data_9DFU
# 
_entry.id   9DFU 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9DFU         pdb_00009dfu 10.2210/pdb9dfu/pdb 
WWPDB D_1000287993 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-02-19 ? 
2 'Structure model' 1 1 2025-05-28 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.country'                 
2 2 'Structure model' '_citation.journal_abbrev'          
3 2 'Structure model' '_citation.journal_id_ASTM'         
4 2 'Structure model' '_citation.journal_id_CSD'          
5 2 'Structure model' '_citation.journal_id_ISSN'         
6 2 'Structure model' '_citation.pdbx_database_id_DOI'    
7 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
8 2 'Structure model' '_citation.title'                   
9 2 'Structure model' '_citation.year'                    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DFU 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-30 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        'same citation' 
_pdbx_database_related.db_id          9DFN 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              tyler.grove@einsteinmed.edu 
_pdbx_contact_author.name_first         Tyler 
_pdbx_contact_author.name_last          Grove 
_pdbx_contact_author.name_mi            L 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4763-0646 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lachowicz, J.C.' 1 ? 
'Bonanno, J.B.'   2 ? 
'Grove, T.L.'     3 ? 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Structure 
_citation.journal_id_ASTM           STRUE6 
_citation.journal_id_CSD            2005 
_citation.journal_id_ISSN           0969-2126 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Structural insights from active site variants and beta-8 loop interactions in viperin-like enzymes.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.str.2025.04.009 
_citation.pdbx_database_id_PubMed   40373765 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Lachowicz, J.C.' 1 ? 
primary 'Grudman, S.'     2 ? 
primary 'Bonanno, J.B.'   3 ? 
primary 'Fiser, A.'       4 ? 
primary 'Grove, T.L.'     5 ? 
# 
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 'Radical SAM core domain-containing protein' 37369.562 1  ? F40H ? ? 
2 non-polymer syn "CYTIDINE-5'-TRIPHOSPHATE"                   483.156   1  ? ?    ? ? 
3 non-polymer nat 'IRON/SULFUR CLUSTER'                        351.640   1  ? ?    ? ? 
4 non-polymer syn S-ADENOSYLMETHIONINE                         398.437   1  ? ?    ? ? 
5 non-polymer syn 'CHLORIDE ION'                               35.453    1  ? ?    ? ? 
6 water       nat water                                        18.015    91 ? ?    ? ? 
# 
_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       
;MHHHHHHSSGVDLGTENLYFQSMGQIPVSVNYHFTRKCNKSCGFCFHTAKTSHMEDISRAKRGLQLLQRAGMKKINFAGG
EPFLYPKFLGELVDFCKEDLHLESVSIITNGSLVREEWVRKHAKNIDILACSCDSFDENMNIEIGRGTGNQVEILYRIAK
WCRKNEIKFKLNTVVTRLNYEEDMNEHIDTLQPFRWKVFQVLIVEGENDSEKTLRDARRFTISDKQFEVFCSKHRHHKSF
VAEPNRLMASSYLLVDEYMRFIDKDGNKLTKSILDVGVEAAMKEIKWDVDAFQERGGVYEWTKENEQVEACSTGMSEKLV
W
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MHHHHHHSSGVDLGTENLYFQSMGQIPVSVNYHFTRKCNKSCGFCFHTAKTSHMEDISRAKRGLQLLQRAGMKKINFAGG
EPFLYPKFLGELVDFCKEDLHLESVSIITNGSLVREEWVRKHAKNIDILACSCDSFDENMNIEIGRGTGNQVEILYRIAK
WCRKNEIKFKLNTVVTRLNYEEDMNEHIDTLQPFRWKVFQVLIVEGENDSEKTLRDARRFTISDKQFEVFCSKHRHHKSF
VAEPNRLMASSYLLVDEYMRFIDKDGNKLTKSILDVGVEAAMKEIKWDVDAFQERGGVYEWTKENEQVEACSTGMSEKLV
W
;
_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 "CYTIDINE-5'-TRIPHOSPHATE" CTP 
3 'IRON/SULFUR CLUSTER'      SF4 
4 S-ADENOSYLMETHIONINE       SAM 
5 'CHLORIDE ION'             CL  
6 water                      HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   HIS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   SER n 
1 9   SER n 
1 10  GLY n 
1 11  VAL n 
1 12  ASP n 
1 13  LEU n 
1 14  GLY n 
1 15  THR n 
1 16  GLU n 
1 17  ASN n 
1 18  LEU n 
1 19  TYR n 
1 20  PHE n 
1 21  GLN n 
1 22  SER n 
1 23  MET n 
1 24  GLY n 
1 25  GLN n 
1 26  ILE n 
1 27  PRO n 
1 28  VAL n 
1 29  SER n 
1 30  VAL n 
1 31  ASN n 
1 32  TYR n 
1 33  HIS n 
1 34  PHE n 
1 35  THR n 
1 36  ARG n 
1 37  LYS n 
1 38  CYS n 
1 39  ASN n 
1 40  LYS n 
1 41  SER n 
1 42  CYS n 
1 43  GLY n 
1 44  PHE n 
1 45  CYS n 
1 46  PHE n 
1 47  HIS n 
1 48  THR n 
1 49  ALA n 
1 50  LYS n 
1 51  THR n 
1 52  SER n 
1 53  HIS n 
1 54  MET n 
1 55  GLU n 
1 56  ASP n 
1 57  ILE n 
1 58  SER n 
1 59  ARG n 
1 60  ALA n 
1 61  LYS n 
1 62  ARG n 
1 63  GLY n 
1 64  LEU n 
1 65  GLN n 
1 66  LEU n 
1 67  LEU n 
1 68  GLN n 
1 69  ARG n 
1 70  ALA n 
1 71  GLY n 
1 72  MET n 
1 73  LYS n 
1 74  LYS n 
1 75  ILE n 
1 76  ASN n 
1 77  PHE n 
1 78  ALA n 
1 79  GLY n 
1 80  GLY n 
1 81  GLU n 
1 82  PRO n 
1 83  PHE n 
1 84  LEU n 
1 85  TYR n 
1 86  PRO n 
1 87  LYS n 
1 88  PHE n 
1 89  LEU n 
1 90  GLY n 
1 91  GLU n 
1 92  LEU n 
1 93  VAL n 
1 94  ASP n 
1 95  PHE n 
1 96  CYS n 
1 97  LYS n 
1 98  GLU n 
1 99  ASP n 
1 100 LEU n 
1 101 HIS n 
1 102 LEU n 
1 103 GLU n 
1 104 SER n 
1 105 VAL n 
1 106 SER n 
1 107 ILE n 
1 108 ILE n 
1 109 THR n 
1 110 ASN n 
1 111 GLY n 
1 112 SER n 
1 113 LEU n 
1 114 VAL n 
1 115 ARG n 
1 116 GLU n 
1 117 GLU n 
1 118 TRP n 
1 119 VAL n 
1 120 ARG n 
1 121 LYS n 
1 122 HIS n 
1 123 ALA n 
1 124 LYS n 
1 125 ASN n 
1 126 ILE n 
1 127 ASP n 
1 128 ILE n 
1 129 LEU n 
1 130 ALA n 
1 131 CYS n 
1 132 SER n 
1 133 CYS n 
1 134 ASP n 
1 135 SER n 
1 136 PHE n 
1 137 ASP n 
1 138 GLU n 
1 139 ASN n 
1 140 MET n 
1 141 ASN n 
1 142 ILE n 
1 143 GLU n 
1 144 ILE n 
1 145 GLY n 
1 146 ARG n 
1 147 GLY n 
1 148 THR n 
1 149 GLY n 
1 150 ASN n 
1 151 GLN n 
1 152 VAL n 
1 153 GLU n 
1 154 ILE n 
1 155 LEU n 
1 156 TYR n 
1 157 ARG n 
1 158 ILE n 
1 159 ALA n 
1 160 LYS n 
1 161 TRP n 
1 162 CYS n 
1 163 ARG n 
1 164 LYS n 
1 165 ASN n 
1 166 GLU n 
1 167 ILE n 
1 168 LYS n 
1 169 PHE n 
1 170 LYS n 
1 171 LEU n 
1 172 ASN n 
1 173 THR n 
1 174 VAL n 
1 175 VAL n 
1 176 THR n 
1 177 ARG n 
1 178 LEU n 
1 179 ASN n 
1 180 TYR n 
1 181 GLU n 
1 182 GLU n 
1 183 ASP n 
1 184 MET n 
1 185 ASN n 
1 186 GLU n 
1 187 HIS n 
1 188 ILE n 
1 189 ASP n 
1 190 THR n 
1 191 LEU n 
1 192 GLN n 
1 193 PRO n 
1 194 PHE n 
1 195 ARG n 
1 196 TRP n 
1 197 LYS n 
1 198 VAL n 
1 199 PHE n 
1 200 GLN n 
1 201 VAL n 
1 202 LEU n 
1 203 ILE n 
1 204 VAL n 
1 205 GLU n 
1 206 GLY n 
1 207 GLU n 
1 208 ASN n 
1 209 ASP n 
1 210 SER n 
1 211 GLU n 
1 212 LYS n 
1 213 THR n 
1 214 LEU n 
1 215 ARG n 
1 216 ASP n 
1 217 ALA n 
1 218 ARG n 
1 219 ARG n 
1 220 PHE n 
1 221 THR n 
1 222 ILE n 
1 223 SER n 
1 224 ASP n 
1 225 LYS n 
1 226 GLN n 
1 227 PHE n 
1 228 GLU n 
1 229 VAL n 
1 230 PHE n 
1 231 CYS n 
1 232 SER n 
1 233 LYS n 
1 234 HIS n 
1 235 ARG n 
1 236 HIS n 
1 237 HIS n 
1 238 LYS n 
1 239 SER n 
1 240 PHE n 
1 241 VAL n 
1 242 ALA n 
1 243 GLU n 
1 244 PRO n 
1 245 ASN n 
1 246 ARG n 
1 247 LEU n 
1 248 MET n 
1 249 ALA n 
1 250 SER n 
1 251 SER n 
1 252 TYR n 
1 253 LEU n 
1 254 LEU n 
1 255 VAL n 
1 256 ASP n 
1 257 GLU n 
1 258 TYR n 
1 259 MET n 
1 260 ARG n 
1 261 PHE n 
1 262 ILE n 
1 263 ASP n 
1 264 LYS n 
1 265 ASP n 
1 266 GLY n 
1 267 ASN n 
1 268 LYS n 
1 269 LEU n 
1 270 THR n 
1 271 LYS n 
1 272 SER n 
1 273 ILE n 
1 274 LEU n 
1 275 ASP n 
1 276 VAL n 
1 277 GLY n 
1 278 VAL n 
1 279 GLU n 
1 280 ALA n 
1 281 ALA n 
1 282 MET n 
1 283 LYS n 
1 284 GLU n 
1 285 ILE n 
1 286 LYS n 
1 287 TRP n 
1 288 ASP n 
1 289 VAL n 
1 290 ASP n 
1 291 ALA n 
1 292 PHE n 
1 293 GLN n 
1 294 GLU n 
1 295 ARG n 
1 296 GLY n 
1 297 GLY n 
1 298 VAL n 
1 299 TYR n 
1 300 GLU n 
1 301 TRP n 
1 302 THR n 
1 303 LYS n 
1 304 GLU n 
1 305 ASN n 
1 306 GLU n 
1 307 GLN n 
1 308 VAL n 
1 309 GLU n 
1 310 ALA n 
1 311 CYS n 
1 312 SER n 
1 313 THR n 
1 314 GLY n 
1 315 MET n 
1 316 SER n 
1 317 GLU n 
1 318 LYS n 
1 319 LEU n 
1 320 VAL n 
1 321 TRP 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                   321 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 TRIVIDRAFT_46896 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    Gv29-8 
_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      'Trichoderma virens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     413071 
_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 
CL  non-polymer         . 'CHLORIDE ION'             ? 'Cl -1'            35.453  
CTP non-polymer         . "CYTIDINE-5'-TRIPHOSPHATE" ? 'C9 H16 N3 O14 P3' 483.156 
CYS 'L-peptide linking' y CYSTEINE                   ? 'C3 H7 N O2 S'     121.158 
GLN 'L-peptide linking' y GLUTAMINE                  ? 'C5 H10 N2 O3'     146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'            ? 'C5 H9 N O4'       147.129 
GLY 'peptide linking'   y GLYCINE                    ? 'C2 H5 N O2'       75.067  
HIS 'L-peptide linking' y HISTIDINE                  ? 'C6 H10 N3 O2 1'   156.162 
HOH non-polymer         . WATER                      ? 'H2 O'             18.015  
ILE 'L-peptide linking' y ISOLEUCINE                 ? 'C6 H13 N O2'      131.173 
LEU 'L-peptide linking' y LEUCINE                    ? 'C6 H13 N O2'      131.173 
LYS 'L-peptide linking' y LYSINE                     ? 'C6 H15 N2 O2 1'   147.195 
MET 'L-peptide linking' y METHIONINE                 ? 'C5 H11 N O2 S'    149.211 
PHE 'L-peptide linking' y PHENYLALANINE              ? 'C9 H11 N O2'      165.189 
PRO 'L-peptide linking' y PROLINE                    ? 'C5 H9 N O2'       115.130 
SAM non-polymer         . S-ADENOSYLMETHIONINE       ? 'C15 H22 N6 O5 S'  398.437 
SER 'L-peptide linking' y SERINE                     ? 'C3 H7 N O3'       105.093 
SF4 non-polymer         . 'IRON/SULFUR CLUSTER'      ? 'Fe4 S4'           351.640 
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   8   ?   ?   ?   A . n 
A 1 2   HIS 2   9   ?   ?   ?   A . n 
A 1 3   HIS 3   10  ?   ?   ?   A . n 
A 1 4   HIS 4   11  ?   ?   ?   A . n 
A 1 5   HIS 5   12  ?   ?   ?   A . n 
A 1 6   HIS 6   13  ?   ?   ?   A . n 
A 1 7   HIS 7   14  ?   ?   ?   A . n 
A 1 8   SER 8   15  ?   ?   ?   A . n 
A 1 9   SER 9   16  ?   ?   ?   A . n 
A 1 10  GLY 10  17  ?   ?   ?   A . n 
A 1 11  VAL 11  18  ?   ?   ?   A . n 
A 1 12  ASP 12  19  ?   ?   ?   A . n 
A 1 13  LEU 13  20  ?   ?   ?   A . n 
A 1 14  GLY 14  21  ?   ?   ?   A . n 
A 1 15  THR 15  22  ?   ?   ?   A . n 
A 1 16  GLU 16  23  ?   ?   ?   A . n 
A 1 17  ASN 17  24  ?   ?   ?   A . n 
A 1 18  LEU 18  25  ?   ?   ?   A . n 
A 1 19  TYR 19  26  ?   ?   ?   A . n 
A 1 20  PHE 20  27  ?   ?   ?   A . n 
A 1 21  GLN 21  28  ?   ?   ?   A . n 
A 1 22  SER 22  29  ?   ?   ?   A . n 
A 1 23  MET 23  30  ?   ?   ?   A . n 
A 1 24  GLY 24  31  ?   ?   ?   A . n 
A 1 25  GLN 25  32  32  GLN GLN A . n 
A 1 26  ILE 26  33  33  ILE ILE A . n 
A 1 27  PRO 27  34  34  PRO PRO A . n 
A 1 28  VAL 28  35  35  VAL VAL A . n 
A 1 29  SER 29  36  36  SER SER A . n 
A 1 30  VAL 30  37  37  VAL VAL A . n 
A 1 31  ASN 31  38  38  ASN ASN A . n 
A 1 32  TYR 32  39  39  TYR TYR A . n 
A 1 33  HIS 33  40  40  HIS HIS A . n 
A 1 34  PHE 34  41  41  PHE PHE A . n 
A 1 35  THR 35  42  42  THR THR A . n 
A 1 36  ARG 36  43  43  ARG ARG A . n 
A 1 37  LYS 37  44  44  LYS LYS A . n 
A 1 38  CYS 38  45  45  CYS CYS A . n 
A 1 39  ASN 39  46  46  ASN ASN A . n 
A 1 40  LYS 40  47  47  LYS LYS A . n 
A 1 41  SER 41  48  48  SER SER A . n 
A 1 42  CYS 42  49  49  CYS CYS A . n 
A 1 43  GLY 43  50  50  GLY GLY A . n 
A 1 44  PHE 44  51  51  PHE PHE A . n 
A 1 45  CYS 45  52  52  CYS CYS A . n 
A 1 46  PHE 46  53  53  PHE PHE A . n 
A 1 47  HIS 47  54  54  HIS HIS A . n 
A 1 48  THR 48  55  55  THR THR A . n 
A 1 49  ALA 49  56  56  ALA ALA A . n 
A 1 50  LYS 50  57  57  LYS LYS A . n 
A 1 51  THR 51  58  58  THR THR A . n 
A 1 52  SER 52  59  59  SER SER A . n 
A 1 53  HIS 53  60  60  HIS HIS A . n 
A 1 54  MET 54  61  61  MET MET A . n 
A 1 55  GLU 55  62  62  GLU GLU A . n 
A 1 56  ASP 56  63  63  ASP ASP A . n 
A 1 57  ILE 57  64  64  ILE ILE A . n 
A 1 58  SER 58  65  65  SER SER A . n 
A 1 59  ARG 59  66  66  ARG ARG A . n 
A 1 60  ALA 60  67  67  ALA ALA A . n 
A 1 61  LYS 61  68  68  LYS LYS A . n 
A 1 62  ARG 62  69  69  ARG ARG A . n 
A 1 63  GLY 63  70  70  GLY GLY A . n 
A 1 64  LEU 64  71  71  LEU LEU A . n 
A 1 65  GLN 65  72  72  GLN GLN A . n 
A 1 66  LEU 66  73  73  LEU LEU A . n 
A 1 67  LEU 67  74  74  LEU LEU A . n 
A 1 68  GLN 68  75  75  GLN GLN A . n 
A 1 69  ARG 69  76  76  ARG ARG A . n 
A 1 70  ALA 70  77  77  ALA ALA A . n 
A 1 71  GLY 71  78  78  GLY GLY A . n 
A 1 72  MET 72  79  79  MET MET A . n 
A 1 73  LYS 73  80  80  LYS LYS A . n 
A 1 74  LYS 74  81  81  LYS LYS A . n 
A 1 75  ILE 75  82  82  ILE ILE A . n 
A 1 76  ASN 76  83  83  ASN ASN A . n 
A 1 77  PHE 77  84  84  PHE PHE A . n 
A 1 78  ALA 78  85  85  ALA ALA A . n 
A 1 79  GLY 79  86  86  GLY GLY A . n 
A 1 80  GLY 80  87  87  GLY GLY A . n 
A 1 81  GLU 81  88  88  GLU GLU A . n 
A 1 82  PRO 82  89  89  PRO PRO A . n 
A 1 83  PHE 83  90  90  PHE PHE A . n 
A 1 84  LEU 84  91  91  LEU LEU A . n 
A 1 85  TYR 85  92  92  TYR TYR A . n 
A 1 86  PRO 86  93  93  PRO PRO A . n 
A 1 87  LYS 87  94  94  LYS LYS A . n 
A 1 88  PHE 88  95  95  PHE PHE A . n 
A 1 89  LEU 89  96  96  LEU LEU A . n 
A 1 90  GLY 90  97  97  GLY GLY A . n 
A 1 91  GLU 91  98  98  GLU GLU A . n 
A 1 92  LEU 92  99  99  LEU LEU A . n 
A 1 93  VAL 93  100 100 VAL VAL A . n 
A 1 94  ASP 94  101 101 ASP ASP A . n 
A 1 95  PHE 95  102 102 PHE PHE A . n 
A 1 96  CYS 96  103 103 CYS CYS A . n 
A 1 97  LYS 97  104 104 LYS LYS A . n 
A 1 98  GLU 98  105 105 GLU GLU A . n 
A 1 99  ASP 99  106 106 ASP ASP A . n 
A 1 100 LEU 100 107 107 LEU LEU A . n 
A 1 101 HIS 101 108 108 HIS HIS A . n 
A 1 102 LEU 102 109 109 LEU LEU A . n 
A 1 103 GLU 103 110 110 GLU GLU A . n 
A 1 104 SER 104 111 111 SER SER A . n 
A 1 105 VAL 105 112 112 VAL VAL A . n 
A 1 106 SER 106 113 113 SER SER A . n 
A 1 107 ILE 107 114 114 ILE ILE A . n 
A 1 108 ILE 108 115 115 ILE ILE A . n 
A 1 109 THR 109 116 116 THR THR A . n 
A 1 110 ASN 110 117 117 ASN ASN A . n 
A 1 111 GLY 111 118 118 GLY GLY A . n 
A 1 112 SER 112 119 119 SER SER A . n 
A 1 113 LEU 113 120 120 LEU LEU A . n 
A 1 114 VAL 114 121 121 VAL VAL A . n 
A 1 115 ARG 115 122 122 ARG ARG A . n 
A 1 116 GLU 116 123 123 GLU GLU A . n 
A 1 117 GLU 117 124 124 GLU GLU A . n 
A 1 118 TRP 118 125 125 TRP TRP A . n 
A 1 119 VAL 119 126 126 VAL VAL A . n 
A 1 120 ARG 120 127 127 ARG ARG A . n 
A 1 121 LYS 121 128 128 LYS LYS A . n 
A 1 122 HIS 122 129 129 HIS HIS A . n 
A 1 123 ALA 123 130 130 ALA ALA A . n 
A 1 124 LYS 124 131 131 LYS LYS A . n 
A 1 125 ASN 125 132 132 ASN ASN A . n 
A 1 126 ILE 126 133 133 ILE ILE A . n 
A 1 127 ASP 127 134 134 ASP ASP A . n 
A 1 128 ILE 128 135 135 ILE ILE A . n 
A 1 129 LEU 129 136 136 LEU LEU A . n 
A 1 130 ALA 130 137 137 ALA ALA A . n 
A 1 131 CYS 131 138 138 CYS CYS A . n 
A 1 132 SER 132 139 139 SER SER A . n 
A 1 133 CYS 133 140 140 CYS CYS A . n 
A 1 134 ASP 134 141 141 ASP ASP A . n 
A 1 135 SER 135 142 142 SER SER A . n 
A 1 136 PHE 136 143 143 PHE PHE A . n 
A 1 137 ASP 137 144 144 ASP ASP A . n 
A 1 138 GLU 138 145 145 GLU GLU A . n 
A 1 139 ASN 139 146 146 ASN ASN A . n 
A 1 140 MET 140 147 147 MET MET A . n 
A 1 141 ASN 141 148 148 ASN ASN A . n 
A 1 142 ILE 142 149 149 ILE ILE A . n 
A 1 143 GLU 143 150 150 GLU GLU A . n 
A 1 144 ILE 144 151 151 ILE ILE A . n 
A 1 145 GLY 145 152 152 GLY GLY A . n 
A 1 146 ARG 146 153 153 ARG ARG A . n 
A 1 147 GLY 147 154 154 GLY GLY A . n 
A 1 148 THR 148 155 155 THR THR A . n 
A 1 149 GLY 149 156 156 GLY GLY A . n 
A 1 150 ASN 150 157 157 ASN ASN A . n 
A 1 151 GLN 151 158 158 GLN GLN A . n 
A 1 152 VAL 152 159 159 VAL VAL A . n 
A 1 153 GLU 153 160 160 GLU GLU A . n 
A 1 154 ILE 154 161 161 ILE ILE A . n 
A 1 155 LEU 155 162 162 LEU LEU A . n 
A 1 156 TYR 156 163 163 TYR TYR A . n 
A 1 157 ARG 157 164 164 ARG ARG A . n 
A 1 158 ILE 158 165 165 ILE ILE A . n 
A 1 159 ALA 159 166 166 ALA ALA A . n 
A 1 160 LYS 160 167 167 LYS LYS A . n 
A 1 161 TRP 161 168 168 TRP TRP A . n 
A 1 162 CYS 162 169 169 CYS CYS A . n 
A 1 163 ARG 163 170 170 ARG ARG A . n 
A 1 164 LYS 164 171 171 LYS LYS A . n 
A 1 165 ASN 165 172 172 ASN ASN A . n 
A 1 166 GLU 166 173 173 GLU GLU A . n 
A 1 167 ILE 167 174 174 ILE ILE A . n 
A 1 168 LYS 168 175 175 LYS LYS A . n 
A 1 169 PHE 169 176 176 PHE PHE A . n 
A 1 170 LYS 170 177 177 LYS LYS A . n 
A 1 171 LEU 171 178 178 LEU LEU A . n 
A 1 172 ASN 172 179 179 ASN ASN A . n 
A 1 173 THR 173 180 180 THR THR A . n 
A 1 174 VAL 174 181 181 VAL VAL A . n 
A 1 175 VAL 175 182 182 VAL VAL A . n 
A 1 176 THR 176 183 183 THR THR A . n 
A 1 177 ARG 177 184 184 ARG ARG A . n 
A 1 178 LEU 178 185 185 LEU LEU A . n 
A 1 179 ASN 179 186 186 ASN ASN A . n 
A 1 180 TYR 180 187 187 TYR TYR A . n 
A 1 181 GLU 181 188 188 GLU GLU A . n 
A 1 182 GLU 182 189 189 GLU GLU A . n 
A 1 183 ASP 183 190 190 ASP ASP A . n 
A 1 184 MET 184 191 191 MET MET A . n 
A 1 185 ASN 185 192 192 ASN ASN A . n 
A 1 186 GLU 186 193 193 GLU GLU A . n 
A 1 187 HIS 187 194 194 HIS HIS A . n 
A 1 188 ILE 188 195 195 ILE ILE A . n 
A 1 189 ASP 189 196 196 ASP ASP A . n 
A 1 190 THR 190 197 197 THR THR A . n 
A 1 191 LEU 191 198 198 LEU LEU A . n 
A 1 192 GLN 192 199 199 GLN GLN A . n 
A 1 193 PRO 193 200 200 PRO PRO A . n 
A 1 194 PHE 194 201 201 PHE PHE A . n 
A 1 195 ARG 195 202 202 ARG ARG A . n 
A 1 196 TRP 196 203 203 TRP TRP A . n 
A 1 197 LYS 197 204 204 LYS LYS A . n 
A 1 198 VAL 198 205 205 VAL VAL A . n 
A 1 199 PHE 199 206 206 PHE PHE A . n 
A 1 200 GLN 200 207 207 GLN GLN A . n 
A 1 201 VAL 201 208 208 VAL VAL A . n 
A 1 202 LEU 202 209 209 LEU LEU A . n 
A 1 203 ILE 203 210 210 ILE ILE A . n 
A 1 204 VAL 204 211 211 VAL VAL A . n 
A 1 205 GLU 205 212 212 GLU GLU A . n 
A 1 206 GLY 206 213 213 GLY GLY A . n 
A 1 207 GLU 207 214 214 GLU GLU A . n 
A 1 208 ASN 208 215 215 ASN ASN A . n 
A 1 209 ASP 209 216 216 ASP ASP A . n 
A 1 210 SER 210 217 217 SER SER A . n 
A 1 211 GLU 211 218 218 GLU GLU A . n 
A 1 212 LYS 212 219 219 LYS LYS A . n 
A 1 213 THR 213 220 220 THR THR A . n 
A 1 214 LEU 214 221 221 LEU LEU A . n 
A 1 215 ARG 215 222 222 ARG ARG A . n 
A 1 216 ASP 216 223 223 ASP ASP A . n 
A 1 217 ALA 217 224 224 ALA ALA A . n 
A 1 218 ARG 218 225 225 ARG ARG A . n 
A 1 219 ARG 219 226 226 ARG ARG A . n 
A 1 220 PHE 220 227 227 PHE PHE A . n 
A 1 221 THR 221 228 228 THR THR A . n 
A 1 222 ILE 222 229 229 ILE ILE A . n 
A 1 223 SER 223 230 230 SER SER A . n 
A 1 224 ASP 224 231 231 ASP ASP A . n 
A 1 225 LYS 225 232 232 LYS LYS A . n 
A 1 226 GLN 226 233 233 GLN GLN A . n 
A 1 227 PHE 227 234 234 PHE PHE A . n 
A 1 228 GLU 228 235 235 GLU GLU A . n 
A 1 229 VAL 229 236 236 VAL VAL A . n 
A 1 230 PHE 230 237 237 PHE PHE A . n 
A 1 231 CYS 231 238 238 CYS CYS A . n 
A 1 232 SER 232 239 239 SER SER A . n 
A 1 233 LYS 233 240 240 LYS LYS A . n 
A 1 234 HIS 234 241 241 HIS HIS A . n 
A 1 235 ARG 235 242 242 ARG ARG A . n 
A 1 236 HIS 236 243 243 HIS HIS A . n 
A 1 237 HIS 237 244 244 HIS HIS A . n 
A 1 238 LYS 238 245 245 LYS LYS A . n 
A 1 239 SER 239 246 246 SER SER A . n 
A 1 240 PHE 240 247 247 PHE PHE A . n 
A 1 241 VAL 241 248 248 VAL VAL A . n 
A 1 242 ALA 242 249 249 ALA ALA A . n 
A 1 243 GLU 243 250 250 GLU GLU A . n 
A 1 244 PRO 244 251 251 PRO PRO A . n 
A 1 245 ASN 245 252 252 ASN ASN A . n 
A 1 246 ARG 246 253 253 ARG ARG A . n 
A 1 247 LEU 247 254 254 LEU LEU A . n 
A 1 248 MET 248 255 255 MET MET A . n 
A 1 249 ALA 249 256 256 ALA ALA A . n 
A 1 250 SER 250 257 257 SER SER A . n 
A 1 251 SER 251 258 258 SER SER A . n 
A 1 252 TYR 252 259 259 TYR TYR A . n 
A 1 253 LEU 253 260 260 LEU LEU A . n 
A 1 254 LEU 254 261 261 LEU LEU A . n 
A 1 255 VAL 255 262 262 VAL VAL A . n 
A 1 256 ASP 256 263 263 ASP ASP A . n 
A 1 257 GLU 257 264 264 GLU GLU A . n 
A 1 258 TYR 258 265 265 TYR TYR A . n 
A 1 259 MET 259 266 266 MET MET A . n 
A 1 260 ARG 260 267 267 ARG ARG A . n 
A 1 261 PHE 261 268 268 PHE PHE A . n 
A 1 262 ILE 262 269 269 ILE ILE A . n 
A 1 263 ASP 263 270 270 ASP ASP A . n 
A 1 264 LYS 264 271 271 LYS LYS A . n 
A 1 265 ASP 265 272 272 ASP ASP A . n 
A 1 266 GLY 266 273 273 GLY GLY A . n 
A 1 267 ASN 267 274 274 ASN ASN A . n 
A 1 268 LYS 268 275 275 LYS LYS A . n 
A 1 269 LEU 269 276 276 LEU LEU A . n 
A 1 270 THR 270 277 277 THR THR A . n 
A 1 271 LYS 271 278 278 LYS LYS A . n 
A 1 272 SER 272 279 279 SER SER A . n 
A 1 273 ILE 273 280 280 ILE ILE A . n 
A 1 274 LEU 274 281 281 LEU LEU A . n 
A 1 275 ASP 275 282 282 ASP ASP A . n 
A 1 276 VAL 276 283 283 VAL VAL A . n 
A 1 277 GLY 277 284 284 GLY GLY A . n 
A 1 278 VAL 278 285 285 VAL VAL A . n 
A 1 279 GLU 279 286 286 GLU GLU A . n 
A 1 280 ALA 280 287 287 ALA ALA A . n 
A 1 281 ALA 281 288 288 ALA ALA A . n 
A 1 282 MET 282 289 289 MET MET A . n 
A 1 283 LYS 283 290 290 LYS LYS A . n 
A 1 284 GLU 284 291 291 GLU GLU A . n 
A 1 285 ILE 285 292 292 ILE ILE A . n 
A 1 286 LYS 286 293 293 LYS LYS A . n 
A 1 287 TRP 287 294 294 TRP TRP A . n 
A 1 288 ASP 288 295 295 ASP ASP A . n 
A 1 289 VAL 289 296 296 VAL VAL A . n 
A 1 290 ASP 290 297 297 ASP ASP A . n 
A 1 291 ALA 291 298 298 ALA ALA A . n 
A 1 292 PHE 292 299 299 PHE PHE A . n 
A 1 293 GLN 293 300 300 GLN GLN A . n 
A 1 294 GLU 294 301 301 GLU GLU A . n 
A 1 295 ARG 295 302 302 ARG ARG A . n 
A 1 296 GLY 296 303 303 GLY GLY A . n 
A 1 297 GLY 297 304 304 GLY GLY A . n 
A 1 298 VAL 298 305 305 VAL VAL A . n 
A 1 299 TYR 299 306 306 TYR TYR A . n 
A 1 300 GLU 300 307 307 GLU GLU A . n 
A 1 301 TRP 301 308 308 TRP TRP A . n 
A 1 302 THR 302 309 309 THR THR A . n 
A 1 303 LYS 303 310 310 LYS LYS A . n 
A 1 304 GLU 304 311 311 GLU GLU A . n 
A 1 305 ASN 305 312 ?   ?   ?   A . n 
A 1 306 GLU 306 313 ?   ?   ?   A . n 
A 1 307 GLN 307 314 ?   ?   ?   A . n 
A 1 308 VAL 308 315 ?   ?   ?   A . n 
A 1 309 GLU 309 316 ?   ?   ?   A . n 
A 1 310 ALA 310 317 ?   ?   ?   A . n 
A 1 311 CYS 311 318 ?   ?   ?   A . n 
A 1 312 SER 312 319 ?   ?   ?   A . n 
A 1 313 THR 313 320 ?   ?   ?   A . n 
A 1 314 GLY 314 321 ?   ?   ?   A . n 
A 1 315 MET 315 322 ?   ?   ?   A . n 
A 1 316 SER 316 323 ?   ?   ?   A . n 
A 1 317 GLU 317 324 ?   ?   ?   A . n 
A 1 318 LYS 318 325 ?   ?   ?   A . n 
A 1 319 LEU 319 326 ?   ?   ?   A . n 
A 1 320 VAL 320 327 ?   ?   ?   A . n 
A 1 321 TRP 321 328 ?   ?   ?   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 CTP ? ? CTP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 SAM ? ? SAM ? ? 'SUBJECT OF INVESTIGATION' ? 
3 SF4 ? ? SF4 ? ? '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 CTP 1  401 401 CTP CTP A . 
C 3 SF4 1  402 402 SF4 SF4 A . 
D 4 SAM 1  403 403 SAM SAM A . 
E 5 CL  1  404 1   CL  CL  A . 
F 6 HOH 1  501 91  HOH HOH A . 
F 6 HOH 2  502 131 HOH HOH A . 
F 6 HOH 3  503 12  HOH HOH A . 
F 6 HOH 4  504 9   HOH HOH A . 
F 6 HOH 5  505 77  HOH HOH A . 
F 6 HOH 6  506 52  HOH HOH A . 
F 6 HOH 7  507 3   HOH HOH A . 
F 6 HOH 8  508 85  HOH HOH A . 
F 6 HOH 9  509 59  HOH HOH A . 
F 6 HOH 10 510 61  HOH HOH A . 
F 6 HOH 11 511 4   HOH HOH A . 
F 6 HOH 12 512 68  HOH HOH A . 
F 6 HOH 13 513 48  HOH HOH A . 
F 6 HOH 14 514 18  HOH HOH A . 
F 6 HOH 15 515 32  HOH HOH A . 
F 6 HOH 16 516 126 HOH HOH A . 
F 6 HOH 17 517 54  HOH HOH A . 
F 6 HOH 18 518 117 HOH HOH A . 
F 6 HOH 19 519 5   HOH HOH A . 
F 6 HOH 20 520 13  HOH HOH A . 
F 6 HOH 21 521 1   HOH HOH A . 
F 6 HOH 22 522 64  HOH HOH A . 
F 6 HOH 23 523 60  HOH HOH A . 
F 6 HOH 24 524 31  HOH HOH A . 
F 6 HOH 25 525 10  HOH HOH A . 
F 6 HOH 26 526 19  HOH HOH A . 
F 6 HOH 27 527 58  HOH HOH A . 
F 6 HOH 28 528 41  HOH HOH A . 
F 6 HOH 29 529 35  HOH HOH A . 
F 6 HOH 30 530 25  HOH HOH A . 
F 6 HOH 31 531 42  HOH HOH A . 
F 6 HOH 32 532 6   HOH HOH A . 
F 6 HOH 33 533 8   HOH HOH A . 
F 6 HOH 34 534 11  HOH HOH A . 
F 6 HOH 35 535 2   HOH HOH A . 
F 6 HOH 36 536 27  HOH HOH A . 
F 6 HOH 37 537 39  HOH HOH A . 
F 6 HOH 38 538 34  HOH HOH A . 
F 6 HOH 39 539 90  HOH HOH A . 
F 6 HOH 40 540 36  HOH HOH A . 
F 6 HOH 41 541 24  HOH HOH A . 
F 6 HOH 42 542 22  HOH HOH A . 
F 6 HOH 43 543 51  HOH HOH A . 
F 6 HOH 44 544 40  HOH HOH A . 
F 6 HOH 45 545 21  HOH HOH A . 
F 6 HOH 46 546 110 HOH HOH A . 
F 6 HOH 47 547 20  HOH HOH A . 
F 6 HOH 48 548 16  HOH HOH A . 
F 6 HOH 49 549 109 HOH HOH A . 
F 6 HOH 50 550 74  HOH HOH A . 
F 6 HOH 51 551 49  HOH HOH A . 
F 6 HOH 52 552 46  HOH HOH A . 
F 6 HOH 53 553 76  HOH HOH A . 
F 6 HOH 54 554 69  HOH HOH A . 
F 6 HOH 55 555 55  HOH HOH A . 
F 6 HOH 56 556 28  HOH HOH A . 
F 6 HOH 57 557 15  HOH HOH A . 
F 6 HOH 58 558 72  HOH HOH A . 
F 6 HOH 59 559 71  HOH HOH A . 
F 6 HOH 60 560 98  HOH HOH A . 
F 6 HOH 61 561 70  HOH HOH A . 
F 6 HOH 62 562 23  HOH HOH A . 
F 6 HOH 63 563 33  HOH HOH A . 
F 6 HOH 64 564 7   HOH HOH A . 
F 6 HOH 65 565 38  HOH HOH A . 
F 6 HOH 66 566 14  HOH HOH A . 
F 6 HOH 67 567 63  HOH HOH A . 
F 6 HOH 68 568 80  HOH HOH A . 
F 6 HOH 69 569 100 HOH HOH A . 
F 6 HOH 70 570 62  HOH HOH A . 
F 6 HOH 71 571 95  HOH HOH A . 
F 6 HOH 72 572 50  HOH HOH A . 
F 6 HOH 73 573 89  HOH HOH A . 
F 6 HOH 74 574 67  HOH HOH A . 
F 6 HOH 75 575 53  HOH HOH A . 
F 6 HOH 76 576 114 HOH HOH A . 
F 6 HOH 77 577 30  HOH HOH A . 
F 6 HOH 78 578 82  HOH HOH A . 
F 6 HOH 79 579 81  HOH HOH A . 
F 6 HOH 80 580 94  HOH HOH A . 
F 6 HOH 81 581 105 HOH HOH A . 
F 6 HOH 82 582 43  HOH HOH A . 
F 6 HOH 83 583 47  HOH HOH A . 
F 6 HOH 84 584 102 HOH HOH A . 
F 6 HOH 85 585 124 HOH HOH A . 
F 6 HOH 86 586 45  HOH HOH A . 
F 6 HOH 87 587 57  HOH HOH A . 
F 6 HOH 88 588 122 HOH HOH A . 
F 6 HOH 89 589 127 HOH HOH A . 
F 6 HOH 90 590 119 HOH HOH A . 
F 6 HOH 91 591 118 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A GLU 286 ? CG  ? A GLU 279 CG  
2 1 Y 1 A GLU 286 ? CD  ? A GLU 279 CD  
3 1 Y 1 A GLU 286 ? OE1 ? A GLU 279 OE1 
4 1 Y 1 A GLU 286 ? OE2 ? A GLU 279 OE2 
# 
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          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DFU 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     37.137 
_cell.length_a_esd                 ? 
_cell.length_b                     55.959 
_cell.length_b_esd                 ? 
_cell.length_c                     152.810 
_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                         9DFU 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9DFU 
_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             2.12 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.10 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M HEPES (pH 7.5), 25% (w/v) PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-12-13 
_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   0.9201 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'NSLS-II BEAMLINE 17-ID-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9201 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID-2 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9DFU 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.3 
_reflns.d_resolution_low                               33.4 
_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                                     14839 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.268 
_reflns.pdbx_Rpim_I_all                                0.154 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.979 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.217 
_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                                    2.3 
_reflns_shell.d_res_low                                     2.38 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1427 
_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                               0.976 
_reflns_shell.pdbx_Rpim_I_all                               0.553 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.57 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.799 
_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                                 9DFU 
_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                            2.30 
_refine.ls_d_res_low                             19.66 
_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                     14765 
_refine.ls_number_reflns_R_free                  751 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.57 
_refine.ls_percent_reflns_R_free                 5.09 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2278 
_refine.ls_R_factor_R_free                       0.2603 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2260 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_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       ML 
_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                 26.60 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.30 
_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                       2.30 
_refine_hist.d_res_low                        19.66 
_refine_hist.number_atoms_solvent             91 
_refine_hist.number_atoms_total               2448 
_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        2292 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         65 
_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' ? 0.013  ? 2426 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.686  ? 3279 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 18.094 ? 921  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.106  ? 350  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 412  ? 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' 2.30 2.48  . . 151 2759 100.00 . . . . 0.2795 . . . . . . . . . . . 0.3032 
'X-RAY DIFFRACTION' 2.48 2.73  . . 134 2742 100.00 . . . . 0.2775 . . . . . . . . . . . 0.3152 
'X-RAY DIFFRACTION' 2.73 3.12  . . 147 2791 100.00 . . . . 0.2744 . . . . . . . . . . . 0.3344 
'X-RAY DIFFRACTION' 3.12 3.92  . . 143 2795 99.00  . . . . 0.2078 . . . . . . . . . . . 0.2495 
'X-RAY DIFFRACTION' 3.92 19.66 . . 176 2927 99.00  . . . . 0.1832 . . . . . . . . . . . 0.2069 
# 
_struct.entry_id                     9DFU 
_struct.title                        
'X-ray crystal structure of the second Viperin-like enzyme from T. virens variant F40H with bound CTP and SAM' 
_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        9DFU 
_struct_keywords.text            'viperin-like enzyme, CTP, SAM, 4Fe-4S cluster, ddhCTP, ANTIVIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'ANTIVIRAL PROTEIN' 
# 
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 ? 
F N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    G9N0G3_HYPVG 
_struct_ref.pdbx_db_accession          G9N0G3 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;GQIPVSVNYFFTRKCNKSCGFCFHTAKTSHMEDISRAKRGLQLLQRAGMKKINFAGGEPFLYPKFLGELVDFCKEDLHLE
SVSIITNGSLVREEWVRKHAKNIDILACSCDSFDENMNIEIGRGTGNQVEILYRIAKWCRKNEIKFKLNTVVTRLNYEED
MNEHIDTLQPFRWKVFQVLIVEGENDSEKTLRDARRFTISDKQFEVFCSKHRHHKSFVAEPNRLMASSYLLVDEYMRFID
KDGNKLTKSILDVGVEAAMKEIKWDVDAFQERGGVYEWTKENEQVEACSTGMSEKLVW
;
_struct_ref.pdbx_align_begin           31 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9DFU 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 24 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 321 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             G9N0G3 
_struct_ref_seq.db_align_beg                  31 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  328 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       31 
_struct_ref_seq.pdbx_auth_seq_align_end       328 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9DFU MET A 1  ? UNP G9N0G3 ?   ?  'initiating methionine' 8  1  
1 9DFU HIS A 2  ? UNP G9N0G3 ?   ?  'expression tag'        9  2  
1 9DFU HIS A 3  ? UNP G9N0G3 ?   ?  'expression tag'        10 3  
1 9DFU HIS A 4  ? UNP G9N0G3 ?   ?  'expression tag'        11 4  
1 9DFU HIS A 5  ? UNP G9N0G3 ?   ?  'expression tag'        12 5  
1 9DFU HIS A 6  ? UNP G9N0G3 ?   ?  'expression tag'        13 6  
1 9DFU HIS A 7  ? UNP G9N0G3 ?   ?  'expression tag'        14 7  
1 9DFU SER A 8  ? UNP G9N0G3 ?   ?  'expression tag'        15 8  
1 9DFU SER A 9  ? UNP G9N0G3 ?   ?  'expression tag'        16 9  
1 9DFU GLY A 10 ? UNP G9N0G3 ?   ?  'expression tag'        17 10 
1 9DFU VAL A 11 ? UNP G9N0G3 ?   ?  'expression tag'        18 11 
1 9DFU ASP A 12 ? UNP G9N0G3 ?   ?  'expression tag'        19 12 
1 9DFU LEU A 13 ? UNP G9N0G3 ?   ?  'expression tag'        20 13 
1 9DFU GLY A 14 ? UNP G9N0G3 ?   ?  'expression tag'        21 14 
1 9DFU THR A 15 ? UNP G9N0G3 ?   ?  'expression tag'        22 15 
1 9DFU GLU A 16 ? UNP G9N0G3 ?   ?  'expression tag'        23 16 
1 9DFU ASN A 17 ? UNP G9N0G3 ?   ?  'expression tag'        24 17 
1 9DFU LEU A 18 ? UNP G9N0G3 ?   ?  'expression tag'        25 18 
1 9DFU TYR A 19 ? UNP G9N0G3 ?   ?  'expression tag'        26 19 
1 9DFU PHE A 20 ? UNP G9N0G3 ?   ?  'expression tag'        27 20 
1 9DFU GLN A 21 ? UNP G9N0G3 ?   ?  'expression tag'        28 21 
1 9DFU SER A 22 ? UNP G9N0G3 ?   ?  'expression tag'        29 22 
1 9DFU MET A 23 ? UNP G9N0G3 ?   ?  'expression tag'        30 23 
1 9DFU HIS A 33 ? UNP G9N0G3 PHE 40 'engineered mutation'   40 24 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_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 ASP A 56  ? ALA A 70  ? ASP A 63  ALA A 77  1 ? 15 
HELX_P HELX_P2  AA2 GLU A 81  ? LEU A 84  ? GLU A 88  LEU A 91  5 ? 4  
HELX_P HELX_P3  AA3 TYR A 85  ? ASP A 99  ? TYR A 92  ASP A 106 1 ? 15 
HELX_P HELX_P4  AA4 ARG A 115 ? ALA A 123 ? ARG A 122 ALA A 130 1 ? 9  
HELX_P HELX_P5  AA5 LYS A 124 ? ILE A 126 ? LYS A 131 ILE A 133 5 ? 3  
HELX_P HELX_P6  AA6 ASP A 137 ? GLY A 145 ? ASP A 144 GLY A 152 1 ? 9  
HELX_P HELX_P7  AA7 ASN A 150 ? ASN A 165 ? ASN A 157 ASN A 172 1 ? 16 
HELX_P HELX_P8  AA8 MET A 184 ? GLN A 192 ? MET A 191 GLN A 199 1 ? 9  
HELX_P HELX_P9  AA9 ASP A 216 ? THR A 221 ? ASP A 223 THR A 228 5 ? 6  
HELX_P HELX_P10 AB1 SER A 223 ? ARG A 235 ? SER A 230 ARG A 242 1 ? 13 
HELX_P HELX_P11 AB2 PRO A 244 ? ALA A 249 ? PRO A 251 ALA A 256 1 ? 6  
HELX_P HELX_P12 AB3 SER A 272 ? GLY A 277 ? SER A 279 GLY A 284 1 ? 6  
HELX_P HELX_P13 AB4 GLY A 277 ? LYS A 283 ? GLY A 284 LYS A 290 1 ? 7  
HELX_P HELX_P14 AB5 ASP A 288 ? ARG A 295 ? ASP A 295 ARG A 302 1 ? 8  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 38 SG  ? ? ? 1_555 C SF4 . FE4 ? ? A CYS 45  A SF4 402 1_555 ? ? ? ? ? ? ? 2.075 ? ? 
metalc2 metalc ? ? A CYS 42 SG  ? ? ? 1_555 C SF4 . FE1 ? ? A CYS 49  A SF4 402 1_555 ? ? ? ? ? ? ? 1.974 ? ? 
metalc3 metalc ? ? A CYS 45 SG  ? ? ? 1_555 C SF4 . FE3 ? ? A CYS 52  A SF4 402 1_555 ? ? ? ? ? ? ? 2.100 ? ? 
metalc4 metalc ? ? C SF4 .  FE2 ? ? ? 1_555 D SAM . N   ? ? A SF4 402 A SAM 403 1_555 ? ? ? ? ? ? ? 2.630 ? ? 
metalc5 metalc ? ? C SF4 .  FE2 ? ? ? 1_555 D SAM . OXT ? ? A SF4 402 A SAM 403 1_555 ? ? ? ? ? ? ? 2.725 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG ? A CYS 38 ? A CYS 45  ? 1_555 FE4 ? C SF4 . ? A SF4 402 ? 1_555 S1  ? C SF4 . ? A SF4 402 ? 1_555 128.9 ? 
2  SG ? A CYS 38 ? A CYS 45  ? 1_555 FE4 ? C SF4 . ? A SF4 402 ? 1_555 S2  ? C SF4 . ? A SF4 402 ? 1_555 136.6 ? 
3  S1 ? C SF4 .  ? A SF4 402 ? 1_555 FE4 ? C SF4 . ? A SF4 402 ? 1_555 S2  ? C SF4 . ? A SF4 402 ? 1_555 89.2  ? 
4  SG ? A CYS 38 ? A CYS 45  ? 1_555 FE4 ? C SF4 . ? A SF4 402 ? 1_555 S3  ? C SF4 . ? A SF4 402 ? 1_555 106.9 ? 
5  S1 ? C SF4 .  ? A SF4 402 ? 1_555 FE4 ? C SF4 . ? A SF4 402 ? 1_555 S3  ? C SF4 . ? A SF4 402 ? 1_555 91.6  ? 
6  S2 ? C SF4 .  ? A SF4 402 ? 1_555 FE4 ? C SF4 . ? A SF4 402 ? 1_555 S3  ? C SF4 . ? A SF4 402 ? 1_555 89.5  ? 
7  SG ? A CYS 42 ? A CYS 49  ? 1_555 FE1 ? C SF4 . ? A SF4 402 ? 1_555 S2  ? C SF4 . ? A SF4 402 ? 1_555 117.8 ? 
8  SG ? A CYS 42 ? A CYS 49  ? 1_555 FE1 ? C SF4 . ? A SF4 402 ? 1_555 S3  ? C SF4 . ? A SF4 402 ? 1_555 133.6 ? 
9  S2 ? C SF4 .  ? A SF4 402 ? 1_555 FE1 ? C SF4 . ? A SF4 402 ? 1_555 S3  ? C SF4 . ? A SF4 402 ? 1_555 89.3  ? 
10 SG ? A CYS 42 ? A CYS 49  ? 1_555 FE1 ? C SF4 . ? A SF4 402 ? 1_555 S4  ? C SF4 . ? A SF4 402 ? 1_555 125.9 ? 
11 S2 ? C SF4 .  ? A SF4 402 ? 1_555 FE1 ? C SF4 . ? A SF4 402 ? 1_555 S4  ? C SF4 . ? A SF4 402 ? 1_555 88.0  ? 
12 S3 ? C SF4 .  ? A SF4 402 ? 1_555 FE1 ? C SF4 . ? A SF4 402 ? 1_555 S4  ? C SF4 . ? A SF4 402 ? 1_555 89.2  ? 
13 SG ? A CYS 45 ? A CYS 52  ? 1_555 FE3 ? C SF4 . ? A SF4 402 ? 1_555 S1  ? C SF4 . ? A SF4 402 ? 1_555 130.7 ? 
14 SG ? A CYS 45 ? A CYS 52  ? 1_555 FE3 ? C SF4 . ? A SF4 402 ? 1_555 S2  ? C SF4 . ? A SF4 402 ? 1_555 118.9 ? 
15 S1 ? C SF4 .  ? A SF4 402 ? 1_555 FE3 ? C SF4 . ? A SF4 402 ? 1_555 S2  ? C SF4 . ? A SF4 402 ? 1_555 88.5  ? 
16 SG ? A CYS 45 ? A CYS 52  ? 1_555 FE3 ? C SF4 . ? A SF4 402 ? 1_555 S4  ? C SF4 . ? A SF4 402 ? 1_555 129.3 ? 
17 S1 ? C SF4 .  ? A SF4 402 ? 1_555 FE3 ? C SF4 . ? A SF4 402 ? 1_555 S4  ? C SF4 . ? A SF4 402 ? 1_555 88.0  ? 
18 S2 ? C SF4 .  ? A SF4 402 ? 1_555 FE3 ? C SF4 . ? A SF4 402 ? 1_555 S4  ? C SF4 . ? A SF4 402 ? 1_555 88.1  ? 
19 N  ? D SAM .  ? A SAM 403 ? 1_555 FE2 ? C SF4 . ? A SF4 402 ? 1_555 S1  ? C SF4 . ? A SF4 402 ? 1_555 99.9  ? 
20 N  ? D SAM .  ? A SAM 403 ? 1_555 FE2 ? C SF4 . ? A SF4 402 ? 1_555 S3  ? C SF4 . ? A SF4 402 ? 1_555 94.9  ? 
21 S1 ? C SF4 .  ? A SF4 402 ? 1_555 FE2 ? C SF4 . ? A SF4 402 ? 1_555 S3  ? C SF4 . ? A SF4 402 ? 1_555 90.7  ? 
22 N  ? D SAM .  ? A SAM 403 ? 1_555 FE2 ? C SF4 . ? A SF4 402 ? 1_555 S4  ? C SF4 . ? A SF4 402 ? 1_555 171.3 ? 
23 S1 ? C SF4 .  ? A SF4 402 ? 1_555 FE2 ? C SF4 . ? A SF4 402 ? 1_555 S4  ? C SF4 . ? A SF4 402 ? 1_555 87.9  ? 
24 S3 ? C SF4 .  ? A SF4 402 ? 1_555 FE2 ? C SF4 . ? A SF4 402 ? 1_555 S4  ? C SF4 . ? A SF4 402 ? 1_555 89.0  ? 
25 N  ? D SAM .  ? A SAM 403 ? 1_555 FE2 ? C SF4 . ? A SF4 402 ? 1_555 OXT ? D SAM . ? A SAM 403 ? 1_555 61.6  ? 
26 S1 ? C SF4 .  ? A SF4 402 ? 1_555 FE2 ? C SF4 . ? A SF4 402 ? 1_555 OXT ? D SAM . ? A SAM 403 ? 1_555 159.9 ? 
27 S3 ? C SF4 .  ? A SF4 402 ? 1_555 FE2 ? C SF4 . ? A SF4 402 ? 1_555 OXT ? D SAM . ? A SAM 403 ? 1_555 98.3  ? 
28 S4 ? C SF4 .  ? A SF4 402 ? 1_555 FE2 ? C SF4 . ? A SF4 402 ? 1_555 OXT ? D SAM . ? A SAM 403 ? 1_555 110.1 ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   10 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA1 2 3  ? parallel      
AA1 3 4  ? parallel      
AA1 4 5  ? parallel      
AA1 5 6  ? parallel      
AA1 6 7  ? parallel      
AA1 7 8  ? parallel      
AA1 8 9  ? anti-parallel 
AA1 9 10 ? 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  PHE A 240 ? GLU A 243 ? PHE A 247 GLU A 250 
AA1 2  ARG A 195 ? GLN A 200 ? ARG A 202 GLN A 207 
AA1 3  LYS A 168 ? VAL A 175 ? LYS A 175 VAL A 182 
AA1 4  ILE A 128 ? SER A 132 ? ILE A 135 SER A 139 
AA1 5  SER A 104 ? THR A 109 ? SER A 111 THR A 116 
AA1 6  LYS A 74  ? GLY A 79  ? LYS A 81  GLY A 86  
AA1 7  SER A 29  ? THR A 35  ? SER A 36  THR A 42  
AA1 8  LEU A 254 ? VAL A 255 ? LEU A 261 VAL A 262 
AA1 9  PHE A 261 ? ASP A 263 ? PHE A 268 ASP A 270 
AA1 10 LYS A 268 ? LEU A 269 ? LYS A 275 LEU A 276 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  O VAL A 241 ? O VAL A 248 N VAL A 198 ? N VAL A 205 
AA1 2 3  O PHE A 199 ? O PHE A 206 N VAL A 175 ? N VAL A 182 
AA1 3 4  O LYS A 168 ? O LYS A 175 N LEU A 129 ? N LEU A 136 
AA1 4 5  O ALA A 130 ? O ALA A 137 N ILE A 107 ? N ILE A 114 
AA1 5 6  O SER A 104 ? O SER A 111 N ILE A 75  ? N ILE A 82  
AA1 6 7  O ASN A 76  ? O ASN A 83  N TYR A 32  ? N TYR A 39  
AA1 7 8  N ASN A 31  ? N ASN A 38  O VAL A 255 ? O VAL A 262 
AA1 8 9  N LEU A 254 ? N LEU A 261 O ILE A 262 ? O ILE A 269 
AA1 9 10 N ASP A 263 ? N ASP A 270 O LYS A 268 ? O LYS A 275 
# 
_pdbx_entry_details.entry_id                   9DFU 
_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_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ALA A 85  ? ? -157.05 -158.02 
2 1 ASN A 186 ? ? -141.96 15.12   
3 1 ASN A 215 ? ? -153.93 31.28   
4 1 LYS A 310 ? ? 103.06  109.41  
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 8   ? A MET 1   
2  1 Y 1 A HIS 9   ? A HIS 2   
3  1 Y 1 A HIS 10  ? A HIS 3   
4  1 Y 1 A HIS 11  ? A HIS 4   
5  1 Y 1 A HIS 12  ? A HIS 5   
6  1 Y 1 A HIS 13  ? A HIS 6   
7  1 Y 1 A HIS 14  ? A HIS 7   
8  1 Y 1 A SER 15  ? A SER 8   
9  1 Y 1 A SER 16  ? A SER 9   
10 1 Y 1 A GLY 17  ? A GLY 10  
11 1 Y 1 A VAL 18  ? A VAL 11  
12 1 Y 1 A ASP 19  ? A ASP 12  
13 1 Y 1 A LEU 20  ? A LEU 13  
14 1 Y 1 A GLY 21  ? A GLY 14  
15 1 Y 1 A THR 22  ? A THR 15  
16 1 Y 1 A GLU 23  ? A GLU 16  
17 1 Y 1 A ASN 24  ? A ASN 17  
18 1 Y 1 A LEU 25  ? A LEU 18  
19 1 Y 1 A TYR 26  ? A TYR 19  
20 1 Y 1 A PHE 27  ? A PHE 20  
21 1 Y 1 A GLN 28  ? A GLN 21  
22 1 Y 1 A SER 29  ? A SER 22  
23 1 Y 1 A MET 30  ? A MET 23  
24 1 Y 1 A GLY 31  ? A GLY 24  
25 1 Y 1 A ASN 312 ? A ASN 305 
26 1 Y 1 A GLU 313 ? A GLU 306 
27 1 Y 1 A GLN 314 ? A GLN 307 
28 1 Y 1 A VAL 315 ? A VAL 308 
29 1 Y 1 A GLU 316 ? A GLU 309 
30 1 Y 1 A ALA 317 ? A ALA 310 
31 1 Y 1 A CYS 318 ? A CYS 311 
32 1 Y 1 A SER 319 ? A SER 312 
33 1 Y 1 A THR 320 ? A THR 313 
34 1 Y 1 A GLY 321 ? A GLY 314 
35 1 Y 1 A MET 322 ? A MET 315 
36 1 Y 1 A SER 323 ? A SER 316 
37 1 Y 1 A GLU 324 ? A GLU 317 
38 1 Y 1 A LYS 325 ? A LYS 318 
39 1 Y 1 A LEU 326 ? A LEU 319 
40 1 Y 1 A VAL 327 ? A VAL 320 
41 1 Y 1 A TRP 328 ? A TRP 321 
# 
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  
CL  CL     CL N N 74  
CTP N1     N  N N 75  
CTP C2     C  N N 76  
CTP N3     N  N N 77  
CTP C4     C  N N 78  
CTP C5     C  N N 79  
CTP C6     C  N N 80  
CTP O2     O  N N 81  
CTP N4     N  N N 82  
CTP "C1'"  C  N R 83  
CTP "C2'"  C  N R 84  
CTP "O2'"  O  N N 85  
CTP "C3'"  C  N S 86  
CTP "C4'"  C  N R 87  
CTP "O4'"  O  N N 88  
CTP "O3'"  O  N N 89  
CTP "C5'"  C  N N 90  
CTP "O5'"  O  N N 91  
CTP PA     P  N S 92  
CTP O1A    O  N N 93  
CTP O2A    O  N N 94  
CTP O3A    O  N N 95  
CTP PB     P  N R 96  
CTP O1B    O  N N 97  
CTP O2B    O  N N 98  
CTP O3B    O  N N 99  
CTP PG     P  N N 100 
CTP O1G    O  N N 101 
CTP O2G    O  N N 102 
CTP O3G    O  N N 103 
CTP H5     H  N N 104 
CTP H6     H  N N 105 
CTP HN41   H  N N 106 
CTP HN42   H  N N 107 
CTP "H1'"  H  N N 108 
CTP "H2'"  H  N N 109 
CTP "HO2'" H  N N 110 
CTP "H3'"  H  N N 111 
CTP "H4'"  H  N N 112 
CTP "HO3'" H  N N 113 
CTP "H5'1" H  N N 114 
CTP "H5'2" H  N N 115 
CTP HOA2   H  N N 116 
CTP HOB2   H  N N 117 
CTP HOG2   H  N N 118 
CTP HOG3   H  N N 119 
CYS N      N  N N 120 
CYS CA     C  N R 121 
CYS C      C  N N 122 
CYS O      O  N N 123 
CYS CB     C  N N 124 
CYS SG     S  N N 125 
CYS OXT    O  N N 126 
CYS H      H  N N 127 
CYS H2     H  N N 128 
CYS HA     H  N N 129 
CYS HB2    H  N N 130 
CYS HB3    H  N N 131 
CYS HG     H  N N 132 
CYS HXT    H  N N 133 
GLN N      N  N N 134 
GLN CA     C  N S 135 
GLN C      C  N N 136 
GLN O      O  N N 137 
GLN CB     C  N N 138 
GLN CG     C  N N 139 
GLN CD     C  N N 140 
GLN OE1    O  N N 141 
GLN NE2    N  N N 142 
GLN OXT    O  N N 143 
GLN H      H  N N 144 
GLN H2     H  N N 145 
GLN HA     H  N N 146 
GLN HB2    H  N N 147 
GLN HB3    H  N N 148 
GLN HG2    H  N N 149 
GLN HG3    H  N N 150 
GLN HE21   H  N N 151 
GLN HE22   H  N N 152 
GLN HXT    H  N N 153 
GLU N      N  N N 154 
GLU CA     C  N S 155 
GLU C      C  N N 156 
GLU O      O  N N 157 
GLU CB     C  N N 158 
GLU CG     C  N N 159 
GLU CD     C  N N 160 
GLU OE1    O  N N 161 
GLU OE2    O  N N 162 
GLU OXT    O  N N 163 
GLU H      H  N N 164 
GLU H2     H  N N 165 
GLU HA     H  N N 166 
GLU HB2    H  N N 167 
GLU HB3    H  N N 168 
GLU HG2    H  N N 169 
GLU HG3    H  N N 170 
GLU HE2    H  N N 171 
GLU HXT    H  N N 172 
GLY N      N  N N 173 
GLY CA     C  N N 174 
GLY C      C  N N 175 
GLY O      O  N N 176 
GLY OXT    O  N N 177 
GLY H      H  N N 178 
GLY H2     H  N N 179 
GLY HA2    H  N N 180 
GLY HA3    H  N N 181 
GLY HXT    H  N N 182 
HIS N      N  N N 183 
HIS CA     C  N S 184 
HIS C      C  N N 185 
HIS O      O  N N 186 
HIS CB     C  N N 187 
HIS CG     C  Y N 188 
HIS ND1    N  Y N 189 
HIS CD2    C  Y N 190 
HIS CE1    C  Y N 191 
HIS NE2    N  Y N 192 
HIS OXT    O  N N 193 
HIS H      H  N N 194 
HIS H2     H  N N 195 
HIS HA     H  N N 196 
HIS HB2    H  N N 197 
HIS HB3    H  N N 198 
HIS HD1    H  N N 199 
HIS HD2    H  N N 200 
HIS HE1    H  N N 201 
HIS HE2    H  N N 202 
HIS HXT    H  N N 203 
HOH O      O  N N 204 
HOH H1     H  N N 205 
HOH H2     H  N N 206 
ILE N      N  N N 207 
ILE CA     C  N S 208 
ILE C      C  N N 209 
ILE O      O  N N 210 
ILE CB     C  N S 211 
ILE CG1    C  N N 212 
ILE CG2    C  N N 213 
ILE CD1    C  N N 214 
ILE OXT    O  N N 215 
ILE H      H  N N 216 
ILE H2     H  N N 217 
ILE HA     H  N N 218 
ILE HB     H  N N 219 
ILE HG12   H  N N 220 
ILE HG13   H  N N 221 
ILE HG21   H  N N 222 
ILE HG22   H  N N 223 
ILE HG23   H  N N 224 
ILE HD11   H  N N 225 
ILE HD12   H  N N 226 
ILE HD13   H  N N 227 
ILE HXT    H  N N 228 
LEU N      N  N N 229 
LEU CA     C  N S 230 
LEU C      C  N N 231 
LEU O      O  N N 232 
LEU CB     C  N N 233 
LEU CG     C  N N 234 
LEU CD1    C  N N 235 
LEU CD2    C  N N 236 
LEU OXT    O  N N 237 
LEU H      H  N N 238 
LEU H2     H  N N 239 
LEU HA     H  N N 240 
LEU HB2    H  N N 241 
LEU HB3    H  N N 242 
LEU HG     H  N N 243 
LEU HD11   H  N N 244 
LEU HD12   H  N N 245 
LEU HD13   H  N N 246 
LEU HD21   H  N N 247 
LEU HD22   H  N N 248 
LEU HD23   H  N N 249 
LEU HXT    H  N N 250 
LYS N      N  N N 251 
LYS CA     C  N S 252 
LYS C      C  N N 253 
LYS O      O  N N 254 
LYS CB     C  N N 255 
LYS CG     C  N N 256 
LYS CD     C  N N 257 
LYS CE     C  N N 258 
LYS NZ     N  N N 259 
LYS OXT    O  N N 260 
LYS H      H  N N 261 
LYS H2     H  N N 262 
LYS HA     H  N N 263 
LYS HB2    H  N N 264 
LYS HB3    H  N N 265 
LYS HG2    H  N N 266 
LYS HG3    H  N N 267 
LYS HD2    H  N N 268 
LYS HD3    H  N N 269 
LYS HE2    H  N N 270 
LYS HE3    H  N N 271 
LYS HZ1    H  N N 272 
LYS HZ2    H  N N 273 
LYS HZ3    H  N N 274 
LYS HXT    H  N N 275 
MET N      N  N N 276 
MET CA     C  N S 277 
MET C      C  N N 278 
MET O      O  N N 279 
MET CB     C  N N 280 
MET CG     C  N N 281 
MET SD     S  N N 282 
MET CE     C  N N 283 
MET OXT    O  N N 284 
MET H      H  N N 285 
MET H2     H  N N 286 
MET HA     H  N N 287 
MET HB2    H  N N 288 
MET HB3    H  N N 289 
MET HG2    H  N N 290 
MET HG3    H  N N 291 
MET HE1    H  N N 292 
MET HE2    H  N N 293 
MET HE3    H  N N 294 
MET HXT    H  N N 295 
PHE N      N  N N 296 
PHE CA     C  N S 297 
PHE C      C  N N 298 
PHE O      O  N N 299 
PHE CB     C  N N 300 
PHE CG     C  Y N 301 
PHE CD1    C  Y N 302 
PHE CD2    C  Y N 303 
PHE CE1    C  Y N 304 
PHE CE2    C  Y N 305 
PHE CZ     C  Y N 306 
PHE OXT    O  N N 307 
PHE H      H  N N 308 
PHE H2     H  N N 309 
PHE HA     H  N N 310 
PHE HB2    H  N N 311 
PHE HB3    H  N N 312 
PHE HD1    H  N N 313 
PHE HD2    H  N N 314 
PHE HE1    H  N N 315 
PHE HE2    H  N N 316 
PHE HZ     H  N N 317 
PHE HXT    H  N N 318 
PRO N      N  N N 319 
PRO CA     C  N S 320 
PRO C      C  N N 321 
PRO O      O  N N 322 
PRO CB     C  N N 323 
PRO CG     C  N N 324 
PRO CD     C  N N 325 
PRO OXT    O  N N 326 
PRO H      H  N N 327 
PRO HA     H  N N 328 
PRO HB2    H  N N 329 
PRO HB3    H  N N 330 
PRO HG2    H  N N 331 
PRO HG3    H  N N 332 
PRO HD2    H  N N 333 
PRO HD3    H  N N 334 
PRO HXT    H  N N 335 
SAM N      N  N N 336 
SAM CA     C  N S 337 
SAM C      C  N N 338 
SAM O      O  N N 339 
SAM OXT    O  N N 340 
SAM CB     C  N N 341 
SAM CG     C  N N 342 
SAM SD     S  N S 343 
SAM CE     C  N N 344 
SAM "C5'"  C  N N 345 
SAM "C4'"  C  N S 346 
SAM "O4'"  O  N N 347 
SAM "C3'"  C  N S 348 
SAM "O3'"  O  N N 349 
SAM "C2'"  C  N R 350 
SAM "O2'"  O  N N 351 
SAM "C1'"  C  N R 352 
SAM N9     N  Y N 353 
SAM C8     C  Y N 354 
SAM N7     N  Y N 355 
SAM C5     C  Y N 356 
SAM C6     C  Y N 357 
SAM N6     N  N N 358 
SAM N1     N  Y N 359 
SAM C2     C  Y N 360 
SAM N3     N  Y N 361 
SAM C4     C  Y N 362 
SAM HN1    H  N N 363 
SAM HN2    H  N N 364 
SAM HA     H  N N 365 
SAM HB1    H  N N 366 
SAM HB2    H  N N 367 
SAM HG1    H  N N 368 
SAM HG2    H  N N 369 
SAM HE1    H  N N 370 
SAM HE2    H  N N 371 
SAM HE3    H  N N 372 
SAM "H5'1" H  N N 373 
SAM "H5'2" H  N N 374 
SAM "H4'"  H  N N 375 
SAM "H3'"  H  N N 376 
SAM "HO3'" H  N N 377 
SAM "H2'"  H  N N 378 
SAM "HO2'" H  N N 379 
SAM "H1'"  H  N N 380 
SAM H8     H  N N 381 
SAM HN61   H  N N 382 
SAM HN62   H  N N 383 
SAM H2     H  N N 384 
SER N      N  N N 385 
SER CA     C  N S 386 
SER C      C  N N 387 
SER O      O  N N 388 
SER CB     C  N N 389 
SER OG     O  N N 390 
SER OXT    O  N N 391 
SER H      H  N N 392 
SER H2     H  N N 393 
SER HA     H  N N 394 
SER HB2    H  N N 395 
SER HB3    H  N N 396 
SER HG     H  N N 397 
SER HXT    H  N N 398 
SF4 FE1    FE N N 399 
SF4 FE2    FE N N 400 
SF4 FE3    FE N N 401 
SF4 FE4    FE N N 402 
SF4 S1     S  N N 403 
SF4 S2     S  N N 404 
SF4 S3     S  N N 405 
SF4 S4     S  N N 406 
THR N      N  N N 407 
THR CA     C  N S 408 
THR C      C  N N 409 
THR O      O  N N 410 
THR CB     C  N R 411 
THR OG1    O  N N 412 
THR CG2    C  N N 413 
THR OXT    O  N N 414 
THR H      H  N N 415 
THR H2     H  N N 416 
THR HA     H  N N 417 
THR HB     H  N N 418 
THR HG1    H  N N 419 
THR HG21   H  N N 420 
THR HG22   H  N N 421 
THR HG23   H  N N 422 
THR HXT    H  N N 423 
TRP N      N  N N 424 
TRP CA     C  N S 425 
TRP C      C  N N 426 
TRP O      O  N N 427 
TRP CB     C  N N 428 
TRP CG     C  Y N 429 
TRP CD1    C  Y N 430 
TRP CD2    C  Y N 431 
TRP NE1    N  Y N 432 
TRP CE2    C  Y N 433 
TRP CE3    C  Y N 434 
TRP CZ2    C  Y N 435 
TRP CZ3    C  Y N 436 
TRP CH2    C  Y N 437 
TRP OXT    O  N N 438 
TRP H      H  N N 439 
TRP H2     H  N N 440 
TRP HA     H  N N 441 
TRP HB2    H  N N 442 
TRP HB3    H  N N 443 
TRP HD1    H  N N 444 
TRP HE1    H  N N 445 
TRP HE3    H  N N 446 
TRP HZ2    H  N N 447 
TRP HZ3    H  N N 448 
TRP HH2    H  N N 449 
TRP HXT    H  N N 450 
TYR N      N  N N 451 
TYR CA     C  N S 452 
TYR C      C  N N 453 
TYR O      O  N N 454 
TYR CB     C  N N 455 
TYR CG     C  Y N 456 
TYR CD1    C  Y N 457 
TYR CD2    C  Y N 458 
TYR CE1    C  Y N 459 
TYR CE2    C  Y N 460 
TYR CZ     C  Y N 461 
TYR OH     O  N N 462 
TYR OXT    O  N N 463 
TYR H      H  N N 464 
TYR H2     H  N N 465 
TYR HA     H  N N 466 
TYR HB2    H  N N 467 
TYR HB3    H  N N 468 
TYR HD1    H  N N 469 
TYR HD2    H  N N 470 
TYR HE1    H  N N 471 
TYR HE2    H  N N 472 
TYR HH     H  N N 473 
TYR HXT    H  N N 474 
VAL N      N  N N 475 
VAL CA     C  N S 476 
VAL C      C  N N 477 
VAL O      O  N N 478 
VAL CB     C  N N 479 
VAL CG1    C  N N 480 
VAL CG2    C  N N 481 
VAL OXT    O  N N 482 
VAL H      H  N N 483 
VAL H2     H  N N 484 
VAL HA     H  N N 485 
VAL HB     H  N N 486 
VAL HG11   H  N N 487 
VAL HG12   H  N N 488 
VAL HG13   H  N N 489 
VAL HG21   H  N N 490 
VAL HG22   H  N N 491 
VAL HG23   H  N N 492 
VAL HXT    H  N N 493 
# 
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  
CTP N1    C2     sing N N 70  
CTP N1    C6     sing N N 71  
CTP N1    "C1'"  sing N N 72  
CTP C2    N3     sing N N 73  
CTP C2    O2     doub N N 74  
CTP N3    C4     doub N N 75  
CTP C4    C5     sing N N 76  
CTP C4    N4     sing N N 77  
CTP C5    C6     doub N N 78  
CTP C5    H5     sing N N 79  
CTP C6    H6     sing N N 80  
CTP N4    HN41   sing N N 81  
CTP N4    HN42   sing N N 82  
CTP "C1'" "C2'"  sing N N 83  
CTP "C1'" "O4'"  sing N N 84  
CTP "C1'" "H1'"  sing N N 85  
CTP "C2'" "O2'"  sing N N 86  
CTP "C2'" "C3'"  sing N N 87  
CTP "C2'" "H2'"  sing N N 88  
CTP "O2'" "HO2'" sing N N 89  
CTP "C3'" "C4'"  sing N N 90  
CTP "C3'" "O3'"  sing N N 91  
CTP "C3'" "H3'"  sing N N 92  
CTP "C4'" "O4'"  sing N N 93  
CTP "C4'" "C5'"  sing N N 94  
CTP "C4'" "H4'"  sing N N 95  
CTP "O3'" "HO3'" sing N N 96  
CTP "C5'" "O5'"  sing N N 97  
CTP "C5'" "H5'1" sing N N 98  
CTP "C5'" "H5'2" sing N N 99  
CTP "O5'" PA     sing N N 100 
CTP PA    O1A    doub N N 101 
CTP PA    O2A    sing N N 102 
CTP PA    O3A    sing N N 103 
CTP O2A   HOA2   sing N N 104 
CTP O3A   PB     sing N N 105 
CTP PB    O1B    doub N N 106 
CTP PB    O2B    sing N N 107 
CTP PB    O3B    sing N N 108 
CTP O2B   HOB2   sing N N 109 
CTP O3B   PG     sing N N 110 
CTP PG    O1G    doub N N 111 
CTP PG    O2G    sing N N 112 
CTP PG    O3G    sing N N 113 
CTP O2G   HOG2   sing N N 114 
CTP O3G   HOG3   sing N N 115 
CYS N     CA     sing N N 116 
CYS N     H      sing N N 117 
CYS N     H2     sing N N 118 
CYS CA    C      sing N N 119 
CYS CA    CB     sing N N 120 
CYS CA    HA     sing N N 121 
CYS C     O      doub N N 122 
CYS C     OXT    sing N N 123 
CYS CB    SG     sing N N 124 
CYS CB    HB2    sing N N 125 
CYS CB    HB3    sing N N 126 
CYS SG    HG     sing N N 127 
CYS OXT   HXT    sing N N 128 
GLN N     CA     sing N N 129 
GLN N     H      sing N N 130 
GLN N     H2     sing N N 131 
GLN CA    C      sing N N 132 
GLN CA    CB     sing N N 133 
GLN CA    HA     sing N N 134 
GLN C     O      doub N N 135 
GLN C     OXT    sing N N 136 
GLN CB    CG     sing N N 137 
GLN CB    HB2    sing N N 138 
GLN CB    HB3    sing N N 139 
GLN CG    CD     sing N N 140 
GLN CG    HG2    sing N N 141 
GLN CG    HG3    sing N N 142 
GLN CD    OE1    doub N N 143 
GLN CD    NE2    sing N N 144 
GLN NE2   HE21   sing N N 145 
GLN NE2   HE22   sing N N 146 
GLN OXT   HXT    sing N N 147 
GLU N     CA     sing N N 148 
GLU N     H      sing N N 149 
GLU N     H2     sing N N 150 
GLU CA    C      sing N N 151 
GLU CA    CB     sing N N 152 
GLU CA    HA     sing N N 153 
GLU C     O      doub N N 154 
GLU C     OXT    sing N N 155 
GLU CB    CG     sing N N 156 
GLU CB    HB2    sing N N 157 
GLU CB    HB3    sing N N 158 
GLU CG    CD     sing N N 159 
GLU CG    HG2    sing N N 160 
GLU CG    HG3    sing N N 161 
GLU CD    OE1    doub N N 162 
GLU CD    OE2    sing N N 163 
GLU OE2   HE2    sing N N 164 
GLU OXT   HXT    sing N N 165 
GLY N     CA     sing N N 166 
GLY N     H      sing N N 167 
GLY N     H2     sing N N 168 
GLY CA    C      sing N N 169 
GLY CA    HA2    sing N N 170 
GLY CA    HA3    sing N N 171 
GLY C     O      doub N N 172 
GLY C     OXT    sing N N 173 
GLY OXT   HXT    sing N N 174 
HIS N     CA     sing N N 175 
HIS N     H      sing N N 176 
HIS N     H2     sing N N 177 
HIS CA    C      sing N N 178 
HIS CA    CB     sing N N 179 
HIS CA    HA     sing N N 180 
HIS C     O      doub N N 181 
HIS C     OXT    sing N N 182 
HIS CB    CG     sing N N 183 
HIS CB    HB2    sing N N 184 
HIS CB    HB3    sing N N 185 
HIS CG    ND1    sing Y N 186 
HIS CG    CD2    doub Y N 187 
HIS ND1   CE1    doub Y N 188 
HIS ND1   HD1    sing N N 189 
HIS CD2   NE2    sing Y N 190 
HIS CD2   HD2    sing N N 191 
HIS CE1   NE2    sing Y N 192 
HIS CE1   HE1    sing N N 193 
HIS NE2   HE2    sing N N 194 
HIS OXT   HXT    sing N N 195 
HOH O     H1     sing N N 196 
HOH O     H2     sing N N 197 
ILE N     CA     sing N N 198 
ILE N     H      sing N N 199 
ILE N     H2     sing N N 200 
ILE CA    C      sing N N 201 
ILE CA    CB     sing N N 202 
ILE CA    HA     sing N N 203 
ILE C     O      doub N N 204 
ILE C     OXT    sing N N 205 
ILE CB    CG1    sing N N 206 
ILE CB    CG2    sing N N 207 
ILE CB    HB     sing N N 208 
ILE CG1   CD1    sing N N 209 
ILE CG1   HG12   sing N N 210 
ILE CG1   HG13   sing N N 211 
ILE CG2   HG21   sing N N 212 
ILE CG2   HG22   sing N N 213 
ILE CG2   HG23   sing N N 214 
ILE CD1   HD11   sing N N 215 
ILE CD1   HD12   sing N N 216 
ILE CD1   HD13   sing N N 217 
ILE OXT   HXT    sing N N 218 
LEU N     CA     sing N N 219 
LEU N     H      sing N N 220 
LEU N     H2     sing N N 221 
LEU CA    C      sing N N 222 
LEU CA    CB     sing N N 223 
LEU CA    HA     sing N N 224 
LEU C     O      doub N N 225 
LEU C     OXT    sing N N 226 
LEU CB    CG     sing N N 227 
LEU CB    HB2    sing N N 228 
LEU CB    HB3    sing N N 229 
LEU CG    CD1    sing N N 230 
LEU CG    CD2    sing N N 231 
LEU CG    HG     sing N N 232 
LEU CD1   HD11   sing N N 233 
LEU CD1   HD12   sing N N 234 
LEU CD1   HD13   sing N N 235 
LEU CD2   HD21   sing N N 236 
LEU CD2   HD22   sing N N 237 
LEU CD2   HD23   sing N N 238 
LEU OXT   HXT    sing N N 239 
LYS N     CA     sing N N 240 
LYS N     H      sing N N 241 
LYS N     H2     sing N N 242 
LYS CA    C      sing N N 243 
LYS CA    CB     sing N N 244 
LYS CA    HA     sing N N 245 
LYS C     O      doub N N 246 
LYS C     OXT    sing N N 247 
LYS CB    CG     sing N N 248 
LYS CB    HB2    sing N N 249 
LYS CB    HB3    sing N N 250 
LYS CG    CD     sing N N 251 
LYS CG    HG2    sing N N 252 
LYS CG    HG3    sing N N 253 
LYS CD    CE     sing N N 254 
LYS CD    HD2    sing N N 255 
LYS CD    HD3    sing N N 256 
LYS CE    NZ     sing N N 257 
LYS CE    HE2    sing N N 258 
LYS CE    HE3    sing N N 259 
LYS NZ    HZ1    sing N N 260 
LYS NZ    HZ2    sing N N 261 
LYS NZ    HZ3    sing N N 262 
LYS OXT   HXT    sing N N 263 
MET N     CA     sing N N 264 
MET N     H      sing N N 265 
MET N     H2     sing N N 266 
MET CA    C      sing N N 267 
MET CA    CB     sing N N 268 
MET CA    HA     sing N N 269 
MET C     O      doub N N 270 
MET C     OXT    sing N N 271 
MET CB    CG     sing N N 272 
MET CB    HB2    sing N N 273 
MET CB    HB3    sing N N 274 
MET CG    SD     sing N N 275 
MET CG    HG2    sing N N 276 
MET CG    HG3    sing N N 277 
MET SD    CE     sing N N 278 
MET CE    HE1    sing N N 279 
MET CE    HE2    sing N N 280 
MET CE    HE3    sing N N 281 
MET OXT   HXT    sing N N 282 
PHE N     CA     sing N N 283 
PHE N     H      sing N N 284 
PHE N     H2     sing N N 285 
PHE CA    C      sing N N 286 
PHE CA    CB     sing N N 287 
PHE CA    HA     sing N N 288 
PHE C     O      doub N N 289 
PHE C     OXT    sing N N 290 
PHE CB    CG     sing N N 291 
PHE CB    HB2    sing N N 292 
PHE CB    HB3    sing N N 293 
PHE CG    CD1    doub Y N 294 
PHE CG    CD2    sing Y N 295 
PHE CD1   CE1    sing Y N 296 
PHE CD1   HD1    sing N N 297 
PHE CD2   CE2    doub Y N 298 
PHE CD2   HD2    sing N N 299 
PHE CE1   CZ     doub Y N 300 
PHE CE1   HE1    sing N N 301 
PHE CE2   CZ     sing Y N 302 
PHE CE2   HE2    sing N N 303 
PHE CZ    HZ     sing N N 304 
PHE OXT   HXT    sing N N 305 
PRO N     CA     sing N N 306 
PRO N     CD     sing N N 307 
PRO N     H      sing N N 308 
PRO CA    C      sing N N 309 
PRO CA    CB     sing N N 310 
PRO CA    HA     sing N N 311 
PRO C     O      doub N N 312 
PRO C     OXT    sing N N 313 
PRO CB    CG     sing N N 314 
PRO CB    HB2    sing N N 315 
PRO CB    HB3    sing N N 316 
PRO CG    CD     sing N N 317 
PRO CG    HG2    sing N N 318 
PRO CG    HG3    sing N N 319 
PRO CD    HD2    sing N N 320 
PRO CD    HD3    sing N N 321 
PRO OXT   HXT    sing N N 322 
SAM N     CA     sing N N 323 
SAM N     HN1    sing N N 324 
SAM N     HN2    sing N N 325 
SAM CA    C      sing N N 326 
SAM CA    CB     sing N N 327 
SAM CA    HA     sing N N 328 
SAM C     O      doub N N 329 
SAM C     OXT    sing N N 330 
SAM CB    CG     sing N N 331 
SAM CB    HB1    sing N N 332 
SAM CB    HB2    sing N N 333 
SAM CG    SD     sing N N 334 
SAM CG    HG1    sing N N 335 
SAM CG    HG2    sing N N 336 
SAM SD    CE     sing N N 337 
SAM SD    "C5'"  sing N N 338 
SAM CE    HE1    sing N N 339 
SAM CE    HE2    sing N N 340 
SAM CE    HE3    sing N N 341 
SAM "C5'" "C4'"  sing N N 342 
SAM "C5'" "H5'1" sing N N 343 
SAM "C5'" "H5'2" sing N N 344 
SAM "C4'" "O4'"  sing N N 345 
SAM "C4'" "C3'"  sing N N 346 
SAM "C4'" "H4'"  sing N N 347 
SAM "O4'" "C1'"  sing N N 348 
SAM "C3'" "O3'"  sing N N 349 
SAM "C3'" "C2'"  sing N N 350 
SAM "C3'" "H3'"  sing N N 351 
SAM "O3'" "HO3'" sing N N 352 
SAM "C2'" "O2'"  sing N N 353 
SAM "C2'" "C1'"  sing N N 354 
SAM "C2'" "H2'"  sing N N 355 
SAM "O2'" "HO2'" sing N N 356 
SAM "C1'" N9     sing N N 357 
SAM "C1'" "H1'"  sing N N 358 
SAM N9    C8     sing Y N 359 
SAM N9    C4     sing Y N 360 
SAM C8    N7     doub Y N 361 
SAM C8    H8     sing N N 362 
SAM N7    C5     sing Y N 363 
SAM C5    C6     sing Y N 364 
SAM C5    C4     doub Y N 365 
SAM C6    N6     sing N N 366 
SAM C6    N1     doub Y N 367 
SAM N6    HN61   sing N N 368 
SAM N6    HN62   sing N N 369 
SAM N1    C2     sing Y N 370 
SAM C2    N3     doub Y N 371 
SAM C2    H2     sing N N 372 
SAM N3    C4     sing Y N 373 
SER N     CA     sing N N 374 
SER N     H      sing N N 375 
SER N     H2     sing N N 376 
SER CA    C      sing N N 377 
SER CA    CB     sing N N 378 
SER CA    HA     sing N N 379 
SER C     O      doub N N 380 
SER C     OXT    sing N N 381 
SER CB    OG     sing N N 382 
SER CB    HB2    sing N N 383 
SER CB    HB3    sing N N 384 
SER OG    HG     sing N N 385 
SER OXT   HXT    sing N N 386 
SF4 FE1   S2     sing N N 387 
SF4 FE1   S3     sing N N 388 
SF4 FE1   S4     sing N N 389 
SF4 FE2   S1     sing N N 390 
SF4 FE2   S3     sing N N 391 
SF4 FE2   S4     sing N N 392 
SF4 FE3   S1     sing N N 393 
SF4 FE3   S2     sing N N 394 
SF4 FE3   S4     sing N N 395 
SF4 FE4   S1     sing N N 396 
SF4 FE4   S2     sing N N 397 
SF4 FE4   S3     sing N N 398 
THR N     CA     sing N N 399 
THR N     H      sing N N 400 
THR N     H2     sing N N 401 
THR CA    C      sing N N 402 
THR CA    CB     sing N N 403 
THR CA    HA     sing N N 404 
THR C     O      doub N N 405 
THR C     OXT    sing N N 406 
THR CB    OG1    sing N N 407 
THR CB    CG2    sing N N 408 
THR CB    HB     sing N N 409 
THR OG1   HG1    sing N N 410 
THR CG2   HG21   sing N N 411 
THR CG2   HG22   sing N N 412 
THR CG2   HG23   sing N N 413 
THR OXT   HXT    sing N N 414 
TRP N     CA     sing N N 415 
TRP N     H      sing N N 416 
TRP N     H2     sing N N 417 
TRP CA    C      sing N N 418 
TRP CA    CB     sing N N 419 
TRP CA    HA     sing N N 420 
TRP C     O      doub N N 421 
TRP C     OXT    sing N N 422 
TRP CB    CG     sing N N 423 
TRP CB    HB2    sing N N 424 
TRP CB    HB3    sing N N 425 
TRP CG    CD1    doub Y N 426 
TRP CG    CD2    sing Y N 427 
TRP CD1   NE1    sing Y N 428 
TRP CD1   HD1    sing N N 429 
TRP CD2   CE2    doub Y N 430 
TRP CD2   CE3    sing Y N 431 
TRP NE1   CE2    sing Y N 432 
TRP NE1   HE1    sing N N 433 
TRP CE2   CZ2    sing Y N 434 
TRP CE3   CZ3    doub Y N 435 
TRP CE3   HE3    sing N N 436 
TRP CZ2   CH2    doub Y N 437 
TRP CZ2   HZ2    sing N N 438 
TRP CZ3   CH2    sing Y N 439 
TRP CZ3   HZ3    sing N N 440 
TRP CH2   HH2    sing N N 441 
TRP OXT   HXT    sing N N 442 
TYR N     CA     sing N N 443 
TYR N     H      sing N N 444 
TYR N     H2     sing N N 445 
TYR CA    C      sing N N 446 
TYR CA    CB     sing N N 447 
TYR CA    HA     sing N N 448 
TYR C     O      doub N N 449 
TYR C     OXT    sing N N 450 
TYR CB    CG     sing N N 451 
TYR CB    HB2    sing N N 452 
TYR CB    HB3    sing N N 453 
TYR CG    CD1    doub Y N 454 
TYR CG    CD2    sing Y N 455 
TYR CD1   CE1    sing Y N 456 
TYR CD1   HD1    sing N N 457 
TYR CD2   CE2    doub Y N 458 
TYR CD2   HD2    sing N N 459 
TYR CE1   CZ     doub Y N 460 
TYR CE1   HE1    sing N N 461 
TYR CE2   CZ     sing Y N 462 
TYR CE2   HE2    sing N N 463 
TYR CZ    OH     sing N N 464 
TYR OH    HH     sing N N 465 
TYR OXT   HXT    sing N N 466 
VAL N     CA     sing N N 467 
VAL N     H      sing N N 468 
VAL N     H2     sing N N 469 
VAL CA    C      sing N N 470 
VAL CA    CB     sing N N 471 
VAL CA    HA     sing N N 472 
VAL C     O      doub N N 473 
VAL C     OXT    sing N N 474 
VAL CB    CG1    sing N N 475 
VAL CB    CG2    sing N N 476 
VAL CB    HB     sing N N 477 
VAL CG1   HG11   sing N N 478 
VAL CG1   HG12   sing N N 479 
VAL CG1   HG13   sing N N 480 
VAL CG2   HG21   sing N N 481 
VAL CG2   HG22   sing N N 482 
VAL CG2   HG23   sing N N 483 
VAL OXT   HXT    sing N N 484 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           GM007491 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7N7I 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9DFU 
_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]   0.026927 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017870 
_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]   0.006544 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
FE 
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     . GLN A 1 25  ? -5.576  -4.033  0.815  1.00 39.81 ? 32  GLN A N     1 
ATOM   2    C  CA    . GLN A 1 25  ? -5.823  -4.396  2.192  1.00 35.66 ? 32  GLN A CA    1 
ATOM   3    C  C     . GLN A 1 25  ? -6.244  -5.839  2.296  1.00 29.30 ? 32  GLN A C     1 
ATOM   4    O  O     . GLN A 1 25  ? -7.359  -6.188  1.973  1.00 29.63 ? 32  GLN A O     1 
ATOM   5    C  CB    . GLN A 1 25  ? -6.894  -3.495  2.793  1.00 35.67 ? 32  GLN A CB    1 
ATOM   6    C  CG    . GLN A 1 25  ? -6.564  -2.015  2.710  1.00 43.82 ? 32  GLN A CG    1 
ATOM   7    C  CD    . GLN A 1 25  ? -5.998  -1.449  3.998  1.00 38.22 ? 32  GLN A CD    1 
ATOM   8    O  OE1   . GLN A 1 25  ? -4.905  -1.806  4.419  1.00 36.64 ? 32  GLN A OE1   1 
ATOM   9    N  NE2   . GLN A 1 25  ? -6.743  -0.550  4.622  1.00 35.45 ? 32  GLN A NE2   1 
ATOM   10   N  N     . ILE A 1 26  ? -5.336  -6.704  2.687  1.00 26.66 ? 33  ILE A N     1 
ATOM   11   C  CA    . ILE A 1 26  ? -5.726  -8.086  2.891  1.00 27.02 ? 33  ILE A CA    1 
ATOM   12   C  C     . ILE A 1 26  ? -6.287  -8.239  4.309  1.00 25.91 ? 33  ILE A C     1 
ATOM   13   O  O     . ILE A 1 26  ? -5.562  -8.106  5.264  1.00 26.54 ? 33  ILE A O     1 
ATOM   14   C  CB    . ILE A 1 26  ? -4.573  -9.082  2.621  1.00 25.70 ? 33  ILE A CB    1 
ATOM   15   C  CG1   . ILE A 1 26  ? -3.865  -8.746  1.307  1.00 27.16 ? 33  ILE A CG1   1 
ATOM   16   C  CG2   . ILE A 1 26  ? -5.090  -10.507 2.638  1.00 21.09 ? 33  ILE A CG2   1 
ATOM   17   C  CD1   . ILE A 1 26  ? -4.766  -8.758  0.094  1.00 28.41 ? 33  ILE A CD1   1 
ATOM   18   N  N     . PRO A 1 27  ? -7.600  -8.503  4.421  1.00 26.13 ? 34  PRO A N     1 
ATOM   19   C  CA    . PRO A 1 27  ? -8.214  -8.651  5.748  1.00 25.25 ? 34  PRO A CA    1 
ATOM   20   C  C     . PRO A 1 27  ? -7.813  -9.944  6.436  1.00 24.84 ? 34  PRO A C     1 
ATOM   21   O  O     . PRO A 1 27  ? -8.644  -10.835 6.626  1.00 23.76 ? 34  PRO A O     1 
ATOM   22   C  CB    . PRO A 1 27  ? -9.714  -8.621  5.440  1.00 26.12 ? 34  PRO A CB    1 
ATOM   23   C  CG    . PRO A 1 27  ? -9.810  -9.176  4.062  1.00 21.52 ? 34  PRO A CG    1 
ATOM   24   C  CD    . PRO A 1 27  ? -8.582  -8.685  3.337  1.00 21.36 ? 34  PRO A CD    1 
ATOM   25   N  N     . VAL A 1 28  ? -6.542  -10.049 6.834  1.00 19.15 ? 35  VAL A N     1 
ATOM   26   C  CA    . VAL A 1 28  ? -6.018  -11.314 7.336  1.00 23.40 ? 35  VAL A CA    1 
ATOM   27   C  C     . VAL A 1 28  ? -6.566  -11.667 8.715  1.00 27.20 ? 35  VAL A C     1 
ATOM   28   O  O     . VAL A 1 28  ? -6.519  -12.836 9.114  1.00 24.39 ? 35  VAL A O     1 
ATOM   29   C  CB    . VAL A 1 28  ? -4.477  -11.264 7.340  1.00 21.65 ? 35  VAL A CB    1 
ATOM   30   C  CG1   . VAL A 1 28  ? -3.966  -10.410 8.494  1.00 26.40 ? 35  VAL A CG1   1 
ATOM   31   C  CG2   . VAL A 1 28  ? -3.887  -12.667 7.391  1.00 20.38 ? 35  VAL A CG2   1 
ATOM   32   N  N     . SER A 1 29  ? -7.096  -10.693 9.454  1.00 25.56 ? 36  SER A N     1 
ATOM   33   C  CA    . SER A 1 29  ? -7.581  -10.917 10.812 1.00 21.15 ? 36  SER A CA    1 
ATOM   34   C  C     . SER A 1 29  ? -8.817  -10.060 11.029 1.00 18.16 ? 36  SER A C     1 
ATOM   35   O  O     . SER A 1 29  ? -8.742  -8.831  10.948 1.00 20.69 ? 36  SER A O     1 
ATOM   36   C  CB    . SER A 1 29  ? -6.500  -10.583 11.846 1.00 23.91 ? 36  SER A CB    1 
ATOM   37   O  OG    . SER A 1 29  ? -6.681  -11.325 13.039 1.00 21.75 ? 36  SER A OG    1 
ATOM   38   N  N     . VAL A 1 30  ? -9.948  -10.705 11.306 1.00 16.63 ? 37  VAL A N     1 
ATOM   39   C  CA    . VAL A 1 30  ? -11.244 -10.042 11.348 1.00 17.54 ? 37  VAL A CA    1 
ATOM   40   C  C     . VAL A 1 30  ? -11.937 -10.367 12.665 1.00 16.91 ? 37  VAL A C     1 
ATOM   41   O  O     . VAL A 1 30  ? -11.907 -11.512 13.128 1.00 18.07 ? 37  VAL A O     1 
ATOM   42   C  CB    . VAL A 1 30  ? -12.123 -10.463 10.150 1.00 18.62 ? 37  VAL A CB    1 
ATOM   43   C  CG1   . VAL A 1 30  ? -13.492 -9.835  10.250 1.00 13.32 ? 37  VAL A CG1   1 
ATOM   44   C  CG2   . VAL A 1 30  ? -11.458 -10.072 8.836  1.00 21.58 ? 37  VAL A CG2   1 
ATOM   45   N  N     . ASN A 1 31  ? -12.553 -9.353  13.269 1.00 14.64 ? 38  ASN A N     1 
ATOM   46   C  CA    . ASN A 1 31  ? -13.419 -9.527  14.428 1.00 14.99 ? 38  ASN A CA    1 
ATOM   47   C  C     . ASN A 1 31  ? -14.871 -9.422  13.975 1.00 18.28 ? 38  ASN A C     1 
ATOM   48   O  O     . ASN A 1 31  ? -15.286 -8.382  13.453 1.00 16.08 ? 38  ASN A O     1 
ATOM   49   C  CB    . ASN A 1 31  ? -13.118 -8.480  15.501 1.00 15.36 ? 38  ASN A CB    1 
ATOM   50   C  CG    . ASN A 1 31  ? -11.867 -8.799  16.298 1.00 18.13 ? 38  ASN A CG    1 
ATOM   51   O  OD1   . ASN A 1 31  ? -11.931 -9.437  17.348 1.00 17.00 ? 38  ASN A OD1   1 
ATOM   52   N  ND2   . ASN A 1 31  ? -10.719 -8.354  15.798 1.00 12.03 ? 38  ASN A ND2   1 
ATOM   53   N  N     . TYR A 1 32  ? -15.638 -10.492 14.177 1.00 19.64 ? 39  TYR A N     1 
ATOM   54   C  CA    . TYR A 1 32  ? -17.057 -10.520 13.823 1.00 17.66 ? 39  TYR A CA    1 
ATOM   55   C  C     . TYR A 1 32  ? -17.870 -10.362 15.104 1.00 15.88 ? 39  TYR A C     1 
ATOM   56   O  O     . TYR A 1 32  ? -18.023 -11.309 15.879 1.00 18.65 ? 39  TYR A O     1 
ATOM   57   C  CB    . TYR A 1 32  ? -17.415 -11.808 13.087 1.00 19.61 ? 39  TYR A CB    1 
ATOM   58   C  CG    . TYR A 1 32  ? -18.890 -11.951 12.753 1.00 16.65 ? 39  TYR A CG    1 
ATOM   59   C  CD1   . TYR A 1 32  ? -19.694 -10.835 12.548 1.00 20.41 ? 39  TYR A CD1   1 
ATOM   60   C  CD2   . TYR A 1 32  ? -19.472 -13.206 12.628 1.00 16.45 ? 39  TYR A CD2   1 
ATOM   61   C  CE1   . TYR A 1 32  ? -21.035 -10.963 12.240 1.00 19.61 ? 39  TYR A CE1   1 
ATOM   62   C  CE2   . TYR A 1 32  ? -20.812 -13.344 12.317 1.00 18.96 ? 39  TYR A CE2   1 
ATOM   63   C  CZ    . TYR A 1 32  ? -21.588 -12.219 12.124 1.00 21.16 ? 39  TYR A CZ    1 
ATOM   64   O  OH    . TYR A 1 32  ? -22.923 -12.348 11.818 1.00 24.82 ? 39  TYR A OH    1 
ATOM   65   N  N     . HIS A 1 33  ? -18.395 -9.156  15.317 1.00 16.09 ? 40  HIS A N     1 
ATOM   66   C  CA    . HIS A 1 33  ? -19.277 -8.870  16.445 1.00 17.11 ? 40  HIS A CA    1 
ATOM   67   C  C     . HIS A 1 33  ? -20.703 -9.229  16.031 1.00 16.68 ? 40  HIS A C     1 
ATOM   68   O  O     . HIS A 1 33  ? -21.506 -8.383  15.628 1.00 18.43 ? 40  HIS A O     1 
ATOM   69   C  CB    . HIS A 1 33  ? -19.150 -7.409  16.859 1.00 14.36 ? 40  HIS A CB    1 
ATOM   70   C  CG    . HIS A 1 33  ? -17.737 -6.963  17.091 1.00 20.01 ? 40  HIS A CG    1 
ATOM   71   N  ND1   . HIS A 1 33  ? -17.178 -6.877  18.348 1.00 17.29 ? 40  HIS A ND1   1 
ATOM   72   C  CD2   . HIS A 1 33  ? -16.771 -6.577  16.224 1.00 18.06 ? 40  HIS A CD2   1 
ATOM   73   C  CE1   . HIS A 1 33  ? -15.929 -6.458  18.247 1.00 19.49 ? 40  HIS A CE1   1 
ATOM   74   N  NE2   . HIS A 1 33  ? -15.657 -6.270  16.968 1.00 18.93 ? 40  HIS A NE2   1 
ATOM   75   N  N     . PHE A 1 34  ? -21.024 -10.524 16.133 1.00 16.34 ? 41  PHE A N     1 
ATOM   76   C  CA    . PHE A 1 34  ? -22.276 -11.008 15.558 1.00 20.59 ? 41  PHE A CA    1 
ATOM   77   C  C     . PHE A 1 34  ? -23.500 -10.576 16.357 1.00 20.76 ? 41  PHE A C     1 
ATOM   78   O  O     . PHE A 1 34  ? -24.599 -10.529 15.794 1.00 24.52 ? 41  PHE A O     1 
ATOM   79   C  CB    . PHE A 1 34  ? -22.242 -12.536 15.396 1.00 18.82 ? 41  PHE A CB    1 
ATOM   80   C  CG    . PHE A 1 34  ? -22.360 -13.306 16.681 1.00 20.31 ? 41  PHE A CG    1 
ATOM   81   C  CD1   . PHE A 1 34  ? -21.235 -13.634 17.417 1.00 19.15 ? 41  PHE A CD1   1 
ATOM   82   C  CD2   . PHE A 1 34  ? -23.596 -13.743 17.129 1.00 20.83 ? 41  PHE A CD2   1 
ATOM   83   C  CE1   . PHE A 1 34  ? -21.346 -14.355 18.591 1.00 19.70 ? 41  PHE A CE1   1 
ATOM   84   C  CE2   . PHE A 1 34  ? -23.712 -14.462 18.300 1.00 18.93 ? 41  PHE A CE2   1 
ATOM   85   C  CZ    . PHE A 1 34  ? -22.588 -14.769 19.031 1.00 23.52 ? 41  PHE A CZ    1 
ATOM   86   N  N     . THR A 1 35  ? -23.342 -10.250 17.638 1.00 23.04 ? 42  THR A N     1 
ATOM   87   C  CA    . THR A 1 35  ? -24.440 -9.748  18.450 1.00 17.95 ? 42  THR A CA    1 
ATOM   88   C  C     . THR A 1 35  ? -23.976 -8.533  19.241 1.00 21.04 ? 42  THR A C     1 
ATOM   89   O  O     . THR A 1 35  ? -22.782 -8.335  19.474 1.00 18.28 ? 42  THR A O     1 
ATOM   90   C  CB    . THR A 1 35  ? -24.978 -10.813 19.416 1.00 16.16 ? 42  THR A CB    1 
ATOM   91   O  OG1   . THR A 1 35  ? -25.933 -10.213 20.300 1.00 20.16 ? 42  THR A OG1   1 
ATOM   92   C  CG2   . THR A 1 35  ? -23.848 -11.403 20.242 1.00 20.20 ? 42  THR A CG2   1 
ATOM   93   N  N     . ARG A 1 36  ? -24.943 -7.710  19.645 1.00 19.71 ? 43  ARG A N     1 
ATOM   94   C  CA    . ARG A 1 36  ? -24.683 -6.580  20.525 1.00 19.18 ? 43  ARG A CA    1 
ATOM   95   C  C     . ARG A 1 36  ? -25.326 -6.741  21.894 1.00 19.02 ? 43  ARG A C     1 
ATOM   96   O  O     . ARG A 1 36  ? -25.148 -5.872  22.754 1.00 20.77 ? 43  ARG A O     1 
ATOM   97   C  CB    . ARG A 1 36  ? -25.154 -5.272  19.873 1.00 16.87 ? 43  ARG A CB    1 
ATOM   98   C  CG    . ARG A 1 36  ? -24.162 -4.707  18.861 1.00 18.06 ? 43  ARG A CG    1 
ATOM   99   C  CD    . ARG A 1 36  ? -24.588 -3.338  18.345 1.00 17.44 ? 43  ARG A CD    1 
ATOM   100  N  NE    . ARG A 1 36  ? -23.674 -2.811  17.336 1.00 16.60 ? 43  ARG A NE    1 
ATOM   101  C  CZ    . ARG A 1 36  ? -22.676 -1.974  17.590 1.00 20.65 ? 43  ARG A CZ    1 
ATOM   102  N  NH1   . ARG A 1 36  ? -22.427 -1.547  18.817 1.00 17.76 ? 43  ARG A NH1   1 
ATOM   103  N  NH2   . ARG A 1 36  ? -21.909 -1.555  16.586 1.00 16.87 ? 43  ARG A NH2   1 
ATOM   104  N  N     . LYS A 1 37  ? -26.034 -7.829  22.122 1.00 18.32 ? 44  LYS A N     1 
ATOM   105  C  CA    . LYS A 1 37  ? -26.588 -8.077  23.430 1.00 19.43 ? 44  LYS A CA    1 
ATOM   106  C  C     . LYS A 1 37  ? -25.550 -8.600  24.396 1.00 18.36 ? 44  LYS A C     1 
ATOM   107  O  O     . LYS A 1 37  ? -24.603 -9.233  23.989 1.00 21.61 ? 44  LYS A O     1 
ATOM   108  C  CB    . LYS A 1 37  ? -27.772 -9.032  23.362 1.00 20.05 ? 44  LYS A CB    1 
ATOM   109  C  CG    . LYS A 1 37  ? -29.056 -8.423  22.839 1.00 29.11 ? 44  LYS A CG    1 
ATOM   110  C  CD    . LYS A 1 37  ? -30.152 -9.467  22.728 1.00 29.89 ? 44  LYS A CD    1 
ATOM   111  C  CE    . LYS A 1 37  ? -30.397 -10.173 24.051 1.00 30.02 ? 44  LYS A CE    1 
ATOM   112  N  NZ    . LYS A 1 37  ? -30.895 -9.246  25.100 1.00 31.75 ? 44  LYS A NZ    1 
ATOM   113  N  N     . CYS A 1 38  ? -25.695 -8.301  25.668 1.00 16.05 ? 45  CYS A N     1 
ATOM   114  C  CA    . CYS A 1 38  ? -24.808 -8.802  26.696 1.00 17.06 ? 45  CYS A CA    1 
ATOM   115  C  C     . CYS A 1 38  ? -25.552 -8.983  27.993 1.00 16.32 ? 45  CYS A C     1 
ATOM   116  O  O     . CYS A 1 38  ? -26.593 -8.398  28.176 1.00 19.62 ? 45  CYS A O     1 
ATOM   117  C  CB    . CYS A 1 38  ? -23.609 -7.846  26.944 1.00 15.58 ? 45  CYS A CB    1 
ATOM   118  S  SG    . CYS A 1 38  ? -22.321 -8.348  28.089 1.00 19.03 ? 45  CYS A SG    1 
ATOM   119  N  N     . ASN A 1 39  ? -24.981 -9.736  28.905 1.00 15.08 ? 46  ASN A N     1 
ATOM   120  C  CA    . ASN A 1 39  ? -25.554 -9.969  30.222 1.00 16.73 ? 46  ASN A CA    1 
ATOM   121  C  C     . ASN A 1 39  ? -24.873 -9.165  31.324 1.00 16.05 ? 46  ASN A C     1 
ATOM   122  O  O     . ASN A 1 39  ? -25.216 -9.345  32.495 1.00 25.02 ? 46  ASN A O     1 
ATOM   123  C  CB    . ASN A 1 39  ? -25.497 -11.460 30.568 1.00 16.84 ? 46  ASN A CB    1 
ATOM   124  C  CG    . ASN A 1 39  ? -24.087 -12.006 30.545 1.00 19.79 ? 46  ASN A CG    1 
ATOM   125  O  OD1   . ASN A 1 39  ? -23.250 -11.563 29.762 1.00 22.46 ? 46  ASN A OD1   1 
ATOM   126  N  ND2   . ASN A 1 39  ? -23.816 -12.974 31.412 1.00 20.90 ? 46  ASN A ND2   1 
ATOM   127  N  N     . LYS A 1 40  ? -23.925 -8.289  30.985 1.00 22.21 ? 47  LYS A N     1 
ATOM   128  C  CA    . LYS A 1 40  ? -23.208 -7.462  31.951 1.00 21.31 ? 47  LYS A CA    1 
ATOM   129  C  C     . LYS A 1 40  ? -23.287 -5.999  31.520 1.00 19.01 ? 47  LYS A C     1 
ATOM   130  O  O     . LYS A 1 40  ? -23.859 -5.665  30.477 1.00 18.17 ? 47  LYS A O     1 
ATOM   131  C  CB    . LYS A 1 40  ? -21.749 -7.913  32.096 1.00 17.45 ? 47  LYS A CB    1 
ATOM   132  C  CG    . LYS A 1 40  ? -21.577 -9.407  32.336 1.00 18.92 ? 47  LYS A CG    1 
ATOM   133  C  CD    . LYS A 1 40  ? -22.038 -9.794  33.729 1.00 21.03 ? 47  LYS A CD    1 
ATOM   134  C  CE    . LYS A 1 40  ? -21.950 -11.293 33.954 1.00 18.57 ? 47  LYS A CE    1 
ATOM   135  N  NZ    . LYS A 1 40  ? -21.445 -11.612 35.314 1.00 20.35 ? 47  LYS A NZ    1 
ATOM   136  N  N     . SER A 1 41  ? -22.698 -5.107  32.324 1.00 18.31 ? 48  SER A N     1 
ATOM   137  C  CA    . SER A 1 41  ? -22.804 -3.675  32.050 1.00 20.98 ? 48  SER A CA    1 
ATOM   138  C  C     . SER A 1 41  ? -21.527 -2.987  32.535 1.00 21.42 ? 48  SER A C     1 
ATOM   139  O  O     . SER A 1 41  ? -21.512 -2.223  33.504 1.00 22.44 ? 48  SER A O     1 
ATOM   140  C  CB    . SER A 1 41  ? -24.046 -3.072  32.708 1.00 26.35 ? 48  SER A CB    1 
ATOM   141  O  OG    . SER A 1 41  ? -24.301 -3.721  33.937 1.00 22.67 ? 48  SER A OG    1 
ATOM   142  N  N     . CYS A 1 42  ? -20.426 -3.287  31.851 1.00 18.71 ? 49  CYS A N     1 
ATOM   143  C  CA    . CYS A 1 42  ? -19.176 -2.593  32.118 1.00 15.16 ? 49  CYS A CA    1 
ATOM   144  C  C     . CYS A 1 42  ? -19.309 -1.139  31.696 1.00 16.66 ? 49  CYS A C     1 
ATOM   145  O  O     . CYS A 1 42  ? -19.793 -0.841  30.602 1.00 16.81 ? 49  CYS A O     1 
ATOM   146  C  CB    . CYS A 1 42  ? -18.010 -3.271  31.391 1.00 14.86 ? 49  CYS A CB    1 
ATOM   147  S  SG    . CYS A 1 42  ? -18.102 -5.076  31.252 1.00 15.68 ? 49  CYS A SG    1 
ATOM   148  N  N     . GLY A 1 43  ? -18.898 -0.230  32.580 1.00 16.18 ? 50  GLY A N     1 
ATOM   149  C  CA    . GLY A 1 43  ? -19.154 1.179   32.353 1.00 15.65 ? 50  GLY A CA    1 
ATOM   150  C  C     . GLY A 1 43  ? -18.422 1.767   31.166 1.00 16.88 ? 50  GLY A C     1 
ATOM   151  O  O     . GLY A 1 43  ? -18.826 2.821   30.661 1.00 16.56 ? 50  GLY A O     1 
ATOM   152  N  N     . PHE A 1 44  ? -17.357 1.113   30.705 1.00 13.53 ? 51  PHE A N     1 
ATOM   153  C  CA    . PHE A 1 44  ? -16.521 1.662   29.648 1.00 17.24 ? 51  PHE A CA    1 
ATOM   154  C  C     . PHE A 1 44  ? -16.776 1.044   28.281 1.00 18.34 ? 51  PHE A C     1 
ATOM   155  O  O     . PHE A 1 44  ? -16.068 1.391   27.331 1.00 15.84 ? 51  PHE A O     1 
ATOM   156  C  CB    . PHE A 1 44  ? -15.040 1.495   29.998 1.00 12.45 ? 51  PHE A CB    1 
ATOM   157  C  CG    . PHE A 1 44  ? -14.676 0.114   30.472 1.00 12.22 ? 51  PHE A CG    1 
ATOM   158  C  CD1   . PHE A 1 44  ? -14.749 -0.977  29.619 1.00 9.66  ? 51  PHE A CD1   1 
ATOM   159  C  CD2   . PHE A 1 44  ? -14.249 -0.088  31.769 1.00 9.93  ? 51  PHE A CD2   1 
ATOM   160  C  CE1   . PHE A 1 44  ? -14.412 -2.239  30.064 1.00 11.28 ? 51  PHE A CE1   1 
ATOM   161  C  CE2   . PHE A 1 44  ? -13.908 -1.343  32.216 1.00 10.72 ? 51  PHE A CE2   1 
ATOM   162  C  CZ    . PHE A 1 44  ? -13.990 -2.420  31.367 1.00 10.01 ? 51  PHE A CZ    1 
ATOM   163  N  N     . CYS A 1 45  ? -17.748 0.140   28.162 1.00 15.27 ? 52  CYS A N     1 
ATOM   164  C  CA    . CYS A 1 45  ? -17.979 -0.617  26.932 1.00 18.16 ? 52  CYS A CA    1 
ATOM   165  C  C     . CYS A 1 45  ? -18.030 0.273   25.696 1.00 15.65 ? 52  CYS A C     1 
ATOM   166  O  O     . CYS A 1 45  ? -18.825 1.217   25.623 1.00 16.98 ? 52  CYS A O     1 
ATOM   167  C  CB    . CYS A 1 45  ? -19.283 -1.409  27.046 1.00 14.96 ? 52  CYS A CB    1 
ATOM   168  S  SG    . CYS A 1 45  ? -19.450 -2.718  25.809 1.00 14.58 ? 52  CYS A SG    1 
ATOM   169  N  N     . PHE A 1 46  ? -17.192 -0.058  24.709 1.00 12.33 ? 53  PHE A N     1 
ATOM   170  C  CA    . PHE A 1 46  ? -17.164 0.628   23.424 1.00 12.43 ? 53  PHE A CA    1 
ATOM   171  C  C     . PHE A 1 46  ? -17.850 -0.171  22.318 1.00 14.12 ? 53  PHE A C     1 
ATOM   172  O  O     . PHE A 1 46  ? -17.585 0.063   21.134 1.00 15.80 ? 53  PHE A O     1 
ATOM   173  C  CB    . PHE A 1 46  ? -15.723 0.992   23.031 1.00 16.37 ? 53  PHE A CB    1 
ATOM   174  C  CG    . PHE A 1 46  ? -14.765 -0.186  22.873 1.00 11.37 ? 53  PHE A CG    1 
ATOM   175  C  CD1   . PHE A 1 46  ? -15.183 -1.509  22.949 1.00 13.65 ? 53  PHE A CD1   1 
ATOM   176  C  CD2   . PHE A 1 46  ? -13.422 0.060   22.624 1.00 13.56 ? 53  PHE A CD2   1 
ATOM   177  C  CE1   . PHE A 1 46  ? -14.282 -2.554  22.791 1.00 14.92 ? 53  PHE A CE1   1 
ATOM   178  C  CE2   . PHE A 1 46  ? -12.520 -0.979  22.466 1.00 15.49 ? 53  PHE A CE2   1 
ATOM   179  C  CZ    . PHE A 1 46  ? -12.951 -2.288  22.549 1.00 16.21 ? 53  PHE A CZ    1 
ATOM   180  N  N     . HIS A 1 47  ? -18.725 -1.115  22.685 1.00 14.12 ? 54  HIS A N     1 
ATOM   181  C  CA    . HIS A 1 47  ? -19.536 -1.864  21.725 1.00 17.64 ? 54  HIS A CA    1 
ATOM   182  C  C     . HIS A 1 47  ? -20.871 -2.161  22.418 1.00 17.63 ? 54  HIS A C     1 
ATOM   183  O  O     . HIS A 1 47  ? -21.129 -3.266  22.899 1.00 18.79 ? 54  HIS A O     1 
ATOM   184  C  CB    . HIS A 1 47  ? -18.841 -3.141  21.254 1.00 18.57 ? 54  HIS A CB    1 
ATOM   185  C  CG    . HIS A 1 47  ? -19.329 -3.631  19.928 1.00 17.45 ? 54  HIS A CG    1 
ATOM   186  N  ND1   . HIS A 1 47  ? -18.946 -3.056  18.736 1.00 19.56 ? 54  HIS A ND1   1 
ATOM   187  C  CD2   . HIS A 1 47  ? -20.182 -4.631  19.606 1.00 18.12 ? 54  HIS A CD2   1 
ATOM   188  C  CE1   . HIS A 1 47  ? -19.540 -3.682  17.736 1.00 19.96 ? 54  HIS A CE1   1 
ATOM   189  N  NE2   . HIS A 1 47  ? -20.296 -4.642  18.237 1.00 17.74 ? 54  HIS A NE2   1 
ATOM   190  N  N     . THR A 1 48  ? -21.735 -1.149  22.457 1.00 16.36 ? 55  THR A N     1 
ATOM   191  C  CA    . THR A 1 48  ? -22.929 -1.168  23.291 1.00 19.78 ? 55  THR A CA    1 
ATOM   192  C  C     . THR A 1 48  ? -24.097 -1.877  22.599 1.00 20.56 ? 55  THR A C     1 
ATOM   193  O  O     . THR A 1 48  ? -24.082 -2.135  21.395 1.00 18.88 ? 55  THR A O     1 
ATOM   194  C  CB    . THR A 1 48  ? -23.322 0.261   23.679 1.00 22.03 ? 55  THR A CB    1 
ATOM   195  O  OG1   . THR A 1 48  ? -23.459 1.059   22.496 1.00 18.14 ? 55  THR A OG1   1 
ATOM   196  C  CG2   . THR A 1 48  ? -22.260 0.884   24.588 1.00 18.80 ? 55  THR A CG2   1 
ATOM   197  N  N     . ALA A 1 49  ? -25.128 -2.187  23.390 1.00 17.32 ? 56  ALA A N     1 
ATOM   198  C  CA    . ALA A 1 49  ? -26.298 -2.933  22.918 1.00 21.94 ? 56  ALA A CA    1 
ATOM   199  C  C     . ALA A 1 49  ? -27.257 -2.037  22.131 1.00 24.45 ? 56  ALA A C     1 
ATOM   200  O  O     . ALA A 1 49  ? -28.396 -1.789  22.523 1.00 25.47 ? 56  ALA A O     1 
ATOM   201  C  CB    . ALA A 1 49  ? -27.013 -3.592  24.091 1.00 17.83 ? 56  ALA A CB    1 
ATOM   202  N  N     . LYS A 1 50  ? -26.782 -1.564  20.979 1.00 21.67 ? 57  LYS A N     1 
ATOM   203  C  CA    . LYS A 1 50  ? -27.600 -0.666  20.170 1.00 23.25 ? 57  LYS A CA    1 
ATOM   204  C  C     . LYS A 1 50  ? -28.738 -1.415  19.483 1.00 28.33 ? 57  LYS A C     1 
ATOM   205  O  O     . LYS A 1 50  ? -29.839 -0.874  19.324 1.00 26.15 ? 57  LYS A O     1 
ATOM   206  C  CB    . LYS A 1 50  ? -26.725 0.045   19.140 1.00 23.71 ? 57  LYS A CB    1 
ATOM   207  C  CG    . LYS A 1 50  ? -25.588 0.839   19.758 1.00 21.15 ? 57  LYS A CG    1 
ATOM   208  C  CD    . LYS A 1 50  ? -24.773 1.553   18.694 1.00 16.65 ? 57  LYS A CD    1 
ATOM   209  C  CE    . LYS A 1 50  ? -24.399 2.958   19.136 1.00 20.67 ? 57  LYS A CE    1 
ATOM   210  N  NZ    . LYS A 1 50  ? -23.239 3.509   18.380 1.00 20.60 ? 57  LYS A NZ    1 
ATOM   211  N  N     . THR A 1 51  ? -28.491 -2.655  19.058 1.00 25.35 ? 58  THR A N     1 
ATOM   212  C  CA    . THR A 1 51  ? -29.487 -3.462  18.369 1.00 28.05 ? 58  THR A CA    1 
ATOM   213  C  C     . THR A 1 51  ? -29.522 -4.864  18.957 1.00 28.33 ? 58  THR A C     1 
ATOM   214  O  O     . THR A 1 51  ? -28.504 -5.392  19.412 1.00 27.21 ? 58  THR A O     1 
ATOM   215  C  CB    . THR A 1 51  ? -29.206 -3.571  16.855 1.00 28.43 ? 58  THR A CB    1 
ATOM   216  O  OG1   . THR A 1 51  ? -28.013 -4.335  16.640 1.00 28.54 ? 58  THR A OG1   1 
ATOM   217  C  CG2   . THR A 1 51  ? -29.049 -2.194  16.224 1.00 24.26 ? 58  THR A CG2   1 
ATOM   218  N  N     . SER A 1 52  ? -30.652 -5.516  18.787 1.00 27.47 ? 59  SER A N     1 
ATOM   219  C  CA    . SER A 1 52  ? -30.766 -6.895  19.169 1.00 27.95 ? 59  SER A CA    1 
ATOM   220  C  C     . SER A 1 52  ? -30.662 -7.687  17.870 1.00 29.89 ? 59  SER A C     1 
ATOM   221  O  O     . SER A 1 52  ? -30.767 -8.897  17.875 1.00 33.67 ? 59  SER A O     1 
ATOM   222  C  CB    . SER A 1 52  ? -32.095 -7.136  19.822 1.00 24.43 ? 59  SER A CB    1 
ATOM   223  O  OG    . SER A 1 52  ? -32.441 -6.080  20.699 1.00 31.83 ? 59  SER A OG    1 
ATOM   224  N  N     . HIS A 1 53  ? -30.449 -6.998  16.756 1.00 22.13 ? 60  HIS A N     1 
ATOM   225  C  CA    . HIS A 1 53  ? -30.394 -7.672  15.470 1.00 26.87 ? 60  HIS A CA    1 
ATOM   226  C  C     . HIS A 1 53  ? -29.239 -8.660  15.423 1.00 28.28 ? 60  HIS A C     1 
ATOM   227  O  O     . HIS A 1 53  ? -28.137 -8.390  15.914 1.00 30.18 ? 60  HIS A O     1 
ATOM   228  C  CB    . HIS A 1 53  ? -30.249 -6.670  14.327 1.00 28.47 ? 60  HIS A CB    1 
ATOM   229  C  CG    . HIS A 1 53  ? -29.955 -7.313  13.006 1.00 27.75 ? 60  HIS A CG    1 
ATOM   230  N  ND1   . HIS A 1 53  ? -30.946 -7.760  12.159 1.00 30.22 ? 60  HIS A ND1   1 
ATOM   231  C  CD2   . HIS A 1 53  ? -28.781 -7.612  12.402 1.00 29.57 ? 60  HIS A CD2   1 
ATOM   232  C  CE1   . HIS A 1 53  ? -30.396 -8.291  11.082 1.00 31.77 ? 60  HIS A CE1   1 
ATOM   233  N  NE2   . HIS A 1 53  ? -29.083 -8.215  11.205 1.00 31.68 ? 60  HIS A NE2   1 
ATOM   234  N  N     . MET A 1 54  ? -29.461 -9.718  14.679 1.00 26.72 ? 61  MET A N     1 
ATOM   235  C  CA    . MET A 1 54  ? -28.471 -10.737 14.544 1.00 26.58 ? 61  MET A CA    1 
ATOM   236  C  C     . MET A 1 54  ? -28.662 -11.300 13.171 1.00 25.88 ? 61  MET A C     1 
ATOM   237  O  O     . MET A 1 54  ? -29.770 -11.465 12.716 1.00 25.72 ? 61  MET A O     1 
ATOM   238  C  CB    . MET A 1 54  ? -28.672 -11.811 15.603 1.00 27.56 ? 61  MET A CB    1 
ATOM   239  C  CG    . MET A 1 54  ? -27.474 -12.671 15.904 1.00 28.14 ? 61  MET A CG    1 
ATOM   240  S  SD    . MET A 1 54  ? -27.828 -13.590 17.400 1.00 38.97 ? 61  MET A SD    1 
ATOM   241  C  CE    . MET A 1 54  ? -27.030 -15.146 17.059 1.00 23.31 ? 61  MET A CE    1 
ATOM   242  N  N     . GLU A 1 55  ? -27.565 -11.627 12.526 1.00 25.76 ? 62  GLU A N     1 
ATOM   243  C  CA    . GLU A 1 55  ? -27.617 -12.140 11.170 1.00 28.57 ? 62  GLU A CA    1 
ATOM   244  C  C     . GLU A 1 55  ? -28.094 -13.589 11.174 1.00 30.95 ? 62  GLU A C     1 
ATOM   245  O  O     . GLU A 1 55  ? -28.032 -14.292 12.186 1.00 27.71 ? 62  GLU A O     1 
ATOM   246  C  CB    . GLU A 1 55  ? -26.246 -12.028 10.505 1.00 28.77 ? 62  GLU A CB    1 
ATOM   247  C  CG    . GLU A 1 55  ? -26.290 -11.863 8.996  1.00 29.77 ? 62  GLU A CG    1 
ATOM   248  C  CD    . GLU A 1 55  ? -27.341 -10.869 8.541  1.00 29.02 ? 62  GLU A CD    1 
ATOM   249  O  OE1   . GLU A 1 55  ? -27.274 -9.690  8.950  1.00 32.60 ? 62  GLU A OE1   1 
ATOM   250  O  OE2   . GLU A 1 55  ? -28.242 -11.271 7.776  1.00 32.49 ? 62  GLU A OE2   1 
ATOM   251  N  N     . ASP A 1 56  ? -28.577 -14.049 10.027 1.00 32.54 ? 63  ASP A N     1 
ATOM   252  C  CA    . ASP A 1 56  ? -29.001 -15.440 9.901  1.00 31.08 ? 63  ASP A CA    1 
ATOM   253  C  C     . ASP A 1 56  ? -27.798 -16.301 9.701  1.00 28.21 ? 63  ASP A C     1 
ATOM   254  O  O     . ASP A 1 56  ? -26.774 -15.833 9.240  1.00 25.49 ? 63  ASP A O     1 
ATOM   255  C  CB    . ASP A 1 56  ? -29.992 -15.643 8.755  1.00 29.30 ? 63  ASP A CB    1 
ATOM   256  C  CG    . ASP A 1 56  ? -30.705 -16.949 8.828  1.00 30.07 ? 63  ASP A CG    1 
ATOM   257  O  OD1   . ASP A 1 56  ? -31.646 -17.060 9.631  1.00 31.90 ? 63  ASP A OD1   1 
ATOM   258  O  OD2   . ASP A 1 56  ? -30.333 -17.859 8.069  1.00 34.76 ? 63  ASP A OD2   1 
ATOM   259  N  N     . ILE A 1 57  ? -27.933 -17.565 10.070 1.00 26.97 ? 64  ILE A N     1 
ATOM   260  C  CA    . ILE A 1 57  ? -26.800 -18.484 10.010 1.00 26.21 ? 64  ILE A CA    1 
ATOM   261  C  C     . ILE A 1 57  ? -26.357 -18.723 8.572  1.00 28.15 ? 64  ILE A C     1 
ATOM   262  O  O     . ILE A 1 57  ? -25.169 -18.947 8.312  1.00 28.15 ? 64  ILE A O     1 
ATOM   263  C  CB    . ILE A 1 57  ? -27.139 -19.805 10.732 1.00 25.64 ? 64  ILE A CB    1 
ATOM   264  C  CG1   . ILE A 1 57  ? -25.866 -20.612 10.997 1.00 27.81 ? 64  ILE A CG1   1 
ATOM   265  C  CG2   . ILE A 1 57  ? -28.138 -20.627 9.937  1.00 31.62 ? 64  ILE A CG2   1 
ATOM   266  C  CD1   . ILE A 1 57  ? -25.107 -20.179 12.220 1.00 23.64 ? 64  ILE A CD1   1 
ATOM   267  N  N     . SER A 1 58  ? -27.286 -18.663 7.614  1.00 27.24 ? 65  SER A N     1 
ATOM   268  C  CA    . SER A 1 58  ? -26.895 -18.782 6.214  1.00 26.87 ? 65  SER A CA    1 
ATOM   269  C  C     . SER A 1 58  ? -26.137 -17.543 5.752  1.00 25.96 ? 65  SER A C     1 
ATOM   270  O  O     . SER A 1 58  ? -25.156 -17.649 5.006  1.00 26.59 ? 65  SER A O     1 
ATOM   271  C  CB    . SER A 1 58  ? -28.127 -19.017 5.340  1.00 25.52 ? 65  SER A CB    1 
ATOM   272  O  OG    . SER A 1 58  ? -29.256 -19.341 6.131  1.00 34.93 ? 65  SER A OG    1 
ATOM   273  N  N     . ARG A 1 59  ? -26.571 -16.360 6.195  1.00 26.37 ? 66  ARG A N     1 
ATOM   274  C  CA    . ARG A 1 59  ? -25.899 -15.128 5.797  1.00 27.87 ? 66  ARG A CA    1 
ATOM   275  C  C     . ARG A 1 59  ? -24.549 -14.982 6.490  1.00 26.49 ? 66  ARG A C     1 
ATOM   276  O  O     . ARG A 1 59  ? -23.573 -14.540 5.872  1.00 27.61 ? 66  ARG A O     1 
ATOM   277  C  CB    . ARG A 1 59  ? -26.793 -13.925 6.100  1.00 27.88 ? 66  ARG A CB    1 
ATOM   278  C  CG    . ARG A 1 59  ? -28.271 -14.163 5.836  1.00 29.74 ? 66  ARG A CG    1 
ATOM   279  C  CD    . ARG A 1 59  ? -28.809 -13.168 4.823  1.00 30.24 ? 66  ARG A CD    1 
ATOM   280  N  NE    . ARG A 1 59  ? -28.378 -11.807 5.120  1.00 29.55 ? 66  ARG A NE    1 
ATOM   281  C  CZ    . ARG A 1 59  ? -28.313 -10.829 4.226  1.00 27.83 ? 66  ARG A CZ    1 
ATOM   282  N  NH1   . ARG A 1 59  ? -28.628 -11.029 2.957  1.00 27.04 ? 66  ARG A NH1   1 
ATOM   283  N  NH2   . ARG A 1 59  ? -27.920 -9.619  4.616  1.00 20.66 ? 66  ARG A NH2   1 
ATOM   284  N  N     . ALA A 1 60  ? -24.475 -15.347 7.773  1.00 24.20 ? 67  ALA A N     1 
ATOM   285  C  CA    . ALA A 1 60  ? -23.211 -15.273 8.500  1.00 23.97 ? 67  ALA A CA    1 
ATOM   286  C  C     . ALA A 1 60  ? -22.181 -16.223 7.904  1.00 24.78 ? 67  ALA A C     1 
ATOM   287  O  O     . ALA A 1 60  ? -21.026 -15.844 7.680  1.00 22.45 ? 67  ALA A O     1 
ATOM   288  C  CB    . ALA A 1 60  ? -23.437 -15.583 9.980  1.00 19.97 ? 67  ALA A CB    1 
ATOM   289  N  N     . LYS A 1 61  ? -22.569 -17.448 7.644  1.00 25.73 ? 68  LYS A N     1 
ATOM   290  C  CA    . LYS A 1 61  ? -21.669 -18.365 7.003  1.00 22.76 ? 68  LYS A CA    1 
ATOM   291  C  C     . LYS A 1 61  ? -21.225 -17.845 5.638  1.00 23.92 ? 68  LYS A C     1 
ATOM   292  O  O     . LYS A 1 61  ? -20.081 -18.000 5.275  1.00 23.84 ? 68  LYS A O     1 
ATOM   293  C  CB    . LYS A 1 61  ? -22.333 -19.723 6.896  1.00 25.19 ? 68  LYS A CB    1 
ATOM   294  C  CG    . LYS A 1 61  ? -22.364 -20.543 8.156  1.00 23.93 ? 68  LYS A CG    1 
ATOM   295  C  CD    . LYS A 1 61  ? -23.035 -21.859 7.844  1.00 26.84 ? 68  LYS A CD    1 
ATOM   296  C  CE    . LYS A 1 61  ? -22.969 -22.815 9.012  1.00 25.61 ? 68  LYS A CE    1 
ATOM   297  N  NZ    . LYS A 1 61  ? -23.573 -24.113 8.634  1.00 26.89 ? 68  LYS A NZ    1 
ATOM   298  N  N     . ARG A 1 62  ? -22.138 -17.219 4.894  1.00 24.88 ? 69  ARG A N     1 
ATOM   299  C  CA    . ARG A 1 62  ? -21.769 -16.641 3.606  1.00 26.29 ? 69  ARG A CA    1 
ATOM   300  C  C     . ARG A 1 62  ? -20.816 -15.466 3.781  1.00 24.81 ? 69  ARG A C     1 
ATOM   301  O  O     . ARG A 1 62  ? -19.897 -15.280 2.976  1.00 21.27 ? 69  ARG A O     1 
ATOM   302  C  CB    . ARG A 1 62  ? -23.026 -16.211 2.850  1.00 23.07 ? 69  ARG A CB    1 
ATOM   303  C  CG    . ARG A 1 62  ? -22.762 -15.639 1.470  1.00 24.54 ? 69  ARG A CG    1 
ATOM   304  C  CD    . ARG A 1 62  ? -23.988 -15.773 0.586  1.00 27.46 ? 69  ARG A CD    1 
ATOM   305  N  NE    . ARG A 1 62  ? -25.046 -14.843 0.962  1.00 21.84 ? 69  ARG A NE    1 
ATOM   306  C  CZ    . ARG A 1 62  ? -25.106 -13.580 0.564  1.00 24.61 ? 69  ARG A CZ    1 
ATOM   307  N  NH1   . ARG A 1 62  ? -24.175 -13.056 -0.217 1.00 25.21 ? 69  ARG A NH1   1 
ATOM   308  N  NH2   . ARG A 1 62  ? -26.130 -12.825 0.953  1.00 23.53 ? 69  ARG A NH2   1 
ATOM   309  N  N     . GLY A 1 63  ? -21.019 -14.663 4.826  1.00 25.61 ? 70  GLY A N     1 
ATOM   310  C  CA    . GLY A 1 63  ? -20.097 -13.572 5.096  1.00 25.91 ? 70  GLY A CA    1 
ATOM   311  C  C     . GLY A 1 63  ? -18.724 -14.065 5.511  1.00 19.10 ? 70  GLY A C     1 
ATOM   312  O  O     . GLY A 1 63  ? -17.703 -13.521 5.079  1.00 21.69 ? 70  GLY A O     1 
ATOM   313  N  N     . LEU A 1 64  ? -18.679 -15.102 6.351  1.00 18.29 ? 71  LEU A N     1 
ATOM   314  C  CA    . LEU A 1 64  ? -17.401 -15.699 6.726  1.00 21.45 ? 71  LEU A CA    1 
ATOM   315  C  C     . LEU A 1 64  ? -16.724 -16.362 5.534  1.00 24.03 ? 71  LEU A C     1 
ATOM   316  O  O     . LEU A 1 64  ? -15.490 -16.386 5.456  1.00 22.40 ? 71  LEU A O     1 
ATOM   317  C  CB    . LEU A 1 64  ? -17.606 -16.704 7.857  1.00 19.70 ? 71  LEU A CB    1 
ATOM   318  C  CG    . LEU A 1 64  ? -18.012 -16.093 9.199  1.00 21.19 ? 71  LEU A CG    1 
ATOM   319  C  CD1   . LEU A 1 64  ? -18.508 -17.159 10.163 1.00 24.93 ? 71  LEU A CD1   1 
ATOM   320  C  CD2   . LEU A 1 64  ? -16.858 -15.309 9.806  1.00 22.83 ? 71  LEU A CD2   1 
ATOM   321  N  N     . GLN A 1 65  ? -17.508 -16.906 4.602  1.00 22.84 ? 72  GLN A N     1 
ATOM   322  C  CA    . GLN A 1 65  ? -16.931 -17.423 3.365  1.00 22.14 ? 72  GLN A CA    1 
ATOM   323  C  C     . GLN A 1 65  ? -16.379 -16.295 2.505  1.00 23.58 ? 72  GLN A C     1 
ATOM   324  O  O     . GLN A 1 65  ? -15.304 -16.432 1.908  1.00 27.00 ? 72  GLN A O     1 
ATOM   325  C  CB    . GLN A 1 65  ? -17.974 -18.218 2.583  1.00 27.97 ? 72  GLN A CB    1 
ATOM   326  C  CG    . GLN A 1 65  ? -17.401 -19.026 1.430  1.00 23.88 ? 72  GLN A CG    1 
ATOM   327  C  CD    . GLN A 1 65  ? -18.315 -20.158 1.006  1.00 29.26 ? 72  GLN A CD    1 
ATOM   328  O  OE1   . GLN A 1 65  ? -19.538 -20.044 1.086  1.00 35.60 ? 72  GLN A OE1   1 
ATOM   329  N  NE2   . GLN A 1 65  ? -17.727 -21.257 0.547  1.00 31.82 ? 72  GLN A NE2   1 
ATOM   330  N  N     . LEU A 1 66  ? -17.108 -15.181 2.415  1.00 21.17 ? 73  LEU A N     1 
ATOM   331  C  CA    . LEU A 1 66  ? -16.620 -14.040 1.646  1.00 21.17 ? 73  LEU A CA    1 
ATOM   332  C  C     . LEU A 1 66  ? -15.291 -13.539 2.193  1.00 23.71 ? 73  LEU A C     1 
ATOM   333  O  O     . LEU A 1 66  ? -14.369 -13.235 1.427  1.00 25.66 ? 73  LEU A O     1 
ATOM   334  C  CB    . LEU A 1 66  ? -17.655 -12.918 1.654  1.00 22.02 ? 73  LEU A CB    1 
ATOM   335  C  CG    . LEU A 1 66  ? -18.573 -12.779 0.441  1.00 23.87 ? 73  LEU A CG    1 
ATOM   336  C  CD1   . LEU A 1 66  ? -19.082 -14.135 -0.029 1.00 24.38 ? 73  LEU A CD1   1 
ATOM   337  C  CD2   . LEU A 1 66  ? -19.727 -11.854 0.777  1.00 21.98 ? 73  LEU A CD2   1 
ATOM   338  N  N     . LEU A 1 67  ? -15.172 -13.453 3.520  1.00 23.12 ? 74  LEU A N     1 
ATOM   339  C  CA    . LEU A 1 67  ? -13.929 -12.984 4.121  1.00 21.03 ? 74  LEU A CA    1 
ATOM   340  C  C     . LEU A 1 67  ? -12.811 -14.007 3.972  1.00 21.07 ? 74  LEU A C     1 
ATOM   341  O  O     . LEU A 1 67  ? -11.641 -13.627 3.849  1.00 22.96 ? 74  LEU A O     1 
ATOM   342  C  CB    . LEU A 1 67  ? -14.158 -12.643 5.593  1.00 18.77 ? 74  LEU A CB    1 
ATOM   343  C  CG    . LEU A 1 67  ? -15.044 -11.418 5.836  1.00 21.11 ? 74  LEU A CG    1 
ATOM   344  C  CD1   . LEU A 1 67  ? -15.626 -11.426 7.242  1.00 18.65 ? 74  LEU A CD1   1 
ATOM   345  C  CD2   . LEU A 1 67  ? -14.270 -10.129 5.583  1.00 15.83 ? 74  LEU A CD2   1 
ATOM   346  N  N     . GLN A 1 68  ? -13.144 -15.299 3.980  1.00 21.69 ? 75  GLN A N     1 
ATOM   347  C  CA    . GLN A 1 68  ? -12.140 -16.324 3.713  1.00 19.14 ? 75  GLN A CA    1 
ATOM   348  C  C     . GLN A 1 68  ? -11.562 -16.164 2.313  1.00 23.08 ? 75  GLN A C     1 
ATOM   349  O  O     . GLN A 1 68  ? -10.343 -16.244 2.116  1.00 24.12 ? 75  GLN A O     1 
ATOM   350  C  CB    . GLN A 1 68  ? -12.754 -17.716 3.884  1.00 21.84 ? 75  GLN A CB    1 
ATOM   351  C  CG    . GLN A 1 68  ? -11.739 -18.848 3.997  1.00 24.02 ? 75  GLN A CG    1 
ATOM   352  C  CD    . GLN A 1 68  ? -11.168 -19.264 2.658  1.00 25.87 ? 75  GLN A CD    1 
ATOM   353  O  OE1   . GLN A 1 68  ? -11.877 -19.299 1.653  1.00 29.08 ? 75  GLN A OE1   1 
ATOM   354  N  NE2   . GLN A 1 68  ? -9.876  -19.571 2.634  1.00 25.24 ? 75  GLN A NE2   1 
ATOM   355  N  N     . ARG A 1 69  ? -12.429 -15.940 1.322  1.00 22.61 ? 76  ARG A N     1 
ATOM   356  C  CA    . ARG A 1 69  ? -11.977 -15.809 -0.058 1.00 23.83 ? 76  ARG A CA    1 
ATOM   357  C  C     . ARG A 1 69  ? -11.160 -14.544 -0.285 1.00 23.66 ? 76  ARG A C     1 
ATOM   358  O  O     . ARG A 1 69  ? -10.417 -14.470 -1.268 1.00 27.37 ? 76  ARG A O     1 
ATOM   359  C  CB    . ARG A 1 69  ? -13.177 -15.837 -1.003 1.00 18.19 ? 76  ARG A CB    1 
ATOM   360  C  CG    . ARG A 1 69  ? -13.792 -17.214 -1.155 1.00 23.01 ? 76  ARG A CG    1 
ATOM   361  C  CD    . ARG A 1 69  ? -15.001 -17.183 -2.075 1.00 28.47 ? 76  ARG A CD    1 
ATOM   362  N  NE    . ARG A 1 69  ? -14.755 -16.401 -3.282 1.00 29.90 ? 76  ARG A NE    1 
ATOM   363  C  CZ    . ARG A 1 69  ? -13.992 -16.793 -4.294 1.00 31.00 ? 76  ARG A CZ    1 
ATOM   364  N  NH1   . ARG A 1 69  ? -13.385 -17.969 -4.289 1.00 28.13 ? 76  ARG A NH1   1 
ATOM   365  N  NH2   . ARG A 1 69  ? -13.834 -15.984 -5.338 1.00 35.84 ? 76  ARG A NH2   1 
ATOM   366  N  N     . ALA A 1 70  ? -11.277 -13.558 0.600  1.00 23.05 ? 77  ALA A N     1 
ATOM   367  C  CA    . ALA A 1 70  ? -10.495 -12.334 0.514  1.00 20.83 ? 77  ALA A CA    1 
ATOM   368  C  C     . ALA A 1 70  ? -9.170  -12.421 1.260  1.00 21.69 ? 77  ALA A C     1 
ATOM   369  O  O     . ALA A 1 70  ? -8.380  -11.474 1.197  1.00 20.47 ? 77  ALA A O     1 
ATOM   370  C  CB    . ALA A 1 70  ? -11.307 -11.152 1.046  1.00 24.24 ? 77  ALA A CB    1 
ATOM   371  N  N     . GLY A 1 71  ? -8.913  -13.516 1.972  1.00 20.40 ? 78  GLY A N     1 
ATOM   372  C  CA    . GLY A 1 71  ? -7.611  -13.720 2.576  1.00 17.94 ? 78  GLY A CA    1 
ATOM   373  C  C     . GLY A 1 71  ? -7.586  -13.818 4.087  1.00 23.71 ? 78  GLY A C     1 
ATOM   374  O  O     . GLY A 1 71  ? -6.504  -13.859 4.680  1.00 29.03 ? 78  GLY A O     1 
ATOM   375  N  N     . MET A 1 72  ? -8.750  -13.862 4.728  1.00 21.72 ? 79  MET A N     1 
ATOM   376  C  CA    . MET A 1 72  ? -8.784  -13.899 6.185  1.00 21.68 ? 79  MET A CA    1 
ATOM   377  C  C     . MET A 1 72  ? -8.303  -15.255 6.684  1.00 21.25 ? 79  MET A C     1 
ATOM   378  O  O     . MET A 1 72  ? -8.855  -16.295 6.313  1.00 22.95 ? 79  MET A O     1 
ATOM   379  C  CB    . MET A 1 72  ? -10.190 -13.608 6.701  1.00 23.82 ? 79  MET A CB    1 
ATOM   380  C  CG    . MET A 1 72  ? -10.417 -14.080 8.127  1.00 19.02 ? 79  MET A CG    1 
ATOM   381  S  SD    . MET A 1 72  ? -12.131 -13.940 8.667  1.00 20.39 ? 79  MET A SD    1 
ATOM   382  C  CE    . MET A 1 72  ? -12.905 -15.282 7.767  1.00 17.87 ? 79  MET A CE    1 
ATOM   383  N  N     . LYS A 1 73  ? -7.269  -15.242 7.521  1.00 21.28 ? 80  LYS A N     1 
ATOM   384  C  CA    . LYS A 1 73  ? -6.744  -16.461 8.118  1.00 23.52 ? 80  LYS A CA    1 
ATOM   385  C  C     . LYS A 1 73  ? -7.211  -16.671 9.549  1.00 21.24 ? 80  LYS A C     1 
ATOM   386  O  O     . LYS A 1 73  ? -7.298  -17.818 9.996  1.00 17.28 ? 80  LYS A O     1 
ATOM   387  C  CB    . LYS A 1 73  ? -5.213  -16.452 8.088  1.00 27.72 ? 80  LYS A CB    1 
ATOM   388  C  CG    . LYS A 1 73  ? -4.616  -16.207 6.711  1.00 23.37 ? 80  LYS A CG    1 
ATOM   389  C  CD    . LYS A 1 73  ? -5.204  -17.149 5.671  1.00 25.08 ? 80  LYS A CD    1 
ATOM   390  C  CE    . LYS A 1 73  ? -4.114  -17.776 4.812  1.00 29.56 ? 80  LYS A CE    1 
ATOM   391  N  NZ    . LYS A 1 73  ? -4.646  -18.325 3.532  1.00 30.12 ? 80  LYS A NZ    1 
ATOM   392  N  N     . LYS A 1 74  ? -7.514  -15.595 10.272 1.00 22.63 ? 81  LYS A N     1 
ATOM   393  C  CA    . LYS A 1 74  ? -7.959  -15.667 11.657 1.00 20.97 ? 81  LYS A CA    1 
ATOM   394  C  C     . LYS A 1 74  ? -9.306  -14.975 11.789 1.00 20.07 ? 81  LYS A C     1 
ATOM   395  O  O     . LYS A 1 74  ? -9.448  -13.807 11.411 1.00 20.52 ? 81  LYS A O     1 
ATOM   396  C  CB    . LYS A 1 74  ? -6.944  -15.023 12.602 1.00 19.07 ? 81  LYS A CB    1 
ATOM   397  C  CG    . LYS A 1 74  ? -7.469  -14.864 14.018 1.00 18.76 ? 81  LYS A CG    1 
ATOM   398  C  CD    . LYS A 1 74  ? -6.400  -14.365 14.969 1.00 18.53 ? 81  LYS A CD    1 
ATOM   399  C  CE    . LYS A 1 74  ? -6.784  -14.620 16.418 1.00 19.98 ? 81  LYS A CE    1 
ATOM   400  N  NZ    . LYS A 1 74  ? -7.794  -13.641 16.910 1.00 22.71 ? 81  LYS A NZ    1 
ATOM   401  N  N     . ILE A 1 75  ? -10.289 -15.694 12.323 1.00 15.54 ? 82  ILE A N     1 
ATOM   402  C  CA    . ILE A 1 75  ? -11.567 -15.116 12.713 1.00 15.40 ? 82  ILE A CA    1 
ATOM   403  C  C     . ILE A 1 75  ? -11.605 -15.039 14.231 1.00 18.94 ? 82  ILE A C     1 
ATOM   404  O  O     . ILE A 1 75  ? -11.112 -15.938 14.926 1.00 13.92 ? 82  ILE A O     1 
ATOM   405  C  CB    . ILE A 1 75  ? -12.763 -15.926 12.171 1.00 15.24 ? 82  ILE A CB    1 
ATOM   406  C  CG1   . ILE A 1 75  ? -14.067 -15.145 12.357 1.00 19.42 ? 82  ILE A CG1   1 
ATOM   407  C  CG2   . ILE A 1 75  ? -12.851 -17.291 12.852 1.00 16.53 ? 82  ILE A CG2   1 
ATOM   408  C  CD1   . ILE A 1 75  ? -14.070 -13.775 11.702 1.00 16.33 ? 82  ILE A CD1   1 
ATOM   409  N  N     . ASN A 1 76  ? -12.166 -13.949 14.746 1.00 18.05 ? 83  ASN A N     1 
ATOM   410  C  CA    . ASN A 1 76  ? -12.376 -13.775 16.175 1.00 16.83 ? 83  ASN A CA    1 
ATOM   411  C  C     . ASN A 1 76  ? -13.837 -13.425 16.404 1.00 16.02 ? 83  ASN A C     1 
ATOM   412  O  O     . ASN A 1 76  ? -14.371 -12.518 15.758 1.00 15.31 ? 83  ASN A O     1 
ATOM   413  C  CB    . ASN A 1 76  ? -11.465 -12.687 16.752 1.00 18.37 ? 83  ASN A CB    1 
ATOM   414  C  CG    . ASN A 1 76  ? -11.584 -12.569 18.257 1.00 15.63 ? 83  ASN A CG    1 
ATOM   415  O  OD1   . ASN A 1 76  ? -11.592 -13.574 18.969 1.00 16.74 ? 83  ASN A OD1   1 
ATOM   416  N  ND2   . ASN A 1 76  ? -11.679 -11.341 18.751 1.00 17.29 ? 83  ASN A ND2   1 
ATOM   417  N  N     . PHE A 1 77  ? -14.478 -14.148 17.313 1.00 16.93 ? 84  PHE A N     1 
ATOM   418  C  CA    . PHE A 1 77  ? -15.890 -13.965 17.615 1.00 14.86 ? 84  PHE A CA    1 
ATOM   419  C  C     . PHE A 1 77  ? -16.030 -13.049 18.824 1.00 14.14 ? 84  PHE A C     1 
ATOM   420  O  O     . PHE A 1 77  ? -15.382 -13.271 19.853 1.00 15.52 ? 84  PHE A O     1 
ATOM   421  C  CB    . PHE A 1 77  ? -16.555 -15.317 17.870 1.00 13.80 ? 84  PHE A CB    1 
ATOM   422  C  CG    . PHE A 1 77  ? -16.685 -16.157 16.635 1.00 16.94 ? 84  PHE A CG    1 
ATOM   423  C  CD1   . PHE A 1 77  ? -17.653 -15.869 15.689 1.00 16.30 ? 84  PHE A CD1   1 
ATOM   424  C  CD2   . PHE A 1 77  ? -15.824 -17.218 16.405 1.00 15.81 ? 84  PHE A CD2   1 
ATOM   425  C  CE1   . PHE A 1 77  ? -17.770 -16.632 14.544 1.00 16.12 ? 84  PHE A CE1   1 
ATOM   426  C  CE2   . PHE A 1 77  ? -15.936 -17.986 15.261 1.00 16.82 ? 84  PHE A CE2   1 
ATOM   427  C  CZ    . PHE A 1 77  ? -16.910 -17.692 14.329 1.00 20.99 ? 84  PHE A CZ    1 
ATOM   428  N  N     . ALA A 1 78  ? -16.864 -12.022 18.696 1.00 13.45 ? 85  ALA A N     1 
ATOM   429  C  CA    . ALA A 1 78  ? -16.936 -10.970 19.704 1.00 17.11 ? 85  ALA A CA    1 
ATOM   430  C  C     . ALA A 1 78  ? -18.295 -10.283 19.610 1.00 19.71 ? 85  ALA A C     1 
ATOM   431  O  O     . ALA A 1 78  ? -19.257 -10.859 19.082 1.00 16.47 ? 85  ALA A O     1 
ATOM   432  C  CB    . ALA A 1 78  ? -15.774 -9.978  19.521 1.00 16.57 ? 85  ALA A CB    1 
ATOM   433  N  N     . GLY A 1 79  ? -18.375 -9.052  20.112 1.00 20.83 ? 86  GLY A N     1 
ATOM   434  C  CA    . GLY A 1 79  ? -19.593 -8.269  20.052 1.00 18.37 ? 86  GLY A CA    1 
ATOM   435  C  C     . GLY A 1 79  ? -20.064 -7.818  21.413 1.00 23.08 ? 86  GLY A C     1 
ATOM   436  O  O     . GLY A 1 79  ? -19.331 -7.145  22.143 1.00 25.82 ? 86  GLY A O     1 
ATOM   437  N  N     . GLY A 1 80  ? -21.304 -8.160  21.748 1.00 21.45 ? 87  GLY A N     1 
ATOM   438  C  CA    . GLY A 1 80  ? -21.718 -8.193  23.133 1.00 18.26 ? 87  GLY A CA    1 
ATOM   439  C  C     . GLY A 1 80  ? -21.138 -9.441  23.763 1.00 18.03 ? 87  GLY A C     1 
ATOM   440  O  O     . GLY A 1 80  ? -19.916 -9.598  23.813 1.00 18.25 ? 87  GLY A O     1 
ATOM   441  N  N     . GLU A 1 81  ? -21.989 -10.355 24.216 1.00 14.95 ? 88  GLU A N     1 
ATOM   442  C  CA    . GLU A 1 81  ? -21.506 -11.614 24.770 1.00 14.67 ? 88  GLU A CA    1 
ATOM   443  C  C     . GLU A 1 81  ? -21.753 -12.732 23.769 1.00 17.88 ? 88  GLU A C     1 
ATOM   444  O  O     . GLU A 1 81  ? -22.916 -13.102 23.542 1.00 17.54 ? 88  GLU A O     1 
ATOM   445  C  CB    . GLU A 1 81  ? -22.192 -11.922 26.101 1.00 15.78 ? 88  GLU A CB    1 
ATOM   446  C  CG    . GLU A 1 81  ? -21.567 -13.071 26.878 1.00 14.03 ? 88  GLU A CG    1 
ATOM   447  C  CD    . GLU A 1 81  ? -20.065 -13.174 26.673 1.00 17.73 ? 88  GLU A CD    1 
ATOM   448  O  OE1   . GLU A 1 81  ? -19.346 -12.184 26.930 1.00 13.94 ? 88  GLU A OE1   1 
ATOM   449  O  OE2   . GLU A 1 81  ? -19.603 -14.252 26.248 1.00 17.39 ? 88  GLU A OE2   1 
ATOM   450  N  N     . PRO A 1 82  ? -20.712 -13.284 23.137 1.00 18.15 ? 89  PRO A N     1 
ATOM   451  C  CA    . PRO A 1 82  ? -20.947 -14.351 22.149 1.00 18.63 ? 89  PRO A CA    1 
ATOM   452  C  C     . PRO A 1 82  ? -21.646 -15.567 22.725 1.00 16.58 ? 89  PRO A C     1 
ATOM   453  O  O     . PRO A 1 82  ? -22.451 -16.201 22.031 1.00 17.76 ? 89  PRO A O     1 
ATOM   454  C  CB    . PRO A 1 82  ? -19.531 -14.686 21.661 1.00 14.23 ? 89  PRO A CB    1 
ATOM   455  C  CG    . PRO A 1 82  ? -18.762 -13.417 21.869 1.00 19.11 ? 89  PRO A CG    1 
ATOM   456  C  CD    . PRO A 1 82  ? -19.307 -12.839 23.148 1.00 15.97 ? 89  PRO A CD    1 
ATOM   457  N  N     . PHE A 1 83  ? -21.371 -15.910 23.978 1.00 15.80 ? 90  PHE A N     1 
ATOM   458  C  CA    . PHE A 1 83  ? -21.962 -17.095 24.581 1.00 17.69 ? 90  PHE A CA    1 
ATOM   459  C  C     . PHE A 1 83  ? -23.385 -16.875 25.071 1.00 19.51 ? 90  PHE A C     1 
ATOM   460  O  O     . PHE A 1 83  ? -23.909 -17.722 25.802 1.00 17.95 ? 90  PHE A O     1 
ATOM   461  C  CB    . PHE A 1 83  ? -21.074 -17.597 25.717 1.00 16.08 ? 90  PHE A CB    1 
ATOM   462  C  CG    . PHE A 1 83  ? -19.886 -18.375 25.243 1.00 21.21 ? 90  PHE A CG    1 
ATOM   463  C  CD1   . PHE A 1 83  ? -19.986 -19.737 25.017 1.00 18.37 ? 90  PHE A CD1   1 
ATOM   464  C  CD2   . PHE A 1 83  ? -18.672 -17.747 25.012 1.00 19.32 ? 90  PHE A CD2   1 
ATOM   465  C  CE1   . PHE A 1 83  ? -18.896 -20.462 24.582 1.00 21.08 ? 90  PHE A CE1   1 
ATOM   466  C  CE2   . PHE A 1 83  ? -17.574 -18.467 24.575 1.00 15.81 ? 90  PHE A CE2   1 
ATOM   467  C  CZ    . PHE A 1 83  ? -17.686 -19.826 24.360 1.00 18.70 ? 90  PHE A CZ    1 
ATOM   468  N  N     . LEU A 1 84  ? -24.015 -15.759 24.698 1.00 20.27 ? 91  LEU A N     1 
ATOM   469  C  CA    . LEU A 1 84  ? -25.466 -15.673 24.781 1.00 22.45 ? 91  LEU A CA    1 
ATOM   470  C  C     . LEU A 1 84  ? -26.134 -16.590 23.767 1.00 22.33 ? 91  LEU A C     1 
ATOM   471  O  O     . LEU A 1 84  ? -27.288 -16.981 23.963 1.00 21.40 ? 91  LEU A O     1 
ATOM   472  C  CB    . LEU A 1 84  ? -25.926 -14.232 24.557 1.00 17.88 ? 91  LEU A CB    1 
ATOM   473  C  CG    . LEU A 1 84  ? -25.941 -13.298 25.767 1.00 19.78 ? 91  LEU A CG    1 
ATOM   474  C  CD1   . LEU A 1 84  ? -26.223 -11.877 25.322 1.00 19.30 ? 91  LEU A CD1   1 
ATOM   475  C  CD2   . LEU A 1 84  ? -26.971 -13.747 26.793 1.00 20.40 ? 91  LEU A CD2   1 
ATOM   476  N  N     . TYR A 1 85  ? -25.428 -16.944 22.696 1.00 22.83 ? 92  TYR A N     1 
ATOM   477  C  CA    . TYR A 1 85  ? -25.949 -17.806 21.637 1.00 20.53 ? 92  TYR A CA    1 
ATOM   478  C  C     . TYR A 1 85  ? -24.921 -18.893 21.350 1.00 19.85 ? 92  TYR A C     1 
ATOM   479  O  O     . TYR A 1 85  ? -24.308 -18.920 20.276 1.00 18.53 ? 92  TYR A O     1 
ATOM   480  C  CB    . TYR A 1 85  ? -26.251 -16.995 20.377 1.00 20.10 ? 92  TYR A CB    1 
ATOM   481  C  CG    . TYR A 1 85  ? -27.130 -15.784 20.607 1.00 22.82 ? 92  TYR A CG    1 
ATOM   482  C  CD1   . TYR A 1 85  ? -26.577 -14.562 20.972 1.00 22.16 ? 92  TYR A CD1   1 
ATOM   483  C  CD2   . TYR A 1 85  ? -28.506 -15.853 20.434 1.00 24.60 ? 92  TYR A CD2   1 
ATOM   484  C  CE1   . TYR A 1 85  ? -27.371 -13.451 21.175 1.00 24.28 ? 92  TYR A CE1   1 
ATOM   485  C  CE2   . TYR A 1 85  ? -29.309 -14.746 20.633 1.00 22.53 ? 92  TYR A CE2   1 
ATOM   486  C  CZ    . TYR A 1 85  ? -28.736 -13.548 21.003 1.00 24.55 ? 92  TYR A CZ    1 
ATOM   487  O  OH    . TYR A 1 85  ? -29.535 -12.444 21.202 1.00 27.01 ? 92  TYR A OH    1 
ATOM   488  N  N     . PRO A 1 86  ? -24.705 -19.812 22.298 1.00 22.43 ? 93  PRO A N     1 
ATOM   489  C  CA    . PRO A 1 86  ? -23.664 -20.833 22.099 1.00 22.08 ? 93  PRO A CA    1 
ATOM   490  C  C     . PRO A 1 86  ? -23.977 -21.800 20.973 1.00 24.92 ? 93  PRO A C     1 
ATOM   491  O  O     . PRO A 1 86  ? -23.047 -22.384 20.403 1.00 22.94 ? 93  PRO A O     1 
ATOM   492  C  CB    . PRO A 1 86  ? -23.614 -21.544 23.456 1.00 23.32 ? 93  PRO A CB    1 
ATOM   493  C  CG    . PRO A 1 86  ? -25.003 -21.393 23.986 1.00 18.96 ? 93  PRO A CG    1 
ATOM   494  C  CD    . PRO A 1 86  ? -25.446 -20.020 23.554 1.00 21.61 ? 93  PRO A CD    1 
ATOM   495  N  N     . LYS A 1 87  ? -25.253 -21.984 20.637 1.00 22.58 ? 94  LYS A N     1 
ATOM   496  C  CA    . LYS A 1 87  ? -25.613 -22.813 19.493 1.00 21.38 ? 94  LYS A CA    1 
ATOM   497  C  C     . LYS A 1 87  ? -25.200 -22.141 18.188 1.00 21.61 ? 94  LYS A C     1 
ATOM   498  O  O     . LYS A 1 87  ? -24.608 -22.778 17.308 1.00 22.18 ? 94  LYS A O     1 
ATOM   499  C  CB    . LYS A 1 87  ? -27.119 -23.113 19.513 1.00 23.73 ? 94  LYS A CB    1 
ATOM   500  C  CG    . LYS A 1 87  ? -28.055 -21.913 19.299 1.00 28.30 ? 94  LYS A CG    1 
ATOM   501  C  CD    . LYS A 1 87  ? -28.127 -20.959 20.490 1.00 21.70 ? 94  LYS A CD    1 
ATOM   502  C  CE    . LYS A 1 87  ? -28.873 -21.575 21.655 1.00 23.34 ? 94  LYS A CE    1 
ATOM   503  N  NZ    . LYS A 1 87  ? -28.875 -20.667 22.831 1.00 31.67 ? 94  LYS A NZ    1 
ATOM   504  N  N     . PHE A 1 88  ? -25.490 -20.843 18.055 1.00 20.73 ? 95  PHE A N     1 
ATOM   505  C  CA    . PHE A 1 88  ? -25.063 -20.086 16.884 1.00 21.64 ? 95  PHE A CA    1 
ATOM   506  C  C     . PHE A 1 88  ? -23.544 -19.979 16.827 1.00 23.11 ? 95  PHE A C     1 
ATOM   507  O  O     . PHE A 1 88  ? -22.940 -20.141 15.760 1.00 21.67 ? 95  PHE A O     1 
ATOM   508  C  CB    . PHE A 1 88  ? -25.708 -18.698 16.920 1.00 19.59 ? 95  PHE A CB    1 
ATOM   509  C  CG    . PHE A 1 88  ? -25.383 -17.828 15.738 1.00 26.61 ? 95  PHE A CG    1 
ATOM   510  C  CD1   . PHE A 1 88  ? -24.268 -17.007 15.749 1.00 21.62 ? 95  PHE A CD1   1 
ATOM   511  C  CD2   . PHE A 1 88  ? -26.211 -17.808 14.626 1.00 29.61 ? 95  PHE A CD2   1 
ATOM   512  C  CE1   . PHE A 1 88  ? -23.976 -16.195 14.672 1.00 27.07 ? 95  PHE A CE1   1 
ATOM   513  C  CE2   . PHE A 1 88  ? -25.921 -16.995 13.543 1.00 28.89 ? 95  PHE A CE2   1 
ATOM   514  C  CZ    . PHE A 1 88  ? -24.801 -16.189 13.567 1.00 25.13 ? 95  PHE A CZ    1 
ATOM   515  N  N     . LEU A 1 89  ? -22.914 -19.707 17.972 1.00 20.55 ? 96  LEU A N     1 
ATOM   516  C  CA    . LEU A 1 89  ? -21.461 -19.593 18.032 1.00 17.46 ? 96  LEU A CA    1 
ATOM   517  C  C     . LEU A 1 89  ? -20.792 -20.904 17.634 1.00 20.31 ? 96  LEU A C     1 
ATOM   518  O  O     . LEU A 1 89  ? -19.954 -20.939 16.726 1.00 17.90 ? 96  LEU A O     1 
ATOM   519  C  CB    . LEU A 1 89  ? -21.042 -19.171 19.444 1.00 15.67 ? 96  LEU A CB    1 
ATOM   520  C  CG    . LEU A 1 89  ? -19.562 -18.926 19.746 1.00 17.44 ? 96  LEU A CG    1 
ATOM   521  C  CD1   . LEU A 1 89  ? -19.008 -17.822 18.868 1.00 15.20 ? 96  LEU A CD1   1 
ATOM   522  C  CD2   . LEU A 1 89  ? -19.373 -18.586 21.217 1.00 16.63 ? 96  LEU A CD2   1 
ATOM   523  N  N     . GLY A 1 90  ? -21.163 -21.998 18.304 1.00 19.95 ? 97  GLY A N     1 
ATOM   524  C  CA    . GLY A 1 90  ? -20.531 -23.279 18.026 1.00 18.74 ? 97  GLY A CA    1 
ATOM   525  C  C     . GLY A 1 90  ? -20.709 -23.730 16.589 1.00 20.90 ? 97  GLY A C     1 
ATOM   526  O  O     . GLY A 1 90  ? -19.820 -24.362 16.013 1.00 19.83 ? 97  GLY A O     1 
ATOM   527  N  N     . GLU A 1 91  ? -21.860 -23.413 15.990 1.00 19.11 ? 98  GLU A N     1 
ATOM   528  C  CA    . GLU A 1 91  ? -22.066 -23.725 14.579 1.00 20.90 ? 98  GLU A CA    1 
ATOM   529  C  C     . GLU A 1 91  ? -21.048 -23.005 13.705 1.00 19.02 ? 98  GLU A C     1 
ATOM   530  O  O     . GLU A 1 91  ? -20.544 -23.572 12.729 1.00 22.25 ? 98  GLU A O     1 
ATOM   531  C  CB    . GLU A 1 91  ? -23.484 -23.351 14.151 1.00 22.54 ? 98  GLU A CB    1 
ATOM   532  C  CG    . GLU A 1 91  ? -24.349 -24.526 13.714 1.00 26.01 ? 98  GLU A CG    1 
ATOM   533  C  CD    . GLU A 1 91  ? -25.758 -24.099 13.346 1.00 33.55 ? 98  GLU A CD    1 
ATOM   534  O  OE1   . GLU A 1 91  ? -26.554 -23.805 14.264 1.00 33.90 ? 98  GLU A OE1   1 
ATOM   535  O  OE2   . GLU A 1 91  ? -26.064 -24.044 12.136 1.00 30.70 ? 98  GLU A OE2   1 
ATOM   536  N  N     . LEU A 1 92  ? -20.731 -21.754 14.042 1.00 19.34 ? 99  LEU A N     1 
ATOM   537  C  CA    . LEU A 1 92  ? -19.816 -20.975 13.218 1.00 21.20 ? 99  LEU A CA    1 
ATOM   538  C  C     . LEU A 1 92  ? -18.359 -21.361 13.442 1.00 17.45 ? 99  LEU A C     1 
ATOM   539  O  O     . LEU A 1 92  ? -17.546 -21.223 12.523 1.00 20.20 ? 99  LEU A O     1 
ATOM   540  C  CB    . LEU A 1 92  ? -20.014 -19.483 13.483 1.00 16.21 ? 99  LEU A CB    1 
ATOM   541  C  CG    . LEU A 1 92  ? -21.266 -18.867 12.854 1.00 23.90 ? 99  LEU A CG    1 
ATOM   542  C  CD1   . LEU A 1 92  ? -21.197 -17.350 12.886 1.00 20.61 ? 99  LEU A CD1   1 
ATOM   543  C  CD2   . LEU A 1 92  ? -21.473 -19.369 11.429 1.00 20.64 ? 99  LEU A CD2   1 
ATOM   544  N  N     . VAL A 1 93  ? -18.002 -21.841 14.637 1.00 20.88 ? 100 VAL A N     1 
ATOM   545  C  CA    . VAL A 1 93  ? -16.613 -22.232 14.871 1.00 20.16 ? 100 VAL A CA    1 
ATOM   546  C  C     . VAL A 1 93  ? -16.306 -23.565 14.194 1.00 21.27 ? 100 VAL A C     1 
ATOM   547  O  O     . VAL A 1 93  ? -15.199 -23.772 13.682 1.00 24.58 ? 100 VAL A O     1 
ATOM   548  C  CB    . VAL A 1 93  ? -16.295 -22.254 16.381 1.00 19.15 ? 100 VAL A CB    1 
ATOM   549  C  CG1   . VAL A 1 93  ? -16.862 -21.019 17.056 1.00 21.09 ? 100 VAL A CG1   1 
ATOM   550  C  CG2   . VAL A 1 93  ? -16.827 -23.513 17.052 1.00 21.51 ? 100 VAL A CG2   1 
ATOM   551  N  N     . ASP A 1 94  ? -17.277 -24.482 14.161 1.00 23.74 ? 101 ASP A N     1 
ATOM   552  C  CA    . ASP A 1 94  ? -17.093 -25.714 13.402 1.00 22.76 ? 101 ASP A CA    1 
ATOM   553  C  C     . ASP A 1 94  ? -17.059 -25.424 11.907 1.00 22.70 ? 101 ASP A C     1 
ATOM   554  O  O     . ASP A 1 94  ? -16.321 -26.071 11.154 1.00 24.86 ? 101 ASP A O     1 
ATOM   555  C  CB    . ASP A 1 94  ? -18.206 -26.708 13.734 1.00 25.21 ? 101 ASP A CB    1 
ATOM   556  C  CG    . ASP A 1 94  ? -18.169 -27.175 15.184 1.00 22.58 ? 101 ASP A CG    1 
ATOM   557  O  OD1   . ASP A 1 94  ? -17.191 -26.871 15.898 1.00 22.21 ? 101 ASP A OD1   1 
ATOM   558  O  OD2   . ASP A 1 94  ? -19.125 -27.858 15.608 1.00 24.71 ? 101 ASP A OD2   1 
ATOM   559  N  N     . PHE A 1 95  ? -17.849 -24.446 11.465 1.00 21.64 ? 102 PHE A N     1 
ATOM   560  C  CA    . PHE A 1 95  ? -17.849 -24.054 10.061 1.00 21.48 ? 102 PHE A CA    1 
ATOM   561  C  C     . PHE A 1 95  ? -16.509 -23.453 9.659  1.00 22.84 ? 102 PHE A C     1 
ATOM   562  O  O     . PHE A 1 95  ? -15.900 -23.868 8.666  1.00 22.95 ? 102 PHE A O     1 
ATOM   563  C  CB    . PHE A 1 95  ? -18.986 -23.064 9.814  1.00 22.16 ? 102 PHE A CB    1 
ATOM   564  C  CG    . PHE A 1 95  ? -19.059 -22.559 8.408  1.00 27.63 ? 102 PHE A CG    1 
ATOM   565  C  CD1   . PHE A 1 95  ? -19.451 -23.394 7.377  1.00 27.04 ? 102 PHE A CD1   1 
ATOM   566  C  CD2   . PHE A 1 95  ? -18.745 -21.244 8.117  1.00 26.74 ? 102 PHE A CD2   1 
ATOM   567  C  CE1   . PHE A 1 95  ? -19.525 -22.928 6.083  1.00 23.96 ? 102 PHE A CE1   1 
ATOM   568  C  CE2   . PHE A 1 95  ? -18.818 -20.772 6.826  1.00 25.83 ? 102 PHE A CE2   1 
ATOM   569  C  CZ    . PHE A 1 95  ? -19.207 -21.615 5.806  1.00 26.43 ? 102 PHE A CZ    1 
ATOM   570  N  N     . CYS A 1 96  ? -16.026 -22.477 10.433 1.00 24.61 ? 103 CYS A N     1 
ATOM   571  C  CA    . CYS A 1 96  ? -14.794 -21.782 10.074 1.00 21.82 ? 103 CYS A CA    1 
ATOM   572  C  C     . CYS A 1 96  ? -13.596 -22.721 10.037 1.00 22.80 ? 103 CYS A C     1 
ATOM   573  O  O     . CYS A 1 96  ? -12.673 -22.515 9.241  1.00 23.86 ? 103 CYS A O     1 
ATOM   574  C  CB    . CYS A 1 96  ? -14.541 -20.634 11.052 1.00 19.05 ? 103 CYS A CB    1 
ATOM   575  S  SG    . CYS A 1 96  ? -15.673 -19.239 10.855 1.00 17.56 ? 103 CYS A SG    1 
ATOM   576  N  N     . LYS A 1 97  ? -13.592 -23.757 10.872 1.00 23.82 ? 104 LYS A N     1 
ATOM   577  C  CA    . LYS A 1 97  ? -12.440 -24.646 10.952 1.00 22.17 ? 104 LYS A CA    1 
ATOM   578  C  C     . LYS A 1 97  ? -12.560 -25.841 10.012 1.00 24.74 ? 104 LYS A C     1 
ATOM   579  O  O     . LYS A 1 97  ? -11.609 -26.164 9.295  1.00 25.79 ? 104 LYS A O     1 
ATOM   580  C  CB    . LYS A 1 97  ? -12.246 -25.121 12.394 1.00 19.63 ? 104 LYS A CB    1 
ATOM   581  C  CG    . LYS A 1 97  ? -10.971 -25.913 12.623 1.00 22.80 ? 104 LYS A CG    1 
ATOM   582  C  CD    . LYS A 1 97  ? -9.759  -25.218 12.030 1.00 21.34 ? 104 LYS A CD    1 
ATOM   583  C  CE    . LYS A 1 97  ? -9.314  -24.052 12.892 1.00 20.25 ? 104 LYS A CE    1 
ATOM   584  N  NZ    . LYS A 1 97  ? -7.885  -23.721 12.644 1.00 19.89 ? 104 LYS A NZ    1 
ATOM   585  N  N     . GLU A 1 98  ? -13.715 -26.509 10.006 1.00 24.70 ? 105 GLU A N     1 
ATOM   586  C  CA    . GLU A 1 98  ? -13.864 -27.703 9.181  1.00 27.74 ? 105 GLU A CA    1 
ATOM   587  C  C     . GLU A 1 98  ? -14.076 -27.356 7.714  1.00 28.71 ? 105 GLU A C     1 
ATOM   588  O  O     . GLU A 1 98  ? -13.495 -27.999 6.833  1.00 27.08 ? 105 GLU A O     1 
ATOM   589  C  CB    . GLU A 1 98  ? -15.023 -28.563 9.690  1.00 22.64 ? 105 GLU A CB    1 
ATOM   590  C  CG    . GLU A 1 98  ? -14.798 -29.181 11.059 1.00 25.21 ? 105 GLU A CG    1 
ATOM   591  C  CD    . GLU A 1 98  ? -16.078 -29.709 11.675 1.00 26.90 ? 105 GLU A CD    1 
ATOM   592  O  OE1   . GLU A 1 98  ? -17.156 -29.509 11.075 1.00 31.26 ? 105 GLU A OE1   1 
ATOM   593  O  OE2   . GLU A 1 98  ? -16.005 -30.339 12.751 1.00 29.11 ? 105 GLU A OE2   1 
ATOM   594  N  N     . ASP A 1 99  ? -14.890 -26.340 7.431  1.00 27.43 ? 106 ASP A N     1 
ATOM   595  C  CA    . ASP A 1 99  ? -15.288 -26.024 6.064  1.00 23.91 ? 106 ASP A CA    1 
ATOM   596  C  C     . ASP A 1 99  ? -14.408 -24.961 5.416  1.00 28.23 ? 106 ASP A C     1 
ATOM   597  O  O     . ASP A 1 99  ? -13.918 -25.164 4.302  1.00 32.17 ? 106 ASP A O     1 
ATOM   598  C  CB    . ASP A 1 99  ? -16.756 -25.586 6.041  1.00 28.11 ? 106 ASP A CB    1 
ATOM   599  C  CG    . ASP A 1 99  ? -17.690 -26.675 6.532  1.00 29.82 ? 106 ASP A CG    1 
ATOM   600  O  OD1   . ASP A 1 99  ? -17.279 -27.855 6.515  1.00 30.92 ? 106 ASP A OD1   1 
ATOM   601  O  OD2   . ASP A 1 99  ? -18.830 -26.358 6.933  1.00 34.29 ? 106 ASP A OD2   1 
ATOM   602  N  N     . LEU A 1 100 ? -14.195 -23.829 6.088  1.00 26.06 ? 107 LEU A N     1 
ATOM   603  C  CA    . LEU A 1 100 ? -13.322 -22.799 5.543  1.00 20.66 ? 107 LEU A CA    1 
ATOM   604  C  C     . LEU A 1 100 ? -11.853 -23.045 5.853  1.00 23.77 ? 107 LEU A C     1 
ATOM   605  O  O     . LEU A 1 100 ? -11.000 -22.342 5.301  1.00 27.92 ? 107 LEU A O     1 
ATOM   606  C  CB    . LEU A 1 100 ? -13.728 -21.418 6.066  1.00 22.23 ? 107 LEU A CB    1 
ATOM   607  C  CG    . LEU A 1 100 ? -15.206 -21.054 5.921  1.00 24.70 ? 107 LEU A CG    1 
ATOM   608  C  CD1   . LEU A 1 100 ? -15.480 -19.698 6.550  1.00 22.64 ? 107 LEU A CD1   1 
ATOM   609  C  CD2   . LEU A 1 100 ? -15.626 -21.068 4.457  1.00 21.05 ? 107 LEU A CD2   1 
ATOM   610  N  N     . HIS A 1 101 ? -11.545 -24.018 6.712  1.00 24.41 ? 108 HIS A N     1 
ATOM   611  C  CA    . HIS A 1 101 ? -10.165 -24.386 7.033  1.00 24.91 ? 108 HIS A CA    1 
ATOM   612  C  C     . HIS A 1 101 ? -9.346  -23.170 7.454  1.00 26.62 ? 108 HIS A C     1 
ATOM   613  O  O     . HIS A 1 101 ? -8.163  -23.046 7.128  1.00 25.37 ? 108 HIS A O     1 
ATOM   614  C  CB    . HIS A 1 101 ? -9.504  -25.112 5.861  1.00 24.54 ? 108 HIS A CB    1 
ATOM   615  C  CG    . HIS A 1 101 ? -10.180 -26.393 5.485  1.00 30.22 ? 108 HIS A CG    1 
ATOM   616  N  ND1   . HIS A 1 101 ? -11.048 -26.493 4.419  1.00 33.21 ? 108 HIS A ND1   1 
ATOM   617  C  CD2   . HIS A 1 101 ? -10.121 -27.627 6.040  1.00 30.66 ? 108 HIS A CD2   1 
ATOM   618  C  CE1   . HIS A 1 101 ? -11.489 -27.735 4.329  1.00 33.59 ? 108 HIS A CE1   1 
ATOM   619  N  NE2   . HIS A 1 101 ? -10.942 -28.443 5.301  1.00 35.80 ? 108 HIS A NE2   1 
ATOM   620  N  N     . LEU A 1 102 ? -9.991  -22.260 8.180  1.00 23.65 ? 109 LEU A N     1 
ATOM   621  C  CA    . LEU A 1 102 ? -9.311  -21.076 8.684  1.00 22.51 ? 109 LEU A CA    1 
ATOM   622  C  C     . LEU A 1 102 ? -8.113  -21.476 9.535  1.00 20.63 ? 109 LEU A C     1 
ATOM   623  O  O     . LEU A 1 102 ? -8.121  -22.506 10.215 1.00 22.50 ? 109 LEU A O     1 
ATOM   624  C  CB    . LEU A 1 102 ? -10.276 -20.225 9.510  1.00 22.36 ? 109 LEU A CB    1 
ATOM   625  C  CG    . LEU A 1 102 ? -11.356 -19.461 8.741  1.00 22.68 ? 109 LEU A CG    1 
ATOM   626  C  CD1   . LEU A 1 102 ? -11.920 -18.341 9.586  1.00 18.77 ? 109 LEU A CD1   1 
ATOM   627  C  CD2   . LEU A 1 102 ? -10.798 -18.911 7.445  1.00 21.31 ? 109 LEU A CD2   1 
ATOM   628  N  N     . GLU A 1 103 ? -7.065  -20.653 9.483  1.00 19.75 ? 110 GLU A N     1 
ATOM   629  C  CA    . GLU A 1 103 ? -5.908  -20.887 10.338 1.00 22.41 ? 110 GLU A CA    1 
ATOM   630  C  C     . GLU A 1 103 ? -6.296  -20.806 11.810 1.00 22.47 ? 110 GLU A C     1 
ATOM   631  O  O     . GLU A 1 103 ? -6.090  -21.754 12.576 1.00 24.37 ? 110 GLU A O     1 
ATOM   632  C  CB    . GLU A 1 103 ? -4.798  -19.883 10.016 1.00 26.69 ? 110 GLU A CB    1 
ATOM   633  C  CG    . GLU A 1 103 ? -3.776  -20.381 9.008  1.00 22.75 ? 110 GLU A CG    1 
ATOM   634  C  CD    . GLU A 1 103 ? -2.748  -19.324 8.648  1.00 29.22 ? 110 GLU A CD    1 
ATOM   635  O  OE1   . GLU A 1 103 ? -2.339  -18.562 9.549  1.00 31.49 ? 110 GLU A OE1   1 
ATOM   636  O  OE2   . GLU A 1 103 ? -2.340  -19.262 7.469  1.00 37.37 ? 110 GLU A OE2   1 
ATOM   637  N  N     . SER A 1 104 ? -6.879  -19.682 12.221 1.00 19.84 ? 111 SER A N     1 
ATOM   638  C  CA    . SER A 1 104 ? -7.145  -19.422 13.630 1.00 21.79 ? 111 SER A CA    1 
ATOM   639  C  C     . SER A 1 104 ? -8.618  -19.116 13.846 1.00 19.77 ? 111 SER A C     1 
ATOM   640  O  O     . SER A 1 104 ? -9.175  -18.232 13.189 1.00 19.38 ? 111 SER A O     1 
ATOM   641  C  CB    . SER A 1 104 ? -6.294  -18.257 14.140 1.00 21.19 ? 111 SER A CB    1 
ATOM   642  O  OG    . SER A 1 104 ? -6.402  -18.137 15.548 1.00 20.87 ? 111 SER A OG    1 
ATOM   643  N  N     . VAL A 1 105 ? -9.243  -19.846 14.764 1.00 18.91 ? 112 VAL A N     1 
ATOM   644  C  CA    . VAL A 1 105 ? -10.580 -19.532 15.255 1.00 18.85 ? 112 VAL A CA    1 
ATOM   645  C  C     . VAL A 1 105 ? -10.449 -19.162 16.727 1.00 19.54 ? 112 VAL A C     1 
ATOM   646  O  O     . VAL A 1 105 ? -9.968  -19.966 17.535 1.00 18.50 ? 112 VAL A O     1 
ATOM   647  C  CB    . VAL A 1 105 ? -11.553 -20.703 15.058 1.00 19.84 ? 112 VAL A CB    1 
ATOM   648  C  CG1   . VAL A 1 105 ? -12.829 -20.462 15.839 1.00 18.55 ? 112 VAL A CG1   1 
ATOM   649  C  CG2   . VAL A 1 105 ? -11.854 -20.892 13.579 1.00 18.84 ? 112 VAL A CG2   1 
ATOM   650  N  N     . SER A 1 106 ? -10.864 -17.944 17.075 1.00 18.15 ? 113 SER A N     1 
ATOM   651  C  CA    . SER A 1 106 ? -10.685 -17.420 18.421 1.00 16.63 ? 113 SER A CA    1 
ATOM   652  C  C     . SER A 1 106 ? -11.986 -16.812 18.928 1.00 16.09 ? 113 SER A C     1 
ATOM   653  O  O     . SER A 1 106 ? -12.831 -16.373 18.145 1.00 14.78 ? 113 SER A O     1 
ATOM   654  C  CB    . SER A 1 106 ? -9.560  -16.375 18.462 1.00 16.19 ? 113 SER A CB    1 
ATOM   655  O  OG    . SER A 1 106 ? -9.825  -15.366 19.420 1.00 25.98 ? 113 SER A OG    1 
ATOM   656  N  N     . ILE A 1 107 ? -12.141 -16.801 20.253 1.00 16.44 ? 114 ILE A N     1 
ATOM   657  C  CA    . ILE A 1 107 ? -13.323 -16.251 20.911 1.00 20.18 ? 114 ILE A CA    1 
ATOM   658  C  C     . ILE A 1 107 ? -12.879 -15.380 22.077 1.00 17.94 ? 114 ILE A C     1 
ATOM   659  O  O     . ILE A 1 107 ? -11.960 -15.740 22.821 1.00 15.21 ? 114 ILE A O     1 
ATOM   660  C  CB    . ILE A 1 107 ? -14.282 -17.356 21.410 1.00 17.00 ? 114 ILE A CB    1 
ATOM   661  C  CG1   . ILE A 1 107 ? -14.525 -18.406 20.329 1.00 17.34 ? 114 ILE A CG1   1 
ATOM   662  C  CG2   . ILE A 1 107 ? -15.608 -16.761 21.855 1.00 13.21 ? 114 ILE A CG2   1 
ATOM   663  C  CD1   . ILE A 1 107 ? -14.762 -19.784 20.882 1.00 18.77 ? 114 ILE A CD1   1 
ATOM   664  N  N     . ILE A 1 108 ? -13.531 -14.229 22.231 1.00 15.89 ? 115 ILE A N     1 
ATOM   665  C  CA    . ILE A 1 108 ? -13.389 -13.376 23.405 1.00 13.40 ? 115 ILE A CA    1 
ATOM   666  C  C     . ILE A 1 108 ? -14.748 -13.301 24.093 1.00 15.37 ? 115 ILE A C     1 
ATOM   667  O  O     . ILE A 1 108 ? -15.764 -13.024 23.445 1.00 13.91 ? 115 ILE A O     1 
ATOM   668  C  CB    . ILE A 1 108 ? -12.854 -11.976 23.038 1.00 13.20 ? 115 ILE A CB    1 
ATOM   669  C  CG1   . ILE A 1 108 ? -12.927 -11.028 24.238 1.00 12.86 ? 115 ILE A CG1   1 
ATOM   670  C  CG2   . ILE A 1 108 ? -13.587 -11.406 21.845 1.00 17.89 ? 115 ILE A CG2   1 
ATOM   671  C  CD1   . ILE A 1 108 ? -12.099 -11.493 25.423 1.00 11.91 ? 115 ILE A CD1   1 
ATOM   672  N  N     . THR A 1 109 ? -14.765 -13.573 25.397 1.00 13.58 ? 116 THR A N     1 
ATOM   673  C  CA    . THR A 1 109 ? -16.001 -13.695 26.158 1.00 14.65 ? 116 THR A CA    1 
ATOM   674  C  C     . THR A 1 109 ? -15.791 -13.143 27.560 1.00 15.88 ? 116 THR A C     1 
ATOM   675  O  O     . THR A 1 109 ? -14.660 -13.030 28.037 1.00 13.85 ? 116 THR A O     1 
ATOM   676  C  CB    . THR A 1 109 ? -16.468 -15.157 26.241 1.00 13.92 ? 116 THR A CB    1 
ATOM   677  O  OG1   . THR A 1 109 ? -17.580 -15.255 27.140 1.00 16.50 ? 116 THR A OG1   1 
ATOM   678  C  CG2   . THR A 1 109 ? -15.343 -16.053 26.742 1.00 12.88 ? 116 THR A CG2   1 
ATOM   679  N  N     . ASN A 1 110 ? -16.893 -12.795 28.227 1.00 16.33 ? 117 ASN A N     1 
ATOM   680  C  CA    . ASN A 1 110 ? -16.784 -12.444 29.637 1.00 16.64 ? 117 ASN A CA    1 
ATOM   681  C  C     . ASN A 1 110 ? -16.794 -13.670 30.541 1.00 17.64 ? 117 ASN A C     1 
ATOM   682  O  O     . ASN A 1 110 ? -16.599 -13.529 31.754 1.00 15.71 ? 117 ASN A O     1 
ATOM   683  C  CB    . ASN A 1 110 ? -17.884 -11.444 30.039 1.00 15.01 ? 117 ASN A CB    1 
ATOM   684  C  CG    . ASN A 1 110 ? -19.289 -12.030 29.991 1.00 15.95 ? 117 ASN A CG    1 
ATOM   685  O  OD1   . ASN A 1 110 ? -19.524 -13.184 30.348 1.00 17.58 ? 117 ASN A OD1   1 
ATOM   686  N  ND2   . ASN A 1 110 ? -20.240 -11.216 29.548 1.00 12.77 ? 117 ASN A ND2   1 
ATOM   687  N  N     . GLY A 1 111 ? -17.018 -14.860 29.980 1.00 16.47 ? 118 GLY A N     1 
ATOM   688  C  CA    . GLY A 1 111 ? -16.807 -16.109 30.673 1.00 15.54 ? 118 GLY A CA    1 
ATOM   689  C  C     . GLY A 1 111 ? -17.982 -16.630 31.474 1.00 17.85 ? 118 GLY A C     1 
ATOM   690  O  O     . GLY A 1 111 ? -18.013 -17.826 31.784 1.00 17.23 ? 118 GLY A O     1 
ATOM   691  N  N     . SER A 1 112 ? -18.953 -15.779 31.815 1.00 22.56 ? 119 SER A N     1 
ATOM   692  C  CA    . SER A 1 112 ? -19.975 -16.178 32.780 1.00 18.68 ? 119 SER A CA    1 
ATOM   693  C  C     . SER A 1 112 ? -20.935 -17.223 32.220 1.00 20.24 ? 119 SER A C     1 
ATOM   694  O  O     . SER A 1 112 ? -21.450 -18.052 32.979 1.00 23.66 ? 119 SER A O     1 
ATOM   695  C  CB    . SER A 1 112 ? -20.752 -14.952 33.259 1.00 14.53 ? 119 SER A CB    1 
ATOM   696  O  OG    . SER A 1 112 ? -21.395 -14.298 32.180 1.00 17.67 ? 119 SER A OG    1 
ATOM   697  N  N     . LEU A 1 113 ? -21.194 -17.205 30.913 1.00 22.61 ? 120 LEU A N     1 
ATOM   698  C  CA    . LEU A 1 113 ? -22.181 -18.092 30.308 1.00 22.58 ? 120 LEU A CA    1 
ATOM   699  C  C     . LEU A 1 113 ? -21.557 -19.276 29.586 1.00 22.34 ? 120 LEU A C     1 
ATOM   700  O  O     . LEU A 1 113 ? -22.255 -19.970 28.841 1.00 23.92 ? 120 LEU A O     1 
ATOM   701  C  CB    . LEU A 1 113 ? -23.069 -17.309 29.341 1.00 16.78 ? 120 LEU A CB    1 
ATOM   702  C  CG    . LEU A 1 113 ? -23.924 -16.220 29.985 1.00 19.89 ? 120 LEU A CG    1 
ATOM   703  C  CD1   . LEU A 1 113 ? -24.517 -15.311 28.926 1.00 17.72 ? 120 LEU A CD1   1 
ATOM   704  C  CD2   . LEU A 1 113 ? -25.016 -16.838 30.843 1.00 16.54 ? 120 LEU A CD2   1 
ATOM   705  N  N     . VAL A 1 114 ? -20.270 -19.523 29.787 1.00 22.66 ? 121 VAL A N     1 
ATOM   706  C  CA    . VAL A 1 114 ? -19.602 -20.650 29.146 1.00 24.86 ? 121 VAL A CA    1 
ATOM   707  C  C     . VAL A 1 114 ? -19.942 -21.931 29.899 1.00 29.42 ? 121 VAL A C     1 
ATOM   708  O  O     . VAL A 1 114 ? -19.874 -21.980 31.134 1.00 30.29 ? 121 VAL A O     1 
ATOM   709  C  CB    . VAL A 1 114 ? -18.084 -20.423 29.094 1.00 24.36 ? 121 VAL A CB    1 
ATOM   710  C  CG1   . VAL A 1 114 ? -17.376 -21.679 28.634 1.00 26.93 ? 121 VAL A CG1   1 
ATOM   711  C  CG2   . VAL A 1 114 ? -17.747 -19.254 28.181 1.00 23.34 ? 121 VAL A CG2   1 
ATOM   712  N  N     . ARG A 1 115 ? -20.327 -22.967 29.177 1.00 26.37 ? 122 ARG A N     1 
ATOM   713  C  CA    . ARG A 1 115 ? -20.580 -24.273 29.789 1.00 27.32 ? 122 ARG A CA    1 
ATOM   714  C  C     . ARG A 1 115 ? -19.482 -25.254 29.394 1.00 26.13 ? 122 ARG A C     1 
ATOM   715  O  O     . ARG A 1 115 ? -19.022 -25.240 28.282 1.00 30.78 ? 122 ARG A O     1 
ATOM   716  C  CB    . ARG A 1 115 ? -21.950 -24.810 29.368 1.00 29.16 ? 122 ARG A CB    1 
ATOM   717  C  CG    . ARG A 1 115 ? -23.132 -23.936 29.712 1.00 27.55 ? 122 ARG A CG    1 
ATOM   718  C  CD    . ARG A 1 115 ? -23.798 -24.401 30.988 1.00 27.48 ? 122 ARG A CD    1 
ATOM   719  N  NE    . ARG A 1 115 ? -22.955 -24.169 32.146 1.00 29.55 ? 122 ARG A NE    1 
ATOM   720  C  CZ    . ARG A 1 115 ? -22.822 -22.990 32.731 1.00 28.51 ? 122 ARG A CZ    1 
ATOM   721  N  NH1   . ARG A 1 115 ? -23.465 -21.940 32.259 1.00 32.67 ? 122 ARG A NH1   1 
ATOM   722  N  NH2   . ARG A 1 115 ? -22.043 -22.859 33.788 1.00 32.75 ? 122 ARG A NH2   1 
ATOM   723  N  N     . GLU A 1 116 ? -19.073 -26.103 30.311 1.00 26.15 ? 123 GLU A N     1 
ATOM   724  C  CA    A GLU A 1 116 ? -17.928 -26.985 30.106 0.58 26.88 ? 123 GLU A CA    1 
ATOM   725  C  CA    B GLU A 1 116 ? -17.924 -26.978 30.101 0.42 27.27 ? 123 GLU A CA    1 
ATOM   726  C  C     . GLU A 1 116 ? -18.143 -27.931 28.932 1.00 28.37 ? 123 GLU A C     1 
ATOM   727  O  O     . GLU A 1 116 ? -17.190 -28.265 28.218 1.00 28.10 ? 123 GLU A O     1 
ATOM   728  C  CB    A GLU A 1 116 ? -17.638 -27.779 31.380 0.58 28.13 ? 123 GLU A CB    1 
ATOM   729  C  CB    B GLU A 1 116 ? -17.613 -27.764 31.377 0.42 28.24 ? 123 GLU A CB    1 
ATOM   730  C  CG    A GLU A 1 116 ? -16.227 -28.345 31.451 0.58 27.84 ? 123 GLU A CG    1 
ATOM   731  C  CG    B GLU A 1 116 ? -16.360 -28.628 31.276 0.42 27.90 ? 123 GLU A CG    1 
ATOM   732  C  CD    A GLU A 1 116 ? -16.106 -29.724 30.823 0.58 28.08 ? 123 GLU A CD    1 
ATOM   733  C  CD    B GLU A 1 116 ? -15.779 -28.979 32.630 0.42 27.13 ? 123 GLU A CD    1 
ATOM   734  O  OE1   A GLU A 1 116 ? -17.146 -30.308 30.448 0.58 25.55 ? 123 GLU A OE1   1 
ATOM   735  O  OE1   B GLU A 1 116 ? -16.445 -28.707 33.651 0.42 29.76 ? 123 GLU A OE1   1 
ATOM   736  O  OE2   A GLU A 1 116 ? -14.967 -30.219 30.696 0.58 31.07 ? 123 GLU A OE2   1 
ATOM   737  O  OE2   B GLU A 1 116 ? -14.653 -29.520 32.677 0.42 26.07 ? 123 GLU A OE2   1 
ATOM   738  N  N     . GLU A 1 117 ? -19.364 -28.407 28.719 1.00 27.31 ? 124 GLU A N     1 
ATOM   739  C  CA    . GLU A 1 117 ? -19.649 -29.328 27.634 1.00 26.48 ? 124 GLU A CA    1 
ATOM   740  C  C     . GLU A 1 117 ? -19.505 -28.668 26.265 1.00 22.32 ? 124 GLU A C     1 
ATOM   741  O  O     . GLU A 1 117 ? -19.138 -29.313 25.322 1.00 21.81 ? 124 GLU A O     1 
ATOM   742  C  CB    . GLU A 1 117 ? -21.025 -29.972 27.798 1.00 27.18 ? 124 GLU A CB    1 
ATOM   743  C  CG    . GLU A 1 117 ? -22.155 -29.285 27.058 1.00 31.84 ? 124 GLU A CG    1 
ATOM   744  C  CD    . GLU A 1 117 ? -22.694 -28.075 27.788 1.00 35.61 ? 124 GLU A CD    1 
ATOM   745  O  OE1   . GLU A 1 117 ? -22.900 -28.156 29.015 1.00 40.19 ? 124 GLU A OE1   1 
ATOM   746  O  OE2   . GLU A 1 117 ? -22.932 -27.052 27.131 1.00 34.34 ? 124 GLU A OE2   1 
ATOM   747  N  N     . TRP A 1 118 ? -19.808 -27.383 26.180 1.00 25.99 ? 125 TRP A N     1 
ATOM   748  C  CA    . TRP A 1 118 ? -19.593 -26.666 24.927 1.00 19.72 ? 125 TRP A CA    1 
ATOM   749  C  C     . TRP A 1 118 ? -18.110 -26.587 24.591 1.00 25.04 ? 125 TRP A C     1 
ATOM   750  O  O     . TRP A 1 118 ? -17.718 -26.767 23.432 1.00 25.03 ? 125 TRP A O     1 
ATOM   751  C  CB    . TRP A 1 118 ? -20.199 -25.263 25.011 1.00 23.43 ? 125 TRP A CB    1 
ATOM   752  C  CG    . TRP A 1 118 ? -20.216 -24.510 23.710 1.00 20.32 ? 125 TRP A CG    1 
ATOM   753  C  CD1   . TRP A 1 118 ? -21.268 -24.390 22.850 1.00 20.68 ? 125 TRP A CD1   1 
ATOM   754  C  CD2   . TRP A 1 118 ? -19.140 -23.757 23.134 1.00 22.41 ? 125 TRP A CD2   1 
ATOM   755  N  NE1   . TRP A 1 118 ? -20.913 -23.617 21.771 1.00 19.72 ? 125 TRP A NE1   1 
ATOM   756  C  CE2   . TRP A 1 118 ? -19.612 -23.215 21.921 1.00 21.17 ? 125 TRP A CE2   1 
ATOM   757  C  CE3   . TRP A 1 118 ? -17.823 -23.492 23.523 1.00 20.44 ? 125 TRP A CE3   1 
ATOM   758  C  CZ2   . TRP A 1 118 ? -18.815 -22.425 21.096 1.00 21.55 ? 125 TRP A CZ2   1 
ATOM   759  C  CZ3   . TRP A 1 118 ? -17.035 -22.708 22.702 1.00 20.13 ? 125 TRP A CZ3   1 
ATOM   760  C  CH2   . TRP A 1 118 ? -17.533 -22.184 21.503 1.00 20.23 ? 125 TRP A CH2   1 
ATOM   761  N  N     . VAL A 1 119 ? -17.272 -26.319 25.595 1.00 23.54 ? 126 VAL A N     1 
ATOM   762  C  CA    . VAL A 1 119 ? -15.827 -26.296 25.382 1.00 24.29 ? 126 VAL A CA    1 
ATOM   763  C  C     . VAL A 1 119 ? -15.335 -27.669 24.946 1.00 26.24 ? 126 VAL A C     1 
ATOM   764  O  O     . VAL A 1 119 ? -14.521 -27.793 24.022 1.00 29.21 ? 126 VAL A O     1 
ATOM   765  C  CB    . VAL A 1 119 ? -15.104 -25.822 26.656 1.00 28.36 ? 126 VAL A CB    1 
ATOM   766  C  CG1   . VAL A 1 119 ? -13.631 -25.568 26.372 1.00 22.59 ? 126 VAL A CG1   1 
ATOM   767  C  CG2   . VAL A 1 119 ? -15.770 -24.580 27.216 1.00 26.49 ? 126 VAL A CG2   1 
ATOM   768  N  N     . ARG A 1 120 ? -15.817 -28.722 25.611 1.00 27.72 ? 127 ARG A N     1 
ATOM   769  C  CA    . ARG A 1 120 ? -15.395 -30.078 25.274 1.00 29.63 ? 127 ARG A CA    1 
ATOM   770  C  C     . ARG A 1 120 ? -15.814 -30.451 23.857 1.00 28.24 ? 127 ARG A C     1 
ATOM   771  O  O     . ARG A 1 120 ? -15.053 -31.093 23.123 1.00 25.68 ? 127 ARG A O     1 
ATOM   772  C  CB    . ARG A 1 120 ? -15.982 -31.064 26.286 1.00 27.89 ? 127 ARG A CB    1 
ATOM   773  C  CG    . ARG A 1 120 ? -14.967 -31.949 26.989 1.00 28.50 ? 127 ARG A CG    1 
ATOM   774  C  CD    . ARG A 1 120 ? -15.664 -33.119 27.670 1.00 29.92 ? 127 ARG A CD    1 
ATOM   775  N  NE    . ARG A 1 120 ? -16.674 -32.671 28.622 1.00 30.65 ? 127 ARG A NE    1 
ATOM   776  C  CZ    . ARG A 1 120 ? -17.957 -33.005 28.575 1.00 30.49 ? 127 ARG A CZ    1 
ATOM   777  N  NH1   . ARG A 1 120 ? -18.432 -33.794 27.625 1.00 36.80 ? 127 ARG A NH1   1 
ATOM   778  N  NH2   . ARG A 1 120 ? -18.785 -32.533 29.502 1.00 24.17 ? 127 ARG A NH2   1 
ATOM   779  N  N     . LYS A 1 121 ? -16.980 -30.035 23.429 1.00 26.08 ? 128 LYS A N     1 
ATOM   780  C  CA    . LYS A 1 121 ? -17.472 -30.438 22.125 1.00 28.47 ? 128 LYS A CA    1 
ATOM   781  C  C     . LYS A 1 121 ? -16.823 -29.708 20.988 1.00 30.15 ? 128 LYS A C     1 
ATOM   782  O  O     . LYS A 1 121 ? -16.670 -30.255 19.914 1.00 28.54 ? 128 LYS A O     1 
ATOM   783  C  CB    . LYS A 1 121 ? -18.993 -30.225 22.069 1.00 25.82 ? 128 LYS A CB    1 
ATOM   784  C  CG    . LYS A 1 121 ? -19.630 -30.397 20.708 1.00 30.59 ? 128 LYS A CG    1 
ATOM   785  C  CD    . LYS A 1 121 ? -21.048 -29.860 20.717 1.00 31.87 ? 128 LYS A CD    1 
ATOM   786  C  CE    . LYS A 1 121 ? -21.768 -30.165 19.418 1.00 27.70 ? 128 LYS A CE    1 
ATOM   787  N  NZ    . LYS A 1 121 ? -23.170 -29.677 19.461 1.00 23.69 ? 128 LYS A NZ    1 
ATOM   788  N  N     . HIS A 1 122 ? -16.416 -28.485 21.236 1.00 28.26 ? 129 HIS A N     1 
ATOM   789  C  CA    . HIS A 1 122 ? -15.875 -27.643 20.177 1.00 25.12 ? 129 HIS A CA    1 
ATOM   790  C  C     . HIS A 1 122 ? -14.388 -27.362 20.337 1.00 24.28 ? 129 HIS A C     1 
ATOM   791  O  O     . HIS A 1 122 ? -13.871 -26.450 19.685 1.00 29.03 ? 129 HIS A O     1 
ATOM   792  C  CB    . HIS A 1 122 ? -16.641 -26.319 20.114 1.00 20.00 ? 129 HIS A CB    1 
ATOM   793  C  CG    . HIS A 1 122 ? -18.090 -26.473 19.780 1.00 22.54 ? 129 HIS A CG    1 
ATOM   794  N  ND1   . HIS A 1 122 ? -18.546 -26.611 18.487 1.00 20.82 ? 129 HIS A ND1   1 
ATOM   795  C  CD2   . HIS A 1 122 ? -19.188 -26.501 20.572 1.00 20.77 ? 129 HIS A CD2   1 
ATOM   796  C  CE1   . HIS A 1 122 ? -19.862 -26.723 18.497 1.00 21.54 ? 129 HIS A CE1   1 
ATOM   797  N  NE2   . HIS A 1 122 ? -20.277 -26.658 19.750 1.00 21.16 ? 129 HIS A NE2   1 
ATOM   798  N  N     . ALA A 1 123 ? -13.683 -28.122 21.177 1.00 22.04 ? 130 ALA A N     1 
ATOM   799  C  CA    . ALA A 1 123 ? -12.281 -27.807 21.440 1.00 26.17 ? 130 ALA A CA    1 
ATOM   800  C  C     . ALA A 1 123 ? -11.421 -28.005 20.199 1.00 28.38 ? 130 ALA A C     1 
ATOM   801  O  O     . ALA A 1 123 ? -10.449 -27.271 19.984 1.00 31.16 ? 130 ALA A O     1 
ATOM   802  C  CB    . ALA A 1 123 ? -11.758 -28.663 22.593 1.00 24.24 ? 130 ALA A CB    1 
ATOM   803  N  N     . LYS A 1 124 ? -11.781 -28.945 19.351 1.00 25.52 ? 131 LYS A N     1 
ATOM   804  C  CA    . LYS A 1 124 ? -10.992 -29.271 18.191 1.00 27.35 ? 131 LYS A CA    1 
ATOM   805  C  C     . LYS A 1 124 ? -10.967 -28.207 17.150 1.00 30.17 ? 131 LYS A C     1 
ATOM   806  O  O     . LYS A 1 124 ? -10.060 -28.154 16.345 1.00 33.23 ? 131 LYS A O     1 
ATOM   807  C  CB    . LYS A 1 124 ? -11.565 -30.543 17.561 1.00 27.84 ? 131 LYS A CB    1 
ATOM   808  C  CG    . LYS A 1 124 ? -13.006 -30.461 17.114 1.00 26.81 ? 131 LYS A CG    1 
ATOM   809  C  CD    . LYS A 1 124 ? -13.614 -31.851 17.089 1.00 25.69 ? 131 LYS A CD    1 
ATOM   810  C  CE    . LYS A 1 124 ? -14.904 -31.871 16.298 1.00 30.73 ? 131 LYS A CE    1 
ATOM   811  N  NZ    . LYS A 1 124 ? -15.763 -30.710 16.633 1.00 34.63 ? 131 LYS A NZ    1 
ATOM   812  N  N     . ASN A 1 125 ? -11.953 -27.368 17.157 1.00 22.17 ? 132 ASN A N     1 
ATOM   813  C  CA    . ASN A 1 125 ? -12.085 -26.324 16.152 1.00 20.76 ? 132 ASN A CA    1 
ATOM   814  C  C     . ASN A 1 125 ? -11.733 -24.943 16.681 1.00 21.45 ? 132 ASN A C     1 
ATOM   815  O  O     . ASN A 1 125 ? -11.758 -23.976 15.914 1.00 19.34 ? 132 ASN A O     1 
ATOM   816  C  CB    . ASN A 1 125 ? -13.510 -26.316 15.587 1.00 22.89 ? 132 ASN A CB    1 
ATOM   817  C  CG    . ASN A 1 125 ? -13.827 -27.570 14.802 1.00 25.44 ? 132 ASN A CG    1 
ATOM   818  O  OD1   . ASN A 1 125 ? -12.949 -28.154 14.168 1.00 28.07 ? 132 ASN A OD1   1 
ATOM   819  N  ND2   . ASN A 1 125 ? -15.085 -27.994 14.842 1.00 21.15 ? 132 ASN A ND2   1 
ATOM   820  N  N     . ILE A 1 126 ? -11.405 -24.823 17.964 1.00 20.96 ? 133 ILE A N     1 
ATOM   821  C  CA    . ILE A 1 126 ? -11.080 -23.546 18.587 1.00 19.89 ? 133 ILE A CA    1 
ATOM   822  C  C     . ILE A 1 126 ? -9.578  -23.500 18.809 1.00 19.93 ? 133 ILE A C     1 
ATOM   823  O  O     . ILE A 1 126 ? -9.017  -24.378 19.476 1.00 23.16 ? 133 ILE A O     1 
ATOM   824  C  CB    . ILE A 1 126 ? -11.827 -23.356 19.914 1.00 20.87 ? 133 ILE A CB    1 
ATOM   825  C  CG1   . ILE A 1 126 ? -13.333 -23.310 19.677 1.00 18.33 ? 133 ILE A CG1   1 
ATOM   826  C  CG2   . ILE A 1 126 ? -11.355 -22.089 20.613 1.00 18.32 ? 133 ILE A CG2   1 
ATOM   827  C  CD1   . ILE A 1 126 ? -14.131 -23.345 20.946 1.00 19.43 ? 133 ILE A CD1   1 
ATOM   828  N  N     . ASP A 1 127 ? -8.925  -22.474 18.263 1.00 16.94 ? 134 ASP A N     1 
ATOM   829  C  CA    . ASP A 1 127 ? -7.501  -22.301 18.521 1.00 18.58 ? 134 ASP A CA    1 
ATOM   830  C  C     . ASP A 1 127 ? -7.261  -21.544 19.824 1.00 17.98 ? 134 ASP A C     1 
ATOM   831  O  O     . ASP A 1 127 ? -6.371  -21.909 20.600 1.00 22.80 ? 134 ASP A O     1 
ATOM   832  C  CB    . ASP A 1 127 ? -6.836  -21.580 17.344 1.00 21.58 ? 134 ASP A CB    1 
ATOM   833  C  CG    . ASP A 1 127 ? -6.788  -22.432 16.080 1.00 22.71 ? 134 ASP A CG    1 
ATOM   834  O  OD1   . ASP A 1 127 ? -5.907  -23.315 15.981 1.00 22.33 ? 134 ASP A OD1   1 
ATOM   835  O  OD2   . ASP A 1 127 ? -7.635  -22.224 15.184 1.00 21.64 ? 134 ASP A OD2   1 
ATOM   836  N  N     . ILE A 1 128 ? -8.047  -20.501 20.086 1.00 16.06 ? 135 ILE A N     1 
ATOM   837  C  CA    . ILE A 1 128 ? -7.843  -19.620 21.231 1.00 16.19 ? 135 ILE A CA    1 
ATOM   838  C  C     . ILE A 1 128 ? -9.200  -19.293 21.846 1.00 19.20 ? 135 ILE A C     1 
ATOM   839  O  O     . ILE A 1 128 ? -10.181 -19.068 21.129 1.00 14.37 ? 135 ILE A O     1 
ATOM   840  C  CB    . ILE A 1 128 ? -7.098  -18.325 20.824 1.00 17.76 ? 135 ILE A CB    1 
ATOM   841  C  CG1   . ILE A 1 128 ? -5.718  -18.643 20.231 1.00 19.62 ? 135 ILE A CG1   1 
ATOM   842  C  CG2   . ILE A 1 128 ? -6.948  -17.377 22.007 1.00 13.71 ? 135 ILE A CG2   1 
ATOM   843  C  CD1   . ILE A 1 128 ? -5.312  -17.750 19.059 1.00 19.13 ? 135 ILE A CD1   1 
ATOM   844  N  N     . LEU A 1 129 ? -9.259  -19.286 23.176 1.00 15.71 ? 136 LEU A N     1 
ATOM   845  C  CA    . LEU A 1 129 ? -10.416 -18.788 23.909 1.00 15.77 ? 136 LEU A CA    1 
ATOM   846  C  C     . LEU A 1 129 ? -9.930  -17.696 24.848 1.00 15.68 ? 136 LEU A C     1 
ATOM   847  O  O     . LEU A 1 129 ? -9.077  -17.949 25.704 1.00 15.94 ? 136 LEU A O     1 
ATOM   848  C  CB    . LEU A 1 129 ? -11.115 -19.911 24.682 1.00 20.32 ? 136 LEU A CB    1 
ATOM   849  C  CG    . LEU A 1 129 ? -12.595 -19.698 25.007 1.00 21.59 ? 136 LEU A CG    1 
ATOM   850  C  CD1   . LEU A 1 129 ? -13.230 -21.027 25.341 1.00 23.83 ? 136 LEU A CD1   1 
ATOM   851  C  CD2   . LEU A 1 129 ? -12.775 -18.729 26.160 1.00 21.15 ? 136 LEU A CD2   1 
ATOM   852  N  N     . ALA A 1 130 ? -10.457 -16.487 24.686 1.00 12.65 ? 137 ALA A N     1 
ATOM   853  C  CA    . ALA A 1 130 ? -10.035 -15.343 25.482 1.00 15.41 ? 137 ALA A CA    1 
ATOM   854  C  C     . ALA A 1 130 ? -11.131 -14.974 26.472 1.00 14.56 ? 137 ALA A C     1 
ATOM   855  O  O     . ALA A 1 130 ? -12.298 -14.848 26.091 1.00 13.22 ? 137 ALA A O     1 
ATOM   856  C  CB    . ALA A 1 130 ? -9.702  -14.147 24.587 1.00 13.63 ? 137 ALA A CB    1 
ATOM   857  N  N     . CYS A 1 131 ? -10.758 -14.805 27.740 1.00 11.49 ? 138 CYS A N     1 
ATOM   858  C  CA    . CYS A 1 131 ? -11.687 -14.383 28.780 1.00 13.73 ? 138 CYS A CA    1 
ATOM   859  C  C     . CYS A 1 131 ? -11.240 -13.047 29.354 1.00 15.69 ? 138 CYS A C     1 
ATOM   860  O  O     . CYS A 1 131 ? -10.047 -12.825 29.584 1.00 15.66 ? 138 CYS A O     1 
ATOM   861  C  CB    . CYS A 1 131 ? -11.798 -15.425 29.902 1.00 17.96 ? 138 CYS A CB    1 
ATOM   862  S  SG    . CYS A 1 131 ? -13.110 -15.093 31.119 1.00 14.44 ? 138 CYS A SG    1 
ATOM   863  N  N     . SER A 1 132 ? -12.205 -12.165 29.593 1.00 11.12 ? 139 SER A N     1 
ATOM   864  C  CA    . SER A 1 132 ? -11.920 -10.819 30.067 1.00 12.87 ? 139 SER A CA    1 
ATOM   865  C  C     . SER A 1 132 ? -11.888 -10.771 31.588 1.00 19.24 ? 139 SER A C     1 
ATOM   866  O  O     . SER A 1 132 ? -12.725 -11.375 32.264 1.00 21.74 ? 139 SER A O     1 
ATOM   867  C  CB    . SER A 1 132 ? -12.961 -9.832  29.536 1.00 16.25 ? 139 SER A CB    1 
ATOM   868  O  OG    . SER A 1 132 ? -12.864 -9.711  28.130 1.00 12.94 ? 139 SER A OG    1 
ATOM   869  N  N     . CYS A 1 133 ? -10.903 -10.051 32.118 1.00 13.38 ? 140 CYS A N     1 
ATOM   870  C  CA    . CYS A 1 133 ? -10.822 -9.787  33.551 1.00 17.82 ? 140 CYS A CA    1 
ATOM   871  C  C     . CYS A 1 133 ? -9.999  -8.524  33.733 1.00 17.40 ? 140 CYS A C     1 
ATOM   872  O  O     . CYS A 1 133 ? -8.814  -8.507  33.388 1.00 15.41 ? 140 CYS A O     1 
ATOM   873  C  CB    . CYS A 1 133 ? -10.198 -10.960 34.303 1.00 19.90 ? 140 CYS A CB    1 
ATOM   874  S  SG    . CYS A 1 133 ? -10.321 -10.819 36.100 1.00 22.86 ? 140 CYS A SG    1 
ATOM   875  N  N     . ASP A 1 134 ? -10.625 -7.471  34.257 1.00 17.81 ? 141 ASP A N     1 
ATOM   876  C  CA    . ASP A 1 134 ? -9.985  -6.168  34.368 1.00 15.62 ? 141 ASP A CA    1 
ATOM   877  C  C     . ASP A 1 134 ? -9.320  -5.937  35.716 1.00 18.99 ? 141 ASP A C     1 
ATOM   878  O  O     . ASP A 1 134 ? -8.479  -5.037  35.831 1.00 20.19 ? 141 ASP A O     1 
ATOM   879  C  CB    . ASP A 1 134 ? -11.010 -5.059  34.106 1.00 15.07 ? 141 ASP A CB    1 
ATOM   880  C  CG    . ASP A 1 134 ? -11.848 -5.326  32.871 1.00 18.81 ? 141 ASP A CG    1 
ATOM   881  O  OD1   . ASP A 1 134 ? -11.266 -5.628  31.806 1.00 19.29 ? 141 ASP A OD1   1 
ATOM   882  O  OD2   . ASP A 1 134 ? -13.090 -5.242  32.970 1.00 23.74 ? 141 ASP A OD2   1 
ATOM   883  N  N     . SER A 1 135 ? -9.670  -6.725  36.728 1.00 17.05 ? 142 SER A N     1 
ATOM   884  C  CA    . SER A 1 135 ? -9.026  -6.644  38.027 1.00 16.11 ? 142 SER A CA    1 
ATOM   885  C  C     . SER A 1 135 ? -9.176  -7.986  38.723 1.00 17.80 ? 142 SER A C     1 
ATOM   886  O  O     . SER A 1 135 ? -10.133 -8.727  38.478 1.00 19.71 ? 142 SER A O     1 
ATOM   887  C  CB    . SER A 1 135 ? -9.622  -5.527  38.895 1.00 18.27 ? 142 SER A CB    1 
ATOM   888  O  OG    . SER A 1 135 ? -9.126  -5.587  40.223 1.00 16.84 ? 142 SER A OG    1 
ATOM   889  N  N     . PHE A 1 136 ? -8.205  -8.303  39.574 1.00 17.60 ? 143 PHE A N     1 
ATOM   890  C  CA    . PHE A 1 136 ? -8.315  -9.433  40.481 1.00 22.51 ? 143 PHE A CA    1 
ATOM   891  C  C     . PHE A 1 136 ? -8.752  -8.990  41.869 1.00 21.49 ? 143 PHE A C     1 
ATOM   892  O  O     . PHE A 1 136 ? -8.678  -9.774  42.820 1.00 22.43 ? 143 PHE A O     1 
ATOM   893  C  CB    . PHE A 1 136 ? -6.996  -10.201 40.527 1.00 19.51 ? 143 PHE A CB    1 
ATOM   894  C  CG    . PHE A 1 136 ? -6.636  -10.844 39.215 1.00 18.63 ? 143 PHE A CG    1 
ATOM   895  C  CD1   . PHE A 1 136 ? -5.912  -10.146 38.266 1.00 17.28 ? 143 PHE A CD1   1 
ATOM   896  C  CD2   . PHE A 1 136 ? -7.045  -12.133 38.919 1.00 19.70 ? 143 PHE A CD2   1 
ATOM   897  C  CE1   . PHE A 1 136 ? -5.584  -10.722 37.052 1.00 15.88 ? 143 PHE A CE1   1 
ATOM   898  C  CE2   . PHE A 1 136 ? -6.721  -12.717 37.706 1.00 21.14 ? 143 PHE A CE2   1 
ATOM   899  C  CZ    . PHE A 1 136 ? -5.990  -12.009 36.772 1.00 19.85 ? 143 PHE A CZ    1 
ATOM   900  N  N     . ASP A 1 137 ? -9.200  -7.743  41.994 1.00 21.09 ? 144 ASP A N     1 
ATOM   901  C  CA    . ASP A 1 137 ? -9.853  -7.213  43.184 1.00 23.60 ? 144 ASP A CA    1 
ATOM   902  C  C     . ASP A 1 137 ? -11.337 -7.139  42.843 1.00 20.42 ? 144 ASP A C     1 
ATOM   903  O  O     . ASP A 1 137 ? -11.764 -6.260  42.090 1.00 18.00 ? 144 ASP A O     1 
ATOM   904  C  CB    . ASP A 1 137 ? -9.271  -5.849  43.556 1.00 18.74 ? 144 ASP A CB    1 
ATOM   905  C  CG    . ASP A 1 137 ? -10.085 -5.121  44.614 1.00 21.20 ? 144 ASP A CG    1 
ATOM   906  O  OD1   . ASP A 1 137 ? -10.867 -5.769  45.340 1.00 20.09 ? 144 ASP A OD1   1 
ATOM   907  O  OD2   . ASP A 1 137 ? -9.937  -3.885  44.718 1.00 25.33 ? 144 ASP A OD2   1 
ATOM   908  N  N     . GLU A 1 138 ? -12.120 -8.069  43.400 1.00 22.78 ? 145 GLU A N     1 
ATOM   909  C  CA    . GLU A 1 138 ? -13.513 -8.225  42.990 1.00 21.52 ? 145 GLU A CA    1 
ATOM   910  C  C     . GLU A 1 138 ? -14.355 -6.989  43.275 1.00 20.13 ? 145 GLU A C     1 
ATOM   911  O  O     . GLU A 1 138 ? -15.385 -6.793  42.620 1.00 21.27 ? 145 GLU A O     1 
ATOM   912  C  CB    . GLU A 1 138 ? -14.130 -9.444  43.675 1.00 25.14 ? 145 GLU A CB    1 
ATOM   913  C  CG    . GLU A 1 138 ? -13.471 -10.765 43.306 1.00 24.95 ? 145 GLU A CG    1 
ATOM   914  C  CD    . GLU A 1 138 ? -13.947 -11.321 41.973 1.00 27.17 ? 145 GLU A CD    1 
ATOM   915  O  OE1   . GLU A 1 138 ? -14.544 -10.569 41.172 1.00 23.36 ? 145 GLU A OE1   1 
ATOM   916  O  OE2   . GLU A 1 138 ? -13.729 -12.527 41.736 1.00 30.57 ? 145 GLU A OE2   1 
ATOM   917  N  N     . ASN A 1 139 ? -13.949 -6.153  44.230 1.00 18.16 ? 146 ASN A N     1 
ATOM   918  C  CA    . ASN A 1 139 ? -14.668 -4.905  44.453 1.00 20.85 ? 146 ASN A CA    1 
ATOM   919  C  C     . ASN A 1 139 ? -14.581 -4.000  43.232 1.00 20.77 ? 146 ASN A C     1 
ATOM   920  O  O     . ASN A 1 139 ? -15.556 -3.325  42.881 1.00 20.80 ? 146 ASN A O     1 
ATOM   921  C  CB    . ASN A 1 139 ? -14.121 -4.194  45.687 1.00 18.84 ? 146 ASN A CB    1 
ATOM   922  C  CG    . ASN A 1 139 ? -14.523 -4.877  46.970 1.00 22.17 ? 146 ASN A CG    1 
ATOM   923  O  OD1   . ASN A 1 139 ? -15.704 -5.128  47.208 1.00 24.29 ? 146 ASN A OD1   1 
ATOM   924  N  ND2   . ASN A 1 139 ? -13.541 -5.193  47.804 1.00 19.16 ? 146 ASN A ND2   1 
ATOM   925  N  N     . MET A 1 140 ? -13.421 -3.974  42.570 1.00 17.72 ? 147 MET A N     1 
ATOM   926  C  CA    . MET A 1 140 ? -13.270 -3.142  41.382 1.00 23.25 ? 147 MET A CA    1 
ATOM   927  C  C     . MET A 1 140 ? -14.029 -3.716  40.193 1.00 20.22 ? 147 MET A C     1 
ATOM   928  O  O     . MET A 1 140 ? -14.441 -2.964  39.304 1.00 21.62 ? 147 MET A O     1 
ATOM   929  C  CB    . MET A 1 140 ? -11.788 -2.975  41.045 1.00 23.29 ? 147 MET A CB    1 
ATOM   930  C  CG    . MET A 1 140 ? -11.356 -1.533  40.825 1.00 22.13 ? 147 MET A CG    1 
ATOM   931  S  SD    . MET A 1 140 ? -11.576 -0.518  42.301 1.00 33.50 ? 147 MET A SD    1 
ATOM   932  C  CE    . MET A 1 140 ? -9.921  -0.501  42.988 1.00 28.17 ? 147 MET A CE    1 
ATOM   933  N  N     . ASN A 1 141 ? -14.214 -5.039  40.152 1.00 18.83 ? 148 ASN A N     1 
ATOM   934  C  CA    . ASN A 1 141 ? -15.060 -5.629  39.121 1.00 21.35 ? 148 ASN A CA    1 
ATOM   935  C  C     . ASN A 1 141 ? -16.527 -5.256  39.325 1.00 21.86 ? 148 ASN A C     1 
ATOM   936  O  O     . ASN A 1 141 ? -17.289 -5.186  38.354 1.00 16.11 ? 148 ASN A O     1 
ATOM   937  C  CB    . ASN A 1 141 ? -14.882 -7.150  39.096 1.00 20.15 ? 148 ASN A CB    1 
ATOM   938  C  CG    . ASN A 1 141 ? -13.513 -7.574  38.590 1.00 22.16 ? 148 ASN A CG    1 
ATOM   939  O  OD1   . ASN A 1 141 ? -12.998 -7.023  37.616 1.00 19.84 ? 148 ASN A OD1   1 
ATOM   940  N  ND2   . ASN A 1 141 ? -12.920 -8.565  39.248 1.00 20.66 ? 148 ASN A ND2   1 
ATOM   941  N  N     . ILE A 1 142 ? -16.940 -5.009  40.570 1.00 22.88 ? 149 ILE A N     1 
ATOM   942  C  CA    . ILE A 1 142 ? -18.292 -4.521  40.825 1.00 21.20 ? 149 ILE A CA    1 
ATOM   943  C  C     . ILE A 1 142 ? -18.401 -3.050  40.442 1.00 22.30 ? 149 ILE A C     1 
ATOM   944  O  O     . ILE A 1 142 ? -19.351 -2.634  39.770 1.00 24.82 ? 149 ILE A O     1 
ATOM   945  C  CB    . ILE A 1 142 ? -18.672 -4.752  42.297 1.00 21.76 ? 149 ILE A CB    1 
ATOM   946  C  CG1   . ILE A 1 142 ? -18.977 -6.228  42.545 1.00 20.05 ? 149 ILE A CG1   1 
ATOM   947  C  CG2   . ILE A 1 142 ? -19.872 -3.903  42.679 1.00 21.63 ? 149 ILE A CG2   1 
ATOM   948  C  CD1   . ILE A 1 142 ? -18.582 -6.696  43.919 1.00 21.84 ? 149 ILE A CD1   1 
ATOM   949  N  N     . GLU A 1 143 ? -17.421 -2.245  40.864 1.00 22.11 ? 150 GLU A N     1 
ATOM   950  C  CA    . GLU A 1 143 ? -17.392 -0.835  40.488 1.00 21.54 ? 150 GLU A CA    1 
ATOM   951  C  C     . GLU A 1 143 ? -17.413 -0.665  38.975 1.00 24.35 ? 150 GLU A C     1 
ATOM   952  O  O     . GLU A 1 143 ? -18.092 0.227   38.452 1.00 24.75 ? 150 GLU A O     1 
ATOM   953  C  CB    . GLU A 1 143 ? -16.150 -0.172  41.080 1.00 25.67 ? 150 GLU A CB    1 
ATOM   954  C  CG    . GLU A 1 143 ? -16.344 0.393   42.471 1.00 26.86 ? 150 GLU A CG    1 
ATOM   955  C  CD    . GLU A 1 143 ? -16.355 1.906   42.495 1.00 29.73 ? 150 GLU A CD    1 
ATOM   956  O  OE1   . GLU A 1 143 ? -16.884 2.524   41.546 1.00 35.48 ? 150 GLU A OE1   1 
ATOM   957  O  OE2   . GLU A 1 143 ? -15.827 2.478   43.470 1.00 32.45 ? 150 GLU A OE2   1 
ATOM   958  N  N     . ILE A 1 144 ? -16.671 -1.510  38.258 1.00 20.89 ? 151 ILE A N     1 
ATOM   959  C  CA    . ILE A 1 144 ? -16.648 -1.436  36.801 1.00 19.32 ? 151 ILE A CA    1 
ATOM   960  C  C     . ILE A 1 144 ? -18.005 -1.814  36.225 1.00 20.44 ? 151 ILE A C     1 
ATOM   961  O  O     . ILE A 1 144 ? -18.512 -1.159  35.306 1.00 22.27 ? 151 ILE A O     1 
ATOM   962  C  CB    . ILE A 1 144 ? -15.525 -2.333  36.250 1.00 20.01 ? 151 ILE A CB    1 
ATOM   963  C  CG1   . ILE A 1 144 ? -14.167 -1.650  36.402 1.00 15.77 ? 151 ILE A CG1   1 
ATOM   964  C  CG2   . ILE A 1 144 ? -15.795 -2.724  34.802 1.00 18.17 ? 151 ILE A CG2   1 
ATOM   965  C  CD1   . ILE A 1 144 ? -13.009 -2.592  36.201 1.00 14.11 ? 151 ILE A CD1   1 
ATOM   966  N  N     . GLY A 1 145 ? -18.615 -2.866  36.756 1.00 19.79 ? 152 GLY A N     1 
ATOM   967  C  CA    . GLY A 1 145 ? -19.914 -3.308  36.304 1.00 21.31 ? 152 GLY A CA    1 
ATOM   968  C  C     . GLY A 1 145 ? -19.915 -4.595  35.518 1.00 22.35 ? 152 GLY A C     1 
ATOM   969  O  O     . GLY A 1 145 ? -20.927 -4.904  34.876 1.00 20.94 ? 152 GLY A O     1 
ATOM   970  N  N     . ARG A 1 146 ? -18.819 -5.351  35.541 1.00 21.36 ? 153 ARG A N     1 
ATOM   971  C  CA    . ARG A 1 146 ? -18.728 -6.622  34.836 1.00 23.43 ? 153 ARG A CA    1 
ATOM   972  C  C     . ARG A 1 146 ? -19.424 -7.757  35.573 1.00 26.57 ? 153 ARG A C     1 
ATOM   973  O  O     . ARG A 1 146 ? -19.325 -8.913  35.148 1.00 32.08 ? 153 ARG A O     1 
ATOM   974  C  CB    . ARG A 1 146 ? -17.259 -6.983  34.592 1.00 21.37 ? 153 ARG A CB    1 
ATOM   975  C  CG    . ARG A 1 146 ? -17.063 -7.911  33.400 1.00 22.71 ? 153 ARG A CG    1 
ATOM   976  C  CD    . ARG A 1 146 ? -15.617 -8.326  33.206 1.00 24.56 ? 153 ARG A CD    1 
ATOM   977  N  NE    . ARG A 1 146 ? -14.882 -7.360  32.398 1.00 18.58 ? 153 ARG A NE    1 
ATOM   978  C  CZ    . ARG A 1 146 ? -14.988 -7.245  31.082 1.00 17.84 ? 153 ARG A CZ    1 
ATOM   979  N  NH1   . ARG A 1 146 ? -15.795 -8.025  30.382 1.00 19.08 ? 153 ARG A NH1   1 
ATOM   980  N  NH2   . ARG A 1 146 ? -14.267 -6.322  30.452 1.00 20.30 ? 153 ARG A NH2   1 
ATOM   981  N  N     . GLY A 1 147 ? -20.118 -7.468  36.662 1.00 28.70 ? 154 GLY A N     1 
ATOM   982  C  CA    . GLY A 1 147 ? -20.824 -8.485  37.403 1.00 22.66 ? 154 GLY A CA    1 
ATOM   983  C  C     . GLY A 1 147 ? -20.928 -8.099  38.863 1.00 23.52 ? 154 GLY A C     1 
ATOM   984  O  O     . GLY A 1 147 ? -20.758 -6.938  39.224 1.00 23.94 ? 154 GLY A O     1 
ATOM   985  N  N     . THR A 1 148 ? -21.203 -9.109  39.691 1.00 26.86 ? 155 THR A N     1 
ATOM   986  C  CA    . THR A 1 148 ? -21.437 -8.920  41.117 1.00 28.84 ? 155 THR A CA    1 
ATOM   987  C  C     . THR A 1 148 ? -20.262 -9.390  41.971 1.00 34.81 ? 155 THR A C     1 
ATOM   988  O  O     . THR A 1 148 ? -20.418 -9.578  43.181 1.00 36.12 ? 155 THR A O     1 
ATOM   989  C  CB    . THR A 1 148 ? -22.723 -9.634  41.536 1.00 32.86 ? 155 THR A CB    1 
ATOM   990  O  OG1   . THR A 1 148 ? -22.555 -11.051 41.401 1.00 32.76 ? 155 THR A OG1   1 
ATOM   991  C  CG2   . THR A 1 148 ? -23.891 -9.185  40.666 1.00 22.12 ? 155 THR A CG2   1 
ATOM   992  N  N     . GLY A 1 149 ? -19.091 -9.587  41.367 1.00 35.48 ? 156 GLY A N     1 
ATOM   993  C  CA    . GLY A 1 149 ? -17.890 -9.867  42.133 1.00 27.39 ? 156 GLY A CA    1 
ATOM   994  C  C     . GLY A 1 149 ? -17.397 -11.298 42.078 1.00 26.69 ? 156 GLY A C     1 
ATOM   995  O  O     . GLY A 1 149 ? -16.875 -11.818 43.068 1.00 31.35 ? 156 GLY A O     1 
ATOM   996  N  N     . ASN A 1 150 ? -17.427 -11.904 40.920 1.00 24.14 ? 157 ASN A N     1 
ATOM   997  C  CA    . ASN A 1 150 ? -17.023 -13.282 40.786 1.00 28.06 ? 157 ASN A CA    1 
ATOM   998  C  C     . ASN A 1 150 ? -16.203 -13.489 39.539 1.00 27.95 ? 157 ASN A C     1 
ATOM   999  O  O     . ASN A 1 150 ? -15.972 -14.615 39.138 1.00 29.30 ? 157 ASN A O     1 
ATOM   1000 C  CB    . ASN A 1 150 ? -18.292 -14.116 40.695 1.00 24.39 ? 157 ASN A CB    1 
ATOM   1001 C  CG    . ASN A 1 150 ? -19.212 -13.672 39.583 1.00 24.88 ? 157 ASN A CG    1 
ATOM   1002 O  OD1   . ASN A 1 150 ? -19.353 -12.490 39.308 1.00 25.48 ? 157 ASN A OD1   1 
ATOM   1003 N  ND2   . ASN A 1 150 ? -19.858 -14.627 38.952 1.00 27.87 ? 157 ASN A ND2   1 
ATOM   1004 N  N     . GLN A 1 151 ? -15.765 -12.400 38.921 1.00 24.72 ? 158 GLN A N     1 
ATOM   1005 C  CA    . GLN A 1 151 ? -15.066 -12.494 37.643 1.00 23.36 ? 158 GLN A CA    1 
ATOM   1006 C  C     . GLN A 1 151 ? -13.783 -13.307 37.761 1.00 23.83 ? 158 GLN A C     1 
ATOM   1007 O  O     . GLN A 1 151 ? -13.429 -14.050 36.839 1.00 28.65 ? 158 GLN A O     1 
ATOM   1008 C  CB    . GLN A 1 151 ? -14.773 -11.091 37.101 1.00 26.01 ? 158 GLN A CB    1 
ATOM   1009 C  CG    . GLN A 1 151 ? -14.431 -11.044 35.610 1.00 22.14 ? 158 GLN A CG    1 
ATOM   1010 C  CD    . GLN A 1 151 ? -15.549 -11.564 34.717 1.00 24.33 ? 158 GLN A CD    1 
ATOM   1011 O  OE1   . GLN A 1 151 ? -16.725 -11.528 35.082 1.00 22.18 ? 158 GLN A OE1   1 
ATOM   1012 N  NE2   . GLN A 1 151 ? -15.182 -12.051 33.536 1.00 20.30 ? 158 GLN A NE2   1 
ATOM   1013 N  N     . VAL A 1 152 ? -13.072 -13.185 38.884 1.00 20.98 ? 159 VAL A N     1 
ATOM   1014 C  CA    . VAL A 1 152 ? -11.849 -13.961 39.060 1.00 26.69 ? 159 VAL A CA    1 
ATOM   1015 C  C     . VAL A 1 152 ? -12.171 -15.448 39.157 1.00 24.16 ? 159 VAL A C     1 
ATOM   1016 O  O     . VAL A 1 152 ? -11.450 -16.290 38.609 1.00 23.83 ? 159 VAL A O     1 
ATOM   1017 C  CB    . VAL A 1 152 ? -11.072 -13.458 40.288 1.00 28.25 ? 159 VAL A CB    1 
ATOM   1018 C  CG1   . VAL A 1 152 ? -9.768  -14.223 40.441 1.00 21.86 ? 159 VAL A CG1   1 
ATOM   1019 C  CG2   . VAL A 1 152 ? -10.815 -11.969 40.167 1.00 21.68 ? 159 VAL A CG2   1 
ATOM   1020 N  N     . GLU A 1 153 ? -13.259 -15.796 39.849 1.00 23.75 ? 160 GLU A N     1 
ATOM   1021 C  CA    . GLU A 1 153 ? -13.708 -17.185 39.871 1.00 25.63 ? 160 GLU A CA    1 
ATOM   1022 C  C     . GLU A 1 153 ? -14.061 -17.660 38.467 1.00 25.76 ? 160 GLU A C     1 
ATOM   1023 O  O     . GLU A 1 153 ? -13.656 -18.750 38.045 1.00 19.19 ? 160 GLU A O     1 
ATOM   1024 C  CB    . GLU A 1 153 ? -14.907 -17.331 40.808 1.00 26.36 ? 160 GLU A CB    1 
ATOM   1025 C  CG    . GLU A 1 153 ? -15.308 -18.772 41.088 1.00 26.53 ? 160 GLU A CG    1 
ATOM   1026 C  CD    . GLU A 1 153 ? -16.263 -19.329 40.047 1.00 24.50 ? 160 GLU A CD    1 
ATOM   1027 O  OE1   . GLU A 1 153 ? -17.136 -18.574 39.571 1.00 26.21 ? 160 GLU A OE1   1 
ATOM   1028 O  OE2   . GLU A 1 153 ? -16.132 -20.521 39.696 1.00 22.63 ? 160 GLU A OE2   1 
ATOM   1029 N  N     . ILE A 1 154 ? -14.831 -16.852 37.734 1.00 28.06 ? 161 ILE A N     1 
ATOM   1030 C  CA    . ILE A 1 154 ? -15.135 -17.153 36.337 1.00 22.87 ? 161 ILE A CA    1 
ATOM   1031 C  C     . ILE A 1 154 ? -13.847 -17.312 35.541 1.00 24.26 ? 161 ILE A C     1 
ATOM   1032 O  O     . ILE A 1 154 ? -13.687 -18.257 34.759 1.00 26.90 ? 161 ILE A O     1 
ATOM   1033 C  CB    . ILE A 1 154 ? -16.027 -16.051 35.737 1.00 22.24 ? 161 ILE A CB    1 
ATOM   1034 C  CG1   . ILE A 1 154 ? -17.398 -16.022 36.418 1.00 24.70 ? 161 ILE A CG1   1 
ATOM   1035 C  CG2   . ILE A 1 154 ? -16.163 -16.233 34.240 1.00 20.77 ? 161 ILE A CG2   1 
ATOM   1036 C  CD1   . ILE A 1 154 ? -18.228 -14.804 36.060 1.00 19.41 ? 161 ILE A CD1   1 
ATOM   1037 N  N     . LEU A 1 155 ? -12.903 -16.391 35.747 1.00 25.23 ? 162 LEU A N     1 
ATOM   1038 C  CA    . LEU A 1 155 ? -11.670 -16.366 34.965 1.00 25.30 ? 162 LEU A CA    1 
ATOM   1039 C  C     . LEU A 1 155 ? -10.897 -17.673 35.110 1.00 22.87 ? 162 LEU A C     1 
ATOM   1040 O  O     . LEU A 1 155 ? -10.590 -18.341 34.116 1.00 25.51 ? 162 LEU A O     1 
ATOM   1041 C  CB    . LEU A 1 155 ? -10.815 -15.171 35.398 1.00 27.47 ? 162 LEU A CB    1 
ATOM   1042 C  CG    . LEU A 1 155 ? -9.729  -14.628 34.464 1.00 27.81 ? 162 LEU A CG    1 
ATOM   1043 C  CD1   . LEU A 1 155 ? -8.473  -15.455 34.555 1.00 29.66 ? 162 LEU A CD1   1 
ATOM   1044 C  CD2   . LEU A 1 155 ? -10.214 -14.578 33.033 1.00 21.81 ? 162 LEU A CD2   1 
ATOM   1045 N  N     . TYR A 1 156 ? -10.568 -18.049 36.350 1.00 25.32 ? 163 TYR A N     1 
ATOM   1046 C  CA    . TYR A 1 156 ? -9.776  -19.254 36.582 1.00 20.81 ? 163 TYR A CA    1 
ATOM   1047 C  C     . TYR A 1 156 ? -10.486 -20.507 36.084 1.00 22.34 ? 163 TYR A C     1 
ATOM   1048 O  O     . TYR A 1 156 ? -9.830  -21.441 35.607 1.00 21.50 ? 163 TYR A O     1 
ATOM   1049 C  CB    . TYR A 1 156 ? -9.449  -19.390 38.070 1.00 23.27 ? 163 TYR A CB    1 
ATOM   1050 C  CG    . TYR A 1 156 ? -8.201  -18.648 38.497 1.00 23.19 ? 163 TYR A CG    1 
ATOM   1051 C  CD1   . TYR A 1 156 ? -6.953  -19.252 38.428 1.00 19.93 ? 163 TYR A CD1   1 
ATOM   1052 C  CD2   . TYR A 1 156 ? -8.272  -17.346 38.973 1.00 22.18 ? 163 TYR A CD2   1 
ATOM   1053 C  CE1   . TYR A 1 156 ? -5.809  -18.577 38.816 1.00 25.73 ? 163 TYR A CE1   1 
ATOM   1054 C  CE2   . TYR A 1 156 ? -7.133  -16.664 39.365 1.00 18.91 ? 163 TYR A CE2   1 
ATOM   1055 C  CZ    . TYR A 1 156 ? -5.905  -17.283 39.284 1.00 23.17 ? 163 TYR A CZ    1 
ATOM   1056 O  OH    . TYR A 1 156 ? -4.772  -16.605 39.673 1.00 27.71 ? 163 TYR A OH    1 
ATOM   1057 N  N     . ARG A 1 157 ? -11.817 -20.550 36.185 1.00 23.21 ? 164 ARG A N     1 
ATOM   1058 C  CA    . ARG A 1 157 ? -12.553 -21.721 35.717 1.00 26.68 ? 164 ARG A CA    1 
ATOM   1059 C  C     . ARG A 1 157 ? -12.486 -21.849 34.200 1.00 28.34 ? 164 ARG A C     1 
ATOM   1060 O  O     . ARG A 1 157 ? -12.376 -22.962 33.671 1.00 28.68 ? 164 ARG A O     1 
ATOM   1061 C  CB    . ARG A 1 157 ? -14.005 -21.653 36.189 1.00 22.99 ? 164 ARG A CB    1 
ATOM   1062 C  CG    . ARG A 1 157 ? -14.763 -22.963 36.042 1.00 26.24 ? 164 ARG A CG    1 
ATOM   1063 C  CD    . ARG A 1 157 ? -15.955 -23.035 36.987 1.00 26.74 ? 164 ARG A CD    1 
ATOM   1064 N  NE    . ARG A 1 157 ? -16.566 -21.730 37.214 1.00 26.38 ? 164 ARG A NE    1 
ATOM   1065 C  CZ    . ARG A 1 157 ? -17.383 -21.123 36.363 1.00 21.03 ? 164 ARG A CZ    1 
ATOM   1066 N  NH1   . ARG A 1 157 ? -17.712 -21.673 35.206 1.00 26.34 ? 164 ARG A NH1   1 
ATOM   1067 N  NH2   . ARG A 1 157 ? -17.880 -19.931 36.680 1.00 23.80 ? 164 ARG A NH2   1 
ATOM   1068 N  N     . ILE A 1 158 ? -12.553 -20.724 33.483 1.00 25.71 ? 165 ILE A N     1 
ATOM   1069 C  CA    . ILE A 1 158 ? -12.405 -20.754 32.030 1.00 26.63 ? 165 ILE A CA    1 
ATOM   1070 C  C     . ILE A 1 158 ? -11.028 -21.287 31.653 1.00 24.93 ? 165 ILE A C     1 
ATOM   1071 O  O     . ILE A 1 158 ? -10.891 -22.132 30.760 1.00 26.03 ? 165 ILE A O     1 
ATOM   1072 C  CB    . ILE A 1 158 ? -12.646 -19.354 31.435 1.00 27.92 ? 165 ILE A CB    1 
ATOM   1073 C  CG1   . ILE A 1 158 ? -14.089 -18.905 31.678 1.00 23.06 ? 165 ILE A CG1   1 
ATOM   1074 C  CG2   . ILE A 1 158 ? -12.321 -19.333 29.943 1.00 28.12 ? 165 ILE A CG2   1 
ATOM   1075 C  CD1   . ILE A 1 158 ? -15.109 -19.652 30.861 1.00 21.07 ? 165 ILE A CD1   1 
ATOM   1076 N  N     . ALA A 1 159 ? -9.987  -20.807 32.338 1.00 25.77 ? 166 ALA A N     1 
ATOM   1077 C  CA    . ALA A 1 159 ? -8.633  -21.257 32.035 1.00 25.94 ? 166 ALA A CA    1 
ATOM   1078 C  C     . ALA A 1 159 ? -8.443  -22.727 32.390 1.00 28.43 ? 166 ALA A C     1 
ATOM   1079 O  O     . ALA A 1 159 ? -7.712  -23.445 31.698 1.00 26.95 ? 166 ALA A O     1 
ATOM   1080 C  CB    . ALA A 1 159 ? -7.612  -20.391 32.773 1.00 21.88 ? 166 ALA A CB    1 
ATOM   1081 N  N     . LYS A 1 160 ? -9.079  -23.189 33.469 1.00 27.97 ? 167 LYS A N     1 
ATOM   1082 C  CA    . LYS A 1 160 ? -9.018  -24.609 33.804 1.00 32.31 ? 167 LYS A CA    1 
ATOM   1083 C  C     . LYS A 1 160 ? -9.610  -25.455 32.687 1.00 30.47 ? 167 LYS A C     1 
ATOM   1084 O  O     . LYS A 1 160 ? -9.054  -26.497 32.320 1.00 33.94 ? 167 LYS A O     1 
ATOM   1085 C  CB    . LYS A 1 160 ? -9.750  -24.877 35.119 1.00 34.90 ? 167 LYS A CB    1 
ATOM   1086 C  CG    . LYS A 1 160 ? -9.422  -26.229 35.734 1.00 36.31 ? 167 LYS A CG    1 
ATOM   1087 C  CD    . LYS A 1 160 ? -10.667 -26.927 36.264 1.00 30.30 ? 167 LYS A CD    1 
ATOM   1088 C  CE    . LYS A 1 160 ? -11.378 -26.088 37.317 1.00 34.44 ? 167 LYS A CE    1 
ATOM   1089 N  NZ    . LYS A 1 160 ? -12.850 -26.332 37.340 1.00 42.97 ? 167 LYS A NZ    1 
ATOM   1090 N  N     . TRP A 1 161 ? -10.740 -25.015 32.132 1.00 30.50 ? 168 TRP A N     1 
ATOM   1091 C  CA    . TRP A 1 161 ? -11.372 -25.745 31.041 1.00 26.48 ? 168 TRP A CA    1 
ATOM   1092 C  C     . TRP A 1 161 ? -10.513 -25.715 29.782 1.00 27.26 ? 168 TRP A C     1 
ATOM   1093 O  O     . TRP A 1 161 ? -10.449 -26.704 29.044 1.00 30.07 ? 168 TRP A O     1 
ATOM   1094 C  CB    . TRP A 1 161 ? -12.753 -25.161 30.759 1.00 28.55 ? 168 TRP A CB    1 
ATOM   1095 C  CG    . TRP A 1 161 ? -13.751 -25.410 31.847 1.00 28.50 ? 168 TRP A CG    1 
ATOM   1096 C  CD1   . TRP A 1 161 ? -13.663 -26.332 32.850 1.00 25.10 ? 168 TRP A CD1   1 
ATOM   1097 C  CD2   . TRP A 1 161 ? -14.999 -24.734 32.031 1.00 29.01 ? 168 TRP A CD2   1 
ATOM   1098 N  NE1   . TRP A 1 161 ? -14.778 -26.264 33.652 1.00 31.24 ? 168 TRP A NE1   1 
ATOM   1099 C  CE2   . TRP A 1 161 ? -15.614 -25.292 33.168 1.00 30.20 ? 168 TRP A CE2   1 
ATOM   1100 C  CE3   . TRP A 1 161 ? -15.654 -23.707 31.344 1.00 28.35 ? 168 TRP A CE3   1 
ATOM   1101 C  CZ2   . TRP A 1 161 ? -16.854 -24.858 33.634 1.00 34.54 ? 168 TRP A CZ2   1 
ATOM   1102 C  CZ3   . TRP A 1 161 ? -16.883 -23.278 31.808 1.00 30.36 ? 168 TRP A CZ3   1 
ATOM   1103 C  CH2   . TRP A 1 161 ? -17.471 -23.853 32.940 1.00 30.48 ? 168 TRP A CH2   1 
ATOM   1104 N  N     . CYS A 1 162 ? -9.843  -24.588 29.522 1.00 28.25 ? 169 CYS A N     1 
ATOM   1105 C  CA    . CYS A 1 162 ? -9.033  -24.471 28.312 1.00 28.44 ? 169 CYS A CA    1 
ATOM   1106 C  C     . CYS A 1 162 ? -7.865  -25.446 28.325 1.00 27.19 ? 169 CYS A C     1 
ATOM   1107 O  O     . CYS A 1 162 ? -7.583  -26.102 27.315 1.00 30.10 ? 169 CYS A O     1 
ATOM   1108 C  CB    . CYS A 1 162 ? -8.528  -23.039 28.154 1.00 22.91 ? 169 CYS A CB    1 
ATOM   1109 S  SG    . CYS A 1 162 ? -9.809  -21.860 27.704 1.00 20.93 ? 169 CYS A SG    1 
ATOM   1110 N  N     . ARG A 1 163 ? -7.171  -25.553 29.458 1.00 31.23 ? 170 ARG A N     1 
ATOM   1111 C  CA    . ARG A 1 163 ? -6.036  -26.464 29.551 1.00 31.06 ? 170 ARG A CA    1 
ATOM   1112 C  C     . ARG A 1 163 ? -6.468  -27.924 29.565 1.00 32.34 ? 170 ARG A C     1 
ATOM   1113 O  O     . ARG A 1 163 ? -5.668  -28.797 29.213 1.00 31.11 ? 170 ARG A O     1 
ATOM   1114 C  CB    . ARG A 1 163 ? -5.210  -26.151 30.800 1.00 26.87 ? 170 ARG A CB    1 
ATOM   1115 C  CG    . ARG A 1 163 ? -4.151  -25.069 30.604 1.00 27.20 ? 170 ARG A CG    1 
ATOM   1116 C  CD    . ARG A 1 163 ? -4.782  -23.690 30.528 1.00 24.42 ? 170 ARG A CD    1 
ATOM   1117 N  NE    . ARG A 1 163 ? -3.811  -22.648 30.218 1.00 21.53 ? 170 ARG A NE    1 
ATOM   1118 C  CZ    . ARG A 1 163 ? -3.309  -21.803 31.107 1.00 20.35 ? 170 ARG A CZ    1 
ATOM   1119 N  NH1   . ARG A 1 163 ? -3.662  -21.849 32.382 1.00 21.46 ? 170 ARG A NH1   1 
ATOM   1120 N  NH2   . ARG A 1 163 ? -2.432  -20.886 30.707 1.00 22.81 ? 170 ARG A NH2   1 
ATOM   1121 N  N     . LYS A 1 164 ? -7.710  -28.207 29.961 1.00 33.62 ? 171 LYS A N     1 
ATOM   1122 C  CA    . LYS A 1 164 ? -8.206  -29.579 29.917 1.00 36.78 ? 171 LYS A CA    1 
ATOM   1123 C  C     . LYS A 1 164 ? -8.328  -30.068 28.480 1.00 36.07 ? 171 LYS A C     1 
ATOM   1124 O  O     . LYS A 1 164 ? -7.779  -31.116 28.118 1.00 39.70 ? 171 LYS A O     1 
ATOM   1125 C  CB    . LYS A 1 164 ? -9.557  -29.677 30.630 1.00 35.46 ? 171 LYS A CB    1 
ATOM   1126 C  CG    . LYS A 1 164 ? -9.501  -30.217 32.058 1.00 37.51 ? 171 LYS A CG    1 
ATOM   1127 C  CD    . LYS A 1 164 ? -8.561  -31.412 32.216 1.00 40.48 ? 171 LYS A CD    1 
ATOM   1128 C  CE    . LYS A 1 164 ? -9.001  -32.615 31.391 1.00 39.59 ? 171 LYS A CE    1 
ATOM   1129 N  NZ    . LYS A 1 164 ? -7.892  -33.594 31.231 1.00 41.68 ? 171 LYS A NZ    1 
ATOM   1130 N  N     . ASN A 1 165 ? -9.044  -29.316 27.646 1.00 33.46 ? 172 ASN A N     1 
ATOM   1131 C  CA    . ASN A 1 165 ? -9.289  -29.687 26.261 1.00 33.11 ? 172 ASN A CA    1 
ATOM   1132 C  C     . ASN A 1 165 ? -8.356  -28.973 25.289 1.00 36.01 ? 172 ASN A C     1 
ATOM   1133 O  O     . ASN A 1 165 ? -8.682  -28.848 24.103 1.00 35.75 ? 172 ASN A O     1 
ATOM   1134 C  CB    . ASN A 1 165 ? -10.752 -29.431 25.910 1.00 30.07 ? 172 ASN A CB    1 
ATOM   1135 C  CG    . ASN A 1 165 ? -11.681 -29.763 27.058 1.00 30.50 ? 172 ASN A CG    1 
ATOM   1136 O  OD1   . ASN A 1 165 ? -12.427 -28.913 27.540 1.00 33.81 ? 172 ASN A OD1   1 
ATOM   1137 N  ND2   . ASN A 1 165 ? -11.629 -31.010 27.513 1.00 32.10 ? 172 ASN A ND2   1 
ATOM   1138 N  N     . GLU A 1 166 ? -7.217  -28.483 25.781 1.00 32.38 ? 173 GLU A N     1 
ATOM   1139 C  CA    . GLU A 1 166 ? -6.070  -28.122 24.945 1.00 38.05 ? 173 GLU A CA    1 
ATOM   1140 C  C     . GLU A 1 166 ? -6.382  -26.961 24.000 1.00 34.33 ? 173 GLU A C     1 
ATOM   1141 O  O     . GLU A 1 166 ? -6.008  -26.978 22.828 1.00 31.81 ? 173 GLU A O     1 
ATOM   1142 C  CB    . GLU A 1 166 ? -5.570  -29.348 24.175 1.00 41.28 ? 173 GLU A CB    1 
ATOM   1143 C  CG    . GLU A 1 166 ? -5.103  -30.457 25.114 1.00 43.09 ? 173 GLU A CG    1 
ATOM   1144 C  CD    . GLU A 1 166 ? -4.263  -31.523 24.440 1.00 54.49 ? 173 GLU A CD    1 
ATOM   1145 O  OE1   . GLU A 1 166 ? -4.627  -31.955 23.330 1.00 54.18 ? 173 GLU A OE1   1 
ATOM   1146 O  OE2   . GLU A 1 166 ? -3.235  -31.927 25.026 1.00 53.74 ? 173 GLU A OE2   1 
ATOM   1147 N  N     . ILE A 1 167 ? -7.063  -25.944 24.516 1.00 30.78 ? 174 ILE A N     1 
ATOM   1148 C  CA    . ILE A 1 167 ? -7.268  -24.687 23.806 1.00 28.32 ? 174 ILE A CA    1 
ATOM   1149 C  C     . ILE A 1 167 ? -6.290  -23.663 24.362 1.00 25.54 ? 174 ILE A C     1 
ATOM   1150 O  O     . ILE A 1 167 ? -6.083  -23.587 25.580 1.00 26.12 ? 174 ILE A O     1 
ATOM   1151 C  CB    . ILE A 1 167 ? -8.722  -24.193 23.950 1.00 25.00 ? 174 ILE A CB    1 
ATOM   1152 C  CG1   . ILE A 1 167 ? -9.701  -25.242 23.415 1.00 24.14 ? 174 ILE A CG1   1 
ATOM   1153 C  CG2   . ILE A 1 167 ? -8.909  -22.851 23.244 1.00 22.61 ? 174 ILE A CG2   1 
ATOM   1154 C  CD1   . ILE A 1 167 ? -11.150 -24.985 23.791 1.00 18.97 ? 174 ILE A CD1   1 
ATOM   1155 N  N     . LYS A 1 168 ? -5.694  -22.884 23.487 1.00 20.49 ? 175 LYS A N     1 
ATOM   1156 C  CA    . LYS A 1 168 ? -4.846  -21.804 23.952 1.00 22.77 ? 175 LYS A CA    1 
ATOM   1157 C  C     . LYS A 1 168 ? -5.653  -20.817 24.783 1.00 23.41 ? 175 LYS A C     1 
ATOM   1158 O  O     . LYS A 1 168 ? -6.706  -20.365 24.367 1.00 22.09 ? 175 LYS A O     1 
ATOM   1159 C  CB    . LYS A 1 168 ? -4.147  -21.097 22.806 1.00 19.27 ? 175 LYS A CB    1 
ATOM   1160 C  CG    . LYS A 1 168 ? -3.319  -22.006 21.918 1.00 24.20 ? 175 LYS A CG    1 
ATOM   1161 C  CD    . LYS A 1 168 ? -3.026  -21.340 20.586 1.00 24.36 ? 175 LYS A CD    1 
ATOM   1162 C  CE    . LYS A 1 168 ? -1.705  -20.601 20.599 1.00 27.93 ? 175 LYS A CE    1 
ATOM   1163 N  NZ    . LYS A 1 168 ? -0.569  -21.545 20.423 1.00 34.58 ? 175 LYS A NZ    1 
ATOM   1164 N  N     . PHE A 1 169 ? -5.157  -20.507 25.965 1.00 23.23 ? 176 PHE A N     1 
ATOM   1165 C  CA    . PHE A 1 169 ? -5.849  -19.616 26.884 1.00 21.78 ? 176 PHE A CA    1 
ATOM   1166 C  C     . PHE A 1 169 ? -5.290  -18.205 26.758 1.00 18.78 ? 176 PHE A C     1 
ATOM   1167 O  O     . PHE A 1 169 ? -4.072  -18.008 26.782 1.00 18.41 ? 176 PHE A O     1 
ATOM   1168 C  CB    . PHE A 1 169 ? -5.726  -20.099 28.329 1.00 17.89 ? 176 PHE A CB    1 
ATOM   1169 C  CG    . PHE A 1 169 ? -6.220  -19.101 29.337 1.00 20.85 ? 176 PHE A CG    1 
ATOM   1170 C  CD1   . PHE A 1 169 ? -7.543  -18.691 29.324 1.00 19.55 ? 176 PHE A CD1   1 
ATOM   1171 C  CD2   . PHE A 1 169 ? -5.366  -18.562 30.287 1.00 22.22 ? 176 PHE A CD2   1 
ATOM   1172 C  CE1   . PHE A 1 169 ? -8.012  -17.770 30.241 1.00 21.22 ? 176 PHE A CE1   1 
ATOM   1173 C  CE2   . PHE A 1 169 ? -5.829  -17.636 31.212 1.00 20.24 ? 176 PHE A CE2   1 
ATOM   1174 C  CZ    . PHE A 1 169 ? -7.155  -17.240 31.187 1.00 23.37 ? 176 PHE A CZ    1 
ATOM   1175 N  N     . LYS A 1 170 ? -6.186  -17.231 26.644 1.00 15.70 ? 177 LYS A N     1 
ATOM   1176 C  CA    . LYS A 1 170 ? -5.825  -15.836 26.450 1.00 17.83 ? 177 LYS A CA    1 
ATOM   1177 C  C     . LYS A 1 170 ? -6.635  -14.978 27.411 1.00 16.56 ? 177 LYS A C     1 
ATOM   1178 O  O     . LYS A 1 170 ? -7.788  -15.294 27.716 1.00 14.07 ? 177 LYS A O     1 
ATOM   1179 C  CB    . LYS A 1 170 ? -6.068  -15.416 24.992 1.00 19.45 ? 177 LYS A CB    1 
ATOM   1180 C  CG    . LYS A 1 170 ? -6.095  -13.919 24.732 1.00 15.14 ? 177 LYS A CG    1 
ATOM   1181 C  CD    . LYS A 1 170 ? -6.279  -13.642 23.249 1.00 21.16 ? 177 LYS A CD    1 
ATOM   1182 C  CE    . LYS A 1 170 ? -6.702  -12.208 22.993 1.00 20.83 ? 177 LYS A CE    1 
ATOM   1183 N  NZ    . LYS A 1 170 ? -7.451  -12.085 21.713 1.00 22.56 ? 177 LYS A NZ    1 
ATOM   1184 N  N     . LEU A 1 171 ? -6.023  -13.902 27.900 1.00 16.05 ? 178 LEU A N     1 
ATOM   1185 C  CA    . LEU A 1 171 ? -6.641  -13.031 28.890 1.00 15.24 ? 178 LEU A CA    1 
ATOM   1186 C  C     . LEU A 1 171 ? -6.640  -11.596 28.383 1.00 15.25 ? 178 LEU A C     1 
ATOM   1187 O  O     . LEU A 1 171 ? -5.618  -11.110 27.888 1.00 15.57 ? 178 LEU A O     1 
ATOM   1188 C  CB    . LEU A 1 171 ? -5.906  -13.127 30.233 1.00 14.16 ? 178 LEU A CB    1 
ATOM   1189 C  CG    . LEU A 1 171 ? -6.152  -12.019 31.259 1.00 14.10 ? 178 LEU A CG    1 
ATOM   1190 C  CD1   . LEU A 1 171 ? -7.568  -12.086 31.814 1.00 15.86 ? 178 LEU A CD1   1 
ATOM   1191 C  CD2   . LEU A 1 171 ? -5.138  -12.097 32.390 1.00 9.08  ? 178 LEU A CD2   1 
ATOM   1192 N  N     . ASN A 1 172 ? -7.783  -10.927 28.505 1.00 12.68 ? 179 ASN A N     1 
ATOM   1193 C  CA    . ASN A 1 172 ? -7.935  -9.533  28.111 1.00 14.28 ? 179 ASN A CA    1 
ATOM   1194 C  C     . ASN A 1 172 ? -8.162  -8.679  29.351 1.00 13.46 ? 179 ASN A C     1 
ATOM   1195 O  O     . ASN A 1 172 ? -8.926  -9.059  30.242 1.00 15.26 ? 179 ASN A O     1 
ATOM   1196 C  CB    . ASN A 1 172 ? -9.099  -9.358  27.130 1.00 13.80 ? 179 ASN A CB    1 
ATOM   1197 C  CG    . ASN A 1 172 ? -8.768  -9.850  25.735 1.00 16.35 ? 179 ASN A CG    1 
ATOM   1198 O  OD1   . ASN A 1 172 ? -7.900  -10.701 25.557 1.00 16.68 ? 179 ASN A OD1   1 
ATOM   1199 N  ND2   . ASN A 1 172 ? -9.456  -9.307  24.735 1.00 11.33 ? 179 ASN A ND2   1 
ATOM   1200 N  N     . THR A 1 173 ? -7.493  -7.530  29.410 1.00 14.85 ? 180 THR A N     1 
ATOM   1201 C  CA    . THR A 1 173 ? -7.576  -6.657  30.573 1.00 17.24 ? 180 THR A CA    1 
ATOM   1202 C  C     . THR A 1 173 ? -7.733  -5.216  30.122 1.00 13.92 ? 180 THR A C     1 
ATOM   1203 O  O     . THR A 1 173 ? -7.006  -4.756  29.238 1.00 15.04 ? 180 THR A O     1 
ATOM   1204 C  CB    . THR A 1 173 ? -6.334  -6.795  31.460 1.00 12.27 ? 180 THR A CB    1 
ATOM   1205 O  OG1   . THR A 1 173 ? -6.301  -8.109  32.028 1.00 12.10 ? 180 THR A OG1   1 
ATOM   1206 C  CG2   . THR A 1 173 ? -6.355  -5.765  32.577 1.00 11.68 ? 180 THR A CG2   1 
ATOM   1207 N  N     . VAL A 1 174 ? -8.682  -4.511  30.730 1.00 14.20 ? 181 VAL A N     1 
ATOM   1208 C  CA    . VAL A 1 174 ? -8.919  -3.100  30.453 1.00 13.42 ? 181 VAL A CA    1 
ATOM   1209 C  C     . VAL A 1 174 ? -8.366  -2.290  31.615 1.00 12.53 ? 181 VAL A C     1 
ATOM   1210 O  O     . VAL A 1 174 ? -8.777  -2.482  32.766 1.00 12.63 ? 181 VAL A O     1 
ATOM   1211 C  CB    . VAL A 1 174 ? -10.412 -2.813  30.243 1.00 15.67 ? 181 VAL A CB    1 
ATOM   1212 C  CG1   . VAL A 1 174 ? -10.637 -1.328  30.118 1.00 12.11 ? 181 VAL A CG1   1 
ATOM   1213 C  CG2   . VAL A 1 174 ? -10.903 -3.516  29.002 1.00 14.40 ? 181 VAL A CG2   1 
ATOM   1214 N  N     . VAL A 1 175 ? -7.440  -1.385  31.321 1.00 15.37 ? 182 VAL A N     1 
ATOM   1215 C  CA    . VAL A 1 175 ? -6.817  -0.558  32.348 1.00 12.36 ? 182 VAL A CA    1 
ATOM   1216 C  C     . VAL A 1 175 ? -7.577  0.757   32.440 1.00 11.80 ? 182 VAL A C     1 
ATOM   1217 O  O     . VAL A 1 175 ? -7.596  1.544   31.488 1.00 9.74  ? 182 VAL A O     1 
ATOM   1218 C  CB    . VAL A 1 175 ? -5.331  -0.319  32.051 1.00 12.50 ? 182 VAL A CB    1 
ATOM   1219 C  CG1   . VAL A 1 175 ? -4.717  0.538   33.146 1.00 12.06 ? 182 VAL A CG1   1 
ATOM   1220 C  CG2   . VAL A 1 175 ? -4.601  -1.642  31.941 1.00 11.71 ? 182 VAL A CG2   1 
ATOM   1221 N  N     . THR A 1 176 ? -8.204  0.994   33.586 1.00 10.95 ? 183 THR A N     1 
ATOM   1222 C  CA    . THR A 1 176 ? -9.017  2.181   33.820 1.00 14.52 ? 183 THR A CA    1 
ATOM   1223 C  C     . THR A 1 176 ? -8.424  2.998   34.965 1.00 16.39 ? 183 THR A C     1 
ATOM   1224 O  O     . THR A 1 176 ? -7.394  2.647   35.546 1.00 15.29 ? 183 THR A O     1 
ATOM   1225 C  CB    . THR A 1 176 ? -10.469 1.803   34.136 1.00 13.60 ? 183 THR A CB    1 
ATOM   1226 O  OG1   . THR A 1 176 ? -10.593 1.512   35.532 1.00 14.66 ? 183 THR A OG1   1 
ATOM   1227 C  CG2   . THR A 1 176 ? -10.896 0.580   33.348 1.00 12.12 ? 183 THR A CG2   1 
ATOM   1228 N  N     . ARG A 1 177 ? -9.102  4.100   35.294 1.00 12.83 ? 184 ARG A N     1 
ATOM   1229 C  CA    . ARG A 1 177 ? -8.684  4.944   36.408 1.00 15.98 ? 184 ARG A CA    1 
ATOM   1230 C  C     . ARG A 1 177 ? -8.757  4.223   37.749 1.00 14.60 ? 184 ARG A C     1 
ATOM   1231 O  O     . ARG A 1 177 ? -8.170  4.704   38.725 1.00 13.61 ? 184 ARG A O     1 
ATOM   1232 C  CB    . ARG A 1 177 ? -9.540  6.214   36.440 1.00 16.23 ? 184 ARG A CB    1 
ATOM   1233 C  CG    . ARG A 1 177 ? -9.002  7.328   37.328 1.00 17.89 ? 184 ARG A CG    1 
ATOM   1234 C  CD    . ARG A 1 177 ? -9.895  8.549   37.242 1.00 19.64 ? 184 ARG A CD    1 
ATOM   1235 N  NE    . ARG A 1 177 ? -10.126 8.931   35.855 1.00 21.38 ? 184 ARG A NE    1 
ATOM   1236 C  CZ    . ARG A 1 177 ? -10.888 9.945   35.470 1.00 26.12 ? 184 ARG A CZ    1 
ATOM   1237 N  NH1   . ARG A 1 177 ? -11.528 10.701  36.348 1.00 28.20 ? 184 ARG A NH1   1 
ATOM   1238 N  NH2   . ARG A 1 177 ? -11.015 10.204  34.172 1.00 23.53 ? 184 ARG A NH2   1 
ATOM   1239 N  N     . LEU A 1 178 ? -9.432  3.076   37.816 1.00 15.37 ? 185 LEU A N     1 
ATOM   1240 C  CA    . LEU A 1 178 ? -9.635  2.353   39.064 1.00 17.99 ? 185 LEU A CA    1 
ATOM   1241 C  C     . LEU A 1 178 ? -8.659  1.203   39.276 1.00 20.28 ? 185 LEU A C     1 
ATOM   1242 O  O     . LEU A 1 178 ? -8.633  0.636   40.373 1.00 22.73 ? 185 LEU A O     1 
ATOM   1243 C  CB    . LEU A 1 178 ? -11.069 1.812   39.126 1.00 20.73 ? 185 LEU A CB    1 
ATOM   1244 C  CG    . LEU A 1 178 ? -12.144 2.884   39.296 1.00 18.68 ? 185 LEU A CG    1 
ATOM   1245 C  CD1   . LEU A 1 178 ? -12.857 3.119   37.985 1.00 15.99 ? 185 LEU A CD1   1 
ATOM   1246 C  CD2   . LEU A 1 178 ? -13.139 2.498   40.384 1.00 26.15 ? 185 LEU A CD2   1 
ATOM   1247 N  N     . ASN A 1 179 ? -7.856  0.843   38.268 1.00 20.12 ? 186 ASN A N     1 
ATOM   1248 C  CA    . ASN A 1 179 ? -7.004  -0.335  38.393 1.00 17.12 ? 186 ASN A CA    1 
ATOM   1249 C  C     . ASN A 1 179 ? -5.627  -0.157  37.754 1.00 19.71 ? 186 ASN A C     1 
ATOM   1250 O  O     . ASN A 1 179 ? -4.922  -1.152  37.547 1.00 19.83 ? 186 ASN A O     1 
ATOM   1251 C  CB    . ASN A 1 179 ? -7.693  -1.565  37.782 1.00 15.54 ? 186 ASN A CB    1 
ATOM   1252 C  CG    . ASN A 1 179 ? -8.043  -1.373  36.320 1.00 13.97 ? 186 ASN A CG    1 
ATOM   1253 O  OD1   . ASN A 1 179 ? -8.074  -0.250  35.819 1.00 17.03 ? 186 ASN A OD1   1 
ATOM   1254 N  ND2   . ASN A 1 179 ? -8.310  -2.474  35.626 1.00 12.17 ? 186 ASN A ND2   1 
ATOM   1255 N  N     . TYR A 1 180 ? -5.214  1.071   37.439 1.00 19.33 ? 187 TYR A N     1 
ATOM   1256 C  CA    . TYR A 1 180 ? -3.890  1.252   36.855 1.00 19.43 ? 187 TYR A CA    1 
ATOM   1257 C  C     . TYR A 1 180 ? -2.777  1.122   37.886 1.00 20.81 ? 187 TYR A C     1 
ATOM   1258 O  O     . TYR A 1 180 ? -1.638  0.828   37.511 1.00 22.65 ? 187 TYR A O     1 
ATOM   1259 C  CB    . TYR A 1 180 ? -3.792  2.603   36.140 1.00 19.07 ? 187 TYR A CB    1 
ATOM   1260 C  CG    . TYR A 1 180 ? -3.688  3.804   37.053 1.00 21.73 ? 187 TYR A CG    1 
ATOM   1261 C  CD1   . TYR A 1 180 ? -4.818  4.349   37.644 1.00 20.65 ? 187 TYR A CD1   1 
ATOM   1262 C  CD2   . TYR A 1 180 ? -2.459  4.410   37.301 1.00 18.87 ? 187 TYR A CD2   1 
ATOM   1263 C  CE1   . TYR A 1 180 ? -4.732  5.451   38.470 1.00 21.71 ? 187 TYR A CE1   1 
ATOM   1264 C  CE2   . TYR A 1 180 ? -2.363  5.516   38.128 1.00 19.78 ? 187 TYR A CE2   1 
ATOM   1265 C  CZ    . TYR A 1 180 ? -3.504  6.032   38.709 1.00 24.38 ? 187 TYR A CZ    1 
ATOM   1266 O  OH    . TYR A 1 180 ? -3.422  7.131   39.533 1.00 24.46 ? 187 TYR A OH    1 
ATOM   1267 N  N     . GLU A 1 181 ? -3.079  1.325   39.167 1.00 18.17 ? 188 GLU A N     1 
ATOM   1268 C  CA    . GLU A 1 181 ? -2.112  1.104   40.233 1.00 16.89 ? 188 GLU A CA    1 
ATOM   1269 C  C     . GLU A 1 181 ? -2.049  -0.350  40.680 1.00 16.51 ? 188 GLU A C     1 
ATOM   1270 O  O     . GLU A 1 181 ? -1.224  -0.679  41.539 1.00 20.30 ? 188 GLU A O     1 
ATOM   1271 C  CB    . GLU A 1 181 ? -2.445  1.978   41.448 1.00 16.32 ? 188 GLU A CB    1 
ATOM   1272 C  CG    . GLU A 1 181 ? -2.533  3.468   41.178 1.00 21.43 ? 188 GLU A CG    1 
ATOM   1273 C  CD    . GLU A 1 181 ? -2.922  4.249   42.421 1.00 32.38 ? 188 GLU A CD    1 
ATOM   1274 O  OE1   . GLU A 1 181 ? -4.137  4.392   42.675 1.00 32.93 ? 188 GLU A OE1   1 
ATOM   1275 O  OE2   . GLU A 1 181 ? -2.016  4.710   43.147 1.00 32.72 ? 188 GLU A OE2   1 
ATOM   1276 N  N     . GLU A 1 182 ? -2.891  -1.220  40.125 1.00 16.17 ? 189 GLU A N     1 
ATOM   1277 C  CA    . GLU A 1 182 ? -3.024  -2.583  40.623 1.00 17.73 ? 189 GLU A CA    1 
ATOM   1278 C  C     . GLU A 1 182 ? -1.839  -3.436  40.191 1.00 19.07 ? 189 GLU A C     1 
ATOM   1279 O  O     . GLU A 1 182 ? -1.416  -3.391  39.032 1.00 17.22 ? 189 GLU A O     1 
ATOM   1280 C  CB    . GLU A 1 182 ? -4.327  -3.206  40.121 1.00 17.76 ? 189 GLU A CB    1 
ATOM   1281 C  CG    . GLU A 1 182 ? -4.550  -4.650  40.553 1.00 17.42 ? 189 GLU A CG    1 
ATOM   1282 C  CD    . GLU A 1 182 ? -5.984  -5.099  40.343 1.00 21.92 ? 189 GLU A CD    1 
ATOM   1283 O  OE1   . GLU A 1 182 ? -6.875  -4.226  40.275 1.00 21.31 ? 189 GLU A OE1   1 
ATOM   1284 O  OE2   . GLU A 1 182 ? -6.224  -6.322  40.251 1.00 18.84 ? 189 GLU A OE2   1 
ATOM   1285 N  N     . ASP A 1 183 ? -1.310  -4.217  41.130 1.00 20.41 ? 190 ASP A N     1 
ATOM   1286 C  CA    . ASP A 1 183 ? -0.247  -5.176  40.849 1.00 17.27 ? 190 ASP A CA    1 
ATOM   1287 C  C     . ASP A 1 183 ? -0.896  -6.533  40.602 1.00 19.39 ? 190 ASP A C     1 
ATOM   1288 O  O     . ASP A 1 183 ? -1.485  -7.126  41.512 1.00 21.54 ? 190 ASP A O     1 
ATOM   1289 C  CB    . ASP A 1 183 ? 0.751   -5.233  42.003 1.00 17.53 ? 190 ASP A CB    1 
ATOM   1290 C  CG    . ASP A 1 183 ? 2.030   -5.978  41.643 1.00 20.64 ? 190 ASP A CG    1 
ATOM   1291 O  OD1   . ASP A 1 183 ? 1.954   -7.024  40.965 1.00 19.58 ? 190 ASP A OD1   1 
ATOM   1292 O  OD2   . ASP A 1 183 ? 3.119   -5.516  42.042 1.00 17.92 ? 190 ASP A OD2   1 
ATOM   1293 N  N     . MET A 1 184 ? -0.782  -7.023  39.371 1.00 15.88 ? 191 MET A N     1 
ATOM   1294 C  CA    . MET A 1 184 ? -1.443  -8.242  38.933 1.00 15.38 ? 191 MET A CA    1 
ATOM   1295 C  C     . MET A 1 184 ? -0.494  -9.421  38.791 1.00 19.69 ? 191 MET A C     1 
ATOM   1296 O  O     . MET A 1 184 ? -0.920  -10.489 38.342 1.00 21.90 ? 191 MET A O     1 
ATOM   1297 C  CB    . MET A 1 184 ? -2.137  -8.004  37.589 1.00 17.55 ? 191 MET A CB    1 
ATOM   1298 C  CG    . MET A 1 184 ? -3.630  -7.812  37.688 1.00 20.78 ? 191 MET A CG    1 
ATOM   1299 S  SD    . MET A 1 184 ? -4.375  -7.262  36.140 1.00 18.36 ? 191 MET A SD    1 
ATOM   1300 C  CE    . MET A 1 184 ? -5.173  -5.738  36.646 1.00 13.77 ? 191 MET A CE    1 
ATOM   1301 N  N     . ASN A 1 185 ? 0.774   -9.257  39.169 1.00 16.66 ? 192 ASN A N     1 
ATOM   1302 C  CA    . ASN A 1 185 ? 1.795   -10.216 38.763 1.00 19.78 ? 192 ASN A CA    1 
ATOM   1303 C  C     . ASN A 1 185 ? 1.657   -11.555 39.473 1.00 20.62 ? 192 ASN A C     1 
ATOM   1304 O  O     . ASN A 1 185 ? 2.109   -12.576 38.942 1.00 23.44 ? 192 ASN A O     1 
ATOM   1305 C  CB    . ASN A 1 185 ? 3.183   -9.631  38.997 1.00 19.05 ? 192 ASN A CB    1 
ATOM   1306 C  CG    . ASN A 1 185 ? 3.609   -8.720  37.876 1.00 17.68 ? 192 ASN A CG    1 
ATOM   1307 O  OD1   . ASN A 1 185 ? 3.630   -9.126  36.715 1.00 17.54 ? 192 ASN A OD1   1 
ATOM   1308 N  ND2   . ASN A 1 185 ? 3.951   -7.482  38.209 1.00 15.75 ? 192 ASN A ND2   1 
ATOM   1309 N  N     . GLU A 1 186 ? 1.053   -11.584 40.662 1.00 19.56 ? 193 GLU A N     1 
ATOM   1310 C  CA    . GLU A 1 186 ? 0.837   -12.866 41.327 1.00 21.67 ? 193 GLU A CA    1 
ATOM   1311 C  C     . GLU A 1 186 ? -0.132  -13.739 40.539 1.00 26.07 ? 193 GLU A C     1 
ATOM   1312 O  O     . GLU A 1 186 ? 0.072   -14.953 40.417 1.00 27.85 ? 193 GLU A O     1 
ATOM   1313 C  CB    . GLU A 1 186 ? 0.321   -12.655 42.750 1.00 30.26 ? 193 GLU A CB    1 
ATOM   1314 C  CG    . GLU A 1 186 ? 0.868   -13.662 43.756 1.00 39.45 ? 193 GLU A CG    1 
ATOM   1315 C  CD    . GLU A 1 186 ? 1.060   -13.074 45.142 1.00 42.46 ? 193 GLU A CD    1 
ATOM   1316 O  OE1   . GLU A 1 186 ? 0.217   -12.252 45.560 1.00 45.91 ? 193 GLU A OE1   1 
ATOM   1317 O  OE2   . GLU A 1 186 ? 2.046   -13.444 45.816 1.00 39.56 ? 193 GLU A OE2   1 
ATOM   1318 N  N     . HIS A 1 187 ? -1.196  -13.141 39.999 1.00 25.76 ? 194 HIS A N     1 
ATOM   1319 C  CA    . HIS A 1 187 ? -2.187  -13.912 39.257 1.00 23.17 ? 194 HIS A CA    1 
ATOM   1320 C  C     . HIS A 1 187 ? -1.699  -14.258 37.857 1.00 25.26 ? 194 HIS A C     1 
ATOM   1321 O  O     . HIS A 1 187 ? -1.953  -15.363 37.364 1.00 24.21 ? 194 HIS A O     1 
ATOM   1322 C  CB    . HIS A 1 187 ? -3.502  -13.139 39.185 1.00 18.69 ? 194 HIS A CB    1 
ATOM   1323 C  CG    . HIS A 1 187 ? -4.232  -13.066 40.489 1.00 21.56 ? 194 HIS A CG    1 
ATOM   1324 N  ND1   . HIS A 1 187 ? -5.066  -14.069 40.932 1.00 23.72 ? 194 HIS A ND1   1 
ATOM   1325 C  CD2   . HIS A 1 187 ? -4.245  -12.113 41.451 1.00 24.63 ? 194 HIS A CD2   1 
ATOM   1326 C  CE1   . HIS A 1 187 ? -5.570  -13.732 42.106 1.00 21.44 ? 194 HIS A CE1   1 
ATOM   1327 N  NE2   . HIS A 1 187 ? -5.087  -12.551 42.443 1.00 23.78 ? 194 HIS A NE2   1 
ATOM   1328 N  N     . ILE A 1 188 ? -1.005  -13.328 37.200 1.00 25.49 ? 195 ILE A N     1 
ATOM   1329 C  CA    . ILE A 1 188 ? -0.469  -13.609 35.872 1.00 17.97 ? 195 ILE A CA    1 
ATOM   1330 C  C     . ILE A 1 188 ? 0.585   -14.705 35.945 1.00 25.05 ? 195 ILE A C     1 
ATOM   1331 O  O     . ILE A 1 188 ? 0.704   -15.532 35.032 1.00 30.53 ? 195 ILE A O     1 
ATOM   1332 C  CB    . ILE A 1 188 ? 0.090   -12.325 35.236 1.00 17.60 ? 195 ILE A CB    1 
ATOM   1333 C  CG1   . ILE A 1 188 ? -1.002  -11.259 35.162 1.00 18.09 ? 195 ILE A CG1   1 
ATOM   1334 C  CG2   . ILE A 1 188 ? 0.633   -12.614 33.849 1.00 18.99 ? 195 ILE A CG2   1 
ATOM   1335 C  CD1   . ILE A 1 188 ? -2.275  -11.747 34.519 1.00 13.83 ? 195 ILE A CD1   1 
ATOM   1336 N  N     . ASP A 1 189 ? 1.365   -14.732 37.029 1.00 23.88 ? 196 ASP A N     1 
ATOM   1337 C  CA    . ASP A 1 189 ? 2.341   -15.796 37.233 1.00 26.40 ? 196 ASP A CA    1 
ATOM   1338 C  C     . ASP A 1 189 ? 1.692   -17.135 37.548 1.00 29.10 ? 196 ASP A C     1 
ATOM   1339 O  O     . ASP A 1 189 ? 2.384   -18.158 37.528 1.00 31.27 ? 196 ASP A O     1 
ATOM   1340 C  CB    . ASP A 1 189 ? 3.306   -15.427 38.363 1.00 23.98 ? 196 ASP A CB    1 
ATOM   1341 C  CG    . ASP A 1 189 ? 4.475   -14.590 37.885 1.00 27.38 ? 196 ASP A CG    1 
ATOM   1342 O  OD1   . ASP A 1 189 ? 4.860   -14.713 36.703 1.00 33.82 ? 196 ASP A OD1   1 
ATOM   1343 O  OD2   . ASP A 1 189 ? 5.008   -13.805 38.698 1.00 28.02 ? 196 ASP A OD2   1 
ATOM   1344 N  N     . THR A 1 190 ? 0.392   -17.153 37.843 1.00 27.18 ? 197 THR A N     1 
ATOM   1345 C  CA    . THR A 1 190 ? -0.346  -18.377 38.128 1.00 26.10 ? 197 THR A CA    1 
ATOM   1346 C  C     . THR A 1 190 ? -1.128  -18.875 36.919 1.00 27.26 ? 197 THR A C     1 
ATOM   1347 O  O     . THR A 1 190 ? -0.985  -20.035 36.521 1.00 30.24 ? 197 THR A O     1 
ATOM   1348 C  CB    . THR A 1 190 ? -1.296  -18.152 39.312 1.00 26.12 ? 197 THR A CB    1 
ATOM   1349 O  OG1   . THR A 1 190 ? -0.546  -18.132 40.532 1.00 28.16 ? 197 THR A OG1   1 
ATOM   1350 C  CG2   . THR A 1 190 ? -2.332  -19.260 39.387 1.00 23.58 ? 197 THR A CG2   1 
ATOM   1351 N  N     . LEU A 1 191 ? -1.959  -18.015 36.326 1.00 28.06 ? 198 LEU A N     1 
ATOM   1352 C  CA    . LEU A 1 191 ? -2.702  -18.399 35.130 1.00 24.89 ? 198 LEU A CA    1 
ATOM   1353 C  C     . LEU A 1 191 ? -1.764  -18.685 33.967 1.00 23.79 ? 198 LEU A C     1 
ATOM   1354 O  O     . LEU A 1 191 ? -1.939  -19.677 33.249 1.00 25.69 ? 198 LEU A O     1 
ATOM   1355 C  CB    . LEU A 1 191 ? -3.686  -17.294 34.755 1.00 25.74 ? 198 LEU A CB    1 
ATOM   1356 C  CG    . LEU A 1 191 ? -4.868  -17.123 35.702 1.00 28.86 ? 198 LEU A CG    1 
ATOM   1357 C  CD1   . LEU A 1 191 ? -5.231  -15.655 35.816 1.00 24.89 ? 198 LEU A CD1   1 
ATOM   1358 C  CD2   . LEU A 1 191 ? -6.054  -17.951 35.228 1.00 23.99 ? 198 LEU A CD2   1 
ATOM   1359 N  N     . GLN A 1 192 ? -0.765  -17.830 33.778 1.00 25.27 ? 199 GLN A N     1 
ATOM   1360 C  CA    . GLN A 1 192 ? 0.170   -17.916 32.661 1.00 26.87 ? 199 GLN A CA    1 
ATOM   1361 C  C     . GLN A 1 192 ? -0.541  -18.031 31.313 1.00 25.50 ? 199 GLN A C     1 
ATOM   1362 O  O     . GLN A 1 192 ? -0.357  -19.015 30.589 1.00 20.74 ? 199 GLN A O     1 
ATOM   1363 C  CB    . GLN A 1 192 ? 1.135   -19.080 32.859 1.00 28.77 ? 199 GLN A CB    1 
ATOM   1364 C  CG    . GLN A 1 192 ? 1.965   -18.987 34.128 1.00 29.01 ? 199 GLN A CG    1 
ATOM   1365 C  CD    . GLN A 1 192 ? 3.173   -18.076 33.988 1.00 37.07 ? 199 GLN A CD    1 
ATOM   1366 O  OE1   . GLN A 1 192 ? 3.097   -16.999 33.396 1.00 37.86 ? 199 GLN A OE1   1 
ATOM   1367 N  NE2   . GLN A 1 192 ? 4.299   -18.506 34.546 1.00 44.60 ? 199 GLN A NE2   1 
ATOM   1368 N  N     . PRO A 1 193 ? -1.363  -17.046 30.941 1.00 24.45 ? 200 PRO A N     1 
ATOM   1369 C  CA    . PRO A 1 193 ? -1.950  -17.068 29.600 1.00 21.55 ? 200 PRO A CA    1 
ATOM   1370 C  C     . PRO A 1 193 ? -0.854  -16.913 28.561 1.00 21.43 ? 200 PRO A C     1 
ATOM   1371 O  O     . PRO A 1 193 ? 0.154   -16.243 28.791 1.00 23.67 ? 200 PRO A O     1 
ATOM   1372 C  CB    . PRO A 1 193 ? -2.896  -15.864 29.604 1.00 19.62 ? 200 PRO A CB    1 
ATOM   1373 C  CG    . PRO A 1 193 ? -2.290  -14.933 30.589 1.00 18.97 ? 200 PRO A CG    1 
ATOM   1374 C  CD    . PRO A 1 193 ? -1.726  -15.816 31.668 1.00 20.99 ? 200 PRO A CD    1 
ATOM   1375 N  N     . PHE A 1 194 ? -1.042  -17.562 27.411 1.00 19.49 ? 201 PHE A N     1 
ATOM   1376 C  CA    . PHE A 1 194 ? -0.067  -17.404 26.341 1.00 16.04 ? 201 PHE A CA    1 
ATOM   1377 C  C     . PHE A 1 194 ? -0.144  -16.020 25.709 1.00 16.01 ? 201 PHE A C     1 
ATOM   1378 O  O     . PHE A 1 194 ? 0.831   -15.574 25.095 1.00 19.84 ? 201 PHE A O     1 
ATOM   1379 C  CB    . PHE A 1 194 ? -0.259  -18.488 25.277 1.00 18.67 ? 201 PHE A CB    1 
ATOM   1380 C  CG    . PHE A 1 194 ? -1.074  -18.045 24.097 1.00 24.24 ? 201 PHE A CG    1 
ATOM   1381 C  CD1   . PHE A 1 194 ? -2.444  -17.858 24.205 1.00 24.58 ? 201 PHE A CD1   1 
ATOM   1382 C  CD2   . PHE A 1 194 ? -0.463  -17.804 22.879 1.00 21.41 ? 201 PHE A CD2   1 
ATOM   1383 C  CE1   . PHE A 1 194 ? -3.189  -17.443 23.114 1.00 20.70 ? 201 PHE A CE1   1 
ATOM   1384 C  CE2   . PHE A 1 194 ? -1.198  -17.389 21.788 1.00 21.88 ? 201 PHE A CE2   1 
ATOM   1385 C  CZ    . PHE A 1 194 ? -2.563  -17.209 21.904 1.00 26.34 ? 201 PHE A CZ    1 
ATOM   1386 N  N     . ARG A 1 195 ? -1.273  -15.330 25.865 1.00 19.60 ? 202 ARG A N     1 
ATOM   1387 C  CA    . ARG A 1 195 ? -1.485  -14.003 25.306 1.00 15.13 ? 202 ARG A CA    1 
ATOM   1388 C  C     . ARG A 1 195 ? -2.261  -13.176 26.319 1.00 16.75 ? 202 ARG A C     1 
ATOM   1389 O  O     . ARG A 1 195 ? -3.270  -13.641 26.856 1.00 16.39 ? 202 ARG A O     1 
ATOM   1390 C  CB    . ARG A 1 195 ? -2.249  -14.084 23.979 1.00 15.17 ? 202 ARG A CB    1 
ATOM   1391 C  CG    . ARG A 1 195 ? -2.246  -12.809 23.153 1.00 11.36 ? 202 ARG A CG    1 
ATOM   1392 C  CD    . ARG A 1 195 ? -2.471  -13.129 21.679 1.00 13.84 ? 202 ARG A CD    1 
ATOM   1393 N  NE    . ARG A 1 195 ? -2.429  -11.941 20.836 1.00 15.22 ? 202 ARG A NE    1 
ATOM   1394 C  CZ    . ARG A 1 195 ? -1.312  -11.367 20.408 1.00 16.89 ? 202 ARG A CZ    1 
ATOM   1395 N  NH1   . ARG A 1 195 ? -0.121  -11.854 20.717 1.00 11.79 ? 202 ARG A NH1   1 
ATOM   1396 N  NH2   . ARG A 1 195 ? -1.392  -10.278 19.649 1.00 14.83 ? 202 ARG A NH2   1 
ATOM   1397 N  N     . TRP A 1 196 ? -1.789  -11.960 26.580 1.00 12.12 ? 203 TRP A N     1 
ATOM   1398 C  CA    . TRP A 1 196 ? -2.383  -11.086 27.591 1.00 13.66 ? 203 TRP A CA    1 
ATOM   1399 C  C     . TRP A 1 196 ? -2.514  -9.690  26.992 1.00 14.58 ? 203 TRP A C     1 
ATOM   1400 O  O     . TRP A 1 196 ? -1.550  -8.918  26.972 1.00 12.22 ? 203 TRP A O     1 
ATOM   1401 C  CB    . TRP A 1 196 ? -1.548  -11.073 28.868 1.00 11.36 ? 203 TRP A CB    1 
ATOM   1402 C  CG    . TRP A 1 196 ? -2.129  -10.219 29.956 1.00 14.29 ? 203 TRP A CG    1 
ATOM   1403 C  CD1   . TRP A 1 196 ? -3.439  -9.874  30.114 1.00 15.55 ? 203 TRP A CD1   1 
ATOM   1404 C  CD2   . TRP A 1 196 ? -1.418  -9.596  31.034 1.00 15.16 ? 203 TRP A CD2   1 
ATOM   1405 N  NE1   . TRP A 1 196 ? -3.589  -9.076  31.221 1.00 13.25 ? 203 TRP A NE1   1 
ATOM   1406 C  CE2   . TRP A 1 196 ? -2.364  -8.890  31.804 1.00 18.78 ? 203 TRP A CE2   1 
ATOM   1407 C  CE3   . TRP A 1 196 ? -0.075  -9.566  31.422 1.00 13.95 ? 203 TRP A CE3   1 
ATOM   1408 C  CZ2   . TRP A 1 196 ? -2.011  -8.165  32.939 1.00 17.21 ? 203 TRP A CZ2   1 
ATOM   1409 C  CZ3   . TRP A 1 196 ? 0.273   -8.845  32.550 1.00 16.83 ? 203 TRP A CZ3   1 
ATOM   1410 C  CH2   . TRP A 1 196 ? -0.691  -8.155  33.295 1.00 14.39 ? 203 TRP A CH2   1 
ATOM   1411 N  N     . LYS A 1 197 ? -3.711  -9.378  26.500 1.00 12.16 ? 204 LYS A N     1 
ATOM   1412 C  CA    . LYS A 1 197 ? -3.999  -8.064  25.948 1.00 12.53 ? 204 LYS A CA    1 
ATOM   1413 C  C     . LYS A 1 197 ? -4.284  -7.081  27.074 1.00 13.64 ? 204 LYS A C     1 
ATOM   1414 O  O     . LYS A 1 197 ? -5.106  -7.351  27.956 1.00 12.18 ? 204 LYS A O     1 
ATOM   1415 C  CB    . LYS A 1 197 ? -5.184  -8.142  24.991 1.00 13.65 ? 204 LYS A CB    1 
ATOM   1416 C  CG    . LYS A 1 197 ? -4.951  -9.082  23.831 1.00 16.84 ? 204 LYS A CG    1 
ATOM   1417 C  CD    . LYS A 1 197 ? -4.143  -8.404  22.744 1.00 18.38 ? 204 LYS A CD    1 
ATOM   1418 C  CE    . LYS A 1 197 ? -4.212  -9.184  21.450 1.00 17.94 ? 204 LYS A CE    1 
ATOM   1419 N  NZ    . LYS A 1 197 ? -4.344  -8.280  20.277 1.00 23.49 ? 204 LYS A NZ    1 
ATOM   1420 N  N     . VAL A 1 198 ? -3.595  -5.945  27.042 1.00 12.48 ? 205 VAL A N     1 
ATOM   1421 C  CA    . VAL A 1 198 ? -3.694  -4.915  28.070 1.00 11.43 ? 205 VAL A CA    1 
ATOM   1422 C  C     . VAL A 1 198 ? -4.152  -3.643  27.370 1.00 13.31 ? 205 VAL A C     1 
ATOM   1423 O  O     . VAL A 1 198 ? -3.337  -2.903  26.805 1.00 13.87 ? 205 VAL A O     1 
ATOM   1424 C  CB    . VAL A 1 198 ? -2.368  -4.704  28.806 1.00 13.81 ? 205 VAL A CB    1 
ATOM   1425 C  CG1   . VAL A 1 198 ? -2.460  -3.513  29.744 1.00 13.79 ? 205 VAL A CG1   1 
ATOM   1426 C  CG2   . VAL A 1 198 ? -1.990  -5.962  29.568 1.00 14.66 ? 205 VAL A CG2   1 
ATOM   1427 N  N     . PHE A 1 199 ? -5.455  -3.386  27.400 1.00 13.73 ? 206 PHE A N     1 
ATOM   1428 C  CA    . PHE A 1 199 ? -6.032  -2.233  26.727 1.00 14.40 ? 206 PHE A CA    1 
ATOM   1429 C  C     . PHE A 1 199 ? -6.074  -1.036  27.666 1.00 13.94 ? 206 PHE A C     1 
ATOM   1430 O  O     . PHE A 1 199 ? -6.551  -1.148  28.800 1.00 16.17 ? 206 PHE A O     1 
ATOM   1431 C  CB    . PHE A 1 199 ? -7.453  -2.528  26.241 1.00 16.66 ? 206 PHE A CB    1 
ATOM   1432 C  CG    . PHE A 1 199 ? -7.610  -3.845  25.538 1.00 14.41 ? 206 PHE A CG    1 
ATOM   1433 C  CD1   . PHE A 1 199 ? -6.824  -4.163  24.445 1.00 13.16 ? 206 PHE A CD1   1 
ATOM   1434 C  CD2   . PHE A 1 199 ? -8.577  -4.750  25.947 1.00 15.92 ? 206 PHE A CD2   1 
ATOM   1435 C  CE1   . PHE A 1 199 ? -6.983  -5.367  23.786 1.00 12.60 ? 206 PHE A CE1   1 
ATOM   1436 C  CE2   . PHE A 1 199 ? -8.741  -5.956  25.291 1.00 15.32 ? 206 PHE A CE2   1 
ATOM   1437 C  CZ    . PHE A 1 199 ? -7.943  -6.263  24.209 1.00 12.01 ? 206 PHE A CZ    1 
ATOM   1438 N  N     . GLN A 1 200 ? -5.584  0.105   27.193 1.00 14.10 ? 207 GLN A N     1 
ATOM   1439 C  CA    . GLN A 1 200 ? -5.998  1.371   27.776 1.00 13.74 ? 207 GLN A CA    1 
ATOM   1440 C  C     . GLN A 1 200 ? -7.446  1.639   27.389 1.00 14.95 ? 207 GLN A C     1 
ATOM   1441 O  O     . GLN A 1 200 ? -7.856  1.357   26.260 1.00 16.09 ? 207 GLN A O     1 
ATOM   1442 C  CB    . GLN A 1 200 ? -5.096  2.508   27.293 1.00 15.94 ? 207 GLN A CB    1 
ATOM   1443 C  CG    . GLN A 1 200 ? -5.520  3.889   27.777 1.00 14.84 ? 207 GLN A CG    1 
ATOM   1444 C  CD    . GLN A 1 200 ? -4.685  4.993   27.168 1.00 18.73 ? 207 GLN A CD    1 
ATOM   1445 O  OE1   . GLN A 1 200 ? -3.885  4.750   26.266 1.00 21.99 ? 207 GLN A OE1   1 
ATOM   1446 N  NE2   . GLN A 1 200 ? -4.863  6.217   27.658 1.00 15.77 ? 207 GLN A NE2   1 
ATOM   1447 N  N     . VAL A 1 201 ? -8.231  2.156   28.342 1.00 13.29 ? 208 VAL A N     1 
ATOM   1448 C  CA    . VAL A 1 201 ? -9.620  2.505   28.055 1.00 13.75 ? 208 VAL A CA    1 
ATOM   1449 C  C     . VAL A 1 201 ? -9.676  3.388   26.821 1.00 16.20 ? 208 VAL A C     1 
ATOM   1450 O  O     . VAL A 1 201 ? -8.948  4.381   26.715 1.00 14.60 ? 208 VAL A O     1 
ATOM   1451 C  CB    . VAL A 1 201 ? -10.275 3.197   29.265 1.00 15.46 ? 208 VAL A CB    1 
ATOM   1452 C  CG1   . VAL A 1 201 ? -10.880 2.172   30.193 1.00 11.93 ? 208 VAL A CG1   1 
ATOM   1453 C  CG2   . VAL A 1 201 ? -9.263  4.050   30.009 1.00 15.82 ? 208 VAL A CG2   1 
ATOM   1454 N  N     . LEU A 1 202 ? -10.527 3.013   25.873 1.00 15.65 ? 209 LEU A N     1 
ATOM   1455 C  CA    . LEU A 1 202 ? -10.668 3.728   24.614 1.00 13.84 ? 209 LEU A CA    1 
ATOM   1456 C  C     . LEU A 1 202 ? -12.014 4.434   24.572 1.00 18.22 ? 209 LEU A C     1 
ATOM   1457 O  O     . LEU A 1 202 ? -13.056 3.820   24.831 1.00 19.24 ? 209 LEU A O     1 
ATOM   1458 C  CB    . LEU A 1 202 ? -10.531 2.771   23.427 1.00 19.12 ? 209 LEU A CB    1 
ATOM   1459 C  CG    . LEU A 1 202 ? -10.378 3.436   22.062 1.00 17.23 ? 209 LEU A CG    1 
ATOM   1460 C  CD1   . LEU A 1 202 ? -9.030  4.128   21.973 1.00 19.57 ? 209 LEU A CD1   1 
ATOM   1461 C  CD2   . LEU A 1 202 ? -10.533 2.417   20.952 1.00 17.35 ? 209 LEU A CD2   1 
ATOM   1462 N  N     . ILE A 1 203 ? -11.985 5.722   24.252 1.00 17.75 ? 210 ILE A N     1 
ATOM   1463 C  CA    . ILE A 1 203 ? -13.196 6.498   24.025 1.00 17.78 ? 210 ILE A CA    1 
ATOM   1464 C  C     . ILE A 1 203 ? -13.509 6.437   22.537 1.00 21.47 ? 210 ILE A C     1 
ATOM   1465 O  O     . ILE A 1 203 ? -12.716 6.897   21.708 1.00 24.67 ? 210 ILE A O     1 
ATOM   1466 C  CB    . ILE A 1 203 ? -13.029 7.950   24.497 1.00 19.63 ? 210 ILE A CB    1 
ATOM   1467 C  CG1   . ILE A 1 203 ? -13.065 8.022   26.024 1.00 21.64 ? 210 ILE A CG1   1 
ATOM   1468 C  CG2   . ILE A 1 203 ? -14.113 8.830   23.897 1.00 19.48 ? 210 ILE A CG2   1 
ATOM   1469 C  CD1   . ILE A 1 203 ? -14.276 7.357   26.628 1.00 21.25 ? 210 ILE A CD1   1 
ATOM   1470 N  N     . VAL A 1 204 ? -14.656 5.856   22.197 1.00 16.87 ? 211 VAL A N     1 
ATOM   1471 C  CA    . VAL A 1 204 ? -15.089 5.704   20.814 1.00 19.94 ? 211 VAL A CA    1 
ATOM   1472 C  C     . VAL A 1 204 ? -16.310 6.588   20.597 1.00 23.10 ? 211 VAL A C     1 
ATOM   1473 O  O     . VAL A 1 204 ? -17.342 6.410   21.256 1.00 21.98 ? 211 VAL A O     1 
ATOM   1474 C  CB    . VAL A 1 204 ? -15.396 4.238   20.472 1.00 20.88 ? 211 VAL A CB    1 
ATOM   1475 C  CG1   . VAL A 1 204 ? -15.990 4.141   19.082 1.00 22.89 ? 211 VAL A CG1   1 
ATOM   1476 C  CG2   . VAL A 1 204 ? -14.132 3.398   20.577 1.00 17.54 ? 211 VAL A CG2   1 
ATOM   1477 N  N     . GLU A 1 205 ? -16.199 7.525   19.681 1.00 20.97 ? 212 GLU A N     1 
ATOM   1478 C  CA    . GLU A 1 205 ? -17.306 8.419   19.379 1.00 27.27 ? 212 GLU A CA    1 
ATOM   1479 C  C     . GLU A 1 205 ? -18.582 7.703   19.021 1.00 26.06 ? 212 GLU A C     1 
ATOM   1480 O  O     . GLU A 1 205 ? -18.624 6.839   18.160 1.00 22.11 ? 212 GLU A O     1 
ATOM   1481 C  CB    . GLU A 1 205 ? -16.930 9.376   18.239 1.00 27.18 ? 212 GLU A CB    1 
ATOM   1482 C  CG    . GLU A 1 205 ? -18.043 10.272  17.738 1.00 35.15 ? 212 GLU A CG    1 
ATOM   1483 C  CD    . GLU A 1 205 ? -17.618 11.068  16.519 1.00 42.46 ? 212 GLU A CD    1 
ATOM   1484 O  OE1   . GLU A 1 205 ? -16.424 11.007  16.166 1.00 37.77 ? 212 GLU A OE1   1 
ATOM   1485 O  OE2   . GLU A 1 205 ? -18.472 11.749  15.915 1.00 42.49 ? 212 GLU A OE2   1 
ATOM   1486 N  N     . GLY A 1 206 ? -19.632 8.105   19.690 1.00 28.41 ? 213 GLY A N     1 
ATOM   1487 C  CA    . GLY A 1 206 ? -20.922 7.504   19.434 1.00 23.63 ? 213 GLY A CA    1 
ATOM   1488 C  C     . GLY A 1 206 ? -21.186 6.205   20.158 1.00 24.68 ? 213 GLY A C     1 
ATOM   1489 O  O     . GLY A 1 206 ? -22.313 5.698   20.092 1.00 27.82 ? 213 GLY A O     1 
ATOM   1490 N  N     . GLU A 1 207 ? -20.195 5.641   20.844 1.00 22.40 ? 214 GLU A N     1 
ATOM   1491 C  CA    . GLU A 1 207 ? -20.380 4.418   21.613 1.00 21.63 ? 214 GLU A CA    1 
ATOM   1492 C  C     . GLU A 1 207 ? -20.355 4.658   23.114 1.00 21.84 ? 214 GLU A C     1 
ATOM   1493 O  O     . GLU A 1 207 ? -21.198 4.116   23.837 1.00 21.04 ? 214 GLU A O     1 
ATOM   1494 C  CB    . GLU A 1 207 ? -19.309 3.381   21.234 1.00 23.43 ? 214 GLU A CB    1 
ATOM   1495 C  CG    . GLU A 1 207 ? -19.556 2.671   19.905 1.00 16.77 ? 214 GLU A CG    1 
ATOM   1496 C  CD    . GLU A 1 207 ? -20.490 1.478   20.034 1.00 18.28 ? 214 GLU A CD    1 
ATOM   1497 O  OE1   . GLU A 1 207 ? -21.043 1.268   21.133 1.00 20.41 ? 214 GLU A OE1   1 
ATOM   1498 O  OE2   . GLU A 1 207 ? -20.666 0.748   19.035 1.00 22.00 ? 214 GLU A OE2   1 
ATOM   1499 N  N     . ASN A 1 208 ? -19.409 5.475   23.608 1.00 24.55 ? 215 ASN A N     1 
ATOM   1500 C  CA    . ASN A 1 208 ? -19.262 5.675   25.047 1.00 20.19 ? 215 ASN A CA    1 
ATOM   1501 C  C     . ASN A 1 208 ? -18.636 7.025   25.387 1.00 21.38 ? 215 ASN A C     1 
ATOM   1502 O  O     . ASN A 1 208 ? -17.935 7.139   26.399 1.00 23.74 ? 215 ASN A O     1 
ATOM   1503 C  CB    . ASN A 1 208 ? -18.406 4.559   25.677 1.00 17.91 ? 215 ASN A CB    1 
ATOM   1504 C  CG    . ASN A 1 208 ? -16.999 4.476   25.079 1.00 22.18 ? 215 ASN A CG    1 
ATOM   1505 O  OD1   . ASN A 1 208 ? -16.645 5.227   24.169 1.00 22.85 ? 215 ASN A OD1   1 
ATOM   1506 N  ND2   . ASN A 1 208 ? -16.186 3.570   25.615 1.00 21.87 ? 215 ASN A ND2   1 
ATOM   1507 N  N     . ASP A 1 209 ? -18.872 8.052   24.571 1.00 23.79 ? 216 ASP A N     1 
ATOM   1508 C  CA    . ASP A 1 209 ? -18.166 9.319   24.713 1.00 23.93 ? 216 ASP A CA    1 
ATOM   1509 C  C     . ASP A 1 209 ? -18.967 10.396  25.439 1.00 24.17 ? 216 ASP A C     1 
ATOM   1510 O  O     . ASP A 1 209 ? -18.424 11.475  25.694 1.00 21.15 ? 216 ASP A O     1 
ATOM   1511 C  CB    . ASP A 1 209 ? -17.736 9.845   23.335 1.00 22.07 ? 216 ASP A CB    1 
ATOM   1512 C  CG    . ASP A 1 209 ? -18.906 10.040  22.387 1.00 24.19 ? 216 ASP A CG    1 
ATOM   1513 O  OD1   . ASP A 1 209 ? -19.956 9.394   22.589 1.00 26.25 ? 216 ASP A OD1   1 
ATOM   1514 O  OD2   . ASP A 1 209 ? -18.776 10.841  21.437 1.00 22.37 ? 216 ASP A OD2   1 
ATOM   1515 N  N     . SER A 1 210 ? -20.223 10.143  25.785 1.00 26.39 ? 217 SER A N     1 
ATOM   1516 C  CA    . SER A 1 210 ? -21.031 11.171  26.438 1.00 26.97 ? 217 SER A CA    1 
ATOM   1517 C  C     . SER A 1 210 ? -22.079 10.492  27.315 1.00 30.20 ? 217 SER A C     1 
ATOM   1518 O  O     . SER A 1 210 ? -21.975 9.301   27.625 1.00 30.80 ? 217 SER A O     1 
ATOM   1519 C  CB    . SER A 1 210 ? -21.660 12.107  25.391 1.00 25.79 ? 217 SER A CB    1 
ATOM   1520 O  OG    . SER A 1 210 ? -22.861 11.560  24.871 1.00 22.99 ? 217 SER A OG    1 
ATOM   1521 N  N     . GLU A 1 211 ? -23.086 11.259  27.729 1.00 28.86 ? 218 GLU A N     1 
ATOM   1522 C  CA    . GLU A 1 211 ? -24.240 10.730  28.440 1.00 28.82 ? 218 GLU A CA    1 
ATOM   1523 C  C     . GLU A 1 211 ? -25.431 10.499  27.521 1.00 29.04 ? 218 GLU A C     1 
ATOM   1524 O  O     . GLU A 1 211 ? -26.460 9.994   27.977 1.00 30.86 ? 218 GLU A O     1 
ATOM   1525 C  CB    . GLU A 1 211 ? -24.635 11.667  29.593 1.00 29.96 ? 218 GLU A CB    1 
ATOM   1526 C  CG    . GLU A 1 211 ? -25.356 12.945  29.176 1.00 33.03 ? 218 GLU A CG    1 
ATOM   1527 C  CD    . GLU A 1 211 ? -24.492 13.870  28.339 1.00 34.96 ? 218 GLU A CD    1 
ATOM   1528 O  OE1   . GLU A 1 211 ? -23.250 13.824  28.477 1.00 38.40 ? 218 GLU A OE1   1 
ATOM   1529 O  OE2   . GLU A 1 211 ? -25.059 14.643  27.539 1.00 38.62 ? 218 GLU A OE2   1 
ATOM   1530 N  N     . LYS A 1 212 ? -25.294 10.818  26.250 1.00 28.89 ? 219 LYS A N     1 
ATOM   1531 C  CA    . LYS A 1 212 ? -26.343 10.527  25.297 1.00 33.00 ? 219 LYS A CA    1 
ATOM   1532 C  C     . LYS A 1 212 ? -26.181 9.090   24.769 1.00 36.51 ? 219 LYS A C     1 
ATOM   1533 O  O     . LYS A 1 212 ? -27.119 8.542   24.213 1.00 36.08 ? 219 LYS A O     1 
ATOM   1534 C  CB    . LYS A 1 212 ? -26.280 11.512  24.166 1.00 37.66 ? 219 LYS A CB    1 
ATOM   1535 C  CG    . LYS A 1 212 ? -26.067 12.956  24.565 1.00 39.44 ? 219 LYS A CG    1 
ATOM   1536 C  CD    . LYS A 1 212 ? -25.644 13.768  23.351 1.00 41.84 ? 219 LYS A CD    1 
ATOM   1537 C  CE    . LYS A 1 212 ? -25.182 15.166  23.734 1.00 39.83 ? 219 LYS A CE    1 
ATOM   1538 N  NZ    . LYS A 1 212 ? -26.301 16.022  24.211 1.00 38.26 ? 219 LYS A NZ    1 
ATOM   1539 N  N     . THR A 1 213 ? -25.012 8.483   24.948 1.00 31.09 ? 220 THR A N     1 
ATOM   1540 C  CA    . THR A 1 213 ? -24.763 7.107   24.552 1.00 26.68 ? 220 THR A CA    1 
ATOM   1541 C  C     . THR A 1 213 ? -25.137 6.150   25.684 1.00 23.88 ? 220 THR A C     1 
ATOM   1542 O  O     . THR A 1 213 ? -25.378 6.553   26.825 1.00 23.52 ? 220 THR A O     1 
ATOM   1543 C  CB    . THR A 1 213 ? -23.298 6.922   24.147 1.00 24.27 ? 220 THR A CB    1 
ATOM   1544 O  OG1   . THR A 1 213 ? -22.445 7.485   25.151 1.00 26.79 ? 220 THR A OG1   1 
ATOM   1545 C  CG2   . THR A 1 213 ? -23.028 7.618   22.815 1.00 23.47 ? 220 THR A CG2   1 
ATOM   1546 N  N     . LEU A 1 214 ? -25.186 4.859   25.351 1.00 22.86 ? 221 LEU A N     1 
ATOM   1547 C  CA    . LEU A 1 214 ? -25.609 3.839   26.303 1.00 20.88 ? 221 LEU A CA    1 
ATOM   1548 C  C     . LEU A 1 214 ? -24.618 3.640   27.443 1.00 25.73 ? 221 LEU A C     1 
ATOM   1549 O  O     . LEU A 1 214 ? -24.971 2.996   28.437 1.00 23.11 ? 221 LEU A O     1 
ATOM   1550 C  CB    . LEU A 1 214 ? -25.839 2.515   25.570 1.00 23.01 ? 221 LEU A CB    1 
ATOM   1551 C  CG    . LEU A 1 214 ? -26.834 2.582   24.408 1.00 27.28 ? 221 LEU A CG    1 
ATOM   1552 C  CD1   . LEU A 1 214 ? -26.891 1.265   23.646 1.00 21.39 ? 221 LEU A CD1   1 
ATOM   1553 C  CD2   . LEU A 1 214 ? -28.214 2.972   24.912 1.00 15.94 ? 221 LEU A CD2   1 
ATOM   1554 N  N     . ARG A 1 215 ? -23.398 4.164   27.323 1.00 27.82 ? 222 ARG A N     1 
ATOM   1555 C  CA    . ARG A 1 215 ? -22.409 4.115   28.390 1.00 22.78 ? 222 ARG A CA    1 
ATOM   1556 C  C     . ARG A 1 215 ? -21.619 5.416   28.396 1.00 23.51 ? 222 ARG A C     1 
ATOM   1557 O  O     . ARG A 1 215 ? -21.460 6.069   27.361 1.00 21.65 ? 222 ARG A O     1 
ATOM   1558 C  CB    . ARG A 1 215 ? -21.442 2.928   28.233 1.00 19.24 ? 222 ARG A CB    1 
ATOM   1559 C  CG    . ARG A 1 215 ? -22.094 1.554   28.313 1.00 19.98 ? 222 ARG A CG    1 
ATOM   1560 C  CD    . ARG A 1 215 ? -22.467 1.189   29.740 1.00 14.97 ? 222 ARG A CD    1 
ATOM   1561 N  NE    . ARG A 1 215 ? -23.603 0.276   29.791 1.00 20.22 ? 222 ARG A NE    1 
ATOM   1562 C  CZ    . ARG A 1 215 ? -23.516 -1.036  29.619 1.00 19.73 ? 222 ARG A CZ    1 
ATOM   1563 N  NH1   . ARG A 1 215 ? -22.355 -1.628  29.388 1.00 19.18 ? 222 ARG A NH1   1 
ATOM   1564 N  NH2   . ARG A 1 215 ? -24.622 -1.773  29.676 1.00 21.83 ? 222 ARG A NH2   1 
ATOM   1565 N  N     . ASP A 1 216 ? -21.129 5.787   29.577 1.00 22.03 ? 223 ASP A N     1 
ATOM   1566 C  CA    . ASP A 1 216 ? -20.297 6.974   29.767 1.00 20.15 ? 223 ASP A CA    1 
ATOM   1567 C  C     . ASP A 1 216 ? -18.971 6.508   30.363 1.00 25.64 ? 223 ASP A C     1 
ATOM   1568 O  O     . ASP A 1 216 ? -18.833 6.373   31.582 1.00 24.94 ? 223 ASP A O     1 
ATOM   1569 C  CB    . ASP A 1 216 ? -20.983 8.012   30.657 1.00 18.96 ? 223 ASP A CB    1 
ATOM   1570 C  CG    . ASP A 1 216 ? -20.329 9.382   30.563 1.00 26.34 ? 223 ASP A CG    1 
ATOM   1571 O  OD1   . ASP A 1 216 ? -19.302 9.505   29.864 1.00 25.20 ? 223 ASP A OD1   1 
ATOM   1572 O  OD2   . ASP A 1 216 ? -20.837 10.337  31.189 1.00 28.53 ? 223 ASP A OD2   1 
ATOM   1573 N  N     . ALA A 1 217 ? -17.996 6.266   29.490 1.00 24.77 ? 224 ALA A N     1 
ATOM   1574 C  CA    . ALA A 1 217 ? -16.682 5.780   29.888 1.00 21.57 ? 224 ALA A CA    1 
ATOM   1575 C  C     . ALA A 1 217 ? -15.749 6.888   30.353 1.00 21.43 ? 224 ALA A C     1 
ATOM   1576 O  O     . ALA A 1 217 ? -14.591 6.601   30.676 1.00 17.22 ? 224 ALA A O     1 
ATOM   1577 C  CB    . ALA A 1 217 ? -16.032 5.027   28.725 1.00 17.54 ? 224 ALA A CB    1 
ATOM   1578 N  N     . ARG A 1 218 ? -16.221 8.135   30.406 1.00 22.17 ? 225 ARG A N     1 
ATOM   1579 C  CA    . ARG A 1 218 ? -15.331 9.255   30.691 1.00 22.25 ? 225 ARG A CA    1 
ATOM   1580 C  C     . ARG A 1 218 ? -14.720 9.162   32.084 1.00 18.31 ? 225 ARG A C     1 
ATOM   1581 O  O     . ARG A 1 218 ? -13.601 9.640   32.302 1.00 18.69 ? 225 ARG A O     1 
ATOM   1582 C  CB    . ARG A 1 218 ? -16.085 10.575  30.525 1.00 21.21 ? 225 ARG A CB    1 
ATOM   1583 C  CG    . ARG A 1 218 ? -15.939 11.192  29.144 1.00 22.38 ? 225 ARG A CG    1 
ATOM   1584 C  CD    . ARG A 1 218 ? -16.926 12.325  28.934 1.00 20.35 ? 225 ARG A CD    1 
ATOM   1585 N  NE    . ARG A 1 218 ? -18.203 12.061  29.585 1.00 27.71 ? 225 ARG A NE    1 
ATOM   1586 C  CZ    . ARG A 1 218 ? -19.224 12.907  29.608 1.00 32.21 ? 225 ARG A CZ    1 
ATOM   1587 N  NH1   . ARG A 1 218 ? -19.159 14.086  29.010 1.00 30.59 ? 225 ARG A NH1   1 
ATOM   1588 N  NH2   . ARG A 1 218 ? -20.338 12.561  30.246 1.00 35.67 ? 225 ARG A NH2   1 
ATOM   1589 N  N     . ARG A 1 219 ? -15.423 8.634   33.063 1.00 22.76 ? 226 ARG A N     1 
ATOM   1590 C  CA    A ARG A 1 219 ? -14.855 8.432   34.394 0.52 20.84 ? 226 ARG A CA    1 
ATOM   1591 C  CA    B ARG A 1 219 ? -14.905 8.429   34.388 0.48 20.68 ? 226 ARG A CA    1 
ATOM   1592 C  C     . ARG A 1 219 ? -13.699 7.374   34.522 1.00 21.54 ? 226 ARG A C     1 
ATOM   1593 O  O     . ARG A 1 219 ? -12.935 7.270   35.503 1.00 18.40 ? 226 ARG A O     1 
ATOM   1594 C  CB    A ARG A 1 219 ? -15.986 8.096   35.387 0.52 19.94 ? 226 ARG A CB    1 
ATOM   1595 C  CB    B ARG A 1 219 ? -16.054 8.132   35.357 0.48 19.89 ? 226 ARG A CB    1 
ATOM   1596 C  CG    A ARG A 1 219 ? -16.328 6.621   35.553 0.52 20.21 ? 226 ARG A CG    1 
ATOM   1597 C  CG    B ARG A 1 219 ? -16.556 6.693   35.360 0.48 20.69 ? 226 ARG A CG    1 
ATOM   1598 C  CD    A ARG A 1 219 ? -17.489 6.454   36.529 0.52 20.07 ? 226 ARG A CD    1 
ATOM   1599 C  CD    B ARG A 1 219 ? -17.831 6.577   36.195 0.48 20.47 ? 226 ARG A CD    1 
ATOM   1600 N  NE    A ARG A 1 219 ? -17.948 5.073   36.670 0.52 20.25 ? 226 ARG A NE    1 
ATOM   1601 N  NE    B ARG A 1 219 ? -18.469 5.268   36.101 0.48 19.08 ? 226 ARG A NE    1 
ATOM   1602 C  CZ    A ARG A 1 219 ? -17.718 4.301   37.731 0.52 21.81 ? 226 ARG A CZ    1 
ATOM   1603 C  CZ    B ARG A 1 219 ? -19.346 4.919   35.169 0.48 19.82 ? 226 ARG A CZ    1 
ATOM   1604 N  NH1   A ARG A 1 219 ? -17.043 4.768   38.768 0.52 23.37 ? 226 ARG A NH1   1 
ATOM   1605 N  NH1   B ARG A 1 219 ? -19.698 5.752   34.202 0.48 19.66 ? 226 ARG A NH1   1 
ATOM   1606 N  NH2   A ARG A 1 219 ? -18.177 3.060   37.767 0.52 19.71 ? 226 ARG A NH2   1 
ATOM   1607 N  NH2   B ARG A 1 219 ? -19.884 3.703   35.207 0.48 14.87 ? 226 ARG A NH2   1 
ATOM   1608 N  N     . PHE A 1 220 ? -13.608 6.539   33.501 1.00 18.32 ? 227 PHE A N     1 
ATOM   1609 C  CA    . PHE A 1 220 ? -12.584 5.502   33.532 1.00 17.09 ? 227 PHE A CA    1 
ATOM   1610 C  C     . PHE A 1 220 ? -11.290 5.900   32.831 1.00 18.59 ? 227 PHE A C     1 
ATOM   1611 O  O     . PHE A 1 220 ? -10.306 5.157   32.920 1.00 17.68 ? 227 PHE A O     1 
ATOM   1612 C  CB    . PHE A 1 220 ? -13.116 4.214   32.888 1.00 16.52 ? 227 PHE A CB    1 
ATOM   1613 C  CG    . PHE A 1 220 ? -14.266 3.587   33.624 1.00 15.18 ? 227 PHE A CG    1 
ATOM   1614 C  CD1   . PHE A 1 220 ? -14.038 2.746   34.701 1.00 14.98 ? 227 PHE A CD1   1 
ATOM   1615 C  CD2   . PHE A 1 220 ? -15.574 3.826   33.232 1.00 16.93 ? 227 PHE A CD2   1 
ATOM   1616 C  CE1   . PHE A 1 220 ? -15.093 2.160   35.378 1.00 19.30 ? 227 PHE A CE1   1 
ATOM   1617 C  CE2   . PHE A 1 220 ? -16.635 3.243   33.905 1.00 15.78 ? 227 PHE A CE2   1 
ATOM   1618 C  CZ    . PHE A 1 220 ? -16.394 2.409   34.980 1.00 15.76 ? 227 PHE A CZ    1 
ATOM   1619 N  N     . THR A 1 221 ? -11.262 7.039   32.144 1.00 14.75 ? 228 THR A N     1 
ATOM   1620 C  CA    . THR A 1 221 ? -10.141 7.368   31.274 1.00 18.01 ? 228 THR A CA    1 
ATOM   1621 C  C     . THR A 1 221 ? -8.874  7.649   32.075 1.00 18.06 ? 228 THR A C     1 
ATOM   1622 O  O     . THR A 1 221 ? -8.918  8.165   33.194 1.00 18.49 ? 228 THR A O     1 
ATOM   1623 C  CB    . THR A 1 221 ? -10.477 8.580   30.410 1.00 18.15 ? 228 THR A CB    1 
ATOM   1624 O  OG1   . THR A 1 221 ? -10.938 9.650   31.245 1.00 18.36 ? 228 THR A OG1   1 
ATOM   1625 C  CG2   . THR A 1 221 ? -11.553 8.222   29.403 1.00 17.40 ? 228 THR A CG2   1 
ATOM   1626 N  N     . ILE A 1 222 ? -7.733  7.302   31.478 1.00 18.31 ? 229 ILE A N     1 
ATOM   1627 C  CA    . ILE A 1 222 ? -6.426  7.527   32.076 1.00 16.92 ? 229 ILE A CA    1 
ATOM   1628 C  C     . ILE A 1 222 ? -5.525  8.213   31.061 1.00 20.28 ? 229 ILE A C     1 
ATOM   1629 O  O     . ILE A 1 222 ? -5.797  8.230   29.859 1.00 22.46 ? 229 ILE A O     1 
ATOM   1630 C  CB    . ILE A 1 222 ? -5.764  6.220   32.560 1.00 16.25 ? 229 ILE A CB    1 
ATOM   1631 C  CG1   . ILE A 1 222 ? -5.648  5.224   31.407 1.00 16.81 ? 229 ILE A CG1   1 
ATOM   1632 C  CG2   . ILE A 1 222 ? -6.539  5.625   33.711 1.00 16.92 ? 229 ILE A CG2   1 
ATOM   1633 C  CD1   . ILE A 1 222 ? -5.046  3.903   31.818 1.00 13.40 ? 229 ILE A CD1   1 
ATOM   1634 N  N     . SER A 1 223 ? -4.429  8.768   31.568 1.00 18.39 ? 230 SER A N     1 
ATOM   1635 C  CA    . SER A 1 223 ? -3.437  9.437   30.743 1.00 17.56 ? 230 SER A CA    1 
ATOM   1636 C  C     . SER A 1 223 ? -2.398  8.437   30.239 1.00 19.59 ? 230 SER A C     1 
ATOM   1637 O  O     . SER A 1 223 ? -2.333  7.288   30.680 1.00 18.17 ? 230 SER A O     1 
ATOM   1638 C  CB    . SER A 1 223 ? -2.753  10.555  31.531 1.00 22.12 ? 230 SER A CB    1 
ATOM   1639 O  OG    . SER A 1 223 ? -1.842  10.027  32.481 1.00 21.43 ? 230 SER A OG    1 
ATOM   1640 N  N     . ASP A 1 224 ? -1.580  8.866   29.309 1.00 19.80 ? 231 ASP A N     1 
ATOM   1641 C  CA    . ASP A 1 224 ? -0.495  8.037   28.842 1.00 22.76 ? 231 ASP A CA    1 
ATOM   1642 C  C     . ASP A 1 224 ? 0.493   7.688   29.959 1.00 20.48 ? 231 ASP A C     1 
ATOM   1643 O  O     . ASP A 1 224 ? 1.098   6.631   29.926 1.00 19.11 ? 231 ASP A O     1 
ATOM   1644 C  CB    . ASP A 1 224 ? 0.200   8.726   27.680 1.00 24.00 ? 231 ASP A CB    1 
ATOM   1645 C  CG    . ASP A 1 224 ? -0.063  8.062   26.356 1.00 41.08 ? 231 ASP A CG    1 
ATOM   1646 O  OD1   . ASP A 1 224 ? -0.220  6.824   26.314 1.00 46.62 ? 231 ASP A OD1   1 
ATOM   1647 O  OD2   . ASP A 1 224 ? -0.088  8.783   25.339 1.00 49.20 ? 231 ASP A OD2   1 
ATOM   1648 N  N     . LYS A 1 225 ? 0.609   8.556   30.952 1.00 18.38 ? 232 LYS A N     1 
ATOM   1649 C  CA    . LYS A 1 225 ? 1.479   8.271   32.088 1.00 18.68 ? 232 LYS A CA    1 
ATOM   1650 C  C     . LYS A 1 225 ? 0.857   7.247   33.031 1.00 18.81 ? 232 LYS A C     1 
ATOM   1651 O  O     . LYS A 1 225 ? 1.551   6.345   33.513 1.00 22.23 ? 232 LYS A O     1 
ATOM   1652 C  CB    . LYS A 1 225 ? 1.788   9.564   32.843 1.00 19.15 ? 232 LYS A CB    1 
ATOM   1653 C  CG    . LYS A 1 225 ? 2.306   10.690  31.964 1.00 19.31 ? 232 LYS A CG    1 
ATOM   1654 C  CD    . LYS A 1 225 ? 1.993   12.044  32.582 1.00 24.91 ? 232 LYS A CD    1 
ATOM   1655 C  CE    . LYS A 1 225 ? 3.068   13.069  32.264 1.00 25.56 ? 232 LYS A CE    1 
ATOM   1656 N  NZ    . LYS A 1 225 ? 3.751   12.790  30.970 1.00 30.44 ? 232 LYS A NZ    1 
ATOM   1657 N  N     . GLN A 1 226 ? -0.442  7.376   33.313 1.00 18.60 ? 233 GLN A N     1 
ATOM   1658 C  CA    . GLN A 1 226 ? -1.110  6.408   34.179 1.00 18.35 ? 233 GLN A CA    1 
ATOM   1659 C  C     . GLN A 1 226 ? -1.124  5.022   33.549 1.00 18.44 ? 233 GLN A C     1 
ATOM   1660 O  O     . GLN A 1 226 ? -0.953  4.015   34.247 1.00 18.36 ? 233 GLN A O     1 
ATOM   1661 C  CB    . GLN A 1 226 ? -2.534  6.868   34.485 1.00 18.26 ? 233 GLN A CB    1 
ATOM   1662 C  CG    . GLN A 1 226 ? -2.619  8.019   35.465 1.00 17.53 ? 233 GLN A CG    1 
ATOM   1663 C  CD    . GLN A 1 226 ? -3.981  8.677   35.460 1.00 18.77 ? 233 GLN A CD    1 
ATOM   1664 O  OE1   . GLN A 1 226 ? -4.579  8.885   34.405 1.00 21.55 ? 233 GLN A OE1   1 
ATOM   1665 N  NE2   . GLN A 1 226 ? -4.479  9.015   36.642 1.00 14.14 ? 233 GLN A NE2   1 
ATOM   1666 N  N     . PHE A 1 227 ? -1.337  4.950   32.233 1.00 18.09 ? 234 PHE A N     1 
ATOM   1667 C  CA    . PHE A 1 227 ? -1.242  3.676   31.528 1.00 15.52 ? 234 PHE A CA    1 
ATOM   1668 C  C     . PHE A 1 227 ? 0.153   3.081   31.657 1.00 17.15 ? 234 PHE A C     1 
ATOM   1669 O  O     . PHE A 1 227 ? 0.306   1.872   31.873 1.00 18.47 ? 234 PHE A O     1 
ATOM   1670 C  CB    . PHE A 1 227 ? -1.603  3.867   30.054 1.00 16.19 ? 234 PHE A CB    1 
ATOM   1671 C  CG    . PHE A 1 227 ? -1.706  2.584   29.276 1.00 15.98 ? 234 PHE A CG    1 
ATOM   1672 C  CD1   . PHE A 1 227 ? -2.544  1.564   29.698 1.00 15.43 ? 234 PHE A CD1   1 
ATOM   1673 C  CD2   . PHE A 1 227 ? -0.977  2.406   28.112 1.00 17.37 ? 234 PHE A CD2   1 
ATOM   1674 C  CE1   . PHE A 1 227 ? -2.645  0.383   28.979 1.00 13.03 ? 234 PHE A CE1   1 
ATOM   1675 C  CE2   . PHE A 1 227 ? -1.074  1.230   27.387 1.00 19.19 ? 234 PHE A CE2   1 
ATOM   1676 C  CZ    . PHE A 1 227 ? -1.910  0.216   27.823 1.00 13.16 ? 234 PHE A CZ    1 
ATOM   1677 N  N     . GLU A 1 228 ? 1.184   3.918   31.526 1.00 16.88 ? 235 GLU A N     1 
ATOM   1678 C  CA    . GLU A 1 228 ? 2.555   3.430   31.611 1.00 18.58 ? 235 GLU A CA    1 
ATOM   1679 C  C     . GLU A 1 228 ? 2.879   2.930   33.012 1.00 19.34 ? 235 GLU A C     1 
ATOM   1680 O  O     . GLU A 1 228 ? 3.730   2.047   33.174 1.00 20.72 ? 235 GLU A O     1 
ATOM   1681 C  CB    . GLU A 1 228 ? 3.524   4.533   31.179 1.00 23.88 ? 235 GLU A CB    1 
ATOM   1682 C  CG    . GLU A 1 228 ? 4.963   4.351   31.643 1.00 24.91 ? 235 GLU A CG    1 
ATOM   1683 C  CD    . GLU A 1 228 ? 5.676   3.208   30.941 1.00 27.23 ? 235 GLU A CD    1 
ATOM   1684 O  OE1   . GLU A 1 228 ? 5.164   2.724   29.909 1.00 29.67 ? 235 GLU A OE1   1 
ATOM   1685 O  OE2   . GLU A 1 228 ? 6.749   2.790   31.425 1.00 31.44 ? 235 GLU A OE2   1 
ATOM   1686 N  N     . VAL A 1 229 ? 2.202   3.465   34.030 1.00 18.60 ? 236 VAL A N     1 
ATOM   1687 C  CA    . VAL A 1 229 ? 2.353   2.939   35.385 1.00 16.32 ? 236 VAL A CA    1 
ATOM   1688 C  C     . VAL A 1 229 ? 2.005   1.457   35.417 1.00 18.73 ? 236 VAL A C     1 
ATOM   1689 O  O     . VAL A 1 229 ? 2.746   0.638   35.973 1.00 19.88 ? 236 VAL A O     1 
ATOM   1690 C  CB    . VAL A 1 229 ? 1.489   3.739   36.375 1.00 13.86 ? 236 VAL A CB    1 
ATOM   1691 C  CG1   . VAL A 1 229 ? 1.293   2.948   37.657 1.00 18.24 ? 236 VAL A CG1   1 
ATOM   1692 C  CG2   . VAL A 1 229 ? 2.132   5.078   36.670 1.00 15.96 ? 236 VAL A CG2   1 
ATOM   1693 N  N     . PHE A 1 230 ? 0.875   1.088   34.811 1.00 20.04 ? 237 PHE A N     1 
ATOM   1694 C  CA    . PHE A 1 230 ? 0.493   -0.319  34.765 1.00 18.31 ? 237 PHE A CA    1 
ATOM   1695 C  C     . PHE A 1 230 ? 1.413   -1.113  33.847 1.00 12.51 ? 237 PHE A C     1 
ATOM   1696 O  O     . PHE A 1 230 ? 1.772   -2.256  34.158 1.00 15.13 ? 237 PHE A O     1 
ATOM   1697 C  CB    . PHE A 1 230 ? -0.956  -0.459  34.305 1.00 14.68 ? 237 PHE A CB    1 
ATOM   1698 C  CG    . PHE A 1 230 ? -1.466  -1.872  34.334 1.00 12.34 ? 237 PHE A CG    1 
ATOM   1699 C  CD1   . PHE A 1 230 ? -2.040  -2.391  35.482 1.00 16.77 ? 237 PHE A CD1   1 
ATOM   1700 C  CD2   . PHE A 1 230 ? -1.362  -2.684  33.216 1.00 11.63 ? 237 PHE A CD2   1 
ATOM   1701 C  CE1   . PHE A 1 230 ? -2.507  -3.694  35.514 1.00 17.70 ? 237 PHE A CE1   1 
ATOM   1702 C  CE2   . PHE A 1 230 ? -1.825  -3.986  33.241 1.00 11.68 ? 237 PHE A CE2   1 
ATOM   1703 C  CZ    . PHE A 1 230 ? -2.399  -4.493  34.391 1.00 15.74 ? 237 PHE A CZ    1 
ATOM   1704 N  N     . CYS A 1 231 ? 1.798   -0.532  32.709 1.00 16.48 ? 238 CYS A N     1 
ATOM   1705 C  CA    . CYS A 1 231 ? 2.550   -1.287  31.711 1.00 16.11 ? 238 CYS A CA    1 
ATOM   1706 C  C     . CYS A 1 231 ? 3.926   -1.676  32.235 1.00 17.92 ? 238 CYS A C     1 
ATOM   1707 O  O     . CYS A 1 231 ? 4.332   -2.839  32.133 1.00 21.30 ? 238 CYS A O     1 
ATOM   1708 C  CB    . CYS A 1 231 ? 2.671   -0.478  30.418 1.00 18.84 ? 238 CYS A CB    1 
ATOM   1709 S  SG    . CYS A 1 231 ? 1.143   -0.373  29.458 1.00 18.85 ? 238 CYS A SG    1 
ATOM   1710 N  N     . SER A 1 232 ? 4.659   -0.714  32.807 1.00 19.91 ? 239 SER A N     1 
ATOM   1711 C  CA    . SER A 1 232 ? 6.001   -1.003  33.307 1.00 21.82 ? 239 SER A CA    1 
ATOM   1712 C  C     . SER A 1 232 ? 5.982   -2.061  34.400 1.00 21.89 ? 239 SER A C     1 
ATOM   1713 O  O     . SER A 1 232 ? 6.927   -2.849  34.519 1.00 21.81 ? 239 SER A O     1 
ATOM   1714 C  CB    . SER A 1 232 ? 6.657   0.278   33.824 1.00 25.23 ? 239 SER A CB    1 
ATOM   1715 O  OG    . SER A 1 232 ? 6.486   0.405   35.225 1.00 28.28 ? 239 SER A OG    1 
ATOM   1716 N  N     . LYS A 1 233 ? 4.914   -2.104  35.196 1.00 20.64 ? 240 LYS A N     1 
ATOM   1717 C  CA    . LYS A 1 233 ? 4.815   -3.087  36.265 1.00 18.70 ? 240 LYS A CA    1 
ATOM   1718 C  C     . LYS A 1 233 ? 4.609   -4.504  35.742 1.00 16.11 ? 240 LYS A C     1 
ATOM   1719 O  O     . LYS A 1 233 ? 4.882   -5.464  36.471 1.00 18.71 ? 240 LYS A O     1 
ATOM   1720 C  CB    . LYS A 1 233 ? 3.672   -2.703  37.204 1.00 16.97 ? 240 LYS A CB    1 
ATOM   1721 C  CG    . LYS A 1 233 ? 3.821   -3.233  38.614 1.00 18.17 ? 240 LYS A CG    1 
ATOM   1722 C  CD    . LYS A 1 233 ? 2.852   -2.559  39.572 1.00 19.93 ? 240 LYS A CD    1 
ATOM   1723 C  CE    . LYS A 1 233 ? 2.646   -1.087  39.247 1.00 23.27 ? 240 LYS A CE    1 
ATOM   1724 N  NZ    . LYS A 1 233 ? 1.703   -0.460  40.216 1.00 20.87 ? 240 LYS A NZ    1 
ATOM   1725 N  N     . HIS A 1 234 ? 4.151   -4.664  34.497 1.00 17.33 ? 241 HIS A N     1 
ATOM   1726 C  CA    . HIS A 1 234 ? 3.766   -5.975  33.991 1.00 17.63 ? 241 HIS A CA    1 
ATOM   1727 C  C     . HIS A 1 234 ? 4.361   -6.346  32.639 1.00 18.10 ? 241 HIS A C     1 
ATOM   1728 O  O     . HIS A 1 234 ? 4.150   -7.479  32.196 1.00 15.41 ? 241 HIS A O     1 
ATOM   1729 C  CB    . HIS A 1 234 ? 2.237   -6.075  33.879 1.00 14.81 ? 241 HIS A CB    1 
ATOM   1730 C  CG    . HIS A 1 234 ? 1.516   -5.797  35.161 1.00 14.16 ? 241 HIS A CG    1 
ATOM   1731 N  ND1   . HIS A 1 234 ? 1.109   -4.532  35.525 1.00 15.62 ? 241 HIS A ND1   1 
ATOM   1732 C  CD2   . HIS A 1 234 ? 1.125   -6.620  36.162 1.00 17.45 ? 241 HIS A CD2   1 
ATOM   1733 C  CE1   . HIS A 1 234 ? 0.501   -4.587  36.696 1.00 17.96 ? 241 HIS A CE1   1 
ATOM   1734 N  NE2   . HIS A 1 234 ? 0.497   -5.843  37.104 1.00 18.02 ? 241 HIS A NE2   1 
ATOM   1735 N  N     . ARG A 1 235 ? 5.050   -5.464  31.942 1.00 17.85 ? 242 ARG A N     1 
ATOM   1736 C  CA    . ARG A 1 235 ? 5.527   -5.790  30.597 1.00 17.72 ? 242 ARG A CA    1 
ATOM   1737 C  C     . ARG A 1 235 ? 6.531   -6.939  30.523 1.00 21.44 ? 242 ARG A C     1 
ATOM   1738 O  O     . ARG A 1 235 ? 6.788   -7.463  29.458 1.00 26.61 ? 242 ARG A O     1 
ATOM   1739 C  CB    . ARG A 1 235 ? 6.151   -4.583  29.945 1.00 17.98 ? 242 ARG A CB    1 
ATOM   1740 C  CG    . ARG A 1 235 ? 7.564   -4.274  30.395 1.00 18.52 ? 242 ARG A CG    1 
ATOM   1741 C  CD    . ARG A 1 235 ? 7.758   -2.782  30.554 1.00 20.06 ? 242 ARG A CD    1 
ATOM   1742 N  NE    . ARG A 1 235 ? 7.099   -2.037  29.494 1.00 19.69 ? 242 ARG A NE    1 
ATOM   1743 C  CZ    . ARG A 1 235 ? 6.938   -0.724  29.508 1.00 22.12 ? 242 ARG A CZ    1 
ATOM   1744 N  NH1   . ARG A 1 235 ? 7.388   -0.015  30.525 1.00 25.11 ? 242 ARG A NH1   1 
ATOM   1745 N  NH2   . ARG A 1 235 ? 6.323   -0.122  28.511 1.00 23.53 ? 242 ARG A NH2   1 
ATOM   1746 N  N     . HIS A 1 236 ? 7.106   -7.309  31.642 1.00 14.72 ? 243 HIS A N     1 
ATOM   1747 C  CA    . HIS A 1 236 ? 8.117   -8.358  31.591 1.00 17.58 ? 243 HIS A CA    1 
ATOM   1748 C  C     . HIS A 1 236 ? 7.540   -9.708  31.182 1.00 19.66 ? 243 HIS A C     1 
ATOM   1749 O  O     . HIS A 1 236 ? 8.303   -10.601 30.796 1.00 20.86 ? 243 HIS A O     1 
ATOM   1750 C  CB    . HIS A 1 236 ? 8.812   -8.478  32.945 1.00 19.46 ? 243 HIS A CB    1 
ATOM   1751 C  CG    . HIS A 1 236 ? 7.898   -8.906  34.047 1.00 18.39 ? 243 HIS A CG    1 
ATOM   1752 N  ND1   . HIS A 1 236 ? 7.213   -8.008  34.835 1.00 16.74 ? 243 HIS A ND1   1 
ATOM   1753 C  CD2   . HIS A 1 236 ? 7.549   -10.138 34.488 1.00 17.81 ? 243 HIS A CD2   1 
ATOM   1754 C  CE1   . HIS A 1 236 ? 6.482   -8.667  35.716 1.00 17.41 ? 243 HIS A CE1   1 
ATOM   1755 N  NE2   . HIS A 1 236 ? 6.669   -9.960  35.528 1.00 18.60 ? 243 HIS A NE2   1 
ATOM   1756 N  N     . HIS A 1 237 ? 6.222   -9.879  31.254 1.00 19.80 ? 244 HIS A N     1 
ATOM   1757 C  CA    . HIS A 1 237 ? 5.607   -11.147 30.885 1.00 19.46 ? 244 HIS A CA    1 
ATOM   1758 C  C     . HIS A 1 237 ? 5.649   -11.340 29.373 1.00 15.68 ? 244 HIS A C     1 
ATOM   1759 O  O     . HIS A 1 237 ? 5.446   -10.395 28.604 1.00 16.00 ? 244 HIS A O     1 
ATOM   1760 C  CB    . HIS A 1 237 ? 4.162   -11.201 31.386 1.00 15.84 ? 244 HIS A CB    1 
ATOM   1761 C  CG    . HIS A 1 237 ? 4.038   -11.214 32.879 1.00 16.31 ? 244 HIS A CG    1 
ATOM   1762 N  ND1   . HIS A 1 237 ? 4.249   -12.347 33.636 1.00 15.60 ? 244 HIS A ND1   1 
ATOM   1763 C  CD2   . HIS A 1 237 ? 3.725   -10.230 33.755 1.00 15.66 ? 244 HIS A CD2   1 
ATOM   1764 C  CE1   . HIS A 1 237 ? 4.068   -12.061 34.913 1.00 16.18 ? 244 HIS A CE1   1 
ATOM   1765 N  NE2   . HIS A 1 237 ? 3.751   -10.783 35.013 1.00 15.62 ? 244 HIS A NE2   1 
ATOM   1766 N  N     . LYS A 1 238 ? 5.876   -12.551 28.936 1.00 16.11 ? 245 LYS A N     1 
ATOM   1767 C  CA    . LYS A 1 238 ? 5.940   -12.843 27.518 1.00 20.96 ? 245 LYS A CA    1 
ATOM   1768 C  C     . LYS A 1 238 ? 4.588   -12.658 26.864 1.00 17.87 ? 245 LYS A C     1 
ATOM   1769 O  O     . LYS A 1 238 ? 4.502   -12.188 25.753 1.00 19.90 ? 245 LYS A O     1 
ATOM   1770 C  CB    . LYS A 1 238 ? 6.454   -14.267 27.268 1.00 15.16 ? 245 LYS A CB    1 
ATOM   1771 C  CG    . LYS A 1 238 ? 6.427   -14.642 25.800 1.00 23.12 ? 245 LYS A CG    1 
ATOM   1772 C  CD    . LYS A 1 238 ? 6.967   -16.032 25.554 1.00 22.47 ? 245 LYS A CD    1 
ATOM   1773 C  CE    . LYS A 1 238 ? 6.748   -16.459 24.115 1.00 20.86 ? 245 LYS A CE    1 
ATOM   1774 N  NZ    . LYS A 1 238 ? 7.116   -17.886 23.932 1.00 27.37 ? 245 LYS A NZ    1 
ATOM   1775 N  N     . SER A 1 239 ? 3.541   -13.020 27.581 1.00 20.62 ? 246 SER A N     1 
ATOM   1776 C  CA    . SER A 1 239 ? 2.187   -12.846 27.063 1.00 17.18 ? 246 SER A CA    1 
ATOM   1777 C  C     . SER A 1 239 ? 1.807   -11.383 26.889 1.00 17.13 ? 246 SER A C     1 
ATOM   1778 O  O     . SER A 1 239 ? 0.892   -11.083 26.113 1.00 17.63 ? 246 SER A O     1 
ATOM   1779 C  CB    . SER A 1 239 ? 1.173   -13.510 27.995 1.00 14.18 ? 246 SER A CB    1 
ATOM   1780 O  OG    . SER A 1 239 ? 1.351   -13.087 29.337 1.00 15.59 ? 246 SER A OG    1 
ATOM   1781 N  N     . PHE A 1 240 ? 2.491   -10.476 27.582 1.00 15.28 ? 247 PHE A N     1 
ATOM   1782 C  CA    . PHE A 1 240 ? 2.050   -9.092  27.678 1.00 14.43 ? 247 PHE A CA    1 
ATOM   1783 C  C     . PHE A 1 240 ? 2.010   -8.421  26.311 1.00 13.63 ? 247 PHE A C     1 
ATOM   1784 O  O     . PHE A 1 240 ? 2.994   -8.436  25.566 1.00 21.45 ? 247 PHE A O     1 
ATOM   1785 C  CB    . PHE A 1 240 ? 2.977   -8.327  28.619 1.00 17.88 ? 247 PHE A CB    1 
ATOM   1786 C  CG    . PHE A 1 240 ? 2.628   -6.881  28.772 1.00 17.56 ? 247 PHE A CG    1 
ATOM   1787 C  CD1   . PHE A 1 240 ? 1.669   -6.488  29.687 1.00 16.85 ? 247 PHE A CD1   1 
ATOM   1788 C  CD2   . PHE A 1 240 ? 3.266   -5.912  28.018 1.00 15.49 ? 247 PHE A CD2   1 
ATOM   1789 C  CE1   . PHE A 1 240 ? 1.346   -5.158  29.842 1.00 18.74 ? 247 PHE A CE1   1 
ATOM   1790 C  CE2   . PHE A 1 240 ? 2.948   -4.581  28.172 1.00 17.07 ? 247 PHE A CE2   1 
ATOM   1791 C  CZ    . PHE A 1 240 ? 1.984   -4.203  29.083 1.00 15.98 ? 247 PHE A CZ    1 
ATOM   1792 N  N     . VAL A 1 241 ? 0.861   -7.828  25.988 1.00 13.31 ? 248 VAL A N     1 
ATOM   1793 C  CA    . VAL A 1 241 ? 0.651   -7.068  24.758 1.00 11.72 ? 248 VAL A CA    1 
ATOM   1794 C  C     . VAL A 1 241 ? 0.022   -5.741  25.159 1.00 15.65 ? 248 VAL A C     1 
ATOM   1795 O  O     . VAL A 1 241 ? -1.166  -5.691  25.500 1.00 18.54 ? 248 VAL A O     1 
ATOM   1796 C  CB    . VAL A 1 241 ? -0.238  -7.814  23.751 1.00 13.83 ? 248 VAL A CB    1 
ATOM   1797 C  CG1   . VAL A 1 241 ? -0.486  -6.961  22.508 1.00 13.49 ? 248 VAL A CG1   1 
ATOM   1798 C  CG2   . VAL A 1 241 ? 0.381   -9.150  23.373 1.00 13.84 ? 248 VAL A CG2   1 
ATOM   1799 N  N     . ALA A 1 242 ? 0.813   -4.670  25.128 1.00 15.61 ? 249 ALA A N     1 
ATOM   1800 C  CA    . ALA A 1 242 ? 0.324   -3.345  25.489 1.00 14.46 ? 249 ALA A CA    1 
ATOM   1801 C  C     . ALA A 1 242 ? -0.401  -2.721  24.308 1.00 15.68 ? 249 ALA A C     1 
ATOM   1802 O  O     . ALA A 1 242 ? 0.121   -2.698  23.190 1.00 18.92 ? 249 ALA A O     1 
ATOM   1803 C  CB    . ALA A 1 242 ? 1.478   -2.447  25.927 1.00 20.24 ? 249 ALA A CB    1 
ATOM   1804 N  N     . GLU A 1 243 ? -1.600  -2.202  24.556 1.00 15.57 ? 250 GLU A N     1 
ATOM   1805 C  CA    . GLU A 1 243 ? -2.442  -1.629  23.508 1.00 15.99 ? 250 GLU A CA    1 
ATOM   1806 C  C     . GLU A 1 243 ? -2.934  -0.262  23.959 1.00 19.31 ? 250 GLU A C     1 
ATOM   1807 O  O     . GLU A 1 243 ? -4.082  -0.116  24.400 1.00 17.15 ? 250 GLU A O     1 
ATOM   1808 C  CB    . GLU A 1 243 ? -3.605  -2.564  23.171 1.00 17.66 ? 250 GLU A CB    1 
ATOM   1809 C  CG    . GLU A 1 243 ? -3.180  -3.771  22.350 1.00 17.78 ? 250 GLU A CG    1 
ATOM   1810 C  CD    . GLU A 1 243 ? -4.299  -4.330  21.496 1.00 18.23 ? 250 GLU A CD    1 
ATOM   1811 O  OE1   . GLU A 1 243 ? -5.169  -3.547  21.062 1.00 18.76 ? 250 GLU A OE1   1 
ATOM   1812 O  OE2   . GLU A 1 243 ? -4.306  -5.555  21.256 1.00 19.81 ? 250 GLU A OE2   1 
ATOM   1813 N  N     . PRO A 1 244 ? -2.085  0.763   23.875 1.00 18.49 ? 251 PRO A N     1 
ATOM   1814 C  CA    . PRO A 1 244 ? -2.549  2.125   24.158 1.00 20.19 ? 251 PRO A CA    1 
ATOM   1815 C  C     . PRO A 1 244 ? -3.574  2.567   23.126 1.00 17.44 ? 251 PRO A C     1 
ATOM   1816 O  O     . PRO A 1 244 ? -3.860  1.870   22.148 1.00 19.66 ? 251 PRO A O     1 
ATOM   1817 C  CB    . PRO A 1 244 ? -1.271  2.966   24.079 1.00 14.85 ? 251 PRO A CB    1 
ATOM   1818 C  CG    . PRO A 1 244 ? -0.345  2.176   23.237 1.00 15.17 ? 251 PRO A CG    1 
ATOM   1819 C  CD    . PRO A 1 244 ? -0.659  0.731   23.506 1.00 16.50 ? 251 PRO A CD    1 
ATOM   1820 N  N     . ASN A 1 245 ? -4.126  3.764   23.354 1.00 16.78 ? 252 ASN A N     1 
ATOM   1821 C  CA    . ASN A 1 245 ? -5.170  4.296   22.481 1.00 17.14 ? 252 ASN A CA    1 
ATOM   1822 C  C     . ASN A 1 245 ? -4.705  4.371   21.032 1.00 17.16 ? 252 ASN A C     1 
ATOM   1823 O  O     . ASN A 1 245 ? -5.396  3.899   20.121 1.00 20.74 ? 252 ASN A O     1 
ATOM   1824 C  CB    . ASN A 1 245 ? -5.609  5.675   22.975 1.00 20.28 ? 252 ASN A CB    1 
ATOM   1825 C  CG    . ASN A 1 245 ? -6.567  5.601   24.144 1.00 18.85 ? 252 ASN A CG    1 
ATOM   1826 O  OD1   . ASN A 1 245 ? -6.949  4.520   24.590 1.00 19.46 ? 252 ASN A OD1   1 
ATOM   1827 N  ND2   . ASN A 1 245 ? -6.987  6.762   24.628 1.00 20.15 ? 252 ASN A ND2   1 
ATOM   1828 N  N     . ARG A 1 246 ? -3.524  4.949   20.802 1.00 15.37 ? 253 ARG A N     1 
ATOM   1829 C  CA    . ARG A 1 246 ? -3.014  5.110   19.445 1.00 16.92 ? 253 ARG A CA    1 
ATOM   1830 C  C     . ARG A 1 246 ? -2.841  3.781   18.722 1.00 16.97 ? 253 ARG A C     1 
ATOM   1831 O  O     . ARG A 1 246 ? -2.825  3.761   17.487 1.00 19.81 ? 253 ARG A O     1 
ATOM   1832 C  CB    . ARG A 1 246 ? -1.681  5.855   19.477 1.00 13.51 ? 253 ARG A CB    1 
ATOM   1833 C  CG    . ARG A 1 246 ? -0.519  4.973   19.877 1.00 16.40 ? 253 ARG A CG    1 
ATOM   1834 C  CD    . ARG A 1 246 ? 0.802   5.705   19.833 1.00 25.56 ? 253 ARG A CD    1 
ATOM   1835 N  NE    . ARG A 1 246 ? 1.894   4.820   20.216 1.00 29.57 ? 253 ARG A NE    1 
ATOM   1836 C  CZ    . ARG A 1 246 ? 2.461   3.941   19.402 1.00 32.79 ? 253 ARG A CZ    1 
ATOM   1837 N  NH1   . ARG A 1 246 ? 2.082   3.824   18.139 1.00 28.54 ? 253 ARG A NH1   1 
ATOM   1838 N  NH2   . ARG A 1 246 ? 3.430   3.157   19.866 1.00 34.57 ? 253 ARG A NH2   1 
ATOM   1839 N  N     . LEU A 1 247 ? -2.709  2.675   19.454 1.00 17.38 ? 254 LEU A N     1 
ATOM   1840 C  CA    . LEU A 1 247 ? -2.583  1.358   18.848 1.00 16.07 ? 254 LEU A CA    1 
ATOM   1841 C  C     . LEU A 1 247 ? -3.913  0.625   18.740 1.00 21.42 ? 254 LEU A C     1 
ATOM   1842 O  O     . LEU A 1 247 ? -3.962  -0.451  18.137 1.00 23.52 ? 254 LEU A O     1 
ATOM   1843 C  CB    . LEU A 1 247 ? -1.595  0.500   19.647 1.00 16.49 ? 254 LEU A CB    1 
ATOM   1844 C  CG    . LEU A 1 247 ? -0.104  0.685   19.351 1.00 19.42 ? 254 LEU A CG    1 
ATOM   1845 C  CD1   . LEU A 1 247 ? 0.688   -0.509  19.853 1.00 23.32 ? 254 LEU A CD1   1 
ATOM   1846 C  CD2   . LEU A 1 247 ? 0.138   0.900   17.866 1.00 23.00 ? 254 LEU A CD2   1 
ATOM   1847 N  N     . MET A 1 248 ? -4.986  1.175   19.310 1.00 18.20 ? 255 MET A N     1 
ATOM   1848 C  CA    . MET A 1 248 ? -6.298  0.546   19.275 1.00 22.30 ? 255 MET A CA    1 
ATOM   1849 C  C     . MET A 1 248 ? -7.300  1.235   18.362 1.00 23.74 ? 255 MET A C     1 
ATOM   1850 O  O     . MET A 1 248 ? -8.299  0.611   17.991 1.00 22.67 ? 255 MET A O     1 
ATOM   1851 C  CB    . MET A 1 248 ? -6.904  0.490   20.684 1.00 19.43 ? 255 MET A CB    1 
ATOM   1852 C  CG    . MET A 1 248 ? -7.566  -0.825  21.029 1.00 24.01 ? 255 MET A CG    1 
ATOM   1853 S  SD    . MET A 1 248 ? -7.760  -1.065  22.801 1.00 21.41 ? 255 MET A SD    1 
ATOM   1854 C  CE    . MET A 1 248 ? -9.146  -2.197  22.803 1.00 13.76 ? 255 MET A CE    1 
ATOM   1855 N  N     . ALA A 1 249 ? -7.059  2.496   17.995 1.00 19.29 ? 256 ALA A N     1 
ATOM   1856 C  CA    . ALA A 1 249 ? -8.075  3.290   17.310 1.00 22.63 ? 256 ALA A CA    1 
ATOM   1857 C  C     . ALA A 1 249 ? -8.413  2.725   15.934 1.00 24.21 ? 256 ALA A C     1 
ATOM   1858 O  O     . ALA A 1 249 ? -9.591  2.647   15.566 1.00 23.74 ? 256 ALA A O     1 
ATOM   1859 C  CB    . ALA A 1 249 ? -7.608  4.740   17.196 1.00 20.43 ? 256 ALA A CB    1 
ATOM   1860 N  N     . SER A 1 250 ? -7.400  2.326   15.153 1.00 22.15 ? 257 SER A N     1 
ATOM   1861 C  CA    . SER A 1 250 ? -7.659  1.881   13.787 1.00 23.27 ? 257 SER A CA    1 
ATOM   1862 C  C     . SER A 1 250 ? -6.883  0.622   13.409 1.00 23.72 ? 257 SER A C     1 
ATOM   1863 O  O     . SER A 1 250 ? -6.718  0.347   12.214 1.00 24.52 ? 257 SER A O     1 
ATOM   1864 C  CB    . SER A 1 250 ? -7.324  2.986   12.779 1.00 24.50 ? 257 SER A CB    1 
ATOM   1865 O  OG    . SER A 1 250 ? -7.778  4.250   13.227 1.00 27.42 ? 257 SER A OG    1 
ATOM   1866 N  N     . SER A 1 251 ? -6.409  -0.151  14.383 1.00 24.15 ? 258 SER A N     1 
ATOM   1867 C  CA    . SER A 1 251 ? -5.621  -1.347  14.114 1.00 25.55 ? 258 SER A CA    1 
ATOM   1868 C  C     . SER A 1 251 ? -6.472  -2.595  13.928 1.00 23.82 ? 258 SER A C     1 
ATOM   1869 O  O     . SER A 1 251 ? -5.917  -3.686  13.766 1.00 24.15 ? 258 SER A O     1 
ATOM   1870 C  CB    . SER A 1 251 ? -4.616  -1.586  15.248 1.00 25.70 ? 258 SER A CB    1 
ATOM   1871 O  OG    . SER A 1 251 ? -5.268  -1.721  16.501 1.00 24.76 ? 258 SER A OG    1 
ATOM   1872 N  N     . TYR A 1 252 ? -7.795  -2.466  13.940 1.00 23.45 ? 259 TYR A N     1 
ATOM   1873 C  CA    . TYR A 1 252 ? -8.685  -3.615  13.943 1.00 23.53 ? 259 TYR A CA    1 
ATOM   1874 C  C     . TYR A 1 252 ? -9.599  -3.606  12.728 1.00 22.59 ? 259 TYR A C     1 
ATOM   1875 O  O     . TYR A 1 252 ? -9.903  -2.553  12.159 1.00 22.37 ? 259 TYR A O     1 
ATOM   1876 C  CB    . TYR A 1 252 ? -9.539  -3.654  15.213 1.00 19.90 ? 259 TYR A CB    1 
ATOM   1877 C  CG    . TYR A 1 252 ? -8.804  -4.181  16.419 1.00 19.15 ? 259 TYR A CG    1 
ATOM   1878 C  CD1   . TYR A 1 252 ? -7.955  -3.362  17.148 1.00 20.98 ? 259 TYR A CD1   1 
ATOM   1879 C  CD2   . TYR A 1 252 ? -8.952  -5.501  16.826 1.00 18.89 ? 259 TYR A CD2   1 
ATOM   1880 C  CE1   . TYR A 1 252 ? -7.279  -3.838  18.252 1.00 25.13 ? 259 TYR A CE1   1 
ATOM   1881 C  CE2   . TYR A 1 252 ? -8.279  -5.989  17.931 1.00 19.56 ? 259 TYR A CE2   1 
ATOM   1882 C  CZ    . TYR A 1 252 ? -7.443  -5.151  18.640 1.00 21.84 ? 259 TYR A CZ    1 
ATOM   1883 O  OH    . TYR A 1 252 ? -6.765  -5.620  19.741 1.00 20.78 ? 259 TYR A OH    1 
ATOM   1884 N  N     . LEU A 1 253 ? -10.040 -4.801  12.349 1.00 21.80 ? 260 LEU A N     1 
ATOM   1885 C  CA    . LEU A 1 253 ? -11.023 -4.990  11.288 1.00 17.85 ? 260 LEU A CA    1 
ATOM   1886 C  C     . LEU A 1 253 ? -12.339 -5.364  11.956 1.00 18.10 ? 260 LEU A C     1 
ATOM   1887 O  O     . LEU A 1 253 ? -12.526 -6.501  12.395 1.00 16.67 ? 260 LEU A O     1 
ATOM   1888 C  CB    . LEU A 1 253 ? -10.561 -6.053  10.299 1.00 22.49 ? 260 LEU A CB    1 
ATOM   1889 C  CG    . LEU A 1 253 ? -9.541  -5.483  9.318  1.00 24.73 ? 260 LEU A CG    1 
ATOM   1890 C  CD1   . LEU A 1 253 ? -8.738  -6.565  8.609  1.00 22.25 ? 260 LEU A CD1   1 
ATOM   1891 C  CD2   . LEU A 1 253 ? -10.260 -4.578  8.344  1.00 23.95 ? 260 LEU A CD2   1 
ATOM   1892 N  N     . LEU A 1 254 ? -13.250 -4.401  12.033 1.00 18.45 ? 261 LEU A N     1 
ATOM   1893 C  CA    . LEU A 1 254 ? -14.467 -4.526  12.823 1.00 19.75 ? 261 LEU A CA    1 
ATOM   1894 C  C     . LEU A 1 254 ? -15.637 -4.861  11.906 1.00 22.18 ? 261 LEU A C     1 
ATOM   1895 O  O     . LEU A 1 254 ? -15.938 -4.100  10.980 1.00 26.34 ? 261 LEU A O     1 
ATOM   1896 C  CB    . LEU A 1 254 ? -14.735 -3.227  13.581 1.00 21.52 ? 261 LEU A CB    1 
ATOM   1897 C  CG    . LEU A 1 254 ? -13.811 -2.940  14.761 1.00 19.66 ? 261 LEU A CG    1 
ATOM   1898 C  CD1   . LEU A 1 254 ? -12.971 -1.701  14.490 1.00 21.63 ? 261 LEU A CD1   1 
ATOM   1899 C  CD2   . LEU A 1 254 ? -14.640 -2.762  16.009 1.00 22.22 ? 261 LEU A CD2   1 
ATOM   1900 N  N     . VAL A 1 255 ? -16.299 -5.985  12.167 1.00 25.44 ? 262 VAL A N     1 
ATOM   1901 C  CA    . VAL A 1 255 ? -17.425 -6.441  11.356 1.00 23.89 ? 262 VAL A CA    1 
ATOM   1902 C  C     . VAL A 1 255 ? -18.694 -6.382  12.200 1.00 20.85 ? 262 VAL A C     1 
ATOM   1903 O  O     . VAL A 1 255 ? -18.770 -6.986  13.279 1.00 22.65 ? 262 VAL A O     1 
ATOM   1904 C  CB    . VAL A 1 255 ? -17.181 -7.845  10.784 1.00 21.26 ? 262 VAL A CB    1 
ATOM   1905 C  CG1   . VAL A 1 255 ? -18.483 -8.470  10.343 1.00 19.29 ? 262 VAL A CG1   1 
ATOM   1906 C  CG2   . VAL A 1 255 ? -16.239 -7.755  9.595  1.00 18.32 ? 262 VAL A CG2   1 
ATOM   1907 N  N     . ASP A 1 256 ? -19.689 -5.661  11.685 1.00 23.06 ? 263 ASP A N     1 
ATOM   1908 C  CA    . ASP A 1 256 ? -20.917 -5.294  12.373 1.00 23.97 ? 263 ASP A CA    1 
ATOM   1909 C  C     . ASP A 1 256 ? -21.855 -6.500  12.514 1.00 23.31 ? 263 ASP A C     1 
ATOM   1910 O  O     . ASP A 1 256 ? -21.607 -7.589  11.984 1.00 22.62 ? 263 ASP A O     1 
ATOM   1911 C  CB    . ASP A 1 256 ? -21.569 -4.139  11.608 1.00 23.88 ? 263 ASP A CB    1 
ATOM   1912 C  CG    . ASP A 1 256 ? -22.769 -3.567  12.300 1.00 29.11 ? 263 ASP A CG    1 
ATOM   1913 O  OD1   . ASP A 1 256 ? -23.817 -4.243  12.286 1.00 36.42 ? 263 ASP A OD1   1 
ATOM   1914 O  OD2   . ASP A 1 256 ? -22.692 -2.419  12.781 1.00 37.06 ? 263 ASP A OD2   1 
ATOM   1915 N  N     . GLU A 1 257 ? -22.942 -6.305  13.272 1.00 21.60 ? 264 GLU A N     1 
ATOM   1916 C  CA    . GLU A 1 257 ? -23.948 -7.353  13.404 1.00 24.90 ? 264 GLU A CA    1 
ATOM   1917 C  C     . GLU A 1 257 ? -24.702 -7.592  12.101 1.00 25.33 ? 264 GLU A C     1 
ATOM   1918 O  O     . GLU A 1 257 ? -25.312 -8.654  11.944 1.00 24.86 ? 264 GLU A O     1 
ATOM   1919 C  CB    . GLU A 1 257 ? -24.934 -7.025  14.534 1.00 20.15 ? 264 GLU A CB    1 
ATOM   1920 C  CG    . GLU A 1 257 ? -25.876 -5.864  14.255 1.00 30.39 ? 264 GLU A CG    1 
ATOM   1921 C  CD    . GLU A 1 257 ? -25.294 -4.525  14.663 1.00 29.10 ? 264 GLU A CD    1 
ATOM   1922 O  OE1   . GLU A 1 257 ? -24.166 -4.504  15.199 1.00 24.41 ? 264 GLU A OE1   1 
ATOM   1923 O  OE2   . GLU A 1 257 ? -25.951 -3.491  14.422 1.00 34.21 ? 264 GLU A OE2   1 
ATOM   1924 N  N     . TYR A 1 258 ? -24.681 -6.631  11.177 1.00 25.80 ? 265 TYR A N     1 
ATOM   1925 C  CA    . TYR A 1 258 ? -25.131 -6.829  9.804  1.00 25.67 ? 265 TYR A CA    1 
ATOM   1926 C  C     . TYR A 1 258 ? -23.988 -7.221  8.880  1.00 25.60 ? 265 TYR A C     1 
ATOM   1927 O  O     . TYR A 1 258 ? -24.174 -7.264  7.658  1.00 23.16 ? 265 TYR A O     1 
ATOM   1928 C  CB    . TYR A 1 258 ? -25.807 -5.562  9.275  1.00 25.96 ? 265 TYR A CB    1 
ATOM   1929 C  CG    . TYR A 1 258 ? -27.087 -5.199  9.989  1.00 27.92 ? 265 TYR A CG    1 
ATOM   1930 C  CD1   . TYR A 1 258 ? -27.062 -4.505  11.190 1.00 30.42 ? 265 TYR A CD1   1 
ATOM   1931 C  CD2   . TYR A 1 258 ? -28.321 -5.546  9.457  1.00 29.97 ? 265 TYR A CD2   1 
ATOM   1932 C  CE1   . TYR A 1 258 ? -28.233 -4.171  11.846 1.00 31.90 ? 265 TYR A CE1   1 
ATOM   1933 C  CE2   . TYR A 1 258 ? -29.495 -5.215  10.102 1.00 33.45 ? 265 TYR A CE2   1 
ATOM   1934 C  CZ    . TYR A 1 258 ? -29.447 -4.528  11.296 1.00 32.11 ? 265 TYR A CZ    1 
ATOM   1935 O  OH    . TYR A 1 258 ? -30.618 -4.199  11.941 1.00 32.01 ? 265 TYR A OH    1 
ATOM   1936 N  N     . MET A 1 259 ? -22.826 -7.488  9.430  1.00 25.08 ? 266 MET A N     1 
ATOM   1937 C  CA    . MET A 1 259 ? -21.632 -7.796  8.666  1.00 19.69 ? 266 MET A CA    1 
ATOM   1938 C  C     . MET A 1 259 ? -21.148 -6.594  7.866  1.00 24.00 ? 266 MET A C     1 
ATOM   1939 O  O     . MET A 1 259 ? -20.585 -6.753  6.804  1.00 26.00 ? 266 MET A O     1 
ATOM   1940 C  CB    . MET A 1 259 ? -21.754 -9.111  7.902  1.00 24.95 ? 266 MET A CB    1 
ATOM   1941 C  CG    . MET A 1 259 ? -21.780 -10.329 8.789  1.00 23.64 ? 266 MET A CG    1 
ATOM   1942 S  SD    . MET A 1 259 ? -21.593 -11.830 7.837  1.00 27.73 ? 266 MET A SD    1 
ATOM   1943 C  CE    . MET A 1 259 ? -20.102 -12.484 8.563  1.00 20.67 ? 266 MET A CE    1 
ATOM   1944 N  N     . ARG A 1 260 ? -21.418 -5.397  8.354  1.00 23.04 ? 267 ARG A N     1 
ATOM   1945 C  CA    . ARG A 1 260 ? -20.835 -4.177  7.823  1.00 23.47 ? 267 ARG A CA    1 
ATOM   1946 C  C     . ARG A 1 260 ? -19.508 -3.903  8.522  1.00 24.50 ? 267 ARG A C     1 
ATOM   1947 O  O     . ARG A 1 260 ? -19.233 -4.423  9.605  1.00 21.74 ? 267 ARG A O     1 
ATOM   1948 C  CB    . ARG A 1 260 ? -21.789 -2.994  8.008  1.00 23.75 ? 267 ARG A CB    1 
ATOM   1949 C  CG    . ARG A 1 260 ? -23.197 -3.243  7.491  1.00 19.69 ? 267 ARG A CG    1 
ATOM   1950 C  CD    . ARG A 1 260 ? -24.168 -2.156  7.930  1.00 20.53 ? 267 ARG A CD    1 
ATOM   1951 N  NE    . ARG A 1 260 ? -24.327 -2.105  9.378  1.00 28.21 ? 267 ARG A NE    1 
ATOM   1952 C  CZ    . ARG A 1 260 ? -25.256 -1.397  10.006 1.00 29.86 ? 267 ARG A CZ    1 
ATOM   1953 N  NH1   . ARG A 1 260 ? -26.139 -0.669  9.341  1.00 34.05 ? 267 ARG A NH1   1 
ATOM   1954 N  NH2   . ARG A 1 260 ? -25.300 -1.418  11.335 1.00 30.87 ? 267 ARG A NH2   1 
ATOM   1955 N  N     . PHE A 1 261 ? -18.673 -3.090  7.884  1.00 23.68 ? 268 PHE A N     1 
ATOM   1956 C  CA    . PHE A 1 261 ? -17.387 -2.725  8.460  1.00 22.52 ? 268 PHE A CA    1 
ATOM   1957 C  C     . PHE A 1 261 ? -17.529 -1.419  9.231  1.00 24.60 ? 268 PHE A C     1 
ATOM   1958 O  O     . PHE A 1 261 ? -18.087 -0.445  8.716  1.00 25.14 ? 268 PHE A O     1 
ATOM   1959 C  CB    . PHE A 1 261 ? -16.319 -2.587  7.374  1.00 25.50 ? 268 PHE A CB    1 
ATOM   1960 C  CG    . PHE A 1 261 ? -15.543 -3.847  7.116  1.00 27.60 ? 268 PHE A CG    1 
ATOM   1961 C  CD1   . PHE A 1 261 ? -14.575 -4.279  8.008  1.00 26.12 ? 268 PHE A CD1   1 
ATOM   1962 C  CD2   . PHE A 1 261 ? -15.774 -4.594  5.972  1.00 29.70 ? 268 PHE A CD2   1 
ATOM   1963 C  CE1   . PHE A 1 261 ? -13.859 -5.437  7.767  1.00 27.11 ? 268 PHE A CE1   1 
ATOM   1964 C  CE2   . PHE A 1 261 ? -15.062 -5.753  5.725  1.00 21.89 ? 268 PHE A CE2   1 
ATOM   1965 C  CZ    . PHE A 1 261 ? -14.103 -6.175  6.623  1.00 28.95 ? 268 PHE A CZ    1 
ATOM   1966 N  N     . ILE A 1 262 ? -17.030 -1.406  10.466 1.00 24.58 ? 269 ILE A N     1 
ATOM   1967 C  CA    . ILE A 1 262 ? -17.096 -0.234  11.331 1.00 18.80 ? 269 ILE A CA    1 
ATOM   1968 C  C     . ILE A 1 262 ? -15.737 0.448   11.355 1.00 23.77 ? 269 ILE A C     1 
ATOM   1969 O  O     . ILE A 1 262 ? -14.709 -0.203  11.584 1.00 26.58 ? 269 ILE A O     1 
ATOM   1970 C  CB    . ILE A 1 262 ? -17.533 -0.608  12.758 1.00 16.91 ? 269 ILE A CB    1 
ATOM   1971 C  CG1   . ILE A 1 262 ? -18.587 -1.715  12.737 1.00 25.02 ? 269 ILE A CG1   1 
ATOM   1972 C  CG2   . ILE A 1 262 ? -18.062 0.619   13.488 1.00 26.34 ? 269 ILE A CG2   1 
ATOM   1973 C  CD1   . ILE A 1 262 ? -18.886 -2.281  14.111 1.00 25.09 ? 269 ILE A CD1   1 
ATOM   1974 N  N     . ASP A 1 263 ? -15.731 1.757   11.124 1.00 27.79 ? 270 ASP A N     1 
ATOM   1975 C  CA    . ASP A 1 263 ? -14.561 2.605   11.339 1.00 26.83 ? 270 ASP A CA    1 
ATOM   1976 C  C     . ASP A 1 263 ? -14.847 3.412   12.603 1.00 23.78 ? 270 ASP A C     1 
ATOM   1977 O  O     . ASP A 1 263 ? -15.358 4.532   12.544 1.00 25.83 ? 270 ASP A O     1 
ATOM   1978 C  CB    . ASP A 1 263 ? -14.283 3.503   10.135 1.00 25.33 ? 270 ASP A CB    1 
ATOM   1979 C  CG    . ASP A 1 263 ? -12.919 4.174   10.204 1.00 29.07 ? 270 ASP A CG    1 
ATOM   1980 O  OD1   . ASP A 1 263 ? -12.533 4.655   11.292 1.00 26.81 ? 270 ASP A OD1   1 
ATOM   1981 O  OD2   . ASP A 1 263 ? -12.234 4.223   9.162  1.00 31.35 ? 270 ASP A OD2   1 
ATOM   1982 N  N     . LYS A 1 264 ? -14.515 2.826   13.754 1.00 22.99 ? 271 LYS A N     1 
ATOM   1983 C  CA    . LYS A 1 264 ? -14.805 3.466   15.030 1.00 24.17 ? 271 LYS A CA    1 
ATOM   1984 C  C     . LYS A 1 264 ? -13.931 4.687   15.282 1.00 23.31 ? 271 LYS A C     1 
ATOM   1985 O  O     . LYS A 1 264 ? -14.322 5.562   16.062 1.00 21.83 ? 271 LYS A O     1 
ATOM   1986 C  CB    . LYS A 1 264 ? -14.646 2.451   16.163 1.00 19.60 ? 271 LYS A CB    1 
ATOM   1987 C  CG    . LYS A 1 264 ? -15.799 1.460   16.249 1.00 15.59 ? 271 LYS A CG    1 
ATOM   1988 C  CD    . LYS A 1 264 ? -15.933 0.869   17.642 1.00 18.05 ? 271 LYS A CD    1 
ATOM   1989 C  CE    . LYS A 1 264 ? -16.845 -0.345  17.644 1.00 16.23 ? 271 LYS A CE    1 
ATOM   1990 N  NZ    . LYS A 1 264 ? -16.538 -1.248  18.788 1.00 18.92 ? 271 LYS A NZ    1 
ATOM   1991 N  N     . ASP A 1 265 ? -12.766 4.773   14.637 1.00 23.94 ? 272 ASP A N     1 
ATOM   1992 C  CA    . ASP A 1 265 ? -11.922 5.951   14.799 1.00 23.37 ? 272 ASP A CA    1 
ATOM   1993 C  C     . ASP A 1 265 ? -12.506 7.154   14.067 1.00 26.84 ? 272 ASP A C     1 
ATOM   1994 O  O     . ASP A 1 265 ? -12.434 8.284   14.563 1.00 23.04 ? 272 ASP A O     1 
ATOM   1995 C  CB    . ASP A 1 265 ? -10.507 5.654   14.302 1.00 28.65 ? 272 ASP A CB    1 
ATOM   1996 C  CG    . ASP A 1 265 ? -9.620  6.880   14.311 1.00 28.83 ? 272 ASP A CG    1 
ATOM   1997 O  OD1   . ASP A 1 265 ? -9.195  7.295   15.410 1.00 27.42 ? 272 ASP A OD1   1 
ATOM   1998 O  OD2   . ASP A 1 265 ? -9.350  7.429   13.222 1.00 30.22 ? 272 ASP A OD2   1 
ATOM   1999 N  N     . GLY A 1 266 ? -13.089 6.929   12.893 1.00 27.39 ? 273 GLY A N     1 
ATOM   2000 C  CA    . GLY A 1 266 ? -13.703 7.973   12.100 1.00 29.91 ? 273 GLY A CA    1 
ATOM   2001 C  C     . GLY A 1 266 ? -15.215 8.024   12.143 1.00 31.41 ? 273 GLY A C     1 
ATOM   2002 O  O     . GLY A 1 266 ? -15.806 8.854   11.444 1.00 34.60 ? 273 GLY A O     1 
ATOM   2003 N  N     . ASN A 1 267 ? -15.858 7.166   12.935 1.00 28.16 ? 274 ASN A N     1 
ATOM   2004 C  CA    . ASN A 1 267 ? -17.313 7.148   13.096 1.00 27.23 ? 274 ASN A CA    1 
ATOM   2005 C  C     . ASN A 1 267 ? -18.016 7.014   11.747 1.00 30.97 ? 274 ASN A C     1 
ATOM   2006 O  O     . ASN A 1 267 ? -18.852 7.830   11.358 1.00 37.04 ? 274 ASN A O     1 
ATOM   2007 C  CB    . ASN A 1 267 ? -17.800 8.392   13.841 1.00 29.89 ? 274 ASN A CB    1 
ATOM   2008 C  CG    . ASN A 1 267 ? -19.142 8.177   14.510 1.00 32.77 ? 274 ASN A CG    1 
ATOM   2009 O  OD1   . ASN A 1 267 ? -19.657 7.059   14.544 1.00 27.93 ? 274 ASN A OD1   1 
ATOM   2010 N  ND2   . ASN A 1 267 ? -19.722 9.249   15.034 1.00 29.46 ? 274 ASN A ND2   1 
ATOM   2011 N  N     . LYS A 1 268 ? -17.654 5.954   11.034 1.00 31.75 ? 275 LYS A N     1 
ATOM   2012 C  CA    . LYS A 1 268 ? -18.195 5.680   9.715  1.00 24.75 ? 275 LYS A CA    1 
ATOM   2013 C  C     . LYS A 1 268 ? -18.633 4.224   9.649  1.00 27.40 ? 275 LYS A C     1 
ATOM   2014 O  O     . LYS A 1 268 ? -18.208 3.387   10.449 1.00 26.72 ? 275 LYS A O     1 
ATOM   2015 C  CB    . LYS A 1 268 ? -17.172 5.989   8.616  1.00 25.23 ? 275 LYS A CB    1 
ATOM   2016 C  CG    . LYS A 1 268 ? -16.906 7.481   8.434  1.00 32.13 ? 275 LYS A CG    1 
ATOM   2017 C  CD    . LYS A 1 268 ? -18.146 8.221   7.926  1.00 33.85 ? 275 LYS A CD    1 
ATOM   2018 C  CE    . LYS A 1 268 ? -18.084 8.451   6.419  1.00 43.56 ? 275 LYS A CE    1 
ATOM   2019 N  NZ    . LYS A 1 268 ? -19.361 8.100   5.729  1.00 36.57 ? 275 LYS A NZ    1 
ATOM   2020 N  N     . LEU A 1 269 ? -19.495 3.936   8.676  1.00 25.14 ? 276 LEU A N     1 
ATOM   2021 C  CA    . LEU A 1 269 ? -20.121 2.628   8.553  1.00 23.83 ? 276 LEU A CA    1 
ATOM   2022 C  C     . LEU A 1 269 ? -20.307 2.304   7.079  1.00 27.47 ? 276 LEU A C     1 
ATOM   2023 O  O     . LEU A 1 269 ? -20.751 3.161   6.310  1.00 30.64 ? 276 LEU A O     1 
ATOM   2024 C  CB    . LEU A 1 269 ? -21.468 2.611   9.279  1.00 23.83 ? 276 LEU A CB    1 
ATOM   2025 C  CG    . LEU A 1 269 ? -22.069 1.270   9.680  1.00 28.53 ? 276 LEU A CG    1 
ATOM   2026 C  CD1   . LEU A 1 269 ? -21.087 0.465   10.513 1.00 25.71 ? 276 LEU A CD1   1 
ATOM   2027 C  CD2   . LEU A 1 269 ? -23.355 1.522   10.438 1.00 24.81 ? 276 LEU A CD2   1 
ATOM   2028 N  N     . THR A 1 270 ? -19.969 1.077   6.691  1.00 25.26 ? 277 THR A N     1 
ATOM   2029 C  CA    . THR A 1 270 ? -20.096 0.628   5.311  1.00 29.59 ? 277 THR A CA    1 
ATOM   2030 C  C     . THR A 1 270 ? -21.404 -0.124  5.104  1.00 25.87 ? 277 THR A C     1 
ATOM   2031 O  O     . THR A 1 270 ? -22.155 -0.400  6.042  1.00 26.11 ? 277 THR A O     1 
ATOM   2032 C  CB    . THR A 1 270 ? -18.926 -0.279  4.912  1.00 28.94 ? 277 THR A CB    1 
ATOM   2033 O  OG1   . THR A 1 270 ? -19.158 -1.607  5.399  1.00 27.92 ? 277 THR A OG1   1 
ATOM   2034 C  CG2   . THR A 1 270 ? -17.633 0.234   5.485  1.00 29.37 ? 277 THR A CG2   1 
ATOM   2035 N  N     . LYS A 1 271 ? -21.668 -0.462  3.845  1.00 24.46 ? 278 LYS A N     1 
ATOM   2036 C  CA    . LYS A 1 271 ? -22.712 -1.426  3.549  1.00 23.24 ? 278 LYS A CA    1 
ATOM   2037 C  C     . LYS A 1 271 ? -22.229 -2.827  3.909  1.00 21.54 ? 278 LYS A C     1 
ATOM   2038 O  O     . LYS A 1 271 ? -21.029 -3.086  4.034  1.00 25.04 ? 278 LYS A O     1 
ATOM   2039 C  CB    . LYS A 1 271 ? -23.107 -1.364  2.074  1.00 28.33 ? 278 LYS A CB    1 
ATOM   2040 C  CG    . LYS A 1 271 ? -23.337 0.040   1.550  1.00 28.90 ? 278 LYS A CG    1 
ATOM   2041 C  CD    . LYS A 1 271 ? -24.796 0.436   1.677  1.00 24.35 ? 278 LYS A CD    1 
ATOM   2042 C  CE    . LYS A 1 271 ? -25.161 1.523   0.681  1.00 25.49 ? 278 LYS A CE    1 
ATOM   2043 N  NZ    . LYS A 1 271 ? -26.533 2.049   0.921  1.00 34.03 ? 278 LYS A NZ    1 
ATOM   2044 N  N     . SER A 1 272 ? -23.183 -3.736  4.091  1.00 21.45 ? 279 SER A N     1 
ATOM   2045 C  CA    . SER A 1 272 ? -22.831 -5.109  4.424  1.00 20.34 ? 279 SER A CA    1 
ATOM   2046 C  C     . SER A 1 272 ? -22.051 -5.750  3.285  1.00 27.95 ? 279 SER A C     1 
ATOM   2047 O  O     . SER A 1 272 ? -22.348 -5.529  2.107  1.00 28.38 ? 279 SER A O     1 
ATOM   2048 C  CB    . SER A 1 272 ? -24.087 -5.926  4.719  1.00 20.80 ? 279 SER A CB    1 
ATOM   2049 O  OG    . SER A 1 272 ? -23.783 -7.309  4.762  1.00 23.38 ? 279 SER A OG    1 
ATOM   2050 N  N     . ILE A 1 273 ? -21.044 -6.551  3.643  1.00 25.52 ? 280 ILE A N     1 
ATOM   2051 C  CA    . ILE A 1 273 ? -20.278 -7.277  2.637  1.00 27.22 ? 280 ILE A CA    1 
ATOM   2052 C  C     . ILE A 1 273 ? -21.161 -8.239  1.860  1.00 26.43 ? 280 ILE A C     1 
ATOM   2053 O  O     . ILE A 1 273 ? -20.822 -8.624  0.737  1.00 29.36 ? 280 ILE A O     1 
ATOM   2054 C  CB    . ILE A 1 273 ? -19.098 -8.032  3.288  1.00 23.45 ? 280 ILE A CB    1 
ATOM   2055 C  CG1   . ILE A 1 273 ? -19.612 -9.210  4.122  1.00 24.48 ? 280 ILE A CG1   1 
ATOM   2056 C  CG2   . ILE A 1 273 ? -18.258 -7.083  4.130  1.00 26.15 ? 280 ILE A CG2   1 
ATOM   2057 C  CD1   . ILE A 1 273 ? -18.535 -9.941  4.897  1.00 26.12 ? 280 ILE A CD1   1 
ATOM   2058 N  N     . LEU A 1 274 ? -22.300 -8.635  2.433  1.00 28.48 ? 281 LEU A N     1 
ATOM   2059 C  CA    . LEU A 1 274 ? -23.191 -9.567  1.755  1.00 28.62 ? 281 LEU A CA    1 
ATOM   2060 C  C     . LEU A 1 274 ? -23.776 -8.964  0.484  1.00 26.97 ? 281 LEU A C     1 
ATOM   2061 O  O     . LEU A 1 274 ? -24.126 -9.699  -0.447 1.00 27.88 ? 281 LEU A O     1 
ATOM   2062 C  CB    . LEU A 1 274 ? -24.300 -10.000 2.714  1.00 24.71 ? 281 LEU A CB    1 
ATOM   2063 C  CG    . LEU A 1 274 ? -23.767 -10.592 4.020  1.00 27.83 ? 281 LEU A CG    1 
ATOM   2064 C  CD1   . LEU A 1 274 ? -24.880 -10.805 5.032  1.00 22.73 ? 281 LEU A CD1   1 
ATOM   2065 C  CD2   . LEU A 1 274 ? -23.037 -11.893 3.742  1.00 24.56 ? 281 LEU A CD2   1 
ATOM   2066 N  N     . ASP A 1 275 ? -23.879 -7.635  0.420  1.00 28.55 ? 282 ASP A N     1 
ATOM   2067 C  CA    . ASP A 1 275 ? -24.394 -6.944  -0.756 1.00 26.27 ? 282 ASP A CA    1 
ATOM   2068 C  C     . ASP A 1 275 ? -23.287 -6.392  -1.648 1.00 30.39 ? 282 ASP A C     1 
ATOM   2069 O  O     . ASP A 1 275 ? -23.260 -6.680  -2.848 1.00 30.83 ? 282 ASP A O     1 
ATOM   2070 C  CB    . ASP A 1 275 ? -25.335 -5.808  -0.330 1.00 24.34 ? 282 ASP A CB    1 
ATOM   2071 C  CG    . ASP A 1 275 ? -26.400 -6.267  0.647  1.00 27.38 ? 282 ASP A CG    1 
ATOM   2072 O  OD1   . ASP A 1 275 ? -27.214 -7.142  0.279  1.00 35.95 ? 282 ASP A OD1   1 
ATOM   2073 O  OD2   . ASP A 1 275 ? -26.430 -5.745  1.783  1.00 28.54 ? 282 ASP A OD2   1 
ATOM   2074 N  N     . VAL A 1 276 ? -22.359 -5.614  -1.085 1.00 29.56 ? 283 VAL A N     1 
ATOM   2075 C  CA    . VAL A 1 276 ? -21.346 -4.935  -1.890 1.00 27.24 ? 283 VAL A CA    1 
ATOM   2076 C  C     . VAL A 1 276 ? -20.028 -5.693  -1.966 1.00 30.07 ? 283 VAL A C     1 
ATOM   2077 O  O     . VAL A 1 276 ? -19.142 -5.289  -2.736 1.00 35.05 ? 283 VAL A O     1 
ATOM   2078 C  CB    . VAL A 1 276 ? -21.089 -3.501  -1.376 1.00 30.30 ? 283 VAL A CB    1 
ATOM   2079 C  CG1   . VAL A 1 276 ? -22.275 -2.601  -1.690 1.00 25.79 ? 283 VAL A CG1   1 
ATOM   2080 C  CG2   . VAL A 1 276 ? -20.797 -3.511  0.118  1.00 31.14 ? 283 VAL A CG2   1 
ATOM   2081 N  N     . GLY A 1 277 ? -19.864 -6.767  -1.200 1.00 30.15 ? 284 GLY A N     1 
ATOM   2082 C  CA    . GLY A 1 277 ? -18.645 -7.545  -1.238 1.00 28.81 ? 284 GLY A CA    1 
ATOM   2083 C  C     . GLY A 1 277 ? -17.584 -7.036  -0.277 1.00 32.86 ? 284 GLY A C     1 
ATOM   2084 O  O     . GLY A 1 277 ? -17.650 -5.925  0.256  1.00 35.33 ? 284 GLY A O     1 
ATOM   2085 N  N     . VAL A 1 278 ? -16.571 -7.879  -0.068 1.00 27.80 ? 285 VAL A N     1 
ATOM   2086 C  CA    . VAL A 1 278 ? -15.530 -7.566  0.906  1.00 28.59 ? 285 VAL A CA    1 
ATOM   2087 C  C     . VAL A 1 278 ? -14.681 -6.394  0.428  1.00 31.29 ? 285 VAL A C     1 
ATOM   2088 O  O     . VAL A 1 278 ? -14.550 -5.381  1.123  1.00 36.94 ? 285 VAL A O     1 
ATOM   2089 C  CB    . VAL A 1 278 ? -14.665 -8.807  1.185  1.00 29.50 ? 285 VAL A CB    1 
ATOM   2090 C  CG1   . VAL A 1 278 ? -13.421 -8.419  1.974  1.00 25.50 ? 285 VAL A CG1   1 
ATOM   2091 C  CG2   . VAL A 1 278 ? -15.470 -9.859  1.930  1.00 22.42 ? 285 VAL A CG2   1 
ATOM   2092 N  N     . GLU A 1 279 ? -14.100 -6.510  -0.770 1.00 31.27 ? 286 GLU A N     1 
ATOM   2093 C  CA    . GLU A 1 279 ? -13.094 -5.536  -1.187 1.00 33.38 ? 286 GLU A CA    1 
ATOM   2094 C  C     . GLU A 1 279 ? -13.688 -4.146  -1.379 1.00 31.78 ? 286 GLU A C     1 
ATOM   2095 O  O     . GLU A 1 279 ? -12.991 -3.149  -1.165 1.00 30.43 ? 286 GLU A O     1 
ATOM   2096 C  CB    . GLU A 1 279 ? -12.392 -6.002  -2.467 1.00 37.78 ? 286 GLU A CB    1 
ATOM   2097 N  N     . ALA A 1 280 ? -14.958 -4.052  -1.777 1.00 32.50 ? 287 ALA A N     1 
ATOM   2098 C  CA    . ALA A 1 280 ? -15.566 -2.738  -1.950 1.00 32.02 ? 287 ALA A CA    1 
ATOM   2099 C  C     . ALA A 1 280 ? -15.913 -2.103  -0.613 1.00 35.05 ? 287 ALA A C     1 
ATOM   2100 O  O     . ALA A 1 280 ? -15.841 -0.877  -0.472 1.00 34.60 ? 287 ALA A O     1 
ATOM   2101 C  CB    . ALA A 1 280 ? -16.817 -2.834  -2.825 1.00 32.01 ? 287 ALA A CB    1 
ATOM   2102 N  N     . ALA A 1 281 ? -16.292 -2.917  0.375  1.00 35.71 ? 288 ALA A N     1 
ATOM   2103 C  CA    . ALA A 1 281 ? -16.576 -2.387  1.704  1.00 35.34 ? 288 ALA A CA    1 
ATOM   2104 C  C     . ALA A 1 281 ? -15.297 -1.969  2.419  1.00 30.91 ? 288 ALA A C     1 
ATOM   2105 O  O     . ALA A 1 281 ? -15.267 -0.931  3.091  1.00 29.11 ? 288 ALA A O     1 
ATOM   2106 C  CB    . ALA A 1 281 ? -17.334 -3.425  2.531  1.00 29.34 ? 288 ALA A CB    1 
ATOM   2107 N  N     . MET A 1 282 ? -14.238 -2.772  2.297  1.00 31.04 ? 289 MET A N     1 
ATOM   2108 C  CA    . MET A 1 282 ? -12.963 -2.458  2.938  1.00 31.40 ? 289 MET A CA    1 
ATOM   2109 C  C     . MET A 1 282 ? -12.431 -1.095  2.512  1.00 33.25 ? 289 MET A C     1 
ATOM   2110 O  O     . MET A 1 282 ? -11.794 -0.390  3.304  1.00 35.53 ? 289 MET A O     1 
ATOM   2111 C  CB    . MET A 1 282 ? -11.951 -3.556  2.612  1.00 31.20 ? 289 MET A CB    1 
ATOM   2112 C  CG    . MET A 1 282 ? -12.287 -4.901  3.211  1.00 33.90 ? 289 MET A CG    1 
ATOM   2113 S  SD    . MET A 1 282 ? -10.777 -5.596  3.884  1.00 38.28 ? 289 MET A SD    1 
ATOM   2114 C  CE    . MET A 1 282 ? -10.231 -4.222  4.886  1.00 33.06 ? 289 MET A CE    1 
ATOM   2115 N  N     . LYS A 1 283 ? -12.733 -0.676  1.304  1.00 34.57 ? 290 LYS A N     1 
ATOM   2116 C  CA    . LYS A 1 283 ? -12.169 0.564   0.824  1.00 36.11 ? 290 LYS A CA    1 
ATOM   2117 C  C     . LYS A 1 283 ? -12.729 1.767   1.527  1.00 35.10 ? 290 LYS A C     1 
ATOM   2118 O  O     . LYS A 1 283 ? -12.111 2.812   1.515  1.00 40.00 ? 290 LYS A O     1 
ATOM   2119 C  CB    . LYS A 1 283 ? -12.366 0.673   -0.677 1.00 39.39 ? 290 LYS A CB    1 
ATOM   2120 C  CG    . LYS A 1 283 ? -11.435 -0.217  -1.479 1.00 40.67 ? 290 LYS A CG    1 
ATOM   2121 C  CD    . LYS A 1 283 ? -11.409 0.161   -2.950 1.00 44.07 ? 290 LYS A CD    1 
ATOM   2122 C  CE    . LYS A 1 283 ? -12.771 0.009   -3.602 1.00 38.53 ? 290 LYS A CE    1 
ATOM   2123 N  NZ    . LYS A 1 283 ? -12.692 0.198   -5.075 1.00 35.25 ? 290 LYS A NZ    1 
ATOM   2124 N  N     . GLU A 1 284 ? -13.898 1.651   2.133  1.00 36.81 ? 291 GLU A N     1 
ATOM   2125 C  CA    . GLU A 1 284 ? -14.493 2.751   2.901  1.00 33.83 ? 291 GLU A CA    1 
ATOM   2126 C  C     . GLU A 1 284 ? -13.984 2.928   4.333  1.00 35.35 ? 291 GLU A C     1 
ATOM   2127 O  O     . GLU A 1 284 ? -14.259 3.930   4.976  1.00 35.51 ? 291 GLU A O     1 
ATOM   2128 C  CB    . GLU A 1 284 ? -16.001 2.598   3.019  1.00 32.36 ? 291 GLU A CB    1 
ATOM   2129 C  CG    . GLU A 1 284 ? -16.804 2.736   1.748  1.00 36.07 ? 291 GLU A CG    1 
ATOM   2130 C  CD    . GLU A 1 284 ? -18.287 2.747   2.051  1.00 49.23 ? 291 GLU A CD    1 
ATOM   2131 O  OE1   . GLU A 1 284 ? -18.659 3.208   3.149  1.00 47.02 ? 291 GLU A OE1   1 
ATOM   2132 O  OE2   . GLU A 1 284 ? -19.079 2.295   1.204  1.00 45.08 ? 291 GLU A OE2   1 
ATOM   2133 N  N     . ILE A 1 285 ? -13.291 1.936   4.853  1.00 36.67 ? 292 ILE A N     1 
ATOM   2134 C  CA    . ILE A 1 285 ? -12.803 2.034   6.220  1.00 29.30 ? 292 ILE A CA    1 
ATOM   2135 C  C     . ILE A 1 285 ? -11.319 2.375   6.222  1.00 30.61 ? 292 ILE A C     1 
ATOM   2136 O  O     . ILE A 1 285 ? -10.601 2.187   5.236  1.00 30.73 ? 292 ILE A O     1 
ATOM   2137 C  CB    . ILE A 1 285 ? -13.050 0.737   7.019  1.00 30.93 ? 292 ILE A CB    1 
ATOM   2138 C  CG1   . ILE A 1 285 ? -12.172 -0.395  6.481  1.00 29.29 ? 292 ILE A CG1   1 
ATOM   2139 C  CG2   . ILE A 1 285 ? -14.505 0.365   6.984  1.00 28.35 ? 292 ILE A CG2   1 
ATOM   2140 C  CD1   . ILE A 1 285 ? -11.832 -1.434  7.511  1.00 29.90 ? 292 ILE A CD1   1 
ATOM   2141 N  N     . LYS A 1 286 ? -10.853 2.878   7.362  1.00 27.33 ? 293 LYS A N     1 
ATOM   2142 C  CA    . LYS A 1 286 ? -9.434  3.066   7.622  1.00 28.35 ? 293 LYS A CA    1 
ATOM   2143 C  C     . LYS A 1 286 ? -8.948  1.939   8.522  1.00 29.94 ? 293 LYS A C     1 
ATOM   2144 O  O     . LYS A 1 286 ? -9.527  1.696   9.586  1.00 27.04 ? 293 LYS A O     1 
ATOM   2145 C  CB    . LYS A 1 286 ? -9.164  4.421   8.279  1.00 28.39 ? 293 LYS A CB    1 
ATOM   2146 C  CG    . LYS A 1 286 ? -7.691  4.817   8.309  1.00 30.44 ? 293 LYS A CG    1 
ATOM   2147 C  CD    . LYS A 1 286 ? -7.306  5.436   9.646  1.00 26.44 ? 293 LYS A CD    1 
ATOM   2148 C  CE    . LYS A 1 286 ? -6.168  6.431   9.489  1.00 38.51 ? 293 LYS A CE    1 
ATOM   2149 N  NZ    . LYS A 1 286 ? -5.141  6.293   10.557 1.00 41.04 ? 293 LYS A NZ    1 
ATOM   2150 N  N     . TRP A 1 287 ? -7.898  1.246   8.090  1.00 25.47 ? 294 TRP A N     1 
ATOM   2151 C  CA    . TRP A 1 287 ? -7.296  0.168   8.870  1.00 27.58 ? 294 TRP A CA    1 
ATOM   2152 C  C     . TRP A 1 287 ? -5.789  0.374   8.872  1.00 30.89 ? 294 TRP A C     1 
ATOM   2153 O  O     . TRP A 1 287 ? -5.130  0.165   7.848  1.00 30.27 ? 294 TRP A O     1 
ATOM   2154 C  CB    . TRP A 1 287 ? -7.662  -1.205  8.305  1.00 26.65 ? 294 TRP A CB    1 
ATOM   2155 C  CG    . TRP A 1 287 ? -6.985  -2.334  9.023  1.00 29.89 ? 294 TRP A CG    1 
ATOM   2156 C  CD1   . TRP A 1 287 ? -6.767  -2.435  10.366 1.00 25.86 ? 294 TRP A CD1   1 
ATOM   2157 C  CD2   . TRP A 1 287 ? -6.423  -3.516  8.436  1.00 30.64 ? 294 TRP A CD2   1 
ATOM   2158 N  NE1   . TRP A 1 287 ? -6.111  -3.607  10.653 1.00 25.52 ? 294 TRP A NE1   1 
ATOM   2159 C  CE2   . TRP A 1 287 ? -5.887  -4.288  9.486  1.00 24.41 ? 294 TRP A CE2   1 
ATOM   2160 C  CE3   . TRP A 1 287 ? -6.323  -3.996  7.127  1.00 30.02 ? 294 TRP A CE3   1 
ATOM   2161 C  CZ2   . TRP A 1 287 ? -5.262  -5.514  9.268  1.00 27.41 ? 294 TRP A CZ2   1 
ATOM   2162 C  CZ3   . TRP A 1 287 ? -5.701  -5.214  6.913  1.00 27.83 ? 294 TRP A CZ3   1 
ATOM   2163 C  CH2   . TRP A 1 287 ? -5.179  -5.958  7.978  1.00 27.27 ? 294 TRP A CH2   1 
ATOM   2164 N  N     . ASP A 1 288 ? -5.247  0.784   10.017 1.00 25.24 ? 295 ASP A N     1 
ATOM   2165 C  CA    . ASP A 1 288 ? -3.823  1.083   10.147 1.00 25.37 ? 295 ASP A CA    1 
ATOM   2166 C  C     . ASP A 1 288 ? -3.075  -0.240  10.230 1.00 25.69 ? 295 ASP A C     1 
ATOM   2167 O  O     . ASP A 1 288 ? -2.944  -0.841  11.298 1.00 28.26 ? 295 ASP A O     1 
ATOM   2168 C  CB    . ASP A 1 288 ? -3.563  1.954   11.372 1.00 31.25 ? 295 ASP A CB    1 
ATOM   2169 C  CG    . ASP A 1 288 ? -2.155  2.528   11.396 1.00 32.50 ? 295 ASP A CG    1 
ATOM   2170 O  OD1   . ASP A 1 288 ? -1.291  2.027   10.648 1.00 33.60 ? 295 ASP A OD1   1 
ATOM   2171 O  OD2   . ASP A 1 288 ? -1.915  3.488   12.158 1.00 34.49 ? 295 ASP A OD2   1 
ATOM   2172 N  N     . VAL A 1 289 ? -2.584  -0.704  9.079  1.00 28.05 ? 296 VAL A N     1 
ATOM   2173 C  CA    . VAL A 1 289 ? -1.797  -1.931  9.045  1.00 25.43 ? 296 VAL A CA    1 
ATOM   2174 C  C     . VAL A 1 289 ? -0.499  -1.747  9.816  1.00 28.90 ? 296 VAL A C     1 
ATOM   2175 O  O     . VAL A 1 289 ? 0.025   -2.699  10.409 1.00 24.72 ? 296 VAL A O     1 
ATOM   2176 C  CB    . VAL A 1 289 ? -1.554  -2.352  7.579  1.00 27.84 ? 296 VAL A CB    1 
ATOM   2177 C  CG1   . VAL A 1 289 ? -0.518  -3.459  7.489  1.00 33.08 ? 296 VAL A CG1   1 
ATOM   2178 C  CG2   . VAL A 1 289 ? -2.862  -2.789  6.929  1.00 25.20 ? 296 VAL A CG2   1 
ATOM   2179 N  N     . ASP A 1 290 ? 0.023   -0.521  9.851  1.00 28.59 ? 297 ASP A N     1 
ATOM   2180 C  CA    . ASP A 1 290 ? 1.247   -0.257  10.599 1.00 26.76 ? 297 ASP A CA    1 
ATOM   2181 C  C     . ASP A 1 290 ? 1.036   -0.489  12.089 1.00 24.04 ? 297 ASP A C     1 
ATOM   2182 O  O     . ASP A 1 290 ? 1.843   -1.160  12.742 1.00 27.48 ? 297 ASP A O     1 
ATOM   2183 C  CB    . ASP A 1 290 ? 1.721   1.171   10.336 1.00 31.04 ? 297 ASP A CB    1 
ATOM   2184 C  CG    . ASP A 1 290 ? 2.448   1.303   9.019  1.00 40.22 ? 297 ASP A CG    1 
ATOM   2185 O  OD1   . ASP A 1 290 ? 3.388   0.514   8.780  1.00 41.88 ? 297 ASP A OD1   1 
ATOM   2186 O  OD2   . ASP A 1 290 ? 2.076   2.187   8.221  1.00 47.10 ? 297 ASP A OD2   1 
ATOM   2187 N  N     . ALA A 1 291 ? -0.048  0.059   12.646 1.00 26.53 ? 298 ALA A N     1 
ATOM   2188 C  CA    . ALA A 1 291 ? -0.364  -0.209  14.045 1.00 28.68 ? 298 ALA A CA    1 
ATOM   2189 C  C     . ALA A 1 291 ? -0.786  -1.656  14.250 1.00 24.93 ? 298 ALA A C     1 
ATOM   2190 O  O     . ALA A 1 291 ? -0.592  -2.210  15.338 1.00 26.01 ? 298 ALA A O     1 
ATOM   2191 C  CB    . ALA A 1 291 ? -1.459  0.738   14.537 1.00 18.85 ? 298 ALA A CB    1 
ATOM   2192 N  N     . PHE A 1 292 ? -1.355  -2.283  13.217 1.00 23.30 ? 299 PHE A N     1 
ATOM   2193 C  CA    . PHE A 1 292 ? -1.748  -3.684  13.319 1.00 22.58 ? 299 PHE A CA    1 
ATOM   2194 C  C     . PHE A 1 292 ? -0.541  -4.577  13.579 1.00 25.34 ? 299 PHE A C     1 
ATOM   2195 O  O     . PHE A 1 292 ? -0.604  -5.495  14.406 1.00 26.26 ? 299 PHE A O     1 
ATOM   2196 C  CB    . PHE A 1 292 ? -2.477  -4.106  12.042 1.00 27.15 ? 299 PHE A CB    1 
ATOM   2197 C  CG    . PHE A 1 292 ? -2.826  -5.564  11.989 1.00 29.22 ? 299 PHE A CG    1 
ATOM   2198 C  CD1   . PHE A 1 292 ? -3.904  -6.060  12.702 1.00 27.26 ? 299 PHE A CD1   1 
ATOM   2199 C  CD2   . PHE A 1 292 ? -2.078  -6.440  11.220 1.00 23.90 ? 299 PHE A CD2   1 
ATOM   2200 C  CE1   . PHE A 1 292 ? -4.230  -7.402  12.651 1.00 26.26 ? 299 PHE A CE1   1 
ATOM   2201 C  CE2   . PHE A 1 292 ? -2.397  -7.783  11.166 1.00 21.01 ? 299 PHE A CE2   1 
ATOM   2202 C  CZ    . PHE A 1 292 ? -3.475  -8.265  11.883 1.00 24.43 ? 299 PHE A CZ    1 
ATOM   2203 N  N     . GLN A 1 293 ? 0.573   -4.321  12.891 1.00 27.36 ? 300 GLN A N     1 
ATOM   2204 C  CA    . GLN A 1 293 ? 1.774   -5.110  13.134 1.00 27.09 ? 300 GLN A CA    1 
ATOM   2205 C  C     . GLN A 1 293 ? 2.534   -4.633  14.364 1.00 24.15 ? 300 GLN A C     1 
ATOM   2206 O  O     . GLN A 1 293 ? 3.199   -5.443  15.021 1.00 25.44 ? 300 GLN A O     1 
ATOM   2207 C  CB    . GLN A 1 293 ? 2.694   -5.087  11.913 1.00 26.01 ? 300 GLN A CB    1 
ATOM   2208 C  CG    . GLN A 1 293 ? 1.981   -5.136  10.578 1.00 32.20 ? 300 GLN A CG    1 
ATOM   2209 C  CD    . GLN A 1 293 ? 2.811   -5.817  9.511  1.00 40.59 ? 300 GLN A CD    1 
ATOM   2210 O  OE1   . GLN A 1 293 ? 3.575   -5.166  8.798  1.00 41.84 ? 300 GLN A OE1   1 
ATOM   2211 N  NE2   . GLN A 1 293 ? 2.675   -7.134  9.401  1.00 40.31 ? 300 GLN A NE2   1 
ATOM   2212 N  N     . GLU A 1 294 ? 2.455   -3.340  14.693 1.00 25.03 ? 301 GLU A N     1 
ATOM   2213 C  CA    . GLU A 1 294 ? 3.101   -2.858  15.911 1.00 26.58 ? 301 GLU A CA    1 
ATOM   2214 C  C     . GLU A 1 294 ? 2.515   -3.535  17.145 1.00 27.01 ? 301 GLU A C     1 
ATOM   2215 O  O     . GLU A 1 294 ? 3.251   -3.909  18.066 1.00 24.87 ? 301 GLU A O     1 
ATOM   2216 C  CB    . GLU A 1 294 ? 2.974   -1.339  16.023 1.00 27.02 ? 301 GLU A CB    1 
ATOM   2217 C  CG    . GLU A 1 294 ? 3.481   -0.801  17.353 1.00 26.98 ? 301 GLU A CG    1 
ATOM   2218 C  CD    . GLU A 1 294 ? 3.648   0.704   17.373 1.00 28.52 ? 301 GLU A CD    1 
ATOM   2219 O  OE1   . GLU A 1 294 ? 3.492   1.347   16.313 1.00 26.26 ? 301 GLU A OE1   1 
ATOM   2220 O  OE2   . GLU A 1 294 ? 3.940   1.241   18.463 1.00 26.51 ? 301 GLU A OE2   1 
ATOM   2221 N  N     . ARG A 1 295 ? 1.195   -3.713  17.179 1.00 26.73 ? 302 ARG A N     1 
ATOM   2222 C  CA    . ARG A 1 295 ? 0.551   -4.417  18.281 1.00 29.09 ? 302 ARG A CA    1 
ATOM   2223 C  C     . ARG A 1 295 ? 0.681   -5.931  18.167 1.00 28.25 ? 302 ARG A C     1 
ATOM   2224 O  O     . ARG A 1 295 ? 0.003   -6.652  18.905 1.00 27.77 ? 302 ARG A O     1 
ATOM   2225 C  CB    . ARG A 1 295 ? -0.927  -4.019  18.379 1.00 24.36 ? 302 ARG A CB    1 
ATOM   2226 C  CG    . ARG A 1 295 ? -1.852  -4.587  17.303 1.00 22.18 ? 302 ARG A CG    1 
ATOM   2227 C  CD    . ARG A 1 295 ? -3.308  -4.334  17.692 1.00 22.48 ? 302 ARG A CD    1 
ATOM   2228 N  NE    . ARG A 1 295 ? -4.271  -4.687  16.655 1.00 20.12 ? 302 ARG A NE    1 
ATOM   2229 C  CZ    . ARG A 1 295 ? -4.734  -5.912  16.444 1.00 19.82 ? 302 ARG A CZ    1 
ATOM   2230 N  NH1   . ARG A 1 295 ? -4.317  -6.942  17.163 1.00 18.98 ? 302 ARG A NH1   1 
ATOM   2231 N  NH2   . ARG A 1 295 ? -5.643  -6.108  15.493 1.00 18.93 ? 302 ARG A NH2   1 
ATOM   2232 N  N     . GLY A 1 296 ? 1.542   -6.422  17.281 1.00 25.61 ? 303 GLY A N     1 
ATOM   2233 C  CA    . GLY A 1 296 ? 1.703   -7.857  17.118 1.00 21.48 ? 303 GLY A CA    1 
ATOM   2234 C  C     . GLY A 1 296 ? 0.437   -8.548  16.663 1.00 27.61 ? 303 GLY A C     1 
ATOM   2235 O  O     . GLY A 1 296 ? 0.133   -9.654  17.127 1.00 25.81 ? 303 GLY A O     1 
ATOM   2236 N  N     . GLY A 1 297 ? -0.316  -7.909  15.763 1.00 27.25 ? 304 GLY A N     1 
ATOM   2237 C  CA    . GLY A 1 297 ? -1.563  -8.490  15.293 1.00 25.76 ? 304 GLY A CA    1 
ATOM   2238 C  C     . GLY A 1 297 ? -1.379  -9.810  14.573 1.00 22.91 ? 304 GLY A C     1 
ATOM   2239 O  O     . GLY A 1 297 ? -2.261  -10.671 14.616 1.00 19.55 ? 304 GLY A O     1 
ATOM   2240 N  N     . VAL A 1 298 ? -0.229  -10.010 13.960 1.00 26.90 ? 305 VAL A N     1 
ATOM   2241 C  CA    . VAL A 1 298 ? 0.074   -11.272 13.318 1.00 25.61 ? 305 VAL A CA    1 
ATOM   2242 C  C     . VAL A 1 298 ? 0.985   -12.045 14.242 1.00 23.94 ? 305 VAL A C     1 
ATOM   2243 O  O     . VAL A 1 298 ? 1.954   -11.510 14.728 1.00 27.77 ? 305 VAL A O     1 
ATOM   2244 C  CB    . VAL A 1 298 ? 0.645   -11.088 11.903 1.00 26.84 ? 305 VAL A CB    1 
ATOM   2245 C  CG1   . VAL A 1 298 ? 0.920   -12.446 11.287 1.00 19.58 ? 305 VAL A CG1   1 
ATOM   2246 C  CG2   . VAL A 1 298 ? -0.344  -10.346 11.032 1.00 31.96 ? 305 VAL A CG2   1 
ATOM   2247 N  N     . TYR A 1 299 ? 0.643   -13.286 14.525 1.00 22.68 ? 306 TYR A N     1 
ATOM   2248 C  CA    . TYR A 1 299 ? 1.389   -14.087 15.487 1.00 19.67 ? 306 TYR A CA    1 
ATOM   2249 C  C     . TYR A 1 299 ? 1.046   -15.556 15.268 1.00 20.82 ? 306 TYR A C     1 
ATOM   2250 O  O     . TYR A 1 299 ? 0.284   -15.912 14.364 1.00 24.23 ? 306 TYR A O     1 
ATOM   2251 C  CB    . TYR A 1 299 ? 1.093   -13.644 16.925 1.00 23.99 ? 306 TYR A CB    1 
ATOM   2252 C  CG    . TYR A 1 299 ? -0.342  -13.841 17.363 1.00 21.88 ? 306 TYR A CG    1 
ATOM   2253 C  CD1   . TYR A 1 299 ? -1.316  -12.893 17.074 1.00 21.10 ? 306 TYR A CD1   1 
ATOM   2254 C  CD2   . TYR A 1 299 ? -0.718  -14.967 18.080 1.00 22.58 ? 306 TYR A CD2   1 
ATOM   2255 C  CE1   . TYR A 1 299 ? -2.627  -13.068 17.480 1.00 17.94 ? 306 TYR A CE1   1 
ATOM   2256 C  CE2   . TYR A 1 299 ? -2.024  -15.150 18.490 1.00 21.17 ? 306 TYR A CE2   1 
ATOM   2257 C  CZ    . TYR A 1 299 ? -2.976  -14.199 18.188 1.00 22.07 ? 306 TYR A CZ    1 
ATOM   2258 O  OH    . TYR A 1 299 ? -4.278  -14.381 18.596 1.00 22.91 ? 306 TYR A OH    1 
ATOM   2259 N  N     . GLU A 1 300 ? 1.631   -16.409 16.106 1.00 26.21 ? 307 GLU A N     1 
ATOM   2260 C  CA    . GLU A 1 300 ? 1.426   -17.855 16.043 1.00 27.05 ? 307 GLU A CA    1 
ATOM   2261 C  C     . GLU A 1 300 ? 0.058   -18.151 16.638 1.00 30.64 ? 307 GLU A C     1 
ATOM   2262 O  O     . GLU A 1 300 ? -0.078  -18.447 17.825 1.00 30.81 ? 307 GLU A O     1 
ATOM   2263 C  CB    . GLU A 1 300 ? 2.532   -18.586 16.794 1.00 29.73 ? 307 GLU A CB    1 
ATOM   2264 C  CG    . GLU A 1 300 ? 3.912   -18.404 16.194 1.00 29.09 ? 307 GLU A CG    1 
ATOM   2265 C  CD    . GLU A 1 300 ? 4.005   -18.918 14.773 1.00 33.69 ? 307 GLU A CD    1 
ATOM   2266 O  OE1   . GLU A 1 300 ? 4.196   -20.140 14.602 1.00 44.08 ? 307 GLU A OE1   1 
ATOM   2267 O  OE2   . GLU A 1 300 ? 3.886   -18.107 13.831 1.00 35.51 ? 307 GLU A OE2   1 
ATOM   2268 N  N     . TRP A 1 301 ? -0.966  -18.059 15.810 1.00 24.70 ? 308 TRP A N     1 
ATOM   2269 C  CA    . TRP A 1 301 ? -2.330  -18.163 16.304 1.00 25.63 ? 308 TRP A CA    1 
ATOM   2270 C  C     . TRP A 1 301 ? -3.050  -19.499 16.137 1.00 26.50 ? 308 TRP A C     1 
ATOM   2271 O  O     . TRP A 1 301 ? -4.244  -19.579 16.301 1.00 23.51 ? 308 TRP A O     1 
ATOM   2272 C  CB    . TRP A 1 301 ? -3.117  -17.032 15.643 1.00 21.15 ? 308 TRP A CB    1 
ATOM   2273 C  CG    . TRP A 1 301 ? -3.041  -16.941 14.157 1.00 23.66 ? 308 TRP A CG    1 
ATOM   2274 C  CD1   . TRP A 1 301 ? -2.916  -17.966 13.279 1.00 25.03 ? 308 TRP A CD1   1 
ATOM   2275 C  CD2   . TRP A 1 301 ? -3.126  -15.747 13.370 1.00 21.03 ? 308 TRP A CD2   1 
ATOM   2276 N  NE1   . TRP A 1 301 ? -2.901  -17.490 11.996 1.00 23.83 ? 308 TRP A NE1   1 
ATOM   2277 C  CE2   . TRP A 1 301 ? -3.027  -16.129 12.025 1.00 20.05 ? 308 TRP A CE2   1 
ATOM   2278 C  CE3   . TRP A 1 301 ? -3.260  -14.392 13.677 1.00 18.80 ? 308 TRP A CE3   1 
ATOM   2279 C  CZ2   . TRP A 1 301 ? -3.061  -15.209 10.985 1.00 19.87 ? 308 TRP A CZ2   1 
ATOM   2280 C  CZ3   . TRP A 1 301 ? -3.302  -13.483 12.646 1.00 21.96 ? 308 TRP A CZ3   1 
ATOM   2281 C  CH2   . TRP A 1 301 ? -3.201  -13.893 11.315 1.00 19.12 ? 308 TRP A CH2   1 
ATOM   2282 N  N     . THR A 1 302 ? -2.304  -20.542 15.846 1.00 28.17 ? 309 THR A N     1 
ATOM   2283 C  CA    . THR A 1 302 ? -2.889  -21.847 15.602 1.00 28.13 ? 309 THR A CA    1 
ATOM   2284 C  C     . THR A 1 302 ? -2.453  -22.965 16.554 1.00 37.26 ? 309 THR A C     1 
ATOM   2285 O  O     . THR A 1 302 ? -1.607  -22.739 17.407 1.00 40.82 ? 309 THR A O     1 
ATOM   2286 C  CB    . THR A 1 302 ? -2.576  -22.289 14.164 1.00 28.62 ? 309 THR A CB    1 
ATOM   2287 O  OG1   . THR A 1 302 ? -1.166  -22.436 14.011 1.00 36.00 ? 309 THR A OG1   1 
ATOM   2288 C  CG2   . THR A 1 302 ? -3.080  -21.262 13.174 1.00 24.95 ? 309 THR A CG2   1 
ATOM   2289 N  N     . LYS A 1 303 ? -3.024  -24.155 16.413 1.00 42.15 ? 310 LYS A N     1 
ATOM   2290 C  CA    . LYS A 1 303 ? -2.723  -25.354 17.230 1.00 39.03 ? 310 LYS A CA    1 
ATOM   2291 C  C     . LYS A 1 303 ? -3.781  -25.622 18.260 1.00 44.27 ? 310 LYS A C     1 
ATOM   2292 O  O     . LYS A 1 303 ? -3.933  -24.861 19.191 1.00 40.87 ? 310 LYS A O     1 
ATOM   2293 C  CB    . LYS A 1 303 ? -1.336  -25.443 17.881 1.00 39.54 ? 310 LYS A CB    1 
ATOM   2294 C  CG    . LYS A 1 303 ? -1.284  -26.500 18.970 1.00 40.48 ? 310 LYS A CG    1 
ATOM   2295 C  CD    . LYS A 1 303 ? 0.088   -27.126 19.132 1.00 44.70 ? 310 LYS A CD    1 
ATOM   2296 C  CE    . LYS A 1 303 ? 0.407   -28.052 17.971 1.00 39.33 ? 310 LYS A CE    1 
ATOM   2297 N  NZ    . LYS A 1 303 ? -0.557  -29.178 17.855 1.00 36.56 ? 310 LYS A NZ    1 
ATOM   2298 N  N     . GLU A 1 304 ? -4.546  -26.688 18.045 1.00 50.64 ? 311 GLU A N     1 
ATOM   2299 C  CA    . GLU A 1 304 ? -5.550  -27.149 19.008 1.00 41.50 ? 311 GLU A CA    1 
ATOM   2300 C  C     . GLU A 1 304 ? -6.760  -26.288 19.277 1.00 33.91 ? 311 GLU A C     1 
ATOM   2301 O  O     . GLU A 1 304 ? -7.805  -26.831 19.580 1.00 29.18 ? 311 GLU A O     1 
ATOM   2302 C  CB    . GLU A 1 304 ? -4.839  -27.524 20.317 1.00 43.85 ? 311 GLU A CB    1 
ATOM   2303 C  CG    . GLU A 1 304 ? -4.541  -29.010 20.451 1.00 46.04 ? 311 GLU A CG    1 
ATOM   2304 C  CD    . GLU A 1 304 ? -5.764  -29.838 20.811 1.00 51.42 ? 311 GLU A CD    1 
ATOM   2305 O  OE1   . GLU A 1 304 ? -6.828  -29.264 21.119 1.00 51.66 ? 311 GLU A OE1   1 
ATOM   2306 O  OE2   . GLU A 1 304 ? -5.660  -31.077 20.799 1.00 55.07 ? 311 GLU A OE2   1 
HETATM 2307 N  N1    . CTP B 2 .   ? -12.071 -3.366  19.364 1.00 18.19 ? 401 CTP A N1    1 
HETATM 2308 C  C2    . CTP B 2 .   ? -13.126 -2.495  19.067 1.00 16.77 ? 401 CTP A C2    1 
HETATM 2309 N  N3    . CTP B 2 .   ? -12.883 -1.237  18.684 1.00 16.40 ? 401 CTP A N3    1 
HETATM 2310 C  C4    . CTP B 2 .   ? -11.620 -0.796  18.587 1.00 18.91 ? 401 CTP A C4    1 
HETATM 2311 C  C5    . CTP B 2 .   ? -10.567 -1.645  18.884 1.00 17.79 ? 401 CTP A C5    1 
HETATM 2312 C  C6    . CTP B 2 .   ? -10.817 -2.947  19.275 1.00 19.22 ? 401 CTP A C6    1 
HETATM 2313 O  O2    . CTP B 2 .   ? -14.293 -2.896  19.159 1.00 18.64 ? 401 CTP A O2    1 
HETATM 2314 N  N4    . CTP B 2 .   ? -11.375 0.473   18.202 1.00 14.46 ? 401 CTP A N4    1 
HETATM 2315 C  "C1'" . CTP B 2 .   ? -12.391 -4.725  19.789 1.00 20.39 ? 401 CTP A "C1'" 1 
HETATM 2316 C  "C2'" . CTP B 2 .   ? -11.939 -5.768  18.794 1.00 18.25 ? 401 CTP A "C2'" 1 
HETATM 2317 O  "O2'" . CTP B 2 .   ? -12.907 -5.887  17.768 1.00 20.55 ? 401 CTP A "O2'" 1 
HETATM 2318 C  "C3'" . CTP B 2 .   ? -11.811 -7.000  19.657 1.00 17.60 ? 401 CTP A "C3'" 1 
HETATM 2319 C  "C4'" . CTP B 2 .   ? -11.773 -6.504  21.088 1.00 23.02 ? 401 CTP A "C4'" 1 
HETATM 2320 O  "O4'" . CTP B 2 .   ? -11.719 -5.083  20.992 1.00 22.48 ? 401 CTP A "O4'" 1 
HETATM 2321 O  "O3'" . CTP B 2 .   ? -12.947 -7.832  19.532 1.00 16.99 ? 401 CTP A "O3'" 1 
HETATM 2322 C  "C5'" . CTP B 2 .   ? -10.618 -7.101  21.898 1.00 20.32 ? 401 CTP A "C5'" 1 
HETATM 2323 O  "O5'" . CTP B 2 .   ? -9.444  -7.290  21.125 1.00 22.27 ? 401 CTP A "O5'" 1 
HETATM 2324 P  PA    . CTP B 2 .   ? -8.678  -8.693  21.022 1.00 16.98 ? 401 CTP A PA    1 
HETATM 2325 O  O1A   . CTP B 2 .   ? -9.336  -9.727  21.860 1.00 14.38 ? 401 CTP A O1A   1 
HETATM 2326 O  O2A   . CTP B 2 .   ? -7.240  -8.407  21.265 1.00 24.68 ? 401 CTP A O2A   1 
HETATM 2327 O  O3A   . CTP B 2 .   ? -8.916  -9.007  19.463 1.00 20.26 ? 401 CTP A O3A   1 
HETATM 2328 P  PB    . CTP B 2 .   ? -8.206  -10.135 18.569 1.00 18.24 ? 401 CTP A PB    1 
HETATM 2329 O  O1B   . CTP B 2 .   ? -8.609  -11.486 19.075 1.00 18.82 ? 401 CTP A O1B   1 
HETATM 2330 O  O2B   . CTP B 2 .   ? -8.509  -9.796  17.151 1.00 18.60 ? 401 CTP A O2B   1 
HETATM 2331 O  O3B   . CTP B 2 .   ? -6.648  -9.895  18.832 1.00 21.65 ? 401 CTP A O3B   1 
HETATM 2332 P  PG    . CTP B 2 .   ? -5.498  -10.968 18.522 1.00 21.46 ? 401 CTP A PG    1 
HETATM 2333 O  O1G   . CTP B 2 .   ? -5.518  -11.877 19.705 1.00 24.98 ? 401 CTP A O1G   1 
HETATM 2334 O  O2G   . CTP B 2 .   ? -4.270  -10.125 18.436 1.00 23.84 ? 401 CTP A O2G   1 
HETATM 2335 O  O3G   . CTP B 2 .   ? -5.852  -11.610 17.224 1.00 20.97 ? 401 CTP A O3G   1 
HETATM 2336 FE FE1   . SF4 C 3 .   ? -18.565 -5.795  29.473 1.00 17.24 ? 402 SF4 A FE1   1 
HETATM 2337 FE FE2   . SF4 C 3 .   ? -17.964 -7.398  26.953 1.00 18.25 ? 402 SF4 A FE2   1 
HETATM 2338 FE FE3   . SF4 C 3 .   ? -19.215 -4.595  26.721 1.00 18.32 ? 402 SF4 A FE3   1 
HETATM 2339 FE FE4   . SF4 C 3 .   ? -20.799 -6.970  27.790 1.00 19.33 ? 402 SF4 A FE4   1 
HETATM 2340 S  S1    . SF4 C 3 .   ? -19.702 -6.558  26.021 1.00 19.64 ? 402 SF4 A S1    1 
HETATM 2341 S  S2    . SF4 C 3 .   ? -20.310 -5.022  28.509 1.00 18.10 ? 402 SF4 A S2    1 
HETATM 2342 S  S3    . SF4 C 3 .   ? -19.065 -7.743  28.758 1.00 23.26 ? 402 SF4 A S3    1 
HETATM 2343 S  S4    . SF4 C 3 .   ? -17.493 -5.438  27.657 1.00 24.34 ? 402 SF4 A S4    1 
HETATM 2344 N  N     . SAM D 4 .   ? -18.149 -9.879  26.101 1.00 15.60 ? 403 SAM A N     1 
HETATM 2345 C  CA    . SAM D 4 .   ? -16.835 -10.212 25.607 1.00 17.30 ? 403 SAM A CA    1 
HETATM 2346 C  C     . SAM D 4 .   ? -15.748 -9.899  26.603 1.00 14.35 ? 403 SAM A C     1 
HETATM 2347 O  O     . SAM D 4 .   ? -14.711 -10.504 26.554 1.00 18.99 ? 403 SAM A O     1 
HETATM 2348 O  OXT   . SAM D 4 .   ? -15.882 -9.090  27.430 1.00 14.96 ? 403 SAM A OXT   1 
HETATM 2349 C  CB    . SAM D 4 .   ? -16.647 -9.518  24.258 1.00 15.40 ? 403 SAM A CB    1 
HETATM 2350 C  CG    . SAM D 4 .   ? -17.097 -8.068  24.199 1.00 20.04 ? 403 SAM A CG    1 
HETATM 2351 S  SD    . SAM D 4 .   ? -15.953 -6.978  24.668 1.00 23.47 ? 403 SAM A SD    1 
HETATM 2352 C  CE    . SAM D 4 .   ? -16.461 -5.497  24.153 1.00 21.17 ? 403 SAM A CE    1 
HETATM 2353 C  "C5'" . SAM D 4 .   ? -14.483 -7.340  23.966 1.00 20.81 ? 403 SAM A "C5'" 1 
HETATM 2354 C  "C4'" . SAM D 4 .   ? -13.246 -6.775  24.671 1.00 17.86 ? 403 SAM A "C4'" 1 
HETATM 2355 O  "O4'" . SAM D 4 .   ? -13.166 -5.352  24.594 1.00 18.86 ? 403 SAM A "O4'" 1 
HETATM 2356 C  "C3'" . SAM D 4 .   ? -13.225 -7.125  26.147 1.00 18.76 ? 403 SAM A "C3'" 1 
HETATM 2357 O  "O3'" . SAM D 4 .   ? -11.951 -7.650  26.477 1.00 12.69 ? 403 SAM A "O3'" 1 
HETATM 2358 C  "C2'" . SAM D 4 .   ? -13.480 -5.818  26.854 1.00 14.52 ? 403 SAM A "C2'" 1 
HETATM 2359 O  "O2'" . SAM D 4 .   ? -12.870 -5.790  28.132 1.00 20.21 ? 403 SAM A "O2'" 1 
HETATM 2360 C  "C1'" . SAM D 4 .   ? -12.867 -4.827  25.887 1.00 15.31 ? 403 SAM A "C1'" 1 
HETATM 2361 N  N9    . SAM D 4 .   ? -13.399 -3.451  26.005 1.00 16.74 ? 403 SAM A N9    1 
HETATM 2362 C  C8    . SAM D 4 .   ? -14.668 -3.075  26.140 1.00 13.65 ? 403 SAM A C8    1 
HETATM 2363 N  N7    . SAM D 4 .   ? -14.769 -1.735  26.205 1.00 14.18 ? 403 SAM A N7    1 
HETATM 2364 C  C5    . SAM D 4 .   ? -13.542 -1.229  26.101 1.00 14.48 ? 403 SAM A C5    1 
HETATM 2365 C  C6    . SAM D 4 .   ? -12.941 0.117   26.094 1.00 16.23 ? 403 SAM A C6    1 
HETATM 2366 N  N6    . SAM D 4 .   ? -13.710 1.211   26.207 1.00 14.89 ? 403 SAM A N6    1 
HETATM 2367 N  N1    . SAM D 4 .   ? -11.607 0.206   25.965 1.00 12.31 ? 403 SAM A N1    1 
HETATM 2368 C  C2    . SAM D 4 .   ? -10.847 -0.889  25.843 1.00 14.13 ? 403 SAM A C2    1 
HETATM 2369 N  N3    . SAM D 4 .   ? -11.324 -2.138  25.842 1.00 14.35 ? 403 SAM A N3    1 
HETATM 2370 C  C4    . SAM D 4 .   ? -12.641 -2.367  25.968 1.00 12.59 ? 403 SAM A C4    1 
HETATM 2371 CL CL    . CL  E 5 .   ? -1.944  -21.579 27.049 1.00 32.05 ? 404 CL  A CL    1 
HETATM 2372 O  O     . HOH F 6 .   ? -8.466  -18.690 4.077  1.00 31.76 ? 501 HOH A O     1 
HETATM 2373 O  O     . HOH F 6 .   ? 4.385   -13.663 40.812 1.00 27.90 ? 502 HOH A O     1 
HETATM 2374 O  O     . HOH F 6 .   ? -9.727  -14.237 21.401 1.00 23.63 ? 503 HOH A O     1 
HETATM 2375 O  O     . HOH F 6 .   ? -21.575 -27.803 30.842 1.00 25.09 ? 504 HOH A O     1 
HETATM 2376 O  O     . HOH F 6 .   ? 2.163   5.285   28.409 1.00 27.24 ? 505 HOH A O     1 
HETATM 2377 O  O     . HOH F 6 .   ? -5.837  -25.302 14.836 1.00 26.59 ? 506 HOH A O     1 
HETATM 2378 O  O     . HOH F 6 .   ? -24.881 -10.777 12.842 1.00 22.44 ? 507 HOH A O     1 
HETATM 2379 O  O     . HOH F 6 .   ? -3.667  -7.935  41.813 1.00 25.18 ? 508 HOH A O     1 
HETATM 2380 O  O     . HOH F 6 .   ? -15.905 6.754   39.539 1.00 27.00 ? 509 HOH A O     1 
HETATM 2381 O  O     . HOH F 6 .   ? 0.453   3.831   12.687 1.00 27.77 ? 510 HOH A O     1 
HETATM 2382 O  O     . HOH F 6 .   ? -2.390  -7.111  19.206 1.00 19.05 ? 511 HOH A O     1 
HETATM 2383 O  O     . HOH F 6 .   ? -23.155 -19.981 33.708 1.00 31.92 ? 512 HOH A O     1 
HETATM 2384 O  O     . HOH F 6 .   ? -1.989  -3.967  43.479 1.00 24.57 ? 513 HOH A O     1 
HETATM 2385 O  O     . HOH F 6 .   ? 0.362   4.033   43.221 1.00 30.14 ? 514 HOH A O     1 
HETATM 2386 O  O     . HOH F 6 .   ? -31.184 -2.693  13.843 1.00 28.35 ? 515 HOH A O     1 
HETATM 2387 O  O     . HOH F 6 .   ? -18.342 8.456   32.885 1.00 28.34 ? 516 HOH A O     1 
HETATM 2388 O  O     . HOH F 6 .   ? -7.737  -4.438  -0.405 1.00 35.39 ? 517 HOH A O     1 
HETATM 2389 O  O     . HOH F 6 .   ? -20.398 12.022  33.025 1.00 35.28 ? 518 HOH A O     1 
HETATM 2390 O  O     . HOH F 6 .   ? -0.116  -1.130  38.029 1.00 21.52 ? 519 HOH A O     1 
HETATM 2391 O  O     . HOH F 6 .   ? -5.103  -10.695 14.932 1.00 24.89 ? 520 HOH A O     1 
HETATM 2392 O  O     . HOH F 6 .   ? -13.329 -7.382  35.118 1.00 18.15 ? 521 HOH A O     1 
HETATM 2393 O  O     . HOH F 6 .   ? -6.919  8.277   16.037 1.00 30.97 ? 522 HOH A O     1 
HETATM 2394 O  O     . HOH F 6 .   ? -23.109 -6.048  35.610 1.00 26.56 ? 523 HOH A O     1 
HETATM 2395 O  O     . HOH F 6 .   ? -28.899 -9.460  27.739 1.00 17.85 ? 524 HOH A O     1 
HETATM 2396 O  O     . HOH F 6 .   ? -21.912 -5.614  16.475 1.00 19.91 ? 525 HOH A O     1 
HETATM 2397 O  O     . HOH F 6 .   ? -20.389 1.273   35.939 1.00 23.93 ? 526 HOH A O     1 
HETATM 2398 O  O     . HOH F 6 .   ? -12.431 -20.501 39.523 1.00 29.79 ? 527 HOH A O     1 
HETATM 2399 O  O     . HOH F 6 .   ? 6.205   -11.646 37.460 1.00 27.21 ? 528 HOH A O     1 
HETATM 2400 O  O     . HOH F 6 .   ? 3.762   -14.629 29.619 1.00 22.82 ? 529 HOH A O     1 
HETATM 2401 O  O     . HOH F 6 .   ? -30.615 -11.993 8.577  1.00 33.23 ? 530 HOH A O     1 
HETATM 2402 O  O     . HOH F 6 .   ? -23.855 3.665   22.625 1.00 23.08 ? 531 HOH A O     1 
HETATM 2403 O  O     . HOH F 6 .   ? -17.018 5.801   16.307 1.00 26.12 ? 532 HOH A O     1 
HETATM 2404 O  O     . HOH F 6 .   ? -11.048 -7.113  29.603 1.00 17.85 ? 533 HOH A O     1 
HETATM 2405 O  O     . HOH F 6 .   ? -6.885  -8.480  15.470 1.00 21.26 ? 534 HOH A O     1 
HETATM 2406 O  O     . HOH F 6 .   ? -8.726  -11.716 15.295 1.00 18.55 ? 535 HOH A O     1 
HETATM 2407 O  O     . HOH F 6 .   ? 1.505   1.960   41.350 1.00 19.94 ? 536 HOH A O     1 
HETATM 2408 O  O     . HOH F 6 .   ? -3.951  -13.843 3.795  1.00 23.53 ? 537 HOH A O     1 
HETATM 2409 O  O     . HOH F 6 .   ? -12.255 5.930   19.224 1.00 20.16 ? 538 HOH A O     1 
HETATM 2410 O  O     . HOH F 6 .   ? -22.198 8.351   15.747 1.00 33.10 ? 539 HOH A O     1 
HETATM 2411 O  O     . HOH F 6 .   ? -9.608  7.372   24.175 1.00 22.23 ? 540 HOH A O     1 
HETATM 2412 O  O     . HOH F 6 .   ? -12.996 -2.143  10.510 1.00 22.16 ? 541 HOH A O     1 
HETATM 2413 O  O     . HOH F 6 .   ? -18.877 -12.072 33.454 1.00 22.17 ? 542 HOH A O     1 
HETATM 2414 O  O     . HOH F 6 .   ? -24.218 -4.368  28.062 1.00 19.94 ? 543 HOH A O     1 
HETATM 2415 O  O     . HOH F 6 .   ? -20.485 -18.825 35.453 1.00 27.45 ? 544 HOH A O     1 
HETATM 2416 O  O     . HOH F 6 .   ? -17.195 -2.440  44.934 1.00 22.28 ? 545 HOH A O     1 
HETATM 2417 O  O     . HOH F 6 .   ? -32.052 -0.047  20.780 1.00 37.64 ? 546 HOH A O     1 
HETATM 2418 O  O     . HOH F 6 .   ? -20.223 -15.648 28.822 1.00 21.04 ? 547 HOH A O     1 
HETATM 2419 O  O     . HOH F 6 .   ? -11.144 -9.785  45.361 1.00 22.17 ? 548 HOH A O     1 
HETATM 2420 O  O     . HOH F 6 .   ? -18.997 -20.185 33.228 1.00 27.15 ? 549 HOH A O     1 
HETATM 2421 O  O     . HOH F 6 .   ? -4.607  2.423   15.176 1.00 26.64 ? 550 HOH A O     1 
HETATM 2422 O  O     . HOH F 6 .   ? 3.506   -4.891  24.396 1.00 20.73 ? 551 HOH A O     1 
HETATM 2423 O  O     . HOH F 6 .   ? -26.941 -16.368 2.348  1.00 31.87 ? 552 HOH A O     1 
HETATM 2424 O  O     . HOH F 6 .   ? -12.241 -30.933 30.828 1.00 38.71 ? 553 HOH A O     1 
HETATM 2425 O  O     . HOH F 6 .   ? -21.716 -22.737 26.727 1.00 27.14 ? 554 HOH A O     1 
HETATM 2426 O  O     . HOH F 6 .   ? -21.479 4.214   31.912 1.00 24.91 ? 555 HOH A O     1 
HETATM 2427 O  O     . HOH F 6 .   ? 2.145   -10.846 19.236 1.00 24.80 ? 556 HOH A O     1 
HETATM 2428 O  O     . HOH F 6 .   ? -26.715 -5.796  29.986 1.00 18.51 ? 557 HOH A O     1 
HETATM 2429 O  O     . HOH F 6 .   ? -28.410 6.135   23.198 1.00 27.12 ? 558 HOH A O     1 
HETATM 2430 O  O     . HOH F 6 .   ? 4.372   7.081   33.719 1.00 24.28 ? 559 HOH A O     1 
HETATM 2431 O  O     . HOH F 6 .   ? -24.686 -1.047  26.046 1.00 21.52 ? 560 HOH A O     1 
HETATM 2432 O  O     . HOH F 6 .   ? -26.997 -10.115 -0.073 1.00 29.88 ? 561 HOH A O     1 
HETATM 2433 O  O     . HOH F 6 .   ? -12.118 3.264   17.689 1.00 27.79 ? 562 HOH A O     1 
HETATM 2434 O  O     . HOH F 6 .   ? -20.447 4.773   17.077 1.00 22.16 ? 563 HOH A O     1 
HETATM 2435 O  O     . HOH F 6 .   ? -6.425  1.624   23.678 1.00 18.90 ? 564 HOH A O     1 
HETATM 2436 O  O     . HOH F 6 .   ? -8.901  -7.466  13.599 1.00 20.41 ? 565 HOH A O     1 
HETATM 2437 O  O     . HOH F 6 .   ? -8.116  6.590   28.553 1.00 18.17 ? 566 HOH A O     1 
HETATM 2438 O  O     . HOH F 6 .   ? 0.836   -14.313 22.329 1.00 25.85 ? 567 HOH A O     1 
HETATM 2439 O  O     . HOH F 6 .   ? 1.084   -9.311  42.780 1.00 28.40 ? 568 HOH A O     1 
HETATM 2440 O  O     . HOH F 6 .   ? -28.195 -21.430 15.253 1.00 31.20 ? 569 HOH A O     1 
HETATM 2441 O  O     . HOH F 6 .   ? -6.922  -22.433 35.723 1.00 23.06 ? 570 HOH A O     1 
HETATM 2442 O  O     . HOH F 6 .   ? -1.941  6.745   22.774 1.00 26.72 ? 571 HOH A O     1 
HETATM 2443 O  O     . HOH F 6 .   ? -11.281 -3.078  47.446 1.00 35.44 ? 572 HOH A O     1 
HETATM 2444 O  O     . HOH F 6 .   ? -26.726 -18.681 26.731 1.00 28.33 ? 573 HOH A O     1 
HETATM 2445 O  O     . HOH F 6 .   ? -13.738 -31.275 20.241 1.00 31.78 ? 574 HOH A O     1 
HETATM 2446 O  O     . HOH F 6 .   ? -8.305  -22.171 3.704  1.00 29.02 ? 575 HOH A O     1 
HETATM 2447 O  O     . HOH F 6 .   ? -21.938 -14.609 36.572 1.00 25.41 ? 576 HOH A O     1 
HETATM 2448 O  O     . HOH F 6 .   ? 7.276   -14.557 30.961 1.00 25.80 ? 577 HOH A O     1 
HETATM 2449 O  O     . HOH F 6 .   ? -19.698 -29.754 7.445  1.00 35.49 ? 578 HOH A O     1 
HETATM 2450 O  O     . HOH F 6 .   ? -4.374  -27.006 14.722 1.00 35.20 ? 579 HOH A O     1 
HETATM 2451 O  O     . HOH F 6 .   ? -2.116  -25.613 21.919 1.00 37.09 ? 580 HOH A O     1 
HETATM 2452 O  O     . HOH F 6 .   ? -24.144 -24.215 25.750 1.00 30.20 ? 581 HOH A O     1 
HETATM 2453 O  O     . HOH F 6 .   ? -22.660 -3.491  26.452 1.00 15.53 ? 582 HOH A O     1 
HETATM 2454 O  O     . HOH F 6 .   ? -25.565 5.397   21.373 1.00 22.38 ? 583 HOH A O     1 
HETATM 2455 O  O     . HOH F 6 .   ? 3.828   -16.529 27.541 1.00 25.46 ? 584 HOH A O     1 
HETATM 2456 O  O     . HOH F 6 .   ? 4.159   7.194   28.262 1.00 28.80 ? 585 HOH A O     1 
HETATM 2457 O  O     . HOH F 6 .   ? 9.839   -1.721  27.251 1.00 19.98 ? 586 HOH A O     1 
HETATM 2458 O  O     . HOH F 6 .   ? -26.626 -4.406  27.734 1.00 23.07 ? 587 HOH A O     1 
HETATM 2459 O  O     . HOH F 6 .   ? -27.179 0.321   14.670 1.00 35.93 ? 588 HOH A O     1 
HETATM 2460 O  O     . HOH F 6 .   ? 6.600   -10.370 40.079 1.00 30.59 ? 589 HOH A O     1 
HETATM 2461 O  O     . HOH F 6 .   ? -28.695 2.026   16.685 1.00 29.95 ? 590 HOH A O     1 
HETATM 2462 O  O     . HOH F 6 .   ? -3.270  -27.507 12.076 1.00 37.49 ? 591 HOH A O     1 
# 
