36.87 ? 77  VAL A CG1   1 
ATOM   581  C CG2   . VAL A 1 77  ? 24.060  -0.339  27.453 1.00 32.62 ? 77  VAL A CG2   1 
ATOM   582  N N     . ARG A 1 78  ? 26.476  -3.625  29.703 1.00 27.34 ? 78  ARG A N     1 
ATOM   583  C CA    . ARG A 1 78  ? 27.340  -4.219  30.709 1.00 27.32 ? 78  ARG A CA    1 
ATOM   584  C C     . ARG A 1 78  ? 28.345  -3.192  31.226 1.00 26.49 ? 78  ARG A C     1 
ATOM   585  O O     . ARG A 1 78  ? 28.642  -2.187  30.575 1.00 23.79 ? 78  ARG A O     1 
ATOM   586  C CB    . ARG A 1 78  ? 28.056  -5.442  30.135 1.00 30.52 ? 78  ARG A CB    1 
ATOM   587  C CG    . ARG A 1 78  ? 27.159  -6.669  30.046 1.00 28.61 ? 78  ARG A CG    1 
ATOM   588  C CD    . ARG A 1 78  ? 27.702  -7.729  29.101 1.00 26.36 ? 78  ARG A CD    1 
ATOM   589  N NE    . ARG A 1 78  ? 26.724  -8.790  28.887 1.00 25.77 ? 78  ARG A NE    1 
ATOM   590  C CZ    . ARG A 1 78  ? 26.488  -9.389  27.726 1.00 22.07 ? 78  ARG A CZ    1 
ATOM   591  N NH1   . ARG A 1 78  ? 27.168  -9.079  26.633 1.00 23.28 ? 78  ARG A NH1   1 
ATOM   592  N NH2   . ARG A 1 78  ? 25.545  -10.324 27.659 1.00 39.47 ? 78  ARG A NH2   1 
ATOM   593  N N     . ASP A 1 79  ? 28.874  -3.463  32.422 1.00 30.49 ? 79  ASP A N     1 
ATOM   594  C CA    . ASP A 1 79  ? 29.679  -2.480  33.139 1.00 24.80 ? 79  ASP A CA    1 
ATOM   595  C C     . ASP A 1 79  ? 31.065  -2.280  32.542 1.00 27.99 ? 79  ASP A C     1 
ATOM   596  O O     . ASP A 1 79  ? 31.793  -1.395  33.005 1.00 22.02 ? 79  ASP A O     1 
ATOM   597  C CB    . ASP A 1 79  ? 29.812  -2.891  34.606 1.00 27.13 ? 79  ASP A CB    1 
ATOM   598  C CG    . ASP A 1 79  ? 28.470  -3.057  35.286 1.00 33.55 ? 79  ASP A CG    1 
ATOM   599  O OD1   . ASP A 1 79  ? 27.641  -2.127  35.196 1.00 35.70 ? 79  ASP A OD1   1 
ATOM   600  O OD2   . ASP A 1 79  ? 28.245  -4.113  35.912 1.00 36.92 ? 79  ASP A OD2   1 
ATOM   601  N N     . GLY A 1 80  ? 31.450  -3.069  31.543 1.00 27.75 ? 80  GLY A N     1 
ATOM   602  C CA    . GLY A 1 80  ? 32.733  -2.884  30.895 1.00 32.28 ? 80  GLY A CA    1 
ATOM   603  C C     . GLY A 1 80  ? 32.673  -1.874  29.768 1.00 33.41 ? 80  GLY A C     1 
ATOM   604  O O     . GLY A 1 80  ? 33.707  -1.355  29.339 1.00 37.58 ? 80  GLY A O     1 
ATOM   605  N N     . GLY A 1 81  ? 31.474  -1.592  29.278 1.00 32.14 ? 81  GLY A N     1 
ATOM   606  C CA    . GLY A 1 81  ? 31.280  -0.567  28.273 1.00 26.68 ? 81  GLY A CA    1 
ATOM   607  C C     . GLY A 1 81  ? 31.186  -1.128  26.869 1.00 23.84 ? 81  GLY A C     1 
ATOM   608  O O     . GLY A 1 81  ? 31.091  -2.337  26.639 1.00 26.25 ? 81  GLY A O     1 
ATOM   609  N N     . VAL A 1 82  ? 31.230  -0.207  25.910 1.00 30.94 ? 82  VAL A N     1 
ATOM   610  C CA    . VAL A 1 82  ? 31.024  -0.527  24.499 1.00 34.66 ? 82  VAL A CA    1 
ATOM   611  C C     . VAL A 1 82  ? 32.202  -0.005  23.682 1.00 37.21 ? 82  VAL A C     1 
ATOM   612  O O     . VAL A 1 82  ? 32.387  1.217   23.581 1.00 36.70 ? 82  VAL A O     1 
ATOM   613  C CB    . VAL A 1 82  ? 29.700  0.066   23.992 1.00 33.12 ? 82  VAL A CB    1 
ATOM   614  C CG1   . VAL A 1 82  ? 29.342  -0.509  22.630 1.00 19.86 ? 82  VAL A CG1   1 
ATOM   615  C CG2   . VAL A 1 82  ? 28.587  -0.190  24.999 1.00 31.07 ? 82  VAL A CG2   1 
ATOM   616  N N     . PRO A 1 83  ? 33.022  -0.873  23.090 1.00 35.48 ? 83  PRO A N     1 
ATOM   617  C CA    . PRO A 1 83  ? 34.124  -0.388  22.252 1.00 38.59 ? 83  PRO A CA    1 
ATOM   618  C C     . PRO A 1 83  ? 33.626  0.246   20.962 1.00 44.59 ? 83  PRO A C     1 
ATOM   619  O O     . PRO A 1 83  ? 32.508  0.004   20.499 1.00 45.42 ? 83  PRO A O     1 
ATOM   620  C CB    . PRO A 1 83  ? 34.943  -1.652  21.962 1.00 45.96 ? 83  PRO A CB    1 
ATOM   621  C CG    . PRO A 1 83  ? 34.538  -2.632  23.003 1.00 40.59 ? 83  PRO A CG    1 
ATOM   622  C CD    . PRO A 1 83  ? 33.114  -2.323  23.331 1.00 37.43 ? 83  PRO A CD    1 
ATOM   623  N N     . GLY A 1 84  ? 34.494  1.065   20.375 1.00 53.33 ? 84  GLY A N     1 
ATOM   624  C CA    . GLY A 1 84  ? 34.183  1.736   19.129 1.00 50.20 ? 84  GLY A CA    1 
ATOM   625  C C     . GLY A 1 84  ? 33.299  2.948   19.326 1.00 42.26 ? 84  GLY A C     1 
ATOM   626  O O     . GLY A 1 84  ? 33.444  3.675   20.313 1.00 35.78 ? 84  GLY A O     1 
ATOM   627  N N     . PHE A 1 85  ? 32.376  3.175   18.397 1.00 48.57 ? 85  PHE A N     1 
ATOM   628  C CA    . PHE A 1 85  ? 31.524  4.354   18.409 1.00 49.01 ? 85  PHE A CA    1 
ATOM   629  C C     . PHE A 1 85  ? 30.087  3.978   18.737 1.00 46.88 ? 85  PHE A C     1 
ATOM   630  O O     . PHE A 1 85  ? 29.604  2.912   18.342 1.00 45.69 ? 85  PHE A O     1 
ATOM   631  C CB    . PHE A 1 85  ? 31.566  5.074   17.059 1.00 50.20 ? 85  PHE A CB    1 
ATOM   632  C CG    . PHE A 1 85  ? 32.776  5.936   16.873 1.00 59.63 ? 85  PHE A CG    1 
ATOM   633  C CD1   . PHE A 1 85  ? 32.798  7.231   17.359 1.00 52.28 ? 85  PHE A CD1   1 
ATOM   634  C CD2   . PHE A 1 85  ? 33.893  5.451   16.217 1.00 59.45 ? 85  PHE A CD2   1 
ATOM   635  C CE1   . PHE A 1 85  ? 33.912  8.028   17.192 1.00 65.61 ? 85  PHE A CE1   1 
ATOM   636  C CE2   . PHE A 1 85  ? 35.011  6.243   16.046 1.00 56.90 ? 85  PHE A CE2   1 
ATOM   637  C CZ    . PHE A 1 85  ? 35.021  7.534   16.535 1.00 58.19 ? 85  PHE A CZ    1 
ATOM   638  N N     . VAL A 1 86  ? 29.417  4.865   19.466 1.00 50.34 ? 86  VAL A N     1 
ATOM   639  C CA    . VAL A 1 86  ? 27.985  4.783   19.722 1.00 42.78 ? 86  VAL A CA    1 
ATOM   640  C C     . VAL A 1 86  ? 27.339  5.994   19.068 1.00 36.60 ? 86  VAL A C     1 
ATOM   641  O O     . VAL A 1 86  ? 27.735  7.134   19.336 1.00 36.59 ? 86  VAL A O     1 
ATOM   642  C CB    . VAL A 1 86  ? 27.675  4.742   21.229 1.00 42.15 ? 86  VAL A CB    1 
ATOM   643  C CG1   . VAL A 1 86  ? 26.171  4.777   21.464 1.00 44.41 ? 86  VAL A CG1   1 
ATOM   644  C CG2   . VAL A 1 86  ? 28.293  3.507   21.862 1.00 40.72 ? 86  VAL A CG2   1 
ATOM   645  N N     . VAL A 1 87  ? 26.357  5.749   18.208 1.00 43.09 ? 87  VAL A N     1 
ATOM   646  C CA    . VAL A 1 87  ? 25.712  6.797   17.427 1.00 35.84 ? 87  VAL A CA    1 
ATOM   647  C C     . VAL A 1 87  ? 24.307  6.997   17.972 1.00 33.26 ? 87  VAL A C     1 
ATOM   648  O O     . VAL A 1 87  ? 23.490  6.067   17.960 1.00 39.02 ? 87  VAL A O     1 
ATOM   649  C CB    . VAL A 1 87  ? 25.681  6.447   15.931 1.00 36.81 ? 87  VAL A CB    1 
ATOM   650  C CG1   . VAL A 1 87  ? 24.683  7.331   15.193 1.00 52.20 ? 87  VAL A CG1   1 
ATOM   651  C CG2   . VAL A 1 87  ? 27.069  6.585   15.330 1.00 47.05 ? 87  VAL A CG2   1 
ATOM   652  N N     . ARG A 1 88  ? 24.028  8.204   18.459 1.00 34.94 ? 88  ARG A N     1 
ATOM   653  C CA    . ARG A 1 88  ? 22.673  8.621   18.802 1.00 41.65 ? 88  ARG A CA    1 
ATOM   654  C C     . ARG A 1 88  ? 22.335  9.825   17.937 1.00 39.72 ? 88  ARG A C     1 
ATOM   655  O O     . ARG A 1 88  ? 22.838  10.929  18.175 1.00 48.88 ? 88  ARG A O     1 
ATOM   656  C CB    . ARG A 1 88  ? 22.527  8.956   20.285 1.00 45.23 ? 88  ARG A CB    1 
ATOM   657  C CG    . ARG A 1 88  ? 21.063  9.040   20.696 1.00 34.81 ? 88  ARG A CG    1 
ATOM   658  C CD    . ARG A 1 88  ? 20.858  9.352   22.165 1.00 31.96 ? 88  ARG A CD    1 
ATOM   659  N NE    . ARG A 1 88  ? 21.191  10.731  22.498 1.00 24.40 ? 88  ARG A NE    1 
ATOM   660  C CZ    . ARG A 1 88  ? 21.227  11.209  23.734 1.00 26.06 ? 88  ARG A CZ    1 
ATOM   661  N NH1   . ARG A 1 88  ? 20.922  10.453  24.776 1.00 26.93 ? 88  ARG A NH1   1 
ATOM   662  N NH2   . ARG A 1 88  ? 21.563  12.480  23.928 1.00 34.34 ? 88  ARG A NH2   1 
ATOM   663  N N     . LEU A 1 89  ? 21.486  9.611   16.938 1.00 44.07 ? 89  LEU A N     1 
ATOM   664  C CA    . LEU A 1 89  ? 21.155  10.674  16.003 1.00 40.57 ? 89  LEU A CA    1 
ATOM   665  C C     . LEU A 1 89  ? 20.525  11.849  16.742 1.00 37.01 ? 89  LEU A C     1 
ATOM   666  O O     . LEU A 1 89  ? 19.890  11.688  17.788 1.00 39.74 ? 89  LEU A O     1 
ATOM   667  C CB    . LEU A 1 89  ? 20.207  10.155  14.922 1.00 51.50 ? 89  LEU A CB    1 
ATOM   668  C CG    . LEU A 1 89  ? 20.504  8.791   14.298 1.00 53.52 ? 89  LEU A CG    1 
ATOM   669  C CD1   . LEU A 1 89  ? 19.288  8.322   13.523 1.00 52.93 ? 89  LEU A CD1   1 
ATOM   670  C CD2   . LEU A 1 89  ? 21.720  8.866   13.394 1.00 43.53 ? 89  LEU A CD2   1 
ATOM   671  N N     . SER A 1 90  ? 20.705  13.046  16.189 1.00 36.87 ? 90  SER A N     1 
ATOM   672  C CA    . SER A 1 90  ? 20.284  14.258  16.875 1.00 33.97 ? 90  SER A CA    1 
ATOM   673  C C     . SER A 1 90  ? 18.775  14.432  16.796 1.00 38.62 ? 90  SER A C     1 
ATOM   674  O O     . SER A 1 90  ? 18.156  14.198  15.753 1.00 37.42 ? 90  SER A O     1 
ATOM   675  C CB    . SER A 1 90  ? 20.976  15.486  16.280 1.00 30.65 ? 90  SER A CB    1 
ATOM   676  O OG    . SER A 1 90  ? 20.741  15.587  14.887 1.00 51.54 ? 90  SER A OG    1 
ATOM   677  N N     . ALA A 1 91  ? 18.185  14.844  17.918 1.00 44.52 ? 91  ALA A N     1 
ATOM   678  C CA    . ALA A 1 91  ? 16.768  15.186  17.937 1.00 43.36 ? 91  ALA A CA    1 
ATOM   679  C C     . ALA A 1 91  ? 16.456  16.253  16.895 1.00 51.27 ? 91  ALA A C     1 
ATOM   680  O O     . ALA A 1 91  ? 15.585  16.070  16.037 1.00 57.66 ? 91  ALA A O     1 
ATOM   681  C CB    . ALA A 1 91  ? 16.374  15.660  19.336 1.00 35.17 ? 91  ALA A CB    1 
ATOM   682  N N     . LYS A 1 92  ? 17.169  17.381  16.956 1.00 43.42 ? 92  LYS A N     1 
ATOM   683  C CA    . LYS A 1 92  ? 16.936  18.467  16.007 1.00 45.11 ? 92  LYS A CA    1 
ATOM   684  C C     . LYS A 1 92  ? 17.052  17.986  14.567 1.00 49.80 ? 92  LYS A C     1 
ATOM   685  O O     . LYS A 1 92  ? 16.299  18.430  13.692 1.00 62.48 ? 92  LYS A O     1 
ATOM   686  C CB    . LYS A 1 92  ? 17.927  19.604  16.260 1.00 51.08 ? 92  LYS A CB    1 
ATOM   687  C CG    . LYS A 1 92  ? 17.726  20.820  15.358 1.00 57.51 ? 92  LYS A CG    1 
ATOM   688  C CD    . LYS A 1 92  ? 18.683  20.817  14.167 1.00 67.12 ? 92  LYS A CD    1 
ATOM   689  C CE    . LYS A 1 92  ? 18.035  21.420  12.926 1.00 72.50 ? 92  LYS A CE    1 
ATOM   690  N NZ    . LYS A 1 92  ? 19.041  21.823  11.902 1.00 59.74 ? 92  LYS A NZ    1 
ATOM   691  N N     . GLY A 1 93  ? 17.993  17.079  14.300 1.00 42.25 ? 93  GLY A N     1 
ATOM   692  C CA    . GLY A 1 93  ? 18.248  16.673  12.931 1.00 43.63 ? 93  GLY A CA    1 
ATOM   693  C C     . GLY A 1 93  ? 17.330  15.582  12.430 1.00 48.64 ? 93  GLY A C     1 
ATOM   694  O O     . GLY A 1 93  ? 16.997  15.551  11.241 1.00 44.52 ? 93  GLY A O     1 
ATOM   695  N N     . PHE A 1 94  ? 16.903  14.680  13.317 1.00 44.14 ? 94  PHE A N     1 
ATOM   696  C CA    . PHE A 1 94  ? 16.171  13.486  12.912 1.00 48.62 ? 94  PHE A CA    1 
ATOM   697  C C     . PHE A 1 94  ? 14.878  13.300  13.700 1.00 43.22 ? 94  PHE A C     1 
ATOM   698  O O     . PHE A 1 94  ? 14.347  12.186  13.742 1.00 50.18 ? 94  PHE A O     1 
ATOM   699  C CB    . PHE A 1 94  ? 17.043  12.239  13.078 1.00 47.95 ? 94  PHE A CB    1 
ATOM   700  C CG    . PHE A 1 94  ? 18.407  12.348  12.451 1.00 43.61 ? 94  PHE A CG    1 
ATOM   701  C CD1   . PHE A 1 94  ? 19.448  12.971  13.121 1.00 40.53 ? 94  PHE A CD1   1 
ATOM   702  C CD2   . PHE A 1 94  ? 18.655  11.797  11.205 1.00 52.12 ? 94  PHE A CD2   1 
ATOM   703  C CE1   . PHE A 1 94  ? 20.705  13.052  12.554 1.00 42.08 ? 94  PHE A CE1   1 
ATOM   704  C CE2   . PHE A 1 94  ? 19.910  11.879  10.633 1.00 54.99 ? 94  PHE A CE2   1 
ATOM   705  C CZ    . PHE A 1 94  ? 20.936  12.506  11.309 1.00 49.93 ? 94  PHE A CZ    1 
ATOM   706  N N     . GLY A 1 95  ? 14.363  14.349  14.334 1.00 43.88 ? 95  GLY A N     1 
ATOM   707  C CA    . GLY A 1 95  ? 13.161  14.250  15.134 1.00 43.02 ? 95  GLY A CA    1 
ATOM   708  C C     . GLY A 1 95  ? 11.909  14.815  14.501 1.00 49.99 ? 95  GLY A C     1 
ATOM   709  O O     . GLY A 1 95  ? 10.871  14.873  15.171 1.00 41.29 ? 95  GLY A O     1 
ATOM   710  N N     . GLU A 1 96  ? 11.960  15.221  13.236 1.00 45.72 ? 96  GLU A N     1 
ATOM   711  C CA    . GLU A 1 96  ? 10.825  15.895  12.622 1.00 47.66 ? 96  GLU A CA    1 
ATOM   712  C C     . GLU A 1 96  ? 9.706   14.913  12.304 1.00 50.14 ? 96  GLU A C     1 
ATOM   713  O O     . GLU A 1 96  ? 9.945   13.810  11.805 1.00 49.14 ? 96  GLU A O     1 
ATOM   714  C CB    . GLU A 1 96  ? 11.255  16.606  11.342 1.00 65.19 ? 96  GLU A CB    1 
ATOM   715  C CG    . GLU A 1 96  ? 12.018  17.896  11.562 1.00 68.17 ? 96  GLU A CG    1 
ATOM   716  C CD    . GLU A 1 96  ? 12.349  18.592  10.257 1.00 79.11 ? 96  GLU A CD    1 
ATOM   717  O OE1   . GLU A 1 96  ? 12.465  17.896  9.226  1.00 67.78 ? 96  GLU A OE1   1 
ATOM   718  O OE2   . GLU A 1 96  ? 12.487  19.833  10.259 1.00 80.24 ? 96  GLU A OE2   1 
ATOM   719  N N     . VAL A 1 97  ? 8.474   15.333  12.583 1.00 59.46 ? 97  VAL A N     1 
ATOM   720  C CA    . VAL A 1 97  ? 7.271   14.575  12.259 1.00 50.02 ? 97  VAL A CA    1 
ATOM   721  C C     . VAL A 1 97  ? 6.332   15.510  11.512 1.00 56.81 ? 97  VAL A C     1 
ATOM   722  O O     . VAL A 1 97  ? 5.876   16.513  12.076 1.00 53.08 ? 97  VAL A O     1 
ATOM   723  C CB    . VAL A 1 97  ? 6.586   14.011  13.515 1.00 46.59 ? 97  VAL A CB    1 
ATOM   724  C CG1   . VAL A 1 97  ? 5.368   13.183  13.131 1.00 49.39 ? 97  VAL A CG1   1 
ATOM   725  C CG2   . VAL A 1 97  ? 7.568   13.191  14.335 1.00 48.36 ? 97  VAL A CG2   1 
ATOM   726  N N     . GLU A 1 98  ? 6.046   15.192  10.251 1.00 58.20 ? 98  GLU A N     1 
ATOM   727  C CA    . GLU A 1 98  ? 5.200   16.039  9.424  1.00 58.29 ? 98  GLU A CA    1 
ATOM   728  C C     . GLU A 1 98  ? 4.219   15.187  8.635  1.00 50.33 ? 98  GLU A C     1 
ATOM   729  O O     . GLU A 1 98  ? 4.516   14.049  8.260  1.00 51.97 ? 98  GLU A O     1 
ATOM   730  C CB    . GLU A 1 98  ? 6.020   16.897  8.447  1.00 61.52 ? 98  GLU A CB    1 
ATOM   731  C CG    . GLU A 1 98  ? 7.436   17.210  8.904  1.00 72.44 ? 98  GLU A CG    1 
ATOM   732  C CD    . GLU A 1 98  ? 7.945   18.527  8.353  1.00 77.90 ? 98  GLU A CD    1 
ATOM   733  O OE1   . GLU A 1 98  ? 7.648   18.837  7.180  1.00 69.69 ? 98  GLU A OE1   1 
ATOM   734  O OE2   . GLU A 1 98  ? 8.640   19.254  9.094  1.00 76.82 ? 98  GLU A OE2   1 
ATOM   735  N N     . GLN A 1 99  ? 3.043   15.756  8.389  1.00 52.19 ? 99  GLN A N     1 
ATOM   736  C CA    . GLN A 1 99  ? 2.075   15.145  7.494  1.00 59.27 ? 99  GLN A CA    1 
ATOM   737  C C     . GLN A 1 99  ? 2.403   15.522  6.056  1.00 55.72 ? 99  GLN A C     1 
ATOM   738  O O     . GLN A 1 99  ? 2.775   16.663  5.765  1.00 50.66 ? 99  GLN A O     1 
ATOM   739  C CB    . GLN A 1 99  ? 0.657   15.592  7.849  1.00 59.95 ? 99  GLN A CB    1 
ATOM   740  C CG    . GLN A 1 99  ? -0.432  14.612  7.434  1.00 63.45 ? 99  GLN A CG    1 
ATOM   741  C CD    . GLN A 1 99  ? -1.821  15.217  7.514  1.00 65.06 ? 99  GLN A CD    1 
ATOM   742  O OE1   . GLN A 1 99  ? -1.980  16.391  7.846  1.00 53.12 ? 99  GLN A OE1   1 
ATOM   743  N NE2   . GLN A 1 99  ? -2.835  14.414  7.210  1.00 68.54 ? 99  GLN A NE2   1 
ATOM   744  N N     . VAL A 1 100 ? 2.265   14.552  5.157  1.00 55.37 ? 100 VAL A N     1 
ATOM   745  C CA    . VAL A 1 100 ? 2.617   14.739  3.762  1.00 67.85 ? 100 VAL A CA    1 
ATOM   746  C C     . VAL A 1 100 ? 1.392   14.774  2.860  1.00 71.23 ? 100 VAL A C     1 
ATOM   747  O O     . VAL A 1 100 ? 1.405   15.477  1.842  1.00 63.72 ? 100 VAL A O     1 
ATOM   748  C CB    . VAL A 1 100 ? 3.594   13.635  3.311  1.00 64.50 ? 100 VAL A CB    1 
ATOM   749  C CG1   . VAL A 1 100 ? 4.775   13.566  4.262  1.00 60.71 ? 100 VAL A CG1   1 
ATOM   750  C CG2   . VAL A 1 100 ? 2.881   12.290  3.242  1.00 60.68 ? 100 VAL A CG2   1 
ATOM   751  N N     . CYS A 1 101 ? 0.338   14.039  3.201  1.00 61.75 ? 101 CYS A N     1 
ATOM   752  C CA    . CYS A 1 101 ? -0.904  14.080  2.449  1.00 63.45 ? 101 CYS A CA    1 
ATOM   753  C C     . CYS A 1 101 ? -2.072  14.022  3.425  1.00 66.04 ? 101 CYS A C     1 
ATOM   754  O O     . CYS A 1 101 ? -2.145  14.846  4.342  1.00 68.76 ? 101 CYS A O     1 
ATOM   755  C CB    . CYS A 1 101 ? -0.931  12.945  1.430  1.00 67.83 ? 101 CYS A CB    1 
ATOM   756  S SG    . CYS A 1 101 ? -0.753  11.274  2.057  1.00 65.75 ? 101 CYS A SG    1 
ATOM   757  N N     . ASP A 1 102 ? -2.982  13.065  3.258  1.00 71.38 ? 102 ASP A N     1 
ATOM   758  C CA    . ASP A 1 102 ? -4.143  12.963  4.130  1.00 70.67 ? 102 ASP A CA    1 
ATOM   759  C C     . ASP A 1 102 ? -4.215  11.638  4.869  1.00 60.90 ? 102 ASP A C     1 
ATOM   760  O O     . ASP A 1 102 ? -5.129  11.443  5.680  1.00 60.41 ? 102 ASP A O     1 
ATOM   761  C CB    . ASP A 1 102 ? -5.427  13.176  3.320  1.00 75.51 ? 102 ASP A CB    1 
ATOM   762  C CG    . ASP A 1 102 ? -5.982  14.577  3.477  1.00 84.86 ? 102 ASP A CG    1 
ATOM   763  O OD1   . ASP A 1 102 ? -6.285  14.970  4.624  1.00 79.83 ? 102 ASP A OD1   1 
ATOM   764  O OD2   . ASP A 1 102 ? -6.111  15.285  2.457  1.00 85.33 ? 102 ASP A OD2   1 
ATOM   765  N N     . THR A 1 103 ? -3.274  10.730  4.621  1.00 61.45 ? 103 THR A N     1 
ATOM   766  C CA    . THR A 1 103 ? -3.228  9.443   5.291  1.00 62.01 ? 103 THR A CA    1 
ATOM   767  C C     . THR A 1 103 ? -1.835  9.078   5.774  1.00 60.53 ? 103 THR A C     1 
ATOM   768  O O     . THR A 1 103 ? -1.688  8.052   6.446  1.00 61.81 ? 103 THR A O     1 
ATOM   769  C CB    . THR A 1 103 ? -3.728  8.333   4.354  1.00 53.36 ? 103 THR A CB    1 
ATOM   770  O OG1   . THR A 1 103 ? -3.428  7.051   4.919  1.00 59.18 ? 103 THR A OG1   1 
ATOM   771  C CG2   . THR A 1 103 ? -3.059  8.449   2.990  1.00 60.05 ? 103 THR A CG2   1 
ATOM   772  N N     . GLN A 1 104 ? -0.819  9.883   5.469  1.00 61.91 ? 104 GLN A N     1 
ATOM   773  C CA    . GLN A 1 104 ? 0.569   9.497   5.661  1.00 60.51 ? 104 GLN A CA    1 
ATOM   774  C C     . GLN A 1 104 ? 1.311   10.507  6.524  1.00 60.81 ? 104 GLN A C     1 
ATOM   775  O O     . GLN A 1 104 ? 1.004   11.704  6.524  1.00 67.42 ? 104 GLN A O     1 
ATOM   776  C CB    . GLN A 1 104 ? 1.284   9.356   4.312  1.00 52.74 ? 104 GLN A CB    1 
ATOM   777  C CG    . GLN A 1 104 ? 0.998   8.046   3.602  1.00 50.04 ? 104 GLN A CG    1 
ATOM   778  C CD    . GLN A 1 104 ? 1.768   7.902   2.307  1.00 56.81 ? 104 GLN A CD    1 
ATOM   779  O OE1   . GLN A 1 104 ? 2.299   8.876   1.774  1.00 55.94 ? 104 GLN A OE1   1 
ATOM   780  N NE2   . GLN A 1 104 ? 1.837   6.679   1.795  1.00 56.72 ? 104 GLN A NE2   1 
ATOM   781  N N     . LEU A 1 105 ? 2.304   10.001  7.255  1.00 56.87 ? 105 LEU A N     1 
ATOM   782  C CA    . LEU A 1 105 ? 3.180   10.802  8.097  1.00 57.50 ? 105 LEU A CA    1 
ATOM   783  C C     . LEU A 1 105 ? 4.625   10.423  7.812  1.00 51.95 ? 105 LEU A C     1 
ATOM   784  O O     . LEU A 1 105 ? 4.937   9.244   7.619  1.00 52.31 ? 105 LEU A O     1 
ATOM   785  C CB    . LEU A 1 105 ? 2.899   10.578  9.589  1.00 50.56 ? 105 LEU A CB    1 
ATOM   786  C CG    . LEU A 1 105 ? 1.528   10.906  10.177 1.00 51.54 ? 105 LEU A CG    1 
ATOM   787  C CD1   . LEU A 1 105 ? 1.550   10.576  11.662 1.00 52.91 ? 105 LEU A CD1   1 
ATOM   788  C CD2   . LEU A 1 105 ? 1.157   12.359  9.956  1.00 54.84 ? 105 LEU A CD2   1 
ATOM   789  N N     . ARG A 1 106 ? 5.506   11.419  7.797  1.00 49.28 ? 106 ARG A N     1 
ATOM   790  C CA    . ARG A 1 106 ? 6.943   11.194  7.722  1.00 52.33 ? 106 ARG A CA    1 
ATOM   791  C C     . ARG A 1 106 ? 7.571   11.566  9.057  1.00 54.52 ? 106 ARG A C     1 
ATOM   792  O O     . ARG A 1 106 ? 7.298   12.644  9.596  1.00 51.22 ? 106 ARG A O     1 
ATOM   793  C CB    . ARG A 1 106 ? 7.582   12.007  6.596  1.00 48.38 ? 106 ARG A CB    1 
ATOM   794  C CG    . ARG A 1 106 ? 9.061   11.702  6.407  1.00 50.61 ? 106 ARG A CG    1 
ATOM   795  C CD    . ARG A 1 106 ? 9.690   12.551  5.310  1.00 68.83 ? 106 ARG A CD    1 
ATOM   796  N NE    . ARG A 1 106 ? 8.858   12.648  4.116  1.00 64.18 ? 106 ARG A NE    1 
ATOM   797  C CZ    . ARG A 1 106 ? 8.482   11.619  3.366  1.00 69.67 ? 106 ARG A CZ    1 
ATOM   798  N NH1   . ARG A 1 106 ? 8.857   10.381  3.646  1.00 69.22 ? 106 ARG A NH1   1 
ATOM   799  N NH2   . ARG A 1 106 ? 7.713   11.839  2.304  1.00 64.28 ? 106 ARG A NH2   1 
ATOM   800  N N     . ALA A 1 107 ? 8.412   10.679  9.584  1.00 55.74 ? 107 ALA A N     1 
ATOM   801  C CA    . ALA A 1 107 ? 9.040   10.888  10.881 1.00 51.42 ? 107 ALA A CA    1 
ATOM   802  C C     . ALA A 1 107 ? 10.512  10.522  10.809 1.00 53.57 ? 107 ALA A C     1 
ATOM   803  O O     . ALA A 1 107 ? 10.859  9.409   10.402 1.00 54.50 ? 107 ALA A O     1 
ATOM   804  C CB    . ALA A 1 107 ? 8.352   10.055  11.968 1.00 39.81 ? 107 ALA A CB    1 
ATOM   805  N N     . GLY A 1 108 ? 11.373  11.459  11.200 1.00 49.85 ? 108 GLY A N     1 
ATOM   806  C CA    . GLY A 1 108 ? 12.769  11.131  11.398 1.00 42.94 ? 108 GLY A CA    1 
ATOM   807  C C     . GLY A 1 108 ? 12.952  10.096  12.491 1.00 41.28 ? 108 GLY A C     1 
ATOM   808  O O     . GLY A 1 108 ? 12.120  9.935   13.385 1.00 34.55 ? 108 GLY A O     1 
ATOM   809  N N     . ALA A 1 109 ? 14.080  9.387   12.420 1.00 39.32 ? 109 ALA A N     1 
ATOM   810  C CA    . ALA A 1 109 ? 14.276  8.221   13.273 1.00 32.73 ? 109 ALA A CA    1 
ATOM   811  C C     . ALA A 1 109 ? 14.485  8.582   14.739 1.00 35.85 ? 109 ALA A C     1 
ATOM   812  O O     . ALA A 1 109 ? 14.299  7.719   15.604 1.00 29.79 ? 109 ALA A O     1 
ATOM   813  C CB    . ALA A 1 109 ? 15.461  7.399   12.768 1.00 40.36 ? 109 ALA A CB    1 
ATOM   814  N N     . ALA A 1 110 ? 14.868  9.823   15.044 1.00 34.68 ? 110 ALA A N     1 
ATOM   815  C CA    . ALA A 1 110 ? 15.030  10.235  16.433 1.00 34.61 ? 110 ALA A CA    1 
ATOM   816  C C     . ALA A 1 110 ? 13.722  10.673  17.074 1.00 28.56 ? 110 ALA A C     1 
ATOM   817  O O     . ALA A 1 110 ? 13.661  10.789  18.303 1.00 26.91 ? 110 ALA A O     1 
ATOM   818  C CB    . ALA A 1 110 ? 16.047  11.375  16.533 1.00 43.44 ? 110 ALA A CB    1 
ATOM   819  N N     . ALA A 1 111 ? 12.687  10.910  16.280 1.00 40.18 ? 111 ALA A N     1 
ATOM   820  C CA    . ALA A 1 111 ? 11.406  11.368  16.795 1.00 37.27 ? 111 ALA A CA    1 
ATOM   821  C C     . ALA A 1 111 ? 10.874  10.391  17.838 1.00 29.57 ? 111 ALA A C     1 
ATOM   822  O O     . ALA A 1 111 ? 10.697  9.204   17.525 1.00 41.74 ? 111 ALA A O     1 
ATOM   823  C CB    . ALA A 1 111 ? 10.408  11.507  15.648 1.00 31.55 ? 111 ALA A CB    1 
ATOM   824  N N     . PRO A 1 112 ? 10.616  10.825  19.073 1.00 21.08 ? 112 PRO A N     1 
ATOM   825  C CA    . PRO A 1 112 ? 10.000  9.914   20.043 1.00 24.26 ? 112 PRO A CA    1 
ATOM   826  C C     . PRO A 1 112 ? 8.679   9.378   19.514 1.00 38.16 ? 112 PRO A C     1 
ATOM   827  O O     . PRO A 1 112 ? 7.935   10.078  18.824 1.00 35.07 ? 112 PRO A O     1 
ATOM   828  C CB    . PRO A 1 112 ? 9.798   10.788  21.287 1.00 18.28 ? 112 PRO A CB    1 
ATOM   829  C CG    . PRO A 1 112 ? 10.727  11.927  21.127 1.00 19.91 ? 112 PRO A CG    1 
ATOM   830  C CD    . PRO A 1 112 ? 10.894  12.149  19.656 1.00 28.58 ? 112 PRO A CD    1 
ATOM   831  N N     . ASP A 1 113 ? 8.400   8.114   19.836 1.00 36.16 ? 113 ASP A N     1 
ATOM   832  C CA    . ASP A 1 113 ? 7.147   7.504   19.408 1.00 35.70 ? 113 ASP A CA    1 
ATOM   833  C C     . ASP A 1 113 ? 5.957   8.382   19.769 1.00 34.92 ? 113 ASP A C     1 
ATOM   834  O O     . ASP A 1 113 ? 5.020   8.533   18.977 1.00 31.01 ? 113 ASP A O     1 
ATOM   835  C CB    . ASP A 1 113 ? 7.005   6.120   20.044 1.00 41.71 ? 113 ASP A CB    1 
ATOM   836  C CG    . ASP A 1 113 ? 8.051   5.143   19.548 1.00 36.40 ? 113 ASP A CG    1 
ATOM   837  O OD1   . ASP A 1 113 ? 8.899   5.548   18.727 1.00 34.32 ? 113 ASP A OD1   1 
ATOM   838  O OD2   . ASP A 1 113 ? 8.028   3.973   19.983 1.00 39.73 ? 113 ASP A OD2   1 
ATOM   839  N N     . LYS A 1 114 ? 5.989   8.991   20.956 1.00 31.02 ? 114 LYS A N     1 
ATOM   840  C CA    . LYS A 1 114 ? 4.844   9.761   21.427 1.00 38.02 ? 114 LYS A CA    1 
ATOM   841  C C     . LYS A 1 114 ? 4.581   10.980  20.552 1.00 41.62 ? 114 LYS A C     1 
ATOM   842  O O     . LYS A 1 114 ? 3.442   11.455  20.480 1.00 46.71 ? 114 LYS A O     1 
ATOM   843  C CB    . LYS A 1 114 ? 5.072   10.174  22.880 1.00 30.98 ? 114 LYS A CB    1 
ATOM   844  C CG    . LYS A 1 114 ? 5.482   9.008   23.763 1.00 28.17 ? 114 LYS A CG    1 
ATOM   845  C CD    . LYS A 1 114 ? 5.012   9.168   25.193 1.00 25.97 ? 114 LYS A CD    1 
ATOM   846  C CE    . LYS A 1 114 ? 5.340   7.926   26.003 1.00 32.50 ? 114 LYS A CE    1 
ATOM   847  N NZ    . LYS A 1 114 ? 4.989   8.073   27.440 1.00 33.02 ? 114 LYS A NZ    1 
ATOM   848  N N     . ARG A 1 115 ? 5.611   11.503  19.883 1.00 36.44 ? 115 ARG A N     1 
ATOM   849  C CA    . ARG A 1 115 ? 5.382   12.590  18.938 1.00 35.25 ? 115 ARG A CA    1 
ATOM   850  C C     . ARG A 1 115 ? 4.611   12.105  17.718 1.00 45.17 ? 115 ARG A C     1 
ATOM   851  O O     . ARG A 1 115 ? 3.845   12.872  17.124 1.00 39.08 ? 115 ARG A O     1 
ATOM   852  C CB    . ARG A 1 115 ? 6.710   13.210  18.508 1.00 33.42 ? 115 ARG A CB    1 
ATOM   853  C CG    . ARG A 1 115 ? 6.554   14.480  17.684 1.00 50.83 ? 115 ARG A CG    1 
ATOM   854  C CD    . ARG A 1 115 ? 7.895   15.147  17.420 1.00 39.77 ? 115 ARG A CD    1 
ATOM   855  N NE    . ARG A 1 115 ? 8.600   15.467  18.656 1.00 40.01 ? 115 ARG A NE    1 
ATOM   856  C CZ    . ARG A 1 115 ? 9.919   15.435  18.805 1.00 42.03 ? 115 ARG A CZ    1 
ATOM   857  N NH1   . ARG A 1 115 ? 10.722  15.100  17.808 1.00 41.04 ? 115 ARG A NH1   1 
ATOM   858  N NH2   . ARG A 1 115 ? 10.445  15.744  19.987 1.00 33.63 ? 115 ARG A NH2   1 
ATOM   859  N N     . VAL A 1 116 ? 4.800   10.841  17.332 1.00 49.05 ? 116 VAL A N     1 
ATOM   860  C CA    . VAL A 1 116 ? 4.038   10.285  16.220 1.00 44.07 ? 116 VAL A CA    1 
ATOM   861  C C     . VAL A 1 116 ? 2.604   10.010  16.648 1.00 36.58 ? 116 VAL A C     1 
ATOM   862  O O     . VAL A 1 116 ? 1.684   10.041  15.821 1.00 44.25 ? 116 VAL A O     1 
ATOM   863  C CB    . VAL A 1 116 ? 4.728   9.015   15.690 1.00 43.38 ? 116 VAL A CB    1 
ATOM   864  C CG1   . VAL A 1 116 ? 3.985   8.467   14.482 1.00 38.67 ? 116 VAL A CG1   1 
ATOM   865  C CG2   . VAL A 1 116 ? 6.181   9.314   15.345 1.00 31.19 ? 116 VAL A CG2   1 
ATOM   866  N N     . ALA A 1 117 ? 2.386   9.735   17.934 1.00 30.07 ? 117 ALA A N     1 
ATOM   867  C CA    . ALA A 1 117 ? 1.025   9.636   18.450 1.00 39.77 ? 117 ALA A CA    1 
ATOM   868  C C     . ALA A 1 117 ? 0.295   10.966  18.309 1.00 43.47 ? 117 ALA A C     1 
ATOM   869  O O     . ALA A 1 117 ? -0.792  11.034  17.726 1.00 42.91 ? 117 ALA A O     1 
ATOM   870  C CB    . ALA A 1 117 ? 1.055   9.189   19.911 1.00 46.54 ? 117 ALA A CB    1 
ATOM   871  N N     . ALA A 1 118 ? 0.888   12.040  18.835 1.00 45.94 ? 118 ALA A N     1 
ATOM   872  C CA    . ALA A 1 118 ? 0.244   13.348  18.773 1.00 35.77 ? 118 ALA A CA    1 
ATOM   873  C C     . ALA A 1 118 ? 0.073   13.816  17.334 1.00 35.81 ? 118 ALA A C     1 
ATOM   874  O O     . ALA A 1 118 ? -0.927  14.462  16.999 1.00 48.45 ? 118 ALA A O     1 
ATOM   875  C CB    . ALA A 1 118 ? 1.058   14.367  19.570 1.00 44.57 ? 118 ALA A CB    1 
ATOM   876  N N     . ALA A 1 119 ? 1.038   13.502  16.467 1.00 44.39 ? 119 ALA A N     1 
ATOM   877  C CA    . ALA A 1 119 ? 0.965   13.971  15.087 1.00 44.91 ? 119 ALA A CA    1 
ATOM   878  C C     . ALA A 1 119 ? -0.184  13.306  14.338 1.00 43.97 ? 119 ALA A C     1 
ATOM   879  O O     . ALA A 1 119 ? -0.834  13.941  13.500 1.00 45.01 ? 119 ALA A O     1 
ATOM   880  C CB    . ALA A 1 119 ? 2.293   13.714  14.375 1.00 38.30 ? 119 ALA A CB    1 
ATOM   881  N N     . ALA A 1 120 ? -0.446  12.029  14.624 1.00 52.39 ? 120 ALA A N     1 
ATOM   882  C CA    . ALA A 1 120 ? -1.567  11.347  13.984 1.00 49.75 ? 120 ALA A CA    1 
ATOM   883  C C     . ALA A 1 120 ? -2.901  11.887  14.485 1.00 45.91 ? 120 ALA A C     1 
ATOM   884  O O     . ALA A 1 120 ? -3.859  12.001  13.712 1.00 58.23 ? 120 ALA A O     1 
ATOM   885  C CB    . ALA A 1 120 ? -1.469  9.842   14.225 1.00 49.01 ? 120 ALA A CB    1 
ATOM   886  N N     . LEU A 1 121 ? -2.986  12.222  15.776 1.00 43.01 ? 121 LEU A N     1 
ATOM   887  C CA    . LEU A 1 121 ? -4.206  12.830  16.300 1.00 43.07 ? 121 LEU A CA    1 
ATOM   888  C C     . LEU A 1 121 ? -4.487  14.159  15.612 1.00 44.19 ? 121 LEU A C     1 
ATOM   889  O O     . LEU A 1 121 ? -5.631  14.452  15.246 1.00 46.83 ? 121 LEU A O     1 
ATOM   890  C CB    . LEU A 1 121 ? -4.087  13.030  17.812 1.00 35.82 ? 121 LEU A CB    1 
ATOM   891  C CG    . LEU A 1 121 ? -5.266  13.703  18.523 1.00 41.99 ? 121 LEU A CG    1 
ATOM   892  C CD1   . LEU A 1 121 ? -6.583  13.017  18.199 1.00 48.01 ? 121 LEU A CD1   1 
ATOM   893  C CD2   . LEU A 1 121 ? -5.036  13.709  20.024 1.00 41.83 ? 121 LEU A CD2   1 
ATOM   894  N N     . GLU A 1 122 ? -3.447  14.971  15.420 1.00 42.05 ? 122 GLU A N     1 
ATOM   895  C CA    . GLU A 1 122 ? -3.544  16.261  14.748 1.00 43.28 ? 122 GLU A CA    1 
ATOM   896  C C     . GLU A 1 122 ? -3.757  16.121  13.248 1.00 50.81 ? 122 GLU A C     1 
ATOM   897  O O     . GLU A 1 122 ? -3.840  17.134  12.544 1.00 57.15 ? 122 GLU A O     1 
ATOM   898  C CB    . GLU A 1 122 ? -2.275  17.063  15.040 1.00 44.19 ? 122 GLU A CB    1 
ATOM   899  C CG    . GLU A 1 122 ? -2.202  18.448  14.417 1.00 49.80 ? 122 GLU A CG    1 
ATOM   900  C CD    . GLU A 1 122 ? -0.897  19.148  14.737 1.00 59.23 ? 122 GLU A CD    1 
ATOM   901  O OE1   . GLU A 1 122 ? -0.824  20.383  14.569 1.00 55.07 ? 122 GLU A OE1   1 
ATOM   902  O OE2   . GLU A 1 122 ? 0.058   18.459  15.154 1.00 60.59 ? 122 GLU A OE2   1 
ATOM   903  N N     . ALA A 1 123 ? -3.876  14.896  12.751 1.00 42.47 ? 123 ALA A N     1 
ATOM   904  C CA    . ALA A 1 123 ? -4.091  14.643  11.340 1.00 36.19 ? 123 ALA A CA    1 
ATOM   905  C C     . ALA A 1 123 ? -5.289  13.738  11.108 1.00 40.68 ? 123 ALA A C     1 
ATOM   906  O O     . ALA A 1 123 ? -5.598  13.428  9.952  1.00 49.77 ? 123 ALA A O     1 
ATOM   907  C CB    . ALA A 1 123 ? -2.835  14.016  10.719 1.00 49.65 ? 123 ALA A CB    1 
ATOM   908  N N     . GLY A 1 124 ? -5.969  13.313  12.170 1.00 44.06 ? 124 GLY A N     1 
ATOM   909  C CA    . GLY A 1 124 ? -7.099  12.423  12.042 1.00 52.04 ? 124 GLY A CA    1 
ATOM   910  C C     . GLY A 1 124 ? -6.668  11.124  11.406 1.00 47.68 ? 124 GLY A C     1 
ATOM   911  O O     . GLY A 1 124 ? -7.079  10.803  10.288 1.00 63.76 ? 124 GLY A O     1 
ATOM   912  N N     . LEU A 1 125 ? -5.815  10.381  12.107 1.00 49.51 ? 125 LEU A N     1 
ATOM   913  C CA    . LEU A 1 125 ? -5.302  9.110   11.617 1.00 44.53 ? 125 LEU A CA    1 
ATOM   914  C C     . LEU A 1 125 ? -5.307  8.114   12.759 1.00 51.10 ? 125 LEU A C     1 
ATOM   915  O O     . LEU A 1 125 ? -4.676  8.341   13.796 1.00 57.55 ? 125 LEU A O     1 
ATOM   916  C CB    . LEU A 1 125 ? -3.895  9.259   11.039 1.00 41.99 ? 125 LEU A CB    1 
ATOM   917  C CG    . LEU A 1 125 ? -3.813  10.025  9.720  1.00 48.00 ? 125 LEU A CG    1 
ATOM   918  C CD1   . LEU A 1 125 ? -2.394  9.982   9.210  1.00 44.26 ? 125 LEU A CD1   1 
ATOM   919  C CD2   . LEU A 1 125 ? -4.763  9.446   8.686  1.00 53.80 ? 125 LEU A CD2   1 
ATOM   920  N N     . ALA A 1 126 ? -6.017  7.017   12.557 1.00 51.14 ? 126 ALA A N     1 
ATOM   921  C CA    . ALA A 1 126 ? -6.152  5.972   13.551 1.00 58.01 ? 126 ALA A CA    1 
ATOM   922  C C     . ALA A 1 126 ? -5.043  4.941   13.377 1.00 56.68 ? 126 ALA A C     1 
ATOM   923  O O     . ALA A 1 126 ? -4.442  4.810   12.308 1.00 41.29 ? 126 ALA A O     1 
ATOM   924  C CB    . ALA A 1 126 ? -7.526  5.321   13.430 1.00 51.29 ? 126 ALA A CB    1 
ATOM   925  N N     . GLY A 1 127 ? -4.767  4.213   14.456 1.00 56.52 ? 127 GLY A N     1 
ATOM   926  C CA    . GLY A 1 127 ? -3.732  3.203   14.450 1.00 48.13 ? 127 GLY A CA    1 
ATOM   927  C C     . GLY A 1 127 ? -2.375  3.666   14.930 1.00 53.27 ? 127 GLY A C     1 
ATOM   928  O O     . GLY A 1 127 ? -1.424  2.876   14.893 1.00 53.96 ? 127 GLY A O     1 
ATOM   929  N N     . PHE A 1 128 ? -2.248  4.917   15.373 1.00 58.23 ? 128 PHE A N     1 
ATOM   930  C CA    . PHE A 1 128 ? -0.999  5.440   15.908 1.00 51.32 ? 128 PHE A CA    1 
ATOM   931  C C     . PHE A 1 128 ? -1.040  5.616   17.419 1.00 34.19 ? 128 PHE A C     1 
ATOM   932  O O     . PHE A 1 128 ? -0.067  6.106   18.002 1.00 36.04 ? 128 PHE A O     1 
ATOM   933  C CB    . PHE A 1 128 ? -0.662  6.782   15.249 1.00 46.56 ? 128 PHE A CB    1 
ATOM   934  C CG    . PHE A 1 128 ? -0.176  6.659   13.835 1.00 44.74 ? 128 PHE A CG    1 
ATOM   935  C CD1   . PHE A 1 128 ? 1.169   6.483   13.564 1.00 40.38 ? 128 PHE A CD1   1 
ATOM   936  C CD2   . PHE A 1 128 ? -1.066  6.725   12.776 1.00 46.78 ? 128 PHE A CD2   1 
ATOM   937  C CE1   . PHE A 1 128 ? 1.616   6.371   12.263 1.00 43.98 ? 128 PHE A CE1   1 
ATOM   938  C CE2   . PHE A 1 128 ? -0.624  6.615   11.475 1.00 46.74 ? 128 PHE A CE2   1 
ATOM   939  C CZ    . PHE A 1 128 ? 0.715   6.438   11.219 1.00 47.88 ? 128 PHE A CZ    1 
ATOM   940  N N     . HIS A 1 129 ? -2.140  5.228   18.064 1.00 33.46 ? 129 HIS A N     1 
ATOM   941  C CA    . HIS A 1 129 ? -2.305  5.438   19.496 1.00 36.73 ? 129 HIS A CA    1 
ATOM   942  C C     . HIS A 1 129 ? -1.381  4.563   20.332 1.00 39.03 ? 129 HIS A C     1 
ATOM   943  O O     . HIS A 1 129 ? -1.198  4.843   21.522 1.00 33.76 ? 129 HIS A O     1 
ATOM   944  C CB    . HIS A 1 129 ? -3.755  5.162   19.883 1.00 40.07 ? 129 HIS A CB    1 
ATOM   945  C CG    . HIS A 1 129 ? -4.187  3.758   19.602 1.00 38.51 ? 129 HIS A CG    1 
ATOM   946  N ND1   . HIS A 1 129 ? -4.528  3.327   18.338 1.00 37.57 ? 129 HIS A ND1   1 
ATOM   947  C CD2   . HIS A 1 129 ? -4.315  2.683   20.414 1.00 35.54 ? 129 HIS A CD2   1 
ATOM   948  C CE1   . HIS A 1 129 ? -4.856  2.048   18.386 1.00 38.29 ? 129 HIS A CE1   1 
ATOM   949  N NE2   . HIS A 1 129 ? -4.736  1.633   19.634 1.00 40.75 ? 129 HIS A NE2   1 
ATOM   950  N N     . PHE A 1 130 ? -0.808  3.507   19.752 1.00 40.37 ? 130 PHE A N     1 
ATOM   951  C CA    . PHE A 1 130 ? 0.067   2.629   20.518 1.00 37.70 ? 130 PHE A CA    1 
ATOM   952  C C     . PHE A 1 130 ? 1.459   3.217   20.704 1.00 40.20 ? 130 PHE A C     1 
ATOM   953  O O     . PHE A 1 130 ? 2.184   2.784   21.605 1.00 39.76 ? 130 PHE A O     1 
ATOM   954  C CB    . PHE A 1 130 ? 0.151   1.253   19.848 1.00 31.91 ? 130 PHE A CB    1 
ATOM   955  C CG    . PHE A 1 130 ? 0.977   1.227   18.593 1.00 39.08 ? 130 PHE A CG    1 
ATOM   956  C CD1   . PHE A 1 130 ? 0.401   1.493   17.362 1.00 34.02 ? 130 PHE A CD1   1 
ATOM   957  C CD2   . PHE A 1 130 ? 2.327   0.920   18.641 1.00 34.20 ? 130 PHE A CD2   1 
ATOM   958  C CE1   . PHE A 1 130 ? 1.155   1.460   16.205 1.00 30.22 ? 130 PHE A CE1   1 
ATOM   959  C CE2   . PHE A 1 130 ? 3.086   0.886   17.488 1.00 28.83 ? 130 PHE A CE2   1 
ATOM   960  C CZ    . PHE A 1 130 ? 2.499   1.157   16.269 1.00 35.74 ? 130 PHE A CZ    1 
ATOM   961  N N     . TYR A 1 131 ? 1.842   4.194   19.879 1.00 43.66 ? 131 TYR A N     1 
ATOM   962  C CA    . TYR A 1 131 ? 3.078   4.934   20.096 1.00 32.74 ? 131 TYR A CA    1 
ATOM   963  C C     . TYR A 1 131 ? 2.980   5.897   21.273 1.00 38.36 ? 131 TYR A C     1 
ATOM   964  O O     . TYR A 1 131 ? 4.008   6.435   21.698 1.00 41.69 ? 131 TYR A O     1 
ATOM   965  C CB    . TYR A 1 131 ? 3.448   5.714   18.832 1.00 30.31 ? 131 TYR A CB    1 
ATOM   966  C CG    . TYR A 1 131 ? 4.089   4.889   17.735 1.00 28.05 ? 131 TYR A CG    1 
ATOM   967  C CD1   . TYR A 1 131 ? 4.994   3.878   18.030 1.00 35.01 ? 131 TYR A CD1   1 
ATOM   968  C CD2   . TYR A 1 131 ? 3.792   5.131   16.400 1.00 30.64 ? 131 TYR A CD2   1 
ATOM   969  C CE1   . TYR A 1 131 ? 5.580   3.128   17.029 1.00 29.62 ? 131 TYR A CE1   1 
ATOM   970  C CE2   . TYR A 1 131 ? 4.374   4.386   15.391 1.00 33.37 ? 131 TYR A CE2   1 
ATOM   971  C CZ    . TYR A 1 131 ? 5.268   3.386   15.712 1.00 31.03 ? 131 TYR A CZ    1 
ATOM   972  O OH    . TYR A 1 131 ? 5.852   2.640   14.715 1.00 25.72 ? 131 TYR A OH    1 
ATOM   973  N N     . HIS A 1 132 ? 1.777   6.126   21.802 1.00 34.97 ? 132 HIS A N     1 
ATOM   974  C CA    . HIS A 1 132 ? 1.602   7.046   22.919 1.00 30.15 ? 132 HIS A CA    1 
ATOM   975  C C     . HIS A 1 132 ? 2.120   6.471   24.230 1.00 28.65 ? 132 HIS A C     1 
ATOM   976  O O     . HIS A 1 132 ? 2.357   7.233   25.174 1.00 40.95 ? 132 HIS A O     1 
ATOM   977  C CB    . HIS A 1 132 ? 0.120   7.407   23.054 1.00 43.31 ? 132 HIS A CB    1 
ATOM   978  C CG    . HIS A 1 132 ? -0.164  8.445   24.095 1.00 35.84 ? 132 HIS A CG    1 
ATOM   979  N ND1   . HIS A 1 132 ? 0.328   9.731   24.021 1.00 28.24 ? 132 HIS A ND1   1 
ATOM   980  C CD2   . HIS A 1 132 ? -0.902  8.391   25.229 1.00 36.33 ? 132 HIS A CD2   1 
ATOM   981  C CE1   . HIS A 1 132 ? -0.088  10.421  25.068 1.00 24.09 ? 132 HIS A CE1   1 
ATOM   982  N NE2   . HIS A 1 132 ? -0.837  9.631   25.816 1.00 30.33 ? 132 HIS A NE2   1 
ATOM   983  N N     . GLY A 1 133 ? 2.307   5.155   24.309 1.00 34.99 ? 133 GLY A N     1 
ATOM   984  C CA    . GLY A 1 133 ? 2.733   4.522   25.542 1.00 38.13 ? 133 GLY A CA    1 
ATOM   985  C C     . GLY A 1 133 ? 4.164   4.025   25.520 1.00 28.94 ? 133 GLY A C     1 
ATOM   986  O O     . GLY A 1 133 ? 4.764   3.804   26.577 1.00 32.53 ? 133 GLY A O     1 
ATOM   987  N N     . ILE A 1 134 ? 4.723   3.845   24.330 1.00 26.24 ? 134 ILE A N     1 
ATOM   988  C CA    . ILE A 1 134 ? 6.069   3.302   24.169 1.00 29.46 ? 134 ILE A CA    1 
ATOM   989  C C     . ILE A 1 134 ? 7.058   4.459   24.279 1.00 39.28 ? 134 ILE A C     1 
ATOM   990  O O     . ILE A 1 134 ? 7.026   5.365   23.432 1.00 37.82 ? 134 ILE A O     1 
ATOM   991  C CB    . ILE A 1 134 ? 6.219   2.571   22.829 1.00 38.05 ? 134 ILE A CB    1 
ATOM   992  C CG1   . ILE A 1 134 ? 5.253   1.384   22.775 1.00 29.07 ? 134 ILE A CG1   1 
ATOM   993  C CG2   . ILE A 1 134 ? 7.651   2.088   22.640 1.00 37.95 ? 134 ILE A CG2   1 
ATOM   994  C CD1   . ILE A 1 134 ? 4.927   0.909   21.376 1.00 36.83 ? 134 ILE A CD1   1 
ATOM   995  N N     . PRO A 1 135 ? 7.938   4.474   25.283 1.00 38.56 ? 135 PRO A N     1 
ATOM   996  C CA    . PRO A 1 135 ? 8.811   5.632   25.500 1.00 37.50 ? 135 PRO A CA    1 
ATOM   997  C C     . PRO A 1 135 ? 10.061  5.661   24.634 1.00 36.34 ? 135 PRO A C     1 
ATOM   998  O O     . PRO A 1 135 ? 10.938  6.493   24.881 1.00 38.49 ? 135 PRO A O     1 
ATOM   999  C CB    . PRO A 1 135 ? 9.184   5.474   26.980 1.00 34.21 ? 135 PRO A CB    1 
ATOM   1000 C CG    . PRO A 1 135 ? 9.299   4.002   27.140 1.00 37.40 ? 135 PRO A CG    1 
ATOM   1001 C CD    . PRO A 1 135 ? 8.199   3.415   26.276 1.00 38.12 ? 135 PRO A CD    1 
ATOM   1002 N N     . GLY A 1 136 ? 10.171  4.783   23.640 1.00 34.44 ? 136 GLY A N     1 
ATOM   1003 C CA    . GLY A 1 136 ? 11.333  4.733   22.782 1.00 27.22 ? 136 GLY A CA    1 
ATOM   1004 C C     . GLY A 1 136 ? 11.238  5.712   21.629 1.00 25.62 ? 136 GLY A C     1 
ATOM   1005 O O     . GLY A 1 136 ? 10.366  6.581   21.573 1.00 32.04 ? 136 GLY A O     1 
ATOM   1006 N N     . GLY A 1 137 ? 12.170  5.558   20.689 1.00 28.53 ? 137 GLY A N     1 
ATOM   1007 C CA    . GLY A 1 137 ? 12.224  6.375   19.501 1.00 25.78 ? 137 GLY A CA    1 
ATOM   1008 C C     . GLY A 1 137 ? 11.794  5.589   18.274 1.00 24.29 ? 137 GLY A C     1 
ATOM   1009 O O     . GLY A 1 137 ? 11.653  4.368   18.295 1.00 30.63 ? 137 GLY A O     1 
ATOM   1010 N N     . ILE A 1 138 ? 11.591  6.327   17.183 1.00 34.70 ? 138 ILE A N     1 
ATOM   1011 C CA    . ILE A 1 138 ? 11.069  5.708   15.971 1.00 28.97 ? 138 ILE A CA    1 
ATOM   1012 C C     . ILE A 1 138 ? 12.130  4.844   15.304 1.00 36.27 ? 138 ILE A C     1 
ATOM   1013 O O     . ILE A 1 138 ? 11.802  3.874   14.610 1.00 39.05 ? 138 ILE A O     1 
ATOM   1014 C CB    . ILE A 1 138 ? 10.528  6.793   15.021 1.00 29.11 ? 138 ILE A CB    1 
ATOM   1015 C CG1   . ILE A 1 138 ? 9.176   7.316   15.526 1.00 35.51 ? 138 ILE A CG1   1 
ATOM   1016 C CG2   . ILE A 1 138 ? 10.413  6.260   13.599 1.00 34.42 ? 138 ILE A CG2   1 
ATOM   1017 C CD1   . ILE A 1 138 ? 8.062   6.277   15.565 1.00 34.07 ? 138 ILE A CD1   1 
ATOM   1018 N N     . GLY A 1 139 ? 13.410  5.166   15.499 1.00 36.90 ? 139 GLY A N     1 
ATOM   1019 C CA    . GLY A 1 139 ? 14.459  4.318   14.958 1.00 26.24 ? 139 GLY A CA    1 
ATOM   1020 C C     . GLY A 1 139 ? 14.453  2.931   15.570 1.00 19.61 ? 139 GLY A C     1 
ATOM   1021 O O     . GLY A 1 139 ? 14.647  1.932   14.873 1.00 24.45 ? 139 GLY A O     1 
ATOM   1022 N N     . GLY A 1 140 ? 14.228  2.849   16.884 1.00 19.88 ? 140 GLY A N     1 
ATOM   1023 C CA    . GLY A 1 140 ? 14.157  1.555   17.539 1.00 23.76 ? 140 GLY A CA    1 
ATOM   1024 C C     . GLY A 1 140 ? 12.855  0.828   17.295 1.00 29.66 ? 140 GLY A C     1 
ATOM   1025 O O     . GLY A 1 140 ? 12.830  -0.406  17.266 1.00 33.25 ? 140 GLY A O     1 
ATOM   1026 N N     . ALA A 1 141 ? 11.758  1.569   17.126 1.00 36.92 ? 141 ALA A N     1 
ATOM   1027 C CA    . ALA A 1 141 ? 10.494  0.942   16.755 1.00 33.42 ? 141 ALA A CA    1 
ATOM   1028 C C     . ALA A 1 141 ? 10.630  0.190   15.437 1.00 28.58 ? 141 ALA A C     1 
ATOM   1029 O O     . ALA A 1 141 ? 10.253  -0.983  15.335 1.00 33.79 ? 141 ALA A O     1 
ATOM   1030 C CB    . ALA A 1 141 ? 9.394   1.999   16.662 1.00 35.04 ? 141 ALA A CB    1 
ATOM   1031 N N     . LEU A 1 142 ? 11.176  0.852   14.414 1.00 30.31 ? 142 LEU A N     1 
ATOM   1032 C CA    . LEU A 1 142 ? 11.333  0.205   13.116 1.00 28.64 ? 142 LEU A CA    1 
ATOM   1033 C C     . LEU A 1 142 ? 12.214  -1.031  13.209 1.00 39.48 ? 142 LEU A C     1 
ATOM   1034 O O     . LEU A 1 142 ? 12.028  -1.988  12.448 1.00 43.22 ? 142 LEU A O     1 
ATOM   1035 C CB    . LEU A 1 142 ? 11.928  1.184   12.106 1.00 35.87 ? 142 LEU A CB    1 
ATOM   1036 C CG    . LEU A 1 142 ? 11.152  2.471   11.835 1.00 38.86 ? 142 LEU A CG    1 
ATOM   1037 C CD1   . LEU A 1 142 ? 12.070  3.491   11.183 1.00 47.89 ? 142 LEU A CD1   1 
ATOM   1038 C CD2   . LEU A 1 142 ? 9.942   2.197   10.960 1.00 41.58 ? 142 LEU A CD2   1 
ATOM   1039 N N     . ARG A 1 143 ? 13.179  -1.029  14.127 1.00 43.18 ? 143 ARG A N     1 
ATOM   1040 C CA    . ARG A 1 143 ? 14.098  -2.153  14.244 1.00 46.24 ? 143 ARG A CA    1 
ATOM   1041 C C     . ARG A 1 143 ? 13.498  -3.265  15.099 1.00 35.23 ? 143 ARG A C     1 
ATOM   1042 O O     . ARG A 1 143 ? 13.659  -4.450  14.784 1.00 37.78 ? 143 ARG A O     1 
ATOM   1043 C CB    . ARG A 1 143 ? 15.431  -1.654  14.816 1.00 39.13 ? 143 ARG A CB    1 
ATOM   1044 C CG    . ARG A 1 143 ? 16.321  -2.720  15.413 1.00 33.44 ? 143 ARG A CG    1 
ATOM   1045 C CD    . ARG A 1 143 ? 16.912  -3.675  14.407 1.00 33.69 ? 143 ARG A CD    1 
ATOM   1046 N NE    . ARG A 1 143 ? 17.782  -3.024  13.437 1.00 40.38 ? 143 ARG A NE    1 
ATOM   1047 C CZ    . ARG A 1 143 ? 17.938  -3.429  12.184 1.00 52.57 ? 143 ARG A CZ    1 
ATOM   1048 N NH1   . ARG A 1 143 ? 17.188  -4.390  11.669 1.00 58.04 ? 143 ARG A NH1   1 
ATOM   1049 N NH2   . ARG A 1 143 ? 18.863  -2.847  11.426 1.00 46.86 ? 143 ARG A NH2   1 
ATOM   1050 N N     . MET A 1 144 ? 12.799  -2.901  16.172 1.00 26.96 ? 144 MET A N     1 
ATOM   1051 C CA    . MET A 1 144 ? 12.189  -3.851  17.092 1.00 42.51 ? 144 MET A CA    1 
ATOM   1052 C C     . MET A 1 144 ? 10.764  -4.219  16.725 1.00 44.93 ? 144 MET A C     1 
ATOM   1053 O O     . MET A 1 144 ? 10.107  -4.911  17.507 1.00 47.85 ? 144 MET A O     1 
ATOM   1054 C CB    . MET A 1 144 ? 12.190  -3.284  18.513 1.00 38.08 ? 144 MET A CB    1 
ATOM   1055 C CG    . MET A 1 144 ? 13.526  -2.784  19.016 1.00 27.28 ? 144 MET A CG    1 
ATOM   1056 S SD    . MET A 1 144 ? 14.638  -4.144  19.445 1.00 33.71 ? 144 MET A SD    1 
ATOM   1057 C CE    . MET A 1 144 ? 15.155  -4.755  17.845 1.00 39.92 ? 144 MET A CE    1 
ATOM   1058 N N     . ASN A 1 145 ? 10.272  -3.786  15.571 1.00 39.54 ? 145 ASN A N     1 
ATOM   1059 C CA    . ASN A 1 145 ? 8.853   -3.895  15.249 1.00 43.56 ? 145 ASN A CA    1 
ATOM   1060 C C     . ASN A 1 145 ? 8.020   -3.652  16.504 1.00 42.50 ? 145 ASN A C     1 
ATOM   1061 O O     . ASN A 1 145 ? 7.196   -4.471  16.915 1.00 45.39 ? 145 ASN A O     1 
ATOM   1062 C CB    . ASN A 1 145 ? 8.527   -5.253  14.635 1.00 48.01 ? 145 ASN A CB    1 
ATOM   1063 C CG    . ASN A 1 145 ? 7.077   -5.359  14.200 1.00 45.39 ? 145 ASN A CG    1 
ATOM   1064 O OD1   . ASN A 1 145 ? 6.369   -4.355  14.121 1.00 49.00 ? 145 ASN A OD1   1 
ATOM   1065 N ND2   . ASN A 1 145 ? 6.626   -6.576  13.926 1.00 43.39 ? 145 ASN A ND2   1 
ATOM   1066 N N     . ALA A 1 146 ? 8.282   -2.512  17.137 1.00 33.45 ? 146 ALA A N     1 
ATOM   1067 C CA    . ALA A 1 146 ? 7.670   -2.223  18.424 1.00 35.37 ? 146 ALA A CA    1 
ATOM   1068 C C     . ALA A 1 146 ? 6.152   -2.240  18.300 1.00 31.73 ? 146 ALA A C     1 
ATOM   1069 O O     . ALA A 1 146 ? 5.585   -1.863  17.272 1.00 39.22 ? 146 ALA A O     1 
ATOM   1070 C CB    . ALA A 1 146 ? 8.146   -0.870  18.951 1.00 37.10 ? 146 ALA A CB    1 
ATOM   1071 N N     . GLY A 1 147 ? 5.492   -2.693  19.361 1.00 26.80 ? 147 GLY A N     1 
ATOM   1072 C CA    . GLY A 1 147 ? 4.055   -2.866  19.317 1.00 27.07 ? 147 GLY A CA    1 
ATOM   1073 C C     . GLY A 1 147 ? 3.466   -2.997  20.700 1.00 32.30 ? 147 GLY A C     1 
ATOM   1074 O O     . GLY A 1 147 ? 4.142   -3.407  21.649 1.00 32.96 ? 147 GLY A O     1 
ATOM   1075 N N     . ALA A 1 148 ? 2.191   -2.640  20.809 1.00 41.34 ? 148 ALA A N     1 
ATOM   1076 C CA    . ALA A 1 148 ? 1.432   -2.789  22.041 1.00 33.96 ? 148 ALA A CA    1 
ATOM   1077 C C     . ALA A 1 148 ? -0.043  -2.658  21.695 1.00 31.94 ? 148 ALA A C     1 
ATOM   1078 O O     . ALA A 1 148 ? -0.407  -2.205  20.607 1.00 35.92 ? 148 ALA A O     1 
ATOM   1079 C CB    . ALA A 1 148 ? 1.847   -1.752  23.089 1.00 29.12 ? 148 ALA A CB    1 
ATOM   1080 N N     . ASN A 1 149 ? -0.891  -3.072  22.633 1.00 36.00 ? 149 ASN A N     1 
ATOM   1081 C CA    . ASN A 1 149 ? -2.340  -2.933  22.507 1.00 44.06 ? 149 ASN A CA    1 
ATOM   1082 C C     . ASN A 1 149 ? -2.892  -3.636  21.271 1.00 44.51 ? 149 ASN A C     1 
ATOM   1083 O O     . ASN A 1 149 ? -4.009  -3.339  20.835 1.00 51.10 ? 149 ASN A O     1 
ATOM   1084 C CB    . ASN A 1 149 ? -2.747  -1.455  22.478 1.00 48.58 ? 149 ASN A CB    1 
ATOM   1085 C CG    . ASN A 1 149 ? -2.066  -0.641  23.559 1.00 41.54 ? 149 ASN A CG    1 
ATOM   1086 O OD1   . ASN A 1 149 ? -1.238  0.224   23.272 1.00 39.57 ? 149 ASN A OD1   1 
ATOM   1087 N ND2   . ASN A 1 149 ? -2.417  -0.909  24.811 1.00 45.82 ? 149 ASN A ND2   1 
ATOM   1088 N N     . GLY A 1 150 ? -2.137  -4.562  20.689 1.00 41.75 ? 150 GLY A N     1 
ATOM   1089 C CA    . GLY A 1 150 ? -2.578  -5.262  19.501 1.00 29.18 ? 150 GLY A CA    1 
ATOM   1090 C C     . GLY A 1 150 ? -2.175  -4.627  18.191 1.00 27.37 ? 150 GLY A C     1 
ATOM   1091 O O     . GLY A 1 150 ? -2.640  -5.079  17.137 1.00 28.94 ? 150 GLY A O     1 
ATOM   1092 N N     . VAL A 1 151 ? -1.337  -3.594  18.218 1.00 38.01 ? 151 VAL A N     1 
ATOM   1093 C CA    . VAL A 1 151 ? -0.803  -2.971  17.014 1.00 34.49 ? 151 VAL A CA    1 
ATOM   1094 C C     . VAL A 1 151 ? 0.715   -3.065  17.060 1.00 31.75 ? 151 VAL A C     1 
ATOM   1095 O O     . VAL A 1 151 ? 1.323   -2.919  18.126 1.00 33.26 ? 151 VAL A O     1 
ATOM   1096 C CB    . VAL A 1 151 ? -1.244  -1.499  16.876 1.00 34.77 ? 151 VAL A CB    1 
ATOM   1097 C CG1   . VAL A 1 151 ? -1.083  -1.031  15.435 1.00 40.89 ? 151 VAL A CG1   1 
ATOM   1098 C CG2   . VAL A 1 151 ? -2.678  -1.313  17.348 1.00 34.55 ? 151 VAL A CG2   1 
ATOM   1099 N N     . GLU A 1 152 ? 1.323   -3.312  15.903 1.00 39.53 ? 152 GLU A N     1 
ATOM   1100 C CA    . GLU A 1 152 ? 2.769   -3.335  15.767 1.00 42.53 ? 152 GLU A CA    1 
ATOM   1101 C C     . GLU A 1 152 ? 3.212   -2.260  14.784 1.00 37.23 ? 152 GLU A C     1 
ATOM   1102 O O     . GLU A 1 152 ? 2.412   -1.718  14.016 1.00 36.81 ? 152 GLU A O     1 
ATOM   1103 C CB    . GLU A 1 152 ? 3.276   -4.702  15.290 1.00 38.22 ? 152 GLU A CB    1 
ATOM   1104 C CG    . GLU A 1 152 ? 2.895   -5.866  16.186 1.00 42.69 ? 152 GLU A CG    1 
ATOM   1105 C CD    . GLU A 1 152 ? 3.479   -7.178  15.702 1.00 40.40 ? 152 GLU A CD    1 
ATOM   1106 O OE1   . GLU A 1 152 ? 3.589   -7.362  14.471 1.00 36.84 ? 152 GLU A OE1   1 
ATOM   1107 O OE2   . GLU A 1 152 ? 3.827   -8.025  16.551 1.00 36.93 ? 152 GLU A OE2   1 
ATOM   1108 N N     . THR A 1 153 ? 4.511   -1.962  14.820 1.00 37.54 ? 153 THR A N     1 
ATOM   1109 C CA    . THR A 1 153 ? 5.072   -0.976  13.903 1.00 39.33 ? 153 THR A CA    1 
ATOM   1110 C C     . THR A 1 153 ? 4.887   -1.400  12.451 1.00 42.37 ? 153 THR A C     1 
ATOM   1111 O O     . THR A 1 153 ? 4.660   -0.557  11.574 1.00 44.44 ? 153 THR A O     1 
ATOM   1112 C CB    . THR A 1 153 ? 6.557   -0.771  14.206 1.00 33.09 ? 153 THR A CB    1 
ATOM   1113 O OG1   . THR A 1 153 ? 6.704   -0.011  15.412 1.00 31.41 ? 153 THR A OG1   1 
ATOM   1114 C CG2   . THR A 1 153 ? 7.249   -0.049  13.058 1.00 31.12 ? 153 THR A CG2   1 
ATOM   1115 N N     . ARG A 1 154 ? 4.977   -2.704  12.178 1.00 37.34 ? 154 ARG A N     1 
ATOM   1116 C CA    . ARG A 1 154 ? 5.000   -3.175  10.796 1.00 39.11 ? 154 ARG A CA    1 
ATOM   1117 C C     . ARG A 1 154 ? 3.763   -2.740  10.023 1.00 43.08 ? 154 ARG A C     1 
ATOM   1118 O O     . ARG A 1 154 ? 3.824   -2.571  8.799  1.00 36.95 ? 154 ARG A O     1 
ATOM   1119 C CB    . ARG A 1 154 ? 5.125   -4.699  10.770 1.00 48.47 ? 154 ARG A CB    1 
ATOM   1120 C CG    . ARG A 1 154 ? 3.912   -5.435  11.324 1.00 49.47 ? 154 ARG A CG    1 
ATOM   1121 C CD    . ARG A 1 154 ? 4.114   -6.941  11.292 1.00 50.45 ? 154 ARG A CD    1 
ATOM   1122 N NE    . ARG A 1 154 ? 4.142   -7.460  9.929  1.00 51.19 ? 154 ARG A NE    1 
ATOM   1123 C CZ    . ARG A 1 154 ? 4.566   -8.671  9.594  1.00 50.09 ? 154 ARG A CZ    1 
ATOM   1124 N NH1   . ARG A 1 154 ? 5.001   -9.528  10.503 1.00 43.75 ? 154 ARG A NH1   1 
ATOM   1125 N NH2   . ARG A 1 154 ? 4.552   -9.031  8.314  1.00 45.67 ? 154 ARG A NH2   1 
ATOM   1126 N N     . GLU A 1 155 ? 2.639   -2.548  10.712 1.00 51.75 ? 155 GLU A N     1 
ATOM   1127 C CA    . GLU A 1 155 ? 1.372   -2.292  10.039 1.00 44.04 ? 155 GLU A CA    1 
ATOM   1128 C C     . GLU A 1 155 ? 1.231   -0.854  9.559  1.00 43.08 ? 155 GLU A C     1 
ATOM   1129 O O     . GLU A 1 155 ? 0.401   -0.590  8.682  1.00 48.96 ? 155 GLU A O     1 
ATOM   1130 C CB    . GLU A 1 155 ? 0.215   -2.641  10.977 1.00 45.97 ? 155 GLU A CB    1 
ATOM   1131 C CG    . GLU A 1 155 ? 0.274   -4.069  11.503 1.00 43.29 ? 155 GLU A CG    1 
ATOM   1132 C CD    . GLU A 1 155 ? -0.667  -4.307  12.666 1.00 44.00 ? 155 GLU A CD    1 
ATOM   1133 O OE1   . GLU A 1 155 ? -0.979  -3.337  13.388 1.00 41.97 ? 155 GLU A OE1   1 
ATOM   1134 O OE2   . GLU A 1 155 ? -1.089  -5.466  12.859 1.00 39.91 ? 155 GLU A OE2   1 
ATOM   1135 N N     . ARG A 1 156 ? 2.017   0.075   10.103 1.00 44.91 ? 156 ARG A N     1 
ATOM   1136 C CA    . ARG A 1 156 ? 1.976   1.471   9.690  1.00 44.73 ? 156 ARG A CA    1 
ATOM   1137 C C     . ARG A 1 156 ? 3.173   1.871   8.839  1.00 46.62 ? 156 ARG A C     1 
ATOM   1138 O O     . ARG A 1 156 ? 3.227   3.013   8.373  1.00 50.57 ? 156 ARG A O     1 
ATOM   1139 C CB    . ARG A 1 156 ? 1.898   2.390   10.919 1.00 51.17 ? 156 ARG A CB    1 
ATOM   1140 C CG    . ARG A 1 156 ? 0.824   2.017   11.943 1.00 51.63 ? 156 ARG A CG    1 
ATOM   1141 C CD    . ARG A 1 156 ? -0.548  2.555   11.556 1.00 49.06 ? 156 ARG A CD    1 
ATOM   1142 N NE    . ARG A 1 156 ? -1.252  1.632   10.673 1.00 45.84 ? 156 ARG A NE    1 
ATOM   1143 C CZ    . ARG A 1 156 ? -2.035  0.643   11.084 1.00 45.75 ? 156 ARG A CZ    1 
ATOM   1144 N NH1   . ARG A 1 156 ? -2.287  0.443   12.368 1.00 35.94 ? 156 ARG A NH1   1 
ATOM   1145 N NH2   . ARG A 1 156 ? -2.579  -0.169  10.182 1.00 44.55 ? 156 ARG A NH2   1 
ATOM   1146 N N     . VAL A 1 157 ? 4.126   0.970   8.618  1.00 54.03 ? 157 VAL A N     1 
ATOM   1147 C CA    . VAL A 1 157 ? 5.342   1.296   7.879  1.00 59.49 ? 157 VAL A CA    1 
ATOM   1148 C C     . VAL A 1 157 ? 5.055   1.215   6.385  1.00 52.45 ? 157 VAL A C     1 
ATOM   1149 O O     . VAL A 1 157 ? 4.654   0.162   5.876  1.00 48.83 ? 157 VAL A O     1 
ATOM   1150 C CB    . VAL A 1 157 ? 6.492   0.354   8.265  1.00 53.49 ? 157 VAL A CB    1 
ATOM   1151 C CG1   . VAL A 1 157 ? 7.618   0.436   7.238  1.00 53.88 ? 157 VAL A CG1   1 
ATOM   1152 C CG2   . VAL A 1 157 ? 7.010   0.678   9.658  1.00 41.95 ? 157 VAL A CG2   1 
ATOM   1153 N N     . VAL A 1 158 ? 5.267   2.324   5.677  1.00 53.50 ? 158 VAL A N     1 
ATOM   1154 C CA    . VAL A 1 158 ? 5.201   2.328   4.219  1.00 63.38 ? 158 VAL A CA    1 
ATOM   1155 C C     . VAL A 1 158 ? 6.594   2.043   3.675  1.00 52.69 ? 158 VAL A C     1 
ATOM   1156 O O     . VAL A 1 158 ? 6.875   0.934   3.207  1.00 51.03 ? 158 VAL A O     1 
ATOM   1157 C CB    . VAL A 1 158 ? 4.656   3.660   3.674  1.00 56.20 ? 158 VAL A CB    1 
ATOM   1158 C CG1   . VAL A 1 158 ? 4.721   3.678   2.152  1.00 51.49 ? 158 VAL A CG1   1 
ATOM   1159 C CG2   . VAL A 1 158 ? 3.232   3.880   4.141  1.00 46.37 ? 158 VAL A CG2   1 
ATOM   1160 N N     . GLU A 1 159 ? 7.476   3.040   3.735  1.00 58.44 ? 159 GLU A N     1 
ATOM   1161 C CA    . GLU A 1 159 ? 8.850   2.897   3.277  1.00 62.59 ? 159 GLU A CA    1 
ATOM   1162 C C     . GLU A 1 159 ? 9.798   3.469   4.321  1.00 56.22 ? 159 GLU A C     1 
ATOM   1163 O O     . GLU A 1 159 ? 9.472   4.433   5.019  1.00 52.43 ? 159 GLU A O     1 
ATOM   1164 C CB    . GLU A 1 159 ? 9.073   3.597   1.922  1.00 61.45 ? 159 GLU A CB    1 
ATOM   1165 C CG    . GLU A 1 159 ? 8.923   5.114   1.947  1.00 62.16 ? 159 GLU A CG    1 
ATOM   1166 C CD    . GLU A 1 159 ? 9.419   5.767   0.670  1.00 58.90 ? 159 GLU A CD    1 
ATOM   1167 O OE1   . GLU A 1 159 ? 9.571   5.053   -0.344 1.00 51.45 ? 159 GLU A OE1   1 
ATOM   1168 O OE2   . GLU A 1 159 ? 9.659   6.993   0.679  1.00 55.01 ? 159 GLU A OE2   1 
ATOM   1169 N N     . VAL A 1 160 ? 10.978  2.861   4.419  1.00 61.88 ? 160 VAL A N     1 
ATOM   1170 C CA    . VAL A 1 160 ? 12.014  3.294   5.346  1.00 59.23 ? 160 VAL A CA    1 
ATOM   1171 C C     . VAL A 1 160 ? 13.210  3.791   4.548  1.00 50.43 ? 160 VAL A C     1 
ATOM   1172 O O     . VAL A 1 160 ? 13.479  3.330   3.432  1.00 59.02 ? 160 VAL A O     1 
ATOM   1173 C CB    . VAL A 1 160 ? 12.440  2.168   6.312  1.00 47.10 ? 160 VAL A CB    1 
ATOM   1174 C CG1   . VAL A 1 160 ? 13.321  2.726   7.421  1.00 42.99 ? 160 VAL A CG1   1 
ATOM   1175 C CG2   . VAL A 1 160 ? 11.228  1.461   6.891  1.00 52.35 ? 160 VAL A CG2   1 
ATOM   1176 N N     . ARG A 1 161 ? 13.932  4.741   5.135  1.00 51.63 ? 161 ARG A N     1 
ATOM   1177 C CA    . ARG A 1 161 ? 15.122  5.334   4.542  1.00 52.76 ? 161 ARG A CA    1 
ATOM   1178 C C     . ARG A 1 161 ? 16.279  5.152   5.513  1.00 58.31 ? 161 ARG A C     1 
ATOM   1179 O O     . ARG A 1 161 ? 16.140  5.436   6.707  1.00 55.94 ? 161 ARG A O     1 
ATOM   1180 C CB    . ARG A 1 161 ? 14.885  6.816   4.236  1.00 50.96 ? 161 ARG A CB    1 
ATOM   1181 C CG    . ARG A 1 161 ? 16.073  7.565   3.659  1.00 52.14 ? 161 ARG A CG    1 
ATOM   1182 C CD    . ARG A 1 161 ? 15.849  9.064   3.783  1.00 48.35 ? 161 ARG A CD    1 
ATOM   1183 N NE    . ARG A 1 161 ? 16.895  9.844   3.134  1.00 50.21 ? 161 ARG A NE    1 
ATOM   1184 C CZ    . ARG A 1 161 ? 16.981  10.045  1.826  1.00 53.84 ? 161 ARG A CZ    1 
ATOM   1185 N NH1   . ARG A 1 161 ? 16.100  9.526   0.986  1.00 52.85 ? 161 ARG A NH1   1 
ATOM   1186 N NH2   . ARG A 1 161 ? 17.974  10.789  1.349  1.00 46.76 ? 161 ARG A NH2   1 
ATOM   1187 N N     . ALA A 1 162 ? 17.415  4.679   5.004  1.00 58.17 ? 162 ALA A N     1 
ATOM   1188 C CA    . ALA A 1 162 ? 18.519  4.294   5.870  1.00 49.33 ? 162 ALA A CA    1 
ATOM   1189 C C     . ALA A 1 162 ? 19.845  4.541   5.168  1.00 57.97 ? 162 ALA A C     1 
ATOM   1190 O O     . ALA A 1 162 ? 19.906  4.717   3.949  1.00 63.87 ? 162 ALA A O     1 
ATOM   1191 C CB    . ALA A 1 162 ? 18.416  2.820   6.281  1.00 54.40 ? 162 ALA A CB    1 
ATOM   1192 N N     . LEU A 1 163 ? 20.909  4.554   5.966  1.00 55.03 ? 163 LEU A N     1 
ATOM   1193 C CA    . LEU A 1 163 ? 22.277  4.554   5.473  1.00 43.69 ? 163 LEU A CA    1 
ATOM   1194 C C     . LEU A 1 163 ? 22.932  3.228   5.829  1.00 37.93 ? 163 LEU A C     1 
ATOM   1195 O O     . LEU A 1 163 ? 22.682  2.672   6.903  1.00 41.33 ? 163 LEU A O     1 
ATOM   1196 C CB    . LEU A 1 163 ? 23.093  5.704   6.071  1.00 44.28 ? 163 LEU A CB    1 
ATOM   1197 C CG    . LEU A 1 163 ? 22.695  7.123   5.667  1.00 37.77 ? 163 LEU A CG    1 
ATOM   1198 C CD1   . LEU A 1 163 ? 23.523  8.148   6.425  1.00 46.99 ? 163 LEU A CD1   1 
ATOM   1199 C CD2   . LEU A 1 163 ? 22.856  7.313   4.172  1.00 50.31 ? 163 LEU A CD2   1 
ATOM   1200 N N     . ASP A 1 164 ? 23.762  2.722   4.924  1.00 52.34 ? 164 ASP A N     1 
ATOM   1201 C CA    . ASP A 1 164 ? 24.566  1.549   5.214  1.00 58.20 ? 164 ASP A CA    1 
ATOM   1202 C C     . ASP A 1 164 ? 25.932  1.996   5.734  1.00 59.75 ? 164 ASP A C     1 
ATOM   1203 O O     . ASP A 1 164 ? 26.241  3.189   5.801  1.00 56.45 ? 164 ASP A O     1 
ATOM   1204 C CB    . ASP A 1 164 ? 24.681  0.658   3.976  1.00 62.55 ? 164 ASP A CB    1 
ATOM   1205 C CG    . ASP A 1 164 ? 25.289  1.375   2.786  1.00 65.76 ? 164 ASP A CG    1 
ATOM   1206 O OD1   . ASP A 1 164 ? 25.747  2.526   2.944  1.00 74.50 ? 164 ASP A OD1   1 
ATOM   1207 O OD2   . ASP A 1 164 ? 25.305  0.785   1.685  1.00 58.28 ? 164 ASP A OD2   1 
ATOM   1208 N N     . ARG A 1 165 ? 26.765  1.028   6.113  1.00 56.06 ? 165 ARG A N     1 
ATOM   1209 C CA    . ARG A 1 165 ? 28.030  1.342   6.767  1.00 62.28 ? 165 ARG A CA    1 
ATOM   1210 C C     . ARG A 1 165 ? 29.005  2.054   5.834  1.00 65.16 ? 165 ARG A C     1 
ATOM   1211 O O     . ARG A 1 165 ? 30.005  2.601   6.312  1.00 65.66 ? 165 ARG A O     1 
ATOM   1212 C CB    . ARG A 1 165 ? 28.614  0.042   7.346  1.00 55.33 ? 165 ARG A CB    1 
ATOM   1213 C CG    . ARG A 1 165 ? 30.098  0.024   7.728  1.00 44.08 ? 165 ARG A CG    1 
ATOM   1214 C CD    . ARG A 1 165 ? 30.255  0.361   9.201  1.00 39.68 ? 165 ARG A CD    1 
ATOM   1215 N NE    . ARG A 1 165 ? 31.592  0.814   9.564  1.00 55.76 ? 165 ARG A NE    1 
ATOM   1216 C CZ    . ARG A 1 165 ? 32.055  2.039   9.354  1.00 51.78 ? 165 ARG A CZ    1 
ATOM   1217 N NH1   . ARG A 1 165 ? 31.381  2.920   8.633  1.00 51.86 ? 165 ARG A NH1   1 
ATOM   1218 N NH2   . ARG A 1 165 ? 33.228  2.385   9.872  1.00 53.15 ? 165 ARG A NH2   1 
ATOM   1219 N N     . LYS A 1 166 ? 28.726  2.093   4.531  1.00 70.72 ? 166 LYS A N     1 
ATOM   1220 C CA    . LYS A 1 166 ? 29.491  2.897   3.588  1.00 66.83 ? 166 LYS A CA    1 
ATOM   1221 C C     . LYS A 1 166 ? 28.825  4.238   3.295  1.00 70.52 ? 166 LYS A C     1 
ATOM   1222 O O     . LYS A 1 166 ? 29.217  4.918   2.341  1.00 72.21 ? 166 LYS A O     1 
ATOM   1223 C CB    . LYS A 1 166 ? 29.705  2.126   2.284  1.00 64.88 ? 166 LYS A CB    1 
ATOM   1224 C CG    . LYS A 1 166 ? 30.411  0.786   2.455  1.00 75.23 ? 166 LYS A CG    1 
ATOM   1225 C CD    . LYS A 1 166 ? 30.015  -0.227  1.379  1.00 68.23 ? 166 LYS A CD    1 
ATOM   1226 C CE    . LYS A 1 166 ? 30.071  0.349   -0.035 1.00 73.82 ? 166 LYS A CE    1 
ATOM   1227 N NZ    . LYS A 1 166 ? 29.404  -0.550  -1.016 1.00 68.88 ? 166 LYS A NZ    1 
ATOM   1228 N N     . GLY A 1 167 ? 27.826  4.626   4.086  1.00 69.46 ? 167 GLY A N     1 
ATOM   1229 C CA    . GLY A 1 167 ? 27.216  5.935   3.951  1.00 61.46 ? 167 GLY A CA    1 
ATOM   1230 C C     . GLY A 1 167 ? 26.363  6.134   2.720  1.00 64.66 ? 167 GLY A C     1 
ATOM   1231 O O     . GLY A 1 167 ? 26.116  7.279   2.333  1.00 65.00 ? 167 GLY A O     1 
ATOM   1232 N N     . GLU A 1 168 ? 25.896  5.057   2.095  1.00 73.27 ? 168 GLU A N     1 
ATOM   1233 C CA    . GLU A 1 168 ? 25.077  5.146   0.893  1.00 74.09 ? 168 GLU A CA    1 
ATOM   1234 C C     . GLU A 1 168 ? 23.611  4.916   1.240  1.00 68.35 ? 168 GLU A C     1 
ATOM   1235 O O     . GLU A 1 168 ? 23.279  4.040   2.045  1.00 59.39 ? 168 GLU A O     1 
ATOM   1236 C CB    . GLU A 1 168 ? 25.550  4.137   -0.155 1.00 74.46 ? 168 GLU A CB    1 
ATOM   1237 C CG    . GLU A 1 168 ? 26.959  4.413   -0.668 1.00 64.96 ? 168 GLU A CG    1 
ATOM   1238 C CD    . GLU A 1 168 ? 27.062  5.729   -1.416 1.00 75.38 ? 168 GLU A CD    1 
ATOM   1239 O OE1   . GLU A 1 168 ? 26.368  5.888   -2.442 1.00 93.74 ? 168 GLU A OE1   1 
ATOM   1240 O OE2   . GLU A 1 168 ? 27.836  6.606   -0.977 1.00 68.33 ? 168 GLU A OE2   1 
ATOM   1241 N N     . VAL A 1 169 ? 22.736  5.708   0.616  1.00 76.06 ? 169 VAL A N     1 
ATOM   1242 C CA    . VAL A 1 169 ? 21.334  5.764   1.015  1.00 63.89 ? 169 VAL A CA    1 
ATOM   1243 C C     . VAL A 1 169 ? 20.588  4.516   0.549  1.00 58.87 ? 169 VAL A C     1 
ATOM   1244 O O     . VAL A 1 169 ? 20.949  3.878   -0.449 1.00 64.58 ? 169 VAL A O     1 
ATOM   1245 C CB    . VAL A 1 169 ? 20.685  7.043   0.453  1.00 63.65 ? 169 VAL A CB    1 
ATOM   1246 C CG1   . VAL A 1 169 ? 19.230  7.150   0.885  1.00 64.19 ? 169 VAL A CG1   1 
ATOM   1247 C CG2   . VAL A 1 169 ? 21.470  8.276   0.892  1.00 54.53 ? 169 VAL A CG2   1 
ATOM   1248 N N     . HIS A 1 170 ? 19.529  4.168   1.282  1.00 58.11 ? 170 HIS A N     1 
ATOM   1249 C CA    . HIS A 1 170 ? 18.683  3.025   0.948  1.00 64.67 ? 170 HIS A CA    1 
ATOM   1250 C C     . HIS A 1 170 ? 17.245  3.353   1.321  1.00 58.35 ? 170 HIS A C     1 
ATOM   1251 O O     . HIS A 1 170 ? 16.956  3.598   2.496  1.00 61.47 ? 170 HIS A O     1 
ATOM   1252 C CB    . HIS A 1 170 ? 19.139  1.762   1.686  1.00 69.29 ? 170 HIS A CB    1 
ATOM   1253 C CG    . HIS A 1 170 ? 20.311  1.075   1.057  1.00 72.08 ? 170 HIS A CG    1 
ATOM   1254 N ND1   . HIS A 1 170 ? 21.500  0.873   1.725  1.00 74.40 ? 170 HIS A ND1   1 
ATOM   1255 C CD2   . HIS A 1 170 ? 20.472  0.527   -0.171 1.00 80.32 ? 170 HIS A CD2   1 
ATOM   1256 C CE1   . HIS A 1 170 ? 22.345  0.238   0.933  1.00 79.13 ? 170 HIS A CE1   1 
ATOM   1257 N NE2   . HIS A 1 170 ? 21.746  0.017   -0.223 1.00 85.95 ? 170 HIS A NE2   1 
ATOM   1258 N N     . VAL A 1 171 ? 16.348  3.350   0.337  1.00 57.55 ? 171 VAL A N     1 
ATOM   1259 C CA    . VAL A 1 171 ? 14.914  3.489   0.573  1.00 56.15 ? 171 VAL A CA    1 
ATOM   1260 C C     . VAL A 1 171 ? 14.321  2.086   0.495  1.00 53.50 ? 171 VAL A C     1 
ATOM   1261 O O     . VAL A 1 171 ? 14.152  1.529   -0.593 1.00 49.75 ? 171 VAL A O     1 
ATOM   1262 C CB    . VAL A 1 171 ? 14.248  4.435   -0.430 1.00 57.97 ? 171 VAL A CB    1 
ATOM   1263 C CG1   . VAL A 1 171 ? 12.801  4.694   -0.020 1.00 57.00 ? 171 VAL A CG1   1 
ATOM   1264 C CG2   . VAL A 1 171 ? 15.018  5.742   -0.545 1.00 54.79 ? 171 VAL A CG2   1 
ATOM   1265 N N     . LEU A 1 172 ? 13.994  1.514   1.649  1.00 58.23 ? 172 LEU A N     1 
ATOM   1266 C CA    . LEU A 1 172 ? 13.510  0.145   1.742  1.00 59.63 ? 172 LEU A CA    1 
ATOM   1267 C C     . LEU A 1 172 ? 12.050  0.127   2.186  1.00 57.55 ? 172 LEU A C     1 
ATOM   1268 O O     . LEU A 1 172 ? 11.572  1.058   2.839  1.00 52.79 ? 172 LEU A O     1 
ATOM   1269 C CB    . LEU A 1 172 ? 14.400  -0.661  2.696  1.00 60.28 ? 172 LEU A CB    1 
ATOM   1270 C CG    . LEU A 1 172 ? 14.222  -0.561  4.208  1.00 59.79 ? 172 LEU A CG    1 
ATOM   1271 C CD1   . LEU A 1 172 ? 14.628  -1.882  4.814  1.00 59.80 ? 172 LEU A CD1   1 
ATOM   1272 C CD2   . LEU A 1 172 ? 15.063  0.569   4.789  1.00 66.28 ? 172 LEU A CD2   1 
ATOM   1273 N N     . SER A 1 173 ? 11.341  -0.938  1.813  1.00 66.49 ? 173 SER A N     1 
ATOM   1274 C CA    . SER A 1 173 ? 9.889   -1.008  1.927  1.00 61.52 ? 173 SER A CA    1 
ATOM   1275 C C     . SER A 1 173 ? 9.458   -1.977  3.023  1.00 56.01 ? 173 SER A C     1 
ATOM   1276 O O     . SER A 1 173 ? 10.255  -2.744  3.570  1.00 64.73 ? 173 SER A O     1 
ATOM   1277 C CB    . SER A 1 173 ? 9.263   -1.425  0.590  1.00 58.04 ? 173 SER A CB    1 
ATOM   1278 O OG    . SER A 1 173 ? 9.526   -2.788  0.304  1.00 66.46 ? 173 SER A OG    1 
ATOM   1279 N N     . ASN A 1 174 ? 8.155   -1.930  3.326  1.00 54.56 ? 174 ASN A N     1 
ATOM   1280 C CA    . ASN A 1 174 ? 7.580   -2.780  4.366  1.00 59.37 ? 174 ASN A CA    1 
ATOM   1281 C C     . ASN A 1 174 ? 7.923   -4.248  4.143  1.00 53.31 ? 174 ASN A C     1 
ATOM   1282 O O     . ASN A 1 174 ? 8.142   -4.996  5.103  1.00 46.08 ? 174 ASN A O     1 
ATOM   1283 C CB    . ASN A 1 174 ? 6.061   -2.585  4.406  1.00 57.71 ? 174 ASN A CB    1 
ATOM   1284 C CG    . ASN A 1 174 ? 5.398   -3.341  5.545  1.00 51.59 ? 174 ASN A CG    1 
ATOM   1285 O OD1   . ASN A 1 174 ? 5.563   -4.553  5.684  1.00 54.93 ? 174 ASN A OD1   1 
ATOM   1286 N ND2   . ASN A 1 174 ? 4.629   -2.626  6.360  1.00 39.20 ? 174 ASN A ND2   1 
ATOM   1287 N N     . ALA A 1 175 ? 7.961   -4.683  2.882  1.00 61.19 ? 175 ALA A N     1 
ATOM   1288 C CA    . ALA A 1 175 ? 8.345   -6.061  2.595  1.00 65.65 ? 175 ALA A CA    1 
ATOM   1289 C C     . ALA A 1 175 ? 9.822   -6.290  2.886  1.00 58.94 ? 175 ALA A C     1 
ATOM   1290 O O     . ALA A 1 175 ? 10.195  -7.311  3.476  1.00 54.91 ? 175 ALA A O     1 
ATOM   1291 C CB    . ALA A 1 175 ? 8.027   -6.402  1.140  1.00 72.54 ? 175 ALA A CB    1 
ATOM   1292 N N     . ASP A 1 176 ? 10.678  -5.348  2.482  1.00 52.33 ? 176 ASP A N     1 
ATOM   1293 C CA    . ASP A 1 176 ? 12.110  -5.499  2.714  1.00 48.40 ? 176 ASP A CA    1 
ATOM   1294 C C     . ASP A 1 176 ? 12.436  -5.575  4.199  1.00 50.69 ? 176 ASP A C     1 
ATOM   1295 O O     . ASP A 1 176 ? 13.418  -6.221  4.585  1.00 57.22 ? 176 ASP A O     1 
ATOM   1296 C CB    . ASP A 1 176 ? 12.871  -4.338  2.072  1.00 55.92 ? 176 ASP A CB    1 
ATOM   1297 C CG    . ASP A 1 176 ? 12.602  -4.214  0.586  1.00 50.53 ? 176 ASP A CG    1 
ATOM   1298 O OD1   . ASP A 1 176 ? 12.769  -5.220  -0.135 1.00 57.40 ? 176 ASP A OD1   1 
ATOM   1299 O OD2   . ASP A 1 176 ? 12.226  -3.111  0.138  1.00 48.70 ? 176 ASP A OD2   1 
ATOM   1300 N N     . MET A 1 177 ? 11.634  -4.926  5.047  1.00 51.39 ? 177 MET A N     1 
ATOM   1301 C CA    . MET A 1 177 ? 11.934  -4.918  6.474  1.00 48.23 ? 177 MET A CA    1 
ATOM   1302 C C     . MET A 1 177 ? 11.884  -6.321  7.063  1.00 44.24 ? 177 MET A C     1 
ATOM   1303 O O     . MET A 1 177 ? 12.535  -6.589  8.080  1.00 43.87 ? 177 MET A O     1 
ATOM   1304 C CB    . MET A 1 177 ? 10.960  -4.001  7.216  1.00 53.92 ? 177 MET A CB    1 
ATOM   1305 C CG    . MET A 1 177 ? 11.231  -2.510  7.044  1.00 61.19 ? 177 MET A CG    1 
ATOM   1306 S SD    . MET A 1 177 ? 12.864  -2.009  7.621  1.00 54.20 ? 177 MET A SD    1 
ATOM   1307 C CE    . MET A 1 177 ? 12.565  -1.576  9.329  1.00 42.74 ? 177 MET A CE    1 
ATOM   1308 N N     . GLY A 1 178 ? 11.125  -7.225  6.447  1.00 49.36 ? 178 GLY A N     1 
ATOM   1309 C CA    . GLY A 1 178 ? 11.039  -8.591  6.925  1.00 48.31 ? 178 GLY A CA    1 
ATOM   1310 C C     . GLY A 1 178 ? 10.603  -8.649  8.372  1.00 40.73 ? 178 GLY A C     1 
ATOM   1311 O O     . GLY A 1 178 ? 11.386  -9.016  9.253  1.00 46.27 ? 178 GLY A O     1 
ATOM   1312 N N     . TYR A 1 179 ? 9.352   -8.292  8.627  1.00 40.11 ? 179 TYR A N     1 
ATOM   1313 C CA    . TYR A 1 179 ? 8.879   -8.104  9.987  1.00 43.56 ? 179 TYR A CA    1 
ATOM   1314 C C     . TYR A 1 179 ? 8.320   -9.394  10.569 1.00 46.74 ? 179 TYR A C     1 
ATOM   1315 O O     . TYR A 1 179 ? 7.814   -10.264 9.855  1.00 46.53 ? 179 TYR A O     1 
ATOM   1316 C CB    . TYR A 1 179 ? 7.815   -7.007  10.034 1.00 46.21 ? 179 TYR A CB    1 
ATOM   1317 C CG    . TYR A 1 179 ? 8.393   -5.618  10.159 1.00 42.80 ? 179 TYR A CG    1 
ATOM   1318 C CD1   . TYR A 1 179 ? 9.188   -5.275  11.242 1.00 37.23 ? 179 TYR A CD1   1 
ATOM   1319 C CD2   . TYR A 1 179 ? 8.148   -4.650  9.196  1.00 40.16 ? 179 TYR A CD2   1 
ATOM   1320 C CE1   . TYR A 1 179 ? 9.722   -4.011  11.368 1.00 34.91 ? 179 TYR A CE1   1 
ATOM   1321 C CE2   . TYR A 1 179 ? 8.676   -3.379  9.314  1.00 51.40 ? 179 TYR A CE2   1 
ATOM   1322 C CZ    . TYR A 1 179 ? 9.464   -3.067  10.401 1.00 48.23 ? 179 TYR A CZ    1 
ATOM   1323 O OH    . TYR A 1 179 ? 9.994   -1.805  10.527 1.00 53.17 ? 179 TYR A OH    1 
ATOM   1324 N N     . ALA A 1 180 ? 8.428   -9.502  11.887 1.00 37.49 ? 180 ALA A N     1 
ATOM   1325 C CA    . ALA A 1 180 ? 7.897   -10.612 12.664 1.00 40.96 ? 180 ALA A CA    1 
ATOM   1326 C C     . ALA A 1 180 ? 7.671   -10.086 14.076 1.00 33.07 ? 180 ALA A C     1 
ATOM   1327 O O     . ALA A 1 180 ? 7.798   -8.883  14.328 1.00 39.80 ? 180 ALA A O     1 
ATOM   1328 C CB    . ALA A 1 180 ? 8.848   -11.813 12.626 1.00 59.72 ? 180 ALA A CB    1 
ATOM   1329 N N     . TYR A 1 181 ? 7.334   -10.975 15.005 1.00 30.29 ? 181 TYR A N     1 
ATOM   1330 C CA    . TYR A 1 181 ? 7.233   -10.554 16.395 1.00 35.32 ? 181 TYR A CA    1 
ATOM   1331 C C     . TYR A 1 181 ? 8.556   -9.951  16.836 1.00 48.13 ? 181 TYR A C     1 
ATOM   1332 O O     . TYR A 1 181 ? 9.590   -10.627 16.830 1.00 51.36 ? 181 TYR A O     1 
ATOM   1333 C CB    . TYR A 1 181 ? 6.861   -11.727 17.298 1.00 37.14 ? 181 TYR A CB    1 
ATOM   1334 C CG    . TYR A 1 181 ? 6.908   -11.394 18.779 1.00 31.13 ? 181 TYR A CG    1 
ATOM   1335 C CD1   . TYR A 1 181 ? 5.907   -10.637 19.375 1.00 36.69 ? 181 TYR A CD1   1 
ATOM   1336 C CD2   . TYR A 1 181 ? 7.954   -11.837 19.579 1.00 40.86 ? 181 TYR A CD2   1 
ATOM   1337 C CE1   . TYR A 1 181 ? 5.945   -10.332 20.726 1.00 41.14 ? 181 TYR A CE1   1 
ATOM   1338 C CE2   . TYR A 1 181 ? 8.001   -11.537 20.931 1.00 41.89 ? 181 TYR A CE2   1 
ATOM   1339 C CZ    . TYR A 1 181 ? 6.994   -10.786 21.499 1.00 35.38 ? 181 TYR A CZ    1 
ATOM   1340 O OH    . TYR A 1 181 ? 7.036   -10.484 22.842 1.00 37.33 ? 181 TYR A OH    1 
ATOM   1341 N N     . ARG A 1 182 ? 8.523   -8.673  17.197 1.00 49.24 ? 182 ARG A N     1 
ATOM   1342 C CA    . ARG A 1 182 ? 9.682   -7.972  17.739 1.00 44.64 ? 182 ARG A CA    1 
ATOM   1343 C C     . ARG A 1 182 ? 10.945  -8.286  16.937 1.00 43.52 ? 182 ARG A C     1 
ATOM   1344 O O     . ARG A 1 182 ? 11.983  -8.668  17.483 1.00 53.54 ? 182 ARG A O     1 
ATOM   1345 C CB    . ARG A 1 182 ? 9.862   -8.317  19.218 1.00 36.21 ? 182 ARG A CB    1 
ATOM   1346 C CG    . ARG A 1 182 ? 8.634   -7.991  20.070 1.00 49.15 ? 182 ARG A CG    1 
ATOM   1347 C CD    . ARG A 1 182 ? 8.770   -6.641  20.758 1.00 59.18 ? 182 ARG A CD    1 
ATOM   1348 N NE    . ARG A 1 182 ? 7.935   -6.513  21.947 1.00 44.88 ? 182 ARG A NE    1 
ATOM   1349 C CZ    . ARG A 1 182 ? 6.655   -6.166  21.929 1.00 28.14 ? 182 ARG A CZ    1 
ATOM   1350 N NH1   . ARG A 1 182 ? 5.992   -6.027  20.793 1.00 33.97 ? 182 ARG A NH1   1 
ATOM   1351 N NH2   . ARG A 1 182 ? 6.023   -5.956  23.081 1.00 33.96 ? 182 ARG A NH2   1 
ATOM   1352 N N     . HIS A 1 183 ? 10.857  -8.115  15.617 1.00 34.91 ? 183 HIS A N     1 
ATOM   1353 C CA    . HIS A 1 183 ? 11.972  -8.476  14.753 1.00 43.03 ? 183 HIS A CA    1 
ATOM   1354 C C     . HIS A 1 183 ? 11.824  -7.849  13.373 1.00 37.56 ? 183 HIS A C     1 
ATOM   1355 O O     . HIS A 1 183 ? 10.723  -7.806  12.818 1.00 43.35 ? 183 HIS A O     1 
ATOM   1356 C CB    . HIS A 1 183 ? 12.082  -9.997  14.604 1.00 48.66 ? 183 HIS A CB    1 
ATOM   1357 C CG    . HIS A 1 183 ? 13.091  -10.423 13.586 1.00 49.12 ? 183 HIS A CG    1 
ATOM   1358 N ND1   . HIS A 1 183 ? 14.423  -10.609 13.889 1.00 47.97 ? 183 HIS A ND1   1 
ATOM   1359 C CD2   . HIS A 1 183 ? 12.967  -10.678 12.262 1.00 46.96 ? 183 HIS A CD2   1 
ATOM   1360 C CE1   . HIS A 1 183 ? 15.074  -10.969 12.797 1.00 52.76 ? 183 HIS A CE1   1 
ATOM   1361 N NE2   . HIS A 1 183 ? 14.214  -11.018 11.796 1.00 50.07 ? 183 HIS A NE2   1 
ATOM   1362 N N     . SER A 1 184 ? 12.949  -7.386  12.821 1.00 36.58 ? 184 SER A N     1 
ATOM   1363 C CA    . SER A 1 184 ? 13.055  -7.010  11.417 1.00 44.10 ? 184 SER A CA    1 
ATOM   1364 C C     . SER A 1 184 ? 14.268  -7.695  10.801 1.00 48.54 ? 184 SER A C     1 
ATOM   1365 O O     . SER A 1 184 ? 15.312  -7.828  11.447 1.00 53.52 ? 184 SER A O     1 
ATOM   1366 C CB    . SER A 1 184 ? 13.179  -5.490  11.236 1.00 46.82 ? 184 SER A CB    1 
ATOM   1367 O OG    . SER A 1 184 ? 14.246  -4.964  12.004 1.00 52.70 ? 184 SER A OG    1 
ATOM   1368 N N     . SER A 1 185 ? 14.124  -8.121  9.547  1.00 49.44 ? 185 SER A N     1 
ATOM   1369 C CA    . SER A 1 185 ? 15.185  -8.802  8.814  1.00 54.36 ? 185 SER A CA    1 
ATOM   1370 C C     . SER A 1 185 ? 16.137  -7.844  8.111  1.00 48.63 ? 185 SER A C     1 
ATOM   1371 O O     . SER A 1 185 ? 17.044  -8.302  7.408  1.00 46.73 ? 185 SER A O     1 
ATOM   1372 C CB    . SER A 1 185 ? 14.580  -9.758  7.779  1.00 65.04 ? 185 SER A CB    1 
ATOM   1373 O OG    . SER A 1 185 ? 13.471  -10.459 8.314  1.00 65.88 ? 185 SER A OG    1 
ATOM   1374 N N     . ALA A 1 186 ? 15.953  -6.536  8.272  1.00 51.39 ? 186 ALA A N     1 
ATOM   1375 C CA    . ALA A 1 186 ? 16.838  -5.578  7.626  1.00 55.69 ? 186 ALA A CA    1 
ATOM   1376 C C     . ALA A 1 186 ? 18.263  -5.738  8.144  1.00 54.15 ? 186 ALA A C     1 
ATOM   1377 O O     . ALA A 1 186 ? 18.492  -6.129  9.292  1.00 42.63 ? 186 ALA A O     1 
ATOM   1378 C CB    . ALA A 1 186 ? 16.342  -4.152  7.867  1.00 51.17 ? 186 ALA A CB    1 
ATOM   1379 N N     . SER A 1 187 ? 19.225  -5.433  7.279  1.00 54.02 ? 187 SER A N     1 
ATOM   1380 C CA    . SER A 1 187 ? 20.625  -5.626  7.626  1.00 59.33 ? 187 SER A CA    1 
ATOM   1381 C C     . SER A 1 187 ? 20.955  -4.881  8.918  1.00 59.31 ? 187 SER A C     1 
ATOM   1382 O O     . SER A 1 187 ? 20.414  -3.796  9.165  1.00 59.81 ? 187 SER A O     1 
ATOM   1383 C CB    . SER A 1 187 ? 21.526  -5.136  6.490  1.00 53.98 ? 187 SER A CB    1 
ATOM   1384 O OG    . SER A 1 187 ? 22.893  -5.196  6.856  1.00 53.03 ? 187 SER A OG    1 
ATOM   1385 N N     . PRO A 1 188 ? 21.831  -5.429  9.768  1.00 45.88 ? 188 PRO A N     1 
ATOM   1386 C CA    . PRO A 1 188 ? 22.160  -4.749  11.027 1.00 48.37 ? 188 PRO A CA    1 
ATOM   1387 C C     . PRO A 1 188 ? 23.154  -3.610  10.877 1.00 42.69 ? 188 PRO A C     1 
ATOM   1388 O O     . PRO A 1 188 ? 23.351  -2.857  11.840 1.00 45.89 ? 188 PRO A O     1 
ATOM   1389 C CB    . PRO A 1 188 ? 22.744  -5.879  11.881 1.00 49.45 ? 188 PRO A CB    1 
ATOM   1390 C CG    . PRO A 1 188 ? 23.397  -6.770  10.887 1.00 54.35 ? 188 PRO A CG    1 
ATOM   1391 C CD    . PRO A 1 188 ? 22.523  -6.726  9.653  1.00 48.97 ? 188 PRO A CD    1 
ATOM   1392 N N     . ASP A 1 189 ? 23.791  -3.464  9.717  1.00 38.35 ? 189 ASP A N     1 
ATOM   1393 C CA    . ASP A 1 189 ? 24.648  -2.315  9.456  1.00 50.91 ? 189 ASP A CA    1 
ATOM   1394 C C     . ASP A 1 189 ? 23.859  -1.083  9.033  1.00 56.94 ? 189 ASP A C     1 
ATOM   1395 O O     . ASP A 1 189 ? 24.453  -0.012  8.872  1.00 53.68 ? 189 ASP A O     1 
ATOM   1396 C CB    . ASP A 1 189 ? 25.681  -2.663  8.379  1.00 49.57 ? 189 ASP A CB    1 
ATOM   1397 C CG    . ASP A 1 189 ? 25.189  -2.361  6.973  1.00 71.37 ? 189 ASP A CG    1 
ATOM   1398 O OD1   . ASP A 1 189 ? 23.996  -2.606  6.697  1.00 70.74 ? 189 ASP A OD1   1 
ATOM   1399 O OD2   . ASP A 1 189 ? 25.993  -1.884  6.143  1.00 61.93 ? 189 ASP A OD2   1 
ATOM   1400 N N     . LEU A 1 190 ? 22.546  -1.209  8.858  1.00 61.04 ? 190 LEU A N     1 
ATOM   1401 C CA    . LEU A 1 190 ? 21.728  -0.103  8.386  1.00 54.78 ? 190 LEU A CA    1 
ATOM   1402 C C     . LEU A 1 190 ? 21.358  0.828   9.532  1.00 45.56 ? 190 LEU A C     1 
ATOM   1403 O O     . LEU A 1 190 ? 21.016  0.382   10.632 1.00 46.82 ? 190 LEU A O     1 
ATOM   1404 C CB    . LEU A 1 190 ? 20.454  -0.629  7.722  1.00 57.34 ? 190 LEU A CB    1 
ATOM   1405 C CG    . LEU A 1 190 ? 20.546  -1.114  6.271  1.00 65.41 ? 190 LEU A CG    1 
ATOM   1406 C CD1   . LEU A 1 190 ? 19.151  -1.347  5.711  1.00 53.23 ? 190 LEU A CD1   1 
ATOM   1407 C CD2   . LEU A 1 190 ? 21.315  -0.134  5.396  1.00 60.07 ? 190 LEU A CD2   1 
ATOM   1408 N N     . ILE A 1 191 ? 21.425  2.129   9.264  1.00 50.13 ? 191 ILE A N     1 
ATOM   1409 C CA    . ILE A 1 191 ? 21.008  3.161   10.206 1.00 46.37 ? 191 ILE A CA    1 
ATOM   1410 C C     . ILE A 1 191 ? 19.781  3.855   9.627  1.00 37.75 ? 191 ILE A C     1 
ATOM   1411 O O     . ILE A 1 191 ? 19.864  4.525   8.590  1.00 37.02 ? 191 ILE A O     1 
ATOM   1412 C CB    . ILE A 1 191 ? 22.134  4.166   10.489 1.00 49.06 ? 191 ILE A CB    1 
ATOM   1413 C CG1   . ILE A 1 191 ? 23.450  3.421   10.737 1.00 54.63 ? 191 ILE A CG1   1 
ATOM   1414 C CG2   . ILE A 1 191 ? 21.760  5.043   11.680 1.00 51.76 ? 191 ILE A CG2   1 
ATOM   1415 C CD1   . ILE A 1 191 ? 24.567  4.287   11.289 1.00 58.37 ? 191 ILE A CD1   1 
ATOM   1416 N N     . PHE A 1 192 ? 18.644  3.672   10.291 1.00 39.51 ? 192 PHE A N     1 
ATOM   1417 C CA    . PHE A 1 192 ? 17.398  4.311   9.894  1.00 42.82 ? 192 PHE A CA    1 
ATOM   1418 C C     . PHE A 1 192 ? 17.446  5.810   10.159 1.00 34.84 ? 192 PHE A C     1 
ATOM   1419 O O     . PHE A 1 192 ? 17.769  6.249   11.267 1.00 36.68 ? 192 PHE A O     1 
ATOM   1420 C CB    . PHE A 1 192 ? 16.235  3.680   10.657 1.00 36.71 ? 192 PHE A CB    1 
ATOM   1421 C CG    . PHE A 1 192 ? 16.193  2.183   10.554 1.00 30.87 ? 192 PHE A CG    1 
ATOM   1422 C CD1   . PHE A 1 192 ? 16.515  1.556   9.364  1.00 34.87 ? 192 PHE A CD1   1 
ATOM   1423 C CD2   . PHE A 1 192 ? 15.845  1.404   11.643 1.00 34.52 ? 192 PHE A CD2   1 
ATOM   1424 C CE1   . PHE A 1 192 ? 16.485  0.181   9.258  1.00 30.67 ? 192 PHE A CE1   1 
ATOM   1425 C CE2   . PHE A 1 192 ? 15.813  0.026   11.542 1.00 31.15 ? 192 PHE A CE2   1 
ATOM   1426 C CZ    . PHE A 1 192 ? 16.134  -0.585  10.348 1.00 22.44 ? 192 PHE A CZ    1 
ATOM   1427 N N     . THR A 1 193 ? 17.105  6.595   9.138  1.00 38.07 ? 193 THR A N     1 
ATOM   1428 C CA    . THR A 1 193 ? 17.081  8.047   9.235  1.00 42.92 ? 193 THR A CA    1 
ATOM   1429 C C     . THR A 1 193 ? 15.678  8.634   9.217  1.00 42.58 ? 193 THR A C     1 
ATOM   1430 O O     . THR A 1 193 ? 15.449  9.665   9.851  1.00 40.45 ? 193 THR A O     1 
ATOM   1431 C CB    . THR A 1 193 ? 17.894  8.664   8.091  1.00 50.49 ? 193 THR A CB    1 
ATOM   1432 O OG1   . THR A 1 193 ? 17.406  8.175   6.836  1.00 49.12 ? 193 THR A OG1   1 
ATOM   1433 C CG2   . THR A 1 193 ? 19.364  8.299   8.239  1.00 41.56 ? 193 THR A CG2   1 
ATOM   1434 N N     . SER A 1 194 ? 14.738  8.009   8.512  1.00 50.15 ? 194 SER A N     1 
ATOM   1435 C CA    . SER A 1 194 ? 13.344  8.434   8.551  1.00 47.71 ? 194 SER A CA    1 
ATOM   1436 C C     . SER A 1 194 ? 12.484  7.326   7.960  1.00 47.53 ? 194 SER A C     1 
ATOM   1437 O O     . SER A 1 194 ? 12.987  6.331   7.431  1.00 38.95 ? 194 SER A O     1 
ATOM   1438 C CB    . SER A 1 194 ? 13.127  9.751   7.803  1.00 37.39 ? 194 SER A CB    1 
ATOM   1439 O OG    . SER A 1 194 ? 12.664  9.520   6.484  1.00 30.53 ? 194 SER A OG    1 
ATOM   1440 N N     . VAL A 1 195 ? 11.169  7.522   8.053  1.00 57.77 ? 195 VAL A N     1 
ATOM   1441 C CA    . VAL A 1 195 ? 10.190  6.518   7.660  1.00 51.36 ? 195 VAL A CA    1 
ATOM   1442 C C     . VAL A 1 195 ? 8.936   7.238   7.191  1.00 51.45 ? 195 VAL A C     1 
ATOM   1443 O O     . VAL A 1 195 ? 8.653   8.362   7.612  1.00 52.41 ? 195 VAL A O     1 
ATOM   1444 C CB    . VAL A 1 195 ? 9.868   5.559   8.831  1.00 41.17 ? 195 VAL A CB    1 
ATOM   1445 C CG1   . VAL A 1 195 ? 9.556   6.358   10.093 1.00 45.60 ? 195 VAL A CG1   1 
ATOM   1446 C CG2   . VAL A 1 195 ? 8.706   4.643   8.475  1.00 47.72 ? 195 VAL A CG2   1 
ATOM   1447 N N     . LEU A 1 196 ? 8.182   6.584   6.313  1.00 57.31 ? 196 LEU A N     1 
ATOM   1448 C CA    . LEU A 1 196 ? 6.876   7.069   5.886  1.00 54.33 ? 196 LEU A CA    1 
ATOM   1449 C C     . LEU A 1 196 ? 5.807   6.185   6.510  1.00 44.42 ? 196 LEU A C     1 
ATOM   1450 O O     . LEU A 1 196 ? 5.827   4.961   6.339  1.00 45.71 ? 196 LEU A O     1 
ATOM   1451 C CB    . LEU A 1 196 ? 6.752   7.076   4.363  1.00 57.74 ? 196 LEU A CB    1 
ATOM   1452 C CG    . LEU A 1 196 ? 5.474   7.732   3.832  1.00 52.39 ? 196 LEU A CG    1 
ATOM   1453 C CD1   . LEU A 1 196 ? 5.401   9.203   4.226  1.00 50.97 ? 196 LEU A CD1   1 
ATOM   1454 C CD2   . LEU A 1 196 ? 5.384   7.578   2.325  1.00 43.25 ? 196 LEU A CD2   1 
ATOM   1455 N N     . PHE A 1 197 ? 4.881   6.807   7.230  1.00 45.53 ? 197 PHE A N     1 
ATOM   1456 C CA    . PHE A 1 197 ? 3.817   6.112   7.935  1.00 56.35 ? 197 PHE A CA    1 
ATOM   1457 C C     . PHE A 1 197 ? 2.494   6.333   7.211  1.00 62.42 ? 197 PHE A C     1 
ATOM   1458 O O     . PHE A 1 197 ? 2.316   7.333   6.512  1.00 53.56 ? 197 PHE A O     1 
ATOM   1459 C CB    . PHE A 1 197 ? 3.710   6.610   9.380  1.00 57.45 ? 197 PHE A CB    1 
ATOM   1460 C CG    . PHE A 1 197 ? 4.839   6.165   10.276 1.00 58.38 ? 197 PHE A CG    1 
ATOM   1461 C CD1   . PHE A 1 197 ? 5.487   4.957   10.071 1.00 61.21 ? 197 PHE A CD1   1 
ATOM   1462 C CD2   . PHE A 1 197 ? 5.246   6.962   11.334 1.00 58.17 ? 197 PHE A CD2   1 
ATOM   1463 C CE1   . PHE A 1 197 ? 6.517   4.556   10.902 1.00 52.42 ? 197 PHE A CE1   1 
ATOM   1464 C CE2   . PHE A 1 197 ? 6.275   6.566   12.167 1.00 50.83 ? 197 PHE A CE2   1 
ATOM   1465 C CZ    . PHE A 1 197 ? 6.910   5.362   11.950 1.00 39.62 ? 197 PHE A CZ    1 
ATOM   1466 N N     . GLU A 1 198 ? 1.567   5.388   7.379  1.00 59.78 ? 198 GLU A N     1 
ATOM   1467 C CA    . GLU A 1 198 ? 0.253   5.466   6.745  1.00 58.26 ? 198 GLU A CA    1 
ATOM   1468 C C     . GLU A 1 198 ? -0.789  4.860   7.674  1.00 56.94 ? 198 GLU A C     1 
ATOM   1469 O O     . GLU A 1 198 ? -0.674  3.692   8.059  1.00 54.03 ? 198 GLU A O     1 
ATOM   1470 C CB    . GLU A 1 198 ? 0.249   4.743   5.394  1.00 59.00 ? 198 GLU A CB    1 
ATOM   1471 C CG    . GLU A 1 198 ? -0.828  5.210   4.426  1.00 59.77 ? 198 GLU A CG    1 
ATOM   1472 C CD    . GLU A 1 198 ? -0.606  4.689   3.017  1.00 61.23 ? 198 GLU A CD    1 
ATOM   1473 O OE1   . GLU A 1 198 ? -0.615  3.454   2.830  1.00 70.30 ? 198 GLU A OE1   1 
ATOM   1474 O OE2   . GLU A 1 198 ? -0.421  5.515   2.098  1.00 57.82 ? 198 GLU A OE2   1 
ATOM   1475 N N     . GLY A 1 199 ? -1.803  5.653   8.026  1.00 58.96 ? 199 GLY A N     1 
ATOM   1476 C CA    . GLY A 1 199 ? -2.893  5.174   8.845  1.00 56.60 ? 199 GLY A CA    1 
ATOM   1477 C C     . GLY A 1 199 ? -4.231  5.507   8.214  1.00 64.55 ? 199 GLY A C     1 
ATOM   1478 O O     . GLY A 1 199 ? -4.334  6.355   7.326  1.00 64.35 ? 199 GLY A O     1 
ATOM   1479 N N     . VAL A 1 200 ? -5.263  4.822   8.691  1.00 58.55 ? 200 VAL A N     1 
ATOM   1480 C CA    . VAL A 1 200 ? -6.612  5.017   8.153  1.00 54.09 ? 200 VAL A CA    1 
ATOM   1481 C C     . VAL A 1 200 ? -7.231  6.250   8.809  1.00 53.51 ? 200 VAL A C     1 
ATOM   1482 O O     . VAL A 1 200 ? -7.223  6.351   10.046 1.00 51.54 ? 200 VAL A O     1 
ATOM   1483 C CB    . VAL A 1 200 ? -7.481  3.778   8.379  1.00 53.43 ? 200 VAL A CB    1 
ATOM   1484 C CG1   . VAL A 1 200 ? -7.106  2.676   7.395  1.00 45.42 ? 200 VAL A CG1   1 
ATOM   1485 C CG2   . VAL A 1 200 ? -7.398  3.279   9.825  1.00 57.02 ? 200 VAL A CG2   1 
ATOM   1486 N N     . PRO A 1 201 ? -7.773  7.194   8.036  1.00 58.37 ? 201 PRO A N     1 
ATOM   1487 C CA    . PRO A 1 201 ? -8.333  8.409   8.645  1.00 45.75 ? 201 PRO A CA    1 
ATOM   1488 C C     . PRO A 1 201 ? -9.487  8.086   9.586  1.00 42.58 ? 201 PRO A C     1 
ATOM   1489 O O     . PRO A 1 201 ? -10.268 7.163   9.348  1.00 50.70 ? 201 PRO A O     1 
ATOM   1490 C CB    . PRO A 1 201 ? -8.794  9.229   7.433  1.00 52.05 ? 201 PRO A CB    1 
ATOM   1491 C CG    . PRO A 1 201 ? -7.974  8.700   6.289  1.00 50.92 ? 201 PRO A CG    1 
ATOM   1492 C CD    . PRO A 1 201 ? -7.860  7.239   6.566  1.00 59.14 ? 201 PRO A CD    1 
ATOM   1493 N N     . GLY A 1 202 ? -9.591  8.863   10.667 1.00 46.06 ? 202 GLY A N     1 
ATOM   1494 C CA    . GLY A 1 202 ? -10.559 8.553   11.706 1.00 45.26 ? 202 GLY A CA    1 
ATOM   1495 C C     . GLY A 1 202 ? -10.974 9.765   12.512 1.00 41.70 ? 202 GLY A C     1 
ATOM   1496 O O     . GLY A 1 202 ? -10.392 10.848  12.408 1.00 43.00 ? 202 GLY A O     1 
ATOM   1497 N N     . GLU A 1 203 ? -12.002 9.554   13.333 1.00 42.03 ? 203 GLU A N     1 
ATOM   1498 C CA    . GLU A 1 203 ? -12.538 10.614  14.179 1.00 53.71 ? 203 GLU A CA    1 
ATOM   1499 C C     . GLU A 1 203 ? -11.592 10.899  15.340 1.00 55.20 ? 203 GLU A C     1 
ATOM   1500 O O     . GLU A 1 203 ? -11.071 9.981   15.979 1.00 59.91 ? 203 GLU A O     1 
ATOM   1501 C CB    . GLU A 1 203 ? -13.922 10.215  14.701 1.00 54.70 ? 203 GLU A CB    1 
ATOM   1502 C CG    . GLU A 1 203 ? -14.516 11.142  15.761 1.00 61.51 ? 203 GLU A CG    1 
ATOM   1503 C CD    . GLU A 1 203 ? -14.756 12.549  15.248 1.00 65.29 ? 203 GLU A CD    1 
ATOM   1504 O OE1   . GLU A 1 203 ? -15.205 12.694  14.092 1.00 56.14 ? 203 GLU A OE1   1 
ATOM   1505 O OE2   . GLU A 1 203 ? -14.502 13.510  16.006 1.00 52.18 ? 203 GLU A OE2   1 
ATOM   1506 N N     . ARG A 1 204 ? -11.383 12.187  15.620 1.00 52.55 ? 204 ARG A N     1 
ATOM   1507 C CA    . ARG A 1 204 ? -10.380 12.575  16.608 1.00 48.15 ? 204 ARG A CA    1 
ATOM   1508 C C     . ARG A 1 204 ? -10.828 12.239  18.025 1.00 50.19 ? 204 ARG A C     1 
ATOM   1509 O O     . ARG A 1 204 ? -10.006 11.846  18.861 1.00 48.78 ? 204 ARG A O     1 
ATOM   1510 C CB    . ARG A 1 204 ? -10.081 14.067  16.490 1.00 54.86 ? 204 ARG A CB    1 
ATOM   1511 C CG    . ARG A 1 204 ? -9.201  14.448  15.315 1.00 54.42 ? 204 ARG A CG    1 
ATOM   1512 C CD    . ARG A 1 204 ? -9.250  15.950  15.111 1.00 61.17 ? 204 ARG A CD    1 
ATOM   1513 N NE    . ARG A 1 204 ? -7.951  16.552  14.839 1.00 50.49 ? 204 ARG A NE    1 
ATOM   1514 C CZ    . ARG A 1 204 ? -7.435  16.714  13.628 1.00 56.16 ? 204 ARG A CZ    1 
ATOM   1515 N NH1   . ARG A 1 204 ? -8.033  16.235  12.549 1.00 45.70 ? 204 ARG A NH1   1 
ATOM   1516 N NH2   . ARG A 1 204 ? -6.293  17.380  13.495 1.00 64.66 ? 204 ARG A NH2   1 
ATOM   1517 N N     . ASP A 1 205 ? -12.120 12.404  18.323 1.00 57.18 ? 205 ASP A N     1 
ATOM   1518 C CA    . ASP A 1 205 ? -12.618 12.012  19.637 1.00 51.43 ? 205 ASP A CA    1 
ATOM   1519 C C     . ASP A 1 205 ? -12.322 10.546  19.918 1.00 48.97 ? 205 ASP A C     1 
ATOM   1520 O O     . ASP A 1 205 ? -12.153 10.156  21.079 1.00 41.96 ? 205 ASP A O     1 
ATOM   1521 C CB    . ASP A 1 205 ? -14.121 12.276  19.735 1.00 55.99 ? 205 ASP A CB    1 
ATOM   1522 C CG    . ASP A 1 205 ? -14.439 13.714  20.095 1.00 67.10 ? 205 ASP A CG    1 
ATOM   1523 O OD1   . ASP A 1 205 ? -14.303 14.076  21.283 1.00 68.54 ? 205 ASP A OD1   1 
ATOM   1524 O OD2   . ASP A 1 205 ? -14.828 14.483  19.191 1.00 70.71 ? 205 ASP A OD2   1 
ATOM   1525 N N     . ASP A 1 206 ? -12.254 9.723   18.870 1.00 49.11 ? 206 ASP A N     1 
ATOM   1526 C CA    . ASP A 1 206 ? -11.891 8.322   19.038 1.00 53.02 ? 206 ASP A CA    1 
ATOM   1527 C C     . ASP A 1 206 ? -10.391 8.162   19.252 1.00 48.86 ? 206 ASP A C     1 
ATOM   1528 O O     . ASP A 1 206 ? -9.963  7.388   20.115 1.00 53.52 ? 206 ASP A O     1 
ATOM   1529 C CB    . ASP A 1 206 ? -12.342 7.518   17.818 1.00 57.04 ? 206 ASP A CB    1 
ATOM   1530 C CG    . ASP A 1 206 ? -13.852 7.417   17.713 1.00 65.16 ? 206 ASP A CG    1 
ATOM   1531 O OD1   . ASP A 1 206 ? -14.521 7.354   18.766 1.00 51.91 ? 206 ASP A OD1   1 
ATOM   1532 O OD2   . ASP A 1 206 ? -14.369 7.400   16.575 1.00 53.07 ? 206 ASP A OD2   1 
ATOM   1533 N N     . ILE A 1 207 ? -9.581  8.889   18.479 1.00 51.92 ? 207 ILE A N     1 
ATOM   1534 C CA    . ILE A 1 207 ? -8.132  8.791   18.623 1.00 45.76 ? 207 ILE A CA    1 
ATOM   1535 C C     . ILE A 1 207 ? -7.708  9.231   20.020 1.00 40.57 ? 207 ILE A C     1 
ATOM   1536 O O     . ILE A 1 207 ? -6.841  8.607   20.645 1.00 35.72 ? 207 ILE A O     1 
ATOM   1537 C CB    . ILE A 1 207 ? -7.435  9.610   17.520 1.00 43.66 ? 207 ILE A CB    1 
ATOM   1538 C CG1   . ILE A 1 207 ? -7.848  9.101   16.136 1.00 39.78 ? 207 ILE A CG1   1 
ATOM   1539 C CG2   . ILE A 1 207 ? -5.935  9.518   17.662 1.00 53.32 ? 207 ILE A CG2   1 
ATOM   1540 C CD1   . ILE A 1 207 ? -7.267  9.900   14.984 1.00 37.15 ? 207 ILE A CD1   1 
ATOM   1541 N N     . ARG A 1 208 ? -8.306  10.309  20.531 1.00 42.65 ? 208 ARG A N     1 
ATOM   1542 C CA    . ARG A 1 208 ? -8.109  10.681  21.929 1.00 41.37 ? 208 ARG A CA    1 
ATOM   1543 C C     . ARG A 1 208 ? -8.443  9.514   22.848 1.00 41.33 ? 208 ARG A C     1 
ATOM   1544 O O     . ARG A 1 208 ? -7.619  9.080   23.660 1.00 44.37 ? 208 ARG A O     1 
ATOM   1545 C CB    . ARG A 1 208 ? -8.983  11.886  22.284 1.00 45.99 ? 208 ARG A CB    1 
ATOM   1546 C CG    . ARG A 1 208 ? -8.291  13.230  22.189 1.00 53.00 ? 208 ARG A CG    1 
ATOM   1547 C CD    . ARG A 1 208 ? -9.295  14.360  21.995 1.00 53.08 ? 208 ARG A CD    1 
ATOM   1548 N NE    . ARG A 1 208 ? -8.923  15.199  20.861 1.00 69.07 ? 208 ARG A NE    1 
ATOM   1549 C CZ    . ARG A 1 208 ? -9.757  15.624  19.920 1.00 66.18 ? 208 ARG A CZ    1 
ATOM   1550 N NH1   . ARG A 1 208 ? -11.054 15.360  19.967 1.00 66.25 ? 208 ARG A NH1   1 
ATOM   1551 N NH2   . ARG A 1 208 ? -9.277  16.336  18.905 1.00 64.26 ? 208 ARG A NH2   1 
ATOM   1552 N N     . ARG A 1 209 ? -9.671  9.006   22.729 1.00 45.20 ? 209 ARG A N     1 
ATOM   1553 C CA    . ARG A 1 209 ? -10.137 7.921   23.586 1.00 45.92 ? 209 ARG A CA    1 
ATOM   1554 C C     . ARG A 1 209 ? -9.112  6.796   23.661 1.00 38.65 ? 209 ARG A C     1 
ATOM   1555 O O     . ARG A 1 209 ? -8.697  6.387   24.751 1.00 38.41 ? 209 ARG A O     1 
ATOM   1556 C CB    . ARG A 1 209 ? -11.478 7.404   23.060 1.00 49.19 ? 209 ARG A CB    1 
ATOM   1557 C CG    . ARG A 1 209 ? -12.278 6.576   24.051 1.00 45.63 ? 209 ARG A CG    1 
ATOM   1558 C CD    . ARG A 1 209 ? -13.424 5.845   23.358 1.00 61.66 ? 209 ARG A CD    1 
ATOM   1559 N NE    . ARG A 1 209 ? -14.115 6.683   22.383 1.00 77.30 ? 209 ARG A NE    1 
ATOM   1560 C CZ    . ARG A 1 209 ? -14.832 7.758   22.684 1.00 63.87 ? 209 ARG A CZ    1 
ATOM   1561 N NH1   . ARG A 1 209 ? -14.995 8.154   23.936 1.00 60.58 ? 209 ARG A NH1   1 
ATOM   1562 N NH2   . ARG A 1 209 ? -15.404 8.451   21.703 1.00 52.90 ? 209 ARG A NH2   1 
ATOM   1563 N N     . ALA A 1 210 ? -8.680  6.292   22.504 1.00 35.36 ? 210 ALA A N     1 
ATOM   1564 C CA    . ALA A 1 210 ? -7.724  5.189   22.495 1.00 51.04 ? 210 ALA A CA    1 
ATOM   1565 C C     . ALA A 1 210 ? -6.401  5.595   23.133 1.00 42.73 ? 210 ALA A C     1 
ATOM   1566 O O     . ALA A 1 210 ? -5.762  4.788   23.819 1.00 36.75 ? 210 ALA A O     1 
ATOM   1567 C CB    . ALA A 1 210 ? -7.505  4.700   21.064 1.00 43.83 ? 210 ALA A CB    1 
ATOM   1568 N N     . MET A 1 211 ? -5.971  6.842   22.923 1.00 36.20 ? 211 MET A N     1 
ATOM   1569 C CA    . MET A 1 211 ? -4.721  7.291   23.527 1.00 30.37 ? 211 MET A CA    1 
ATOM   1570 C C     . MET A 1 211 ? -4.856  7.457   25.034 1.00 35.60 ? 211 MET A C     1 
ATOM   1571 O O     . MET A 1 211 ? -3.876  7.274   25.766 1.00 39.31 ? 211 MET A O     1 
ATOM   1572 C CB    . MET A 1 211 ? -4.267  8.605   22.892 1.00 35.22 ? 211 MET A CB    1 
ATOM   1573 C CG    . MET A 1 211 ? -3.733  8.444   21.482 1.00 32.26 ? 211 MET A CG    1 
ATOM   1574 S SD    . MET A 1 211 ? -3.727  9.978   20.540 1.00 36.90 ? 211 MET A SD    1 
ATOM   1575 C CE    . MET A 1 211 ? -3.130  9.381   18.962 1.00 35.93 ? 211 MET A CE    1 
ATOM   1576 N N     . ASP A 1 212 ? -6.050  7.804   25.516 1.00 39.77 ? 212 ASP A N     1 
ATOM   1577 C CA    . ASP A 1 212 ? -6.268  7.896   26.954 1.00 28.30 ? 212 ASP A CA    1 
ATOM   1578 C C     . ASP A 1 212 ? -6.417  6.519   27.584 1.00 28.28 ? 212 ASP A C     1 
ATOM   1579 O O     . ASP A 1 212 ? -6.071  6.336   28.756 1.00 29.22 ? 212 ASP A O     1 
ATOM   1580 C CB    . ASP A 1 212 ? -7.505  8.746   27.244 1.00 30.69 ? 212 ASP A CB    1 
ATOM   1581 C CG    . ASP A 1 212 ? -7.269  10.220  26.984 1.00 28.72 ? 212 ASP A CG    1 
ATOM   1582 O OD1   . ASP A 1 212 ? -6.762  10.559  25.894 1.00 35.95 ? 212 ASP A OD1   1 
ATOM   1583 O OD2   . ASP A 1 212 ? -7.589  11.041  27.869 1.00 39.19 ? 212 ASP A OD2   1 
ATOM   1584 N N     . GLU A 1 213 ? -6.933  5.549   26.828 1.00 38.26 ? 213 GLU A N     1 
ATOM   1585 C CA    . GLU A 1 213 ? -6.964  4.174   27.309 1.00 38.72 ? 213 GLU A CA    1 
ATOM   1586 C C     . GLU A 1 213 ? -5.572  3.557   27.268 1.00 32.32 ? 213 GLU A C     1 
ATOM   1587 O O     . GLU A 1 213 ? -5.201  2.783   28.158 1.00 41.08 ? 213 GLU A O     1 
ATOM   1588 C CB    . GLU A 1 213 ? -7.948  3.355   26.475 1.00 43.73 ? 213 GLU A CB    1 
ATOM   1589 C CG    . GLU A 1 213 ? -9.369  3.902   26.501 1.00 41.49 ? 213 GLU A CG    1 
ATOM   1590 C CD    . GLU A 1 213 ? -10.249 3.309   25.419 1.00 55.06 ? 213 GLU A CD    1 
ATOM   1591 O OE1   . GLU A 1 213 ? -11.281 2.694   25.759 1.00 54.99 ? 213 GLU A OE1   1 
ATOM   1592 O OE2   . GLU A 1 213 ? -9.905  3.451   24.227 1.00 63.79 ? 213 GLU A OE2   1 
ATOM   1593 N N     . VAL A 1 214 ? -4.788  3.894   26.242 1.00 38.75 ? 214 VAL A N     1 
ATOM   1594 C CA    . VAL A 1 214 ? -3.398  3.452   26.186 1.00 30.75 ? 214 VAL A CA    1 
ATOM   1595 C C     . VAL A 1 214 ? -2.638  3.955   27.407 1.00 28.86 ? 214 VAL A C     1 
ATOM   1596 O O     . VAL A 1 214 ? -1.961  3.187   28.101 1.00 37.65 ? 214 VAL A O     1 
ATOM   1597 C CB    . VAL A 1 214 ? -2.741  3.926   24.876 1.00 28.66 ? 214 VAL A CB    1 
ATOM   1598 C CG1   . VAL A 1 214 ? -1.224  3.996   25.017 1.00 45.81 ? 214 VAL A CG1   1 
ATOM   1599 C CG2   . VAL A 1 214 ? -3.130  3.011   23.726 1.00 31.55 ? 214 VAL A CG2   1 
ATOM   1600 N N     . GLN A 1 215 ? -2.746  5.255   27.693 1.00 29.17 ? 215 GLN A N     1 
ATOM   1601 C CA    . GLN A 1 215 ? -1.991  5.832   28.799 1.00 34.28 ? 215 GLN A CA    1 
ATOM   1602 C C     . GLN A 1 215 ? -2.508  5.354   30.150 1.00 31.81 ? 215 GLN A C     1 
ATOM   1603 O O     . GLN A 1 215 ? -1.724  5.217   31.096 1.00 29.63 ? 215 GLN A O     1 
ATOM   1604 C CB    . GLN A 1 215 ? -2.035  7.358   28.727 1.00 36.65 ? 215 GLN A CB    1 
ATOM   1605 C CG    . GLN A 1 215 ? -1.656  8.046   30.030 1.00 36.18 ? 215 GLN A CG    1 
ATOM   1606 C CD    . GLN A 1 215 ? -1.401  9.529   29.857 1.00 44.51 ? 215 GLN A CD    1 
ATOM   1607 O OE1   . GLN A 1 215 ? -1.496  10.063  28.752 1.00 48.30 ? 215 GLN A OE1   1 
ATOM   1608 N NE2   . GLN A 1 215 ? -1.074  10.204  30.953 1.00 50.26 ? 215 GLN A NE2   1 
ATOM   1609 N N     . HIS A 1 216 ? -3.814  5.105   30.269 1.00 40.09 ? 216 HIS A N     1 
ATOM   1610 C CA    . HIS A 1 216 ? -4.349  4.622   31.537 1.00 29.94 ? 216 HIS A CA    1 
ATOM   1611 C C     . HIS A 1 216 ? -3.818  3.231   31.859 1.00 24.30 ? 216 HIS A C     1 
ATOM   1612 O O     . HIS A 1 216 ? -3.541  2.917   33.022 1.00 26.07 ? 216 HIS A O     1 
ATOM   1613 C CB    . HIS A 1 216 ? -5.876  4.614   31.497 1.00 28.17 ? 216 HIS A CB    1 
ATOM   1614 C CG    . HIS A 1 216 ? -6.505  4.109   32.757 1.00 22.61 ? 216 HIS A CG    1 
ATOM   1615 N ND1   . HIS A 1 216 ? -7.056  2.850   32.862 1.00 25.87 ? 216 HIS A ND1   1 
ATOM   1616 C CD2   . HIS A 1 216 ? -6.656  4.689   33.971 1.00 24.65 ? 216 HIS A CD2   1 
ATOM   1617 C CE1   . HIS A 1 216 ? -7.527  2.679   34.085 1.00 26.61 ? 216 HIS A CE1   1 
ATOM   1618 N NE2   . HIS A 1 216 ? -7.296  3.779   34.778 1.00 22.86 ? 216 HIS A NE2   1 
ATOM   1619 N N     . HIS A 1 217 ? -3.678  2.386   30.838 1.00 29.07 ? 217 HIS A N     1 
ATOM   1620 C CA    . HIS A 1 217 ? -3.103  1.059   31.028 1.00 30.68 ? 217 HIS A CA    1 
ATOM   1621 C C     . HIS A 1 217 ? -1.677  1.163   31.554 1.00 32.52 ? 217 HIS A C     1 
ATOM   1622 O O     . HIS A 1 217 ? -1.322  0.546   32.566 1.00 28.09 ? 217 HIS A O     1 
ATOM   1623 C CB    . HIS A 1 217 ? -3.158  0.309   29.693 1.00 31.03 ? 217 HIS A CB    1 
ATOM   1624 C CG    . HIS A 1 217 ? -2.232  -0.863  29.597 1.00 37.68 ? 217 HIS A CG    1 
ATOM   1625 N ND1   . HIS A 1 217 ? -1.107  -0.858  28.800 1.00 36.44 ? 217 HIS A ND1   1 
ATOM   1626 C CD2   . HIS A 1 217 ? -2.293  -2.095  30.153 1.00 38.19 ? 217 HIS A CD2   1 
ATOM   1627 C CE1   . HIS A 1 217 ? -0.497  -2.026  28.896 1.00 28.72 ? 217 HIS A CE1   1 
ATOM   1628 N NE2   . HIS A 1 217 ? -1.196  -2.794  29.712 1.00 32.70 ? 217 HIS A NE2   1 
ATOM   1629 N N     . ARG A 1 218 ? -0.854  1.970   30.885 1.00 33.85 ? 218 ARG A N     1 
ATOM   1630 C CA    . ARG A 1 218 ? 0.530   2.177   31.295 1.00 20.93 ? 218 ARG A CA    1 
ATOM   1631 C C     . ARG A 1 218 ? 0.630   2.616   32.754 1.00 23.32 ? 218 ARG A C     1 
ATOM   1632 O O     . ARG A 1 218 ? 1.387   2.033   33.539 1.00 26.92 ? 218 ARG A O     1 
ATOM   1633 C CB    . ARG A 1 218 ? 1.159   3.212   30.363 1.00 22.78 ? 218 ARG A CB    1 
ATOM   1634 C CG    . ARG A 1 218 ? 1.240   2.752   28.907 1.00 26.85 ? 218 ARG A CG    1 
ATOM   1635 C CD    . ARG A 1 218 ? 2.057   1.478   28.734 1.00 21.55 ? 218 ARG A CD    1 
ATOM   1636 N NE    . ARG A 1 218 ? 2.374   1.232   27.331 1.00 19.77 ? 218 ARG A NE    1 
ATOM   1637 C CZ    . ARG A 1 218 ? 3.223   0.309   26.900 1.00 21.88 ? 218 ARG A CZ    1 
ATOM   1638 N NH1   . ARG A 1 218 ? 3.931   -0.427  27.742 1.00 23.50 ? 218 ARG A NH1   1 
ATOM   1639 N NH2   . ARG A 1 218 ? 3.378   0.131   25.591 1.00 18.85 ? 218 ARG A NH2   1 
ATOM   1640 N N     . GLU A 1 219 ? -0.131  3.645   33.139 1.00 27.30 ? 219 GLU A N     1 
ATOM   1641 C CA    . GLU A 1 219 ? -0.041  4.175   34.498 1.00 22.33 ? 219 GLU A CA    1 
ATOM   1642 C C     . GLU A 1 219 ? -0.552  3.198   35.545 1.00 20.60 ? 219 GLU A C     1 
ATOM   1643 O O     . GLU A 1 219 ? -0.240  3.360   36.730 1.00 21.76 ? 219 GLU A O     1 
ATOM   1644 C CB    . GLU A 1 219 ? -0.840  5.472   34.626 1.00 25.93 ? 219 GLU A CB    1 
ATOM   1645 C CG    . GLU A 1 219 ? -0.423  6.577   33.684 1.00 28.48 ? 219 GLU A CG    1 
ATOM   1646 C CD    . GLU A 1 219 ? -1.395  7.739   33.704 1.00 40.77 ? 219 GLU A CD    1 
ATOM   1647 O OE1   . GLU A 1 219 ? -2.415  7.646   34.420 1.00 48.11 ? 219 GLU A OE1   1 
ATOM   1648 O OE2   . GLU A 1 219 ? -1.143  8.742   33.006 1.00 36.07 ? 219 GLU A OE2   1 
ATOM   1649 N N     . THR A 1 220 ? -1.337  2.203   35.143 1.00 34.87 ? 220 THR A N     1 
ATOM   1650 C CA    . THR A 1 220 ? -2.044  1.347   36.083 1.00 23.53 ? 220 THR A CA    1 
ATOM   1651 C C     . THR A 1 220 ? -1.438  -0.039  36.231 1.00 21.47 ? 220 THR A C     1 
ATOM   1652 O O     . THR A 1 220 ? -1.478  -0.595  37.330 1.00 23.93 ? 220 THR A O     1 
ATOM   1653 C CB    . THR A 1 220 ? -3.510  1.204   35.656 1.00 22.55 ? 220 THR A CB    1 
ATOM   1654 O OG1   . THR A 1 220 ? -3.578  0.898   34.257 1.00 27.33 ? 220 THR A OG1   1 
ATOM   1655 C CG2   . THR A 1 220 ? -4.269  2.498   35.928 1.00 33.18 ? 220 THR A CG2   1 
ATOM   1656 N N     . VAL A 1 221 ? -0.870  -0.607  35.167 1.00 19.65 ? 221 VAL A N     1 
ATOM   1657 C CA    . VAL A 1 221 ? -0.390  -1.982  35.191 1.00 36.30 ? 221 VAL A CA    1 
ATOM   1658 C C     . VAL A 1 221 ? 1.107   -2.100  34.942 1.00 35.10 ? 221 VAL A C     1 
ATOM   1659 O O     . VAL A 1 221 ? 1.639   -3.212  35.012 1.00 34.63 ? 221 VAL A O     1 
ATOM   1660 C CB    . VAL A 1 221 ? -1.163  -2.866  34.188 1.00 27.16 ? 221 VAL A CB    1 
ATOM   1661 C CG1   . VAL A 1 221 ? -2.664  -2.608  34.272 1.00 38.05 ? 221 VAL A CG1   1 
ATOM   1662 C CG2   . VAL A 1 221 ? -0.669  -2.659  32.771 1.00 27.37 ? 221 VAL A CG2   1 
ATOM   1663 N N     . GLN A 1 222 ? 1.807   -1.007  34.649 1.00 31.58 ? 222 GLN A N     1 
ATOM   1664 C CA    . GLN A 1 222 ? 3.229   -1.097  34.342 1.00 24.15 ? 222 GLN A CA    1 
ATOM   1665 C C     . GLN A 1 222 ? 4.011   -0.012  35.068 1.00 33.37 ? 222 GLN A C     1 
ATOM   1666 O O     . GLN A 1 222 ? 3.493   1.087   35.300 1.00 37.75 ? 222 GLN A O     1 
ATOM   1667 C CB    . GLN A 1 222 ? 3.490   -0.994  32.830 1.00 20.98 ? 222 GLN A CB    1 
ATOM   1668 C CG    . GLN A 1 222 ? 3.149   -2.264  32.073 1.00 18.58 ? 222 GLN A CG    1 
ATOM   1669 C CD    . GLN A 1 222 ? 3.302   -2.114  30.577 1.00 16.95 ? 222 GLN A CD    1 
ATOM   1670 O OE1   . GLN A 1 222 ? 3.728   -1.069  30.088 1.00 17.44 ? 222 GLN A OE1   1 
ATOM   1671 N NE2   . GLN A 1 222 ? 2.947   -3.159  29.838 1.00 26.93 ? 222 GLN A NE2   1 
ATOM   1672 N N     . PRO A 1 223 ? 5.275   -0.294  35.433 1.00 46.26 ? 223 PRO A N     1 
ATOM   1673 C CA    . PRO A 1 223 ? 6.097   0.651   36.212 1.00 38.78 ? 223 PRO A CA    1 
ATOM   1674 C C     . PRO A 1 223 ? 6.862   1.631   35.324 1.00 29.91 ? 223 PRO A C     1 
ATOM   1675 O O     . PRO A 1 223 ? 8.091   1.741   35.386 1.00 36.12 ? 223 PRO A O     1 
ATOM   1676 C CB    . PRO A 1 223 ? 7.037   -0.297  36.964 1.00 33.94 ? 223 PRO A CB    1 
ATOM   1677 C CG    . PRO A 1 223 ? 7.293   -1.385  35.954 1.00 33.34 ? 223 PRO A CG    1 
ATOM   1678 C CD    . PRO A 1 223 ? 6.002   -1.551  35.176 1.00 37.82 ? 223 PRO A CD    1 
ATOM   1679 N N     . VAL A 1 224 ? 6.127   2.367   34.492 1.00 35.50 ? 224 VAL A N     1 
ATOM   1680 C CA    . VAL A 1 224 ? 6.738   3.104   33.390 1.00 42.05 ? 224 VAL A CA    1 
ATOM   1681 C C     . VAL A 1 224 ? 7.298   4.453   33.831 1.00 28.72 ? 224 VAL A C     1 
ATOM   1682 O O     . VAL A 1 224 ? 7.757   5.240   32.995 1.00 30.59 ? 224 VAL A O     1 
ATOM   1683 C CB    . VAL A 1 224 ? 5.727   3.275   32.240 1.00 37.73 ? 224 VAL A CB    1 
ATOM   1684 C CG1   . VAL A 1 224 ? 5.153   1.921   31.854 1.00 31.59 ? 224 VAL A CG1   1 
ATOM   1685 C CG2   . VAL A 1 224 ? 4.612   4.235   32.629 1.00 30.88 ? 224 VAL A CG2   1 
ATOM   1686 N N     . ARG A 1 225 ? 7.281   4.731   35.134 1.00 29.29 ? 225 ARG A N     1 
ATOM   1687 C CA    . ARG A 1 225 ? 7.982   5.889   35.680 1.00 41.08 ? 225 ARG A CA    1 
ATOM   1688 C C     . ARG A 1 225 ? 9.338   5.529   36.272 1.00 39.78 ? 225 ARG A C     1 
ATOM   1689 O O     . ARG A 1 225 ? 10.028  6.414   36.787 1.00 31.11 ? 225 ARG A O     1 
ATOM   1690 C CB    . ARG A 1 225 ? 7.127   6.584   36.748 1.00 41.17 ? 225 ARG A CB    1 
ATOM   1691 C CG    . ARG A 1 225 ? 6.373   7.800   36.229 1.00 49.51 ? 225 ARG A CG    1 
ATOM   1692 C CD    . ARG A 1 225 ? 4.940   7.869   36.741 1.00 56.02 ? 225 ARG A CD    1 
ATOM   1693 N NE    . ARG A 1 225 ? 4.819   7.679   38.183 1.00 54.34 ? 225 ARG A NE    1 
ATOM   1694 C CZ    . ARG A 1 225 ? 5.224   8.551   39.097 1.00 64.44 ? 225 ARG A CZ    1 
ATOM   1695 N NH1   . ARG A 1 225 ? 5.869   9.657   38.763 1.00 64.25 ? 225 ARG A NH1   1 
ATOM   1696 N NH2   . ARG A 1 225 ? 4.974   8.307   40.381 1.00 67.62 ? 225 ARG A NH2   1 
ATOM   1697 N N     . GLU A 1 226 ? 9.738   4.265   36.200 1.00 41.24 ? 226 GLU A N     1 
ATOM   1698 C CA    . GLU A 1 226 ? 10.958  3.781   36.827 1.00 31.38 ? 226 GLU A CA    1 
ATOM   1699 C C     . GLU A 1 226 ? 12.064  3.617   35.790 1.00 27.26 ? 226 GLU A C     1 
ATOM   1700 O O     . GLU A 1 226 ? 11.836  3.685   34.580 1.00 23.38 ? 226 GLU A O     1 
ATOM   1701 C CB    . GLU A 1 226 ? 10.692  2.449   37.535 1.00 31.60 ? 226 GLU A CB    1 
ATOM   1702 C CG    . GLU A 1 226 ? 9.611   2.518   38.603 1.00 26.80 ? 226 GLU A CG    1 
ATOM   1703 C CD    . GLU A 1 226 ? 10.144  2.953   39.955 1.00 30.61 ? 226 GLU A CD    1 
ATOM   1704 O OE1   . GLU A 1 226 ? 11.379  2.964   40.141 1.00 39.01 ? 226 GLU A OE1   1 
ATOM   1705 O OE2   . GLU A 1 226 ? 9.323   3.288   40.835 1.00 43.29 ? 226 GLU A OE2   1 
ATOM   1706 N N     . LYS A 1 227 ? 13.282  3.400   36.284 1.00 34.01 ? 227 LYS A N     1 
ATOM   1707 C CA    . LYS A 1 227 ? 14.406  3.070   35.414 1.00 28.45 ? 227 LYS A CA    1 
ATOM   1708 C C     . LYS A 1 227 ? 14.310  1.592   35.057 1.00 20.04 ? 227 LYS A C     1 
ATOM   1709 O O     . LYS A 1 227 ? 14.598  0.720   35.884 1.00 21.93 ? 227 LYS A O     1 
ATOM   1710 C CB    . LYS A 1 227 ? 15.737  3.400   36.082 1.00 33.98 ? 227 LYS A CB    1 
ATOM   1711 C CG    . LYS A 1 227 ? 15.841  4.833   36.581 1.00 35.43 ? 227 LYS A CG    1 
ATOM   1712 C CD    . LYS A 1 227 ? 17.202  5.098   37.211 1.00 30.25 ? 227 LYS A CD    1 
ATOM   1713 C CE    . LYS A 1 227 ? 17.104  5.814   38.547 1.00 27.99 ? 227 LYS A CE    1 
ATOM   1714 N NZ    . LYS A 1 227 ? 16.131  5.178   39.475 1.00 36.37 ? 227 LYS A NZ    1 
ATOM   1715 N N     . THR A 1 228 ? 13.896  1.317   33.825 1.00 23.34 ? 228 THR A N     1 
ATOM   1716 C CA    . THR A 1 228 ? 13.640  -0.040  33.375 1.00 16.32 ? 228 THR A CA    1 
ATOM   1717 C C     . THR A 1 228 ? 13.729  -0.060  31.862 1.00 17.81 ? 228 THR A C     1 
ATOM   1718 O O     . THR A 1 228 ? 13.613  0.975   31.203 1.00 21.47 ? 228 THR A O     1 
ATOM   1719 C CB    . THR A 1 228 ? 12.264  -0.536  33.829 1.00 28.94 ? 228 THR A CB    1 
ATOM   1720 O OG1   . THR A 1 228 ? 12.017  -1.844  33.296 1.00 31.81 ? 228 THR A OG1   1 
ATOM   1721 C CG2   . THR A 1 228 ? 11.158  0.417   33.381 1.00 29.88 ? 228 THR A CG2   1 
ATOM   1722 N N     . GLY A 1 229 ? 13.929  -1.254  31.320 1.00 17.21 ? 229 GLY A N     1 
ATOM   1723 C CA    . GLY A 1 229 ? 13.890  -1.462  29.892 1.00 22.77 ? 229 GLY A CA    1 
ATOM   1724 C C     . GLY A 1 229 ? 12.591  -2.055  29.403 1.00 22.38 ? 229 GLY A C     1 
ATOM   1725 O O     . GLY A 1 229 ? 12.493  -2.414  28.224 1.00 23.52 ? 229 GLY A O     1 
ATOM   1726 N N     . GLY A 1 230 ? 11.598  -2.182  30.269 1.00 29.84 ? 230 GLY A N     1 
ATOM   1727 C CA    . GLY A 1 230 ? 10.274  -2.612  29.860 1.00 36.29 ? 230 GLY A CA    1 
ATOM   1728 C C     . GLY A 1 230 ? 10.049  -4.088  30.153 1.00 32.14 ? 230 GLY A C     1 
ATOM   1729 O O     . GLY A 1 230 ? 10.270  -4.546  31.274 1.00 40.62 ? 230 GLY A O     1 
ATOM   1730 N N     . SER A 1 231 ? 9.610   -4.828  29.140 1.00 30.15 ? 231 SER A N     1 
ATOM   1731 C CA    . SER A 1 231 ? 9.291   -6.242  29.297 1.00 35.42 ? 231 SER A CA    1 
ATOM   1732 C C     . SER A 1 231 ? 10.565  -7.050  29.089 1.00 21.01 ? 231 SER A C     1 
ATOM   1733 O O     . SER A 1 231 ? 11.104  -7.110  27.979 1.00 23.12 ? 231 SER A O     1 
ATOM   1734 C CB    . SER A 1 231 ? 8.195   -6.663  28.325 1.00 39.59 ? 231 SER A CB    1 
ATOM   1735 O OG    . SER A 1 231 ? 6.929   -6.214  28.777 1.00 42.77 ? 231 SER A OG    1 
ATOM   1736 N N     . THR A 1 232 ? 11.037  -7.675  30.166 1.00 27.04 ? 232 THR A N     1 
ATOM   1737 C CA    . THR A 1 232 ? 12.316  -8.373  30.135 1.00 26.59 ? 232 THR A CA    1 
ATOM   1738 C C     . THR A 1 232 ? 12.286  -9.541  29.156 1.00 22.98 ? 232 THR A C     1 
ATOM   1739 O O     . THR A 1 232 ? 13.176  -9.677  28.308 1.00 24.32 ? 232 THR A O     1 
ATOM   1740 C CB    . THR A 1 232 ? 12.662  -8.854  31.545 1.00 27.60 ? 232 THR A CB    1 
ATOM   1741 O OG1   . THR A 1 232 ? 12.403  -7.803  32.486 1.00 29.09 ? 232 THR A OG1   1 
ATOM   1742 C CG2   . THR A 1 232 ? 14.119  -9.261  31.643 1.00 29.31 ? 232 THR A CG2   1 
ATOM   1743 N N     . PHE A 1 233 ? 11.266  -10.391 29.253 1.00 34.16 ? 233 PHE A N     1 
ATOM   1744 C CA    . PHE A 1 233 ? 11.215  -11.631 28.495 1.00 29.97 ? 233 PHE A CA    1 
ATOM   1745 C C     . PHE A 1 233 ? 9.922   -11.726 27.700 1.00 37.95 ? 233 PHE A C     1 
ATOM   1746 O O     . PHE A 1 233 ? 8.880   -11.198 28.100 1.00 36.44 ? 233 PHE A O     1 
ATOM   1747 C CB    . PHE A 1 233 ? 11.341  -12.844 29.421 1.00 25.78 ? 233 PHE A CB    1 
ATOM   1748 C CG    . PHE A 1 233 ? 12.581  -12.830 30.260 1.00 26.42 ? 233 PHE A CG    1 
ATOM   1749 C CD1   . PHE A 1 233 ? 13.818  -13.054 29.684 1.00 22.94 ? 233 PHE A CD1   1 
ATOM   1750 C CD2   . PHE A 1 233 ? 12.514  -12.581 31.620 1.00 22.13 ? 233 PHE A CD2   1 
ATOM   1751 C CE1   . PHE A 1 233 ? 14.966  -13.037 30.447 1.00 20.65 ? 233 PHE A CE1   1 
ATOM   1752 C CE2   . PHE A 1 233 ? 13.660  -12.563 32.391 1.00 23.47 ? 233 PHE A CE2   1 
ATOM   1753 C CZ    . PHE A 1 233 ? 14.888  -12.792 31.803 1.00 22.17 ? 233 PHE A CZ    1 
ATOM   1754 N N     . LYS A 1 234 ? 10.011  -12.412 26.564 1.00 37.60 ? 234 LYS A N     1 
ATOM   1755 C CA    . LYS A 1 234 ? 8.842   -12.695 25.748 1.00 36.55 ? 234 LYS A CA    1 
ATOM   1756 C C     . LYS A 1 234 ? 7.887   -13.616 26.498 1.00 35.45 ? 234 LYS A C     1 
ATOM   1757 O O     . LYS A 1 234 ? 8.300   -14.458 27.300 1.00 35.07 ? 234 LYS A O     1 
ATOM   1758 C CB    . LYS A 1 234 ? 9.275   -13.333 24.424 1.00 38.15 ? 234 LYS A CB    1 
ATOM   1759 C CG    . LYS A 1 234 ? 8.222   -14.194 23.732 1.00 46.74 ? 234 LYS A CG    1 
ATOM   1760 C CD    . LYS A 1 234 ? 8.777   -14.832 22.465 1.00 41.10 ? 234 LYS A CD    1 
ATOM   1761 C CE    . LYS A 1 234 ? 7.672   -15.455 21.625 1.00 39.91 ? 234 LYS A CE    1 
ATOM   1762 N NZ    . LYS A 1 234 ? 7.905   -15.298 20.162 1.00 45.66 ? 234 LYS A NZ    1 
ATOM   1763 N N     . ASN A 1 235 ? 6.599   -13.446 26.234 1.00 43.25 ? 235 ASN A N     1 
ATOM   1764 C CA    . ASN A 1 235 ? 5.593   -14.325 26.818 1.00 30.78 ? 235 ASN A CA    1 
ATOM   1765 C C     . ASN A 1 235 ? 5.694   -15.704 26.178 1.00 26.89 ? 235 ASN A C     1 
ATOM   1766 O O     . ASN A 1 235 ? 5.595   -15.810 24.948 1.00 25.91 ? 235 ASN A O     1 
ATOM   1767 C CB    . ASN A 1 235 ? 4.195   -13.750 26.610 1.00 32.02 ? 235 ASN A CB    1 
ATOM   1768 C CG    . ASN A 1 235 ? 3.960   -12.482 27.405 1.00 25.57 ? 235 ASN A CG    1 
ATOM   1769 O OD1   . ASN A 1 235 ? 4.234   -12.427 28.604 1.00 34.60 ? 235 ASN A OD1   1 
ATOM   1770 N ND2   . ASN A 1 235 ? 3.445   -11.455 26.740 1.00 28.53 ? 235 ASN A ND2   1 
ATOM   1771 N N     . PRO A 1 236 ? 5.895   -16.775 26.945 1.00 29.81 ? 236 PRO A N     1 
ATOM   1772 C CA    . PRO A 1 236 ? 5.911   -18.109 26.331 1.00 36.72 ? 236 PRO A CA    1 
ATOM   1773 C C     . PRO A 1 236 ? 4.528   -18.485 25.823 1.00 47.46 ? 236 PRO A C     1 
ATOM   1774 O O     . PRO A 1 236 ? 3.511   -18.155 26.438 1.00 48.75 ? 236 PRO A O     1 
ATOM   1775 C CB    . PRO A 1 236 ? 6.370   -19.039 27.463 1.00 32.06 ? 236 PRO A CB    1 
ATOM   1776 C CG    . PRO A 1 236 ? 6.484   -18.214 28.693 1.00 28.60 ? 236 PRO A CG    1 
ATOM   1777 C CD    . PRO A 1 236 ? 6.062   -16.814 28.408 1.00 28.60 ? 236 PRO A CD    1 
ATOM   1778 N N     . GLU A 1 237 ? 4.500   -19.172 24.681 1.00 47.93 ? 237 GLU A N     1 
ATOM   1779 C CA    . GLU A 1 237 ? 3.235   -19.572 24.080 1.00 41.08 ? 237 GLU A CA    1 
ATOM   1780 C C     . GLU A 1 237 ? 2.340   -20.240 25.116 1.00 41.89 ? 237 GLU A C     1 
ATOM   1781 O O     . GLU A 1 237 ? 2.792   -21.069 25.911 1.00 40.24 ? 237 GLU A O     1 
ATOM   1782 C CB    . GLU A 1 237 ? 3.478   -20.525 22.906 1.00 39.16 ? 237 GLU A CB    1 
ATOM   1783 C CG    . GLU A 1 237 ? 2.474   -20.377 21.765 1.00 46.50 ? 237 GLU A CG    1 
ATOM   1784 C CD    . GLU A 1 237 ? 3.096   -20.569 20.390 1.00 50.44 ? 237 GLU A CD    1 
ATOM   1785 O OE1   . GLU A 1 237 ? 4.271   -20.986 20.310 1.00 44.20 ? 237 GLU A OE1   1 
ATOM   1786 O OE2   . GLU A 1 237 ? 2.405   -20.302 19.384 1.00 46.37 ? 237 GLU A OE2   1 
ATOM   1787 N N     . GLY A 1 238 ? 1.064   -19.861 25.110 1.00 39.39 ? 238 GLY A N     1 
ATOM   1788 C CA    . GLY A 1 238 ? 0.100   -20.453 26.015 1.00 24.45 ? 238 GLY A CA    1 
ATOM   1789 C C     . GLY A 1 238 ? 0.204   -20.003 27.453 1.00 31.52 ? 238 GLY A C     1 
ATOM   1790 O O     . GLY A 1 238 ? -0.459  -20.585 28.317 1.00 31.11 ? 238 GLY A O     1 
ATOM   1791 N N     . THR A 1 239 ? 1.017   -18.993 27.741 1.00 37.65 ? 239 THR A N     1 
ATOM   1792 C CA    . THR A 1 239 ? 1.116   -18.422 29.079 1.00 29.19 ? 239 THR A CA    1 
ATOM   1793 C C     . THR A 1 239 ? 1.758   -17.045 28.944 1.00 30.07 ? 239 THR A C     1 
ATOM   1794 O O     . THR A 1 239 ? 1.898   -16.517 27.835 1.00 25.81 ? 239 THR A O     1 
ATOM   1795 C CB    . THR A 1 239 ? 1.898   -19.350 30.018 1.00 32.48 ? 239 THR A CB    1 
ATOM   1796 O OG1   . THR A 1 239 ? 1.959   -18.773 31.329 1.00 27.39 ? 239 THR A OG1   1 
ATOM   1797 C CG2   . THR A 1 239 ? 3.309   -19.584 29.500 1.00 35.49 ? 239 THR A CG2   1 
ATOM   1798 N N     . SER A 1 240 ? 2.149   -16.454 30.072 1.00 31.87 ? 240 SER A N     1 
ATOM   1799 C CA    . SER A 1 240 ? 2.756   -15.132 30.067 1.00 33.40 ? 240 SER A CA    1 
ATOM   1800 C C     . SER A 1 240 ? 3.965   -15.112 30.990 1.00 30.65 ? 240 SER A C     1 
ATOM   1801 O O     . SER A 1 240 ? 3.998   -15.794 32.018 1.00 26.06 ? 240 SER A O     1 
ATOM   1802 C CB    . SER A 1 240 ? 1.759   -14.047 30.492 1.00 27.66 ? 240 SER A CB    1 
ATOM   1803 O OG    . SER A 1 240 ? 1.546   -14.064 31.892 1.00 24.90 ? 240 SER A OG    1 
ATOM   1804 N N     . ALA A 1 241 ? 4.959   -14.307 30.605 1.00 31.11 ? 241 ALA A N     1 
ATOM   1805 C CA    . ALA A 1 241 ? 6.206   -14.236 31.358 1.00 22.45 ? 241 ALA A CA    1 
ATOM   1806 C C     . ALA A 1 241 ? 5.965   -13.824 32.804 1.00 25.52 ? 241 ALA A C     1 
ATOM   1807 O O     . ALA A 1 241 ? 6.474   -14.461 33.734 1.00 28.98 ? 241 ALA A O     1 
ATOM   1808 C CB    . ALA A 1 241 ? 7.164   -13.256 30.682 1.00 32.21 ? 241 ALA A CB    1 
ATOM   1809 N N     . TRP A 1 242 ? 5.195   -12.752 33.019 1.00 24.31 ? 242 TRP A N     1 
ATOM   1810 C CA    . TRP A 1 242 ? 5.035   -12.249 34.379 1.00 19.46 ? 242 TRP A CA    1 
ATOM   1811 C C     . TRP A 1 242 ? 4.420   -13.305 35.260 1.00 20.52 ? 242 TRP A C     1 
ATOM   1812 O O     . TRP A 1 242 ? 4.709   -13.382 36.460 1.00 24.90 ? 242 TRP A O     1 
ATOM   1813 C CB    . TRP A 1 242 ? 4.178   -10.981 34.400 1.00 27.04 ? 242 TRP A CB    1 
ATOM   1814 C CG    . TRP A 1 242 ? 2.667   -11.167 34.288 1.00 27.25 ? 242 TRP A CG    1 
ATOM   1815 C CD1   . TRP A 1 242 ? 1.917   -11.060 33.151 1.00 26.17 ? 242 TRP A CD1   1 
ATOM   1816 C CD2   . TRP A 1 242 ? 1.736   -11.441 35.353 1.00 18.28 ? 242 TRP A CD2   1 
ATOM   1817 N NE1   . TRP A 1 242 ? 0.588   -11.261 33.436 1.00 22.29 ? 242 TRP A NE1   1 
ATOM   1818 C CE2   . TRP A 1 242 ? 0.449   -11.496 34.778 1.00 18.19 ? 242 TRP A CE2   1 
ATOM   1819 C CE3   . TRP A 1 242 ? 1.866   -11.650 36.731 1.00 18.99 ? 242 TRP A CE3   1 
ATOM   1820 C CZ2   . TRP A 1 242 ? -0.698  -11.755 35.530 1.00 21.06 ? 242 TRP A CZ2   1 
ATOM   1821 C CZ3   . TRP A 1 242 ? 0.721   -11.904 37.477 1.00 21.50 ? 242 TRP A CZ3   1 
ATOM   1822 C CH2   . TRP A 1 242 ? -0.541  -11.955 36.873 1.00 23.64 ? 242 TRP A CH2   1 
ATOM   1823 N N     . LYS A 1 243 ? 3.594   -14.142 34.671 1.00 30.20 ? 243 LYS A N     1 
ATOM   1824 C CA    . LYS A 1 243 ? 2.955   -15.169 35.449 1.00 30.12 ? 243 LYS A CA    1 
ATOM   1825 C C     . LYS A 1 243 ? 3.912   -16.275 35.831 1.00 17.46 ? 243 LYS A C     1 
ATOM   1826 O O     . LYS A 1 243 ? 4.015   -16.663 37.003 1.00 29.45 ? 243 LYS A O     1 
ATOM   1827 C CB    . LYS A 1 243 ? 1.786   -15.729 34.641 1.00 33.57 ? 243 LYS A CB    1 
ATOM   1828 C CG    . LYS A 1 243 ? 0.787   -16.313 35.446 1.00 38.60 ? 243 LYS A CG    1 
ATOM   1829 C CD    . LYS A 1 243 ? 0.868   -15.548 36.680 1.00 46.67 ? 243 LYS A CD    1 
ATOM   1830 C CE    . LYS A 1 243 ? -0.177  -15.674 37.437 1.00 50.49 ? 243 LYS A CE    1 
ATOM   1831 N NZ    . LYS A 1 243 ? 0.401   -15.434 38.676 1.00 56.99 ? 243 LYS A NZ    1 
ATOM   1832 N N     . GLU A 1 244 ? 4.590   -16.805 34.834 1.00 23.39 ? 244 GLU A N     1 
ATOM   1833 C CA    . GLU A 1 244 ? 5.598   -17.813 35.067 1.00 28.39 ? 244 GLU A CA    1 
ATOM   1834 C C     . GLU A 1 244 ? 6.693   -17.292 35.990 1.00 27.73 ? 244 GLU A C     1 
ATOM   1835 O O     . GLU A 1 244 ? 7.312   -18.073 36.721 1.00 31.41 ? 244 GLU A O     1 
ATOM   1836 C CB    . GLU A 1 244 ? 6.134   -18.240 33.706 1.00 25.21 ? 244 GLU A CB    1 
ATOM   1837 C CG    . GLU A 1 244 ? 5.048   -18.834 32.797 1.00 31.11 ? 244 GLU A CG    1 
ATOM   1838 C CD    . GLU A 1 244 ? 4.466   -20.131 33.329 1.00 33.59 ? 244 GLU A CD    1 
ATOM   1839 O OE1   . GLU A 1 244 ? 4.960   -20.634 34.359 1.00 36.88 ? 244 GLU A OE1   1 
ATOM   1840 O OE2   . GLU A 1 244 ? 3.513   -20.651 32.711 1.00 41.04 ? 244 GLU A OE2   1 
ATOM   1841 N N     . ILE A 1 245 ? 6.922   -15.974 35.996 1.00 26.42 ? 245 ILE A N     1 
ATOM   1842 C CA    . ILE A 1 245 ? 7.897   -15.386 36.913 1.00 22.91 ? 245 ILE A CA    1 
ATOM   1843 C C     . ILE A 1 245 ? 7.337   -15.349 38.329 1.00 28.52 ? 245 ILE A C     1 
ATOM   1844 O O     . ILE A 1 245 ? 8.000   -15.762 39.288 1.00 28.25 ? 245 ILE A O     1 
ATOM   1845 C CB    . ILE A 1 245 ? 8.305   -13.981 36.433 1.00 24.41 ? 245 ILE A CB    1 
ATOM   1846 C CG1   . ILE A 1 245 ? 9.158   -14.074 35.169 1.00 19.52 ? 245 ILE A CG1   1 
ATOM   1847 C CG2   . ILE A 1 245 ? 9.081   -13.239 37.514 1.00 22.59 ? 245 ILE A CG2   1 
ATOM   1848 C CD1   . ILE A 1 245 ? 9.168   -12.805 34.352 1.00 23.72 ? 245 ILE A CD1   1 
ATOM   1849 N N     . ASP A 1 246 ? 6.116   -14.834 38.486 1.00 31.08 ? 246 ASP A N     1 
ATOM   1850 C CA    . ASP A 1 246 ? 5.485   -14.825 39.802 1.00 30.56 ? 246 ASP A CA    1 
ATOM   1851 C C     . ASP A 1 246 ? 5.352   -16.240 40.351 1.00 24.13 ? 246 ASP A C     1 
ATOM   1852 O O     . ASP A 1 246 ? 5.484   -16.462 41.560 1.00 22.44 ? 246 ASP A O     1 
ATOM   1853 C CB    . ASP A 1 246 ? 4.117   -14.146 39.717 1.00 36.16 ? 246 ASP A CB    1 
ATOM   1854 C CG    . ASP A 1 246 ? 3.535   -13.828 41.082 1.00 34.18 ? 246 ASP A CG    1 
ATOM   1855 O OD1   . ASP A 1 246 ? 4.175   -14.165 42.100 1.00 47.88 ? 246 ASP A OD1   1 
ATOM   1856 O OD2   . ASP A 1 246 ? 2.435   -13.236 41.135 1.00 33.67 ? 246 ASP A OD2   1 
ATOM   1857 N N     . LYS A 1 247 ? 5.098   -17.212 39.473 1.00 22.52 ? 247 LYS A N     1 
ATOM   1858 C CA    . LYS A 1 247 ? 4.998   -18.601 39.907 1.00 33.24 ? 247 LYS A CA    1 
ATOM   1859 C C     . LYS A 1 247 ? 6.318   -19.090 40.487 1.00 32.43 ? 247 LYS A C     1 
ATOM   1860 O O     . LYS A 1 247 ? 6.348   -19.737 41.540 1.00 25.62 ? 247 LYS A O     1 
ATOM   1861 C CB    . LYS A 1 247 ? 4.586   -19.487 38.735 1.00 33.14 ? 247 LYS A CB    1 
ATOM   1862 C CG    . LYS A 1 247 ? 3.100   -19.564 38.475 1.00 27.58 ? 247 LYS A CG    1 
ATOM   1863 C CD    . LYS A 1 247 ? 2.874   -20.235 37.137 1.00 30.69 ? 247 LYS A CD    1 
ATOM   1864 C CE    . LYS A 1 247 ? 1.421   -20.256 36.728 1.00 34.54 ? 247 LYS A CE    1 
ATOM   1865 N NZ    . LYS A 1 247 ? 1.311   -20.687 35.309 1.00 36.35 ? 247 LYS A NZ    1 
ATOM   1866 N N     . ALA A 1 248 ? 7.425   -18.792 39.806 1.00 33.26 ? 248 ALA A N     1 
ATOM   1867 C CA    . ALA A 1 248 ? 8.745   -19.191 40.276 1.00 27.83 ? 248 ALA A CA    1 
ATOM   1868 C C     . ALA A 1 248 ? 9.101   -18.496 41.587 1.00 36.27 ? 248 ALA A C     1 
ATOM   1869 O O     . ALA A 1 248 ? 10.161  -18.762 42.162 1.00 36.97 ? 248 ALA A O     1 
ATOM   1870 C CB    . ALA A 1 248 ? 9.801   -18.886 39.210 1.00 34.75 ? 248 ALA A CB    1 
ATOM   1871 N N     . GLY A 1 249 ? 8.231   -17.606 42.062 1.00 34.19 ? 249 GLY A N     1 
ATOM   1872 C CA    . GLY A 1 249 ? 8.457   -16.918 43.316 1.00 26.43 ? 249 GLY A CA    1 
ATOM   1873 C C     . GLY A 1 249 ? 9.331   -15.694 43.208 1.00 24.92 ? 249 GLY A C     1 
ATOM   1874 O O     . GLY A 1 249 ? 9.923   -15.283 44.211 1.00 27.16 ? 249 GLY A O     1 
ATOM   1875 N N     . CYS A 1 250 ? 9.416   -15.085 42.027 1.00 30.79 ? 250 CYS A N     1 
ATOM   1876 C CA    . CYS A 1 250 ? 10.432  -14.084 41.734 1.00 36.61 ? 250 CYS A CA    1 
ATOM   1877 C C     . CYS A 1 250 ? 9.938   -12.646 41.845 1.00 42.99 ? 250 CYS A C     1 
ATOM   1878 O O     . CYS A 1 250 ? 10.747  -11.725 41.691 1.00 31.79 ? 250 CYS A O     1 
ATOM   1879 C CB    . CYS A 1 250 ? 10.991  -14.318 40.327 1.00 32.82 ? 250 CYS A CB    1 
ATOM   1880 S SG    . CYS A 1 250 ? 12.202  -15.657 40.222 1.00 31.93 ? 250 CYS A SG    1 
ATOM   1881 N N     . ARG A 1 251 ? 8.649   -12.422 42.097 1.00 43.92 ? 251 ARG A N     1 
ATOM   1882 C CA    . ARG A 1 251 ? 8.164   -11.061 42.298 1.00 33.94 ? 251 ARG A CA    1 
ATOM   1883 C C     . ARG A 1 251 ? 8.904   -10.425 43.469 1.00 30.87 ? 251 ARG A C     1 
ATOM   1884 O O     . ARG A 1 251 ? 8.864   -10.937 44.592 1.00 33.26 ? 251 ARG A O     1 
ATOM   1885 C CB    . ARG A 1 251 ? 6.654   -11.057 42.548 1.00 37.24 ? 251 ARG A CB    1 
ATOM   1886 C CG    . ARG A 1 251 ? 6.044   -9.656  42.653 1.00 40.09 ? 251 ARG A CG    1 
ATOM   1887 C CD    . ARG A 1 251 ? 4.564   -9.695  43.033 1.00 30.41 ? 251 ARG A CD    1 
ATOM   1888 N NE    . ARG A 1 251 ? 3.770   -10.435 42.059 1.00 18.62 ? 251 ARG A NE    1 
ATOM   1889 C CZ    . ARG A 1 251 ? 3.388   -9.960  40.881 1.00 21.68 ? 251 ARG A CZ    1 
ATOM   1890 N NH1   . ARG A 1 251 ? 3.649   -8.715  40.518 1.00 26.16 ? 251 ARG A NH1   1 
ATOM   1891 N NH2   . ARG A 1 251 ? 2.723   -10.754 40.047 1.00 37.75 ? 251 ARG A NH2   1 
ATOM   1892 N N     . GLY A 1 252 ? 9.588   -9.314  43.202 1.00 33.03 ? 252 GLY A N     1 
ATOM   1893 C CA    . GLY A 1 252 ? 10.374  -8.635  44.210 1.00 39.65 ? 252 GLY A CA    1 
ATOM   1894 C C     . GLY A 1 252 ? 11.806  -9.110  44.337 1.00 36.90 ? 252 GLY A C     1 
ATOM   1895 O O     . GLY A 1 252 ? 12.551  -8.561  45.159 1.00 37.51 ? 252 GLY A O     1 
ATOM   1896 N N     . LEU A 1 253 ? 12.217  -10.102 43.550 1.00 32.77 ? 253 LEU A N     1 
ATOM   1897 C CA    . LEU A 1 253 ? 13.557  -10.661 43.677 1.00 31.58 ? 253 LEU A CA    1 
ATOM   1898 C C     . LEU A 1 253 ? 14.616  -9.599  43.403 1.00 23.63 ? 253 LEU A C     1 
ATOM   1899 O O     . LEU A 1 253 ? 14.506  -8.818  42.454 1.00 29.51 ? 253 LEU A O     1 
ATOM   1900 C CB    . LEU A 1 253 ? 13.722  -11.836 42.713 1.00 32.20 ? 253 LEU A CB    1 
ATOM   1901 C CG    . LEU A 1 253 ? 15.105  -12.484 42.639 1.00 20.29 ? 253 LEU A CG    1 
ATOM   1902 C CD1   . LEU A 1 253 ? 15.452  -13.154 43.958 1.00 21.76 ? 253 LEU A CD1   1 
ATOM   1903 C CD2   . LEU A 1 253 ? 15.152  -13.481 41.496 1.00 15.93 ? 253 LEU A CD2   1 
ATOM   1904 N N     . ARG A 1 254 ? 15.657  -9.587  44.234 1.00 35.87 ? 254 ARG A N     1 
ATOM   1905 C CA    . ARG A 1 254 ? 16.697  -8.568  44.189 1.00 38.71 ? 254 ARG A CA    1 
ATOM   1906 C C     . ARG A 1 254 ? 18.052  -9.177  43.854 1.00 26.45 ? 254 ARG A C     1 
ATOM   1907 O O     . ARG A 1 254 ? 18.382  -10.278 44.306 1.00 23.90 ? 254 ARG A O     1 
ATOM   1908 C CB    . ARG A 1 254 ? 16.813  -7.839  45.531 1.00 35.83 ? 254 ARG A CB    1 
ATOM   1909 C CG    . ARG A 1 254 ? 15.680  -6.886  45.847 1.00 32.08 ? 254 ARG A CG    1 
ATOM   1910 C CD    . ARG A 1 254 ? 15.981  -6.126  47.125 1.00 37.99 ? 254 ARG A CD    1 
ATOM   1911 N NE    . ARG A 1 254 ? 14.800  -5.488  47.695 1.00 38.37 ? 254 ARG A NE    1 
ATOM   1912 C CZ    . ARG A 1 254 ? 14.487  -4.207  47.553 1.00 44.19 ? 254 ARG A CZ    1 
ATOM   1913 N NH1   . ARG A 1 254 ? 15.224  -3.389  46.818 1.00 39.19 ? 254 ARG A NH1   1 
ATOM   1914 N NH2   . ARG A 1 254 ? 13.404  -3.733  48.162 1.00 55.97 ? 254 ARG A NH2   1 
ATOM   1915 N N     . VAL A 1 255 ? 18.834  -8.445  43.060 1.00 36.04 ? 255 VAL A N     1 
ATOM   1916 C CA    . VAL A 1 255 ? 20.267  -8.683  42.927 1.00 32.81 ? 255 VAL A CA    1 
ATOM   1917 C C     . VAL A 1 255 ? 20.967  -7.332  42.977 1.00 20.13 ? 255 VAL A C     1 
ATOM   1918 O O     . VAL A 1 255 ? 21.009  -6.606  41.977 1.00 20.92 ? 255 VAL A O     1 
ATOM   1919 C CB    . VAL A 1 255 ? 20.622  -9.435  41.632 1.00 32.11 ? 255 VAL A CB    1 
ATOM   1920 C CG1   . VAL A 1 255 ? 22.137  -9.528  41.481 1.00 28.59 ? 255 VAL A CG1   1 
ATOM   1921 C CG2   . VAL A 1 255 ? 20.000  -10.821 41.625 1.00 30.16 ? 255 VAL A CG2   1 
ATOM   1922 N N     . GLY A 1 256 ? 21.516  -6.984  44.134 1.00 17.15 ? 256 GLY A N     1 
ATOM   1923 C CA    . GLY A 1 256 ? 22.167  -5.691  44.266 1.00 30.70 ? 256 GLY A CA    1 
ATOM   1924 C C     . GLY A 1 256 ? 21.138  -4.580  44.226 1.00 29.11 ? 256 GLY A C     1 
ATOM   1925 O O     . GLY A 1 256 ? 20.161  -4.582  44.983 1.00 35.06 ? 256 GLY A O     1 
ATOM   1926 N N     . GLY A 1 257 ? 21.351  -3.615  43.336 1.00 31.87 ? 257 GLY A N     1 
ATOM   1927 C CA    . GLY A 1 257 ? 20.408  -2.535  43.149 1.00 42.50 ? 257 GLY A CA    1 
ATOM   1928 C C     . GLY A 1 257 ? 19.264  -2.844  42.215 1.00 40.49 ? 257 GLY A C     1 
ATOM   1929 O O     . GLY A 1 257 ? 18.408  -1.984  41.989 1.00 31.25 ? 257 GLY A O     1 
ATOM   1930 N N     . ALA A 1 258 ? 19.223  -4.053  41.663 1.00 37.69 ? 258 ALA A N     1 
ATOM   1931 C CA    . ALA A 1 258 ? 18.212  -4.449  40.696 1.00 30.53 ? 258 ALA A CA    1 
ATOM   1932 C C     . ALA A 1 258 ? 17.115  -5.246  41.385 1.00 35.60 ? 258 ALA A C     1 
ATOM   1933 O O     . ALA A 1 258 ? 17.391  -6.071  42.261 1.00 32.62 ? 258 ALA A O     1 
ATOM   1934 C CB    . ALA A 1 258 ? 18.834  -5.283  39.574 1.00 32.96 ? 258 ALA A CB    1 
ATOM   1935 N N     . GLN A 1 259 ? 15.869  -4.997  40.987 1.00 34.48 ? 259 GLN A N     1 
ATOM   1936 C CA    . GLN A 1 259 ? 14.736  -5.730  41.529 1.00 29.22 ? 259 GLN A CA    1 
ATOM   1937 C C     . GLN A 1 259 ? 13.741  -6.049  40.425 1.00 27.67 ? 259 GLN A C     1 
ATOM   1938 O O     . GLN A 1 259 ? 13.582  -5.290  39.464 1.00 28.17 ? 259 GLN A O     1 
ATOM   1939 C CB    . GLN A 1 259 ? 14.019  -4.951  42.638 1.00 31.66 ? 259 GLN A CB    1 
ATOM   1940 C CG    . GLN A 1 259 ? 13.156  -5.836  43.523 1.00 28.48 ? 259 GLN A CG    1 
ATOM   1941 C CD    . GLN A 1 259 ? 12.373  -5.052  44.552 1.00 37.87 ? 259 GLN A CD    1 
ATOM   1942 O OE1   . GLN A 1 259 ? 12.345  -3.822  44.525 1.00 43.13 ? 259 GLN A OE1   1 
ATOM   1943 N NE2   . GLN A 1 259 ? 11.731  -5.763  45.473 1.00 38.89 ? 259 GLN A NE2   1 
ATOM   1944 N N     . MET A 1 260 ? 13.079  -7.192  40.576 1.00 38.01 ? 260 MET A N     1 
ATOM   1945 C CA    . MET A 1 260 ? 11.937  -7.543  39.742 1.00 33.64 ? 260 MET A CA    1 
ATOM   1946 C C     . MET A 1 260 ? 10.715  -6.806  40.276 1.00 22.72 ? 260 MET A C     1 
ATOM   1947 O O     . MET A 1 260 ? 10.341  -6.981  41.441 1.00 23.28 ? 260 MET A O     1 
ATOM   1948 C CB    . MET A 1 260 ? 11.721  -9.054  39.757 1.00 26.76 ? 260 MET A CB    1 
ATOM   1949 C CG    . MET A 1 260 ? 11.585  -9.684  38.382 1.00 31.65 ? 260 MET A CG    1 
ATOM   1950 S SD    . MET A 1 260 ? 13.045  -9.438  37.355 1.00 30.29 ? 260 MET A SD    1 
ATOM   1951 C CE    . MET A 1 260 ? 12.315  -9.424  35.719 1.00 19.73 ? 260 MET A CE    1 
ATOM   1952 N N     . SER A 1 261 ? 10.099  -5.978  39.436 1.00 23.00 ? 261 SER A N     1 
ATOM   1953 C CA    . SER A 1 261 ? 9.073   -5.058  39.914 1.00 26.22 ? 261 SER A CA    1 
ATOM   1954 C C     . SER A 1 261 ? 7.908   -5.814  40.536 1.00 20.03 ? 261 SER A C     1 
ATOM   1955 O O     . SER A 1 261 ? 7.298   -6.676  39.894 1.00 22.82 ? 261 SER A O     1 
ATOM   1956 C CB    . SER A 1 261 ? 8.576   -4.178  38.770 1.00 35.87 ? 261 SER A CB    1 
ATOM   1957 O OG    . SER A 1 261 ? 7.452   -3.417  39.177 1.00 32.43 ? 261 SER A OG    1 
ATOM   1958 N N     . GLU A 1 262 ? 7.599   -5.481  41.791 1.00 24.30 ? 262 GLU A N     1 
ATOM   1959 C CA    . GLU A 1 262 ? 6.433   -6.051  42.455 1.00 30.00 ? 262 GLU A CA    1 
ATOM   1960 C C     . GLU A 1 262 ? 5.129   -5.641  41.782 1.00 31.58 ? 262 GLU A C     1 
ATOM   1961 O O     . GLU A 1 262 ? 4.108   -6.309  41.977 1.00 35.66 ? 262 GLU A O     1 
ATOM   1962 C CB    . GLU A 1 262 ? 6.404   -5.624  43.923 1.00 26.84 ? 262 GLU A CB    1 
ATOM   1963 C CG    . GLU A 1 262 ? 7.607   -6.069  44.733 1.00 26.24 ? 262 GLU A CG    1 
ATOM   1964 C CD    . GLU A 1 262 ? 7.520   -5.629  46.182 1.00 31.61 ? 262 GLU A CD    1 
ATOM   1965 O OE1   . GLU A 1 262 ? 6.615   -6.107  46.897 1.00 38.69 ? 262 GLU A OE1   1 
ATOM   1966 O OE2   . GLU A 1 262 ? 8.355   -4.802  46.605 1.00 42.89 ? 262 GLU A OE2   1 
ATOM   1967 N N     . MET A 1 263 ? 5.135   -4.555  41.007 1.00 32.02 ? 263 MET A N     1 
ATOM   1968 C CA    . MET A 1 263 ? 3.921   -4.119  40.326 1.00 29.35 ? 263 MET A CA    1 
ATOM   1969 C C     . MET A 1 263 ? 3.646   -4.980  39.100 1.00 27.44 ? 263 MET A C     1 
ATOM   1970 O O     . MET A 1 263 ? 2.513   -5.421  38.878 1.00 41.57 ? 263 MET A O     1 
ATOM   1971 C CB    . MET A 1 263 ? 4.046   -2.647  39.923 1.00 28.10 ? 263 MET A CB    1 
ATOM   1972 C CG    . MET A 1 263 ? 2.800   -2.068  39.261 1.00 25.15 ? 263 MET A CG    1 
ATOM   1973 S SD    . MET A 1 263 ? 3.164   -0.727  38.113 1.00 33.24 ? 263 MET A SD    1 
ATOM   1974 C CE    . MET A 1 263 ? 3.121   0.688   39.203 1.00 31.23 ? 263 MET A CE    1 
ATOM   1975 N N     . HIS A 1 264 ? 4.677   -5.224  38.297 1.00 19.03 ? 264 HIS A N     1 
ATOM   1976 C CA    . HIS A 1 264 ? 4.553   -6.003  37.068 1.00 20.21 ? 264 HIS A CA    1 
ATOM   1977 C C     . HIS A 1 264 ? 5.879   -6.732  36.901 1.00 28.43 ? 264 HIS A C     1 
ATOM   1978 O O     . HIS A 1 264 ? 6.896   -6.107  36.588 1.00 35.20 ? 264 HIS A O     1 
ATOM   1979 C CB    . HIS A 1 264 ? 4.230   -5.086  35.888 1.00 16.80 ? 264 HIS A CB    1 
ATOM   1980 C CG    . HIS A 1 264 ? 4.086   -5.787  34.571 1.00 18.02 ? 264 HIS A CG    1 
ATOM   1981 N ND1   . HIS A 1 264 ? 4.801   -6.916  34.234 1.00 23.23 ? 264 HIS A ND1   1 
ATOM   1982 C CD2   . HIS A 1 264 ? 3.306   -5.504  33.501 1.00 29.31 ? 264 HIS A CD2   1 
ATOM   1983 C CE1   . HIS A 1 264 ? 4.469   -7.297  33.014 1.00 24.23 ? 264 HIS A CE1   1 
ATOM   1984 N NE2   . HIS A 1 264 ? 3.562   -6.458  32.547 1.00 34.51 ? 264 HIS A NE2   1 
ATOM   1985 N N     . CYS A 1 265 ? 5.871   -8.045  37.129 1.00 31.80 ? 265 CYS A N     1 
ATOM   1986 C CA    . CYS A 1 265 ? 7.092   -8.794  37.396 1.00 22.67 ? 265 CYS A CA    1 
ATOM   1987 C C     . CYS A 1 265 ? 7.783   -9.308  36.136 1.00 17.95 ? 265 CYS A C     1 
ATOM   1988 O O     . CYS A 1 265 ? 8.668   -10.163 36.240 1.00 35.33 ? 265 CYS A O     1 
ATOM   1989 C CB    . CYS A 1 265 ? 6.790   -9.953  38.351 1.00 27.71 ? 265 CYS A CB    1 
ATOM   1990 S SG    . CYS A 1 265 ? 5.492   -11.050 37.805 1.00 39.06 ? 265 CYS A SG    1 
ATOM   1991 N N     . ASN A 1 266 ? 7.410   -8.812  34.957 1.00 18.67 ? 266 ASN A N     1 
ATOM   1992 C CA    . ASN A 1 266 ? 8.255   -8.920  33.775 1.00 19.06 ? 266 ASN A CA    1 
ATOM   1993 C C     . ASN A 1 266 ? 9.075   -7.653  33.549 1.00 24.95 ? 266 ASN A C     1 
ATOM   1994 O O     . ASN A 1 266 ? 9.733   -7.527  32.512 1.00 29.82 ? 266 ASN A O     1 
ATOM   1995 C CB    . ASN A 1 266 ? 7.415   -9.236  32.533 1.00 18.84 ? 266 ASN A CB    1 
ATOM   1996 C CG    . ASN A 1 266 ? 8.250   -9.799  31.390 1.00 20.48 ? 266 ASN A CG    1 
ATOM   1997 O OD1   . ASN A 1 266 ? 9.309   -10.386 31.612 1.00 33.85 ? 266 ASN A OD1   1 
ATOM   1998 N ND2   . ASN A 1 266 ? 7.770   -9.629  30.163 1.00 23.89 ? 266 ASN A ND2   1 
ATOM   1999 N N     . PHE A 1 267 ? 9.045   -6.716  34.497 1.00 30.00 ? 267 PHE A N     1 
ATOM   2000 C CA    . PHE A 1 267 ? 9.849   -5.501  34.447 1.00 32.97 ? 267 PHE A CA    1 
ATOM   2001 C C     . PHE A 1 267 ? 10.962  -5.579  35.484 1.00 24.16 ? 267 PHE A C     1 
ATOM   2002 O O     . PHE A 1 267 ? 10.717  -5.927  36.644 1.00 20.35 ? 267 PHE A O     1 
ATOM   2003 C CB    . PHE A 1 267 ? 9.002   -4.251  34.708 1.00 34.81 ? 267 PHE A CB    1 
ATOM   2004 C CG    . PHE A 1 267 ? 8.169   -3.812  33.535 1.00 41.91 ? 267 PHE A CG    1 
ATOM   2005 C CD1   . PHE A 1 267 ? 7.158   -4.614  33.034 1.00 38.92 ? 267 PHE A CD1   1 
ATOM   2006 C CD2   . PHE A 1 267 ? 8.393   -2.581  32.941 1.00 41.56 ? 267 PHE A CD2   1 
ATOM   2007 C CE1   . PHE A 1 267 ? 6.391   -4.197  31.959 1.00 32.57 ? 267 PHE A CE1   1 
ATOM   2008 C CE2   . PHE A 1 267 ? 7.626   -2.159  31.873 1.00 36.05 ? 267 PHE A CE2   1 
ATOM   2009 C CZ    . PHE A 1 267 ? 6.630   -2.968  31.377 1.00 30.99 ? 267 PHE A CZ    1 
ATOM   2010 N N     . MET A 1 268 ? 12.175  -5.241  35.059 1.00 37.49 ? 268 MET A N     1 
ATOM   2011 C CA    . MET A 1 268 ? 13.348  -5.170  35.921 1.00 26.14 ? 268 MET A CA    1 
ATOM   2012 C C     . MET A 1 268 ? 13.607  -3.710  36.272 1.00 22.59 ? 268 MET A C     1 
ATOM   2013 O O     . MET A 1 268 ? 13.672  -2.862  35.376 1.00 24.41 ? 268 MET A O     1 
ATOM   2014 C CB    . MET A 1 268 ? 14.554  -5.768  35.198 1.00 31.06 ? 268 MET A CB    1 
ATOM   2015 C CG    . MET A 1 268 ? 15.595  -6.420  36.079 1.00 38.55 ? 268 MET A CG    1 
ATOM   2016 S SD    . MET A 1 268 ? 16.323  -7.872  35.287 1.00 24.92 ? 268 MET A SD    1 
ATOM   2017 C CE    . MET A 1 268 ? 16.555  -7.303  33.601 1.00 24.70 ? 268 MET A CE    1 
ATOM   2018 N N     . ILE A 1 269 ? 13.749  -3.412  37.564 1.00 23.07 ? 269 ILE A N     1 
ATOM   2019 C CA    . ILE A 1 269 ? 13.875  -2.035  38.033 1.00 30.12 ? 269 ILE A CA    1 
ATOM   2020 C C     . ILE A 1 269 ? 15.252  -1.824  38.645 1.00 37.69 ? 269 ILE A C     1 
ATOM   2021 O O     . ILE A 1 269 ? 15.700  -2.614  39.485 1.00 32.79 ? 269 ILE A O     1 
ATOM   2022 C CB    . ILE A 1 269 ? 12.777  -1.667  39.052 1.00 25.01 ? 269 ILE A CB    1 
ATOM   2023 C CG1   . ILE A 1 269 ? 11.396  -1.573  38.389 1.00 36.86 ? 269 ILE A CG1   1 
ATOM   2024 C CG2   . ILE A 1 269 ? 13.108  -0.342  39.755 1.00 29.09 ? 269 ILE A CG2   1 
ATOM   2025 C CD1   . ILE A 1 269 ? 11.386  -1.044  36.995 1.00 38.80 ? 269 ILE A CD1   1 
ATOM   2026 N N     . ASN A 1 270 ? 15.905  -0.743  38.226 1.00 28.29 ? 270 ASN A N     1 
ATOM   2027 C CA    . ASN A 1 270 ? 17.079  -0.194  38.897 1.00 21.76 ? 270 ASN A CA    1 
ATOM   2028 C C     . ASN A 1 270 ? 16.581  0.709   40.019 1.00 22.57 ? 270 ASN A C     1 
ATOM   2029 O O     . ASN A 1 270 ? 16.128  1.830   39.775 1.00 29.36 ? 270 ASN A O     1 
ATOM   2030 C CB    . ASN A 1 270 ? 17.941  0.571   37.898 1.00 25.18 ? 270 ASN A CB    1 
ATOM   2031 C CG    . ASN A 1 270 ? 19.038  1.390   38.559 1.00 23.82 ? 270 ASN A CG    1 
ATOM   2032 O OD1   . ASN A 1 270 ? 19.206  1.373   39.778 1.00 30.32 ? 270 ASN A OD1   1 
ATOM   2033 N ND2   . ASN A 1 270 ? 19.788  2.123   37.746 1.00 23.63 ? 270 ASN A ND2   1 
ATOM   2034 N N     . THR A 1 271 ? 16.660  0.227   41.260 1.00 23.96 ? 271 THR A N     1 
ATOM   2035 C CA    . THR A 1 271 ? 16.190  0.984   42.414 1.00 25.37 ? 271 THR A CA    1 
ATOM   2036 C C     . THR A 1 271 ? 17.142  2.105   42.827 1.00 25.79 ? 271 THR A C     1 
ATOM   2037 O O     . THR A 1 271 ? 17.018  2.610   43.949 1.00 31.02 ? 271 THR A O     1 
ATOM   2038 C CB    . THR A 1 271 ? 15.963  0.055   43.612 1.00 27.04 ? 271 THR A CB    1 
ATOM   2039 O OG1   . THR A 1 271 ? 17.180  -0.632  43.931 1.00 42.37 ? 271 THR A OG1   1 
ATOM   2040 C CG2   . THR A 1 271 ? 14.865  -0.956  43.318 1.00 26.60 ? 271 THR A CG2   1 
ATOM   2041 N N     . GLY A 1 272 ? 18.084  2.503   41.973 1.00 22.53 ? 272 GLY A N     1 
ATOM   2042 C CA    . GLY A 1 272 ? 18.984  3.587   42.316 1.00 41.63 ? 272 GLY A CA    1 
ATOM   2043 C C     . GLY A 1 272 ? 20.411  3.394   41.843 1.00 42.33 ? 272 GLY A C     1 
ATOM   2044 O O     . GLY A 1 272 ? 20.894  4.151   40.995 1.00 38.64 ? 272 GLY A O     1 
ATOM   2045 N N     . ASN A 1 273 ? 21.100  2.392   42.385 1.00 30.64 ? 273 ASN A N     1 
ATOM   2046 C CA    . ASN A 1 273 ? 22.513  2.157   42.104 1.00 38.04 ? 273 ASN A CA    1 
ATOM   2047 C C     . ASN A 1 273 ? 22.737  0.718   41.657 1.00 39.25 ? 273 ASN A C     1 
ATOM   2048 O O     . ASN A 1 273 ? 23.626  0.014   42.140 1.00 33.74 ? 273 ASN A O     1 
ATOM   2049 C CB    . ASN A 1 273 ? 23.358  2.493   43.329 1.00 41.01 ? 273 ASN A CB    1 
ATOM   2050 C CG    . ASN A 1 273 ? 23.699  3.967   43.409 1.00 39.01 ? 273 ASN A CG    1 
ATOM   2051 O OD1   . ASN A 1 273 ? 24.415  4.497   42.561 1.00 34.26 ? 273 ASN A OD1   1 
ATOM   2052 N ND2   . ASN A 1 273 ? 23.176  4.639   44.426 1.00 44.97 ? 273 ASN A ND2   1 
ATOM   2053 N N     . ALA A 1 274 ? 21.918  0.262   40.713 1.00 39.95 ? 274 ALA A N     1 
ATOM   2054 C CA    . ALA A 1 274 ? 22.121  -1.040  40.099 1.00 33.62 ? 274 ALA A CA    1 
ATOM   2055 C C     . ALA A 1 274 ? 23.201  -0.954  39.031 1.00 34.44 ? 274 ALA A C     1 
ATOM   2056 O O     . ALA A 1 274 ? 23.249  0.002   38.252 1.00 28.64 ? 274 ALA A O     1 
ATOM   2057 C CB    . ALA A 1 274 ? 20.824  -1.551  39.474 1.00 29.49 ? 274 ALA A CB    1 
ATOM   2058 N N     . THR A 1 275 ? 24.071  -1.958  39.001 1.00 35.85 ? 275 THR A N     1 
ATOM   2059 C CA    . THR A 1 275 ? 25.054  -2.091  37.940 1.00 25.41 ? 275 THR A CA    1 
ATOM   2060 C C     . THR A 1 275 ? 24.460  -2.881  36.778 1.00 24.81 ? 275 THR A C     1 
ATOM   2061 O O     . THR A 1 275 ? 23.397  -3.497  36.887 1.00 36.61 ? 275 THR A O     1 
ATOM   2062 C CB    . THR A 1 275 ? 26.316  -2.788  38.450 1.00 29.28 ? 275 THR A CB    1 
ATOM   2063 O OG1   . THR A 1 275 ? 25.998  -4.127  38.847 1.00 30.40 ? 275 THR A OG1   1 
ATOM   2064 C CG2   . THR A 1 275 ? 26.911  -2.040  39.633 1.00 22.87 ? 275 THR A CG2   1 
ATOM   2065 N N     . GLY A 1 276 ? 25.160  -2.854  35.644 1.00 19.32 ? 276 GLY A N     1 
ATOM   2066 C CA    . GLY A 1 276 ? 24.802  -3.750  34.558 1.00 22.78 ? 276 GLY A CA    1 
ATOM   2067 C C     . GLY A 1 276 ? 24.826  -5.203  34.991 1.00 31.13 ? 276 GLY A C     1 
ATOM   2068 O O     . GLY A 1 276 ? 23.938  -5.984  34.638 1.00 37.42 ? 276 GLY A O     1 
ATOM   2069 N N     . HIS A 1 277 ? 25.840  -5.581  35.774 1.00 29.59 ? 277 HIS A N     1 
ATOM   2070 C CA    . HIS A 1 277 ? 25.931  -6.946  36.284 1.00 27.18 ? 277 HIS A CA    1 
ATOM   2071 C C     . HIS A 1 277 ? 24.728  -7.286  37.156 1.00 25.50 ? 277 HIS A C     1 
ATOM   2072 O O     . HIS A 1 277 ? 24.246  -8.425  37.148 1.00 24.85 ? 277 HIS A O     1 
ATOM   2073 C CB    . HIS A 1 277 ? 27.234  -7.106  37.072 1.00 28.56 ? 277 HIS A CB    1 
ATOM   2074 C CG    . HIS A 1 277 ? 27.649  -8.528  37.294 1.00 24.40 ? 277 HIS A CG    1 
ATOM   2075 N ND1   . HIS A 1 277 ? 27.355  -9.218  38.450 1.00 27.20 ? 277 HIS A ND1   1 
ATOM   2076 C CD2   . HIS A 1 277 ? 28.360  -9.380  36.518 1.00 24.79 ? 277 HIS A CD2   1 
ATOM   2077 C CE1   . HIS A 1 277 ? 27.854  -10.439 38.371 1.00 17.02 ? 277 HIS A CE1   1 
ATOM   2078 N NE2   . HIS A 1 277 ? 28.468  -10.563 37.208 1.00 22.29 ? 277 HIS A NE2   1 
ATOM   2079 N N     . ASP A 1 278 ? 24.231  -6.309  37.918 1.00 29.66 ? 278 ASP A N     1 
ATOM   2080 C CA    . ASP A 1 278 ? 23.064  -6.543  38.762 1.00 28.54 ? 278 ASP A CA    1 
ATOM   2081 C C     . ASP A 1 278 ? 21.853  -6.943  37.931 1.00 27.42 ? 278 ASP A C     1 
ATOM   2082 O O     . ASP A 1 278 ? 21.069  -7.810  38.334 1.00 25.07 ? 278 ASP A O     1 
ATOM   2083 C CB    . ASP A 1 278 ? 22.746  -5.286  39.572 1.00 27.34 ? 278 ASP A CB    1 
ATOM   2084 C CG    . ASP A 1 278 ? 23.533  -5.204  40.863 1.00 28.79 ? 278 ASP A CG    1 
ATOM   2085 O OD1   . ASP A 1 278 ? 24.316  -6.133  41.152 1.00 28.39 ? 278 ASP A OD1   1 
ATOM   2086 O OD2   . ASP A 1 278 ? 23.369  -4.201  41.590 1.00 26.95 ? 278 ASP A OD2   1 
ATOM   2087 N N     . LEU A 1 279 ? 21.684  -6.319  36.766 1.00 25.01 ? 279 LEU A N     1 
ATOM   2088 C CA    . LEU A 1 279 ? 20.476  -6.525  35.978 1.00 23.78 ? 279 LEU A CA    1 
ATOM   2089 C C     . LEU A 1 279 ? 20.547  -7.813  35.169 1.00 29.43 ? 279 LEU A C     1 
ATOM   2090 O O     . LEU A 1 279 ? 19.569  -8.567  35.113 1.00 33.23 ? 279 LEU A O     1 
ATOM   2091 C CB    . LEU A 1 279 ? 20.250  -5.319  35.066 1.00 30.09 ? 279 LEU A CB    1 
ATOM   2092 C CG    . LEU A 1 279 ? 20.005  -4.021  35.841 1.00 29.37 ? 279 LEU A CG    1 
ATOM   2093 C CD1   . LEU A 1 279 ? 20.537  -2.814  35.085 1.00 32.83 ? 279 LEU A CD1   1 
ATOM   2094 C CD2   . LEU A 1 279 ? 18.525  -3.854  36.154 1.00 31.21 ? 279 LEU A CD2   1 
ATOM   2095 N N     . GLU A 1 280 ? 21.692  -8.087  34.540 1.00 34.06 ? 280 GLU A N     1 
ATOM   2096 C CA    . GLU A 1 280 ? 21.835  -9.335  33.799 1.00 27.55 ? 280 GLU A CA    1 
ATOM   2097 C C     . GLU A 1 280 ? 21.866  -10.541 34.730 1.00 23.93 ? 280 GLU A C     1 
ATOM   2098 O O     . GLU A 1 280 ? 21.464  -11.638 34.331 1.00 28.14 ? 280 GLU A O     1 
ATOM   2099 C CB    . GLU A 1 280 ? 23.097  -9.297  32.940 1.00 25.63 ? 280 GLU A CB    1 
ATOM   2100 C CG    . GLU A 1 280 ? 23.233  -10.487 32.006 1.00 28.39 ? 280 GLU A CG    1 
ATOM   2101 C CD    . GLU A 1 280 ? 24.315  -10.290 30.964 1.00 31.38 ? 280 GLU A CD    1 
ATOM   2102 O OE1   . GLU A 1 280 ? 25.005  -9.250  31.013 1.00 36.84 ? 280 GLU A OE1   1 
ATOM   2103 O OE2   . GLU A 1 280 ? 24.475  -11.174 30.097 1.00 24.87 ? 280 GLU A OE2   1 
ATOM   2104 N N     . THR A 1 281 ? 22.338  -10.364 35.966 1.00 26.78 ? 281 THR A N     1 
ATOM   2105 C CA    . THR A 1 281 ? 22.320  -11.472 36.915 1.00 21.87 ? 281 THR A CA    1 
ATOM   2106 C C     . THR A 1 281 ? 20.901  -11.757 37.392 1.00 30.21 ? 281 THR A C     1 
ATOM   2107 O O     . THR A 1 281 ? 20.505  -12.921 37.518 1.00 30.93 ? 281 THR A O     1 
ATOM   2108 C CB    . THR A 1 281 ? 23.234  -11.169 38.102 1.00 20.56 ? 281 THR A CB    1 
ATOM   2109 O OG1   . THR A 1 281 ? 24.598  -11.151 37.666 1.00 24.16 ? 281 THR A OG1   1 
ATOM   2110 C CG2   . THR A 1 281 ? 23.070  -12.227 39.185 1.00 21.09 ? 281 THR A CG2   1 
ATOM   2111 N N     . LEU A 1 282 ? 20.125  -10.706 37.667 1.00 38.00 ? 282 LEU A N     1 
ATOM   2112 C CA    . LEU A 1 282 ? 18.720  -10.893 38.017 1.00 30.51 ? 282 LEU A CA    1 
ATOM   2113 C C     . LEU A 1 282 ? 17.973  -11.594 36.890 1.00 24.49 ? 282 LEU A C     1 
ATOM   2114 O O     . LEU A 1 282 ? 17.263  -12.580 37.118 1.00 28.79 ? 282 LEU A O     1 
ATOM   2115 C CB    . LEU A 1 282 ? 18.079  -9.540  38.332 1.00 36.87 ? 282 LEU A CB    1 
ATOM   2116 C CG    . LEU A 1 282 ? 16.642  -9.545  38.859 1.00 28.02 ? 282 LEU A CG    1 
ATOM   2117 C CD1   . LEU A 1 282 ? 16.551  -10.228 40.211 1.00 31.40 ? 282 LEU A CD1   1 
ATOM   2118 C CD2   . LEU A 1 282 ? 16.127  -8.121  38.958 1.00 32.91 ? 282 LEU A CD2   1 
ATOM   2119 N N     . GLY A 1 283 ? 18.127  -11.097 35.661 1.00 18.32 ? 283 GLY A N     1 
ATOM   2120 C CA    . GLY A 1 283 ? 17.470  -11.731 34.529 1.00 26.23 ? 283 GLY A CA    1 
ATOM   2121 C C     . GLY A 1 283 ? 17.788  -13.207 34.420 1.00 29.78 ? 283 GLY A C     1 
ATOM   2122 O O     . GLY A 1 283 ? 16.889  -14.045 34.324 1.00 30.89 ? 283 GLY A O     1 
ATOM   2123 N N     . GLU A 1 284 ? 19.078  -13.550 34.437 1.00 31.83 ? 284 GLU A N     1 
ATOM   2124 C CA    . GLU A 1 284 ? 19.470  -14.948 34.306 1.00 25.09 ? 284 GLU A CA    1 
ATOM   2125 C C     . GLU A 1 284 ? 19.181  -15.746 35.573 1.00 17.48 ? 284 GLU A C     1 
ATOM   2126 O O     . GLU A 1 284 ? 19.077  -16.975 35.503 1.00 29.05 ? 284 GLU A O     1 
ATOM   2127 C CB    . GLU A 1 284 ? 20.952  -15.046 33.932 1.00 24.04 ? 284 GLU A CB    1 
ATOM   2128 C CG    . GLU A 1 284 ? 21.343  -14.193 32.724 1.00 22.72 ? 284 GLU A CG    1 
ATOM   2129 C CD    . GLU A 1 284 ? 20.890  -14.789 31.403 1.00 23.46 ? 284 GLU A CD    1 
ATOM   2130 O OE1   . GLU A 1 284 ? 20.356  -15.917 31.408 1.00 22.34 ? 284 GLU A OE1   1 
ATOM   2131 O OE2   . GLU A 1 284 ? 21.066  -14.124 30.359 1.00 20.09 ? 284 GLU A OE2   1 
ATOM   2132 N N     . THR A 1 285 ? 19.044  -15.081 36.724 1.00 17.56 ? 285 THR A N     1 
ATOM   2133 C CA    . THR A 1 285 ? 18.544  -15.770 37.910 1.00 22.00 ? 285 THR A CA    1 
ATOM   2134 C C     . THR A 1 285 ? 17.067  -16.113 37.756 1.00 31.58 ? 285 THR A C     1 
ATOM   2135 O O     . THR A 1 285 ? 16.624  -17.186 38.182 1.00 29.97 ? 285 THR A O     1 
ATOM   2136 C CB    . THR A 1 285 ? 18.757  -14.915 39.160 1.00 22.11 ? 285 THR A CB    1 
ATOM   2137 O OG1   . THR A 1 285 ? 20.149  -14.612 39.313 1.00 35.43 ? 285 THR A OG1   1 
ATOM   2138 C CG2   . THR A 1 285 ? 18.258  -15.648 40.403 1.00 15.63 ? 285 THR A CG2   1 
ATOM   2139 N N     . VAL A 1 286 ? 16.291  -15.213 37.151 1.00 32.18 ? 286 VAL A N     1 
ATOM   2140 C CA    . VAL A 1 286 ? 14.875  -15.486 36.921 1.00 38.67 ? 286 VAL A CA    1 
ATOM   2141 C C     . VAL A 1 286 ? 14.714  -16.576 35.868 1.00 27.20 ? 286 VAL A C     1 
ATOM   2142 O O     . VAL A 1 286 ? 13.954  -17.533 36.053 1.00 30.11 ? 286 VAL A O     1 
ATOM   2143 C CB    . VAL A 1 286 ? 14.138  -14.197 36.516 1.00 32.86 ? 286 VAL A CB    1 
ATOM   2144 C CG1   . VAL A 1 286 ? 12.701  -14.507 36.134 1.00 33.62 ? 286 VAL A CG1   1 
ATOM   2145 C CG2   . VAL A 1 286 ? 14.180  -13.178 37.647 1.00 20.29 ? 286 VAL A CG2   1 
ATOM   2146 N N     . ARG A 1 287 ? 15.419  -16.438 34.742 1.00 20.75 ? 287 ARG A N     1 
ATOM   2147 C CA    . ARG A 1 287 ? 15.442  -17.500 33.742 1.00 24.48 ? 287 ARG A CA    1 
ATOM   2148 C C     . ARG A 1 287 ? 15.681  -18.854 34.394 1.00 34.36 ? 287 ARG A C     1 
ATOM   2149 O O     . ARG A 1 287 ? 14.971  -19.830 34.124 1.00 36.97 ? 287 ARG A O     1 
ATOM   2150 C CB    . ARG A 1 287 ? 16.539  -17.233 32.716 1.00 22.68 ? 287 ARG A CB    1 
ATOM   2151 C CG    . ARG A 1 287 ? 16.308  -16.089 31.771 1.00 19.50 ? 287 ARG A CG    1 
ATOM   2152 C CD    . ARG A 1 287 ? 17.465  -16.042 30.800 1.00 15.14 ? 287 ARG A CD    1 
ATOM   2153 N NE    . ARG A 1 287 ? 17.089  -16.439 29.450 1.00 16.98 ? 287 ARG A NE    1 
ATOM   2154 C CZ    . ARG A 1 287 ? 17.937  -16.505 28.434 1.00 15.03 ? 287 ARG A CZ    1 
ATOM   2155 N NH1   . ARG A 1 287 ? 19.230  -16.273 28.597 1.00 25.39 ? 287 ARG A NH1   1 
ATOM   2156 N NH2   . ARG A 1 287 ? 17.480  -16.823 27.227 1.00 20.67 ? 287 ARG A NH2   1 
ATOM   2157 N N     . ALA A 1 288 ? 16.700  -18.928 35.252 1.00 35.69 ? 288 ALA A N     1 
ATOM   2158 C CA    . ALA A 1 288 ? 17.052  -20.189 35.890 1.00 37.14 ? 288 ALA A CA    1 
ATOM   2159 C C     . ALA A 1 288 ? 15.908  -20.705 36.750 1.00 40.15 ? 288 ALA A C     1 
ATOM   2160 O O     . ALA A 1 288 ? 15.564  -21.892 36.703 1.00 44.43 ? 288 ALA A O     1 
ATOM   2161 C CB    . ALA A 1 288 ? 18.317  -20.007 36.730 1.00 36.07 ? 288 ALA A CB    1 
ATOM   2162 N N     . ARG A 1 289 ? 15.300  -19.822 37.544 1.00 37.12 ? 289 ARG A N     1 
ATOM   2163 C CA    . ARG A 1 289 ? 14.262  -20.264 38.466 1.00 34.12 ? 289 ARG A CA    1 
ATOM   2164 C C     . ARG A 1 289 ? 12.963  -20.592 37.743 1.00 31.61 ? 289 ARG A C     1 
ATOM   2165 O O     . ARG A 1 289 ? 12.220  -21.475 38.186 1.00 35.78 ? 289 ARG A O     1 
ATOM   2166 C CB    . ARG A 1 289 ? 14.029  -19.201 39.538 1.00 25.31 ? 289 ARG A CB    1 
ATOM   2167 C CG    . ARG A 1 289 ? 14.934  -19.373 40.745 1.00 28.29 ? 289 ARG A CG    1 
ATOM   2168 C CD    . ARG A 1 289 ? 14.804  -18.222 41.722 1.00 42.12 ? 289 ARG A CD    1 
ATOM   2169 N NE    . ARG A 1 289 ? 13.553  -18.277 42.468 1.00 55.49 ? 289 ARG A NE    1 
ATOM   2170 C CZ    . ARG A 1 289 ? 13.256  -17.489 43.492 1.00 43.81 ? 289 ARG A CZ    1 
ATOM   2171 N NH1   . ARG A 1 289 ? 14.103  -16.571 43.927 1.00 36.39 ? 289 ARG A NH1   1 
ATOM   2172 N NH2   . ARG A 1 289 ? 12.079  -17.627 44.096 1.00 44.63 ? 289 ARG A NH2   1 
ATOM   2173 N N     . VAL A 1 290 ? 12.669  -19.908 36.635 1.00 33.25 ? 290 VAL A N     1 
ATOM   2174 C CA    . VAL A 1 290 ? 11.466  -20.242 35.880 1.00 36.67 ? 290 VAL A CA    1 
ATOM   2175 C C     . VAL A 1 290 ? 11.657  -21.552 35.131 1.00 34.23 ? 290 VAL A C     1 
ATOM   2176 O O     . VAL A 1 290 ? 10.736  -22.374 35.053 1.00 37.36 ? 290 VAL A O     1 
ATOM   2177 C CB    . VAL A 1 290 ? 11.079  -19.100 34.925 1.00 34.97 ? 290 VAL A CB    1 
ATOM   2178 C CG1   . VAL A 1 290 ? 9.940   -19.548 34.015 1.00 38.09 ? 290 VAL A CG1   1 
ATOM   2179 C CG2   . VAL A 1 290 ? 10.674  -17.867 35.713 1.00 29.67 ? 290 VAL A CG2   1 
ATOM   2180 N N     . PHE A 1 291 ? 12.844  -21.774 34.561 1.00 32.70 ? 291 PHE A N     1 
ATOM   2181 C CA    . PHE A 1 291 ? 13.098  -23.064 33.932 1.00 31.07 ? 291 PHE A CA    1 
ATOM   2182 C C     . PHE A 1 291 ? 12.930  -24.193 34.938 1.00 31.78 ? 291 PHE A C     1 
ATOM   2183 O O     . PHE A 1 291 ? 12.270  -25.200 34.659 1.00 40.10 ? 291 PHE A O     1 
ATOM   2184 C CB    . PHE A 1 291 ? 14.497  -23.127 33.327 1.00 30.98 ? 291 PHE A CB    1 
ATOM   2185 C CG    . PHE A 1 291 ? 14.778  -24.438 32.656 1.00 32.12 ? 291 PHE A CG    1 
ATOM   2186 C CD1   . PHE A 1 291 ? 14.389  -24.651 31.346 1.00 31.51 ? 291 PHE A CD1   1 
ATOM   2187 C CD2   . PHE A 1 291 ? 15.371  -25.478 33.353 1.00 29.58 ? 291 PHE A CD2   1 
ATOM   2188 C CE1   . PHE A 1 291 ? 14.621  -25.863 30.730 1.00 29.81 ? 291 PHE A CE1   1 
ATOM   2189 C CE2   . PHE A 1 291 ? 15.603  -26.694 32.742 1.00 31.75 ? 291 PHE A CE2   1 
ATOM   2190 C CZ    . PHE A 1 291 ? 15.227  -26.887 31.428 1.00 31.07 ? 291 PHE A CZ    1 
ATOM   2191 N N     . GLU A 1 292 ? 13.534  -24.044 36.118 1.00 32.91 ? 292 GLU A N     1 
ATOM   2192 C CA    . GLU A 1 292 ? 13.444  -25.092 37.126 1.00 31.05 ? 292 GLU A CA    1 
ATOM   2193 C C     . GLU A 1 292 ? 12.007  -25.310 37.572 1.00 42.20 ? 292 GLU A C     1 
ATOM   2194 O O     . GLU A 1 292 ? 11.617  -26.441 37.882 1.00 51.87 ? 292 GLU A O     1 
ATOM   2195 C CB    . GLU A 1 292 ? 14.323  -24.738 38.326 1.00 43.09 ? 292 GLU A CB    1 
ATOM   2196 C CG    . GLU A 1 292 ? 15.815  -24.827 38.048 1.00 54.58 ? 292 GLU A CG    1 
ATOM   2197 C CD    . GLU A 1 292 ? 16.280  -26.249 37.804 1.00 50.80 ? 292 GLU A CD    1 
ATOM   2198 O OE1   . GLU A 1 292 ? 16.986  -26.481 36.801 1.00 52.77 ? 292 GLU A OE1   1 
ATOM   2199 O OE2   . GLU A 1 292 ? 15.937  -27.136 38.615 1.00 42.64 ? 292 GLU A OE2   1 
ATOM   2200 N N     . ASN A 1 293 ? 11.205  -24.246 37.600 1.00 41.23 ? 293 ASN A N     1 
ATOM   2201 C CA    . ASN A 1 293 ? 9.834   -24.343 38.080 1.00 37.03 ? 293 ASN A CA    1 
ATOM   2202 C C     . ASN A 1 293 ? 8.855   -24.794 37.005 1.00 34.43 ? 293 ASN A C     1 
ATOM   2203 O O     . ASN A 1 293 ? 7.761   -25.258 37.345 1.00 36.92 ? 293 ASN A O     1 
ATOM   2204 C CB    . ASN A 1 293 ? 9.386   -22.989 38.639 1.00 40.98 ? 293 ASN A CB    1 
ATOM   2205 C CG    . ASN A 1 293 ? 7.959   -23.010 39.147 1.00 31.59 ? 293 ASN A CG    1 
ATOM   2206 O OD1   . ASN A 1 293 ? 7.705   -23.339 40.306 1.00 25.81 ? 293 ASN A OD1   1 
ATOM   2207 N ND2   . ASN A 1 293 ? 7.017   -22.656 38.279 1.00 28.45 ? 293 ASN A ND2   1 
ATOM   2208 N N     . SER A 1 294 ? 9.216   -24.685 35.725 1.00 33.68 ? 294 SER A N     1 
ATOM   2209 C CA    . SER A 1 294 ? 8.238   -24.896 34.664 1.00 30.72 ? 294 SER A CA    1 
ATOM   2210 C C     . SER A 1 294 ? 8.824   -25.533 33.408 1.00 27.60 ? 294 SER A C     1 
ATOM   2211 O O     . SER A 1 294 ? 8.076   -25.900 32.496 1.00 28.64 ? 294 SER A O     1 
ATOM   2212 C CB    . SER A 1 294 ? 7.587   -23.561 34.298 1.00 42.45 ? 294 SER A CB    1 
ATOM   2213 O OG    . SER A 1 294 ? 8.417   -22.815 33.424 1.00 34.71 ? 294 SER A OG    1 
ATOM   2214 N N     . GLY A 1 295 ? 10.146  -25.671 33.336 1.00 30.51 ? 295 GLY A N     1 
ATOM   2215 C CA    . GLY A 1 295 ? 10.758  -26.178 32.124 1.00 15.79 ? 295 GLY A CA    1 
ATOM   2216 C C     . GLY A 1 295 ? 10.703  -25.227 30.952 1.00 13.64 ? 295 GLY A C     1 
ATOM   2217 O O     . GLY A 1 295 ? 11.112  -25.599 29.847 1.00 16.60 ? 295 GLY A O     1 
ATOM   2218 N N     . ILE A 1 296 ? 10.204  -24.016 31.158 1.00 29.35 ? 296 ILE A N     1 
ATOM   2219 C CA    . ILE A 1 296 ? 10.164  -22.990 30.125 1.00 33.44 ? 296 ILE A CA    1 
ATOM   2220 C C     . ILE A 1 296 ? 11.469  -22.210 30.191 1.00 23.82 ? 296 ILE A C     1 
ATOM   2221 O O     . ILE A 1 296 ? 11.885  -21.774 31.271 1.00 25.92 ? 296 ILE A O     1 
ATOM   2222 C CB    . ILE A 1 296 ? 8.951   -22.064 30.326 1.00 33.45 ? 296 ILE A CB    1 
ATOM   2223 C CG1   . ILE A 1 296 ? 7.651   -22.854 30.143 1.00 34.94 ? 296 ILE A CG1   1 
ATOM   2224 C CG2   . ILE A 1 296 ? 9.009   -20.872 29.372 1.00 28.80 ? 296 ILE A CG2   1 
ATOM   2225 C CD1   . ILE A 1 296 ? 6.402   -22.096 30.544 1.00 44.32 ? 296 ILE A CD1   1 
ATOM   2226 N N     . ARG A 1 297 ? 12.126  -22.044 29.046 1.00 23.21 ? 297 ARG A N     1 
ATOM   2227 C CA    . ARG A 1 297 ? 13.364  -21.275 28.973 1.00 35.03 ? 297 ARG A CA    1 
ATOM   2228 C C     . ARG A 1 297 ? 13.023  -19.922 28.356 1.00 33.00 ? 297 ARG A C     1 
ATOM   2229 O O     . ARG A 1 297 ? 12.658  -19.836 27.180 1.00 26.97 ? 297 ARG A O     1 
ATOM   2230 C CB    . ARG A 1 297 ? 14.448  -22.036 28.202 1.00 25.83 ? 297 ARG A CB    1 
ATOM   2231 C CG    . ARG A 1 297 ? 14.485  -21.897 26.683 1.00 29.14 ? 297 ARG A CG    1 
ATOM   2232 C CD    . ARG A 1 297 ? 15.768  -22.518 26.110 1.00 39.20 ? 297 ARG A CD    1 
ATOM   2233 N NE    . ARG A 1 297 ? 16.149  -23.764 26.771 1.00 44.19 ? 297 ARG A NE    1 
ATOM   2234 C CZ    . ARG A 1 297 ? 17.398  -24.191 26.922 1.00 46.83 ? 297 ARG A CZ    1 
ATOM   2235 N NH1   . ARG A 1 297 ? 18.433  -23.478 26.504 1.00 44.88 ? 297 ARG A NH1   1 
ATOM   2236 N NH2   . ARG A 1 297 ? 17.615  -25.366 27.507 1.00 42.11 ? 297 ARG A NH2   1 
ATOM   2237 N N     . LEU A 1 298 ? 13.101  -18.872 29.170 1.00 31.94 ? 298 LEU A N     1 
ATOM   2238 C CA    . LEU A 1 298 ? 12.631  -17.565 28.745 1.00 27.07 ? 298 LEU A CA    1 
ATOM   2239 C C     . LEU A 1 298 ? 13.598  -16.928 27.760 1.00 26.64 ? 298 LEU A C     1 
ATOM   2240 O O     . LEU A 1 298 ? 14.808  -17.160 27.792 1.00 35.94 ? 298 LEU A O     1 
ATOM   2241 C CB    . LEU A 1 298 ? 12.438  -16.639 29.942 1.00 25.32 ? 298 LEU A CB    1 
ATOM   2242 C CG    . LEU A 1 298 ? 11.246  -16.966 30.836 1.00 23.15 ? 298 LEU A CG    1 
ATOM   2243 C CD1   . LEU A 1 298 ? 11.348  -16.172 32.119 1.00 25.62 ? 298 LEU A CD1   1 
ATOM   2244 C CD2   . LEU A 1 298 ? 9.930   -16.678 30.121 1.00 40.88 ? 298 LEU A CD2   1 
ATOM   2245 N N     . HIS A 1 299 ? 13.034  -16.108 26.884 1.00 22.41 ? 299 HIS A N     1 
ATOM   2246 C CA    . HIS A 1 299 ? 13.745  -15.473 25.789 1.00 24.06 ? 299 HIS A CA    1 
ATOM   2247 C C     . HIS A 1 299 ? 13.824  -13.981 26.083 1.00 34.99 ? 299 HIS A C     1 
ATOM   2248 O O     . HIS A 1 299 ? 12.797  -13.347 26.350 1.00 30.12 ? 299 HIS A O     1 
ATOM   2249 C CB    . HIS A 1 299 ? 13.014  -15.741 24.470 1.00 35.62 ? 299 HIS A CB    1 
ATOM   2250 C CG    . HIS A 1 299 ? 12.965  -17.192 24.082 1.00 42.39 ? 299 HIS A CG    1 
ATOM   2251 N ND1   . HIS A 1 299 ? 12.875  -18.215 25.003 1.00 49.65 ? 299 HIS A ND1   1 
ATOM   2252 C CD2   . HIS A 1 299 ? 12.960  -17.786 22.865 1.00 32.84 ? 299 HIS A CD2   1 
ATOM   2253 C CE1   . HIS A 1 299 ? 12.840  -19.375 24.371 1.00 36.24 ? 299 HIS A CE1   1 
ATOM   2254 N NE2   . HIS A 1 299 ? 12.887  -19.142 23.073 1.00 33.82 ? 299 HIS A NE2   1 
ATOM   2255 N N     . TRP A 1 300 ? 15.035  -13.426 26.064 1.00 32.98 ? 300 TRP A N     1 
ATOM   2256 C CA    . TRP A 1 300 ? 15.201  -12.016 26.393 1.00 29.24 ? 300 TRP A CA    1 
ATOM   2257 C C     . TRP A 1 300 ? 14.510  -11.148 25.349 1.00 29.92 ? 300 TRP A C     1 
ATOM   2258 O O     . TRP A 1 300 ? 14.574  -11.420 24.146 1.00 26.57 ? 300 TRP A O     1 
ATOM   2259 C CB    . TRP A 1 300 ? 16.685  -11.631 26.467 1.00 33.45 ? 300 TRP A CB    1 
ATOM   2260 C CG    . TRP A 1 300 ? 17.383  -11.939 27.774 1.00 21.79 ? 300 TRP A CG    1 
ATOM   2261 C CD1   . TRP A 1 300 ? 17.973  -13.118 28.123 1.00 26.34 ? 300 TRP A CD1   1 
ATOM   2262 C CD2   . TRP A 1 300 ? 17.588  -11.047 28.884 1.00 22.41 ? 300 TRP A CD2   1 
ATOM   2263 N NE1   . TRP A 1 300 ? 18.521  -13.023 29.379 1.00 26.14 ? 300 TRP A NE1   1 
ATOM   2264 C CE2   . TRP A 1 300 ? 18.298  -11.764 29.869 1.00 22.79 ? 300 TRP A CE2   1 
ATOM   2265 C CE3   . TRP A 1 300 ? 17.235  -9.718  29.143 1.00 29.22 ? 300 TRP A CE3   1 
ATOM   2266 C CZ2   . TRP A 1 300 ? 18.662  -11.199 31.090 1.00 22.63 ? 300 TRP A CZ2   1 
ATOM   2267 C CZ3   . TRP A 1 300 ? 17.597  -9.159  30.362 1.00 28.82 ? 300 TRP A CZ3   1 
ATOM   2268 C CH2   . TRP A 1 300 ? 18.303  -9.900  31.317 1.00 26.52 ? 300 TRP A CH2   1 
ATOM   2269 N N     . GLU A 1 301 ? 13.845  -10.093 25.819 1.00 27.03 ? 301 GLU A N     1 
ATOM   2270 C CA    . GLU A 1 301 ? 13.290  -9.069  24.947 1.00 42.80 ? 301 GLU A CA    1 
ATOM   2271 C C     . GLU A 1 301 ? 14.108  -7.787  24.970 1.00 29.24 ? 301 GLU A C     1 
ATOM   2272 O O     . GLU A 1 301 ? 13.954  -6.953  24.073 1.00 30.01 ? 301 GLU A O     1 
ATOM   2273 C CB    . GLU A 1 301 ? 11.840  -8.764  25.352 1.00 34.87 ? 301 GLU A CB    1 
ATOM   2274 C CG    . GLU A 1 301 ? 10.799  -9.560  24.573 1.00 30.13 ? 301 GLU A CG    1 
ATOM   2275 C CD    . GLU A 1 301 ? 10.612  -9.065  23.155 1.00 41.29 ? 301 GLU A CD    1 
ATOM   2276 O OE1   . GLU A 1 301 ? 11.338  -8.139  22.738 1.00 39.08 ? 301 GLU A OE1   1 
ATOM   2277 O OE2   . GLU A 1 301 ? 9.738   -9.614  22.453 1.00 47.83 ? 301 GLU A OE2   1 
ATOM   2278 N N     . ILE A 1 302 ? 14.974  -7.628  25.968 1.00 32.64 ? 302 ILE A N     1 
ATOM   2279 C CA    . ILE A 1 302 ? 15.902  -6.511  26.094 1.00 28.50 ? 302 ILE A CA    1 
ATOM   2280 C C     . ILE A 1 302 ? 17.258  -6.955  25.560 1.00 23.67 ? 302 ILE A C     1 
ATOM   2281 O O     . ILE A 1 302 ? 17.688  -8.090  25.803 1.00 31.55 ? 302 ILE A O     1 
ATOM   2282 C CB    . ILE A 1 302 ? 15.991  -6.072  27.570 1.00 35.15 ? 302 ILE A CB    1 
ATOM   2283 C CG1   . ILE A 1 302 ? 14.697  -5.368  27.999 1.00 22.52 ? 302 ILE A CG1   1 
ATOM   2284 C CG2   . ILE A 1 302 ? 17.208  -5.195  27.822 1.00 36.47 ? 302 ILE A CG2   1 
ATOM   2285 C CD1   . ILE A 1 302 ? 14.443  -5.423  29.495 1.00 25.65 ? 302 ILE A CD1   1 
ATOM   2286 N N     . LYS A 1 303 ? 17.934  -6.074  24.823 1.00 22.90 ? 303 LYS A N     1 
ATOM   2287 C CA    . LYS A 1 303 ? 19.213  -6.421  24.207 1.00 27.55 ? 303 LYS A CA    1 
ATOM   2288 C C     . LYS A 1 303 ? 20.351  -6.221  25.204 1.00 27.31 ? 303 LYS A C     1 
ATOM   2289 O O     . LYS A 1 303 ? 20.600  -5.097  25.651 1.00 24.74 ? 303 LYS A O     1 
ATOM   2290 C CB    . LYS A 1 303 ? 19.458  -5.580  22.954 1.00 23.83 ? 303 LYS A CB    1 
ATOM   2291 C CG    . LYS A 1 303 ? 20.331  -6.267  21.901 1.00 30.83 ? 303 LYS A CG    1 
ATOM   2292 C CD    . LYS A 1 303 ? 20.421  -5.445  20.615 1.00 32.42 ? 303 LYS A CD    1 
ATOM   2293 C CE    . LYS A 1 303 ? 20.774  -6.301  19.402 1.00 38.70 ? 303 LYS A CE    1 
ATOM   2294 N NZ    . LYS A 1 303 ? 20.060  -5.854  18.172 1.00 37.65 ? 303 LYS A NZ    1 
ATOM   2295 N N     . ARG A 1 304 ? 21.044  -7.307  25.545 1.00 30.37 ? 304 ARG A N     1 
ATOM   2296 C CA    . ARG A 1 304 ? 22.263  -7.206  26.336 1.00 32.65 ? 304 ARG A CA    1 
ATOM   2297 C C     . ARG A 1 304 ? 23.432  -6.843  25.429 1.00 27.19 ? 304 ARG A C     1 
ATOM   2298 O O     . ARG A 1 304 ? 23.465  -7.199  24.248 1.00 39.28 ? 304 ARG A O     1 
ATOM   2299 C CB    . ARG A 1 304 ? 22.549  -8.509  27.078 1.00 31.22 ? 304 ARG A CB    1 
ATOM   2300 C CG    . ARG A 1 304 ? 21.696  -8.697  28.324 1.00 34.32 ? 304 ARG A CG    1 
ATOM   2301 C CD    . ARG A 1 304 ? 20.862  -9.950  28.199 1.00 35.47 ? 304 ARG A CD    1 
ATOM   2302 N NE    . ARG A 1 304 ? 20.020  -9.859  27.012 1.00 39.78 ? 304 ARG A NE    1 
ATOM   2303 C CZ    . ARG A 1 304 ? 20.041  -10.706 25.991 1.00 38.97 ? 304 ARG A CZ    1 
ATOM   2304 N NH1   . ARG A 1 304 ? 20.764  -11.815 26.021 1.00 41.25 ? 304 ARG A NH1   1 
ATOM   2305 N NH2   . ARG A 1 304 ? 19.320  -10.431 24.908 1.00 34.47 ? 304 ARG A NH2   1 
ATOM   2306 N N     . LEU A 1 305 ? 24.406  -6.142  26.001 1.00 30.78 ? 305 LEU A N     1 
ATOM   2307 C CA    . LEU A 1 305 ? 25.246  -5.267  25.200 1.00 32.18 ? 305 LEU A CA    1 
ATOM   2308 C C     . LEU A 1 305 ? 26.500  -4.897  25.979 1.00 26.84 ? 305 LEU A C     1 
ATOM   2309 O O     . LEU A 1 305 ? 26.439  -4.669  27.190 1.00 22.69 ? 305 LEU A O     1 
ATOM   2310 C CB    . LEU A 1 305 ? 24.443  -4.016  24.829 1.00 34.64 ? 305 LEU A CB    1 
ATOM   2311 C CG    . LEU A 1 305 ? 24.807  -3.172  23.618 1.00 45.28 ? 305 LEU A CG    1 
ATOM   2312 C CD1   . LEU A 1 305 ? 23.523  -2.711  22.944 1.00 49.73 ? 305 LEU A CD1   1 
ATOM   2313 C CD2   . LEU A 1 305 ? 25.639  -1.994  24.069 1.00 46.26 ? 305 LEU A CD2   1 
ATOM   2314 N N     . GLY A 1 306 ? 27.627  -4.839  25.279 1.00 35.28 ? 306 GLY A N     1 
ATOM   2315 C CA    . GLY A 1 306 ? 28.872  -4.403  25.883 1.00 30.36 ? 306 GLY A CA    1 
ATOM   2316 C C     . GLY A 1 306 ? 29.708  -5.553  26.412 1.00 27.74 ? 306 GLY A C     1 
ATOM   2317 O O     . GLY A 1 306 ? 29.550  -6.717  26.032 1.00 33.02 ? 306 GLY A O     1 
ATOM   2318 N N     . LEU A 1 307 ? 30.619  -5.204  27.318 1.00 31.33 ? 307 LEU A N     1 
ATOM   2319 C CA    . LEU A 1 307 ? 31.593  -6.139  27.859 1.00 21.12 ? 307 LEU A CA    1 
ATOM   2320 C C     . LEU A 1 307 ? 31.414  -6.304  29.359 1.00 22.16 ? 307 LEU A C     1 
ATOM   2321 O O     . LEU A 1 307 ? 31.070  -5.357  30.072 1.00 29.53 ? 307 LEU A O     1 
ATOM   2322 C CB    . LEU A 1 307 ? 33.027  -5.672  27.596 1.00 25.27 ? 307 LEU A CB    1 
ATOM   2323 C CG    . LEU A 1 307 ? 33.389  -5.304  26.162 1.00 31.14 ? 307 LEU A CG    1 
ATOM   2324 C CD1   . LEU A 1 307 ? 34.868  -4.966  26.081 1.00 36.39 ? 307 LEU A CD1   1 
ATOM   2325 C CD2   . LEU A 1 307 ? 33.034  -6.440  25.221 1.00 32.75 ? 307 LEU A CD2   1 
ATOM   2326 N N     . PHE A 1 308 ? 31.666  -7.521  29.829 1.00 24.18 ? 308 PHE A N     1 
ATOM   2327 C CA    . PHE A 1 308 ? 31.814  -7.755  31.254 1.00 27.81 ? 308 PHE A CA    1 
ATOM   2328 C C     . PHE A 1 308 ? 33.119  -7.142  31.746 1.00 38.36 ? 308 PHE A C     1 
ATOM   2329 O O     . PHE A 1 308 ? 34.077  -6.970  30.986 1.00 30.76 ? 308 PHE A O     1 
ATOM   2330 C CB    . PHE A 1 308 ? 31.808  -9.253  31.554 1.00 33.29 ? 308 PHE A CB    1 
ATOM   2331 C CG    . PHE A 1 308 ? 30.533  -9.946  31.174 1.00 35.16 ? 308 PHE A CG    1 
ATOM   2332 C CD1   . PHE A 1 308 ? 29.353  -9.667  31.841 1.00 31.46 ? 308 PHE A CD1   1 
ATOM   2333 C CD2   . PHE A 1 308 ? 30.515  -10.880 30.152 1.00 34.32 ? 308 PHE A CD2   1 
ATOM   2334 C CE1   . PHE A 1 308 ? 28.179  -10.305 31.496 1.00 29.14 ? 308 PHE A CE1   1 
ATOM   2335 C CE2   . PHE A 1 308 ? 29.343  -11.522 29.802 1.00 35.48 ? 308 PHE A CE2   1 
ATOM   2336 C CZ    . PHE A 1 308 ? 28.174  -11.233 30.475 1.00 31.69 ? 308 PHE A CZ    1 
ATOM   2337 N N     . ARG A 1 309 ? 33.151  -6.800  33.028 1.00 30.65 ? 309 ARG A N     1 
ATOM   2338 C CA    . ARG A 1 309 ? 34.418  -6.459  33.650 1.00 23.29 ? 309 ARG A CA    1 
ATOM   2339 C C     . ARG A 1 309 ? 35.225  -7.733  33.881 1.00 48.28 ? 309 ARG A C     1 
ATOM   2340 O O     . ARG A 1 309 ? 34.691  -8.846  33.869 1.00 48.63 ? 309 ARG A O     1 
ATOM   2341 C CB    . ARG A 1 309 ? 34.191  -5.720  34.968 1.00 20.71 ? 309 ARG A CB    1 
ATOM   2342 C CG    . ARG A 1 309 ? 33.459  -4.397  34.806 1.00 20.99 ? 309 ARG A CG    1 
ATOM   2343 C CD    . ARG A 1 309 ? 33.661  -3.478  36.001 1.00 17.05 ? 309 ARG A CD    1 
ATOM   2344 N NE    . ARG A 1 309 ? 33.356  -4.130  37.270 1.00 16.63 ? 309 ARG A NE    1 
ATOM   2345 C CZ    . ARG A 1 309 ? 33.266  -3.497  38.432 1.00 18.92 ? 309 ARG A CZ    1 
ATOM   2346 N NH1   . ARG A 1 309 ? 33.441  -2.189  38.524 1.00 32.96 ? 309 ARG A NH1   1 
ATOM   2347 N NH2   . ARG A 1 309 ? 32.991  -4.195  39.531 1.00 18.45 ? 309 ARG A NH2   1 
ATOM   2348 N N     . GLU A 1 310 ? 36.531  -7.566  34.073 1.00 54.13 ? 310 GLU A N     1 
ATOM   2349 C CA    . GLU A 1 310 ? 37.385  -8.715  34.343 1.00 44.69 ? 310 GLU A CA    1 
ATOM   2350 C C     . GLU A 1 310 ? 36.852  -9.493  35.539 1.00 31.14 ? 310 GLU A C     1 
ATOM   2351 O O     . GLU A 1 310 ? 36.590  -8.923  36.602 1.00 32.61 ? 310 GLU A O     1 
ATOM   2352 C CB    . GLU A 1 310 ? 38.823  -8.264  34.603 1.00 54.07 ? 310 GLU A CB    1 
ATOM   2353 C CG    . GLU A 1 310 ? 39.871  -9.137  33.926 1.00 50.33 ? 310 GLU A CG    1 
ATOM   2354 C CD    . GLU A 1 310 ? 39.946  -8.906  32.429 1.00 63.59 ? 310 GLU A CD    1 
ATOM   2355 O OE1   . GLU A 1 310 ? 39.981  -7.730  32.010 1.00 69.42 ? 310 GLU A OE1   1 
ATOM   2356 O OE2   . GLU A 1 310 ? 39.969  -9.899  31.672 1.00 68.37 ? 310 GLU A OE2   1 
ATOM   2357 N N     . GLY A 1 311 ? 36.679  -10.799 35.352 1.00 35.37 ? 311 GLY A N     1 
ATOM   2358 C CA    . GLY A 1 311 ? 36.182  -11.645 36.420 1.00 36.51 ? 311 GLY A CA    1 
ATOM   2359 C C     . GLY A 1 311 ? 34.725  -11.432 36.762 1.00 33.84 ? 311 GLY A C     1 
ATOM   2360 O O     . GLY A 1 311 ? 34.321  -11.694 37.899 1.00 33.60 ? 311 GLY A O     1 
ATOM   2361 N N     . GLU A 1 312 ? 33.918  -10.970 35.807 1.00 42.19 ? 312 GLU A N     1 
ATOM   2362 C CA    . GLU A 1 312 ? 32.511  -10.669 36.058 1.00 41.23 ? 312 GLU A CA    1 
ATOM   2363 C C     . GLU A 1 312 ? 31.641  -11.156 34.907 1.00 37.27 ? 312 GLU A C     1 
ATOM   2364 O O     . GLU A 1 312 ? 30.657  -10.510 34.534 1.00 34.12 ? 312 GLU A O     1 
ATOM   2365 C CB    . GLU A 1 312 ? 32.299  -9.173  36.286 1.00 32.20 ? 312 GLU A CB    1 
ATOM   2366 C CG    . GLU A 1 312 ? 32.608  -8.714  37.697 1.00 26.46 ? 312 GLU A CG    1 
ATOM   2367 C CD    . GLU A 1 312 ? 32.130  -7.300  37.962 1.00 30.28 ? 312 GLU A CD    1 
ATOM   2368 O OE1   . GLU A 1 312 ? 31.615  -6.660  37.020 1.00 28.65 ? 312 GLU A OE1   1 
ATOM   2369 O OE2   . GLU A 1 312 ? 32.266  -6.831  39.111 1.00 27.23 ? 312 GLU A OE2   1 
ATOM   2370 N N     . GLN A 1 313 ? 31.987  -12.300 34.327 1.00 41.16 ? 313 GLN A N     1 
ATOM   2371 C CA    . GLN A 1 313 ? 31.120  -12.898 33.326 1.00 31.57 ? 313 GLN A CA    1 
ATOM   2372 C C     . GLN A 1 313 ? 29.886  -13.495 33.990 1.00 24.59 ? 313 GLN A C     1 
ATOM   2373 O O     . GLN A 1 313 ? 29.903  -13.872 35.165 1.00 24.93 ? 313 GLN A O     1 
ATOM   2374 C CB    . GLN A 1 313 ? 31.860  -13.976 32.538 1.00 39.11 ? 313 GLN A CB    1 
ATOM   2375 C CG    . GLN A 1 313 ? 32.927  -13.425 31.615 1.00 54.46 ? 313 GLN A CG    1 
ATOM   2376 C CD    . GLN A 1 313 ? 33.648  -14.507 30.840 1.00 64.76 ? 313 GLN A CD    1 
ATOM   2377 O OE1   . GLN A 1 313 ? 33.358  -15.694 30.990 1.00 75.98 ? 313 GLN A OE1   1 
ATOM   2378 N NE2   . GLN A 1 313 ? 34.600  -14.102 30.008 1.00 72.84 ? 313 GLN A NE2   1 
ATOM   2379 N N     . ILE A 1 314 ? 28.803  -13.563 33.223 1.00 33.63 ? 314 ILE A N     1 
ATOM   2380 C CA    . ILE A 1 314 ? 27.551  -14.159 33.668 1.00 28.22 ? 314 ILE A CA    1 
ATOM   2381 C C     . ILE A 1 314 ? 27.154  -15.213 32.647 1.00 29.68 ? 314 ILE A C     1 
ATOM   2382 O O     . ILE A 1 314 ? 27.164  -14.948 31.440 1.00 29.55 ? 314 ILE A O     1 
ATOM   2383 C CB    . ILE A 1 314 ? 26.433  -13.110 33.828 1.00 29.09 ? 314 ILE A CB    1 
ATOM   2384 C CG1   . ILE A 1 314 ? 26.868  -11.989 34.775 1.00 33.59 ? 314 ILE A CG1   1 
ATOM   2385 C CG2   . ILE A 1 314 ? 25.161  -13.762 34.350 1.00 29.21 ? 314 ILE A CG2   1 
ATOM   2386 C CD1   . ILE A 1 314 ? 26.178  -10.672 34.504 1.00 35.62 ? 314 ILE A CD1   1 
ATOM   2387 N N     . GLU A 1 315 ? 26.823  -16.407 33.128 1.00 28.06 ? 315 GLU A N     1 
ATOM   2388 C CA    . GLU A 1 315 ? 26.368  -17.484 32.262 1.00 29.95 ? 315 GLU A CA    1 
ATOM   2389 C C     . GLU A 1 315 ? 24.851  -17.450 32.154 1.00 24.00 ? 315 GLU A C     1 
ATOM   2390 O O     . GLU A 1 315 ? 24.149  -17.242 33.148 1.00 19.96 ? 315 GLU A O     1 
ATOM   2391 C CB    . GLU A 1 315 ? 26.816  -18.845 32.796 1.00 31.26 ? 315 GLU A CB    1 
ATOM   2392 C CG    . GLU A 1 315 ? 28.292  -18.938 33.142 1.00 41.43 ? 315 GLU A CG    1 
ATOM   2393 C CD    . GLU A 1 315 ? 29.189  -18.709 31.943 1.00 51.02 ? 315 GLU A CD    1 
ATOM   2394 O OE1   . GLU A 1 315 ? 28.872  -19.230 30.853 1.00 42.17 ? 315 GLU A OE1   1 
ATOM   2395 O OE2   . GLU A 1 315 ? 30.214  -18.010 32.092 1.00 59.80 ? 315 GLU A OE2   1 
ATOM   2396 N N     . GLU A 1 316 ? 24.349  -17.647 30.938 1.00 24.32 ? 316 GLU A N     1 
ATOM   2397 C CA    . GLU A 1 316 ? 22.912  -17.755 30.738 1.00 20.67 ? 316 GLU A CA    1 
ATOM   2398 C C     . GLU A 1 316 ? 22.346  -18.847 31.633 1.00 22.62 ? 316 GLU A C     1 
ATOM   2399 O O     . GLU A 1 316 ? 22.846  -19.975 31.651 1.00 34.32 ? 316 GLU A O     1 
ATOM   2400 C CB    . GLU A 1 316 ? 22.610  -18.049 29.269 1.00 20.14 ? 316 GLU A CB    1 
ATOM   2401 C CG    . GLU A 1 316 ? 22.965  -16.898 28.342 1.00 15.16 ? 316 GLU A CG    1 
ATOM   2402 C CD    . GLU A 1 316 ? 22.552  -17.147 26.907 1.00 24.75 ? 316 GLU A CD    1 
ATOM   2403 O OE1   . GLU A 1 316 ? 21.895  -18.177 26.645 1.00 37.39 ? 316 GLU A OE1   1 
ATOM   2404 O OE2   . GLU A 1 316 ? 22.885  -16.312 26.041 1.00 25.18 ? 316 GLU A OE2   1 
ATOM   2405 N N     . PHE A 1 317 ? 21.306  -18.499 32.390 1.00 28.90 ? 317 PHE A N     1 
ATOM   2406 C CA    . PHE A 1 317 ? 20.708  -19.374 33.393 1.00 25.57 ? 317 PHE A CA    1 
ATOM   2407 C C     . PHE A 1 317 ? 21.654  -19.644 34.556 1.00 26.65 ? 317 PHE A C     1 
ATOM   2408 O O     . PHE A 1 317 ? 21.457  -20.604 35.309 1.00 25.02 ? 317 PHE A O     1 
ATOM   2409 C CB    . PHE A 1 317 ? 20.248  -20.698 32.769 1.00 19.84 ? 317 PHE A CB    1 
ATOM   2410 C CG    . PHE A 1 317 ? 19.326  -20.524 31.593 1.00 23.42 ? 317 PHE A CG    1 
ATOM   2411 C CD1   . PHE A 1 317 ? 17.966  -20.346 31.784 1.00 23.82 ? 317 PHE A CD1   1 
ATOM   2412 C CD2   . PHE A 1 317 ? 19.818  -20.534 30.298 1.00 18.95 ? 317 PHE A CD2   1 
ATOM   2413 C CE1   . PHE A 1 317 ? 17.115  -20.185 30.706 1.00 11.91 ? 317 PHE A CE1   1 
ATOM   2414 C CE2   . PHE A 1 317 ? 18.970  -20.372 29.217 1.00 25.59 ? 317 PHE A CE2   1 
ATOM   2415 C CZ    . PHE A 1 317 ? 17.616  -20.196 29.423 1.00 13.17 ? 317 PHE A CZ    1 
ATOM   2416 N N     . LEU A 1 318 ? 22.678  -18.805 34.722 1.00 33.10 ? 318 LEU A N     1 
ATOM   2417 C CA    . LEU A 1 318 ? 23.676  -18.965 35.779 1.00 27.08 ? 318 LEU A CA    1 
ATOM   2418 C C     . LEU A 1 318 ? 24.422  -20.290 35.649 1.00 16.65 ? 318 LEU A C     1 
ATOM   2419 O O     . LEU A 1 318 ? 24.821  -20.894 36.648 1.00 18.63 ? 318 LEU A O     1 
ATOM   2420 C CB    . LEU A 1 318 ? 23.038  -18.840 37.166 1.00 21.82 ? 318 LEU A CB    1 
ATOM   2421 C CG    . LEU A 1 318 ? 22.188  -17.586 37.392 1.00 19.23 ? 318 LEU A CG    1 
ATOM   2422 C CD1   . LEU A 1 318 ? 21.589  -17.593 38.789 1.00 18.03 ? 318 LEU A CD1   1 
ATOM   2423 C CD2   . LEU A 1 318 ? 22.999  -16.316 37.167 1.00 27.57 ? 318 LEU A CD2   1 
ATOM   2424 N N     . GLY A 1 319 ? 24.617  -20.748 34.413 1.00 13.65 ? 319 GLY A N     1 
ATOM   2425 C CA    . GLY A 1 319 ? 25.331  -21.977 34.149 1.00 30.36 ? 319 GLY A CA    1 
ATOM   2426 C C     . GLY A 1 319 ? 24.564  -23.242 34.459 1.00 29.13 ? 319 GLY A C     1 
ATOM   2427 O O     . GLY A 1 319 ? 25.107  -24.337 34.268 1.00 28.17 ? 319 GLY A O     1 
ATOM   2428 N N     . LYS A 1 320 ? 23.317  -23.131 34.920 1.00 29.02 ? 320 LYS A N     1 
ATOM   2429 C CA    . LYS A 1 320 ? 22.575  -24.313 35.340 1.00 22.03 ? 320 LYS A CA    1 
ATOM   2430 C C     . LYS A 1 320 ? 22.153  -25.166 34.152 1.00 17.40 ? 320 LYS A C     1 
ATOM   2431 O O     . LYS A 1 320 ? 22.091  -26.395 34.266 1.00 25.78 ? 320 LYS A O     1 
ATOM   2432 C CB    . LYS A 1 320 ? 21.364  -23.885 36.165 1.00 21.27 ? 320 LYS A CB    1 
ATOM   2433 C CG    . LYS A 1 320 ? 21.762  -23.124 37.422 1.00 23.92 ? 320 LYS A CG    1 
ATOM   2434 C CD    . LYS A 1 320 ? 20.774  -23.312 38.559 1.00 36.38 ? 320 LYS A CD    1 
ATOM   2435 C CE    . LYS A 1 320 ? 21.479  -23.763 39.829 1.00 42.53 ? 320 LYS A CE    1 
ATOM   2436 N NZ    . LYS A 1 320 ? 22.234  -25.035 39.632 1.00 39.22 ? 320 LYS A NZ    1 
ATOM   2437 N N     . ILE A 1 321 ? 21.861  -24.542 33.012 1.00 22.89 ? 321 ILE A N     1 
ATOM   2438 C CA    . ILE A 1 321 ? 21.617  -25.251 31.765 1.00 22.00 ? 321 ILE A CA    1 
ATOM   2439 C C     . ILE A 1 321 ? 22.388  -24.547 30.658 1.00 14.95 ? 321 ILE A C     1 
ATOM   2440 O O     . ILE A 1 321 ? 22.974  -23.482 30.853 1.00 20.32 ? 321 ILE A O     1 
ATOM   2441 C CB    . ILE A 1 321 ? 20.115  -25.339 31.408 1.00 38.12 ? 321 ILE A CB    1 
ATOM   2442 C CG1   . ILE A 1 321 ? 19.501  -23.943 31.253 1.00 29.22 ? 321 ILE A CG1   1 
ATOM   2443 C CG2   . ILE A 1 321 ? 19.361  -26.137 32.463 1.00 31.83 ? 321 ILE A CG2   1 
ATOM   2444 C CD1   . ILE A 1 321 ? 18.149  -23.950 30.564 1.00 31.51 ? 321 ILE A CD1   1 
ATOM   2445 N N     . VAL A 1 322 ? 22.383  -25.166 29.484 1.00 14.18 ? 322 VAL A N     1 
ATOM   2446 C CA    . VAL A 1 322 ? 22.968  -24.565 28.297 1.00 21.84 ? 322 VAL A CA    1 
ATOM   2447 C C     . VAL A 1 322 ? 21.969  -24.722 27.159 1.00 29.02 ? 322 VAL A C     1 
ATOM   2448 O O     . VAL A 1 322 ? 22.067  -24.071 26.120 1.00 34.32 ? 322 VAL A O     1 
ATOM   2449 C CB    . VAL A 1 322 ? 24.330  -25.200 27.947 1.00 35.12 ? 322 VAL A CB    1 
ATOM   2450 C CG1   . VAL A 1 322 ? 24.771  -24.793 26.546 1.00 30.33 ? 322 VAL A CG1   1 
ATOM   2451 C CG2   . VAL A 1 322 ? 25.383  -24.805 28.976 1.00 33.28 ? 322 VAL A CG2   1 
ATOM   2452 O OXT   . VAL A 1 322 ? 21.027  -25.507 27.262 1.00 32.48 ? 322 VAL A OXT   1 
HETATM 2453 S S     . SO4 B 2 .   ? 19.999  15.476  21.617 1.00 48.09 ? 401 SO4 A S     1 
HETATM 2454 O O1    . SO4 B 2 .   ? 18.999  15.377  22.677 1.00 49.13 ? 401 SO4 A O1    1 
HETATM 2455 O O2    . SO4 B 2 .   ? 21.322  15.212  22.175 1.00 59.92 ? 401 SO4 A O2    1 
HETATM 2456 O O3    . SO4 B 2 .   ? 19.707  14.497  20.574 1.00 46.77 ? 401 SO4 A O3    1 
HETATM 2457 O O4    . SO4 B 2 .   ? 19.970  16.818  21.042 1.00 53.51 ? 401 SO4 A O4    1 
HETATM 2458 P PA    . FAD C 3 .   ? 17.252  1.770   21.759 1.00 25.51 ? 402 FAD A PA    1 
HETATM 2459 O O1A   . FAD C 3 .   ? 16.863  1.081   23.013 1.00 19.25 ? 402 FAD A O1A   1 
HETATM 2460 O O2A   . FAD C 3 .   ? 18.310  2.869   21.911 1.00 35.11 ? 402 FAD A O2A   1 
HETATM 2461 O O5B   . FAD C 3 .   ? 17.697  0.726   20.680 1.00 38.09 ? 402 FAD A O5B   1 
HETATM 2462 C C5B   . FAD C 3 .   ? 16.895  -0.439  20.394 1.00 31.27 ? 402 FAD A C5B   1 
HETATM 2463 C C4B   . FAD C 3 .   ? 17.249  -0.964  19.026 1.00 34.63 ? 402 FAD A C4B   1 
HETATM 2464 O O4B   . FAD C 3 .   ? 16.904  0.023   18.027 1.00 28.57 ? 402 FAD A O4B   1 
HETATM 2465 C C3B   . FAD C 3 .   ? 18.732  -1.284  18.828 1.00 42.52 ? 402 FAD A C3B   1 
HETATM 2466 O O3B   . FAD C 3 .   ? 18.903  -2.534  18.170 1.00 42.22 ? 402 FAD A O3B   1 
HETATM 2467 C C2B   . FAD C 3 .   ? 19.230  -0.121  17.966 1.00 41.71 ? 402 FAD A C2B   1 
HETATM 2468 O O2B   . FAD C 3 .   ? 20.317  -0.496  17.128 1.00 46.93 ? 402 FAD A O2B   1 
HETATM 2469 C C1B   . FAD C 3 .   ? 17.986  0.176   17.138 1.00 39.46 ? 402 FAD A C1B   1 
HETATM 2470 N N9A   . FAD C 3 .   ? 17.953  1.521   16.580 1.00 22.86 ? 402 FAD A N9A   1 
HETATM 2471 C C8A   . FAD C 3 .   ? 17.581  2.683   17.203 1.00 22.43 ? 402 FAD A C8A   1 
HETATM 2472 N N7A   . FAD C 3 .   ? 17.664  3.747   16.439 1.00 36.21 ? 402 FAD A N7A   1 
HETATM 2473 C C5A   . FAD C 3 .   ? 18.127  3.247   15.230 1.00 19.77 ? 402 FAD A C5A   1 
HETATM 2474 C C6A   . FAD C 3 .   ? 18.428  3.861   14.000 1.00 25.20 ? 402 FAD A C6A   1 
HETATM 2475 N N6A   . FAD C 3 .   ? 18.304  5.170   13.769 1.00 30.86 ? 402 FAD A N6A   1 
HETATM 2476 N N1A   . FAD C 3 .   ? 18.875  3.071   13.002 1.00 33.18 ? 402 FAD A N1A   1 
HETATM 2477 C C2A   . FAD C 3 .   ? 18.999  1.759   13.215 1.00 30.13 ? 402 FAD A C2A   1 
HETATM 2478 N N3A   . FAD C 3 .   ? 18.745  1.072   14.330 1.00 28.97 ? 402 FAD A N3A   1 
HETATM 2479 C C4A   . FAD C 3 .   ? 18.310  1.878   15.305 1.00 24.14 ? 402 FAD A C4A   1 
HETATM 2480 N N1    . FAD C 3 .   ? 8.746   -2.194  23.305 1.00 36.76 ? 402 FAD A N1    1 
HETATM 2481 C C2    . FAD C 3 .   ? 7.703   -2.659  22.556 1.00 36.94 ? 402 FAD A C2    1 
HETATM 2482 O O2    . FAD C 3 .   ? 7.886   -3.254  21.489 1.00 40.97 ? 402 FAD A O2    1 
HETATM 2483 N N3    . FAD C 3 .   ? 6.403   -2.464  22.990 1.00 37.58 ? 402 FAD A N3    1 
HETATM 2484 C C4    . FAD C 3 .   ? 6.029   -1.826  24.152 1.00 29.54 ? 402 FAD A C4    1 
HETATM 2485 O O4    . FAD C 3 .   ? 4.839   -1.709  24.438 1.00 41.07 ? 402 FAD A O4    1 
HETATM 2486 C C4X   . FAD C 3 .   ? 7.140   -1.334  24.941 1.00 34.19 ? 402 FAD A C4X   1 
HETATM 2487 N N5    . FAD C 3 .   ? 6.872   -0.718  26.052 1.00 29.42 ? 402 FAD A N5    1 
HETATM 2488 C C5X   . FAD C 3 .   ? 7.930   -0.249  26.809 1.00 34.66 ? 402 FAD A C5X   1 
HETATM 2489 C C6    . FAD C 3 .   ? 7.652   0.414   28.003 1.00 35.09 ? 402 FAD A C6    1 
HETATM 2490 C C7    . FAD C 3 .   ? 8.676   0.905   28.805 1.00 37.21 ? 402 FAD A C7    1 
HETATM 2491 C C7M   . FAD C 3 .   ? 8.333   1.619   30.086 1.00 41.83 ? 402 FAD A C7M   1 
HETATM 2492 C C8    . FAD C 3 .   ? 10.012  0.734   28.405 1.00 37.20 ? 402 FAD A C8    1 
HETATM 2493 C C8M   . FAD C 3 .   ? 11.147  1.255   29.248 1.00 31.48 ? 402 FAD A C8M   1 
HETATM 2494 C C9    . FAD C 3 .   ? 10.292  0.072   27.213 1.00 35.90 ? 402 FAD A C9    1 
HETATM 2495 C C9A   . FAD C 3 .   ? 9.265   -0.420  26.414 1.00 34.57 ? 402 FAD A C9A   1 
HETATM 2496 N N10   . FAD C 3 .   ? 9.513   -1.089  25.196 1.00 32.75 ? 402 FAD A N10   1 
HETATM 2497 C C10   . FAD C 3 .   ? 8.468   -1.567  24.436 1.00 34.35 ? 402 FAD A C10   1 
HETATM 2498 C "C1'" . FAD C 3 .   ? 10.890  -1.318  24.727 1.00 32.95 ? 402 FAD A "C1'" 1 
HETATM 2499 C "C2'" . FAD C 3 .   ? 11.448  -0.163  23.898 1.00 34.26 ? 402 FAD A "C2'" 1 
HETATM 2500 O "O2'" . FAD C 3 .   ? 10.668  1.018   24.090 1.00 33.74 ? 402 FAD A "O2'" 1 
HETATM 2501 C "C3'" . FAD C 3 .   ? 11.439  -0.552  22.418 1.00 23.89 ? 402 FAD A "C3'" 1 
HETATM 2502 O "O3'" . FAD C 3 .   ? 12.186  -1.751  22.247 1.00 43.54 ? 402 FAD A "O3'" 1 
HETATM 2503 C "C4'" . FAD C 3 .   ? 12.004  0.509   21.470 1.00 27.62 ? 402 FAD A "C4'" 1 
HETATM 2504 O "O4'" . FAD C 3 .   ? 12.006  -0.022  20.144 1.00 45.64 ? 402 FAD A "O4'" 1 
HETATM 2505 C "C5'" . FAD C 3 .   ? 13.401  0.975   21.822 1.00 33.43 ? 402 FAD A "C5'" 1 
HETATM 2506 O "O5'" . FAD C 3 .   ? 13.538  2.363   21.452 1.00 30.77 ? 402 FAD A "O5'" 1 
HETATM 2507 P P     . FAD C 3 .   ? 14.823  3.189   21.832 1.00 23.00 ? 402 FAD A P     1 
HETATM 2508 O O1P   . FAD C 3 .   ? 14.720  4.587   21.213 1.00 32.37 ? 402 FAD A O1P   1 
HETATM 2509 O O2P   . FAD C 3 .   ? 15.060  3.153   23.296 1.00 22.56 ? 402 FAD A O2P   1 
HETATM 2510 O O3P   . FAD C 3 .   ? 15.977  2.416   21.074 1.00 34.93 ? 402 FAD A O3P   1 
HETATM 2511 N N1U   . EPU D 4 .   ? -0.608  -8.165  35.497 1.00 22.89 ? 403 EPU A N1U   1 
HETATM 2512 C C2U   . EPU D 4 .   ? -0.693  -8.405  36.976 1.00 24.03 ? 403 EPU A C2U   1 
HETATM 2513 N N3U   . EPU D 4 .   ? 0.566   -8.562  37.782 1.00 24.59 ? 403 EPU A N3U   1 
HETATM 2514 C C4U   . EPU D 4 .   ? 1.867   -8.485  37.123 1.00 21.27 ? 403 EPU A C4U   1 
HETATM 2515 C C5U   . EPU D 4 .   ? 1.944   -8.249  35.644 1.00 18.35 ? 403 EPU A C5U   1 
HETATM 2516 C C6U   . EPU D 4 .   ? 0.700   -8.100  34.849 1.00 29.17 ? 403 EPU A C6U   1 
HETATM 2517 O O2U   . EPU D 4 .   ? -1.746  -8.468  37.515 1.00 21.44 ? 403 EPU A O2U   1 
HETATM 2518 O O4U   . EPU D 4 .   ? 2.853   -8.613  37.764 1.00 27.38 ? 403 EPU A O4U   1 
HETATM 2519 C C1D   . EPU D 4 .   ? -1.806  -8.028  34.744 1.00 21.58 ? 403 EPU A C1D   1 
HETATM 2520 C C2D   . EPU D 4 .   ? -1.959  -6.792  34.252 1.00 31.18 ? 403 EPU A C2D   1 
HETATM 2521 O O2D   . EPU D 4 .   ? -2.785  -6.003  35.148 1.00 29.99 ? 403 EPU A O2D   1 
HETATM 2522 C C3D   . EPU D 4 .   ? -2.700  -7.011  32.906 1.00 29.71 ? 403 EPU A C3D   1 
HETATM 2523 C C4D   . EPU D 4 .   ? -2.183  -8.421  32.401 1.00 17.69 ? 403 EPU A C4D   1 
HETATM 2524 O O4D   . EPU D 4 .   ? -1.745  -9.064  33.462 1.00 19.35 ? 403 EPU A O4D   1 
HETATM 2525 O O3D   . EPU D 4 .   ? -4.014  -7.040  33.108 1.00 26.19 ? 403 EPU A O3D   1 
HETATM 2526 C C5D   . EPU D 4 .   ? -1.030  -8.268  31.420 1.00 23.87 ? 403 EPU A C5D   1 
HETATM 2527 O O5D   . EPU D 4 .   ? -0.314  -7.096  31.695 1.00 30.43 ? 403 EPU A O5D   1 
HETATM 2528 P PA    . EPU D 4 .   ? 0.108   -6.223  30.332 1.00 34.16 ? 403 EPU A PA    1 
HETATM 2529 O O1A   . EPU D 4 .   ? -1.081  -5.403  29.860 1.00 46.75 ? 403 EPU A O1A   1 
HETATM 2530 O O2A   . EPU D 4 .   ? 1.293   -5.324  30.622 1.00 37.50 ? 403 EPU A O2A   1 
HETATM 2531 O O3A   . EPU D 4 .   ? 0.492   -7.366  29.180 1.00 44.49 ? 403 EPU A O3A   1 
HETATM 2532 P PB    . EPU D 4 .   ? 1.975   -8.154  29.127 1.00 30.85 ? 403 EPU A PB    1 
HETATM 2533 O O1B   . EPU D 4 .   ? 1.822   -9.530  28.493 1.00 28.81 ? 403 EPU A O1B   1 
HETATM 2534 O O2B   . EPU D 4 .   ? 2.560   -8.280  30.507 1.00 22.63 ? 403 EPU A O2B   1 
HETATM 2535 C C1    . EPU D 4 .   ? 2.724   -7.295  26.825 1.00 32.34 ? 403 EPU A C1    1 
HETATM 2536 C C2    . EPU D 4 .   ? 3.988   -6.757  26.164 1.00 42.50 ? 403 EPU A C2    1 
HETATM 2537 C C3    . EPU D 4 .   ? 4.188   -5.345  26.502 1.00 38.70 ? 403 EPU A C3    1 
HETATM 2538 C C4    . EPU D 4 .   ? 3.007   -4.507  26.127 1.00 35.61 ? 403 EPU A C4    1 
HETATM 2539 C C5    . EPU D 4 .   ? 1.622   -5.083  26.523 1.00 27.56 ? 403 EPU A C5    1 
HETATM 2540 C C6    . EPU D 4 .   ? 0.573   -4.560  25.568 1.00 31.32 ? 403 EPU A C6    1 
HETATM 2541 C C7    . EPU D 4 .   ? 5.501   -8.835  26.003 1.00 32.11 ? 403 EPU A C7    1 
HETATM 2542 C C8    . EPU D 4 .   ? 6.532   -9.755  26.655 1.00 35.24 ? 403 EPU A C8    1 
HETATM 2543 N N2    . EPU D 4 .   ? 5.023   -7.650  26.760 1.00 40.32 ? 403 EPU A N2    1 
HETATM 2544 O O1    . EPU D 4 .   ? 2.958   -7.232  28.159 1.00 26.70 ? 403 EPU A O1    1 
HETATM 2545 O O3    . EPU D 4 .   ? 5.336   -4.840  25.716 1.00 38.96 ? 403 EPU A O3    1 
HETATM 2546 O O4    . EPU D 4 .   ? 3.143   -3.252  26.765 1.00 29.51 ? 403 EPU A O4    1 
HETATM 2547 O O5    . EPU D 4 .   ? 1.492   -6.541  26.467 1.00 40.27 ? 403 EPU A O5    1 
HETATM 2548 O O6    . EPU D 4 .   ? -0.212  -3.582  26.211 1.00 43.24 ? 403 EPU A O6    1 
HETATM 2549 O O7    . EPU D 4 .   ? 5.092   -9.062  24.906 1.00 34.16 ? 403 EPU A O7    1 
HETATM 2550 C C1E   . EPU D 4 .   ? 7.847   -4.454  25.855 1.00 39.74 ? 403 EPU A C1E   1 
HETATM 2551 O O1E   . EPU D 4 .   ? 7.986   -5.111  24.782 1.00 35.69 ? 403 EPU A O1E   1 
HETATM 2552 O O2E   . EPU D 4 .   ? 8.857   -3.995  26.453 1.00 40.96 ? 403 EPU A O2E   1 
HETATM 2553 C C2E   . EPU D 4 .   ? 6.441   -4.236  26.428 1.00 40.88 ? 403 EPU A C2E   1 
HETATM 2554 C C3E   . EPU D 4 .   ? 6.269   -3.498  27.542 1.00 32.54 ? 403 EPU A C3E   1 
HETATM 2555 O O     . HOH E 5 .   ? 5.551   -7.555  29.779 1.00 35.02 ? 501 HOH A O     1 
HETATM 2556 O O     . HOH E 5 .   ? -2.418  -5.827  37.297 1.00 32.87 ? 502 HOH A O     1 
HETATM 2557 O O     . HOH E 5 .   ? 20.795  5.019   38.922 1.00 34.99 ? 503 HOH A O     1 
HETATM 2558 O O     . HOH E 5 .   ? -0.540  -6.381  14.868 1.00 38.14 ? 504 HOH A O     1 
HETATM 2559 O O     . HOH E 5 .   ? 24.317  -21.397 30.612 1.00 29.44 ? 505 HOH A O     1 
HETATM 2560 O O     . HOH E 5 .   ? 9.346   -24.609 41.325 1.00 44.57 ? 506 HOH A O     1 
HETATM 2561 O O     . HOH E 5 .   ? 0.584   -11.453 29.097 1.00 31.31 ? 507 HOH A O     1 
HETATM 2562 O O     . HOH E 5 .   ? 1.171   11.002  22.212 1.00 30.41 ? 508 HOH A O     1 
HETATM 2563 O O     . HOH E 5 .   ? 17.671  -4.068  19.503 1.00 42.63 ? 509 HOH A O     1 
HETATM 2564 O O     . HOH E 5 .   ? -0.741  -2.187  38.944 0.50 16.92 ? 510 HOH A O     1 
HETATM 2565 O O     . HOH E 5 .   ? 19.691  0.933   43.650 1.00 41.39 ? 511 HOH A O     1 
HETATM 2566 O O     . HOH E 5 .   ? 0.872   -5.335  35.830 1.00 27.79 ? 512 HOH A O     1 
HETATM 2567 O O     . HOH E 5 .   ? 23.552  15.725  23.126 1.00 43.23 ? 513 HOH A O     1 
HETATM 2568 O O     . HOH E 5 .   ? 4.835   4.479   28.938 1.00 28.33 ? 514 HOH A O     1 
HETATM 2569 O O     . HOH E 5 .   ? 26.497  0.351   35.316 1.00 34.65 ? 515 HOH A O     1 
HETATM 2570 O O     . HOH E 5 .   ? 17.170  -4.618  44.304 1.00 32.71 ? 516 HOH A O     1 
HETATM 2571 O O     . HOH E 5 .   ? 34.885  -11.259 33.156 1.00 65.82 ? 517 HOH A O     1 
HETATM 2572 O O     . HOH E 5 .   ? -0.901  0.903   26.980 1.00 29.78 ? 518 HOH A O     1 
HETATM 2573 O O     . HOH E 5 .   ? 6.272   -6.809  17.410 1.00 40.05 ? 519 HOH A O     1 
HETATM 2574 O O     . HOH E 5 .   ? 4.656   -6.210  7.417  1.00 42.75 ? 520 HOH A O     1 
HETATM 2575 O O     . HOH E 5 .   ? 4.798   -9.254  13.044 1.00 42.71 ? 521 HOH A O     1 
HETATM 2576 O O     . HOH E 5 .   ? 21.256  12.482  20.226 1.00 42.93 ? 522 HOH A O     1 
HETATM 2577 O O     . HOH E 5 .   ? 30.907  -6.641  34.539 1.00 21.13 ? 523 HOH A O     1 
HETATM 2578 O O     . HOH E 5 .   ? 13.615  3.446   38.868 1.00 21.33 ? 524 HOH A O     1 
HETATM 2579 O O     . HOH E 5 .   ? 1.916   -15.853 25.307 1.00 37.30 ? 525 HOH A O     1 
HETATM 2580 O O     . HOH E 5 .   ? 10.058  -16.258 26.573 1.00 25.00 ? 526 HOH A O     1 
HETATM 2581 O O     . HOH E 5 .   ? 17.391  6.712   28.282 1.00 56.55 ? 527 HOH A O     1 
HETATM 2582 O O     . HOH E 5 .   ? 17.572  0.751   29.004 1.00 44.16 ? 528 HOH A O     1 
HETATM 2583 O O     . HOH E 5 .   ? 10.208  2.485   19.906 1.00 30.84 ? 529 HOH A O     1 
HETATM 2584 O O     . HOH E 5 .   ? 13.719  -19.578 31.801 1.00 21.60 ? 530 HOH A O     1 
HETATM 2585 O O     . HOH E 5 .   ? 38.040  0.626   19.656 1.00 52.74 ? 531 HOH A O     1 
HETATM 2586 O O     . HOH E 5 .   ? 14.535  -7.986  17.179 1.00 40.35 ? 532 HOH A O     1 
HETATM 2587 O O     . HOH E 5 .   ? 14.866  -13.305 22.276 1.00 40.17 ? 533 HOH A O     1 
HETATM 2588 O O     . HOH E 5 .   ? 6.680   -14.319 43.027 1.00 48.19 ? 534 HOH A O     1 
HETATM 2589 O O     . HOH E 5 .   ? 8.310   7.902   22.678 1.00 32.12 ? 535 HOH A O     1 
HETATM 2590 O O     . HOH E 5 .   ? 12.937  -4.538  32.582 1.00 25.36 ? 536 HOH A O     1 
HETATM 2591 O O     . HOH E 5 .   ? 29.646  -13.695 37.857 1.00 39.28 ? 537 HOH A O     1 
HETATM 2592 O O     . HOH E 5 .   ? 8.918   -3.422  43.000 1.00 28.37 ? 538 HOH A O     1 
HETATM 2593 O O     . HOH E 5 .   ? 25.440  -8.582  40.706 1.00 26.99 ? 539 HOH A O     1 
HETATM 2594 O O     . HOH E 5 .   ? 22.785  2.838   38.450 1.00 28.19 ? 540 HOH A O     1 
HETATM 2595 O O     . HOH E 5 .   ? 24.902  -13.944 30.150 1.00 29.61 ? 541 HOH A O     1 
HETATM 2596 O O     . HOH E 5 .   ? 14.833  -6.973  15.065 1.00 47.38 ? 542 HOH A O     1 
HETATM 2597 O O     . HOH E 5 .   ? -6.798  1.185   29.824 1.00 36.02 ? 543 HOH A O     1 
HETATM 2598 O O     . HOH E 5 .   ? 34.133  -0.083  36.745 1.00 27.19 ? 544 HOH A O     1 
HETATM 2599 O O     . HOH E 5 .   ? 10.706  -13.199 16.362 1.00 40.82 ? 545 HOH A O     1 
HETATM 2600 O O     . HOH E 5 .   ? 23.418  -12.574 26.711 1.00 41.88 ? 546 HOH A O     1 
HETATM 2601 O O     . HOH E 5 .   ? 29.875  -2.592  14.116 1.00 37.91 ? 547 HOH A O     1 
HETATM 2602 O O     . HOH E 5 .   ? 45.593  2.915   22.066 1.00 49.11 ? 548 HOH A O     1 
HETATM 2603 O O     . HOH E 5 .   ? 31.391  -2.636  20.317 1.00 52.68 ? 549 HOH A O     1 
HETATM 2604 O O     . HOH E 5 .   ? 17.316  6.589   16.179 1.00 37.36 ? 550 HOH A O     1 
HETATM 2605 O O     . HOH E 5 .   ? -2.550  -6.794  27.810 1.00 24.55 ? 551 HOH A O     1 
HETATM 2606 O O     . HOH E 5 .   ? 17.982  12.171  20.278 1.00 33.12 ? 552 HOH A O     1 
HETATM 2607 O O     . HOH E 5 .   ? 18.971  8.456   17.851 1.00 59.17 ? 553 HOH A O     1 
HETATM 2608 O O     . HOH E 5 .   ? 10.352  -15.678 47.068 1.00 37.76 ? 554 HOH A O     1 
HETATM 2609 O O     . HOH E 5 .   ? -2.644  -11.630 32.403 1.00 37.47 ? 555 HOH A O     1 
HETATM 2610 O O     . HOH E 5 .   ? 0.928   1.879   24.314 1.00 33.40 ? 556 HOH A O     1 
HETATM 2611 O O     . HOH E 5 .   ? 23.358  -21.599 25.237 1.00 25.46 ? 557 HOH A O     1 
HETATM 2612 O O     . HOH E 5 .   ? 17.279  8.463   27.089 1.00 37.00 ? 558 HOH A O     1 
HETATM 2613 O O     . HOH E 5 .   ? 13.855  7.643   34.532 1.00 26.72 ? 559 HOH A O     1 
HETATM 2614 O O     . HOH E 5 .   ? -2.949  -3.105  10.082 1.00 45.11 ? 560 HOH A O     1 
HETATM 2615 O O     . HOH E 5 .   ? -6.090  -0.795  20.740 1.00 40.33 ? 561 HOH A O     1 
HETATM 2616 O O     . HOH E 5 .   ? 26.523  -13.400 38.149 1.00 29.44 ? 562 HOH A O     1 
HETATM 2617 O O     . HOH E 5 .   ? 12.023  -21.048 41.560 1.00 37.36 ? 563 HOH A O     1 
HETATM 2618 O O     . HOH E 5 .   ? 1.708   6.777   28.100 1.00 31.09 ? 564 HOH A O     1 
HETATM 2619 O O     . HOH E 5 .   ? 26.404  6.215   37.771 1.00 42.82 ? 565 HOH A O     1 
HETATM 2620 O O     . HOH E 5 .   ? 15.030  5.558   18.353 1.00 53.84 ? 566 HOH A O     1 
HETATM 2621 O O     . HOH E 5 .   ? 17.414  -15.375 24.542 1.00 26.41 ? 567 HOH A O     1 
HETATM 2622 O O     . HOH E 5 .   ? 20.082  -15.706 24.925 1.00 60.44 ? 568 HOH A O     1 
HETATM 2623 O O     . HOH E 5 .   ? 0.951   -1.068  5.679  1.00 37.90 ? 569 HOH A O     1 
HETATM 2624 O O     . HOH E 5 .   ? -0.061  -6.531  21.909 1.00 25.14 ? 570 HOH A O     1 
HETATM 2625 O O     . HOH E 5 .   ? 30.405  -1.854  37.848 1.00 34.21 ? 571 HOH A O     1 
HETATM 2626 O O     . HOH E 5 .   ? -4.398  -3.015  26.020 1.00 29.31 ? 572 HOH A O     1 
HETATM 2627 O O     . HOH E 5 .   ? 10.848  -22.154 26.082 1.00 28.96 ? 573 HOH A O     1 
HETATM 2628 O O     . HOH E 5 .   ? 2.984   -6.459  22.432 1.00 35.03 ? 574 HOH A O     1 
HETATM 2629 O O     . HOH E 5 .   ? 13.181  8.581   1.707  1.00 37.61 ? 575 HOH A O     1 
HETATM 2630 O O     . HOH E 5 .   ? 19.366  -12.217 22.308 1.00 38.27 ? 576 HOH A O     1 
HETATM 2631 O O     . HOH E 5 .   ? -4.500  -1.749  12.874 1.00 41.10 ? 577 HOH A O     1 
HETATM 2632 O O     . HOH E 5 .   ? 32.668  0.807   37.887 1.00 33.87 ? 578 HOH A O     1 
HETATM 2633 O O     . HOH E 5 .   ? 29.708  4.299   33.056 1.00 43.40 ? 579 HOH A O     1 
HETATM 2634 O O     . HOH E 5 .   ? 13.152  6.799   36.421 1.00 34.65 ? 580 HOH A O     1 
HETATM 2635 O O     . HOH E 5 .   ? 2.096   -7.485  6.861  1.00 50.97 ? 581 HOH A O     1 
HETATM 2636 O O     . HOH E 5 .   ? 17.743  12.359  22.868 1.00 34.02 ? 582 HOH A O     1 
HETATM 2637 O O     . HOH E 5 .   ? 1.062   -13.177 24.968 1.00 57.57 ? 583 HOH A O     1 
HETATM 2638 O O     . HOH E 5 .   ? 11.395  -12.916 46.267 1.00 50.39 ? 584 HOH A O     1 
HETATM 2639 O O     . HOH E 5 .   ? 10.952  -22.125 23.866 1.00 34.53 ? 585 HOH A O     1 
HETATM 2640 O O     . HOH E 5 .   ? 25.890  15.729  25.316 1.00 65.82 ? 586 HOH A O     1 
HETATM 2641 O O     . HOH E 5 .   ? 11.968  2.656   43.790 1.00 49.04 ? 587 HOH A O     1 
HETATM 2642 O O     . HOH E 5 .   ? 20.610  -14.519 42.999 1.00 46.30 ? 588 HOH A O     1 
HETATM 2643 O O     . HOH E 5 .   ? 1.272   -7.847  22.747 1.00 40.67 ? 589 HOH A O     1 
HETATM 2644 O O     . HOH E 5 .   ? 19.973  -9.518  19.694 1.00 51.92 ? 590 HOH A O     1 
HETATM 2645 O O     . HOH E 5 .   ? 7.929   -20.189 22.856 1.00 28.23 ? 591 HOH A O     1 
HETATM 2646 O O     . HOH E 5 .   ? 25.394  -9.886  42.221 1.00 24.19 ? 592 HOH A O     1 
HETATM 2647 O O     . HOH E 5 .   ? -2.518  18.900  1.570  1.00 52.13 ? 593 HOH A O     1 
HETATM 2648 O O     . HOH E 5 .   ? 25.025  -15.822 40.717 1.00 28.20 ? 594 HOH A O     1 
# 
