data_9DNU
# 
_entry.id   9DNU 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9DNU         pdb_00009dnu 10.2210/pdb9dnu/pdb 
WWPDB D_1000288535 ?            ?                   
# 
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 2025-01-22 ? 
2 'Structure model' 1 1 2025-02-26 ? 
# 
_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' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
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_CSD'          
4  2 'Structure model' '_citation.journal_id_ISSN'         
5  2 'Structure model' '_citation.journal_volume'          
6  2 'Structure model' '_citation.page_first'              
7  2 'Structure model' '_citation.page_last'               
8  2 'Structure model' '_citation.pdbx_database_id_DOI'    
9  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
10 2 'Structure model' '_citation.title'                   
11 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                        9DNU 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-18 
_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           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              arnold@cabm.rutgers.edu 
_pdbx_contact_author.name_first         Eddy 
_pdbx_contact_author.name_last          Arnold 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2612-9622 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Ansari, A.' 1 0000-0003-3398-175X 
'Jadhav, P.' 2 0000-0001-8647-0318 
'Arnold, E.' 3 0000-0003-2612-9622 
'Ruiz, F.X.' 4 0000-0002-0457-0030 
'Wang, J.'   5 0000-0002-4845-4621 
# 
_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            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                1604 
_citation.page_last                 1604 
_citation.title                     
'Design of quinoline SARS-CoV-2 papain-like protease inhibitors as oral antiviral drug candidates.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-56902-x 
_citation.pdbx_database_id_PubMed   39948104 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Jadhav, P.' 1  ?                   
primary 'Liang, X.'  2  ?                   
primary 'Ansari, A.' 3  0000-0003-3398-175X 
primary 'Tan, B.'    4  0000-0001-6295-6962 
primary 'Tan, H.'    5  ?                   
primary 'Li, K.'     6  0000-0002-0825-1934 
primary 'Chi, X.'    7  0009-0003-4853-7931 
primary 'Ford, A.'   8  0000-0001-8531-1243 
primary 'Ruiz, F.X.' 9  0000-0002-0457-0030 
primary 'Arnold, E.' 10 ?                   
primary 'Deng, X.'   11 ?                   
primary 'Wang, J.'   12 0000-0002-4845-4621 
# 
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 'Papain-like protease nsp3' 35943.762 1   3.4.19.12,3.4.22.- ? ? ? 
2 non-polymer syn 
;2-methyl-5-[(1R,5S)-8-methyl-3,8-diazabicyclo[3.2.1]octan-3-yl]-N-{(1R)-1-[(2P)-2-(1-methyl-1H-pyrazol-4-yl)quinolin-4-yl]ethyl}benzamide
;
494.631   1   ?                  ? ? ? 
3 non-polymer syn 'ACETATE ION' 59.044    1   ?                  ? ? ? 
4 non-polymer syn 'ZINC ION' 65.409    8   ?                  ? ? ? 
5 non-polymer syn 'CHLORIDE ION' 35.453    4   ?                  ? ? ? 
6 non-polymer syn 1,2-ETHANEDIOL 62.068    1   ?                  ? ? ? 
7 water       nat water 18.015    248 ?                  ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Non-structural protein 3,nsp3,PL2-PRO,Papain-like proteinase,PL-PRO' 
# 
_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       
;SNAEVRTIKVFTTVDNINLHTQVVDMSMTYGQQFGPTYLDGADVTKIKPHNSHEGKTFYVLPNDDTLRVEAFEYYHTTDP
SFLGRYMSALNHTKKWKYPQVNGLTSIKWADNNCYLATALLTLQQIELKFNPPALQDAYYRARAGEAANFCALILAYCNK
TVGELGDVRETMSYLFQHANLDSCKRVLNVVCKTCGQQQTTLKGVEAVMYMGTLSYEQFKKGVQIPCTCGKQATKYLVQQ
ESPFVMMSAPPAQYELKHGTFTCASEYTGNYQCGHYKHITSKETLYCIDGALLTKSSEYKGPITDVFYKENSYTTTIK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SNAEVRTIKVFTTVDNINLHTQVVDMSMTYGQQFGPTYLDGADVTKIKPHNSHEGKTFYVLPNDDTLRVEAFEYYHTTDP
SFLGRYMSALNHTKKWKYPQVNGLTSIKWADNNCYLATALLTLQQIELKFNPPALQDAYYRARAGEAANFCALILAYCNK
TVGELGDVRETMSYLFQHANLDSCKRVLNVVCKTCGQQQTTLKGVEAVMYMGTLSYEQFKKGVQIPCTCGKQATKYLVQQ
ESPFVMMSAPPAQYELKHGTFTCASEYTGNYQCGHYKHITSKETLYCIDGALLTKSSEYKGPITDVFYKENSYTTTIK
;
_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 
;2-methyl-5-[(1R,5S)-8-methyl-3,8-diazabicyclo[3.2.1]octan-3-yl]-N-{(1R)-1-[(2P)-2-(1-methyl-1H-pyrazol-4-yl)quinolin-4-yl]ethyl}benzamide
;
A1BEG 
3 'ACETATE ION' ACT   
4 'ZINC ION' ZN    
5 'CHLORIDE ION' CL    
6 1,2-ETHANEDIOL EDO   
7 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   ASN n 
1 3   ALA n 
1 4   GLU n 
1 5   VAL n 
1 6   ARG n 
1 7   THR n 
1 8   ILE n 
1 9   LYS n 
1 10  VAL n 
1 11  PHE n 
1 12  THR n 
1 13  THR n 
1 14  VAL n 
1 15  ASP n 
1 16  ASN n 
1 17  ILE n 
1 18  ASN n 
1 19  LEU n 
1 20  HIS n 
1 21  THR n 
1 22  GLN n 
1 23  VAL n 
1 24  VAL n 
1 25  ASP n 
1 26  MET n 
1 27  SER n 
1 28  MET n 
1 29  THR n 
1 30  TYR n 
1 31  GLY n 
1 32  GLN n 
1 33  GLN n 
1 34  PHE n 
1 35  GLY n 
1 36  PRO n 
1 37  THR n 
1 38  TYR n 
1 39  LEU n 
1 40  ASP n 
1 41  GLY n 
1 42  ALA n 
1 43  ASP n 
1 44  VAL n 
1 45  THR n 
1 46  LYS n 
1 47  ILE n 
1 48  LYS n 
1 49  PRO n 
1 50  HIS n 
1 51  ASN n 
1 52  SER n 
1 53  HIS n 
1 54  GLU n 
1 55  GLY n 
1 56  LYS n 
1 57  THR n 
1 58  PHE n 
1 59  TYR n 
1 60  VAL n 
1 61  LEU n 
1 62  PRO n 
1 63  ASN n 
1 64  ASP n 
1 65  ASP n 
1 66  THR n 
1 67  LEU n 
1 68  ARG n 
1 69  VAL n 
1 70  GLU n 
1 71  ALA n 
1 72  PHE n 
1 73  GLU n 
1 74  TYR n 
1 75  TYR n 
1 76  HIS n 
1 77  THR n 
1 78  THR n 
1 79  ASP n 
1 80  PRO n 
1 81  SER n 
1 82  PHE n 
1 83  LEU n 
1 84  GLY n 
1 85  ARG n 
1 86  TYR n 
1 87  MET n 
1 88  SER n 
1 89  ALA n 
1 90  LEU n 
1 91  ASN n 
1 92  HIS n 
1 93  THR n 
1 94  LYS n 
1 95  LYS n 
1 96  TRP n 
1 97  LYS n 
1 98  TYR n 
1 99  PRO n 
1 100 GLN n 
1 101 VAL n 
1 102 ASN n 
1 103 GLY n 
1 104 LEU n 
1 105 THR n 
1 106 SER n 
1 107 ILE n 
1 108 LYS n 
1 109 TRP n 
1 110 ALA n 
1 111 ASP n 
1 112 ASN n 
1 113 ASN n 
1 114 CYS n 
1 115 TYR n 
1 116 LEU n 
1 117 ALA n 
1 118 THR n 
1 119 ALA n 
1 120 LEU n 
1 121 LEU n 
1 122 THR n 
1 123 LEU n 
1 124 GLN n 
1 125 GLN n 
1 126 ILE n 
1 127 GLU n 
1 128 LEU n 
1 129 LYS n 
1 130 PHE n 
1 131 ASN n 
1 132 PRO n 
1 133 PRO n 
1 134 ALA n 
1 135 LEU n 
1 136 GLN n 
1 137 ASP n 
1 138 ALA n 
1 139 TYR n 
1 140 TYR n 
1 141 ARG n 
1 142 ALA n 
1 143 ARG n 
1 144 ALA n 
1 145 GLY n 
1 146 GLU n 
1 147 ALA n 
1 148 ALA n 
1 149 ASN n 
1 150 PHE n 
1 151 CYS n 
1 152 ALA n 
1 153 LEU n 
1 154 ILE n 
1 155 LEU n 
1 156 ALA n 
1 157 TYR n 
1 158 CYS n 
1 159 ASN n 
1 160 LYS n 
1 161 THR n 
1 162 VAL n 
1 163 GLY n 
1 164 GLU n 
1 165 LEU n 
1 166 GLY n 
1 167 ASP n 
1 168 VAL n 
1 169 ARG n 
1 170 GLU n 
1 171 THR n 
1 172 MET n 
1 173 SER n 
1 174 TYR n 
1 175 LEU n 
1 176 PHE n 
1 177 GLN n 
1 178 HIS n 
1 179 ALA n 
1 180 ASN n 
1 181 LEU n 
1 182 ASP n 
1 183 SER n 
1 184 CYS n 
1 185 LYS n 
1 186 ARG n 
1 187 VAL n 
1 188 LEU n 
1 189 ASN n 
1 190 VAL n 
1 191 VAL n 
1 192 CYS n 
1 193 LYS n 
1 194 THR n 
1 195 CYS n 
1 196 GLY n 
1 197 GLN n 
1 198 GLN n 
1 199 GLN n 
1 200 THR n 
1 201 THR n 
1 202 LEU n 
1 203 LYS n 
1 204 GLY n 
1 205 VAL n 
1 206 GLU n 
1 207 ALA n 
1 208 VAL n 
1 209 MET n 
1 210 TYR n 
1 211 MET n 
1 212 GLY n 
1 213 THR n 
1 214 LEU n 
1 215 SER n 
1 216 TYR n 
1 217 GLU n 
1 218 GLN n 
1 219 PHE n 
1 220 LYS n 
1 221 LYS n 
1 222 GLY n 
1 223 VAL n 
1 224 GLN n 
1 225 ILE n 
1 226 PRO n 
1 227 CYS n 
1 228 THR n 
1 229 CYS n 
1 230 GLY n 
1 231 LYS n 
1 232 GLN n 
1 233 ALA n 
1 234 THR n 
1 235 LYS n 
1 236 TYR n 
1 237 LEU n 
1 238 VAL n 
1 239 GLN n 
1 240 GLN n 
1 241 GLU n 
1 242 SER n 
1 243 PRO n 
1 244 PHE n 
1 245 VAL n 
1 246 MET n 
1 247 MET n 
1 248 SER n 
1 249 ALA n 
1 250 PRO n 
1 251 PRO n 
1 252 ALA n 
1 253 GLN n 
1 254 TYR n 
1 255 GLU n 
1 256 LEU n 
1 257 LYS n 
1 258 HIS n 
1 259 GLY n 
1 260 THR n 
1 261 PHE n 
1 262 THR n 
1 263 CYS n 
1 264 ALA n 
1 265 SER n 
1 266 GLU n 
1 267 TYR n 
1 268 THR n 
1 269 GLY n 
1 270 ASN n 
1 271 TYR n 
1 272 GLN n 
1 273 CYS n 
1 274 GLY n 
1 275 HIS n 
1 276 TYR n 
1 277 LYS n 
1 278 HIS n 
1 279 ILE n 
1 280 THR n 
1 281 SER n 
1 282 LYS n 
1 283 GLU n 
1 284 THR n 
1 285 LEU n 
1 286 TYR n 
1 287 CYS n 
1 288 ILE n 
1 289 ASP n 
1 290 GLY n 
1 291 ALA n 
1 292 LEU n 
1 293 LEU n 
1 294 THR n 
1 295 LYS n 
1 296 SER n 
1 297 SER n 
1 298 GLU n 
1 299 TYR n 
1 300 LYS n 
1 301 GLY n 
1 302 PRO n 
1 303 ILE n 
1 304 THR n 
1 305 ASP n 
1 306 VAL n 
1 307 PHE n 
1 308 TYR n 
1 309 LYS n 
1 310 GLU n 
1 311 ASN n 
1 312 SER n 
1 313 TYR n 
1 314 THR n 
1 315 THR n 
1 316 THR n 
1 317 ILE n 
1 318 LYS 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                   318 
_entity_src_gen.gene_src_common_name               'SARS-CoV-2, 2019-nCoV, COVID-19 virus' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BEG non-polymer         . 
;2-methyl-5-[(1R,5S)-8-methyl-3,8-diazabicyclo[3.2.1]octan-3-yl]-N-{(1R)-1-[(2P)-2-(1-methyl-1H-pyrazol-4-yl)quinolin-4-yl]ethyl}benzamide
;
?                 'C30 H34 N6 O'   494.631 
ACT   non-polymer         . 'ACETATE ION' ?                 'C2 H3 O2 -1'    59.044  
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  
CYS   'L-peptide linking' y CYSTEINE ?                 'C3 H7 N O2 S'   121.158 
EDO   non-polymer         . 1,2-ETHANEDIOL 'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
GLN   'L-peptide linking' y GLUTAMINE ?                 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ?                 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE ?                 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE ?                 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER ?                 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE ?                 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE ?                 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE ?                 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE ?                 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE ?                 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE ?                 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE ?                 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE ?                 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ?                 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE ?                 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE ?                 'C5 H11 N O2'    117.146 
ZN    non-polymer         . 'ZINC ION' ?                 'Zn 2'           65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   -2  ?   ?   ?   A . n 
A 1 2   ASN 2   -1  ?   ?   ?   A . n 
A 1 3   ALA 3   0   ?   ?   ?   A . n 
A 1 4   GLU 4   1   ?   ?   ?   A . n 
A 1 5   VAL 5   2   ?   ?   ?   A . n 
A 1 6   ARG 6   3   ?   ?   ?   A . n 
A 1 7   THR 7   4   4   THR THR A . n 
A 1 8   ILE 8   5   5   ILE ILE A . n 
A 1 9   LYS 9   6   6   LYS LYS A . n 
A 1 10  VAL 10  7   7   VAL VAL A . n 
A 1 11  PHE 11  8   8   PHE PHE A . n 
A 1 12  THR 12  9   9   THR THR A . n 
A 1 13  THR 13  10  10  THR THR A . n 
A 1 14  VAL 14  11  11  VAL VAL A . n 
A 1 15  ASP 15  12  12  ASP ASP A . n 
A 1 16  ASN 16  13  13  ASN ASN A . n 
A 1 17  ILE 17  14  14  ILE ILE A . n 
A 1 18  ASN 18  15  15  ASN ASN A . n 
A 1 19  LEU 19  16  16  LEU LEU A . n 
A 1 20  HIS 20  17  17  HIS HIS A . n 
A 1 21  THR 21  18  18  THR THR A . n 
A 1 22  GLN 22  19  19  GLN GLN A . n 
A 1 23  VAL 23  20  20  VAL VAL A . n 
A 1 24  VAL 24  21  21  VAL VAL A . n 
A 1 25  ASP 25  22  22  ASP ASP A . n 
A 1 26  MET 26  23  23  MET MET A . n 
A 1 27  SER 27  24  24  SER SER A . n 
A 1 28  MET 28  25  25  MET MET A . n 
A 1 29  THR 29  26  26  THR THR A . n 
A 1 30  TYR 30  27  27  TYR TYR A . n 
A 1 31  GLY 31  28  28  GLY GLY A . n 
A 1 32  GLN 32  29  29  GLN GLN A . n 
A 1 33  GLN 33  30  30  GLN GLN A . n 
A 1 34  PHE 34  31  31  PHE PHE A . n 
A 1 35  GLY 35  32  32  GLY GLY A . n 
A 1 36  PRO 36  33  33  PRO PRO A . n 
A 1 37  THR 37  34  34  THR THR A . n 
A 1 38  TYR 38  35  35  TYR TYR A . n 
A 1 39  LEU 39  36  36  LEU LEU A . n 
A 1 40  ASP 40  37  37  ASP ASP A . n 
A 1 41  GLY 41  38  38  GLY GLY A . n 
A 1 42  ALA 42  39  39  ALA ALA A . n 
A 1 43  ASP 43  40  40  ASP ASP A . n 
A 1 44  VAL 44  41  41  VAL VAL A . n 
A 1 45  THR 45  42  42  THR THR A . n 
A 1 46  LYS 46  43  43  LYS LYS A . n 
A 1 47  ILE 47  44  44  ILE ILE A . n 
A 1 48  LYS 48  45  45  LYS LYS A . n 
A 1 49  PRO 49  46  46  PRO PRO A . n 
A 1 50  HIS 50  47  47  HIS HIS A . n 
A 1 51  ASN 51  48  48  ASN ASN A . n 
A 1 52  SER 52  49  49  SER SER A . n 
A 1 53  HIS 53  50  50  HIS HIS A . n 
A 1 54  GLU 54  51  51  GLU GLU A . n 
A 1 55  GLY 55  52  52  GLY GLY A . n 
A 1 56  LYS 56  53  53  LYS LYS A . n 
A 1 57  THR 57  54  54  THR THR A . n 
A 1 58  PHE 58  55  55  PHE PHE A . n 
A 1 59  TYR 59  56  56  TYR TYR A . n 
A 1 60  VAL 60  57  57  VAL VAL A . n 
A 1 61  LEU 61  58  58  LEU LEU A . n 
A 1 62  PRO 62  59  59  PRO PRO A . n 
A 1 63  ASN 63  60  60  ASN ASN A . n 
A 1 64  ASP 64  61  61  ASP ASP A . n 
A 1 65  ASP 65  62  62  ASP ASP A . n 
A 1 66  THR 66  63  63  THR THR A . n 
A 1 67  LEU 67  64  64  LEU LEU A . n 
A 1 68  ARG 68  65  65  ARG ARG A . n 
A 1 69  VAL 69  66  66  VAL VAL A . n 
A 1 70  GLU 70  67  67  GLU GLU A . n 
A 1 71  ALA 71  68  68  ALA ALA A . n 
A 1 72  PHE 72  69  69  PHE PHE A . n 
A 1 73  GLU 73  70  70  GLU GLU A . n 
A 1 74  TYR 74  71  71  TYR TYR A . n 
A 1 75  TYR 75  72  72  TYR TYR A . n 
A 1 76  HIS 76  73  73  HIS HIS A . n 
A 1 77  THR 77  74  74  THR THR A . n 
A 1 78  THR 78  75  75  THR THR A . n 
A 1 79  ASP 79  76  76  ASP ASP A . n 
A 1 80  PRO 80  77  77  PRO PRO A . n 
A 1 81  SER 81  78  78  SER SER A . n 
A 1 82  PHE 82  79  79  PHE PHE A . n 
A 1 83  LEU 83  80  80  LEU LEU A . n 
A 1 84  GLY 84  81  81  GLY GLY A . n 
A 1 85  ARG 85  82  82  ARG ARG A . n 
A 1 86  TYR 86  83  83  TYR TYR A . n 
A 1 87  MET 87  84  84  MET MET A . n 
A 1 88  SER 88  85  85  SER SER A . n 
A 1 89  ALA 89  86  86  ALA ALA A . n 
A 1 90  LEU 90  87  87  LEU LEU A . n 
A 1 91  ASN 91  88  88  ASN ASN A . n 
A 1 92  HIS 92  89  89  HIS HIS A . n 
A 1 93  THR 93  90  90  THR THR A . n 
A 1 94  LYS 94  91  91  LYS LYS A . n 
A 1 95  LYS 95  92  92  LYS LYS A . n 
A 1 96  TRP 96  93  93  TRP TRP A . n 
A 1 97  LYS 97  94  94  LYS LYS A . n 
A 1 98  TYR 98  95  95  TYR TYR A . n 
A 1 99  PRO 99  96  96  PRO PRO A . n 
A 1 100 GLN 100 97  97  GLN GLN A . n 
A 1 101 VAL 101 98  98  VAL VAL A . n 
A 1 102 ASN 102 99  99  ASN ASN A . n 
A 1 103 GLY 103 100 100 GLY GLY A . n 
A 1 104 LEU 104 101 101 LEU LEU A . n 
A 1 105 THR 105 102 102 THR THR A . n 
A 1 106 SER 106 103 103 SER SER A . n 
A 1 107 ILE 107 104 104 ILE ILE A . n 
A 1 108 LYS 108 105 105 LYS LYS A . n 
A 1 109 TRP 109 106 106 TRP TRP A . n 
A 1 110 ALA 110 107 107 ALA ALA A . n 
A 1 111 ASP 111 108 108 ASP ASP A . n 
A 1 112 ASN 112 109 109 ASN ASN A . n 
A 1 113 ASN 113 110 110 ASN ASN A . n 
A 1 114 CYS 114 111 111 CYS CYS A . n 
A 1 115 TYR 115 112 112 TYR TYR A . n 
A 1 116 LEU 116 113 113 LEU LEU A . n 
A 1 117 ALA 117 114 114 ALA ALA A . n 
A 1 118 THR 118 115 115 THR THR A . n 
A 1 119 ALA 119 116 116 ALA ALA A . n 
A 1 120 LEU 120 117 117 LEU LEU A . n 
A 1 121 LEU 121 118 118 LEU LEU A . n 
A 1 122 THR 122 119 119 THR THR A . n 
A 1 123 LEU 123 120 120 LEU LEU A . n 
A 1 124 GLN 124 121 121 GLN GLN A . n 
A 1 125 GLN 125 122 122 GLN GLN A . n 
A 1 126 ILE 126 123 123 ILE ILE A . n 
A 1 127 GLU 127 124 124 GLU GLU A . n 
A 1 128 LEU 128 125 125 LEU LEU A . n 
A 1 129 LYS 129 126 126 LYS LYS A . n 
A 1 130 PHE 130 127 127 PHE PHE A . n 
A 1 131 ASN 131 128 128 ASN ASN A . n 
A 1 132 PRO 132 129 129 PRO PRO A . n 
A 1 133 PRO 133 130 130 PRO PRO A . n 
A 1 134 ALA 134 131 131 ALA ALA A . n 
A 1 135 LEU 135 132 132 LEU LEU A . n 
A 1 136 GLN 136 133 133 GLN GLN A . n 
A 1 137 ASP 137 134 134 ASP ASP A . n 
A 1 138 ALA 138 135 135 ALA ALA A . n 
A 1 139 TYR 139 136 136 TYR TYR A . n 
A 1 140 TYR 140 137 137 TYR TYR A . n 
A 1 141 ARG 141 138 138 ARG ARG A . n 
A 1 142 ALA 142 139 139 ALA ALA A . n 
A 1 143 ARG 143 140 140 ARG ARG A . n 
A 1 144 ALA 144 141 141 ALA ALA A . n 
A 1 145 GLY 145 142 142 GLY GLY A . n 
A 1 146 GLU 146 143 143 GLU GLU A . n 
A 1 147 ALA 147 144 144 ALA ALA A . n 
A 1 148 ALA 148 145 145 ALA ALA A . n 
A 1 149 ASN 149 146 146 ASN ASN A . n 
A 1 150 PHE 150 147 147 PHE PHE A . n 
A 1 151 CYS 151 148 148 CYS CYS A . n 
A 1 152 ALA 152 149 149 ALA ALA A . n 
A 1 153 LEU 153 150 150 LEU LEU A . n 
A 1 154 ILE 154 151 151 ILE ILE A . n 
A 1 155 LEU 155 152 152 LEU LEU A . n 
A 1 156 ALA 156 153 153 ALA ALA A . n 
A 1 157 TYR 157 154 154 TYR TYR A . n 
A 1 158 CYS 158 155 155 CYS CYS A . n 
A 1 159 ASN 159 156 156 ASN ASN A . n 
A 1 160 LYS 160 157 157 LYS LYS A . n 
A 1 161 THR 161 158 158 THR THR A . n 
A 1 162 VAL 162 159 159 VAL VAL A . n 
A 1 163 GLY 163 160 160 GLY GLY A . n 
A 1 164 GLU 164 161 161 GLU GLU A . n 
A 1 165 LEU 165 162 162 LEU LEU A . n 
A 1 166 GLY 166 163 163 GLY GLY A . n 
A 1 167 ASP 167 164 164 ASP ASP A . n 
A 1 168 VAL 168 165 165 VAL VAL A . n 
A 1 169 ARG 169 166 166 ARG ARG A . n 
A 1 170 GLU 170 167 167 GLU GLU A . n 
A 1 171 THR 171 168 168 THR THR A . n 
A 1 172 MET 172 169 169 MET MET A . n 
A 1 173 SER 173 170 170 SER SER A . n 
A 1 174 TYR 174 171 171 TYR TYR A . n 
A 1 175 LEU 175 172 172 LEU LEU A . n 
A 1 176 PHE 176 173 173 PHE PHE A . n 
A 1 177 GLN 177 174 174 GLN GLN A . n 
A 1 178 HIS 178 175 175 HIS HIS A . n 
A 1 179 ALA 179 176 176 ALA ALA A . n 
A 1 180 ASN 180 177 177 ASN ASN A . n 
A 1 181 LEU 181 178 178 LEU LEU A . n 
A 1 182 ASP 182 179 179 ASP ASP A . n 
A 1 183 SER 183 180 180 SER SER A . n 
A 1 184 CYS 184 181 181 CYS CYS A . n 
A 1 185 LYS 185 182 182 LYS LYS A . n 
A 1 186 ARG 186 183 183 ARG ARG A . n 
A 1 187 VAL 187 184 184 VAL VAL A . n 
A 1 188 LEU 188 185 185 LEU LEU A . n 
A 1 189 ASN 189 186 186 ASN ASN A . n 
A 1 190 VAL 190 187 187 VAL VAL A . n 
A 1 191 VAL 191 188 188 VAL VAL A . n 
A 1 192 CYS 192 189 189 CYS CYS A . n 
A 1 193 LYS 193 190 190 LYS LYS A . n 
A 1 194 THR 194 191 191 THR THR A . n 
A 1 195 CYS 195 192 192 CYS CYS A . n 
A 1 196 GLY 196 193 193 GLY GLY A . n 
A 1 197 GLN 197 194 194 GLN GLN A . n 
A 1 198 GLN 198 195 195 GLN GLN A . n 
A 1 199 GLN 199 196 196 GLN GLN A . n 
A 1 200 THR 200 197 197 THR THR A . n 
A 1 201 THR 201 198 198 THR THR A . n 
A 1 202 LEU 202 199 199 LEU LEU A . n 
A 1 203 LYS 203 200 200 LYS LYS A . n 
A 1 204 GLY 204 201 201 GLY GLY A . n 
A 1 205 VAL 205 202 202 VAL VAL A . n 
A 1 206 GLU 206 203 203 GLU GLU A . n 
A 1 207 ALA 207 204 204 ALA ALA A . n 
A 1 208 VAL 208 205 205 VAL VAL A . n 
A 1 209 MET 209 206 206 MET MET A . n 
A 1 210 TYR 210 207 207 TYR TYR A . n 
A 1 211 MET 211 208 208 MET MET A . n 
A 1 212 GLY 212 209 209 GLY GLY A . n 
A 1 213 THR 213 210 210 THR THR A . n 
A 1 214 LEU 214 211 211 LEU LEU A . n 
A 1 215 SER 215 212 212 SER SER A . n 
A 1 216 TYR 216 213 213 TYR TYR A . n 
A 1 217 GLU 217 214 214 GLU GLU A . n 
A 1 218 GLN 218 215 215 GLN GLN A . n 
A 1 219 PHE 219 216 216 PHE PHE A . n 
A 1 220 LYS 220 217 217 LYS LYS A . n 
A 1 221 LYS 221 218 218 LYS LYS A . n 
A 1 222 GLY 222 219 219 GLY GLY A . n 
A 1 223 VAL 223 220 220 VAL VAL A . n 
A 1 224 GLN 224 221 221 GLN GLN A . n 
A 1 225 ILE 225 222 222 ILE ILE A . n 
A 1 226 PRO 226 223 223 PRO PRO A . n 
A 1 227 CYS 227 224 224 CYS CYS A . n 
A 1 228 THR 228 225 225 THR THR A . n 
A 1 229 CYS 229 226 226 CYS CYS A . n 
A 1 230 GLY 230 227 227 GLY GLY A . n 
A 1 231 LYS 231 228 ?   ?   ?   A . n 
A 1 232 GLN 232 229 229 GLN GLN A . n 
A 1 233 ALA 233 230 230 ALA ALA A . n 
A 1 234 THR 234 231 231 THR THR A . n 
A 1 235 LYS 235 232 232 LYS LYS A . n 
A 1 236 TYR 236 233 233 TYR TYR A . n 
A 1 237 LEU 237 234 234 LEU LEU A . n 
A 1 238 VAL 238 235 235 VAL VAL A . n 
A 1 239 GLN 239 236 236 GLN GLN A . n 
A 1 240 GLN 240 237 237 GLN GLN A . n 
A 1 241 GLU 241 238 238 GLU GLU A . n 
A 1 242 SER 242 239 239 SER SER A . n 
A 1 243 PRO 243 240 240 PRO PRO A . n 
A 1 244 PHE 244 241 241 PHE PHE A . n 
A 1 245 VAL 245 242 242 VAL VAL A . n 
A 1 246 MET 246 243 243 MET MET A . n 
A 1 247 MET 247 244 244 MET MET A . n 
A 1 248 SER 248 245 245 SER SER A . n 
A 1 249 ALA 249 246 246 ALA ALA A . n 
A 1 250 PRO 250 247 247 PRO PRO A . n 
A 1 251 PRO 251 248 248 PRO PRO A . n 
A 1 252 ALA 252 249 249 ALA ALA A . n 
A 1 253 GLN 253 250 250 GLN GLN A . n 
A 1 254 TYR 254 251 251 TYR TYR A . n 
A 1 255 GLU 255 252 252 GLU GLU A . n 
A 1 256 LEU 256 253 253 LEU LEU A . n 
A 1 257 LYS 257 254 254 LYS LYS A . n 
A 1 258 HIS 258 255 255 HIS HIS A . n 
A 1 259 GLY 259 256 256 GLY GLY A . n 
A 1 260 THR 260 257 257 THR THR A . n 
A 1 261 PHE 261 258 258 PHE PHE A . n 
A 1 262 THR 262 259 259 THR THR A . n 
A 1 263 CYS 263 260 260 CYS CYS A . n 
A 1 264 ALA 264 261 261 ALA ALA A . n 
A 1 265 SER 265 262 262 SER SER A . n 
A 1 266 GLU 266 263 263 GLU GLU A . n 
A 1 267 TYR 267 264 264 TYR TYR A . n 
A 1 268 THR 268 265 265 THR THR A . n 
A 1 269 GLY 269 266 266 GLY GLY A . n 
A 1 270 ASN 270 267 267 ASN ASN A . n 
A 1 271 TYR 271 268 268 TYR TYR A . n 
A 1 272 GLN 272 269 269 GLN GLN A . n 
A 1 273 CYS 273 270 270 CYS CYS A . n 
A 1 274 GLY 274 271 271 GLY GLY A . n 
A 1 275 HIS 275 272 272 HIS HIS A . n 
A 1 276 TYR 276 273 273 TYR TYR A . n 
A 1 277 LYS 277 274 274 LYS LYS A . n 
A 1 278 HIS 278 275 275 HIS HIS A . n 
A 1 279 ILE 279 276 276 ILE ILE A . n 
A 1 280 THR 280 277 277 THR THR A . n 
A 1 281 SER 281 278 278 SER SER A . n 
A 1 282 LYS 282 279 279 LYS LYS A . n 
A 1 283 GLU 283 280 280 GLU GLU A . n 
A 1 284 THR 284 281 281 THR THR A . n 
A 1 285 LEU 285 282 282 LEU LEU A . n 
A 1 286 TYR 286 283 283 TYR TYR A . n 
A 1 287 CYS 287 284 284 CYS CYS A . n 
A 1 288 ILE 288 285 285 ILE ILE A . n 
A 1 289 ASP 289 286 286 ASP ASP A . n 
A 1 290 GLY 290 287 287 GLY GLY A . n 
A 1 291 ALA 291 288 288 ALA ALA A . n 
A 1 292 LEU 292 289 289 LEU LEU A . n 
A 1 293 LEU 293 290 290 LEU LEU A . n 
A 1 294 THR 294 291 291 THR THR A . n 
A 1 295 LYS 295 292 292 LYS LYS A . n 
A 1 296 SER 296 293 293 SER SER A . n 
A 1 297 SER 297 294 294 SER SER A . n 
A 1 298 GLU 298 295 295 GLU GLU A . n 
A 1 299 TYR 299 296 296 TYR TYR A . n 
A 1 300 LYS 300 297 297 LYS LYS A . n 
A 1 301 GLY 301 298 298 GLY GLY A . n 
A 1 302 PRO 302 299 299 PRO PRO A . n 
A 1 303 ILE 303 300 300 ILE ILE A . n 
A 1 304 THR 304 301 301 THR THR A . n 
A 1 305 ASP 305 302 302 ASP ASP A . n 
A 1 306 VAL 306 303 303 VAL VAL A . n 
A 1 307 PHE 307 304 304 PHE PHE A . n 
A 1 308 TYR 308 305 305 TYR TYR A . n 
A 1 309 LYS 309 306 306 LYS LYS A . n 
A 1 310 GLU 310 307 307 GLU GLU A . n 
A 1 311 ASN 311 308 308 ASN ASN A . n 
A 1 312 SER 312 309 309 SER SER A . n 
A 1 313 TYR 313 310 310 TYR TYR A . n 
A 1 314 THR 314 311 311 THR THR A . n 
A 1 315 THR 315 312 312 THR THR A . n 
A 1 316 THR 316 313 313 THR THR A . n 
A 1 317 ILE 317 314 314 ILE ILE A . n 
A 1 318 LYS 318 315 315 LYS LYS A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BEG 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BEG 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 A1BEG 1   401 401 A1BEG J31 A . 
C 3 ACT   1   402 402 ACT   ACT A . 
D 4 ZN    1   403 1   ZN    ZN  A . 
E 4 ZN    1   404 4   ZN    ZN  A . 
F 4 ZN    1   405 7   ZN    ZN  A . 
G 4 ZN    1   406 9   ZN    ZN  A . 
H 4 ZN    1   407 11  ZN    ZN  A . 
I 4 ZN    1   408 12  ZN    ZN  A . 
J 4 ZN    1   409 13  ZN    ZN  A . 
K 4 ZN    1   410 14  ZN    ZN  A . 
L 5 CL    1   411 1   CL    CL  A . 
M 5 CL    1   412 2   CL    CL  A . 
N 5 CL    1   413 3   CL    CL  A . 
O 5 CL    1   414 5   CL    CL  A . 
P 6 EDO   1   415 310 EDO   EDO A . 
Q 7 HOH   1   501 230 HOH   HOH A . 
Q 7 HOH   2   502 36  HOH   HOH A . 
Q 7 HOH   3   503 191 HOH   HOH A . 
Q 7 HOH   4   504 164 HOH   HOH A . 
Q 7 HOH   5   505 214 HOH   HOH A . 
Q 7 HOH   6   506 38  HOH   HOH A . 
Q 7 HOH   7   507 103 HOH   HOH A . 
Q 7 HOH   8   508 121 HOH   HOH A . 
Q 7 HOH   9   509 79  HOH   HOH A . 
Q 7 HOH   10  510 204 HOH   HOH A . 
Q 7 HOH   11  511 3   HOH   HOH A . 
Q 7 HOH   12  512 21  HOH   HOH A . 
Q 7 HOH   13  513 26  HOH   HOH A . 
Q 7 HOH   14  514 44  HOH   HOH A . 
Q 7 HOH   15  515 288 HOH   HOH A . 
Q 7 HOH   16  516 43  HOH   HOH A . 
Q 7 HOH   17  517 199 HOH   HOH A . 
Q 7 HOH   18  518 15  HOH   HOH A . 
Q 7 HOH   19  519 68  HOH   HOH A . 
Q 7 HOH   20  520 176 HOH   HOH A . 
Q 7 HOH   21  521 59  HOH   HOH A . 
Q 7 HOH   22  522 1   HOH   HOH A . 
Q 7 HOH   23  523 187 HOH   HOH A . 
Q 7 HOH   24  524 262 HOH   HOH A . 
Q 7 HOH   25  525 34  HOH   HOH A . 
Q 7 HOH   26  526 56  HOH   HOH A . 
Q 7 HOH   27  527 127 HOH   HOH A . 
Q 7 HOH   28  528 290 HOH   HOH A . 
Q 7 HOH   29  529 41  HOH   HOH A . 
Q 7 HOH   30  530 215 HOH   HOH A . 
Q 7 HOH   31  531 186 HOH   HOH A . 
Q 7 HOH   32  532 169 HOH   HOH A . 
Q 7 HOH   33  533 273 HOH   HOH A . 
Q 7 HOH   34  534 183 HOH   HOH A . 
Q 7 HOH   35  535 91  HOH   HOH A . 
Q 7 HOH   36  536 47  HOH   HOH A . 
Q 7 HOH   37  537 73  HOH   HOH A . 
Q 7 HOH   38  538 194 HOH   HOH A . 
Q 7 HOH   39  539 67  HOH   HOH A . 
Q 7 HOH   40  540 4   HOH   HOH A . 
Q 7 HOH   41  541 76  HOH   HOH A . 
Q 7 HOH   42  542 63  HOH   HOH A . 
Q 7 HOH   43  543 138 HOH   HOH A . 
Q 7 HOH   44  544 154 HOH   HOH A . 
Q 7 HOH   45  545 185 HOH   HOH A . 
Q 7 HOH   46  546 227 HOH   HOH A . 
Q 7 HOH   47  547 39  HOH   HOH A . 
Q 7 HOH   48  548 42  HOH   HOH A . 
Q 7 HOH   49  549 46  HOH   HOH A . 
Q 7 HOH   50  550 50  HOH   HOH A . 
Q 7 HOH   51  551 153 HOH   HOH A . 
Q 7 HOH   52  552 10  HOH   HOH A . 
Q 7 HOH   53  553 52  HOH   HOH A . 
Q 7 HOH   54  554 49  HOH   HOH A . 
Q 7 HOH   55  555 25  HOH   HOH A . 
Q 7 HOH   56  556 173 HOH   HOH A . 
Q 7 HOH   57  557 112 HOH   HOH A . 
Q 7 HOH   58  558 45  HOH   HOH A . 
Q 7 HOH   59  559 57  HOH   HOH A . 
Q 7 HOH   60  560 105 HOH   HOH A . 
Q 7 HOH   61  561 87  HOH   HOH A . 
Q 7 HOH   62  562 269 HOH   HOH A . 
Q 7 HOH   63  563 223 HOH   HOH A . 
Q 7 HOH   64  564 118 HOH   HOH A . 
Q 7 HOH   65  565 40  HOH   HOH A . 
Q 7 HOH   66  566 297 HOH   HOH A . 
Q 7 HOH   67  567 74  HOH   HOH A . 
Q 7 HOH   68  568 28  HOH   HOH A . 
Q 7 HOH   69  569 238 HOH   HOH A . 
Q 7 HOH   70  570 95  HOH   HOH A . 
Q 7 HOH   71  571 61  HOH   HOH A . 
Q 7 HOH   72  572 146 HOH   HOH A . 
Q 7 HOH   73  573 106 HOH   HOH A . 
Q 7 HOH   74  574 189 HOH   HOH A . 
Q 7 HOH   75  575 89  HOH   HOH A . 
Q 7 HOH   76  576 53  HOH   HOH A . 
Q 7 HOH   77  577 72  HOH   HOH A . 
Q 7 HOH   78  578 160 HOH   HOH A . 
Q 7 HOH   79  579 98  HOH   HOH A . 
Q 7 HOH   80  580 64  HOH   HOH A . 
Q 7 HOH   81  581 80  HOH   HOH A . 
Q 7 HOH   82  582 286 HOH   HOH A . 
Q 7 HOH   83  583 60  HOH   HOH A . 
Q 7 HOH   84  584 58  HOH   HOH A . 
Q 7 HOH   85  585 208 HOH   HOH A . 
Q 7 HOH   86  586 90  HOH   HOH A . 
Q 7 HOH   87  587 30  HOH   HOH A . 
Q 7 HOH   88  588 130 HOH   HOH A . 
Q 7 HOH   89  589 197 HOH   HOH A . 
Q 7 HOH   90  590 256 HOH   HOH A . 
Q 7 HOH   91  591 170 HOH   HOH A . 
Q 7 HOH   92  592 65  HOH   HOH A . 
Q 7 HOH   93  593 308 HOH   HOH A . 
Q 7 HOH   94  594 129 HOH   HOH A . 
Q 7 HOH   95  595 69  HOH   HOH A . 
Q 7 HOH   96  596 188 HOH   HOH A . 
Q 7 HOH   97  597 102 HOH   HOH A . 
Q 7 HOH   98  598 243 HOH   HOH A . 
Q 7 HOH   99  599 113 HOH   HOH A . 
Q 7 HOH   100 600 218 HOH   HOH A . 
Q 7 HOH   101 601 174 HOH   HOH A . 
Q 7 HOH   102 602 241 HOH   HOH A . 
Q 7 HOH   103 603 161 HOH   HOH A . 
Q 7 HOH   104 604 254 HOH   HOH A . 
Q 7 HOH   105 605 175 HOH   HOH A . 
Q 7 HOH   106 606 190 HOH   HOH A . 
Q 7 HOH   107 607 116 HOH   HOH A . 
Q 7 HOH   108 608 152 HOH   HOH A . 
Q 7 HOH   109 609 307 HOH   HOH A . 
Q 7 HOH   110 610 22  HOH   HOH A . 
Q 7 HOH   111 611 27  HOH   HOH A . 
Q 7 HOH   112 612 184 HOH   HOH A . 
Q 7 HOH   113 613 9   HOH   HOH A . 
Q 7 HOH   114 614 196 HOH   HOH A . 
Q 7 HOH   115 615 96  HOH   HOH A . 
Q 7 HOH   116 616 134 HOH   HOH A . 
Q 7 HOH   117 617 225 HOH   HOH A . 
Q 7 HOH   118 618 81  HOH   HOH A . 
Q 7 HOH   119 619 278 HOH   HOH A . 
Q 7 HOH   120 620 198 HOH   HOH A . 
Q 7 HOH   121 621 84  HOH   HOH A . 
Q 7 HOH   122 622 37  HOH   HOH A . 
Q 7 HOH   123 623 62  HOH   HOH A . 
Q 7 HOH   124 624 104 HOH   HOH A . 
Q 7 HOH   125 625 111 HOH   HOH A . 
Q 7 HOH   126 626 277 HOH   HOH A . 
Q 7 HOH   127 627 122 HOH   HOH A . 
Q 7 HOH   128 628 140 HOH   HOH A . 
Q 7 HOH   129 629 82  HOH   HOH A . 
Q 7 HOH   130 630 171 HOH   HOH A . 
Q 7 HOH   131 631 180 HOH   HOH A . 
Q 7 HOH   132 632 259 HOH   HOH A . 
Q 7 HOH   133 633 18  HOH   HOH A . 
Q 7 HOH   134 634 51  HOH   HOH A . 
Q 7 HOH   135 635 83  HOH   HOH A . 
Q 7 HOH   136 636 110 HOH   HOH A . 
Q 7 HOH   137 637 123 HOH   HOH A . 
Q 7 HOH   138 638 295 HOH   HOH A . 
Q 7 HOH   139 639 137 HOH   HOH A . 
Q 7 HOH   140 640 260 HOH   HOH A . 
Q 7 HOH   141 641 33  HOH   HOH A . 
Q 7 HOH   142 642 78  HOH   HOH A . 
Q 7 HOH   143 643 205 HOH   HOH A . 
Q 7 HOH   144 644 305 HOH   HOH A . 
Q 7 HOH   145 645 8   HOH   HOH A . 
Q 7 HOH   146 646 155 HOH   HOH A . 
Q 7 HOH   147 647 133 HOH   HOH A . 
Q 7 HOH   148 648 280 HOH   HOH A . 
Q 7 HOH   149 649 210 HOH   HOH A . 
Q 7 HOH   150 650 294 HOH   HOH A . 
Q 7 HOH   151 651 206 HOH   HOH A . 
Q 7 HOH   152 652 193 HOH   HOH A . 
Q 7 HOH   153 653 213 HOH   HOH A . 
Q 7 HOH   154 654 221 HOH   HOH A . 
Q 7 HOH   155 655 88  HOH   HOH A . 
Q 7 HOH   156 656 268 HOH   HOH A . 
Q 7 HOH   157 657 35  HOH   HOH A . 
Q 7 HOH   158 658 12  HOH   HOH A . 
Q 7 HOH   159 659 109 HOH   HOH A . 
Q 7 HOH   160 660 48  HOH   HOH A . 
Q 7 HOH   161 661 132 HOH   HOH A . 
Q 7 HOH   162 662 179 HOH   HOH A . 
Q 7 HOH   163 663 284 HOH   HOH A . 
Q 7 HOH   164 664 270 HOH   HOH A . 
Q 7 HOH   165 665 168 HOH   HOH A . 
Q 7 HOH   166 666 258 HOH   HOH A . 
Q 7 HOH   167 667 234 HOH   HOH A . 
Q 7 HOH   168 668 266 HOH   HOH A . 
Q 7 HOH   169 669 165 HOH   HOH A . 
Q 7 HOH   170 670 139 HOH   HOH A . 
Q 7 HOH   171 671 300 HOH   HOH A . 
Q 7 HOH   172 672 128 HOH   HOH A . 
Q 7 HOH   173 673 289 HOH   HOH A . 
Q 7 HOH   174 674 101 HOH   HOH A . 
Q 7 HOH   175 675 29  HOH   HOH A . 
Q 7 HOH   176 676 85  HOH   HOH A . 
Q 7 HOH   177 677 141 HOH   HOH A . 
Q 7 HOH   178 678 75  HOH   HOH A . 
Q 7 HOH   179 679 162 HOH   HOH A . 
Q 7 HOH   180 680 92  HOH   HOH A . 
Q 7 HOH   181 681 209 HOH   HOH A . 
Q 7 HOH   182 682 86  HOH   HOH A . 
Q 7 HOH   183 683 2   HOH   HOH A . 
Q 7 HOH   184 684 224 HOH   HOH A . 
Q 7 HOH   185 685 271 HOH   HOH A . 
Q 7 HOH   186 686 246 HOH   HOH A . 
Q 7 HOH   187 687 1   HOH   HOH A . 
Q 7 HOH   188 688 309 HOH   HOH A . 
Q 7 HOH   189 689 77  HOH   HOH A . 
Q 7 HOH   190 690 66  HOH   HOH A . 
Q 7 HOH   191 691 70  HOH   HOH A . 
Q 7 HOH   192 692 99  HOH   HOH A . 
Q 7 HOH   193 693 276 HOH   HOH A . 
Q 7 HOH   194 694 2   HOH   HOH A . 
Q 7 HOH   195 695 13  HOH   HOH A . 
Q 7 HOH   196 696 250 HOH   HOH A . 
Q 7 HOH   197 697 144 HOH   HOH A . 
Q 7 HOH   198 698 237 HOH   HOH A . 
Q 7 HOH   199 699 71  HOH   HOH A . 
Q 7 HOH   200 700 7   HOH   HOH A . 
Q 7 HOH   201 701 17  HOH   HOH A . 
Q 7 HOH   202 702 293 HOH   HOH A . 
Q 7 HOH   203 703 126 HOH   HOH A . 
Q 7 HOH   204 704 211 HOH   HOH A . 
Q 7 HOH   205 705 296 HOH   HOH A . 
Q 7 HOH   206 706 172 HOH   HOH A . 
Q 7 HOH   207 707 282 HOH   HOH A . 
Q 7 HOH   208 708 251 HOH   HOH A . 
Q 7 HOH   209 709 120 HOH   HOH A . 
Q 7 HOH   210 710 229 HOH   HOH A . 
Q 7 HOH   211 711 285 HOH   HOH A . 
Q 7 HOH   212 712 267 HOH   HOH A . 
Q 7 HOH   213 713 5   HOH   HOH A . 
Q 7 HOH   214 714 142 HOH   HOH A . 
Q 7 HOH   215 715 19  HOH   HOH A . 
Q 7 HOH   216 716 93  HOH   HOH A . 
Q 7 HOH   217 717 240 HOH   HOH A . 
Q 7 HOH   218 718 306 HOH   HOH A . 
Q 7 HOH   219 719 281 HOH   HOH A . 
Q 7 HOH   220 720 4   HOH   HOH A . 
Q 7 HOH   221 721 239 HOH   HOH A . 
Q 7 HOH   222 722 6   HOH   HOH A . 
Q 7 HOH   223 723 125 HOH   HOH A . 
Q 7 HOH   224 724 136 HOH   HOH A . 
Q 7 HOH   225 725 108 HOH   HOH A . 
Q 7 HOH   226 726 299 HOH   HOH A . 
Q 7 HOH   227 727 156 HOH   HOH A . 
Q 7 HOH   228 728 16  HOH   HOH A . 
Q 7 HOH   229 729 97  HOH   HOH A . 
Q 7 HOH   230 730 287 HOH   HOH A . 
Q 7 HOH   231 731 143 HOH   HOH A . 
Q 7 HOH   232 732 303 HOH   HOH A . 
Q 7 HOH   233 733 272 HOH   HOH A . 
Q 7 HOH   234 734 263 HOH   HOH A . 
Q 7 HOH   235 735 283 HOH   HOH A . 
Q 7 HOH   236 736 222 HOH   HOH A . 
Q 7 HOH   237 737 228 HOH   HOH A . 
Q 7 HOH   238 738 14  HOH   HOH A . 
Q 7 HOH   239 739 145 HOH   HOH A . 
Q 7 HOH   240 740 23  HOH   HOH A . 
Q 7 HOH   241 741 107 HOH   HOH A . 
Q 7 HOH   242 742 131 HOH   HOH A . 
Q 7 HOH   243 743 124 HOH   HOH A . 
Q 7 HOH   244 744 244 HOH   HOH A . 
Q 7 HOH   245 745 261 HOH   HOH A . 
Q 7 HOH   246 746 245 HOH   HOH A . 
Q 7 HOH   247 747 20  HOH   HOH A . 
Q 7 HOH   248 748 247 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 ILE 5   ? CG1 ? A ILE 8   CG1 
2 1 Y 1 A ILE 5   ? CG2 ? A ILE 8   CG2 
3 1 Y 1 A ILE 5   ? CD1 ? A ILE 8   CD1 
4 1 Y 1 A LYS 315 ? CG  ? A LYS 318 CG  
5 1 Y 1 A LYS 315 ? CD  ? A LYS 318 CD  
6 1 Y 1 A LYS 315 ? CE  ? A LYS 318 CE  
7 1 Y 1 A LYS 315 ? NZ  ? A LYS 318 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless  ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DNU 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     113.666 
_cell.length_a_esd                 ? 
_cell.length_b                     113.666 
_cell.length_b_esd                 ? 
_cell.length_c                     220.001 
_cell.length_c_esd                 ? 
_cell.volume                       2842404.022 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_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                         9DNU 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                98 
_symmetry.space_group_name_Hall            'I 4bw 2bw' 
_symmetry.space_group_name_H-M             'I 41 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9DNU 
_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             4.94 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          75.11 
_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              5.6 
_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    '200 mM zinc acetate, 0.1 M Bis-Tris pH 5.5-6.6, and 6-20% PEG 8000' 
_exptl_crystal_grow.pdbx_pH_range   5.5-6.6 
_exptl_crystal_grow.temp            277 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-01-24 
_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   0.92 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'NSLS-II BEAMLINE 17-ID-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.92 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID-1 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          49.44 
_reflns.entry_id                                       9DNU 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.3 
_reflns.d_resolution_low                               32.45 
_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                                     32420 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                14.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.9 
_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                                0.127 
_reflns.pdbx_Rpim_I_all                                0.045 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.119 
_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                                     2.37 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.9 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3130 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.690 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.734 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.8 
_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                               64.21 
_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                                 9DNU 
_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                             32.45 
_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                     32387 
_refine.ls_number_reflns_R_free                  1686 
_refine.ls_number_reflns_R_work                  30701 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.97 
_refine.ls_percent_reflns_R_free                 5.21 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1889 
_refine.ls_R_factor_R_free                       0.2121 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1876 
_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       'GeoStd + Monomer Library + CDL v1.2' 
_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             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 22.6877 
_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                            0.2781 
_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                        32.45 
_refine_hist.number_atoms_solvent             248 
_refine_hist.number_atoms_total               2764 
_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        2459 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         57 
_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' ? 0.0064  ? 2578 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.8015  ? 3504 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0498  ? 385  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0063  ? 455  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 16.6897 ? 956  ? f_dihedral_angle_d ? ? 
# 
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 2.37  . . 158 2514 100.00 . . . . 0.2787 . . . . . . . . . . . 0.3139 
'X-RAY DIFFRACTION' 2.37 2.44  . . 149 2486 99.92  . . . . 0.2559 . . . . . . . . . . . 0.2688 
'X-RAY DIFFRACTION' 2.44 2.53  . . 122 2539 99.96  . . . . 0.2470 . . . . . . . . . . . 0.2679 
'X-RAY DIFFRACTION' 2.53 2.63  . . 144 2522 100.00 . . . . 0.2226 . . . . . . . . . . . 0.2527 
'X-RAY DIFFRACTION' 2.63 2.75  . . 131 2523 100.00 . . . . 0.2059 . . . . . . . . . . . 0.2479 
'X-RAY DIFFRACTION' 2.75 2.90  . . 134 2549 100.00 . . . . 0.2098 . . . . . . . . . . . 0.2366 
'X-RAY DIFFRACTION' 2.90 3.08  . . 139 2531 99.96  . . . . 0.2234 . . . . . . . . . . . 0.2813 
'X-RAY DIFFRACTION' 3.08 3.32  . . 142 2530 99.93  . . . . 0.1925 . . . . . . . . . . . 0.2252 
'X-RAY DIFFRACTION' 3.32 3.65  . . 141 2581 100.00 . . . . 0.1847 . . . . . . . . . . . 0.2234 
'X-RAY DIFFRACTION' 3.65 4.18  . . 128 2577 100.00 . . . . 0.1625 . . . . . . . . . . . 0.1866 
'X-RAY DIFFRACTION' 4.18 5.26  . . 164 2598 100.00 . . . . 0.1557 . . . . . . . . . . . 0.1549 
'X-RAY DIFFRACTION' 5.26 32.45 . . 134 2751 99.90  . . . . 0.1815 . . . . . . . . . . . 0.2151 
# 
_struct.entry_id                     9DNU 
_struct.title                        'SARS-CoV-2 papain-like protease (PLpro) with inhibitor Jun13296' 
_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        9DNU 
_struct_keywords.text            
'SARS CoV-2 Papain Like Protease (PLpro), complex, inhibitor, Jun13296, VIRAL PROTEIN, HYDROLASE-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN,HYDROLASE/INHIBITOR' 
# 
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 4 ? 
F N N 4 ? 
G N N 4 ? 
H N N 4 ? 
I N N 4 ? 
J N N 4 ? 
K N N 4 ? 
L N N 5 ? 
M N N 5 ? 
N N N 5 ? 
O N N 5 ? 
P N N 6 ? 
Q N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;EVRTIKVFTTVDNINLHTQVVDMSMTYGQQFGPTYLDGADVTKIKPHNSHEGKTFYVLPNDDTLRVEAFEYYHTTDPSFL
GRYMSALNHTKKWKYPQVNGLTSIKWADNNCYLATALLTLQQIELKFNPPALQDAYYRARAGEAANFCALILAYCNKTVG
ELGDVRETMSYLFQHANLDSCKRVLNVVCKTCGQQQTTLKGVEAVMYMGTLSYEQFKKGVQIPCTCGKQATKYLVQQESP
FVMMSAPPAQYELKHGTFTCASEYTGNYQCGHYKHITSKETLYCIDGALLTKSSEYKGPITDVFYKENSYTTTIK
;
_struct_ref.pdbx_align_begin           1564 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9DNU 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 4 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 318 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P0DTD1 
_struct_ref_seq.db_align_beg                  1564 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1878 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       315 
# 
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 9DNU SER A 1 ? UNP P0DTD1 ? ? 'expression tag' -2 1 
1 9DNU ASN A 2 ? UNP P0DTD1 ? ? 'expression tag' -1 2 
1 9DNU ALA A 3 ? UNP P0DTD1 ? ? 'expression tag' 0  3 
# 
_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,G,H,I,J,K,L,M,N,O,P,Q 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_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 THR A 29  ? PHE A 34  ? THR A 26  PHE A 31  1 ? 6  
HELX_P HELX_P2 AA2 ASP A 64  ? HIS A 76  ? ASP A 61  HIS A 73  1 ? 13 
HELX_P HELX_P3 AA3 SER A 81  ? LYS A 94  ? SER A 78  LYS A 91  1 ? 14 
HELX_P HELX_P4 AA4 ASN A 113 ? GLN A 124 ? ASN A 110 GLN A 121 1 ? 12 
HELX_P HELX_P5 AA5 PRO A 132 ? ALA A 144 ? PRO A 129 ALA A 141 1 ? 13 
HELX_P HELX_P6 AA6 ALA A 147 ? ASN A 159 ? ALA A 144 ASN A 156 1 ? 13 
HELX_P HELX_P7 AA7 ASP A 167 ? HIS A 178 ? ASP A 164 HIS A 175 1 ? 12 
HELX_P HELX_P8 AA8 GLY A 204 ? VAL A 208 ? GLY A 201 VAL A 205 1 ? 5  
HELX_P HELX_P9 AA9 SER A 215 ? GLY A 222 ? SER A 212 GLY A 219 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 HIS 20  NE2 ? ? ? 1_555 K ZN  . ZN ? ? A HIS 17  A ZN  410 1_555  ? ? ? ? ? ? ? 2.289 ? ? 
metalc2  metalc ? ? A ASP 65  OD1 ? ? ? 1_555 E ZN  . ZN ? ? A ASP 62  A ZN  404 10_665 ? ? ? ? ? ? ? 1.894 ? ? 
metalc3  metalc ? ? A GLU 70  OE2 ? ? ? 1_555 K ZN  . ZN ? ? A GLU 67  A ZN  410 1_555  ? ? ? ? ? ? ? 2.417 ? ? 
metalc4  metalc ? ? A HIS 76  ND1 ? ? ? 1_555 E ZN  . ZN ? ? A HIS 73  A ZN  404 1_555  ? ? ? ? ? ? ? 2.174 ? ? 
metalc5  metalc ? ? A HIS 92  ND1 ? ? ? 1_555 G ZN  . ZN A ? A HIS 89  A ZN  406 1_555  ? ? ? ? ? ? ? 2.278 ? ? 
metalc6  metalc ? ? A HIS 92  ND1 ? ? ? 1_555 G ZN  . ZN B ? A HIS 89  A ZN  406 1_555  ? ? ? ? ? ? ? 2.297 ? ? 
metalc7  metalc ? ? A LYS 95  NZ  ? ? ? 1_555 G ZN  . ZN B ? A LYS 92  A ZN  406 1_555  ? ? ? ? ? ? ? 2.404 ? ? 
metalc8  metalc ? ? A ASP 111 OD2 ? ? ? 1_555 G ZN  . ZN A ? A ASP 108 A ZN  406 1_555  ? ? ? ? ? ? ? 2.130 ? ? 
metalc9  metalc ? ? A CYS 114 SG  ? ? ? 1_555 F ZN  . ZN ? ? A CYS 111 A ZN  405 1_555  ? ? ? ? ? ? ? 2.347 ? ? 
metalc10 metalc ? ? A HIS 178 NE2 ? ? ? 1_555 H ZN  . ZN ? ? A HIS 175 A ZN  407 1_555  ? ? ? ? ? ? ? 2.306 ? ? 
metalc11 metalc ? ? A CYS 192 SG  ? ? ? 1_555 D ZN  . ZN ? ? A CYS 189 A ZN  403 1_555  ? ? ? ? ? ? ? 2.318 ? ? 
metalc12 metalc ? ? A CYS 195 SG  ? ? ? 1_555 D ZN  . ZN ? ? A CYS 192 A ZN  403 1_555  ? ? ? ? ? ? ? 2.339 ? ? 
metalc13 metalc ? ? A CYS 195 SG  ? ? ? 1_555 I ZN  . ZN ? ? A CYS 192 A ZN  408 1_555  ? ? ? ? ? ? ? 2.302 ? ? 
metalc14 metalc ? ? A CYS 195 SG  ? ? ? 1_555 I ZN  . ZN ? ? A CYS 192 A ZN  408 8_665  ? ? ? ? ? ? ? 2.897 ? ? 
metalc15 metalc ? ? A CYS 227 SG  ? ? ? 1_555 D ZN  . ZN ? ? A CYS 224 A ZN  403 1_555  ? ? ? ? ? ? ? 2.340 ? ? 
metalc16 metalc ? ? A CYS 229 SG  ? ? ? 1_555 D ZN  . ZN ? ? A CYS 226 A ZN  403 1_555  ? ? ? ? ? ? ? 2.337 ? ? 
metalc17 metalc ? ? A HIS 258 ND1 ? ? ? 1_555 J ZN  . ZN ? ? A HIS 255 A ZN  409 1_555  ? ? ? ? ? ? ? 2.301 ? ? 
metalc18 metalc ? ? A CYS 273 SG  ? ? ? 1_555 G ZN  . ZN A ? A CYS 270 A ZN  406 15_555 ? ? ? ? ? ? ? 2.350 ? ? 
metalc19 metalc ? ? A CYS 273 SG  ? ? ? 1_555 G ZN  . ZN B ? A CYS 270 A ZN  406 15_555 ? ? ? ? ? ? ? 2.317 ? ? 
metalc20 metalc ? ? A HIS 275 ND1 ? ? ? 1_555 F ZN  . ZN ? ? A HIS 272 A ZN  405 1_555  ? ? ? ? ? ? ? 2.362 ? ? 
metalc21 metalc ? ? F ZN  .   ZN  ? ? ? 1_555 Q HOH . O  ? ? A ZN  405 A HOH 533 1_555  ? ? ? ? ? ? ? 2.380 ? ? 
metalc22 metalc ? ? F ZN  .   ZN  ? ? ? 1_555 Q HOH . O  ? ? A ZN  405 A HOH 681 1_555  ? ? ? ? ? ? ? 1.702 ? ? 
metalc23 metalc ? ? H ZN  .   ZN  ? ? ? 1_555 Q HOH . O  ? ? A ZN  407 A HOH 518 1_555  ? ? ? ? ? ? ? 2.495 ? ? 
metalc24 metalc ? ? H ZN  .   ZN  ? ? ? 1_555 Q HOH . O  ? ? A ZN  407 A HOH 658 1_555  ? ? ? ? ? ? ? 2.357 ? ? 
metalc25 metalc ? ? H ZN  .   ZN  ? ? ? 1_555 Q HOH . O  ? ? A ZN  407 A HOH 728 1_555  ? ? ? ? ? ? ? 2.580 ? ? 
# 
_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  NE2 ? A HIS 20  ? A HIS 17  ? 1_555 ZN ? K ZN . ? A ZN 410 ? 1_555  OE2 ? A GLU 70  ? A GLU 67  ? 1_555 108.9 ? 
2  OD1 ? A ASP 65  ? A ASP 62  ? 1_555 ZN ? E ZN . ? A ZN 404 ? 10_665 ND1 ? A HIS 76  ? A HIS 73  ? 1_555 115.7 ? 
3  ND1 ? A HIS 92  ? A HIS 89  ? 1_555 ZN A G ZN . ? A ZN 406 ? 1_555  OD2 ? A ASP 111 ? A ASP 108 ? 1_555 122.6 ? 
4  ND1 ? A HIS 92  ? A HIS 89  ? 1_555 ZN A G ZN . ? A ZN 406 ? 1_555  SG  ? A CYS 273 ? A CYS 270 ? 1_555 110.7 ? 
5  OD2 ? A ASP 111 ? A ASP 108 ? 1_555 ZN A G ZN . ? A ZN 406 ? 1_555  SG  ? A CYS 273 ? A CYS 270 ? 1_555 36.4  ? 
6  ND1 ? A HIS 92  ? A HIS 89  ? 1_555 ZN B G ZN . ? A ZN 406 ? 1_555  NZ  ? A LYS 95  ? A LYS 92  ? 1_555 136.8 ? 
7  ND1 ? A HIS 92  ? A HIS 89  ? 1_555 ZN B G ZN . ? A ZN 406 ? 1_555  SG  ? A CYS 273 ? A CYS 270 ? 1_555 64.0  ? 
8  NZ  ? A LYS 95  ? A LYS 92  ? 1_555 ZN B G ZN . ? A ZN 406 ? 1_555  SG  ? A CYS 273 ? A CYS 270 ? 1_555 156.1 ? 
9  SG  ? A CYS 114 ? A CYS 111 ? 1_555 ZN ? F ZN . ? A ZN 405 ? 1_555  ND1 ? A HIS 275 ? A HIS 272 ? 1_555 93.2  ? 
10 SG  ? A CYS 114 ? A CYS 111 ? 1_555 ZN ? F ZN . ? A ZN 405 ? 1_555  O   ? Q HOH .   ? A HOH 533 ? 1_555 126.6 ? 
11 ND1 ? A HIS 275 ? A HIS 272 ? 1_555 ZN ? F ZN . ? A ZN 405 ? 1_555  O   ? Q HOH .   ? A HOH 533 ? 1_555 77.4  ? 
12 SG  ? A CYS 114 ? A CYS 111 ? 1_555 ZN ? F ZN . ? A ZN 405 ? 1_555  O   ? Q HOH .   ? A HOH 681 ? 1_555 81.2  ? 
13 ND1 ? A HIS 275 ? A HIS 272 ? 1_555 ZN ? F ZN . ? A ZN 405 ? 1_555  O   ? Q HOH .   ? A HOH 681 ? 1_555 146.0 ? 
14 O   ? Q HOH .   ? A HOH 533 ? 1_555 ZN ? F ZN . ? A ZN 405 ? 1_555  O   ? Q HOH .   ? A HOH 681 ? 1_555 79.3  ? 
15 NE2 ? A HIS 178 ? A HIS 175 ? 1_555 ZN ? H ZN . ? A ZN 407 ? 1_555  O   ? Q HOH .   ? A HOH 518 ? 1_555 94.4  ? 
16 NE2 ? A HIS 178 ? A HIS 175 ? 1_555 ZN ? H ZN . ? A ZN 407 ? 1_555  O   ? Q HOH .   ? A HOH 658 ? 1_555 83.7  ? 
17 O   ? Q HOH .   ? A HOH 518 ? 1_555 ZN ? H ZN . ? A ZN 407 ? 1_555  O   ? Q HOH .   ? A HOH 658 ? 1_555 76.5  ? 
18 NE2 ? A HIS 178 ? A HIS 175 ? 1_555 ZN ? H ZN . ? A ZN 407 ? 1_555  O   ? Q HOH .   ? A HOH 728 ? 1_555 110.5 ? 
19 O   ? Q HOH .   ? A HOH 518 ? 1_555 ZN ? H ZN . ? A ZN 407 ? 1_555  O   ? Q HOH .   ? A HOH 728 ? 1_555 74.3  ? 
20 O   ? Q HOH .   ? A HOH 658 ? 1_555 ZN ? H ZN . ? A ZN 407 ? 1_555  O   ? Q HOH .   ? A HOH 728 ? 1_555 148.3 ? 
21 SG  ? A CYS 192 ? A CYS 189 ? 1_555 ZN ? D ZN . ? A ZN 403 ? 1_555  SG  ? A CYS 195 ? A CYS 192 ? 1_555 110.6 ? 
22 SG  ? A CYS 192 ? A CYS 189 ? 1_555 ZN ? D ZN . ? A ZN 403 ? 1_555  SG  ? A CYS 227 ? A CYS 224 ? 1_555 108.5 ? 
23 SG  ? A CYS 195 ? A CYS 192 ? 1_555 ZN ? D ZN . ? A ZN 403 ? 1_555  SG  ? A CYS 227 ? A CYS 224 ? 1_555 109.3 ? 
24 SG  ? A CYS 192 ? A CYS 189 ? 1_555 ZN ? D ZN . ? A ZN 403 ? 1_555  SG  ? A CYS 229 ? A CYS 226 ? 1_555 97.6  ? 
25 SG  ? A CYS 195 ? A CYS 192 ? 1_555 ZN ? D ZN . ? A ZN 403 ? 1_555  SG  ? A CYS 229 ? A CYS 226 ? 1_555 117.0 ? 
26 SG  ? A CYS 227 ? A CYS 224 ? 1_555 ZN ? D ZN . ? A ZN 403 ? 1_555  SG  ? A CYS 229 ? A CYS 226 ? 1_555 113.0 ? 
27 SG  ? A CYS 195 ? A CYS 192 ? 1_555 ZN ? I ZN . ? A ZN 408 ? 1_555  SG  ? A CYS 195 ? A CYS 192 ? 1_555 0.0   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
AA3 ? 4 ? 
AA4 ? 4 ? 
AA5 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA5 6 7 ? 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 HIS A 20  ? VAL A 24  ? HIS A 17  VAL A 21  
AA1 2 ILE A 8   ? THR A 13  ? ILE A 5   THR A 10  
AA1 3 THR A 57  ? VAL A 60  ? THR A 54  VAL A 57  
AA1 4 THR A 37  ? LEU A 39  ? THR A 34  LEU A 36  
AA1 5 ALA A 42  ? ASP A 43  ? ALA A 39  ASP A 40  
AA2 1 GLN A 100 ? VAL A 101 ? GLN A 97  VAL A 98  
AA2 2 LEU A 104 ? THR A 105 ? LEU A 101 THR A 102 
AA3 1 GLY A 196 ? LYS A 203 ? GLY A 193 LYS A 200 
AA3 2 LYS A 185 ? CYS A 192 ? LYS A 182 CYS A 189 
AA3 3 ALA A 233 ? GLU A 241 ? ALA A 230 GLU A 238 
AA3 4 VAL A 223 ? ILE A 225 ? VAL A 220 ILE A 222 
AA4 1 GLY A 196 ? LYS A 203 ? GLY A 193 LYS A 200 
AA4 2 LYS A 185 ? CYS A 192 ? LYS A 182 CYS A 189 
AA4 3 ALA A 233 ? GLU A 241 ? ALA A 230 GLU A 238 
AA4 4 TYR A 313 ? THR A 314 ? TYR A 310 THR A 311 
AA5 1 MET A 209 ? MET A 211 ? MET A 206 MET A 208 
AA5 2 PHE A 244 ? LYS A 257 ? PHE A 241 LYS A 254 
AA5 3 GLU A 298 ? LYS A 309 ? GLU A 295 LYS A 306 
AA5 4 CYS A 263 ? THR A 268 ? CYS A 260 THR A 265 
AA5 5 HIS A 275 ? SER A 281 ? HIS A 272 SER A 278 
AA5 6 LEU A 285 ? ASP A 289 ? LEU A 282 ASP A 286 
AA5 7 LEU A 292 ? SER A 296 ? LEU A 289 SER A 293 
# 
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 24  ? O VAL A 21  N ILE A 8   ? N ILE A 5   
AA1 2 3 N PHE A 11  ? N PHE A 8   O PHE A 58  ? O PHE A 55  
AA1 3 4 O TYR A 59  ? O TYR A 56  N TYR A 38  ? N TYR A 35  
AA1 4 5 N LEU A 39  ? N LEU A 36  O ALA A 42  ? O ALA A 39  
AA2 1 2 N VAL A 101 ? N VAL A 98  O LEU A 104 ? O LEU A 101 
AA3 1 2 O LEU A 202 ? O LEU A 199 N ARG A 186 ? N ARG A 183 
AA3 2 3 N VAL A 191 ? N VAL A 188 O THR A 234 ? O THR A 231 
AA3 3 4 O LYS A 235 ? O LYS A 232 N VAL A 223 ? N VAL A 220 
AA4 1 2 O LEU A 202 ? O LEU A 199 N ARG A 186 ? N ARG A 183 
AA4 2 3 N VAL A 191 ? N VAL A 188 O THR A 234 ? O THR A 231 
AA4 3 4 N GLN A 240 ? N GLN A 237 O TYR A 313 ? O TYR A 310 
AA5 1 2 N TYR A 210 ? N TYR A 207 O SER A 248 ? O SER A 245 
AA5 2 3 N MET A 247 ? N MET A 244 O VAL A 306 ? O VAL A 303 
AA5 3 4 O PHE A 307 ? O PHE A 304 N CYS A 263 ? N CYS A 260 
AA5 4 5 N GLU A 266 ? N GLU A 263 O LYS A 277 ? O LYS A 274 
AA5 5 6 N HIS A 278 ? N HIS A 275 O ILE A 288 ? O ILE A 285 
AA5 6 7 N CYS A 287 ? N CYS A 284 O THR A 294 ? O THR A 291 
# 
_pdbx_entry_details.entry_id                   9DNU 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ILE A 14  ? ? -127.63 -62.12  
2 1 SER A 103 ? ? -109.91 -169.12 
3 1 ALA A 107 ? ? -173.27 144.54  
4 1 TYR A 268 ? ? -36.77  127.26  
5 1 GLN A 269 ? ? 72.03   -38.73  
6 1 LYS A 279 ? ? -107.13 -132.77 
7 1 ASN A 308 ? ? -143.29 -67.46  
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 585 ? Q HOH . 
2 1 A HOH 733 ? Q HOH . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1  x,y,z                
2  -y+1/2,x,z+3/4       
3  y+1/2,-x,z+3/4       
4  x+1/2,-y,-z+3/4      
5  -x+1/2,y,-z+3/4      
6  -x,-y,z              
7  y,x,-z               
8  -y,-x,-z             
9  x+1/2,y+1/2,z+1/2    
10 -y+1,x+1/2,z+5/4     
11 y+1,-x+1/2,z+5/4     
12 x+1,-y+1/2,-z+5/4    
13 -x+1,y+1/2,-z+5/4    
14 -x+1/2,-y+1/2,z+1/2  
15 y+1/2,x+1/2,-z+1/2   
16 -y+1/2,-x+1/2,-z+1/2 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A SER -2  ? A SER 1   
2 1 Y 1 A ASN -1  ? A ASN 2   
3 1 Y 1 A ALA 0   ? A ALA 3   
4 1 Y 1 A GLU 1   ? A GLU 4   
5 1 Y 1 A VAL 2   ? A VAL 5   
6 1 Y 1 A ARG 3   ? A ARG 6   
7 1 Y 1 A LYS 228 ? A LYS 231 
# 
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 
A1BEG C21  C  N R 1   
A1BEG N3   N  Y N 2   
A1BEG C20  C  N N 3   
A1BEG C18  C  Y N 4   
A1BEG C17  C  Y N 5   
A1BEG C16  C  Y N 6   
A1BEG C15  C  N N 7   
A1BEG C14  C  Y N 8   
A1BEG C13  C  Y N 9   
A1BEG C1   C  N N 10  
A1BEG C4   C  Y N 11  
A1BEG C5   C  Y N 12  
A1BEG C7   C  Y N 13  
A1BEG N2   N  Y N 14  
A1BEG C8   C  Y N 15  
A1BEG C12  C  N N 16  
A1BEG C9   C  N R 17  
A1BEG C10  C  N N 18  
A1BEG C6   C  Y N 19  
A1BEG C22  C  N N 20  
A1BEG C23  C  N N 21  
A1BEG C24  C  N S 22  
A1BEG C25  C  N N 23  
A1BEG C27  C  N N 24  
A1BEG C28  C  Y N 25  
A1BEG C30  C  Y N 26  
A1BEG C31  C  Y N 27  
A1BEG C32  C  Y N 28  
A1BEG C33  C  Y N 29  
A1BEG C34  C  Y N 30  
A1BEG C35  C  Y N 31  
A1BEG C37  C  Y N 32  
A1BEG N11  N  N N 33  
A1BEG N19  N  N N 34  
A1BEG N26  N  N N 35  
A1BEG N36  N  Y N 36  
A1BEG O29  O  N N 37  
A1BEG H21  H  N N 38  
A1BEG H20A H  N N 39  
A1BEG H20B H  N N 40  
A1BEG H17  H  N N 41  
A1BEG H16  H  N N 42  
A1BEG H15B H  N N 43  
A1BEG H15A H  N N 44  
A1BEG H15C H  N N 45  
A1BEG H1C  H  N N 46  
A1BEG H1B  H  N N 47  
A1BEG H1A  H  N N 48  
A1BEG H4   H  N N 49  
A1BEG H7   H  N N 50  
A1BEG H9   H  N N 51  
A1BEG H10C H  N N 52  
A1BEG H10B H  N N 53  
A1BEG H10A H  N N 54  
A1BEG H22A H  N N 55  
A1BEG H22B H  N N 56  
A1BEG H23A H  N N 57  
A1BEG H23B H  N N 58  
A1BEG H24  H  N N 59  
A1BEG H25A H  N N 60  
A1BEG H25B H  N N 61  
A1BEG H27B H  N N 62  
A1BEG H27A H  N N 63  
A1BEG H27C H  N N 64  
A1BEG H28  H  N N 65  
A1BEG H31  H  N N 66  
A1BEG H32  H  N N 67  
A1BEG H33  H  N N 68  
A1BEG H34  H  N N 69  
A1BEG H37  H  N N 70  
A1BEG H11  H  N N 71  
ACT   C    C  N N 72  
ACT   O    O  N N 73  
ACT   OXT  O  N N 74  
ACT   CH3  C  N N 75  
ACT   H1   H  N N 76  
ACT   H2   H  N N 77  
ACT   H3   H  N N 78  
ALA   N    N  N N 79  
ALA   CA   C  N S 80  
ALA   C    C  N N 81  
ALA   O    O  N N 82  
ALA   CB   C  N N 83  
ALA   OXT  O  N N 84  
ALA   H    H  N N 85  
ALA   H2   H  N N 86  
ALA   HA   H  N N 87  
ALA   HB1  H  N N 88  
ALA   HB2  H  N N 89  
ALA   HB3  H  N N 90  
ALA   HXT  H  N N 91  
ARG   N    N  N N 92  
ARG   CA   C  N S 93  
ARG   C    C  N N 94  
ARG   O    O  N N 95  
ARG   CB   C  N N 96  
ARG   CG   C  N N 97  
ARG   CD   C  N N 98  
ARG   NE   N  N N 99  
ARG   CZ   C  N N 100 
ARG   NH1  N  N N 101 
ARG   NH2  N  N N 102 
ARG   OXT  O  N N 103 
ARG   H    H  N N 104 
ARG   H2   H  N N 105 
ARG   HA   H  N N 106 
ARG   HB2  H  N N 107 
ARG   HB3  H  N N 108 
ARG   HG2  H  N N 109 
ARG   HG3  H  N N 110 
ARG   HD2  H  N N 111 
ARG   HD3  H  N N 112 
ARG   HE   H  N N 113 
ARG   HH11 H  N N 114 
ARG   HH12 H  N N 115 
ARG   HH21 H  N N 116 
ARG   HH22 H  N N 117 
ARG   HXT  H  N N 118 
ASN   N    N  N N 119 
ASN   CA   C  N S 120 
ASN   C    C  N N 121 
ASN   O    O  N N 122 
ASN   CB   C  N N 123 
ASN   CG   C  N N 124 
ASN   OD1  O  N N 125 
ASN   ND2  N  N N 126 
ASN   OXT  O  N N 127 
ASN   H    H  N N 128 
ASN   H2   H  N N 129 
ASN   HA   H  N N 130 
ASN   HB2  H  N N 131 
ASN   HB3  H  N N 132 
ASN   HD21 H  N N 133 
ASN   HD22 H  N N 134 
ASN   HXT  H  N N 135 
ASP   N    N  N N 136 
ASP   CA   C  N S 137 
ASP   C    C  N N 138 
ASP   O    O  N N 139 
ASP   CB   C  N N 140 
ASP   CG   C  N N 141 
ASP   OD1  O  N N 142 
ASP   OD2  O  N N 143 
ASP   OXT  O  N N 144 
ASP   H    H  N N 145 
ASP   H2   H  N N 146 
ASP   HA   H  N N 147 
ASP   HB2  H  N N 148 
ASP   HB3  H  N N 149 
ASP   HD2  H  N N 150 
ASP   HXT  H  N N 151 
CL    CL   CL N N 152 
CYS   N    N  N N 153 
CYS   CA   C  N R 154 
CYS   C    C  N N 155 
CYS   O    O  N N 156 
CYS   CB   C  N N 157 
CYS   SG   S  N N 158 
CYS   OXT  O  N N 159 
CYS   H    H  N N 160 
CYS   H2   H  N N 161 
CYS   HA   H  N N 162 
CYS   HB2  H  N N 163 
CYS   HB3  H  N N 164 
CYS   HG   H  N N 165 
CYS   HXT  H  N N 166 
EDO   C1   C  N N 167 
EDO   O1   O  N N 168 
EDO   C2   C  N N 169 
EDO   O2   O  N N 170 
EDO   H11  H  N N 171 
EDO   H12  H  N N 172 
EDO   HO1  H  N N 173 
EDO   H21  H  N N 174 
EDO   H22  H  N N 175 
EDO   HO2  H  N N 176 
GLN   N    N  N N 177 
GLN   CA   C  N S 178 
GLN   C    C  N N 179 
GLN   O    O  N N 180 
GLN   CB   C  N N 181 
GLN   CG   C  N N 182 
GLN   CD   C  N N 183 
GLN   OE1  O  N N 184 
GLN   NE2  N  N N 185 
GLN   OXT  O  N N 186 
GLN   H    H  N N 187 
GLN   H2   H  N N 188 
GLN   HA   H  N N 189 
GLN   HB2  H  N N 190 
GLN   HB3  H  N N 191 
GLN   HG2  H  N N 192 
GLN   HG3  H  N N 193 
GLN   HE21 H  N N 194 
GLN   HE22 H  N N 195 
GLN   HXT  H  N N 196 
GLU   N    N  N N 197 
GLU   CA   C  N S 198 
GLU   C    C  N N 199 
GLU   O    O  N N 200 
GLU   CB   C  N N 201 
GLU   CG   C  N N 202 
GLU   CD   C  N N 203 
GLU   OE1  O  N N 204 
GLU   OE2  O  N N 205 
GLU   OXT  O  N N 206 
GLU   H    H  N N 207 
GLU   H2   H  N N 208 
GLU   HA   H  N N 209 
GLU   HB2  H  N N 210 
GLU   HB3  H  N N 211 
GLU   HG2  H  N N 212 
GLU   HG3  H  N N 213 
GLU   HE2  H  N N 214 
GLU   HXT  H  N N 215 
GLY   N    N  N N 216 
GLY   CA   C  N N 217 
GLY   C    C  N N 218 
GLY   O    O  N N 219 
GLY   OXT  O  N N 220 
GLY   H    H  N N 221 
GLY   H2   H  N N 222 
GLY   HA2  H  N N 223 
GLY   HA3  H  N N 224 
GLY   HXT  H  N N 225 
HIS   N    N  N N 226 
HIS   CA   C  N S 227 
HIS   C    C  N N 228 
HIS   O    O  N N 229 
HIS   CB   C  N N 230 
HIS   CG   C  Y N 231 
HIS   ND1  N  Y N 232 
HIS   CD2  C  Y N 233 
HIS   CE1  C  Y N 234 
HIS   NE2  N  Y N 235 
HIS   OXT  O  N N 236 
HIS   H    H  N N 237 
HIS   H2   H  N N 238 
HIS   HA   H  N N 239 
HIS   HB2  H  N N 240 
HIS   HB3  H  N N 241 
HIS   HD1  H  N N 242 
HIS   HD2  H  N N 243 
HIS   HE1  H  N N 244 
HIS   HE2  H  N N 245 
HIS   HXT  H  N N 246 
HOH   O    O  N N 247 
HOH   H1   H  N N 248 
HOH   H2   H  N N 249 
ILE   N    N  N N 250 
ILE   CA   C  N S 251 
ILE   C    C  N N 252 
ILE   O    O  N N 253 
ILE   CB   C  N S 254 
ILE   CG1  C  N N 255 
ILE   CG2  C  N N 256 
ILE   CD1  C  N N 257 
ILE   OXT  O  N N 258 
ILE   H    H  N N 259 
ILE   H2   H  N N 260 
ILE   HA   H  N N 261 
ILE   HB   H  N N 262 
ILE   HG12 H  N N 263 
ILE   HG13 H  N N 264 
ILE   HG21 H  N N 265 
ILE   HG22 H  N N 266 
ILE   HG23 H  N N 267 
ILE   HD11 H  N N 268 
ILE   HD12 H  N N 269 
ILE   HD13 H  N N 270 
ILE   HXT  H  N N 271 
LEU   N    N  N N 272 
LEU   CA   C  N S 273 
LEU   C    C  N N 274 
LEU   O    O  N N 275 
LEU   CB   C  N N 276 
LEU   CG   C  N N 277 
LEU   CD1  C  N N 278 
LEU   CD2  C  N N 279 
LEU   OXT  O  N N 280 
LEU   H    H  N N 281 
LEU   H2   H  N N 282 
LEU   HA   H  N N 283 
LEU   HB2  H  N N 284 
LEU   HB3  H  N N 285 
LEU   HG   H  N N 286 
LEU   HD11 H  N N 287 
LEU   HD12 H  N N 288 
LEU   HD13 H  N N 289 
LEU   HD21 H  N N 290 
LEU   HD22 H  N N 291 
LEU   HD23 H  N N 292 
LEU   HXT  H  N N 293 
LYS   N    N  N N 294 
LYS   CA   C  N S 295 
LYS   C    C  N N 296 
LYS   O    O  N N 297 
LYS   CB   C  N N 298 
LYS   CG   C  N N 299 
LYS   CD   C  N N 300 
LYS   CE   C  N N 301 
LYS   NZ   N  N N 302 
LYS   OXT  O  N N 303 
LYS   H    H  N N 304 
LYS   H2   H  N N 305 
LYS   HA   H  N N 306 
LYS   HB2  H  N N 307 
LYS   HB3  H  N N 308 
LYS   HG2  H  N N 309 
LYS   HG3  H  N N 310 
LYS   HD2  H  N N 311 
LYS   HD3  H  N N 312 
LYS   HE2  H  N N 313 
LYS   HE3  H  N N 314 
LYS   HZ1  H  N N 315 
LYS   HZ2  H  N N 316 
LYS   HZ3  H  N N 317 
LYS   HXT  H  N N 318 
MET   N    N  N N 319 
MET   CA   C  N S 320 
MET   C    C  N N 321 
MET   O    O  N N 322 
MET   CB   C  N N 323 
MET   CG   C  N N 324 
MET   SD   S  N N 325 
MET   CE   C  N N 326 
MET   OXT  O  N N 327 
MET   H    H  N N 328 
MET   H2   H  N N 329 
MET   HA   H  N N 330 
MET   HB2  H  N N 331 
MET   HB3  H  N N 332 
MET   HG2  H  N N 333 
MET   HG3  H  N N 334 
MET   HE1  H  N N 335 
MET   HE2  H  N N 336 
MET   HE3  H  N N 337 
MET   HXT  H  N N 338 
PHE   N    N  N N 339 
PHE   CA   C  N S 340 
PHE   C    C  N N 341 
PHE   O    O  N N 342 
PHE   CB   C  N N 343 
PHE   CG   C  Y N 344 
PHE   CD1  C  Y N 345 
PHE   CD2  C  Y N 346 
PHE   CE1  C  Y N 347 
PHE   CE2  C  Y N 348 
PHE   CZ   C  Y N 349 
PHE   OXT  O  N N 350 
PHE   H    H  N N 351 
PHE   H2   H  N N 352 
PHE   HA   H  N N 353 
PHE   HB2  H  N N 354 
PHE   HB3  H  N N 355 
PHE   HD1  H  N N 356 
PHE   HD2  H  N N 357 
PHE   HE1  H  N N 358 
PHE   HE2  H  N N 359 
PHE   HZ   H  N N 360 
PHE   HXT  H  N N 361 
PRO   N    N  N N 362 
PRO   CA   C  N S 363 
PRO   C    C  N N 364 
PRO   O    O  N N 365 
PRO   CB   C  N N 366 
PRO   CG   C  N N 367 
PRO   CD   C  N N 368 
PRO   OXT  O  N N 369 
PRO   H    H  N N 370 
PRO   HA   H  N N 371 
PRO   HB2  H  N N 372 
PRO   HB3  H  N N 373 
PRO   HG2  H  N N 374 
PRO   HG3  H  N N 375 
PRO   HD2  H  N N 376 
PRO   HD3  H  N N 377 
PRO   HXT  H  N N 378 
SER   N    N  N N 379 
SER   CA   C  N S 380 
SER   C    C  N N 381 
SER   O    O  N N 382 
SER   CB   C  N N 383 
SER   OG   O  N N 384 
SER   OXT  O  N N 385 
SER   H    H  N N 386 
SER   H2   H  N N 387 
SER   HA   H  N N 388 
SER   HB2  H  N N 389 
SER   HB3  H  N N 390 
SER   HG   H  N N 391 
SER   HXT  H  N N 392 
THR   N    N  N N 393 
THR   CA   C  N S 394 
THR   C    C  N N 395 
THR   O    O  N N 396 
THR   CB   C  N R 397 
THR   OG1  O  N N 398 
THR   CG2  C  N N 399 
THR   OXT  O  N N 400 
THR   H    H  N N 401 
THR   H2   H  N N 402 
THR   HA   H  N N 403 
THR   HB   H  N N 404 
THR   HG1  H  N N 405 
THR   HG21 H  N N 406 
THR   HG22 H  N N 407 
THR   HG23 H  N N 408 
THR   HXT  H  N N 409 
TRP   N    N  N N 410 
TRP   CA   C  N S 411 
TRP   C    C  N N 412 
TRP   O    O  N N 413 
TRP   CB   C  N N 414 
TRP   CG   C  Y N 415 
TRP   CD1  C  Y N 416 
TRP   CD2  C  Y N 417 
TRP   NE1  N  Y N 418 
TRP   CE2  C  Y N 419 
TRP   CE3  C  Y N 420 
TRP   CZ2  C  Y N 421 
TRP   CZ3  C  Y N 422 
TRP   CH2  C  Y N 423 
TRP   OXT  O  N N 424 
TRP   H    H  N N 425 
TRP   H2   H  N N 426 
TRP   HA   H  N N 427 
TRP   HB2  H  N N 428 
TRP   HB3  H  N N 429 
TRP   HD1  H  N N 430 
TRP   HE1  H  N N 431 
TRP   HE3  H  N N 432 
TRP   HZ2  H  N N 433 
TRP   HZ3  H  N N 434 
TRP   HH2  H  N N 435 
TRP   HXT  H  N N 436 
TYR   N    N  N N 437 
TYR   CA   C  N S 438 
TYR   C    C  N N 439 
TYR   O    O  N N 440 
TYR   CB   C  N N 441 
TYR   CG   C  Y N 442 
TYR   CD1  C  Y N 443 
TYR   CD2  C  Y N 444 
TYR   CE1  C  Y N 445 
TYR   CE2  C  Y N 446 
TYR   CZ   C  Y N 447 
TYR   OH   O  N N 448 
TYR   OXT  O  N N 449 
TYR   H    H  N N 450 
TYR   H2   H  N N 451 
TYR   HA   H  N N 452 
TYR   HB2  H  N N 453 
TYR   HB3  H  N N 454 
TYR   HD1  H  N N 455 
TYR   HD2  H  N N 456 
TYR   HE1  H  N N 457 
TYR   HE2  H  N N 458 
TYR   HH   H  N N 459 
TYR   HXT  H  N N 460 
VAL   N    N  N N 461 
VAL   CA   C  N S 462 
VAL   C    C  N N 463 
VAL   O    O  N N 464 
VAL   CB   C  N N 465 
VAL   CG1  C  N N 466 
VAL   CG2  C  N N 467 
VAL   OXT  O  N N 468 
VAL   H    H  N N 469 
VAL   H2   H  N N 470 
VAL   HA   H  N N 471 
VAL   HB   H  N N 472 
VAL   HG11 H  N N 473 
VAL   HG12 H  N N 474 
VAL   HG13 H  N N 475 
VAL   HG21 H  N N 476 
VAL   HG22 H  N N 477 
VAL   HG23 H  N N 478 
VAL   HXT  H  N N 479 
ZN    ZN   ZN N N 480 
# 
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 
A1BEG C1  N2   sing N N 1   
A1BEG N2  N3   sing Y N 2   
A1BEG N3  C4   doub Y N 3   
A1BEG C4  C5   sing Y N 4   
A1BEG C5  C6   sing N N 5   
A1BEG C6  C7   doub Y N 6   
A1BEG C7  C8   sing Y N 7   
A1BEG C8  C9   sing N N 8   
A1BEG C9  C10  sing N N 9   
A1BEG C9  N11  sing N N 10  
A1BEG N11 C12  sing N N 11  
A1BEG C12 C13  sing N N 12  
A1BEG C13 C14  doub Y N 13  
A1BEG C14 C15  sing N N 14  
A1BEG C14 C16  sing Y N 15  
A1BEG C16 C17  doub Y N 16  
A1BEG C17 C18  sing Y N 17  
A1BEG C18 N19  sing N N 18  
A1BEG N19 C20  sing N N 19  
A1BEG C20 C21  sing N N 20  
A1BEG C21 C22  sing N N 21  
A1BEG C22 C23  sing N N 22  
A1BEG C23 C24  sing N N 23  
A1BEG C24 C25  sing N N 24  
A1BEG C24 N26  sing N N 25  
A1BEG N26 C27  sing N N 26  
A1BEG C18 C28  doub Y N 27  
A1BEG C12 O29  doub N N 28  
A1BEG C8  C30  doub Y N 29  
A1BEG C30 C31  sing Y N 30  
A1BEG C31 C32  doub Y N 31  
A1BEG C32 C33  sing Y N 32  
A1BEG C33 C34  doub Y N 33  
A1BEG C34 C35  sing Y N 34  
A1BEG C35 N36  doub Y N 35  
A1BEG C5  C37  doub Y N 36  
A1BEG C37 N2   sing Y N 37  
A1BEG N36 C6   sing Y N 38  
A1BEG C28 C13  sing Y N 39  
A1BEG C25 N19  sing N N 40  
A1BEG N26 C21  sing N N 41  
A1BEG C35 C30  sing Y N 42  
A1BEG C21 H21  sing N N 43  
A1BEG C20 H20A sing N N 44  
A1BEG C20 H20B sing N N 45  
A1BEG C17 H17  sing N N 46  
A1BEG C16 H16  sing N N 47  
A1BEG C15 H15B sing N N 48  
A1BEG C15 H15A sing N N 49  
A1BEG C15 H15C sing N N 50  
A1BEG C1  H1C  sing N N 51  
A1BEG C1  H1B  sing N N 52  
A1BEG C1  H1A  sing N N 53  
A1BEG C4  H4   sing N N 54  
A1BEG C7  H7   sing N N 55  
A1BEG C9  H9   sing N N 56  
A1BEG C10 H10C sing N N 57  
A1BEG C10 H10B sing N N 58  
A1BEG C10 H10A sing N N 59  
A1BEG C22 H22A sing N N 60  
A1BEG C22 H22B sing N N 61  
A1BEG C23 H23A sing N N 62  
A1BEG C23 H23B sing N N 63  
A1BEG C24 H24  sing N N 64  
A1BEG C25 H25A sing N N 65  
A1BEG C25 H25B sing N N 66  
A1BEG C27 H27B sing N N 67  
A1BEG C27 H27A sing N N 68  
A1BEG C27 H27C sing N N 69  
A1BEG C28 H28  sing N N 70  
A1BEG C31 H31  sing N N 71  
A1BEG C32 H32  sing N N 72  
A1BEG C33 H33  sing N N 73  
A1BEG C34 H34  sing N N 74  
A1BEG C37 H37  sing N N 75  
A1BEG N11 H11  sing N N 76  
ACT   C   O    doub N N 77  
ACT   C   OXT  sing N N 78  
ACT   C   CH3  sing N N 79  
ACT   CH3 H1   sing N N 80  
ACT   CH3 H2   sing N N 81  
ACT   CH3 H3   sing N N 82  
ALA   N   CA   sing N N 83  
ALA   N   H    sing N N 84  
ALA   N   H2   sing N N 85  
ALA   CA  C    sing N N 86  
ALA   CA  CB   sing N N 87  
ALA   CA  HA   sing N N 88  
ALA   C   O    doub N N 89  
ALA   C   OXT  sing N N 90  
ALA   CB  HB1  sing N N 91  
ALA   CB  HB2  sing N N 92  
ALA   CB  HB3  sing N N 93  
ALA   OXT HXT  sing N N 94  
ARG   N   CA   sing N N 95  
ARG   N   H    sing N N 96  
ARG   N   H2   sing N N 97  
ARG   CA  C    sing N N 98  
ARG   CA  CB   sing N N 99  
ARG   CA  HA   sing N N 100 
ARG   C   O    doub N N 101 
ARG   C   OXT  sing N N 102 
ARG   CB  CG   sing N N 103 
ARG   CB  HB2  sing N N 104 
ARG   CB  HB3  sing N N 105 
ARG   CG  CD   sing N N 106 
ARG   CG  HG2  sing N N 107 
ARG   CG  HG3  sing N N 108 
ARG   CD  NE   sing N N 109 
ARG   CD  HD2  sing N N 110 
ARG   CD  HD3  sing N N 111 
ARG   NE  CZ   sing N N 112 
ARG   NE  HE   sing N N 113 
ARG   CZ  NH1  sing N N 114 
ARG   CZ  NH2  doub N N 115 
ARG   NH1 HH11 sing N N 116 
ARG   NH1 HH12 sing N N 117 
ARG   NH2 HH21 sing N N 118 
ARG   NH2 HH22 sing N N 119 
ARG   OXT HXT  sing N N 120 
ASN   N   CA   sing N N 121 
ASN   N   H    sing N N 122 
ASN   N   H2   sing N N 123 
ASN   CA  C    sing N N 124 
ASN   CA  CB   sing N N 125 
ASN   CA  HA   sing N N 126 
ASN   C   O    doub N N 127 
ASN   C   OXT  sing N N 128 
ASN   CB  CG   sing N N 129 
ASN   CB  HB2  sing N N 130 
ASN   CB  HB3  sing N N 131 
ASN   CG  OD1  doub N N 132 
ASN   CG  ND2  sing N N 133 
ASN   ND2 HD21 sing N N 134 
ASN   ND2 HD22 sing N N 135 
ASN   OXT HXT  sing N N 136 
ASP   N   CA   sing N N 137 
ASP   N   H    sing N N 138 
ASP   N   H2   sing N N 139 
ASP   CA  C    sing N N 140 
ASP   CA  CB   sing N N 141 
ASP   CA  HA   sing N N 142 
ASP   C   O    doub N N 143 
ASP   C   OXT  sing N N 144 
ASP   CB  CG   sing N N 145 
ASP   CB  HB2  sing N N 146 
ASP   CB  HB3  sing N N 147 
ASP   CG  OD1  doub N N 148 
ASP   CG  OD2  sing N N 149 
ASP   OD2 HD2  sing N N 150 
ASP   OXT HXT  sing N N 151 
CYS   N   CA   sing N N 152 
CYS   N   H    sing N N 153 
CYS   N   H2   sing N N 154 
CYS   CA  C    sing N N 155 
CYS   CA  CB   sing N N 156 
CYS   CA  HA   sing N N 157 
CYS   C   O    doub N N 158 
CYS   C   OXT  sing N N 159 
CYS   CB  SG   sing N N 160 
CYS   CB  HB2  sing N N 161 
CYS   CB  HB3  sing N N 162 
CYS   SG  HG   sing N N 163 
CYS   OXT HXT  sing N N 164 
EDO   C1  O1   sing N N 165 
EDO   C1  C2   sing N N 166 
EDO   C1  H11  sing N N 167 
EDO   C1  H12  sing N N 168 
EDO   O1  HO1  sing N N 169 
EDO   C2  O2   sing N N 170 
EDO   C2  H21  sing N N 171 
EDO   C2  H22  sing N N 172 
EDO   O2  HO2  sing N N 173 
GLN   N   CA   sing N N 174 
GLN   N   H    sing N N 175 
GLN   N   H2   sing N N 176 
GLN   CA  C    sing N N 177 
GLN   CA  CB   sing N N 178 
GLN   CA  HA   sing N N 179 
GLN   C   O    doub N N 180 
GLN   C   OXT  sing N N 181 
GLN   CB  CG   sing N N 182 
GLN   CB  HB2  sing N N 183 
GLN   CB  HB3  sing N N 184 
GLN   CG  CD   sing N N 185 
GLN   CG  HG2  sing N N 186 
GLN   CG  HG3  sing N N 187 
GLN   CD  OE1  doub N N 188 
GLN   CD  NE2  sing N N 189 
GLN   NE2 HE21 sing N N 190 
GLN   NE2 HE22 sing N N 191 
GLN   OXT HXT  sing N N 192 
GLU   N   CA   sing N N 193 
GLU   N   H    sing N N 194 
GLU   N   H2   sing N N 195 
GLU   CA  C    sing N N 196 
GLU   CA  CB   sing N N 197 
GLU   CA  HA   sing N N 198 
GLU   C   O    doub N N 199 
GLU   C   OXT  sing N N 200 
GLU   CB  CG   sing N N 201 
GLU   CB  HB2  sing N N 202 
GLU   CB  HB3  sing N N 203 
GLU   CG  CD   sing N N 204 
GLU   CG  HG2  sing N N 205 
GLU   CG  HG3  sing N N 206 
GLU   CD  OE1  doub N N 207 
GLU   CD  OE2  sing N N 208 
GLU   OE2 HE2  sing N N 209 
GLU   OXT HXT  sing N N 210 
GLY   N   CA   sing N N 211 
GLY   N   H    sing N N 212 
GLY   N   H2   sing N N 213 
GLY   CA  C    sing N N 214 
GLY   CA  HA2  sing N N 215 
GLY   CA  HA3  sing N N 216 
GLY   C   O    doub N N 217 
GLY   C   OXT  sing N N 218 
GLY   OXT HXT  sing N N 219 
HIS   N   CA   sing N N 220 
HIS   N   H    sing N N 221 
HIS   N   H2   sing N N 222 
HIS   CA  C    sing N N 223 
HIS   CA  CB   sing N N 224 
HIS   CA  HA   sing N N 225 
HIS   C   O    doub N N 226 
HIS   C   OXT  sing N N 227 
HIS   CB  CG   sing N N 228 
HIS   CB  HB2  sing N N 229 
HIS   CB  HB3  sing N N 230 
HIS   CG  ND1  sing Y N 231 
HIS   CG  CD2  doub Y N 232 
HIS   ND1 CE1  doub Y N 233 
HIS   ND1 HD1  sing N N 234 
HIS   CD2 NE2  sing Y N 235 
HIS   CD2 HD2  sing N N 236 
HIS   CE1 NE2  sing Y N 237 
HIS   CE1 HE1  sing N N 238 
HIS   NE2 HE2  sing N N 239 
HIS   OXT HXT  sing N N 240 
HOH   O   H1   sing N N 241 
HOH   O   H2   sing N N 242 
ILE   N   CA   sing N N 243 
ILE   N   H    sing N N 244 
ILE   N   H2   sing N N 245 
ILE   CA  C    sing N N 246 
ILE   CA  CB   sing N N 247 
ILE   CA  HA   sing N N 248 
ILE   C   O    doub N N 249 
ILE   C   OXT  sing N N 250 
ILE   CB  CG1  sing N N 251 
ILE   CB  CG2  sing N N 252 
ILE   CB  HB   sing N N 253 
ILE   CG1 CD1  sing N N 254 
ILE   CG1 HG12 sing N N 255 
ILE   CG1 HG13 sing N N 256 
ILE   CG2 HG21 sing N N 257 
ILE   CG2 HG22 sing N N 258 
ILE   CG2 HG23 sing N N 259 
ILE   CD1 HD11 sing N N 260 
ILE   CD1 HD12 sing N N 261 
ILE   CD1 HD13 sing N N 262 
ILE   OXT HXT  sing N N 263 
LEU   N   CA   sing N N 264 
LEU   N   H    sing N N 265 
LEU   N   H2   sing N N 266 
LEU   CA  C    sing N N 267 
LEU   CA  CB   sing N N 268 
LEU   CA  HA   sing N N 269 
LEU   C   O    doub N N 270 
LEU   C   OXT  sing N N 271 
LEU   CB  CG   sing N N 272 
LEU   CB  HB2  sing N N 273 
LEU   CB  HB3  sing N N 274 
LEU   CG  CD1  sing N N 275 
LEU   CG  CD2  sing N N 276 
LEU   CG  HG   sing N N 277 
LEU   CD1 HD11 sing N N 278 
LEU   CD1 HD12 sing N N 279 
LEU   CD1 HD13 sing N N 280 
LEU   CD2 HD21 sing N N 281 
LEU   CD2 HD22 sing N N 282 
LEU   CD2 HD23 sing N N 283 
LEU   OXT HXT  sing N N 284 
LYS   N   CA   sing N N 285 
LYS   N   H    sing N N 286 
LYS   N   H2   sing N N 287 
LYS   CA  C    sing N N 288 
LYS   CA  CB   sing N N 289 
LYS   CA  HA   sing N N 290 
LYS   C   O    doub N N 291 
LYS   C   OXT  sing N N 292 
LYS   CB  CG   sing N N 293 
LYS   CB  HB2  sing N N 294 
LYS   CB  HB3  sing N N 295 
LYS   CG  CD   sing N N 296 
LYS   CG  HG2  sing N N 297 
LYS   CG  HG3  sing N N 298 
LYS   CD  CE   sing N N 299 
LYS   CD  HD2  sing N N 300 
LYS   CD  HD3  sing N N 301 
LYS   CE  NZ   sing N N 302 
LYS   CE  HE2  sing N N 303 
LYS   CE  HE3  sing N N 304 
LYS   NZ  HZ1  sing N N 305 
LYS   NZ  HZ2  sing N N 306 
LYS   NZ  HZ3  sing N N 307 
LYS   OXT HXT  sing N N 308 
MET   N   CA   sing N N 309 
MET   N   H    sing N N 310 
MET   N   H2   sing N N 311 
MET   CA  C    sing N N 312 
MET   CA  CB   sing N N 313 
MET   CA  HA   sing N N 314 
MET   C   O    doub N N 315 
MET   C   OXT  sing N N 316 
MET   CB  CG   sing N N 317 
MET   CB  HB2  sing N N 318 
MET   CB  HB3  sing N N 319 
MET   CG  SD   sing N N 320 
MET   CG  HG2  sing N N 321 
MET   CG  HG3  sing N N 322 
MET   SD  CE   sing N N 323 
MET   CE  HE1  sing N N 324 
MET   CE  HE2  sing N N 325 
MET   CE  HE3  sing N N 326 
MET   OXT HXT  sing N N 327 
PHE   N   CA   sing N N 328 
PHE   N   H    sing N N 329 
PHE   N   H2   sing N N 330 
PHE   CA  C    sing N N 331 
PHE   CA  CB   sing N N 332 
PHE   CA  HA   sing N N 333 
PHE   C   O    doub N N 334 
PHE   C   OXT  sing N N 335 
PHE   CB  CG   sing N N 336 
PHE   CB  HB2  sing N N 337 
PHE   CB  HB3  sing N N 338 
PHE   CG  CD1  doub Y N 339 
PHE   CG  CD2  sing Y N 340 
PHE   CD1 CE1  sing Y N 341 
PHE   CD1 HD1  sing N N 342 
PHE   CD2 CE2  doub Y N 343 
PHE   CD2 HD2  sing N N 344 
PHE   CE1 CZ   doub Y N 345 
PHE   CE1 HE1  sing N N 346 
PHE   CE2 CZ   sing Y N 347 
PHE   CE2 HE2  sing N N 348 
PHE   CZ  HZ   sing N N 349 
PHE   OXT HXT  sing N N 350 
PRO   N   CA   sing N N 351 
PRO   N   CD   sing N N 352 
PRO   N   H    sing N N 353 
PRO   CA  C    sing N N 354 
PRO   CA  CB   sing N N 355 
PRO   CA  HA   sing N N 356 
PRO   C   O    doub N N 357 
PRO   C   OXT  sing N N 358 
PRO   CB  CG   sing N N 359 
PRO   CB  HB2  sing N N 360 
PRO   CB  HB3  sing N N 361 
PRO   CG  CD   sing N N 362 
PRO   CG  HG2  sing N N 363 
PRO   CG  HG3  sing N N 364 
PRO   CD  HD2  sing N N 365 
PRO   CD  HD3  sing N N 366 
PRO   OXT HXT  sing N N 367 
SER   N   CA   sing N N 368 
SER   N   H    sing N N 369 
SER   N   H2   sing N N 370 
SER   CA  C    sing N N 371 
SER   CA  CB   sing N N 372 
SER   CA  HA   sing N N 373 
SER   C   O    doub N N 374 
SER   C   OXT  sing N N 375 
SER   CB  OG   sing N N 376 
SER   CB  HB2  sing N N 377 
SER   CB  HB3  sing N N 378 
SER   OG  HG   sing N N 379 
SER   OXT HXT  sing N N 380 
THR   N   CA   sing N N 381 
THR   N   H    sing N N 382 
THR   N   H2   sing N N 383 
THR   CA  C    sing N N 384 
THR   CA  CB   sing N N 385 
THR   CA  HA   sing N N 386 
THR   C   O    doub N N 387 
THR   C   OXT  sing N N 388 
THR   CB  OG1  sing N N 389 
THR   CB  CG2  sing N N 390 
THR   CB  HB   sing N N 391 
THR   OG1 HG1  sing N N 392 
THR   CG2 HG21 sing N N 393 
THR   CG2 HG22 sing N N 394 
THR   CG2 HG23 sing N N 395 
THR   OXT HXT  sing N N 396 
TRP   N   CA   sing N N 397 
TRP   N   H    sing N N 398 
TRP   N   H2   sing N N 399 
TRP   CA  C    sing N N 400 
TRP   CA  CB   sing N N 401 
TRP   CA  HA   sing N N 402 
TRP   C   O    doub N N 403 
TRP   C   OXT  sing N N 404 
TRP   CB  CG   sing N N 405 
TRP   CB  HB2  sing N N 406 
TRP   CB  HB3  sing N N 407 
TRP   CG  CD1  doub Y N 408 
TRP   CG  CD2  sing Y N 409 
TRP   CD1 NE1  sing Y N 410 
TRP   CD1 HD1  sing N N 411 
TRP   CD2 CE2  doub Y N 412 
TRP   CD2 CE3  sing Y N 413 
TRP   NE1 CE2  sing Y N 414 
TRP   NE1 HE1  sing N N 415 
TRP   CE2 CZ2  sing Y N 416 
TRP   CE3 CZ3  doub Y N 417 
TRP   CE3 HE3  sing N N 418 
TRP   CZ2 CH2  doub Y N 419 
TRP   CZ2 HZ2  sing N N 420 
TRP   CZ3 CH2  sing Y N 421 
TRP   CZ3 HZ3  sing N N 422 
TRP   CH2 HH2  sing N N 423 
TRP   OXT HXT  sing N N 424 
TYR   N   CA   sing N N 425 
TYR   N   H    sing N N 426 
TYR   N   H2   sing N N 427 
TYR   CA  C    sing N N 428 
TYR   CA  CB   sing N N 429 
TYR   CA  HA   sing N N 430 
TYR   C   O    doub N N 431 
TYR   C   OXT  sing N N 432 
TYR   CB  CG   sing N N 433 
TYR   CB  HB2  sing N N 434 
TYR   CB  HB3  sing N N 435 
TYR   CG  CD1  doub Y N 436 
TYR   CG  CD2  sing Y N 437 
TYR   CD1 CE1  sing Y N 438 
TYR   CD1 HD1  sing N N 439 
TYR   CD2 CE2  doub Y N 440 
TYR   CD2 HD2  sing N N 441 
TYR   CE1 CZ   doub Y N 442 
TYR   CE1 HE1  sing N N 443 
TYR   CE2 CZ   sing Y N 444 
TYR   CE2 HE2  sing N N 445 
TYR   CZ  OH   sing N N 446 
TYR   OH  HH   sing N N 447 
TYR   OXT HXT  sing N N 448 
VAL   N   CA   sing N N 449 
VAL   N   H    sing N N 450 
VAL   N   H2   sing N N 451 
VAL   CA  C    sing N N 452 
VAL   CA  CB   sing N N 453 
VAL   CA  HA   sing N N 454 
VAL   C   O    doub N N 455 
VAL   C   OXT  sing N N 456 
VAL   CB  CG1  sing N N 457 
VAL   CB  CG2  sing N N 458 
VAL   CB  HB   sing N N 459 
VAL   CG1 HG11 sing N N 460 
VAL   CG1 HG12 sing N N 461 
VAL   CG1 HG13 sing N N 462 
VAL   CG2 HG21 sing N N 463 
VAL   CG2 HG22 sing N N 464 
VAL   CG2 HG23 sing N N 465 
VAL   OXT HXT  sing N N 466 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7NFV 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'I 41 2 2' 
_space_group.name_Hall        'I 4bw 2bw' 
_space_group.IT_number        98 
_space_group.crystal_system   tetragonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9DNU 
_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]   0.008798 
_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]   0.008798 
_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]   0.004545 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL ? ? 9.50761  7.44341 ? ? 1.04373  23.83732 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882  3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
ZN ? ? 24.64596 5.25405 ? ? 2.14387  29.76375 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . THR   A 1 7   ? 24.15100 70.89200 22.96600 1.000 106.23575 ? 4   THR   A N   1 
ATOM   2    C  CA  . THR   A 1 7   ? 25.49200 70.37600 23.22200 1.000 110.52069 ? 4   THR   A CA  1 
ATOM   3    C  C   . THR   A 1 7   ? 25.43500 69.07500 24.01500 1.000 112.14197 ? 4   THR   A C   1 
ATOM   4    O  O   . THR   A 1 7   ? 24.48600 68.83600 24.75900 1.000 114.68430 ? 4   THR   A O   1 
ATOM   5    C  CB  . THR   A 1 7   ? 26.37700 71.39400 23.99700 1.000 108.84765 ? 4   THR   A CB  1 
ATOM   6    O  OG1 . THR   A 1 7   ? 25.98600 71.44100 25.37500 1.000 106.59237 ? 4   THR   A OG1 1 
ATOM   7    C  CG2 . THR   A 1 7   ? 26.26800 72.78400 23.38700 1.000 106.03830 ? 4   THR   A CG2 1 
ATOM   8    N  N   . ILE   A 1 8   ? 26.46000 68.23600 23.84100 1.000 119.31159 ? 5   ILE   A N   1 
ATOM   9    C  CA  . ILE   A 1 8   ? 26.62100 66.99800 24.59000 1.000 113.41307 ? 5   ILE   A CA  1 
ATOM   10   C  C   . ILE   A 1 8   ? 28.06600 66.90600 25.06500 1.000 109.14047 ? 5   ILE   A C   1 
ATOM   11   O  O   . ILE   A 1 8   ? 28.96700 67.54900 24.52100 1.000 109.35106 ? 5   ILE   A O   1 
ATOM   12   C  CB  . ILE   A 1 8   ? 26.24500 65.74900 23.76000 1.000 100.04775 ? 5   ILE   A CB  1 
ATOM   13   N  N   . LYS   A 1 9   ? 28.27700 66.09900 26.10200 1.000 114.61778 ? 6   LYS   A N   1 
ATOM   14   C  CA  . LYS   A 1 9   ? 29.60200 65.85800 26.66000 1.000 121.64425 ? 6   LYS   A CA  1 
ATOM   15   C  C   . LYS   A 1 9   ? 30.06700 64.45500 26.28900 1.000 118.71656 ? 6   LYS   A C   1 
ATOM   16   O  O   . LYS   A 1 9   ? 29.28300 63.49900 26.33200 1.000 113.47309 ? 6   LYS   A O   1 
ATOM   17   C  CB  . LYS   A 1 9   ? 29.60600 66.02400 28.18600 1.000 112.83133 ? 6   LYS   A CB  1 
ATOM   18   C  CG  . LYS   A 1 9   ? 29.25200 67.42400 28.66300 1.000 117.13002 ? 6   LYS   A CG  1 
ATOM   19   C  CD  . LYS   A 1 9   ? 29.26000 67.51300 30.18300 1.000 125.18474 ? 6   LYS   A CD  1 
ATOM   20   C  CE  . LYS   A 1 9   ? 28.78600 68.88000 30.66300 1.000 128.02256 ? 6   LYS   A CE  1 
ATOM   21   N  NZ  . LYS   A 1 9   ? 28.83400 68.99500 32.14900 1.000 123.55608 ? 6   LYS   A NZ  1 
ATOM   22   N  N   . VAL   A 1 10  ? 31.34500 64.33500 25.91900 1.000 105.11100 ? 7   VAL   A N   1 
ATOM   23   C  CA  . VAL   A 1 10  ? 31.93400 63.06700 25.50800 1.000 98.13342  ? 7   VAL   A CA  1 
ATOM   24   C  C   . VAL   A 1 10  ? 33.36800 62.98700 26.01700 1.000 98.77990  ? 7   VAL   A C   1 
ATOM   25   O  O   . VAL   A 1 10  ? 33.95100 63.97300 26.47600 1.000 98.39004  ? 7   VAL   A O   1 
ATOM   26   C  CB  . VAL   A 1 10  ? 31.91300 62.87700 23.97500 1.000 105.95091 ? 7   VAL   A CB  1 
ATOM   27   C  CG1 . VAL   A 1 10  ? 30.50400 62.59100 23.48600 1.000 101.59210 ? 7   VAL   A CG1 1 
ATOM   28   C  CG2 . VAL   A 1 10  ? 32.49400 64.10500 23.28200 1.000 102.75742 ? 7   VAL   A CG2 1 
ATOM   29   N  N   . PHE   A 1 11  ? 33.93000 61.78200 25.93600 1.000 102.98044 ? 8   PHE   A N   1 
ATOM   30   C  CA  . PHE   A 1 11  ? 35.35200 61.54600 26.13800 1.000 87.08579  ? 8   PHE   A CA  1 
ATOM   31   C  C   . PHE   A 1 11  ? 35.98900 61.17100 24.80800 1.000 81.77836  ? 8   PHE   A C   1 
ATOM   32   O  O   . PHE   A 1 11  ? 35.43800 60.36700 24.04500 1.000 82.02273  ? 8   PHE   A O   1 
ATOM   33   C  CB  . PHE   A 1 11  ? 35.60700 60.42500 27.15100 1.000 85.14763  ? 8   PHE   A CB  1 
ATOM   34   C  CG  . PHE   A 1 11  ? 34.94500 60.63600 28.47800 1.000 97.35945  ? 8   PHE   A CG  1 
ATOM   35   C  CD1 . PHE   A 1 11  ? 35.46900 61.53600 29.39400 1.000 92.79739  ? 8   PHE   A CD1 1 
ATOM   36   C  CD2 . PHE   A 1 11  ? 33.80200 59.92300 28.81800 1.000 95.40531  ? 8   PHE   A CD2 1 
ATOM   37   C  CE1 . PHE   A 1 11  ? 34.86300 61.73000 30.62100 1.000 85.67550  ? 8   PHE   A CE1 1 
ATOM   38   C  CE2 . PHE   A 1 11  ? 33.19000 60.11300 30.04400 1.000 90.52758  ? 8   PHE   A CE2 1 
ATOM   39   C  CZ  . PHE   A 1 11  ? 33.72200 61.01900 30.94600 1.000 87.55184  ? 8   PHE   A CZ  1 
ATOM   40   N  N   . THR   A 1 12  ? 37.14600 61.75800 24.52800 1.000 70.12645  ? 9   THR   A N   1 
ATOM   41   C  CA  . THR   A 1 12  ? 37.96700 61.35300 23.40200 1.000 71.43300  ? 9   THR   A CA  1 
ATOM   42   C  C   . THR   A 1 12  ? 39.20100 60.62000 23.91400 1.000 68.57785  ? 9   THR   A C   1 
ATOM   43   O  O   . THR   A 1 12  ? 39.65600 60.84400 25.03700 1.000 58.70502  ? 9   THR   A O   1 
ATOM   44   C  CB  . THR   A 1 12  ? 38.38700 62.55600 22.55800 1.000 63.11094  ? 9   THR   A CB  1 
ATOM   45   O  OG1 . THR   A 1 12  ? 39.08800 63.48700 23.38900 1.000 68.64987  ? 9   THR   A OG1 1 
ATOM   46   C  CG2 . THR   A 1 12  ? 37.17500 63.22300 21.96200 1.000 70.41221  ? 9   THR   A CG2 1 
ATOM   47   N  N   . THR   A 1 13  ? 39.74400 59.74500 23.07600 1.000 60.33730  ? 10  THR   A N   1 
ATOM   48   C  CA  . THR   A 1 13  ? 40.89600 58.95600 23.47800 1.000 58.38221  ? 10  THR   A CA  1 
ATOM   49   C  C   . THR   A 1 13  ? 41.57700 58.42300 22.22900 1.000 59.35304  ? 10  THR   A C   1 
ATOM   50   O  O   . THR   A 1 13  ? 40.97800 58.35800 21.15100 1.000 54.24267  ? 10  THR   A O   1 
ATOM   51   C  CB  . THR   A 1 13  ? 40.48000 57.80500 24.41200 1.000 60.39811  ? 10  THR   A CB  1 
ATOM   52   O  OG1 . THR   A 1 13  ? 41.63400 57.25000 25.04900 1.000 65.13172  ? 10  THR   A OG1 1 
ATOM   53   C  CG2 . THR   A 1 13  ? 39.77100 56.71400 23.63000 1.000 57.39129  ? 10  THR   A CG2 1 
ATOM   54   N  N   . VAL   A 1 14  ? 42.84100 58.03800 22.38600 1.000 52.16805  ? 11  VAL   A N   1 
ATOM   55   C  CA  . VAL   A 1 14  ? 43.51200 57.23200 21.37200 1.000 52.86584  ? 11  VAL   A CA  1 
ATOM   56   C  C   . VAL   A 1 14  ? 43.81700 55.82400 21.85100 1.000 58.82971  ? 11  VAL   A C   1 
ATOM   57   O  O   . VAL   A 1 14  ? 44.13500 54.96500 21.01400 1.000 55.02850  ? 11  VAL   A O   1 
ATOM   58   C  CB  . VAL   A 1 14  ? 44.80400 57.90400 20.86300 1.000 53.66648  ? 11  VAL   A CB  1 
ATOM   59   C  CG1 . VAL   A 1 14  ? 44.50000 59.31800 20.40600 1.000 60.81927  ? 11  VAL   A CG1 1 
ATOM   60   C  CG2 . VAL   A 1 14  ? 45.88600 57.88100 21.94000 1.000 52.95736  ? 11  VAL   A CG2 1 
ATOM   61   N  N   . ASP   A 1 15  ? 43.71700 55.54800 23.15400 1.000 57.41515  ? 12  ASP   A N   1 
ATOM   62   C  CA  . ASP   A 1 15  ? 44.09200 54.24500 23.68400 1.000 54.00370  ? 12  ASP   A CA  1 
ATOM   63   C  C   . ASP   A 1 15  ? 43.00800 53.61000 24.53500 1.000 61.64658  ? 12  ASP   A C   1 
ATOM   64   O  O   . ASP   A 1 15  ? 43.21300 52.49900 25.03600 1.000 66.56727  ? 12  ASP   A O   1 
ATOM   65   C  CB  . ASP   A 1 15  ? 45.38200 54.34800 24.51800 1.000 51.36734  ? 12  ASP   A CB  1 
ATOM   66   C  CG  . ASP   A 1 15  ? 45.30300 55.41700 25.59400 1.000 50.49460  ? 12  ASP   A CG  1 
ATOM   67   O  OD1 . ASP   A 1 15  ? 44.18500 55.85000 25.92800 1.000 56.38257  ? 12  ASP   A OD1 1 
ATOM   68   O  OD2 . ASP   A 1 15  ? 46.36400 55.82700 26.10600 1.000 51.62857  ? 12  ASP   A OD2 1 
ATOM   69   N  N   . ASN   A 1 16  ? 41.87700 54.28800 24.73000 1.000 65.89097  ? 13  ASN   A N   1 
ATOM   70   C  CA  . ASN   A 1 16  ? 40.81000 53.81800 25.60900 1.000 75.61638  ? 13  ASN   A CA  1 
ATOM   71   C  C   . ASN   A 1 16  ? 41.30900 53.60500 27.03500 1.000 61.72856  ? 13  ASN   A C   1 
ATOM   72   O  O   . ASN   A 1 16  ? 40.78900 52.75500 27.75700 1.000 66.14527  ? 13  ASN   A O   1 
ATOM   73   C  CB  . ASN   A 1 16  ? 40.15600 52.54400 25.06100 1.000 76.23630  ? 13  ASN   A CB  1 
ATOM   74   C  CG  . ASN   A 1 16  ? 38.77500 52.31100 25.62900 1.000 76.07906  ? 13  ASN   A CG  1 
ATOM   75   O  OD1 . ASN   A 1 16  ? 38.06200 53.25600 25.96900 1.000 73.80999  ? 13  ASN   A OD1 1 
ATOM   76   N  ND2 . ASN   A 1 16  ? 38.38800 51.04600 25.73500 1.000 88.07024  ? 13  ASN   A ND2 1 
ATOM   77   N  N   . ILE   A 1 17  ? 42.32000 54.37800 27.44300 1.000 65.73133  ? 14  ILE   A N   1 
ATOM   78   C  CA  . ILE   A 1 17  ? 42.85100 54.33900 28.80500 1.000 62.25203  ? 14  ILE   A CA  1 
ATOM   79   C  C   . ILE   A 1 17  ? 42.88200 55.74400 29.38700 1.000 67.78088  ? 14  ILE   A C   1 
ATOM   80   O  O   . ILE   A 1 17  ? 42.24000 56.02000 30.40600 1.000 76.72692  ? 14  ILE   A O   1 
ATOM   81   C  CB  . ILE   A 1 17  ? 44.25700 53.72200 28.85600 1.000 63.54876  ? 14  ILE   A CB  1 
ATOM   82   C  CG1 . ILE   A 1 17  ? 44.18500 52.21800 28.64800 1.000 68.25949  ? 14  ILE   A CG1 1 
ATOM   83   C  CG2 . ILE   A 1 17  ? 44.92300 54.02300 30.18900 1.000 53.03119  ? 14  ILE   A CG2 1 
ATOM   84   C  CD1 . ILE   A 1 17  ? 45.45700 51.65600 28.12500 1.000 62.44662  ? 14  ILE   A CD1 1 
ATOM   85   N  N   . ASN   A 1 18  ? 43.65800 56.62800 28.76300 1.000 63.93901  ? 15  ASN   A N   1 
ATOM   86   C  CA  . ASN   A 1 18  ? 43.63600 58.04800 29.09000 1.000 63.80094  ? 15  ASN   A CA  1 
ATOM   87   C  C   . ASN   A 1 18  ? 42.45400 58.68200 28.36400 1.000 63.69665  ? 15  ASN   A C   1 
ATOM   88   O  O   . ASN   A 1 18  ? 42.45600 58.77900 27.13400 1.000 73.26852  ? 15  ASN   A O   1 
ATOM   89   C  CB  . ASN   A 1 18  ? 44.95200 58.70800 28.68700 1.000 63.85868  ? 15  ASN   A CB  1 
ATOM   90   C  CG  . ASN   A 1 18  ? 46.16600 58.03600 29.32000 1.000 65.69842  ? 15  ASN   A CG  1 
ATOM   91   O  OD1 . ASN   A 1 18  ? 46.52400 58.33300 30.45300 1.000 75.22824  ? 15  ASN   A OD1 1 
ATOM   92   N  ND2 . ASN   A 1 18  ? 46.80400 57.13400 28.58500 1.000 64.24774  ? 15  ASN   A ND2 1 
ATOM   93   N  N   . LEU   A 1 19  ? 41.42600 59.08300 29.10900 1.000 74.06658  ? 16  LEU   A N   1 
ATOM   94   C  CA  . LEU   A 1 19  ? 40.23900 59.69400 28.52100 1.000 75.94745  ? 16  LEU   A CA  1 
ATOM   95   C  C   . LEU   A 1 19  ? 40.26600 61.20300 28.72900 1.000 73.84943  ? 16  LEU   A C   1 
ATOM   96   O  O   . LEU   A 1 19  ? 40.67900 61.69000 29.78300 1.000 75.90108  ? 16  LEU   A O   1 
ATOM   97   C  CB  . LEU   A 1 19  ? 38.95600 59.10800 29.11500 1.000 68.24612  ? 16  LEU   A CB  1 
ATOM   98   C  CG  . LEU   A 1 19  ? 38.88200 57.58500 29.18700 1.000 79.62481  ? 16  LEU   A CG  1 
ATOM   99   C  CD1 . LEU   A 1 19  ? 37.50400 57.15100 29.66400 1.000 75.37106  ? 16  LEU   A CD1 1 
ATOM   100  C  CD2 . LEU   A 1 19  ? 39.20300 56.96700 27.83000 1.000 68.67526  ? 16  LEU   A CD2 1 
ATOM   101  N  N   . HIS   A 1 20  ? 39.82500 61.93900 27.71200 1.000 79.72344  ? 17  HIS   A N   1 
ATOM   102  C  CA  . HIS   A 1 20  ? 39.87300 63.39500 27.71000 1.000 83.32884  ? 17  HIS   A CA  1 
ATOM   103  C  C   . HIS   A 1 20  ? 38.45700 63.93500 27.62800 1.000 87.70655  ? 17  HIS   A C   1 
ATOM   104  O  O   . HIS   A 1 20  ? 37.72200 63.61700 26.68700 1.000 83.74638  ? 17  HIS   A O   1 
ATOM   105  C  CB  . HIS   A 1 20  ? 40.72300 63.90800 26.55100 1.000 77.10155  ? 17  HIS   A CB  1 
ATOM   106  C  CG  . HIS   A 1 20  ? 42.13400 63.41400 26.59400 1.000 86.98213  ? 17  HIS   A CG  1 
ATOM   107  N  ND1 . HIS   A 1 20  ? 42.49700 62.15900 26.15500 1.000 84.47942  ? 17  HIS   A ND1 1 
ATOM   108  C  CD2 . HIS   A 1 20  ? 43.26600 63.98900 27.06900 1.000 87.38806  ? 17  HIS   A CD2 1 
ATOM   109  C  CE1 . HIS   A 1 20  ? 43.79600 61.99100 26.33300 1.000 79.38821  ? 17  HIS   A CE1 1 
ATOM   110  N  NE2 . HIS   A 1 20  ? 44.28500 63.08500 26.88700 1.000 81.59485  ? 17  HIS   A NE2 1 
ATOM   111  N  N   . THR   A 1 21  ? 38.07600 64.74000 28.61400 1.000 97.74857  ? 18  THR   A N   1 
ATOM   112  C  CA  . THR   A 1 21  ? 36.72000 65.26400 28.65700 1.000 95.40388  ? 18  THR   A CA  1 
ATOM   113  C  C   . THR   A 1 21  ? 36.56200 66.38200 27.62500 1.000 96.21995  ? 18  THR   A C   1 
ATOM   114  O  O   . THR   A 1 21  ? 37.43400 67.24500 27.48100 1.000 96.04810  ? 18  THR   A O   1 
ATOM   115  C  CB  . THR   A 1 21  ? 36.38800 65.72900 30.08100 1.000 92.19662  ? 18  THR   A CB  1 
ATOM   116  O  OG1 . THR   A 1 21  ? 34.96800 65.86800 30.22800 1.000 100.54882 ? 18  THR   A OG1 1 
ATOM   117  C  CG2 . THR   A 1 21  ? 37.09400 67.03300 30.44400 1.000 88.23963  ? 18  THR   A CG2 1 
ATOM   118  N  N   . GLN   A 1 22  ? 35.47600 66.32000 26.85500 1.000 90.18887  ? 19  GLN   A N   1 
ATOM   119  C  CA  . GLN   A 1 22  ? 35.22700 67.26900 25.78000 1.000 94.92384  ? 19  GLN   A CA  1 
ATOM   120  C  C   . GLN   A 1 22  ? 33.73900 67.57900 25.71300 1.000 105.62374 ? 19  GLN   A C   1 
ATOM   121  O  O   . GLN   A 1 22  ? 32.90100 66.73900 26.05200 1.000 103.28546 ? 19  GLN   A O   1 
ATOM   122  C  CB  . GLN   A 1 22  ? 35.68500 66.73700 24.41100 1.000 90.99920  ? 19  GLN   A CB  1 
ATOM   123  C  CG  . GLN   A 1 22  ? 37.08100 66.14900 24.36900 1.000 90.69656  ? 19  GLN   A CG  1 
ATOM   124  C  CD  . GLN   A 1 22  ? 38.16700 67.20100 24.42100 1.000 92.57256  ? 19  GLN   A CD  1 
ATOM   125  O  OE1 . GLN   A 1 22  ? 39.06600 67.14200 25.26100 1.000 104.67116 ? 19  GLN   A OE1 1 
ATOM   126  N  NE2 . GLN   A 1 22  ? 38.10200 68.16100 23.51000 1.000 83.45023  ? 19  GLN   A NE2 1 
ATOM   127  N  N   . VAL   A 1 23  ? 33.43800 68.80900 25.27400 1.000 106.42589 ? 20  VAL   A N   1 
ATOM   128  C  CA  . VAL   A 1 23  ? 32.02300 69.23100 25.06900 1.000 110.53150 ? 20  VAL   A CA  1 
ATOM   129  C  C   . VAL   A 1 23  ? 31.86700 69.55900 23.58500 1.000 106.58876 ? 20  VAL   A C   1 
ATOM   130  O  O   . VAL   A 1 23  ? 32.70600 70.31300 23.06400 1.000 100.57077 ? 20  VAL   A O   1 
ATOM   131  C  CB  . VAL   A 1 23  ? 31.63000 70.42600 25.95300 1.000 107.82428 ? 20  VAL   A CB  1 
ATOM   132  C  CG1 . VAL   A 1 23  ? 30.20000 70.86900 25.68500 1.000 107.93477 ? 20  VAL   A CG1 1 
ATOM   133  C  CG2 . VAL   A 1 23  ? 31.82500 70.11800 27.42900 1.000 105.52460 ? 20  VAL   A CG2 1 
ATOM   134  N  N   . VAL   A 1 24  ? 30.83700 69.02400 22.94300 1.000 106.10165 ? 21  VAL   A N   1 
ATOM   135  C  CA  . VAL   A 1 24  ? 30.61800 69.17800 21.51000 1.000 114.68225 ? 21  VAL   A CA  1 
ATOM   136  C  C   . VAL   A 1 24  ? 29.36500 70.01400 21.27200 1.000 115.37618 ? 21  VAL   A C   1 
ATOM   137  O  O   . VAL   A 1 24  ? 28.45800 70.07900 22.10600 1.000 120.11547 ? 21  VAL   A O   1 
ATOM   138  C  CB  . VAL   A 1 24  ? 30.50600 67.81300 20.79000 1.000 110.30319 ? 21  VAL   A CB  1 
ATOM   139  C  CG1 . VAL   A 1 24  ? 31.70700 66.94100 21.10300 1.000 99.98368  ? 21  VAL   A CG1 1 
ATOM   140  C  CG2 . VAL   A 1 24  ? 29.21100 67.09500 21.17200 1.000 109.22391 ? 21  VAL   A CG2 1 
ATOM   141  N  N   . ASP   A 1 25  ? 29.32100 70.66400 20.11100 1.000 113.80895 ? 22  ASP   A N   1 
ATOM   142  C  CA  . ASP   A 1 25  ? 28.10900 71.32100 19.64000 1.000 117.78923 ? 22  ASP   A CA  1 
ATOM   143  C  C   . ASP   A 1 25  ? 27.33700 70.33800 18.76900 1.000 121.04974 ? 22  ASP   A C   1 
ATOM   144  O  O   . ASP   A 1 25  ? 27.91200 69.71000 17.87300 1.000 121.56915 ? 22  ASP   A O   1 
ATOM   145  C  CB  . ASP   A 1 25  ? 28.43800 72.59400 18.85800 1.000 117.02548 ? 22  ASP   A CB  1 
ATOM   146  C  CG  . ASP   A 1 25  ? 27.30800 73.02200 17.93400 1.000 119.33692 ? 22  ASP   A CG  1 
ATOM   147  O  OD1 . ASP   A 1 25  ? 26.13200 72.94100 18.34400 1.000 121.72976 ? 22  ASP   A OD1 1 
ATOM   148  O  OD2 . ASP   A 1 25  ? 27.59700 73.44800 16.79800 1.000 119.17694 ? 22  ASP   A OD2 1 
ATOM   149  N  N   . MET   A 1 26  ? 26.03400 70.21000 19.03100 1.000 116.02152 ? 23  MET   A N   1 
ATOM   150  C  CA  . MET   A 1 26  ? 25.23600 69.17900 18.37500 1.000 121.48763 ? 23  MET   A CA  1 
ATOM   151  C  C   . MET   A 1 26  ? 24.92700 69.49400 16.91200 1.000 121.73294 ? 23  MET   A C   1 
ATOM   152  O  O   . MET   A 1 26  ? 24.36200 68.63800 16.22000 1.000 113.53021 ? 23  MET   A O   1 
ATOM   153  C  CB  . MET   A 1 26  ? 23.93700 68.96000 19.15500 1.000 113.31334 ? 23  MET   A CB  1 
ATOM   154  C  CG  . MET   A 1 26  ? 24.14900 68.31900 20.52100 1.000 119.07015 ? 23  MET   A CG  1 
ATOM   155  S  SD  . MET   A 1 26  ? 23.95200 66.52200 20.54900 1.000 129.13274 ? 23  MET   A SD  1 
ATOM   156  C  CE  . MET   A 1 26  ? 22.63000 66.35900 21.74900 1.000 111.48872 ? 23  MET   A CE  1 
ATOM   157  N  N   . SER   A 1 27  ? 25.28100 70.68200 16.42500 1.000 123.81494 ? 24  SER   A N   1 
ATOM   158  C  CA  . SER   A 1 27  ? 25.07500 71.05100 15.03000 1.000 124.42860 ? 24  SER   A CA  1 
ATOM   159  C  C   . SER   A 1 27  ? 26.35200 70.97100 14.20600 1.000 123.48920 ? 24  SER   A C   1 
ATOM   160  O  O   . SER   A 1 27  ? 26.33500 71.33100 13.02600 1.000 114.72420 ? 24  SER   A O   1 
ATOM   161  C  CB  . SER   A 1 27  ? 24.48900 72.46600 14.93800 1.000 122.99100 ? 24  SER   A CB  1 
ATOM   162  O  OG  . SER   A 1 27  ? 25.50600 73.44900 15.02700 1.000 120.29901 ? 24  SER   A OG  1 
ATOM   163  N  N   . MET   A 1 28  ? 27.45000 70.50500 14.79700 1.000 125.92775 ? 25  MET   A N   1 
ATOM   164  C  CA  . MET   A 1 28  ? 28.74900 70.44000 14.13900 1.000 118.05749 ? 25  MET   A CA  1 
ATOM   165  C  C   . MET   A 1 28  ? 29.20600 68.98700 14.13200 1.000 113.41506 ? 25  MET   A C   1 
ATOM   166  O  O   . MET   A 1 28  ? 29.31100 68.37000 15.19700 1.000 115.22193 ? 25  MET   A O   1 
ATOM   167  C  CB  . MET   A 1 28  ? 29.77100 71.32500 14.86100 1.000 113.01909 ? 25  MET   A CB  1 
ATOM   168  C  CG  . MET   A 1 28  ? 30.63900 72.17200 13.94000 1.000 109.49282 ? 25  MET   A CG  1 
ATOM   169  S  SD  . MET   A 1 28  ? 31.60300 73.44900 14.78700 1.000 126.84447 ? 25  MET   A SD  1 
ATOM   170  C  CE  . MET   A 1 28  ? 30.56300 73.85200 16.18700 1.000 105.12326 ? 25  MET   A CE  1 
ATOM   171  N  N   . THR   A 1 29  ? 29.47600 68.44400 12.94000 1.000 107.02488 ? 26  THR   A N   1 
ATOM   172  C  CA  . THR   A 1 29  ? 29.95500 67.06800 12.85300 1.000 107.19561 ? 26  THR   A CA  1 
ATOM   173  C  C   . THR   A 1 29  ? 31.25800 66.92100 13.62500 1.000 106.36546 ? 26  THR   A C   1 
ATOM   174  O  O   . THR   A 1 29  ? 32.01000 67.88400 13.81500 1.000 102.48685 ? 26  THR   A O   1 
ATOM   175  C  CB  . THR   A 1 29  ? 30.18200 66.62100 11.39800 1.000 102.61879 ? 26  THR   A CB  1 
ATOM   176  O  OG1 . THR   A 1 29  ? 31.04500 67.54100 10.71700 1.000 99.24410  ? 26  THR   A OG1 1 
ATOM   177  C  CG2 . THR   A 1 29  ? 28.87200 66.50100 10.64900 1.000 100.96885 ? 26  THR   A CG2 1 
ATOM   178  N  N   . TYR   A 1 30  ? 31.51900 65.68900 14.06800 1.000 99.40224  ? 27  TYR   A N   1 
ATOM   179  C  CA  . TYR   A 1 30  ? 32.71500 65.41500 14.85400 1.000 93.40764  ? 27  TYR   A CA  1 
ATOM   180  C  C   . TYR   A 1 30  ? 33.97900 65.80100 14.10100 1.000 84.93238  ? 27  TYR   A C   1 
ATOM   181  O  O   . TYR   A 1 30  ? 34.94700 66.26800 14.71300 1.000 81.35702  ? 27  TYR   A O   1 
ATOM   182  C  CB  . TYR   A 1 30  ? 32.74200 63.93600 15.24300 1.000 84.13481  ? 27  TYR   A CB  1 
ATOM   183  C  CG  . TYR   A 1 30  ? 31.72000 63.58000 16.29800 1.000 90.28041  ? 27  TYR   A CG  1 
ATOM   184  C  CD1 . TYR   A 1 30  ? 31.80500 64.11600 17.58400 1.000 76.74751  ? 27  TYR   A CD1 1 
ATOM   185  C  CD2 . TYR   A 1 30  ? 30.66400 62.72000 16.01200 1.000 83.31418  ? 27  TYR   A CD2 1 
ATOM   186  C  CE1 . TYR   A 1 30  ? 30.87500 63.80200 18.55500 1.000 83.06814  ? 27  TYR   A CE1 1 
ATOM   187  C  CE2 . TYR   A 1 30  ? 29.72400 62.39800 16.98100 1.000 91.85677  ? 27  TYR   A CE2 1 
ATOM   188  C  CZ  . TYR   A 1 30  ? 29.83600 62.94400 18.25200 1.000 90.31468  ? 27  TYR   A CZ  1 
ATOM   189  O  OH  . TYR   A 1 30  ? 28.91000 62.63300 19.22200 1.000 89.24606  ? 27  TYR   A OH  1 
ATOM   190  N  N   . GLY   A 1 31  ? 33.97400 65.64500 12.77400 1.000 86.03886  ? 28  GLY   A N   1 
ATOM   191  C  CA  . GLY   A 1 31  ? 35.15900 65.94000 11.98600 1.000 83.33808  ? 28  GLY   A CA  1 
ATOM   192  C  C   . GLY   A 1 31  ? 35.61600 67.38200 12.08300 1.000 91.55586  ? 28  GLY   A C   1 
ATOM   193  O  O   . GLY   A 1 31  ? 36.81800 67.65600 12.04600 1.000 89.09604  ? 28  GLY   A O   1 
ATOM   194  N  N   . GLN   A 1 32  ? 34.67600 68.32200 12.20100 1.000 96.42522  ? 29  GLN   A N   1 
ATOM   195  C  CA  . GLN   A 1 32  ? 35.05300 69.72400 12.32000 1.000 100.21735 ? 29  GLN   A CA  1 
ATOM   196  C  C   . GLN   A 1 32  ? 35.51100 70.09300 13.72100 1.000 90.36847  ? 29  GLN   A C   1 
ATOM   197  O  O   . GLN   A 1 32  ? 36.25100 71.06800 13.87600 1.000 99.44691  ? 29  GLN   A O   1 
ATOM   198  C  CB  . GLN   A 1 32  ? 33.89000 70.62400 11.91000 1.000 108.20039 ? 29  GLN   A CB  1 
ATOM   199  C  CG  . GLN   A 1 32  ? 33.54300 70.53400 10.43900 1.000 120.10403 ? 29  GLN   A CG  1 
ATOM   200  C  CD  . GLN   A 1 32  ? 32.34200 71.37900 10.07300 1.000 129.92831 ? 29  GLN   A CD  1 
ATOM   201  O  OE1 . GLN   A 1 32  ? 31.49900 71.66700 10.92000 1.000 124.22837 ? 29  GLN   A OE1 1 
ATOM   202  N  NE2 . GLN   A 1 32  ? 32.25200 71.77600 8.80700  1.000 126.70136 ? 29  GLN   A NE2 1 
ATOM   203  N  N   . GLN   A 1 33  ? 35.10600 69.33600 14.73500 1.000 86.11932  ? 30  GLN   A N   1 
ATOM   204  C  CA  . GLN   A 1 33  ? 35.48100 69.63900 16.11000 1.000 85.91094  ? 30  GLN   A CA  1 
ATOM   205  C  C   . GLN   A 1 33  ? 36.68200 68.83800 16.60300 1.000 89.55850  ? 30  GLN   A C   1 
ATOM   206  O  O   . GLN   A 1 33  ? 37.51800 69.37700 17.34000 1.000 83.03017  ? 30  GLN   A O   1 
ATOM   207  C  CB  . GLN   A 1 33  ? 34.28600 69.40100 17.03600 1.000 87.78786  ? 30  GLN   A CB  1 
ATOM   208  C  CG  . GLN   A 1 33  ? 32.94000 69.61100 16.36500 1.000 92.21605  ? 30  GLN   A CG  1 
ATOM   209  C  CD  . GLN   A 1 33  ? 31.78400 69.57700 17.35100 1.000 104.25838 ? 30  GLN   A CD  1 
ATOM   210  O  OE1 . GLN   A 1 33  ? 31.73500 70.36500 18.29900 1.000 97.50601  ? 30  GLN   A OE1 1 
ATOM   211  N  NE2 . GLN   A 1 33  ? 30.83800 68.67000 17.12400 1.000 104.41389 ? 30  GLN   A NE2 1 
ATOM   212  N  N   . PHE   A 1 34  ? 36.79300 67.56200 16.21700 1.000 89.22822  ? 31  PHE   A N   1 
ATOM   213  C  CA  . PHE   A 1 34  ? 37.85100 66.68700 16.70900 1.000 74.98792  ? 31  PHE   A CA  1 
ATOM   214  C  C   . PHE   A 1 34  ? 38.81100 66.20300 15.63300 1.000 72.49405  ? 31  PHE   A C   1 
ATOM   215  O  O   . PHE   A 1 34  ? 39.92600 65.79300 15.96800 1.000 78.30051  ? 31  PHE   A O   1 
ATOM   216  C  CB  . PHE   A 1 34  ? 37.25300 65.44700 17.39700 1.000 70.52325  ? 31  PHE   A CB  1 
ATOM   217  C  CG  . PHE   A 1 34  ? 36.54300 65.73900 18.68600 1.000 79.84335  ? 31  PHE   A CG  1 
ATOM   218  C  CD1 . PHE   A 1 34  ? 36.97500 66.75500 19.52200 1.000 73.77868  ? 31  PHE   A CD1 1 
ATOM   219  C  CD2 . PHE   A 1 34  ? 35.44900 64.98000 19.06900 1.000 80.81677  ? 31  PHE   A CD2 1 
ATOM   220  C  CE1 . PHE   A 1 34  ? 36.32400 67.01400 20.70900 1.000 77.43420  ? 31  PHE   A CE1 1 
ATOM   221  C  CE2 . PHE   A 1 34  ? 34.79400 65.23400 20.25800 1.000 77.76992  ? 31  PHE   A CE2 1 
ATOM   222  C  CZ  . PHE   A 1 34  ? 35.23100 66.25100 21.07700 1.000 84.92276  ? 31  PHE   A CZ  1 
ATOM   223  N  N   . GLY   A 1 35  ? 38.42600 66.24500 14.36500 1.000 73.43170  ? 32  GLY   A N   1 
ATOM   224  C  CA  . GLY   A 1 35  ? 39.14500 65.53900 13.33500 1.000 57.02667  ? 32  GLY   A CA  1 
ATOM   225  C  C   . GLY   A 1 35  ? 38.46100 64.20900 13.10700 1.000 62.98110  ? 32  GLY   A C   1 
ATOM   226  O  O   . GLY   A 1 35  ? 37.31500 64.00200 13.52500 1.000 63.47445  ? 32  GLY   A O   1 
ATOM   227  N  N   . PRO   A 1 36  ? 39.15200 63.27300 12.46500 1.000 60.53684  ? 33  PRO   A N   1 
ATOM   228  C  CA  . PRO   A 1 36  ? 38.58200 61.92600 12.29000 1.000 63.92751  ? 33  PRO   A CA  1 
ATOM   229  C  C   . PRO   A 1 36  ? 38.23000 61.29200 13.63300 1.000 68.76552  ? 33  PRO   A C   1 
ATOM   230  O  O   . PRO   A 1 36  ? 39.05400 61.23300 14.55100 1.000 68.13414  ? 33  PRO   A O   1 
ATOM   231  C  CB  . PRO   A 1 36  ? 39.69500 61.16300 11.56500 1.000 63.25516  ? 33  PRO   A CB  1 
ATOM   232  C  CG  . PRO   A 1 36  ? 40.51800 62.25200 10.89400 1.000 65.74581  ? 33  PRO   A CG  1 
ATOM   233  C  CD  . PRO   A 1 36  ? 40.48500 63.40500 11.85500 1.000 56.71224  ? 33  PRO   A CD  1 
ATOM   234  N  N   . THR   A 1 37  ? 36.97300 60.86400 13.75500 1.000 62.09555  ? 34  THR   A N   1 
ATOM   235  C  CA  . THR   A 1 37  ? 36.41000 60.36400 15.00100 1.000 66.44106  ? 34  THR   A CA  1 
ATOM   236  C  C   . THR   A 1 37  ? 35.70700 59.04700 14.72000 1.000 81.58478  ? 34  THR   A C   1 
ATOM   237  O  O   . THR   A 1 37  ? 35.11100 58.87300 13.65200 1.000 71.58605  ? 34  THR   A O   1 
ATOM   238  C  CB  . THR   A 1 37  ? 35.43000 61.36800 15.61000 1.000 63.62820  ? 34  THR   A CB  1 
ATOM   239  O  OG1 . THR   A 1 37  ? 36.05600 62.65400 15.66800 1.000 80.37927  ? 34  THR   A OG1 1 
ATOM   240  C  CG2 . THR   A 1 37  ? 35.02900 60.96300 17.00800 1.000 72.66392  ? 34  THR   A CG2 1 
ATOM   241  N  N   . TYR   A 1 38  ? 35.80800 58.10800 15.66400 1.000 64.84193  ? 35  TYR   A N   1 
ATOM   242  C  CA  . TYR   A 1 38  ? 35.24600 56.78000 15.48000 1.000 66.22524  ? 35  TYR   A CA  1 
ATOM   243  C  C   . TYR   A 1 38  ? 34.50500 56.35800 16.73200 1.000 60.40034  ? 35  TYR   A C   1 
ATOM   244  O  O   . TYR   A 1 38  ? 34.82400 56.79300 17.84200 1.000 72.33106  ? 35  TYR   A O   1 
ATOM   245  C  CB  . TYR   A 1 38  ? 36.31300 55.72800 15.14900 1.000 58.60103  ? 35  TYR   A CB  1 
ATOM   246  C  CG  . TYR   A 1 38  ? 37.19600 56.10700 13.99500 1.000 55.44788  ? 35  TYR   A CG  1 
ATOM   247  C  CD1 . TYR   A 1 38  ? 38.32700 56.89000 14.19800 1.000 55.01242  ? 35  TYR   A CD1 1 
ATOM   248  C  CD2 . TYR   A 1 38  ? 36.90600 55.68600 12.69600 1.000 47.47477  ? 35  TYR   A CD2 1 
ATOM   249  C  CE1 . TYR   A 1 38  ? 39.14700 57.24700 13.15100 1.000 51.13023  ? 35  TYR   A CE1 1 
ATOM   250  C  CE2 . TYR   A 1 38  ? 37.72200 56.03700 11.63400 1.000 45.30130  ? 35  TYR   A CE2 1 
ATOM   251  C  CZ  . TYR   A 1 38  ? 38.84300 56.82000 11.86800 1.000 54.63176  ? 35  TYR   A CZ  1 
ATOM   252  O  OH  . TYR   A 1 38  ? 39.67800 57.18400 10.83300 1.000 64.34795  ? 35  TYR   A OH  1 
ATOM   253  N  N   . LEU   A 1 39  ? 33.49900 55.51200 16.52700 1.000 74.05040  ? 36  LEU   A N   1 
ATOM   254  C  CA  . LEU   A 1 39  ? 32.72900 54.90000 17.60400 1.000 88.03791  ? 36  LEU   A CA  1 
ATOM   255  C  C   . LEU   A 1 39  ? 32.65600 53.40300 17.32500 1.000 81.09352  ? 36  LEU   A C   1 
ATOM   256  O  O   . LEU   A 1 39  ? 32.01100 52.97500 16.36000 1.000 70.87304  ? 36  LEU   A O   1 
ATOM   257  C  CB  . LEU   A 1 39  ? 31.33400 55.51200 17.70700 1.000 78.04185  ? 36  LEU   A CB  1 
ATOM   258  C  CG  . LEU   A 1 39  ? 30.56200 55.13500 18.96300 1.000 80.12378  ? 36  LEU   A CG  1 
ATOM   259  C  CD1 . LEU   A 1 39  ? 31.36300 55.54300 20.17800 1.000 74.87984  ? 36  LEU   A CD1 1 
ATOM   260  C  CD2 . LEU   A 1 39  ? 29.19500 55.80900 18.95300 1.000 86.81390  ? 36  LEU   A CD2 1 
ATOM   261  N  N   . ASP   A 1 40  ? 33.33900 52.62000 18.15400 1.000 66.31558  ? 37  ASP   A N   1 
ATOM   262  C  CA  . ASP   A 1 40  ? 33.32200 51.16900 18.05300 1.000 80.08756  ? 37  ASP   A CA  1 
ATOM   263  C  C   . ASP   A 1 40  ? 33.70000 50.71200 16.64500 1.000 89.18577  ? 37  ASP   A C   1 
ATOM   264  O  O   . ASP   A 1 40  ? 33.12200 49.77300 16.09000 1.000 86.38814  ? 37  ASP   A O   1 
ATOM   265  C  CB  . ASP   A 1 40  ? 31.96100 50.62300 18.48000 1.000 78.35081  ? 37  ASP   A CB  1 
ATOM   266  C  CG  . ASP   A 1 40  ? 31.62200 51.00000 19.91500 1.000 100.87569 ? 37  ASP   A CG  1 
ATOM   267  O  OD1 . ASP   A 1 40  ? 32.37400 50.59200 20.83000 1.000 101.73806 ? 37  ASP   A OD1 1 
ATOM   268  O  OD2 . ASP   A 1 40  ? 30.62600 51.73000 20.12600 1.000 95.36052  ? 37  ASP   A OD2 1 
ATOM   269  N  N   . GLY   A 1 41  ? 34.68600 51.38900 16.05900 1.000 79.15354  ? 38  GLY   A N   1 
ATOM   270  C  CA  . GLY   A 1 41  ? 35.12800 51.09400 14.71900 1.000 72.33555  ? 38  GLY   A CA  1 
ATOM   271  C  C   . GLY   A 1 41  ? 34.41600 51.86400 13.62600 1.000 71.36805  ? 38  GLY   A C   1 
ATOM   272  O  O   . GLY   A 1 41  ? 34.93700 51.94200 12.50700 1.000 72.90118  ? 38  GLY   A O   1 
ATOM   273  N  N   . ALA   A 1 42  ? 33.25600 52.44900 13.91600 1.000 69.30372  ? 39  ALA   A N   1 
ATOM   274  C  CA  . ALA   A 1 42  ? 32.44100 53.09800 12.89300 1.000 80.07994  ? 39  ALA   A CA  1 
ATOM   275  C  C   . ALA   A 1 42  ? 32.91200 54.53200 12.67600 1.000 74.91714  ? 39  ALA   A C   1 
ATOM   276  O  O   . ALA   A 1 42  ? 32.95200 55.32600 13.62200 1.000 79.16622  ? 39  ALA   A O   1 
ATOM   277  C  CB  . ALA   A 1 42  ? 30.96600 53.07600 13.29200 1.000 83.03045  ? 39  ALA   A CB  1 
ATOM   278  N  N   . ASP   A 1 43  ? 33.24700 54.86800 11.43200 1.000 75.49338  ? 40  ASP   A N   1 
ATOM   279  C  CA  . ASP   A 1 43  ? 33.68300 56.22500 11.10100 1.000 81.25725  ? 40  ASP   A CA  1 
ATOM   280  C  C   . ASP   A 1 43  ? 32.52500 57.20300 11.28100 1.000 73.30349  ? 40  ASP   A C   1 
ATOM   281  O  O   . ASP   A 1 43  ? 31.57900 57.20900 10.48700 1.000 81.35584  ? 40  ASP   A O   1 
ATOM   282  C  CB  . ASP   A 1 43  ? 34.22500 56.27400 9.67500  1.000 69.48713  ? 40  ASP   A CB  1 
ATOM   283  C  CG  . ASP   A 1 43  ? 35.07800 57.50500 9.41500  1.000 71.71956  ? 40  ASP   A CG  1 
ATOM   284  O  OD1 . ASP   A 1 43  ? 34.81800 58.55600 10.03800 1.000 66.68321  ? 40  ASP   A OD1 1 
ATOM   285  O  OD2 . ASP   A 1 43  ? 36.01100 57.42200 8.58700  1.000 74.11068  ? 40  ASP   A OD2 1 
ATOM   286  N  N   . VAL   A 1 44  ? 32.59800 58.02700 12.32400 1.000 73.97330  ? 41  VAL   A N   1 
ATOM   287  C  CA  . VAL   A 1 44  ? 31.58100 59.02800 12.62300 1.000 76.40346  ? 41  VAL   A CA  1 
ATOM   288  C  C   . VAL   A 1 44  ? 32.11400 60.44300 12.39500 1.000 85.97246  ? 41  VAL   A C   1 
ATOM   289  O  O   . VAL   A 1 44  ? 31.61800 61.40200 12.99600 1.000 89.82130  ? 41  VAL   A O   1 
ATOM   290  C  CB  . VAL   A 1 44  ? 31.03800 58.86700 14.05300 1.000 75.17131  ? 41  VAL   A CB  1 
ATOM   291  C  CG1 . VAL   A 1 44  ? 30.48800 57.46700 14.25000 1.000 77.91977  ? 41  VAL   A CG1 1 
ATOM   292  C  CG2 . VAL   A 1 44  ? 32.12400 59.17100 15.07300 1.000 75.04082  ? 41  VAL   A CG2 1 
ATOM   293  N  N   . THR   A 1 45  ? 33.13100 60.58300 11.54200 1.000 72.83464  ? 42  THR   A N   1 
ATOM   294  C  CA  . THR   A 1 45  ? 33.69000 61.89800 11.24400 1.000 82.50409  ? 42  THR   A CA  1 
ATOM   295  C  C   . THR   A 1 45  ? 32.63100 62.83100 10.66700 1.000 92.73504  ? 42  THR   A C   1 
ATOM   296  O  O   . THR   A 1 45  ? 32.39400 63.92700 11.18900 1.000 89.96403  ? 42  THR   A O   1 
ATOM   297  C  CB  . THR   A 1 45  ? 34.85800 61.75700 10.26800 1.000 85.64065  ? 42  THR   A CB  1 
ATOM   298  O  OG1 . THR   A 1 45  ? 35.91900 61.03000 10.89200 1.000 80.59042  ? 42  THR   A OG1 1 
ATOM   299  C  CG2 . THR   A 1 45  ? 35.36300 63.11800 9.82900  1.000 77.24986  ? 42  THR   A CG2 1 
ATOM   300  N  N   . LYS   A 1 46  ? 31.97500 62.40100 9.58700  1.000 100.47640 ? 43  LYS   A N   1 
ATOM   301  C  CA  . LYS   A 1 46  ? 31.01000 63.23000 8.87400  1.000 90.71163  ? 43  LYS   A CA  1 
ATOM   302  C  C   . LYS   A 1 46  ? 29.61700 63.08500 9.46700  1.000 93.61056  ? 43  LYS   A C   1 
ATOM   303  O  O   . LYS   A 1 46  ? 28.61800 63.24900 8.76000  1.000 106.11659 ? 43  LYS   A O   1 
ATOM   304  C  CB  . LYS   A 1 46  ? 31.00000 62.86500 7.38600  1.000 82.13995  ? 43  LYS   A CB  1 
ATOM   305  C  CG  . LYS   A 1 46  ? 32.38800 62.64700 6.80200  1.000 89.76931  ? 43  LYS   A CG  1 
ATOM   306  C  CD  . LYS   A 1 46  ? 32.48700 63.12700 5.36000  1.000 98.98458  ? 43  LYS   A CD  1 
ATOM   307  C  CE  . LYS   A 1 46  ? 33.94700 63.32800 4.94600  1.000 106.44238 ? 43  LYS   A CE  1 
ATOM   308  N  NZ  . LYS   A 1 46  ? 34.08300 63.96800 3.59900  1.000 102.95554 ? 43  LYS   A NZ  1 
ATOM   309  N  N   . ILE   A 1 47  ? 29.53700 62.78600 10.76000 1.000 97.55882  ? 44  ILE   A N   1 
ATOM   310  C  CA  . ILE   A 1 47  ? 28.27300 62.58600 11.46000 1.000 100.92288 ? 44  ILE   A CA  1 
ATOM   311  C  C   . ILE   A 1 47  ? 28.16700 63.62600 12.57000 1.000 98.83950  ? 44  ILE   A C   1 
ATOM   312  O  O   . ILE   A 1 47  ? 29.15700 63.93300 13.24200 1.000 101.63350 ? 44  ILE   A O   1 
ATOM   313  C  CB  . ILE   A 1 47  ? 28.16600 61.14900 12.02100 1.000 99.44003  ? 44  ILE   A CB  1 
ATOM   314  C  CG1 . ILE   A 1 47  ? 27.37500 60.22900 11.07900 1.000 99.83532  ? 44  ILE   A CG1 1 
ATOM   315  C  CG2 . ILE   A 1 47  ? 27.53800 61.13600 13.40900 1.000 91.29526  ? 44  ILE   A CG2 1 
ATOM   316  C  CD1 . ILE   A 1 47  ? 27.82700 60.24400 9.63200  1.000 97.04108  ? 44  ILE   A CD1 1 
ATOM   317  N  N   . LYS   A 1 48  ? 26.97000 64.17800 12.75000 1.000 101.38469 ? 45  LYS   A N   1 
ATOM   318  C  CA  . LYS   A 1 48  ? 26.72800 65.14200 13.81200 1.000 107.93057 ? 45  LYS   A CA  1 
ATOM   319  C  C   . LYS   A 1 48  ? 26.47600 64.41900 15.13200 1.000 102.78208 ? 45  LYS   A C   1 
ATOM   320  O  O   . LYS   A 1 48  ? 26.08800 63.24900 15.14000 1.000 101.73923 ? 45  LYS   A O   1 
ATOM   321  C  CB  . LYS   A 1 48  ? 25.53300 66.02600 13.45800 1.000 108.91535 ? 45  LYS   A CB  1 
ATOM   322  C  CG  . LYS   A 1 48  ? 25.53300 66.54200 12.02700 1.000 111.43628 ? 45  LYS   A CG  1 
ATOM   323  C  CD  . LYS   A 1 48  ? 25.60100 68.06400 11.96700 1.000 116.64601 ? 45  LYS   A CD  1 
ATOM   324  C  CE  . LYS   A 1 48  ? 25.59800 68.55400 10.52200 1.000 108.64013 ? 45  LYS   A CE  1 
ATOM   325  N  NZ  . LYS   A 1 48  ? 25.16800 69.97300 10.38100 1.000 105.67349 ? 45  LYS   A NZ  1 
ATOM   326  N  N   . PRO   A 1 49  ? 26.69400 65.08900 16.26700 1.000 99.09682  ? 46  PRO   A N   1 
ATOM   327  C  CA  . PRO   A 1 49  ? 26.43800 64.43700 17.55800 1.000 96.60105  ? 46  PRO   A CA  1 
ATOM   328  C  C   . PRO   A 1 49  ? 24.96500 64.10100 17.72800 1.000 103.38053 ? 46  PRO   A C   1 
ATOM   329  O  O   . PRO   A 1 49  ? 24.08400 64.84600 17.29200 1.000 110.98929 ? 46  PRO   A O   1 
ATOM   330  C  CB  . PRO   A 1 49  ? 26.90000 65.47800 18.58500 1.000 96.07403  ? 46  PRO   A CB  1 
ATOM   331  C  CG  . PRO   A 1 49  ? 27.82800 66.37000 17.83800 1.000 104.04044 ? 46  PRO   A CG  1 
ATOM   332  C  CD  . PRO   A 1 49  ? 27.29500 66.42100 16.43800 1.000 106.75846 ? 46  PRO   A CD  1 
ATOM   333  N  N   . HIS   A 1 50  ? 24.70400 62.95600 18.34900 1.000 107.72292 ? 47  HIS   A N   1 
ATOM   334  C  CA  . HIS   A 1 50  ? 23.35900 62.53100 18.70800 1.000 109.33595 ? 47  HIS   A CA  1 
ATOM   335  C  C   . HIS   A 1 50  ? 23.19900 62.59600 20.22400 1.000 108.10595 ? 47  HIS   A C   1 
ATOM   336  O  O   . HIS   A 1 50  ? 24.13900 62.90200 20.96300 1.000 108.75470 ? 47  HIS   A O   1 
ATOM   337  C  CB  . HIS   A 1 50  ? 23.05800 61.11900 18.18800 1.000 102.41728 ? 47  HIS   A CB  1 
ATOM   338  C  CG  . HIS   A 1 50  ? 23.21500 60.95800 16.70400 1.000 114.75646 ? 47  HIS   A CG  1 
ATOM   339  N  ND1 . HIS   A 1 50  ? 23.70600 61.95400 15.88500 1.000 120.64895 ? 47  HIS   A ND1 1 
ATOM   340  C  CD2 . HIS   A 1 50  ? 22.94100 59.90800 15.89200 1.000 117.01890 ? 47  HIS   A CD2 1 
ATOM   341  C  CE1 . HIS   A 1 50  ? 23.72800 61.52500 14.63500 1.000 116.85991 ? 47  HIS   A CE1 1 
ATOM   342  N  NE2 . HIS   A 1 50  ? 23.26900 60.28600 14.61200 1.000 118.06778 ? 47  HIS   A NE2 1 
ATOM   343  N  N   . ASN   A 1 51  ? 21.98300 62.30700 20.68500 1.000 115.14320 ? 48  ASN   A N   1 
ATOM   344  C  CA  . ASN   A 1 51  ? 21.71600 62.29700 22.11800 1.000 116.69726 ? 48  ASN   A CA  1 
ATOM   345  C  C   . ASN   A 1 51  ? 22.17000 60.99700 22.77000 1.000 115.63103 ? 48  ASN   A C   1 
ATOM   346  O  O   . ASN   A 1 51  ? 22.62200 61.01300 23.92300 1.000 110.22547 ? 48  ASN   A O   1 
ATOM   347  C  CB  . ASN   A 1 51  ? 20.22700 62.53700 22.37300 1.000 118.48575 ? 48  ASN   A CB  1 
ATOM   348  C  CG  . ASN   A 1 51  ? 19.68100 63.71400 21.58000 1.000 118.72105 ? 48  ASN   A CG  1 
ATOM   349  O  OD1 . ASN   A 1 51  ? 19.86000 64.87300 21.96300 1.000 108.86169 ? 48  ASN   A OD1 1 
ATOM   350  N  ND2 . ASN   A 1 51  ? 19.01500 63.42200 20.46600 1.000 114.88072 ? 48  ASN   A ND2 1 
ATOM   351  N  N   . SER   A 1 52  ? 22.06300 59.87200 22.05400 1.000 119.33815 ? 49  SER   A N   1 
ATOM   352  C  CA  . SER   A 1 52  ? 22.63700 58.60800 22.50700 1.000 118.64263 ? 49  SER   A CA  1 
ATOM   353  C  C   . SER   A 1 52  ? 24.15900 58.64000 22.53600 1.000 118.30523 ? 49  SER   A C   1 
ATOM   354  O  O   . SER   A 1 52  ? 24.77300 57.71200 23.07600 1.000 109.74923 ? 49  SER   A O   1 
ATOM   355  C  CB  . SER   A 1 52  ? 22.16700 57.45800 21.61000 1.000 111.91208 ? 49  SER   A CB  1 
ATOM   356  O  OG  . SER   A 1 52  ? 22.74700 57.53800 20.31700 1.000 107.14194 ? 49  SER   A OG  1 
ATOM   357  N  N   . HIS   A 1 53  ? 24.77400 59.67600 21.96700 1.000 117.83170 ? 50  HIS   A N   1 
ATOM   358  C  CA  . HIS   A 1 53  ? 26.21600 59.85200 21.98200 1.000 105.03315 ? 50  HIS   A CA  1 
ATOM   359  C  C   . HIS   A 1 53  ? 26.72000 60.55800 23.23200 1.000 115.06908 ? 50  HIS   A C   1 
ATOM   360  O  O   . HIS   A 1 53  ? 27.93600 60.67400 23.40900 1.000 116.22713 ? 50  HIS   A O   1 
ATOM   361  C  CB  . HIS   A 1 53  ? 26.65700 60.62900 20.74100 1.000 90.38650  ? 50  HIS   A CB  1 
ATOM   362  C  CG  . HIS   A 1 53  ? 26.62200 59.81600 19.48700 1.000 106.90652 ? 50  HIS   A CG  1 
ATOM   363  N  ND1 . HIS   A 1 53  ? 27.04900 60.30100 18.26900 1.000 105.01549 ? 50  HIS   A ND1 1 
ATOM   364  C  CD2 . HIS   A 1 53  ? 26.20700 58.54600 19.26200 1.000 111.44955 ? 50  HIS   A CD2 1 
ATOM   365  C  CE1 . HIS   A 1 53  ? 26.90300 59.36300 17.34900 1.000 109.47599 ? 50  HIS   A CE1 1 
ATOM   366  N  NE2 . HIS   A 1 53  ? 26.39200 58.28900 17.92500 1.000 109.43800 ? 50  HIS   A NE2 1 
ATOM   367  N  N   . GLU   A 1 54  ? 25.82600 61.03200 24.09600 1.000 113.68590 ? 51  GLU   A N   1 
ATOM   368  C  CA  . GLU   A 1 54  ? 26.25900 61.65300 25.33800 1.000 112.40493 ? 51  GLU   A CA  1 
ATOM   369  C  C   . GLU   A 1 54  ? 26.99600 60.63900 26.20400 1.000 112.16541 ? 51  GLU   A C   1 
ATOM   370  O  O   . GLU   A 1 54  ? 26.51900 59.51900 26.41300 1.000 108.35095 ? 51  GLU   A O   1 
ATOM   371  C  CB  . GLU   A 1 54  ? 25.05200 62.22400 26.08500 1.000 123.40327 ? 51  GLU   A CB  1 
ATOM   372  C  CG  . GLU   A 1 54  ? 25.29400 62.49700 27.56600 1.000 130.94958 ? 51  GLU   A CG  1 
ATOM   373  C  CD  . GLU   A 1 54  ? 26.39800 63.51100 27.81200 1.000 122.22341 ? 51  GLU   A CD  1 
ATOM   374  O  OE1 . GLU   A 1 54  ? 26.32700 64.61900 27.23700 1.000 124.83101 ? 51  GLU   A OE1 1 
ATOM   375  O  OE2 . GLU   A 1 54  ? 27.33100 63.20300 28.58700 1.000 113.21651 ? 51  GLU   A OE2 1 
ATOM   376  N  N   . GLY   A 1 55  ? 28.17900 61.02800 26.68300 1.000 110.61948 ? 52  GLY   A N   1 
ATOM   377  C  CA  . GLY   A 1 55  ? 28.95700 60.23700 27.61300 1.000 109.95996 ? 52  GLY   A CA  1 
ATOM   378  C  C   . GLY   A 1 55  ? 29.86800 59.20100 26.98100 1.000 102.96578 ? 52  GLY   A C   1 
ATOM   379  O  O   . GLY   A 1 55  ? 30.89100 58.84600 27.57700 1.000 97.11126  ? 52  GLY   A O   1 
ATOM   380  N  N   . LYS   A 1 56  ? 29.52300 58.71100 25.79000 1.000 111.86346 ? 53  LYS   A N   1 
ATOM   381  C  CA  . LYS   A 1 56  ? 30.31800 57.68500 25.12600 1.000 104.71658 ? 53  LYS   A CA  1 
ATOM   382  C  C   . LYS   A 1 56  ? 31.73200 58.17800 24.83200 1.000 99.29391  ? 53  LYS   A C   1 
ATOM   383  O  O   . LYS   A 1 56  ? 31.98300 59.37800 24.67800 1.000 100.34025 ? 53  LYS   A O   1 
ATOM   384  C  CB  . LYS   A 1 56  ? 29.64500 57.24900 23.82400 1.000 95.21782  ? 53  LYS   A CB  1 
ATOM   385  C  CG  . LYS   A 1 56  ? 28.29600 56.57100 24.01800 1.000 105.43551 ? 53  LYS   A CG  1 
ATOM   386  C  CD  . LYS   A 1 56  ? 27.96500 55.67000 22.83600 1.000 106.57472 ? 53  LYS   A CD  1 
ATOM   387  C  CE  . LYS   A 1 56  ? 26.57400 55.06900 22.95500 1.000 102.78635 ? 53  LYS   A CE  1 
ATOM   388  N  NZ  . LYS   A 1 56  ? 26.21100 54.30100 21.73000 1.000 97.24507  ? 53  LYS   A NZ  1 
ATOM   389  N  N   . THR   A 1 57  ? 32.65900 57.22800 24.74900 1.000 84.34621  ? 54  THR   A N   1 
ATOM   390  C  CA  . THR   A 1 57  ? 34.05800 57.50900 24.46200 1.000 73.91910  ? 54  THR   A CA  1 
ATOM   391  C  C   . THR   A 1 57  ? 34.33000 57.28600 22.98000 1.000 77.85807  ? 54  THR   A C   1 
ATOM   392  O  O   . THR   A 1 57  ? 33.95300 56.24900 22.41700 1.000 68.60053  ? 54  THR   A O   1 
ATOM   393  C  CB  . THR   A 1 57  ? 34.97600 56.62800 25.31500 1.000 79.32676  ? 54  THR   A CB  1 
ATOM   394  O  OG1 . THR   A 1 57  ? 34.83900 56.98400 26.70100 1.000 80.29854  ? 54  THR   A OG1 1 
ATOM   395  C  CG2 . THR   A 1 57  ? 36.41800 56.80100 24.89700 1.000 76.20356  ? 54  THR   A CG2 1 
ATOM   396  N  N   . PHE   A 1 58  ? 34.97500 58.25900 22.34400 1.000 75.79020  ? 55  PHE   A N   1 
ATOM   397  C  CA  . PHE   A 1 58  ? 35.29900 58.16700 20.92800 1.000 72.11681  ? 55  PHE   A CA  1 
ATOM   398  C  C   . PHE   A 1 58  ? 36.80600 58.09800 20.74900 1.000 55.51962  ? 55  PHE   A C   1 
ATOM   399  O  O   . PHE   A 1 58  ? 37.55800 58.72600 21.49800 1.000 63.92947  ? 55  PHE   A O   1 
ATOM   400  C  CB  . PHE   A 1 58  ? 34.74000 59.35900 20.14700 1.000 73.08357  ? 55  PHE   A CB  1 
ATOM   401  C  CG  . PHE   A 1 58  ? 33.24200 59.44500 20.16400 1.000 82.13735  ? 55  PHE   A CG  1 
ATOM   402  C  CD1 . PHE   A 1 58  ? 32.58400 60.09800 21.19700 1.000 76.12191  ? 55  PHE   A CD1 1 
ATOM   403  C  CD2 . PHE   A 1 58  ? 32.49000 58.87800 19.14500 1.000 86.14485  ? 55  PHE   A CD2 1 
ATOM   404  C  CE1 . PHE   A 1 58  ? 31.20900 60.17300 21.21900 1.000 79.84114  ? 55  PHE   A CE1 1 
ATOM   405  C  CE2 . PHE   A 1 58  ? 31.10700 58.95200 19.16400 1.000 88.02013  ? 55  PHE   A CE2 1 
ATOM   406  C  CZ  . PHE   A 1 58  ? 30.46800 59.60000 20.20400 1.000 89.92352  ? 55  PHE   A CZ  1 
ATOM   407  N  N   . TYR   A 1 59  ? 37.23300 57.31200 19.76600 1.000 53.91863  ? 56  TYR   A N   1 
ATOM   408  C  CA  . TYR   A 1 59  ? 38.62000 57.30200 19.32800 1.000 60.16094  ? 56  TYR   A CA  1 
ATOM   409  C  C   . TYR   A 1 59  ? 38.85400 58.45900 18.36300 1.000 62.94373  ? 56  TYR   A C   1 
ATOM   410  O  O   . TYR   A 1 59  ? 38.06100 58.67800 17.44100 1.000 58.24922  ? 56  TYR   A O   1 
ATOM   411  C  CB  . TYR   A 1 59  ? 38.95400 55.98000 18.63300 1.000 58.01135  ? 56  TYR   A CB  1 
ATOM   412  C  CG  . TYR   A 1 59  ? 39.27700 54.82100 19.55000 1.000 57.22928  ? 56  TYR   A CG  1 
ATOM   413  C  CD1 . TYR   A 1 59  ? 38.26700 54.05800 20.12100 1.000 72.55501  ? 56  TYR   A CD1 1 
ATOM   414  C  CD2 . TYR   A 1 59  ? 40.59500 54.46400 19.81400 1.000 61.07261  ? 56  TYR   A CD2 1 
ATOM   415  C  CE1 . TYR   A 1 59  ? 38.56400 52.98500 20.95500 1.000 80.70479  ? 56  TYR   A CE1 1 
ATOM   416  C  CE2 . TYR   A 1 59  ? 40.89800 53.39900 20.64500 1.000 64.93043  ? 56  TYR   A CE2 1 
ATOM   417  C  CZ  . TYR   A 1 59  ? 39.88300 52.66400 21.21000 1.000 68.46392  ? 56  TYR   A CZ  1 
ATOM   418  O  OH  . TYR   A 1 59  ? 40.19500 51.60500 22.02800 1.000 75.30444  ? 56  TYR   A OH  1 
ATOM   419  N  N   . VAL   A 1 60  ? 39.94800 59.19100 18.55900 1.000 53.72353  ? 57  VAL   A N   1 
ATOM   420  C  CA  . VAL   A 1 60  ? 40.30200 60.28700 17.66700 1.000 56.27643  ? 57  VAL   A CA  1 
ATOM   421  C  C   . VAL   A 1 60  ? 41.72000 60.10000 17.15300 1.000 53.15719  ? 57  VAL   A C   1 
ATOM   422  O  O   . VAL   A 1 60  ? 42.59500 59.57600 17.84900 1.000 56.89170  ? 57  VAL   A O   1 
ATOM   423  C  CB  . VAL   A 1 60  ? 40.15900 61.66000 18.35900 1.000 61.27560  ? 57  VAL   A CB  1 
ATOM   424  C  CG1 . VAL   A 1 60  ? 38.68500 61.98000 18.59900 1.000 53.29577  ? 57  VAL   A CG1 1 
ATOM   425  C  CG2 . VAL   A 1 60  ? 40.94500 61.68500 19.66200 1.000 53.38247  ? 57  VAL   A CG2 1 
ATOM   426  N  N   . LEU   A 1 61  ? 41.94100 60.59000 15.93900 1.000 54.41400  ? 58  LEU   A N   1 
ATOM   427  C  CA  . LEU   A 1 61  ? 43.30900 60.56400 15.38000 1.000 62.69889  ? 58  LEU   A CA  1 
ATOM   428  C  C   . LEU   A 1 61  ? 44.09800 61.62200 16.13800 1.000 64.66669  ? 58  LEU   A C   1 
ATOM   429  O  O   . LEU   A 1 61  ? 43.56900 62.72100 16.34100 1.000 71.73697  ? 58  LEU   A O   1 
ATOM   430  C  CB  . LEU   A 1 61  ? 43.24800 60.89300 13.89100 1.000 57.43796  ? 58  LEU   A CB  1 
ATOM   431  C  CG  . LEU   A 1 61  ? 44.57500 61.28500 13.24700 1.000 74.08947  ? 58  LEU   A CG  1 
ATOM   432  C  CD1 . LEU   A 1 61  ? 45.36800 60.05000 12.85400 1.000 68.29412  ? 58  LEU   A CD1 1 
ATOM   433  C  CD2 . LEU   A 1 61  ? 44.34600 62.17600 12.03900 1.000 65.31463  ? 58  LEU   A CD2 1 
ATOM   434  N  N   . PRO   A 1 62  ? 45.32100 61.32900 16.60200 1.000 61.83822  ? 59  PRO   A N   1 
ATOM   435  C  CA  . PRO   A 1 62  ? 46.07100 62.29400 17.42000 1.000 68.02492  ? 59  PRO   A CA  1 
ATOM   436  C  C   . PRO   A 1 62  ? 46.22200 63.62600 16.69900 1.000 55.95723  ? 59  PRO   A C   1 
ATOM   437  O  O   . PRO   A 1 62  ? 46.67000 63.68200 15.55400 1.000 63.55317  ? 59  PRO   A O   1 
ATOM   438  C  CB  . PRO   A 1 62  ? 47.42200 61.60100 17.63300 1.000 60.74486  ? 59  PRO   A CB  1 
ATOM   439  C  CG  . PRO   A 1 62  ? 47.10200 60.13500 17.52100 1.000 55.99899  ? 59  PRO   A CG  1 
ATOM   440  C  CD  . PRO   A 1 62  ? 46.04200 60.05500 16.44700 1.000 48.87776  ? 59  PRO   A CD  1 
ATOM   441  N  N   . ASN   A 1 63  ? 45.81800 64.70600 17.37500 1.000 62.17245  ? 60  ASN   A N   1 
ATOM   442  C  CA  . ASN   A 1 63  ? 45.93600 66.05500 16.83700 1.000 71.49761  ? 60  ASN   A CA  1 
ATOM   443  C  C   . ASN   A 1 63  ? 46.68300 67.01900 17.75300 1.000 66.59396  ? 60  ASN   A C   1 
ATOM   444  O  O   . ASN   A 1 63  ? 46.71000 68.21900 17.46700 1.000 64.40198  ? 60  ASN   A O   1 
ATOM   445  C  CB  . ASN   A 1 63  ? 44.54700 66.62600 16.52200 1.000 67.24822  ? 60  ASN   A CB  1 
ATOM   446  C  CG  . ASN   A 1 63  ? 43.60600 66.52800 17.69700 1.000 72.72220  ? 60  ASN   A CG  1 
ATOM   447  O  OD1 . ASN   A 1 63  ? 44.03600 66.46800 18.84400 1.000 74.70338  ? 60  ASN   A OD1 1 
ATOM   448  N  ND2 . ASN   A 1 63  ? 42.30900 66.49600 17.41600 1.000 88.17178  ? 60  ASN   A ND2 1 
ATOM   449  N  N   . ASP   A 1 64  ? 47.25000 66.54500 18.86000 1.000 58.84046  ? 61  ASP   A N   1 
ATOM   450  C  CA  . ASP   A 1 64  ? 48.19800 67.32200 19.64500 1.000 61.66529  ? 61  ASP   A CA  1 
ATOM   451  C  C   . ASP   A 1 64  ? 49.26900 66.37300 20.15600 1.000 54.65588  ? 61  ASP   A C   1 
ATOM   452  O  O   . ASP   A 1 64  ? 49.16600 65.15200 20.00900 1.000 60.10480  ? 61  ASP   A O   1 
ATOM   453  C  CB  . ASP   A 1 64  ? 47.52700 68.07200 20.80400 1.000 55.25152  ? 61  ASP   A CB  1 
ATOM   454  C  CG  . ASP   A 1 64  ? 46.81500 67.14300 21.77700 1.000 64.13198  ? 61  ASP   A CG  1 
ATOM   455  O  OD1 . ASP   A 1 64  ? 47.44400 66.19700 22.30200 1.000 61.15423  ? 61  ASP   A OD1 1 
ATOM   456  O  OD2 . ASP   A 1 64  ? 45.61800 67.37800 22.03500 1.000 74.84345  ? 61  ASP   A OD2 1 
ATOM   457  N  N   . ASP   A 1 65  ? 50.30100 66.94300 20.77100 1.000 53.77052  ? 62  ASP   A N   1 
ATOM   458  C  CA  . ASP   A 1 65  ? 51.45700 66.14100 21.14100 1.000 55.77216  ? 62  ASP   A CA  1 
ATOM   459  C  C   . ASP   A 1 65  ? 51.13600 65.15600 22.25100 1.000 51.26855  ? 62  ASP   A C   1 
ATOM   460  O  O   . ASP   A 1 65  ? 51.74100 64.08200 22.31000 1.000 47.78520  ? 62  ASP   A O   1 
ATOM   461  C  CB  . ASP   A 1 65  ? 52.60600 67.04500 21.56800 1.000 49.37167  ? 62  ASP   A CB  1 
ATOM   462  C  CG  . ASP   A 1 65  ? 53.93800 66.35500 21.47600 1.000 40.14890  ? 62  ASP   A CG  1 
ATOM   463  O  OD1 . ASP   A 1 65  ? 54.38100 66.05900 20.34100 1.000 44.14383  ? 62  ASP   A OD1 1 
ATOM   464  O  OD2 . ASP   A 1 65  ? 54.55200 66.11500 22.54100 1.000 45.68365  ? 62  ASP   A OD2 1 
ATOM   465  N  N   . THR   A 1 66  ? 50.21700 65.51100 23.14700 1.000 51.89139  ? 63  THR   A N   1 
ATOM   466  C  CA  . THR   A 1 66  ? 49.83600 64.59500 24.21600 1.000 51.16593  ? 63  THR   A CA  1 
ATOM   467  C  C   . THR   A 1 66  ? 49.24300 63.31100 23.64700 1.000 53.88791  ? 63  THR   A C   1 
ATOM   468  O  O   . THR   A 1 66  ? 49.59800 62.20400 24.07600 1.000 49.66041  ? 63  THR   A O   1 
ATOM   469  C  CB  . THR   A 1 66  ? 48.84300 65.28500 25.15700 1.000 58.07749  ? 63  THR   A CB  1 
ATOM   470  O  OG1 . THR   A 1 66  ? 49.51900 66.30200 25.90900 1.000 57.15883  ? 63  THR   A OG1 1 
ATOM   471  C  CG2 . THR   A 1 66  ? 48.24000 64.28900 26.13600 1.000 52.07796  ? 63  THR   A CG2 1 
ATOM   472  N  N   . LEU   A 1 67  ? 48.35300 63.44100 22.66400 1.000 54.56900  ? 64  LEU   A N   1 
ATOM   473  C  CA  . LEU   A 1 67  ? 47.74100 62.27100 22.04900 1.000 54.39624  ? 64  LEU   A CA  1 
ATOM   474  C  C   . LEU   A 1 67  ? 48.74500 61.49800 21.20200 1.000 54.65678  ? 64  LEU   A C   1 
ATOM   475  O  O   . LEU   A 1 67  ? 48.67400 60.26700 21.12300 1.000 51.11716  ? 64  LEU   A O   1 
ATOM   476  C  CB  . LEU   A 1 67  ? 46.54600 62.69300 21.20000 1.000 51.34804  ? 64  LEU   A CB  1 
ATOM   477  C  CG  . LEU   A 1 67  ? 45.41900 63.40500 21.94400 1.000 59.74170  ? 64  LEU   A CG  1 
ATOM   478  C  CD1 . LEU   A 1 67  ? 44.37000 63.91400 20.96200 1.000 61.70164  ? 64  LEU   A CD1 1 
ATOM   479  C  CD2 . LEU   A 1 67  ? 44.79700 62.48300 22.97100 1.000 58.06965  ? 64  LEU   A CD2 1 
ATOM   480  N  N   . ARG   A 1 68  ? 49.67000 62.19800 20.54000 1.000 49.10889  ? 65  ARG   A N   1 
ATOM   481  C  CA  . ARG   A 1 68  ? 50.67400 61.49800 19.74300 1.000 50.41997  ? 65  ARG   A CA  1 
ATOM   482  C  C   . ARG   A 1 68  ? 51.53900 60.61000 20.63000 1.000 44.17376  ? 65  ARG   A C   1 
ATOM   483  O  O   . ARG   A 1 68  ? 51.80000 59.45000 20.29200 1.000 48.35591  ? 65  ARG   A O   1 
ATOM   484  C  CB  . ARG   A 1 68  ? 51.54300 62.49600 18.97500 1.000 38.65983  ? 65  ARG   A CB  1 
ATOM   485  C  CG  . ARG   A 1 68  ? 50.88200 63.11600 17.72700 1.000 49.39713  ? 65  ARG   A CG  1 
ATOM   486  C  CD  . ARG   A 1 68  ? 51.88600 63.89500 16.85700 1.000 51.03759  ? 65  ARG   A CD  1 
ATOM   487  N  NE  . ARG   A 1 68  ? 52.47800 65.03900 17.55400 1.000 48.29970  ? 65  ARG   A NE  1 
ATOM   488  C  CZ  . ARG   A 1 68  ? 51.99700 66.27600 17.50000 1.000 55.82893  ? 65  ARG   A CZ  1 
ATOM   489  N  NH1 . ARG   A 1 68  ? 50.92800 66.57300 16.77900 1.000 47.73900  ? 65  ARG   A NH1 1 
ATOM   490  N  NH2 . ARG   A 1 68  ? 52.59300 67.23400 18.19900 1.000 52.79620  ? 65  ARG   A NH2 1 
ATOM   491  N  N   . VAL   A 1 69  ? 51.97300 61.13400 21.77500 1.000 42.15237  ? 66  VAL   A N   1 
ATOM   492  C  CA  . VAL   A 1 69  ? 52.78600 60.35200 22.69900 1.000 45.33116  ? 66  VAL   A CA  1 
ATOM   493  C  C   . VAL   A 1 69  ? 51.97200 59.19500 23.26600 1.000 50.40135  ? 66  VAL   A C   1 
ATOM   494  O  O   . VAL   A 1 69  ? 52.44700 58.05900 23.34700 1.000 41.98646  ? 66  VAL   A O   1 
ATOM   495  C  CB  . VAL   A 1 69  ? 53.34200 61.25700 23.81200 1.000 50.37838  ? 66  VAL   A CB  1 
ATOM   496  C  CG1 . VAL   A 1 69  ? 54.03100 60.40100 24.90600 1.000 33.64064  ? 66  VAL   A CG1 1 
ATOM   497  C  CG2 . VAL   A 1 69  ? 54.30900 62.26800 23.21000 1.000 39.46688  ? 66  VAL   A CG2 1 
ATOM   498  N  N   . GLU   A 1 70  ? 50.72500 59.46200 23.64800 1.000 48.48915  ? 67  GLU   A N   1 
ATOM   499  C  CA  . GLU   A 1 70  ? 49.87000 58.38500 24.13300 1.000 49.06103  ? 67  GLU   A CA  1 
ATOM   500  C  C   . GLU   A 1 70  ? 49.67000 57.30900 23.07000 1.000 51.64462  ? 67  GLU   A C   1 
ATOM   501  O  O   . GLU   A 1 70  ? 49.68900 56.11300 23.38100 1.000 48.63085  ? 67  GLU   A O   1 
ATOM   502  C  CB  . GLU   A 1 70  ? 48.53500 58.95000 24.59500 1.000 47.74203  ? 67  GLU   A CB  1 
ATOM   503  C  CG  . GLU   A 1 70  ? 48.58200 59.47600 26.02800 1.000 53.13427  ? 67  GLU   A CG  1 
ATOM   504  C  CD  . GLU   A 1 70  ? 47.43600 60.41700 26.36100 1.000 58.29648  ? 67  GLU   A CD  1 
ATOM   505  O  OE1 . GLU   A 1 70  ? 46.46600 60.48900 25.57600 1.000 56.77761  ? 67  GLU   A OE1 1 
ATOM   506  O  OE2 . GLU   A 1 70  ? 47.51600 61.09400 27.40800 1.000 63.26945  ? 67  GLU   A OE2 1 
ATOM   507  N  N   . ALA   A 1 71  ? 49.51000 57.71600 21.80600 1.000 45.72060  ? 68  ALA   A N   1 
ATOM   508  C  CA  . ALA   A 1 71  ? 49.30300 56.75900 20.72300 1.000 48.83151  ? 68  ALA   A CA  1 
ATOM   509  C  C   . ALA   A 1 71  ? 50.52000 55.87500 20.52800 1.000 43.29213  ? 68  ALA   A C   1 
ATOM   510  O  O   . ALA   A 1 71  ? 50.39200 54.65700 20.36700 1.000 42.44628  ? 68  ALA   A O   1 
ATOM   511  C  CB  . ALA   A 1 71  ? 48.97800 57.49400 19.42100 1.000 39.10467  ? 68  ALA   A CB  1 
ATOM   512  N  N   . PHE   A 1 72  ? 51.71300 56.47200 20.51800 1.000 37.71051  ? 69  PHE   A N   1 
ATOM   513  C  CA  . PHE   A 1 72  ? 52.90900 55.66000 20.39600 1.000 46.60766  ? 69  PHE   A CA  1 
ATOM   514  C  C   . PHE   A 1 72  ? 53.05900 54.69800 21.56900 1.000 45.77657  ? 69  PHE   A C   1 
ATOM   515  O  O   . PHE   A 1 72  ? 53.44200 53.54000 21.37600 1.000 43.33312  ? 69  PHE   A O   1 
ATOM   516  C  CB  . PHE   A 1 72  ? 54.16900 56.50900 20.29200 1.000 35.90607  ? 69  PHE   A CB  1 
ATOM   517  C  CG  . PHE   A 1 72  ? 55.39500 55.65700 20.23700 1.000 37.31544  ? 69  PHE   A CG  1 
ATOM   518  C  CD1 . PHE   A 1 72  ? 55.78200 55.07900 19.04600 1.000 38.82190  ? 69  PHE   A CD1 1 
ATOM   519  C  CD2 . PHE   A 1 72  ? 56.09000 55.33500 21.39100 1.000 39.31872  ? 69  PHE   A CD2 1 
ATOM   520  C  CE1 . PHE   A 1 72  ? 56.88500 54.25000 18.98600 1.000 39.11996  ? 69  PHE   A CE1 1 
ATOM   521  C  CE2 . PHE   A 1 72  ? 57.19000 54.50400 21.33700 1.000 36.33288  ? 69  PHE   A CE2 1 
ATOM   522  C  CZ  . PHE   A 1 72  ? 57.58500 53.96200 20.11800 1.000 40.51906  ? 69  PHE   A CZ  1 
ATOM   523  N  N   . GLU   A 1 73  ? 52.80200 55.17100 22.77500 1.000 39.41473  ? 70  GLU   A N   1 
ATOM   524  C  CA  . GLU   A 1 73  ? 53.02500 54.31200 23.95900 1.000 41.88780  ? 70  GLU   A CA  1 
ATOM   525  C  C   . GLU   A 1 73  ? 52.08700 53.10100 23.90800 1.000 49.58525  ? 70  GLU   A C   1 
ATOM   526  O  O   . GLU   A 1 73  ? 52.52500 52.02400 24.30900 1.000 51.11714  ? 70  GLU   A O   1 
ATOM   527  C  CB  . GLU   A 1 73  ? 52.86700 55.14200 25.22800 1.000 44.61216  ? 70  GLU   A CB  1 
ATOM   528  C  CG  . GLU   A 1 73  ? 53.95300 56.18500 25.38100 1.000 55.10600  ? 70  GLU   A CG  1 
ATOM   529  C  CD  . GLU   A 1 73  ? 53.79300 57.08000 26.59400 1.000 90.65994  ? 70  GLU   A CD  1 
ATOM   530  O  OE1 . GLU   A 1 73  ? 52.72600 57.01800 27.22800 1.000 111.86742 ? 70  GLU   A OE1 1 
ATOM   531  O  OE2 . GLU   A 1 73  ? 54.73800 57.83000 26.90200 1.000 86.63306  ? 70  GLU   A OE2 1 
ATOM   532  N  N   . TYR   A 1 74  ? 50.85900 53.28000 23.42900 1.000 40.53232  ? 71  TYR   A N   1 
ATOM   533  C  CA  . TYR   A 1 74  ? 49.91900 52.17000 23.39000 1.000 46.71173  ? 71  TYR   A CA  1 
ATOM   534  C  C   . TYR   A 1 74  ? 50.17000 51.25400 22.19800 1.000 43.65764  ? 71  TYR   A C   1 
ATOM   535  O  O   . TYR   A 1 74  ? 50.12100 50.02900 22.35000 1.000 48.73638  ? 71  TYR   A O   1 
ATOM   536  C  CB  . TYR   A 1 74  ? 48.47000 52.67800 23.38200 1.000 41.78388  ? 71  TYR   A CB  1 
ATOM   537  C  CG  . TYR   A 1 74  ? 47.49400 51.62700 23.88900 1.000 53.37915  ? 71  TYR   A CG  1 
ATOM   538  C  CD1 . TYR   A 1 74  ? 47.72000 50.97600 25.10900 1.000 50.86630  ? 71  TYR   A CD1 1 
ATOM   539  C  CD2 . TYR   A 1 74  ? 46.37000 51.26000 23.15300 1.000 48.20929  ? 71  TYR   A CD2 1 
ATOM   540  C  CE1 . TYR   A 1 74  ? 46.86100 50.00800 25.57800 1.000 45.03992  ? 71  TYR   A CE1 1 
ATOM   541  C  CE2 . TYR   A 1 74  ? 45.48500 50.27800 23.62800 1.000 50.28880  ? 71  TYR   A CE2 1 
ATOM   542  C  CZ  . TYR   A 1 74  ? 45.74800 49.65900 24.84300 1.000 60.54882  ? 71  TYR   A CZ  1 
ATOM   543  O  OH  . TYR   A 1 74  ? 44.90500 48.68900 25.33900 1.000 65.77847  ? 71  TYR   A OH  1 
ATOM   544  N  N   . TYR   A 1 75  ? 50.45500 51.81800 21.01000 1.000 41.46917  ? 72  TYR   A N   1 
ATOM   545  C  CA  . TYR   A 1 75  ? 50.51800 51.04000 19.77500 1.000 35.33696  ? 72  TYR   A CA  1 
ATOM   546  C  C   . TYR   A 1 75  ? 51.91600 50.82800 19.23600 1.000 42.48181  ? 72  TYR   A C   1 
ATOM   547  O  O   . TYR   A 1 75  ? 52.09100 49.98000 18.35600 1.000 42.66640  ? 72  TYR   A O   1 
ATOM   548  C  CB  . TYR   A 1 75  ? 49.68600 51.69800 18.65900 1.000 38.72956  ? 72  TYR   A CB  1 
ATOM   549  C  CG  . TYR   A 1 75  ? 48.23300 51.87700 19.01100 1.000 40.88007  ? 72  TYR   A CG  1 
ATOM   550  C  CD1 . TYR   A 1 75  ? 47.36100 50.80500 18.96900 1.000 39.31010  ? 72  TYR   A CD1 1 
ATOM   551  C  CD2 . TYR   A 1 75  ? 47.73200 53.11400 19.38800 1.000 43.91597  ? 72  TYR   A CD2 1 
ATOM   552  C  CE1 . TYR   A 1 75  ? 46.01800 50.95000 19.29400 1.000 37.72754  ? 72  TYR   A CE1 1 
ATOM   553  C  CE2 . TYR   A 1 75  ? 46.38600 53.27800 19.71700 1.000 43.31718  ? 72  TYR   A CE2 1 
ATOM   554  C  CZ  . TYR   A 1 75  ? 45.53400 52.18600 19.66400 1.000 47.25324  ? 72  TYR   A CZ  1 
ATOM   555  O  OH  . TYR   A 1 75  ? 44.20100 52.32200 19.98200 1.000 52.76871  ? 72  TYR   A OH  1 
ATOM   556  N  N   . HIS   A 1 76  ? 52.89200 51.60200 19.70600 1.000 44.13776  ? 73  HIS   A N   1 
ATOM   557  C  CA  . HIS   A 1 76  ? 54.26400 51.56600 19.20400 1.000 39.98949  ? 73  HIS   A CA  1 
ATOM   558  C  C   . HIS   A 1 76  ? 54.33900 51.91100 17.71700 1.000 43.37009  ? 73  HIS   A C   1 
ATOM   559  O  O   . HIS   A 1 76  ? 55.21500 51.43700 17.00000 1.000 46.09307  ? 73  HIS   A O   1 
ATOM   560  C  CB  . HIS   A 1 76  ? 54.92300 50.21900 19.52100 1.000 41.54363  ? 73  HIS   A CB  1 
ATOM   561  C  CG  . HIS   A 1 76  ? 55.26000 50.07200 20.97400 1.000 45.85534  ? 73  HIS   A CG  1 
ATOM   562  N  ND1 . HIS   A 1 76  ? 56.39600 49.44000 21.42100 1.000 33.98980  ? 73  HIS   A ND1 1 
ATOM   563  C  CD2 . HIS   A 1 76  ? 54.62900 50.54200 22.08300 1.000 38.56522  ? 73  HIS   A CD2 1 
ATOM   564  C  CE1 . HIS   A 1 76  ? 56.43900 49.49600 22.73700 1.000 38.84605  ? 73  HIS   A CE1 1 
ATOM   565  N  NE2 . HIS   A 1 76  ? 55.37800 50.15800 23.16300 1.000 46.51047  ? 73  HIS   A NE2 1 
ATOM   566  N  N   . THR   A 1 77  ? 53.46200 52.79300 17.25100 1.000 41.21096  ? 74  THR   A N   1 
ATOM   567  C  CA  . THR   A 1 77  ? 53.57900 53.31000 15.89700 1.000 55.63118  ? 74  THR   A CA  1 
ATOM   568  C  C   . THR   A 1 77  ? 53.22900 54.79200 15.88700 1.000 55.91196  ? 74  THR   A C   1 
ATOM   569  O  O   . THR   A 1 77  ? 52.43000 55.26500 16.70100 1.000 43.42907  ? 74  THR   A O   1 
ATOM   570  C  CB  . THR   A 1 77  ? 52.67900 52.52900 14.91700 1.000 51.08286  ? 74  THR   A CB  1 
ATOM   571  O  OG1 . THR   A 1 77  ? 52.98300 52.90500 13.56300 1.000 52.47515  ? 74  THR   A OG1 1 
ATOM   572  C  CG2 . THR   A 1 77  ? 51.20700 52.78400 15.21600 1.000 47.20864  ? 74  THR   A CG2 1 
ATOM   573  N  N   . THR   A 1 78  ? 53.85200 55.52600 14.96300 1.000 48.37819  ? 75  THR   A N   1 
ATOM   574  C  CA  . THR   A 1 78  ? 53.48100 56.91000 14.70600 1.000 59.96066  ? 75  THR   A CA  1 
ATOM   575  C  C   . THR   A 1 78  ? 52.74500 57.08000 13.38500 1.000 63.30638  ? 75  THR   A C   1 
ATOM   576  O  O   . THR   A 1 78  ? 52.39300 58.20900 13.03200 1.000 66.07178  ? 75  THR   A O   1 
ATOM   577  C  CB  . THR   A 1 78  ? 54.72400 57.80700 14.72300 1.000 52.66725  ? 75  THR   A CB  1 
ATOM   578  O  OG1 . THR   A 1 78  ? 55.70500 57.27700 13.82900 1.000 50.50318  ? 75  THR   A OG1 1 
ATOM   579  C  CG2 . THR   A 1 78  ? 55.31500 57.83300 16.12100 1.000 55.91579  ? 75  THR   A CG2 1 
ATOM   580  N  N   . ASP   A 1 79  ? 52.50900 55.98600 12.65000 1.000 55.42151  ? 76  ASP   A N   1 
ATOM   581  C  CA  . ASP   A 1 79  ? 51.78800 55.94300 11.38400 1.000 45.90623  ? 76  ASP   A CA  1 
ATOM   582  C  C   . ASP   A 1 79  ? 50.40500 56.56600 11.51500 1.000 47.03645  ? 76  ASP   A C   1 
ATOM   583  O  O   . ASP   A 1 79  ? 49.50700 55.98700 12.13800 1.000 51.31812  ? 76  ASP   A O   1 
ATOM   584  C  CB  . ASP   A 1 79  ? 51.68700 54.49700 10.89500 1.000 53.22344  ? 76  ASP   A CB  1 
ATOM   585  C  CG  . ASP   A 1 79  ? 50.96400 54.35600 9.54900  1.000 60.16256  ? 76  ASP   A CG  1 
ATOM   586  O  OD1 . ASP   A 1 79  ? 50.52500 55.36200 8.94300  1.000 60.41592  ? 76  ASP   A OD1 1 
ATOM   587  O  OD2 . ASP   A 1 79  ? 50.83000 53.20400 9.09500  1.000 55.52858  ? 76  ASP   A OD2 1 
ATOM   588  N  N   . PRO   A 1 80  ? 50.17100 57.71100 10.87100 1.000 58.02908  ? 77  PRO   A N   1 
ATOM   589  C  CA  . PRO   A 1 80  ? 48.86300 58.36700 11.00200 1.000 46.50037  ? 77  PRO   A CA  1 
ATOM   590  C  C   . PRO   A 1 80  ? 47.72400 57.55700 10.40400 1.000 59.54866  ? 77  PRO   A C   1 
ATOM   591  O  O   . PRO   A 1 80  ? 46.56600 57.81500 10.75400 1.000 60.05441  ? 77  PRO   A O   1 
ATOM   592  C  CB  . PRO   A 1 80  ? 49.05500 59.69800 10.25700 1.000 54.96101  ? 77  PRO   A CB  1 
ATOM   593  C  CG  . PRO   A 1 80  ? 50.52200 59.76400 9.88300  1.000 57.63880  ? 77  PRO   A CG  1 
ATOM   594  C  CD  . PRO   A 1 80  ? 51.02700 58.36800 9.86800  1.000 56.33890  ? 77  PRO   A CD  1 
ATOM   595  N  N   . SER   A 1 81  ? 48.00100 56.57900 9.53000  1.000 44.51926  ? 78  SER   A N   1 
ATOM   596  C  CA  . SER   A 1 81  ? 46.91700 55.74600 9.01200  1.000 57.56826  ? 78  SER   A CA  1 
ATOM   597  C  C   . SER   A 1 81  ? 46.52900 54.58900 9.94000  1.000 58.22466  ? 78  SER   A C   1 
ATOM   598  O  O   . SER   A 1 81  ? 45.46900 53.98100 9.73500  1.000 54.37051  ? 78  SER   A O   1 
ATOM   599  C  CB  . SER   A 1 81  ? 47.27800 55.19400 7.62400  1.000 44.11463  ? 78  SER   A CB  1 
ATOM   600  O  OG  . SER   A 1 81  ? 48.31000 54.22600 7.67100  1.000 54.13835  ? 78  SER   A OG  1 
ATOM   601  N  N   . PHE   A 1 82  ? 47.33100 54.29000 10.96700 1.000 48.83060  ? 79  PHE   A N   1 
ATOM   602  C  CA  . PHE   A 1 82  ? 47.10200 53.07200 11.74200 1.000 50.32466  ? 79  PHE   A CA  1 
ATOM   603  C  C   . PHE   A 1 82  ? 45.72100 53.07900 12.38300 1.000 47.23473  ? 79  PHE   A C   1 
ATOM   604  O  O   . PHE   A 1 82  ? 44.98000 52.09000 12.30500 1.000 44.80584  ? 79  PHE   A O   1 
ATOM   605  C  CB  . PHE   A 1 82  ? 48.19000 52.89800 12.80800 1.000 56.40500  ? 79  PHE   A CB  1 
ATOM   606  C  CG  . PHE   A 1 82  ? 48.07100 51.60800 13.59000 1.000 48.91699  ? 79  PHE   A CG  1 
ATOM   607  C  CD1 . PHE   A 1 82  ? 47.27800 51.54200 14.73200 1.000 43.33346  ? 79  PHE   A CD1 1 
ATOM   608  C  CD2 . PHE   A 1 82  ? 48.73900 50.46700 13.17500 1.000 46.59846  ? 79  PHE   A CD2 1 
ATOM   609  C  CE1 . PHE   A 1 82  ? 47.15100 50.36600 15.44700 1.000 45.99687  ? 79  PHE   A CE1 1 
ATOM   610  C  CE2 . PHE   A 1 82  ? 48.62400 49.27800 13.89200 1.000 55.48449  ? 79  PHE   A CE2 1 
ATOM   611  C  CZ  . PHE   A 1 82  ? 47.83200 49.22700 15.02300 1.000 47.15864  ? 79  PHE   A CZ  1 
ATOM   612  N  N   . LEU   A 1 83  ? 45.34400 54.19600 12.99900 1.000 49.46884  ? 80  LEU   A N   1 
ATOM   613  C  CA  . LEU   A 1 83  ? 44.07000 54.24300 13.70400 1.000 44.84640  ? 80  LEU   A CA  1 
ATOM   614  C  C   . LEU   A 1 83  ? 42.90700 53.91800 12.77700 1.000 49.97232  ? 80  LEU   A C   1 
ATOM   615  O  O   . LEU   A 1 83  ? 42.01600 53.13700 13.13500 1.000 55.29653  ? 80  LEU   A O   1 
ATOM   616  C  CB  . LEU   A 1 83  ? 43.87200 55.61000 14.35400 1.000 51.34961  ? 80  LEU   A CB  1 
ATOM   617  C  CG  . LEU   A 1 83  ? 42.53200 55.62900 15.09500 1.000 55.40008  ? 80  LEU   A CG  1 
ATOM   618  C  CD1 . LEU   A 1 83  ? 42.59700 54.75700 16.34400 1.000 58.95658  ? 80  LEU   A CD1 1 
ATOM   619  C  CD2 . LEU   A 1 83  ? 42.05800 57.04500 15.41000 1.000 67.80020  ? 80  LEU   A CD2 1 
ATOM   620  N  N   . GLY   A 1 84  ? 42.90200 54.50000 11.57100 1.000 57.57707  ? 81  GLY   A N   1 
ATOM   621  C  CA  . GLY   A 1 84  ? 41.80100 54.26200 10.65300 1.000 40.36952  ? 81  GLY   A CA  1 
ATOM   622  C  C   . GLY   A 1 84  ? 41.78200 52.84700 10.10700 1.000 41.59599  ? 81  GLY   A C   1 
ATOM   623  O  O   . GLY   A 1 84  ? 40.71700 52.24300 9.96600  1.000 46.13325  ? 81  GLY   A O   1 
ATOM   624  N  N   . ARG   A 1 85  ? 42.95300 52.29800 9.78300  1.000 40.39775  ? 82  ARG   A N   1 
ATOM   625  C  CA  . ARG   A 1 85  ? 42.99100 50.89500 9.37700  1.000 47.81066  ? 82  ARG   A CA  1 
ATOM   626  C  C   . ARG   A 1 85  ? 42.49300 49.99300 10.50000 1.000 52.36694  ? 82  ARG   A C   1 
ATOM   627  O  O   . ARG   A 1 85  ? 41.70300 49.06800 10.26700 1.000 46.55183  ? 82  ARG   A O   1 
ATOM   628  C  CB  . ARG   A 1 85  ? 44.40500 50.51400 8.93200  1.000 44.05173  ? 82  ARG   A CB  1 
ATOM   629  C  CG  . ARG   A 1 85  ? 44.81200 51.35600 7.72300  1.000 52.41961  ? 82  ARG   A CG  1 
ATOM   630  C  CD  . ARG   A 1 85  ? 46.11500 50.95900 7.07400  1.000 52.99889  ? 82  ARG   A CD  1 
ATOM   631  N  NE  . ARG   A 1 85  ? 47.27200 51.31400 7.87700  1.000 53.13554  ? 82  ARG   A NE  1 
ATOM   632  C  CZ  . ARG   A 1 85  ? 47.91300 50.44400 8.64000  1.000 59.52193  ? 82  ARG   A CZ  1 
ATOM   633  N  NH1 . ARG   A 1 85  ? 47.50200 49.18900 8.73500  1.000 57.68479  ? 82  ARG   A NH1 1 
ATOM   634  N  NH2 . ARG   A 1 85  ? 48.98700 50.84100 9.32800  1.000 56.74598  ? 82  ARG   A NH2 1 
ATOM   635  N  N   . TYR   A 1 86  ? 42.89300 50.29400 11.73500 1.000 49.60130  ? 83  TYR   A N   1 
ATOM   636  C  CA  . TYR   A 1 86  ? 42.45100 49.51100 12.88000 1.000 40.80881  ? 83  TYR   A CA  1 
ATOM   637  C  C   . TYR   A 1 86  ? 40.94200 49.60400 13.03600 1.000 44.15199  ? 83  TYR   A C   1 
ATOM   638  O  O   . TYR   A 1 86  ? 40.24500 48.58300 13.14200 1.000 41.84120  ? 83  TYR   A O   1 
ATOM   639  C  CB  . TYR   A 1 86  ? 43.19900 50.00500 14.12300 1.000 39.48208  ? 83  TYR   A CB  1 
ATOM   640  C  CG  . TYR   A 1 86  ? 42.70600 49.52200 15.48600 1.000 52.66474  ? 83  TYR   A CG  1 
ATOM   641  C  CD1 . TYR   A 1 86  ? 42.12500 48.27200 15.65800 1.000 41.77857  ? 83  TYR   A CD1 1 
ATOM   642  C  CD2 . TYR   A 1 86  ? 42.86100 50.33100 16.61000 1.000 56.16248  ? 83  TYR   A CD2 1 
ATOM   643  C  CE1 . TYR   A 1 86  ? 41.68300 47.85700 16.89800 1.000 49.35810  ? 83  TYR   A CE1 1 
ATOM   644  C  CE2 . TYR   A 1 86  ? 42.43800 49.92200 17.85600 1.000 54.21783  ? 83  TYR   A CE2 1 
ATOM   645  C  CZ  . TYR   A 1 86  ? 41.85000 48.69000 18.00000 1.000 57.26720  ? 83  TYR   A CZ  1 
ATOM   646  O  OH  . TYR   A 1 86  ? 41.42700 48.30600 19.25000 1.000 58.21168  ? 83  TYR   A OH  1 
ATOM   647  N  N   . MET   A 1 87  ? 40.41200 50.82600 13.00300 1.000 43.69781  ? 84  MET   A N   1 
ATOM   648  C  CA  . MET   A 1 87  ? 38.97400 50.99400 13.17700 1.000 42.72656  ? 84  MET   A CA  1 
ATOM   649  C  C   . MET   A 1 87  ? 38.18300 50.37700 12.03400 1.000 50.38580  ? 84  MET   A C   1 
ATOM   650  O  O   . MET   A 1 87  ? 37.08900 49.84700 12.25500 1.000 46.67237  ? 84  MET   A O   1 
ATOM   651  C  CB  . MET   A 1 87  ? 38.63100 52.47600 13.31700 1.000 47.85208  ? 84  MET   A CB  1 
ATOM   652  C  CG  . MET   A 1 87  ? 39.23900 53.05600 14.57600 1.000 53.26186  ? 84  MET   A CG  1 
ATOM   653  S  SD  . MET   A 1 87  ? 38.20200 52.66000 15.99900 1.000 54.02577  ? 84  MET   A SD  1 
ATOM   654  C  CE  . MET   A 1 87  ? 39.25600 51.52300 16.89800 1.000 61.06042  ? 84  MET   A CE  1 
ATOM   655  N  N   . SER   A 1 88  ? 38.71400 50.43200 10.80900 1.000 44.16497  ? 85  SER   A N   1 
ATOM   656  C  CA  A SER   A 1 88  ? 38.02300 49.81800 9.68000  0.248 50.21316  ? 85  SER   A CA  1 
ATOM   657  C  CA  B SER   A 1 88  ? 38.01400 49.82100 9.69100  0.752 50.36975  ? 85  SER   A CA  1 
ATOM   658  C  C   . SER   A 1 88  ? 37.92400 48.30900 9.85900  1.000 42.04043  ? 85  SER   A C   1 
ATOM   659  O  O   . SER   A 1 88  ? 36.87100 47.71200 9.60400  1.000 43.21249  ? 85  SER   A O   1 
ATOM   660  C  CB  A SER   A 1 88  ? 38.73900 50.15100 8.37000  0.248 51.15328  ? 85  SER   A CB  1 
ATOM   661  C  CB  B SER   A 1 88  ? 38.71200 50.18600 8.37800  0.752 51.20428  ? 85  SER   A CB  1 
ATOM   662  O  OG  A SER   A 1 88  ? 38.66400 51.53300 8.06700  0.248 48.39972  ? 85  SER   A OG  1 
ATOM   663  O  OG  B SER   A 1 88  ? 38.10200 49.52300 7.29700  0.752 49.15268  ? 85  SER   A OG  1 
ATOM   664  N  N   . ALA   A 1 89  ? 39.01500 47.67400 10.29200 1.000 40.81629  ? 86  ALA   A N   1 
ATOM   665  C  CA  . ALA   A 1 89  ? 38.98100 46.23800 10.56000 1.000 40.54133  ? 86  ALA   A CA  1 
ATOM   666  C  C   . ALA   A 1 89  ? 38.02700 45.91200 11.70100 1.000 40.38617  ? 86  ALA   A C   1 
ATOM   667  O  O   . ALA   A 1 89  ? 37.19800 44.99300 11.58800 1.000 41.02147  ? 86  ALA   A O   1 
ATOM   668  C  CB  . ALA   A 1 89  ? 40.38300 45.73200 10.88900 1.000 45.23454  ? 86  ALA   A CB  1 
ATOM   669  N  N   . LEU   A 1 90  ? 38.12700 46.65700 12.80700 1.000 43.35390  ? 87  LEU   A N   1 
ATOM   670  C  CA  . LEU   A 1 90  ? 37.29100 46.37500 13.97200 1.000 46.83203  ? 87  LEU   A CA  1 
ATOM   671  C  C   . LEU   A 1 90  ? 35.81700 46.38700 13.60400 1.000 43.13037  ? 87  LEU   A C   1 
ATOM   672  O  O   . LEU   A 1 90  ? 35.04200 45.55900 14.10100 1.000 45.07518  ? 87  LEU   A O   1 
ATOM   673  C  CB  . LEU   A 1 90  ? 37.57100 47.39800 15.08800 1.000 38.68850  ? 87  LEU   A CB  1 
ATOM   674  C  CG  . LEU   A 1 90  ? 36.75800 47.21300 16.37300 1.000 53.46886  ? 87  LEU   A CG  1 
ATOM   675  C  CD1 . LEU   A 1 90  ? 37.11300 45.86800 17.03700 1.000 40.71930  ? 87  LEU   A CD1 1 
ATOM   676  C  CD2 . LEU   A 1 90  ? 36.98300 48.38500 17.32300 1.000 45.62708  ? 87  LEU   A CD2 1 
ATOM   677  N  N   . ASN   A 1 91  ? 35.42800 47.29100 12.69900 1.000 47.65410  ? 88  ASN   A N   1 
ATOM   678  C  CA  . ASN   A 1 91  ? 34.04200 47.39500 12.25100 1.000 48.81242  ? 88  ASN   A CA  1 
ATOM   679  C  C   . ASN   A 1 91  ? 33.50300 46.06600 11.72300 1.000 45.14378  ? 88  ASN   A C   1 
ATOM   680  O  O   . ASN   A 1 91  ? 32.32900 45.74500 11.94300 1.000 48.41023  ? 88  ASN   A O   1 
ATOM   681  C  CB  . ASN   A 1 91  ? 33.94400 48.49500 11.19200 1.000 57.16181  ? 88  ASN   A CB  1 
ATOM   682  C  CG  . ASN   A 1 91  ? 32.53300 49.00000 11.00100 1.000 60.67438  ? 88  ASN   A CG  1 
ATOM   683  O  OD1 . ASN   A 1 91  ? 31.76600 49.11100 11.95300 1.000 62.45987  ? 88  ASN   A OD1 1 
ATOM   684  N  ND2 . ASN   A 1 91  ? 32.17900 49.29500 9.75700  1.000 75.07137  ? 88  ASN   A ND2 1 
ATOM   685  N  N   . HIS   A 1 92  ? 34.34100 45.26400 11.05700 1.000 47.82965  ? 89  HIS   A N   1 
ATOM   686  C  CA  . HIS   A 1 92  ? 33.95400 43.90400 10.68700 1.000 49.68414  ? 89  HIS   A CA  1 
ATOM   687  C  C   . HIS   A 1 92  ? 34.20200 42.90500 11.82700 1.000 43.32215  ? 89  HIS   A C   1 
ATOM   688  O  O   . HIS   A 1 92  ? 33.34500 42.07100 12.12000 1.000 46.63257  ? 89  HIS   A O   1 
ATOM   689  C  CB  . HIS   A 1 92  ? 34.71600 43.43100 9.43400  1.000 39.24187  ? 89  HIS   A CB  1 
ATOM   690  C  CG  . HIS   A 1 92  ? 34.53100 44.31000 8.23200  1.000 52.90096  ? 89  HIS   A CG  1 
ATOM   691  N  ND1 . HIS   A 1 92  ? 33.62200 44.03800 7.23000  1.000 48.07938  ? 89  HIS   A ND1 1 
ATOM   692  C  CD2 . HIS   A 1 92  ? 35.16000 45.45400 7.86800  1.000 43.56746  ? 89  HIS   A CD2 1 
ATOM   693  C  CE1 . HIS   A 1 92  ? 33.69300 44.98300 6.30900  1.000 57.07198  ? 89  HIS   A CE1 1 
ATOM   694  N  NE2 . HIS   A 1 92  ? 34.61700 45.85500 6.67300  1.000 50.90631  ? 89  HIS   A NE2 1 
ATOM   695  N  N   . THR   A 1 93  ? 35.37100 42.93900 12.46600 1.000 41.10186  ? 90  THR   A N   1 
ATOM   696  C  CA  . THR   A 1 93  ? 35.70200 41.82900 13.36500 1.000 48.17648  ? 90  THR   A CA  1 
ATOM   697  C  C   . THR   A 1 93  ? 34.76600 41.77200 14.56900 1.000 48.62591  ? 90  THR   A C   1 
ATOM   698  O  O   . THR   A 1 93  ? 34.44900 40.67600 15.04800 1.000 43.75267  ? 90  THR   A O   1 
ATOM   699  C  CB  . THR   A 1 93  ? 37.15400 41.90700 13.82600 1.000 38.19964  ? 90  THR   A CB  1 
ATOM   700  O  OG1 . THR   A 1 93  ? 37.34600 43.08300 14.61300 1.000 42.82856  ? 90  THR   A OG1 1 
ATOM   701  C  CG2 . THR   A 1 93  ? 38.09100 41.93000 12.61700 1.000 38.68717  ? 90  THR   A CG2 1 
ATOM   702  N  N   . LYS   A 1 94  ? 34.25100 42.92000 15.02200 1.000 47.89226  ? 91  LYS   A N   1 
ATOM   703  C  CA  . LYS   A 1 94  ? 33.26700 42.90700 16.10500 1.000 45.97459  ? 91  LYS   A CA  1 
ATOM   704  C  C   . LYS   A 1 94  ? 31.99200 42.17300 15.70500 1.000 47.29362  ? 91  LYS   A C   1 
ATOM   705  O  O   . LYS   A 1 94  ? 31.20900 41.80100 16.58200 1.000 49.11766  ? 91  LYS   A O   1 
ATOM   706  C  CB  . LYS   A 1 94  ? 32.94700 44.33700 16.55600 1.000 45.64608  ? 91  LYS   A CB  1 
ATOM   707  C  CG  . LYS   A 1 94  ? 32.18400 45.14400 15.48400 1.000 67.39786  ? 91  LYS   A CG  1 
ATOM   708  C  CD  . LYS   A 1 94  ? 31.95000 46.63300 15.84700 1.000 66.43573  ? 91  LYS   A CD  1 
ATOM   709  C  CE  . LYS   A 1 94  ? 31.00200 47.31200 14.82100 1.000 68.03590  ? 91  LYS   A CE  1 
ATOM   710  N  NZ  . LYS   A 1 94  ? 31.14800 48.80400 14.75500 1.000 71.98966  ? 91  LYS   A NZ  1 
ATOM   711  N  N   . LYS   A 1 95  ? 31.77500 41.92900 14.40900 1.000 47.70736  ? 92  LYS   A N   1 
ATOM   712  C  CA  . LYS   A 1 95  ? 30.60800 41.18600 13.94600 1.000 48.42565  ? 92  LYS   A CA  1 
ATOM   713  C  C   . LYS   A 1 95  ? 30.89600 39.70400 13.72300 1.000 56.33380  ? 92  LYS   A C   1 
ATOM   714  O  O   . LYS   A 1 95  ? 29.95100 38.92200 13.55700 1.000 52.55878  ? 92  LYS   A O   1 
ATOM   715  C  CB  . LYS   A 1 95  ? 30.06500 41.80200 12.64100 1.000 52.61956  ? 92  LYS   A CB  1 
ATOM   716  C  CG  . LYS   A 1 95  ? 29.40900 43.18700 12.80800 1.000 60.79691  ? 92  LYS   A CG  1 
ATOM   717  C  CD  . LYS   A 1 95  ? 28.70100 43.64500 11.51300 1.000 60.91185  ? 92  LYS   A CD  1 
ATOM   718  C  CE  . LYS   A 1 95  ? 29.64300 44.43800 10.57300 1.000 78.60206  ? 92  LYS   A CE  1 
ATOM   719  N  NZ  . LYS   A 1 95  ? 29.68700 43.96400 9.13200  1.000 58.05391  ? 92  LYS   A NZ  1 
ATOM   720  N  N   . TRP   A 1 96  ? 32.16300 39.29500 13.70400 1.000 47.33684  ? 93  TRP   A N   1 
ATOM   721  C  CA  . TRP   A 1 96  ? 32.47100 37.87500 13.63500 1.000 51.41406  ? 93  TRP   A CA  1 
ATOM   722  C  C   . TRP   A 1 96  ? 32.07200 37.16700 14.93700 1.000 49.20267  ? 93  TRP   A C   1 
ATOM   723  O  O   . TRP   A 1 96  ? 31.91300 37.79300 15.98900 1.000 52.78400  ? 93  TRP   A O   1 
ATOM   724  C  CB  . TRP   A 1 96  ? 33.95700 37.66900 13.37400 1.000 41.62326  ? 93  TRP   A CB  1 
ATOM   725  C  CG  . TRP   A 1 96  ? 34.43400 38.22200 12.06600 1.000 45.36667  ? 93  TRP   A CG  1 
ATOM   726  C  CD1 . TRP   A 1 96  ? 33.66600 38.70300 11.03800 1.000 41.98190  ? 93  TRP   A CD1 1 
ATOM   727  C  CD2 . TRP   A 1 96  ? 35.79300 38.35400 11.64900 1.000 40.43604  ? 93  TRP   A CD2 1 
ATOM   728  N  NE1 . TRP   A 1 96  ? 34.46800 39.13600 10.01400 1.000 43.49208  ? 93  TRP   A NE1 1 
ATOM   729  C  CE2 . TRP   A 1 96  ? 35.77900 38.92200 10.35600 1.000 40.49261  ? 93  TRP   A CE2 1 
ATOM   730  C  CE3 . TRP   A 1 96  ? 37.02100 38.04200 12.24000 1.000 41.58493  ? 93  TRP   A CE3 1 
ATOM   731  C  CZ2 . TRP   A 1 96  ? 36.94300 39.18500 9.64500  1.000 37.73905  ? 93  TRP   A CZ2 1 
ATOM   732  C  CZ3 . TRP   A 1 96  ? 38.18300 38.29800 11.53200 1.000 39.73110  ? 93  TRP   A CZ3 1 
ATOM   733  C  CH2 . TRP   A 1 96  ? 38.13400 38.86700 10.24200 1.000 42.80161  ? 93  TRP   A CH2 1 
ATOM   734  N  N   . LYS   A 1 97  ? 31.91400 35.84400 14.85300 1.000 50.71309  ? 94  LYS   A N   1 
ATOM   735  C  CA  . LYS   A 1 97  ? 31.69900 34.99600 16.02400 1.000 53.89620  ? 94  LYS   A CA  1 
ATOM   736  C  C   . LYS   A 1 97  ? 32.99600 34.29200 16.42500 1.000 51.85713  ? 94  LYS   A C   1 
ATOM   737  O  O   . LYS   A 1 97  ? 33.75900 33.82800 15.56500 1.000 52.58791  ? 94  LYS   A O   1 
ATOM   738  C  CB  . LYS   A 1 97  ? 30.61600 33.94300 15.74900 1.000 53.70861  ? 94  LYS   A CB  1 
ATOM   739  C  CG  . LYS   A 1 97  ? 29.26900 34.52000 15.36000 1.000 64.51431  ? 94  LYS   A CG  1 
ATOM   740  C  CD  . LYS   A 1 97  ? 28.78200 35.53300 16.38300 1.000 65.12276  ? 94  LYS   A CD  1 
ATOM   741  C  CE  . LYS   A 1 97  ? 27.67200 36.40800 15.81700 1.000 68.65828  ? 94  LYS   A CE  1 
ATOM   742  N  NZ  . LYS   A 1 97  ? 27.49000 37.65200 16.62600 1.000 83.48397  ? 94  LYS   A NZ  1 
ATOM   743  N  N   . TYR   A 1 98  ? 33.21200 34.16500 17.73600 1.000 54.03676  ? 95  TYR   A N   1 
ATOM   744  C  CA  . TYR   A 1 98  ? 34.43800 33.60000 18.30300 1.000 47.77378  ? 95  TYR   A CA  1 
ATOM   745  C  C   . TYR   A 1 98  ? 34.10600 32.41100 19.20000 1.000 54.42736  ? 95  TYR   A C   1 
ATOM   746  O  O   . TYR   A 1 98  ? 34.20000 32.49500 20.43000 1.000 46.67262  ? 95  TYR   A O   1 
ATOM   747  C  CB  . TYR   A 1 98  ? 35.21000 34.67700 19.06600 1.000 40.33341  ? 95  TYR   A CB  1 
ATOM   748  C  CG  . TYR   A 1 98  ? 35.58100 35.82400 18.15100 1.000 54.73913  ? 95  TYR   A CG  1 
ATOM   749  C  CD1 . TYR   A 1 98  ? 36.75200 35.78800 17.40500 1.000 45.36869  ? 95  TYR   A CD1 1 
ATOM   750  C  CD2 . TYR   A 1 98  ? 34.73000 36.91500 17.98500 1.000 47.47055  ? 95  TYR   A CD2 1 
ATOM   751  C  CE1 . TYR   A 1 98  ? 37.08700 36.81800 16.54900 1.000 44.78935  ? 95  TYR   A CE1 1 
ATOM   752  C  CE2 . TYR   A 1 98  ? 35.05300 37.94600 17.12700 1.000 48.22112  ? 95  TYR   A CE2 1 
ATOM   753  C  CZ  . TYR   A 1 98  ? 36.22900 37.89800 16.41000 1.000 48.39412  ? 95  TYR   A CZ  1 
ATOM   754  O  OH  . TYR   A 1 98  ? 36.54600 38.92800 15.55000 1.000 43.17700  ? 95  TYR   A OH  1 
ATOM   755  N  N   . PRO   A 1 99  ? 33.73800 31.27300 18.61400 1.000 52.69954  ? 96  PRO   A N   1 
ATOM   756  C  CA  . PRO   A 1 99  ? 33.34900 30.12500 19.44300 1.000 45.97466  ? 96  PRO   A CA  1 
ATOM   757  C  C   . PRO   A 1 99  ? 34.56500 29.49000 20.11900 1.000 56.68206  ? 96  PRO   A C   1 
ATOM   758  O  O   . PRO   A 1 99  ? 35.67200 29.48700 19.57300 1.000 48.05861  ? 96  PRO   A O   1 
ATOM   759  C  CB  . PRO   A 1 99  ? 32.69300 29.17400 18.43500 1.000 45.15734  ? 96  PRO   A CB  1 
ATOM   760  C  CG  . PRO   A 1 99  ? 33.39100 29.48900 17.12000 1.000 50.41887  ? 96  PRO   A CG  1 
ATOM   761  C  CD  . PRO   A 1 99  ? 33.77800 30.94500 17.17200 1.000 42.05883  ? 96  PRO   A CD  1 
ATOM   762  N  N   . GLN   A 1 100 ? 34.36200 29.00300 21.34500 1.000 54.65581  ? 97  GLN   A N   1 
ATOM   763  C  CA  . GLN   A 1 100 ? 35.36000 28.15500 21.99100 1.000 61.25128  ? 97  GLN   A CA  1 
ATOM   764  C  C   . GLN   A 1 100 ? 35.32800 26.76300 21.36300 1.000 49.99623  ? 97  GLN   A C   1 
ATOM   765  O  O   . GLN   A 1 100 ? 34.26900 26.14500 21.25200 1.000 55.35999  ? 97  GLN   A O   1 
ATOM   766  C  CB  . GLN   A 1 100 ? 35.09700 28.05200 23.49800 1.000 57.34496  ? 97  GLN   A CB  1 
ATOM   767  C  CG  . GLN   A 1 100 ? 35.21600 29.36400 24.28900 1.000 55.95059  ? 97  GLN   A CG  1 
ATOM   768  C  CD  . GLN   A 1 100 ? 36.58300 30.01400 24.15900 1.000 65.28992  ? 97  GLN   A CD  1 
ATOM   769  O  OE1 . GLN   A 1 100 ? 37.59600 29.45900 24.60600 1.000 64.31623  ? 97  GLN   A OE1 1 
ATOM   770  N  NE2 . GLN   A 1 100 ? 36.62000 31.20100 23.54900 1.000 66.51974  ? 97  GLN   A NE2 1 
ATOM   771  N  N   . VAL   A 1 101 ? 36.47800 26.28500 20.91400 1.000 43.32732  ? 98  VAL   A N   1 
ATOM   772  C  CA  . VAL   A 1 101 ? 36.58800 24.98700 20.27200 1.000 49.26622  ? 98  VAL   A CA  1 
ATOM   773  C  C   . VAL   A 1 101 ? 37.75000 24.27900 20.94000 1.000 48.69868  ? 98  VAL   A C   1 
ATOM   774  O  O   . VAL   A 1 101 ? 38.89400 24.73800 20.83600 1.000 46.74659  ? 98  VAL   A O   1 
ATOM   775  C  CB  . VAL   A 1 101 ? 36.81100 25.10200 18.75800 1.000 59.78457  ? 98  VAL   A CB  1 
ATOM   776  C  CG1 . VAL   A 1 101 ? 37.09300 23.73300 18.14000 1.000 51.07064  ? 98  VAL   A CG1 1 
ATOM   777  C  CG2 . VAL   A 1 101 ? 35.60100 25.76000 18.08600 1.000 57.94931  ? 98  VAL   A CG2 1 
ATOM   778  N  N   . ASN   A 1 102 ? 37.46300 23.18300 21.65600 1.000 55.48585  ? 99  ASN   A N   1 
ATOM   779  C  CA  . ASN   A 1 102 ? 38.51400 22.38000 22.28200 1.000 45.00670  ? 99  ASN   A CA  1 
ATOM   780  C  C   . ASN   A 1 102 ? 39.32600 23.22900 23.26300 1.000 46.89150  ? 99  ASN   A C   1 
ATOM   781  O  O   . ASN   A 1 102 ? 40.55800 23.16200 23.30500 1.000 45.05277  ? 99  ASN   A O   1 
ATOM   782  C  CB  . ASN   A 1 102 ? 39.40400 21.75500 21.20000 1.000 45.63442  ? 99  ASN   A CB  1 
ATOM   783  C  CG  . ASN   A 1 102 ? 40.37400 20.72000 21.74800 1.000 69.06437  ? 99  ASN   A CG  1 
ATOM   784  O  OD1 . ASN   A 1 102 ? 41.56900 20.73500 21.41400 1.000 62.97453  ? 99  ASN   A OD1 1 
ATOM   785  N  ND2 . ASN   A 1 102 ? 39.87200 19.81900 22.58700 1.000 49.96144  ? 99  ASN   A ND2 1 
ATOM   786  N  N   . GLY   A 1 103 ? 38.63200 24.08900 24.01200 1.000 45.51503  ? 100 GLY   A N   1 
ATOM   787  C  CA  . GLY   A 1 103 ? 39.29100 24.99700 24.92800 1.000 44.72377  ? 100 GLY   A CA  1 
ATOM   788  C  C   . GLY   A 1 103 ? 40.03400 26.16200 24.30300 1.000 50.58926  ? 100 GLY   A C   1 
ATOM   789  O  O   . GLY   A 1 103 ? 40.78100 26.84600 25.01300 1.000 54.69327  ? 100 GLY   A O   1 
ATOM   790  N  N   . LEU   A 1 104 ? 39.86600 26.41600 23.00500 1.000 50.60595  ? 101 LEU   A N   1 
ATOM   791  C  CA  . LEU   A 1 104 ? 40.58600 27.48500 22.32100 1.000 45.80355  ? 101 LEU   A CA  1 
ATOM   792  C  C   . LEU   A 1 104 ? 39.59900 28.43400 21.65500 1.000 48.74449  ? 101 LEU   A C   1 
ATOM   793  O  O   . LEU   A 1 104 ? 38.56100 28.00600 21.14000 1.000 45.11983  ? 101 LEU   A O   1 
ATOM   794  C  CB  . LEU   A 1 104 ? 41.55200 26.91900 21.28400 1.000 42.41721  ? 101 LEU   A CB  1 
ATOM   795  C  CG  . LEU   A 1 104 ? 42.72500 26.10500 21.83500 1.000 47.29140  ? 101 LEU   A CG  1 
ATOM   796  C  CD1 . LEU   A 1 104 ? 43.28000 25.17500 20.76900 1.000 46.16667  ? 101 LEU   A CD1 1 
ATOM   797  C  CD2 . LEU   A 1 104 ? 43.81300 27.02800 22.34900 1.000 41.30994  ? 101 LEU   A CD2 1 
ATOM   798  N  N   . THR   A 1 105 ? 39.91600 29.72500 21.67700 1.000 42.74053  ? 102 THR   A N   1 
ATOM   799  C  CA  . THR   A 1 105 ? 39.09900 30.69900 20.96400 1.000 48.41817  ? 102 THR   A CA  1 
ATOM   800  C  C   . THR   A 1 105 ? 39.38700 30.58500 19.47200 1.000 45.24993  ? 102 THR   A C   1 
ATOM   801  O  O   . THR   A 1 105 ? 40.53200 30.77100 19.04100 1.000 43.64531  ? 102 THR   A O   1 
ATOM   802  C  CB  . THR   A 1 105 ? 39.38100 32.12000 21.44400 1.000 45.75011  ? 102 THR   A CB  1 
ATOM   803  O  OG1 . THR   A 1 105 ? 39.25300 32.18100 22.86000 1.000 42.28797  ? 102 THR   A OG1 1 
ATOM   804  C  CG2 . THR   A 1 105 ? 38.38500 33.11500 20.80000 1.000 46.75101  ? 102 THR   A CG2 1 
ATOM   805  N  N   . SER   A 1 106 ? 38.37100 30.25000 18.69600 1.000 39.52004  ? 103 SER   A N   1 
ATOM   806  C  CA  . SER   A 1 106 ? 38.47200 30.20200 17.25000 1.000 44.68618  ? 103 SER   A CA  1 
ATOM   807  C  C   . SER   A 1 106 ? 37.65900 31.35100 16.64800 1.000 46.64664  ? 103 SER   A C   1 
ATOM   808  O  O   . SER   A 1 106 ? 37.19600 32.24800 17.36400 1.000 45.42375  ? 103 SER   A O   1 
ATOM   809  C  CB  . SER   A 1 106 ? 37.99300 28.84100 16.74300 1.000 42.10843  ? 103 SER   A CB  1 
ATOM   810  O  OG  . SER   A 1 106 ? 38.30300 28.70800 15.37300 1.000 42.74260  ? 103 SER   A OG  1 
ATOM   811  N  N   . ILE   A 1 107 ? 37.46700 31.31200 15.32400 1.000 40.86258  ? 104 ILE   A N   1 
ATOM   812  C  CA  . ILE   A 1 107 ? 36.63500 32.28300 14.61000 1.000 47.52764  ? 104 ILE   A CA  1 
ATOM   813  C  C   . ILE   A 1 107 ? 35.73700 31.54500 13.62700 1.000 47.52792  ? 104 ILE   A C   1 
ATOM   814  O  O   . ILE   A 1 107 ? 36.21900 30.75000 12.81400 1.000 45.00690  ? 104 ILE   A O   1 
ATOM   815  C  CB  . ILE   A 1 107 ? 37.45600 33.34000 13.84000 1.000 40.91901  ? 104 ILE   A CB  1 
ATOM   816  C  CG1 . ILE   A 1 107 ? 38.73700 33.74400 14.57500 1.000 39.93651  ? 104 ILE   A CG1 1 
ATOM   817  C  CG2 . ILE   A 1 107 ? 36.60000 34.57600 13.59100 1.000 47.05107  ? 104 ILE   A CG2 1 
ATOM   818  C  CD1 . ILE   A 1 107 ? 39.59500 34.80700 13.80300 1.000 35.56862  ? 104 ILE   A CD1 1 
ATOM   819  N  N   . LYS   A 1 108 ? 34.44500 31.84400 13.66800 1.000 49.99316  ? 105 LYS   A N   1 
ATOM   820  C  CA  . LYS   A 1 108 ? 33.52600 31.33900 12.65900 1.000 48.92190  ? 105 LYS   A CA  1 
ATOM   821  C  C   . LYS   A 1 108 ? 33.85400 31.94600 11.29400 1.000 53.60845  ? 105 LYS   A C   1 
ATOM   822  O  O   . LYS   A 1 108 ? 34.23800 33.11700 11.19500 1.000 48.45130  ? 105 LYS   A O   1 
ATOM   823  C  CB  . LYS   A 1 108 ? 32.09400 31.66400 13.08100 1.000 61.95351  ? 105 LYS   A CB  1 
ATOM   824  C  CG  . LYS   A 1 108 ? 30.99900 31.18300 12.15200 1.000 72.03003  ? 105 LYS   A CG  1 
ATOM   825  C  CD  . LYS   A 1 108 ? 29.63500 31.49300 12.77900 1.000 83.45661  ? 105 LYS   A CD  1 
ATOM   826  C  CE  . LYS   A 1 108 ? 28.45900 31.05600 11.90700 1.000 75.55161  ? 105 LYS   A CE  1 
ATOM   827  N  NZ  . LYS   A 1 108 ? 28.33600 31.87400 10.67600 1.000 78.22836  ? 105 LYS   A NZ  1 
ATOM   828  N  N   . TRP   A 1 109 ? 33.71000 31.13800 10.23900 1.000 59.01878  ? 106 TRP   A N   1 
ATOM   829  C  CA  . TRP   A 1 109 ? 34.11600 31.53300 8.88700  1.000 53.05584  ? 106 TRP   A CA  1 
ATOM   830  C  C   . TRP   A 1 109 ? 33.42100 32.82200 8.42800  1.000 56.32657  ? 106 TRP   A C   1 
ATOM   831  O  O   . TRP   A 1 109 ? 32.20200 32.96800 8.56500  1.000 58.19311  ? 106 TRP   A O   1 
ATOM   832  C  CB  . TRP   A 1 109 ? 33.81900 30.38600 7.90700  1.000 52.23464  ? 106 TRP   A CB  1 
ATOM   833  C  CG  . TRP   A 1 109 ? 33.44900 30.84500 6.51000  1.000 95.05979  ? 106 TRP   A CG  1 
ATOM   834  C  CD1 . TRP   A 1 109 ? 34.26000 31.50100 5.61600  1.000 94.66202  ? 106 TRP   A CD1 1 
ATOM   835  C  CD2 . TRP   A 1 109 ? 32.18200 30.67700 5.84500  1.000 104.58305 ? 106 TRP   A CD2 1 
ATOM   836  N  NE1 . TRP   A 1 109 ? 33.57300 31.75700 4.44900  1.000 100.82486 ? 106 TRP   A NE1 1 
ATOM   837  C  CE2 . TRP   A 1 109 ? 32.30100 31.26000 4.56200  1.000 104.42366 ? 106 TRP   A CE2 1 
ATOM   838  C  CE3 . TRP   A 1 109 ? 30.96400 30.09300 6.20900  1.000 98.82489  ? 106 TRP   A CE3 1 
ATOM   839  C  CZ2 . TRP   A 1 109 ? 31.24800 31.27500 3.64800  1.000 108.84815 ? 106 TRP   A CZ2 1 
ATOM   840  C  CZ3 . TRP   A 1 109 ? 29.91900 30.11300 5.29800  1.000 108.21431 ? 106 TRP   A CZ3 1 
ATOM   841  C  CH2 . TRP   A 1 109 ? 30.06900 30.69900 4.03300  1.000 115.37025 ? 106 TRP   A CH2 1 
ATOM   842  N  N   . ALA   A 1 110 ? 34.20900 33.75300 7.87400  1.000 50.45979  ? 107 ALA   A N   1 
ATOM   843  C  CA  . ALA   A 1 110 ? 33.74000 35.02500 7.32900  1.000 49.49400  ? 107 ALA   A CA  1 
ATOM   844  C  C   . ALA   A 1 110 ? 34.89200 35.74000 6.64100  1.000 47.94043  ? 107 ALA   A C   1 
ATOM   845  O  O   . ALA   A 1 110 ? 36.02700 35.67200 7.11000  1.000 48.67422  ? 107 ALA   A O   1 
ATOM   846  C  CB  . ALA   A 1 110 ? 33.17200 35.93800 8.42400  1.000 41.88297  ? 107 ALA   A CB  1 
ATOM   847  N  N   . ASP   A 1 111 ? 34.59100 36.44200 5.54700  1.000 51.70895  ? 108 ASP   A N   1 
ATOM   848  C  CA  . ASP   A 1 111 ? 35.49000 37.45900 4.98400  1.000 41.28951  ? 108 ASP   A CA  1 
ATOM   849  C  C   . ASP   A 1 111 ? 36.92000 36.94600 4.82100  1.000 46.47839  ? 108 ASP   A C   1 
ATOM   850  O  O   . ASP   A 1 111 ? 37.88700 37.64000 5.15100  1.000 40.11085  ? 108 ASP   A O   1 
ATOM   851  C  CB  . ASP   A 1 111 ? 35.48800 38.73000 5.84500  1.000 41.39464  ? 108 ASP   A CB  1 
ATOM   852  C  CG  . ASP   A 1 111 ? 34.09700 39.34300 6.00600  1.000 60.03772  ? 108 ASP   A CG  1 
ATOM   853  O  OD1 . ASP   A 1 111 ? 33.18300 38.97400 5.23400  1.000 72.17356  ? 108 ASP   A OD1 1 
ATOM   854  O  OD2 . ASP   A 1 111 ? 33.91700 40.19700 6.90500  1.000 49.17712  ? 108 ASP   A OD2 1 
ATOM   855  N  N   . ASN   A 1 112 ? 37.05000 35.70000 4.35700  1.000 39.28599  ? 109 ASN   A N   1 
ATOM   856  C  CA  . ASN   A 1 112 ? 38.34800 35.04900 4.15400  1.000 42.90949  ? 109 ASN   A CA  1 
ATOM   857  C  C   . ASN   A 1 112 ? 39.21400 35.03000 5.41800  1.000 45.85069  ? 109 ASN   A C   1 
ATOM   858  O  O   . ASN   A 1 112 ? 40.42800 35.20700 5.34700  1.000 44.45039  ? 109 ASN   A O   1 
ATOM   859  C  CB  . ASN   A 1 112 ? 39.11400 35.71300 3.00700  1.000 42.36246  ? 109 ASN   A CB  1 
ATOM   860  C  CG  . ASN   A 1 112 ? 38.49600 35.41900 1.65500  1.000 54.79745  ? 109 ASN   A CG  1 
ATOM   861  O  OD1 . ASN   A 1 112 ? 38.02400 34.31000 1.41200  1.000 59.58840  ? 109 ASN   A OD1 1 
ATOM   862  N  ND2 . ASN   A 1 112 ? 38.47300 36.41800 0.77900  1.000 43.98107  ? 109 ASN   A ND2 1 
ATOM   863  N  N   . ASN   A 1 113 ? 38.60800 34.81000 6.58900  1.000 45.22674  ? 110 ASN   A N   1 
ATOM   864  C  CA  . ASN   A 1 113 ? 39.37100 34.92900 7.82800  1.000 41.27644  ? 110 ASN   A CA  1 
ATOM   865  C  C   . ASN   A 1 113 ? 40.01700 33.61800 8.27500  1.000 48.77683  ? 110 ASN   A C   1 
ATOM   866  O  O   . ASN   A 1 113 ? 40.52600 33.55800 9.40400  1.000 44.90964  ? 110 ASN   A O   1 
ATOM   867  C  CB  . ASN   A 1 113 ? 38.50400 35.50100 8.96200  1.000 36.95861  ? 110 ASN   A CB  1 
ATOM   868  C  CG  . ASN   A 1 113 ? 37.37900 34.55400 9.40000  1.000 42.08786  ? 110 ASN   A CG  1 
ATOM   869  O  OD1 . ASN   A 1 113 ? 37.23300 33.45700 8.87200  1.000 42.04915  ? 110 ASN   A OD1 1 
ATOM   870  N  ND2 . ASN   A 1 113 ? 36.57600 34.99600 10.36200 1.000 38.66147  ? 110 ASN   A ND2 1 
ATOM   871  N  N   . CYS   A 1 114 ? 40.01600 32.57800 7.42500  1.000 46.94377  ? 111 CYS   A N   1 
ATOM   872  C  CA  . CYS   A 1 114 ? 40.57500 31.29200 7.83400  1.000 45.31514  ? 111 CYS   A CA  1 
ATOM   873  C  C   . CYS   A 1 114 ? 42.00700 31.44400 8.34600  1.000 46.92277  ? 111 CYS   A C   1 
ATOM   874  O  O   . CYS   A 1 114 ? 42.34800 30.90800 9.40300  1.000 44.40254  ? 111 CYS   A O   1 
ATOM   875  C  CB  . CYS   A 1 114 ? 40.51500 30.27400 6.68500  1.000 38.69886  ? 111 CYS   A CB  1 
ATOM   876  S  SG  . CYS   A 1 114 ? 41.51100 30.59700 5.21000  1.000 47.46135  ? 111 CYS   A SG  1 
ATOM   877  N  N   . TYR   A 1 115 ? 42.85000 32.20400 7.63500  1.000 42.74098  ? 112 TYR   A N   1 
ATOM   878  C  CA  . TYR   A 1 115 ? 44.22900 32.36600 8.09300  1.000 35.95776  ? 112 TYR   A CA  1 
ATOM   879  C  C   . TYR   A 1 115 ? 44.30600 33.09500 9.43000  1.000 36.12301  ? 112 TYR   A C   1 
ATOM   880  O  O   . TYR   A 1 115 ? 45.23200 32.84600 10.21000 1.000 41.52801  ? 112 TYR   A O   1 
ATOM   881  C  CB  . TYR   A 1 115 ? 45.07200 33.10400 7.04500  1.000 37.67150  ? 112 TYR   A CB  1 
ATOM   882  C  CG  . TYR   A 1 115 ? 44.92000 34.61500 7.03200  1.000 36.80141  ? 112 TYR   A CG  1 
ATOM   883  C  CD1 . TYR   A 1 115 ? 43.78400 35.21100 6.48900  1.000 47.04014  ? 112 TYR   A CD1 1 
ATOM   884  C  CD2 . TYR   A 1 115 ? 45.92000 35.44600 7.52200  1.000 33.71337  ? 112 TYR   A CD2 1 
ATOM   885  C  CE1 . TYR   A 1 115 ? 43.63000 36.59200 6.45000  1.000 35.73958  ? 112 TYR   A CE1 1 
ATOM   886  C  CE2 . TYR   A 1 115 ? 45.78900 36.83000 7.50000  1.000 33.93580  ? 112 TYR   A CE2 1 
ATOM   887  C  CZ  . TYR   A 1 115 ? 44.64100 37.40000 6.95400  1.000 43.13611  ? 112 TYR   A CZ  1 
ATOM   888  O  OH  . TYR   A 1 115 ? 44.50600 38.77100 6.92000  1.000 36.59277  ? 112 TYR   A OH  1 
ATOM   889  N  N   . LEU   A 1 116 ? 43.36200 33.99600 9.70900  1.000 43.70809  ? 113 LEU   A N   1 
ATOM   890  C  CA  . LEU   A 1 116 ? 43.34900 34.67200 11.00400 1.000 37.33721  ? 113 LEU   A CA  1 
ATOM   891  C  C   . LEU   A 1 116 ? 42.94500 33.71800 12.11900 1.000 43.97855  ? 113 LEU   A C   1 
ATOM   892  O  O   . LEU   A 1 116 ? 43.52900 33.74100 13.20800 1.000 41.34284  ? 113 LEU   A O   1 
ATOM   893  C  CB  . LEU   A 1 116 ? 42.39600 35.86800 10.97100 1.000 42.77511  ? 113 LEU   A CB  1 
ATOM   894  C  CG  . LEU   A 1 116 ? 42.87900 37.06700 10.16400 1.000 49.07228  ? 113 LEU   A CG  1 
ATOM   895  C  CD1 . LEU   A 1 116 ? 41.72700 38.04100 9.95100  1.000 44.30551  ? 113 LEU   A CD1 1 
ATOM   896  C  CD2 . LEU   A 1 116 ? 44.05100 37.75800 10.87900 1.000 45.51838  ? 113 LEU   A CD2 1 
ATOM   897  N  N   . ALA   A 1 117 ? 41.93700 32.88300 11.87100 1.000 41.40516  ? 114 ALA   A N   1 
ATOM   898  C  CA  . ALA   A 1 117 ? 41.58600 31.86500 12.85100 1.000 45.63379  ? 114 ALA   A CA  1 
ATOM   899  C  C   . ALA   A 1 117 ? 42.78700 30.97400 13.16400 1.000 43.32999  ? 114 ALA   A C   1 
ATOM   900  O  O   . ALA   A 1 117 ? 43.10700 30.74500 14.33600 1.000 45.25339  ? 114 ALA   A O   1 
ATOM   901  C  CB  . ALA   A 1 117 ? 40.40100 31.04700 12.34300 1.000 39.33166  ? 114 ALA   A CB  1 
ATOM   902  N  N   . THR   A 1 118 ? 43.50500 30.52500 12.13000 1.000 39.12349  ? 115 THR   A N   1 
ATOM   903  C  CA  . THR   A 1 118 ? 44.65100 29.64800 12.35100 1.000 40.98729  ? 115 THR   A CA  1 
ATOM   904  C  C   . THR   A 1 118 ? 45.73700 30.33900 13.16600 1.000 39.92937  ? 115 THR   A C   1 
ATOM   905  O  O   . THR   A 1 118 ? 46.27000 29.75500 14.12000 1.000 44.59561  ? 115 THR   A O   1 
ATOM   906  C  CB  . THR   A 1 118 ? 45.18800 29.15700 11.00900 1.000 41.89525  ? 115 THR   A CB  1 
ATOM   907  O  OG1 . THR   A 1 118 ? 44.17700 28.36700 10.37600 1.000 44.59363  ? 115 THR   A OG1 1 
ATOM   908  C  CG2 . THR   A 1 118 ? 46.44900 28.31300 11.19600 1.000 37.02591  ? 115 THR   A CG2 1 
ATOM   909  N  N   . ALA   A 1 119 ? 46.05500 31.59500 12.83500 1.000 39.99207  ? 116 ALA   A N   1 
ATOM   910  C  CA  . ALA   A 1 119 ? 47.01900 32.34800 13.64600 1.000 43.07072  ? 116 ALA   A CA  1 
ATOM   911  C  C   . ALA   A 1 119 ? 46.52900 32.52500 15.08400 1.000 42.78128  ? 116 ALA   A C   1 
ATOM   912  O  O   . ALA   A 1 119 ? 47.28300 32.32400 16.04600 1.000 41.47773  ? 116 ALA   A O   1 
ATOM   913  C  CB  . ALA   A 1 119 ? 47.28900 33.71600 13.01400 1.000 33.10404  ? 116 ALA   A CB  1 
ATOM   914  N  N   . LEU   A 1 120 ? 45.27200 32.92000 15.24600 1.000 40.38428  ? 117 LEU   A N   1 
ATOM   915  C  CA  . LEU   A 1 120 ? 44.71500 33.11600 16.57300 1.000 40.23357  ? 117 LEU   A CA  1 
ATOM   916  C  C   . LEU   A 1 120 ? 44.84700 31.85000 17.41800 1.000 51.37175  ? 117 LEU   A C   1 
ATOM   917  O  O   . LEU   A 1 120 ? 45.23400 31.90800 18.59700 1.000 40.92573  ? 117 LEU   A O   1 
ATOM   918  C  CB  . LEU   A 1 120 ? 43.25500 33.53400 16.43600 1.000 37.72537  ? 117 LEU   A CB  1 
ATOM   919  C  CG  . LEU   A 1 120 ? 42.47900 33.64400 17.74300 1.000 49.51686  ? 117 LEU   A CG  1 
ATOM   920  C  CD1 . LEU   A 1 120 ? 43.18500 34.62700 18.65400 1.000 37.71989  ? 117 LEU   A CD1 1 
ATOM   921  C  CD2 . LEU   A 1 120 ? 41.03400 34.06200 17.44900 1.000 38.09533  ? 117 LEU   A CD2 1 
ATOM   922  N  N   . LEU   A 1 121 ? 44.53200 30.69800 16.81900 1.000 42.09340  ? 118 LEU   A N   1 
ATOM   923  C  CA  . LEU   A 1 121 ? 44.63500 29.42100 17.51300 1.000 41.16480  ? 118 LEU   A CA  1 
ATOM   924  C  C   . LEU   A 1 121 ? 46.08100 29.09700 17.87300 1.000 38.90962  ? 118 LEU   A C   1 
ATOM   925  O  O   . LEU   A 1 121 ? 46.35600 28.63800 18.98700 1.000 40.07101  ? 118 LEU   A O   1 
ATOM   926  C  CB  . LEU   A 1 121 ? 44.01400 28.31600 16.64300 1.000 38.98842  ? 118 LEU   A CB  1 
ATOM   927  C  CG  . LEU   A 1 121 ? 42.48100 28.43000 16.54400 1.000 42.40542  ? 118 LEU   A CG  1 
ATOM   928  C  CD1 . LEU   A 1 121 ? 41.88400 27.60900 15.39500 1.000 36.15557  ? 118 LEU   A CD1 1 
ATOM   929  C  CD2 . LEU   A 1 121 ? 41.84800 28.02100 17.88300 1.000 36.93868  ? 118 LEU   A CD2 1 
ATOM   930  N  N   . THR   A 1 122 ? 47.01300 29.31800 16.94200 1.000 39.49252  ? 119 THR   A N   1 
ATOM   931  C  CA  . THR   A 1 122 ? 48.42500 29.06100 17.21500 1.000 37.59635  ? 119 THR   A CA  1 
ATOM   932  C  C   . THR   A 1 122 ? 48.94000 29.93100 18.35400 1.000 42.39111  ? 119 THR   A C   1 
ATOM   933  O  O   . THR   A 1 122 ? 49.68500 29.45700 19.22300 1.000 39.31238  ? 119 THR   A O   1 
ATOM   934  C  CB  . THR   A 1 122 ? 49.23900 29.31300 15.94900 1.000 40.43225  ? 119 THR   A CB  1 
ATOM   935  O  OG1 . THR   A 1 122 ? 48.68300 28.54200 14.87700 1.000 38.59701  ? 119 THR   A OG1 1 
ATOM   936  C  CG2 . THR   A 1 122 ? 50.70800 28.93300 16.14400 1.000 36.28318  ? 119 THR   A CG2 1 
ATOM   937  N  N   . LEU   A 1 123 ? 48.53300 31.20300 18.37700 1.000 40.26533  ? 120 LEU   A N   1 
ATOM   938  C  CA  . LEU   A 1 123 ? 49.03800 32.13500 19.37600 1.000 37.20544  ? 120 LEU   A CA  1 
ATOM   939  C  C   . LEU   A 1 123 ? 48.64000 31.72600 20.78800 1.000 46.65104  ? 120 LEU   A C   1 
ATOM   940  O  O   . LEU   A 1 123 ? 49.35000 32.05100 21.74300 1.000 40.59625  ? 120 LEU   A O   1 
ATOM   941  C  CB  . LEU   A 1 123 ? 48.53600 33.54700 19.07900 1.000 37.10798  ? 120 LEU   A CB  1 
ATOM   942  C  CG  . LEU   A 1 123 ? 49.21800 34.21200 17.88100 1.000 45.94375  ? 120 LEU   A CG  1 
ATOM   943  C  CD1 . LEU   A 1 123 ? 48.41200 35.42500 17.43700 1.000 43.86000  ? 120 LEU   A CD1 1 
ATOM   944  C  CD2 . LEU   A 1 123 ? 50.64500 34.59500 18.22800 1.000 42.35859  ? 120 LEU   A CD2 1 
ATOM   945  N  N   . GLN   A 1 124 ? 47.52000 31.01000 20.93600 1.000 41.03323  ? 121 GLN   A N   1 
ATOM   946  C  CA  . GLN   A 1 124 ? 47.08300 30.51400 22.22900 1.000 39.25162  ? 121 GLN   A CA  1 
ATOM   947  C  C   . GLN   A 1 124 ? 47.85700 29.28100 22.67800 1.000 42.28832  ? 121 GLN   A C   1 
ATOM   948  O  O   . GLN   A 1 124 ? 47.60200 28.77600 23.77600 1.000 45.63228  ? 121 GLN   A O   1 
ATOM   949  C  CB  . GLN   A 1 124 ? 45.58500 30.20800 22.19700 1.000 42.67237  ? 121 GLN   A CB  1 
ATOM   950  C  CG  . GLN   A 1 124 ? 44.72000 31.45400 22.10300 1.000 47.44218  ? 121 GLN   A CG  1 
ATOM   951  C  CD  . GLN   A 1 124 ? 43.30600 31.15500 21.64300 1.000 45.17106  ? 121 GLN   A CD  1 
ATOM   952  O  OE1 . GLN   A 1 124 ? 42.43700 30.83600 22.45300 1.000 48.71819  ? 121 GLN   A OE1 1 
ATOM   953  N  NE2 . GLN   A 1 124 ? 43.06600 31.26200 20.34400 1.000 38.41642  ? 121 GLN   A NE2 1 
ATOM   954  N  N   . GLN   A 1 125 ? 48.80100 28.79600 21.87700 1.000 41.05953  ? 122 GLN   A N   1 
ATOM   955  C  CA  . GLN   A 1 125 ? 49.53300 27.58200 22.20800 1.000 41.77550  ? 122 GLN   A CA  1 
ATOM   956  C  C   . GLN   A 1 125 ? 51.04400 27.74800 22.22700 1.000 48.80061  ? 122 GLN   A C   1 
ATOM   957  O  O   . GLN   A 1 125 ? 51.75400 26.75100 22.40900 1.000 44.47074  ? 122 GLN   A O   1 
ATOM   958  C  CB  . GLN   A 1 125 ? 49.16600 26.47400 21.21800 1.000 38.25759  ? 122 GLN   A CB  1 
ATOM   959  C  CG  . GLN   A 1 125 ? 47.71500 26.15300 21.26400 1.000 38.39474  ? 122 GLN   A CG  1 
ATOM   960  C  CD  . GLN   A 1 125 ? 47.35300 25.19700 20.16400 1.000 48.16702  ? 122 GLN   A CD  1 
ATOM   961  O  OE1 . GLN   A 1 125 ? 47.73400 24.02700 20.19900 1.000 41.91167  ? 122 GLN   A OE1 1 
ATOM   962  N  NE2 . GLN   A 1 125 ? 46.65300 25.69900 19.15000 1.000 39.06604  ? 122 GLN   A NE2 1 
ATOM   963  N  N   . ILE   A 1 126 ? 51.56000 28.96100 22.03400 1.000 41.10611  ? 123 ILE   A N   1 
ATOM   964  C  CA  . ILE   A 1 126 ? 52.98900 29.21400 22.12400 1.000 43.17475  ? 123 ILE   A CA  1 
ATOM   965  C  C   . ILE   A 1 126 ? 53.19900 30.40200 23.05400 1.000 48.14141  ? 123 ILE   A C   1 
ATOM   966  O  O   . ILE   A 1 126 ? 52.30300 31.22500 23.25800 1.000 47.28675  ? 123 ILE   A O   1 
ATOM   967  C  CB  . ILE   A 1 126 ? 53.64000 29.47000 20.75000 1.000 37.56067  ? 123 ILE   A CB  1 
ATOM   968  C  CG1 . ILE   A 1 126 ? 52.97000 30.66000 20.04300 1.000 35.84782  ? 123 ILE   A CG1 1 
ATOM   969  C  CG2 . ILE   A 1 126 ? 53.59300 28.19600 19.87400 1.000 35.21845  ? 123 ILE   A CG2 1 
ATOM   970  C  CD1 . ILE   A 1 126 ? 53.65200 31.03900 18.73800 1.000 36.84698  ? 123 ILE   A CD1 1 
ATOM   971  N  N   . GLU   A 1 127 ? 54.39900 30.47100 23.63400 1.000 43.34826  ? 124 GLU   A N   1 
ATOM   972  C  CA  . GLU   A 1 127 ? 54.72500 31.48000 24.64100 1.000 52.71044  ? 124 GLU   A CA  1 
ATOM   973  C  C   . GLU   A 1 127 ? 55.23100 32.74100 23.94800 1.000 45.37636  ? 124 GLU   A C   1 
ATOM   974  O  O   . GLU   A 1 127 ? 56.27100 32.71300 23.28900 1.000 48.83101  ? 124 GLU   A O   1 
ATOM   975  C  CB  . GLU   A 1 127 ? 55.77800 30.95700 25.62300 1.000 54.61408  ? 124 GLU   A CB  1 
ATOM   976  C  CG  . GLU   A 1 127 ? 56.29400 32.00200 26.61800 1.000 54.41139  ? 124 GLU   A CG  1 
ATOM   977  C  CD  . GLU   A 1 127 ? 55.16900 32.60100 27.46600 1.000 68.34389  ? 124 GLU   A CD  1 
ATOM   978  O  OE1 . GLU   A 1 127 ? 54.34400 31.80600 27.96000 1.000 69.12884  ? 124 GLU   A OE1 1 
ATOM   979  O  OE2 . GLU   A 1 127 ? 55.08000 33.85100 27.61000 1.000 61.03473  ? 124 GLU   A OE2 1 
ATOM   980  N  N   . LEU   A 1 128 ? 54.50700 33.84400 24.10800 1.000 47.14099  ? 125 LEU   A N   1 
ATOM   981  C  CA  . LEU   A 1 128 ? 54.83000 35.05300 23.36800 1.000 54.75420  ? 125 LEU   A CA  1 
ATOM   982  C  C   . LEU   A 1 128 ? 54.44000 36.26800 24.18800 1.000 50.71570  ? 125 LEU   A C   1 
ATOM   983  O  O   . LEU   A 1 128 ? 53.35500 36.30500 24.77300 1.000 47.66732  ? 125 LEU   A O   1 
ATOM   984  C  CB  . LEU   A 1 128 ? 54.09700 35.08000 22.02600 1.000 56.05028  ? 125 LEU   A CB  1 
ATOM   985  C  CG  . LEU   A 1 128 ? 54.71200 35.82200 20.85400 1.000 57.92559  ? 125 LEU   A CG  1 
ATOM   986  C  CD1 . LEU   A 1 128 ? 56.08800 35.27800 20.48500 1.000 46.36387  ? 125 LEU   A CD1 1 
ATOM   987  C  CD2 . LEU   A 1 128 ? 53.76500 35.71500 19.69300 1.000 55.81512  ? 125 LEU   A CD2 1 
ATOM   988  N  N   . LYS   A 1 129 ? 55.32800 37.25800 24.22400 1.000 43.60075  ? 126 LYS   A N   1 
ATOM   989  C  CA  . LYS   A 1 129 ? 55.03700 38.54500 24.84300 1.000 50.79192  ? 126 LYS   A CA  1 
ATOM   990  C  C   . LYS   A 1 129 ? 55.12000 39.63500 23.78200 1.000 45.76492  ? 126 LYS   A C   1 
ATOM   991  O  O   . LYS   A 1 129 ? 56.18900 39.86900 23.20900 1.000 47.22522  ? 126 LYS   A O   1 
ATOM   992  C  CB  . LYS   A 1 129 ? 56.00200 38.84900 25.98600 1.000 49.88592  ? 126 LYS   A CB  1 
ATOM   993  C  CG  . LYS   A 1 129 ? 55.69400 40.14600 26.71800 1.000 66.06222  ? 126 LYS   A CG  1 
ATOM   994  C  CD  . LYS   A 1 129 ? 56.77000 40.47900 27.76500 1.000 90.71092  ? 126 LYS   A CD  1 
ATOM   995  C  CE  . LYS   A 1 129 ? 57.30900 41.90800 27.58700 1.000 97.18184  ? 126 LYS   A CE  1 
ATOM   996  N  NZ  . LYS   A 1 129 ? 58.80400 41.99800 27.48300 1.000 84.39636  ? 126 LYS   A NZ  1 
ATOM   997  N  N   . PHE   A 1 130 ? 54.00300 40.31700 23.55100 1.000 41.78145  ? 127 PHE   A N   1 
ATOM   998  C  CA  . PHE   A 1 130 ? 53.94900 41.41800 22.60000 1.000 45.07013  ? 127 PHE   A CA  1 
ATOM   999  C  C   . PHE   A 1 130 ? 54.45900 42.70400 23.24000 1.000 52.70244  ? 127 PHE   A C   1 
ATOM   1000 O  O   . PHE   A 1 130 ? 54.19800 42.97000 24.41400 1.000 44.87453  ? 127 PHE   A O   1 
ATOM   1001 C  CB  . PHE   A 1 130 ? 52.52000 41.62000 22.11100 1.000 37.68620  ? 127 PHE   A CB  1 
ATOM   1002 C  CG  . PHE   A 1 130 ? 52.04200 40.55300 21.17100 1.000 42.56163  ? 127 PHE   A CG  1 
ATOM   1003 C  CD1 . PHE   A 1 130 ? 52.64000 40.38600 19.93300 1.000 43.77592  ? 127 PHE   A CD1 1 
ATOM   1004 C  CD2 . PHE   A 1 130 ? 50.98900 39.72000 21.52000 1.000 40.08084  ? 127 PHE   A CD2 1 
ATOM   1005 C  CE1 . PHE   A 1 130 ? 52.20000 39.40300 19.05600 1.000 41.08350  ? 127 PHE   A CE1 1 
ATOM   1006 C  CE2 . PHE   A 1 130 ? 50.54700 38.73600 20.64800 1.000 46.97404  ? 127 PHE   A CE2 1 
ATOM   1007 C  CZ  . PHE   A 1 130 ? 51.15100 38.59100 19.40300 1.000 39.68519  ? 127 PHE   A CZ  1 
ATOM   1008 N  N   . ASN   A 1 131 ? 55.17600 43.52100 22.45000 1.000 45.43121  ? 128 ASN   A N   1 
ATOM   1009 C  CA  . ASN   A 1 131 ? 55.73900 44.76900 22.96500 1.000 44.85208  ? 128 ASN   A CA  1 
ATOM   1010 C  C   . ASN   A 1 131 ? 54.71400 45.90900 23.02400 1.000 51.29664  ? 128 ASN   A C   1 
ATOM   1011 O  O   . ASN   A 1 131 ? 54.70100 46.64700 24.01500 1.000 47.60861  ? 128 ASN   A O   1 
ATOM   1012 C  CB  . ASN   A 1 131 ? 56.95500 45.17300 22.12600 1.000 49.14556  ? 128 ASN   A CB  1 
ATOM   1013 C  CG  . ASN   A 1 131 ? 58.09800 44.17200 22.25400 1.000 52.88400  ? 128 ASN   A CG  1 
ATOM   1014 O  OD1 . ASN   A 1 131 ? 58.38200 43.68100 23.34500 1.000 57.00013  ? 128 ASN   A OD1 1 
ATOM   1015 N  ND2 . ASN   A 1 131 ? 58.74200 43.85600 21.13800 1.000 50.58737  ? 128 ASN   A ND2 1 
ATOM   1016 N  N   . PRO   A 1 132 ? 53.85400 46.12100 22.02500 1.000 47.76329  ? 129 PRO   A N   1 
ATOM   1017 C  CA  . PRO   A 1 132 ? 52.84000 47.17700 22.17200 1.000 41.24812  ? 129 PRO   A CA  1 
ATOM   1018 C  C   . PRO   A 1 132 ? 51.82100 46.80200 23.23000 1.000 43.26959  ? 129 PRO   A C   1 
ATOM   1019 O  O   . PRO   A 1 132 ? 51.21000 45.72800 23.15400 1.000 45.99475  ? 129 PRO   A O   1 
ATOM   1020 C  CB  . PRO   A 1 132 ? 52.18800 47.25900 20.78000 1.000 37.35365  ? 129 PRO   A CB  1 
ATOM   1021 C  CG  . PRO   A 1 132 ? 53.18300 46.65700 19.84400 1.000 37.68129  ? 129 PRO   A CG  1 
ATOM   1022 C  CD  . PRO   A 1 132 ? 53.86500 45.57600 20.65100 1.000 41.19329  ? 129 PRO   A CD  1 
ATOM   1023 N  N   . PRO   A 1 133 ? 51.59700 47.66500 24.22600 1.000 40.14587  ? 130 PRO   A N   1 
ATOM   1024 C  CA  . PRO   A 1 133 ? 50.51400 47.40300 25.19300 1.000 43.20856  ? 130 PRO   A CA  1 
ATOM   1025 C  C   . PRO   A 1 133 ? 49.18400 47.10500 24.54100 1.000 47.43830  ? 130 PRO   A C   1 
ATOM   1026 O  O   . PRO   A 1 133 ? 48.41400 46.30200 25.07800 1.000 46.60686  ? 130 PRO   A O   1 
ATOM   1027 C  CB  . PRO   A 1 133 ? 50.45700 48.70300 26.01500 1.000 44.04764  ? 130 PRO   A CB  1 
ATOM   1028 C  CG  . PRO   A 1 133 ? 51.85200 49.19400 25.99500 1.000 42.85139  ? 130 PRO   A CG  1 
ATOM   1029 C  CD  . PRO   A 1 133 ? 52.40300 48.84000 24.61200 1.000 39.20627  ? 130 PRO   A CD  1 
ATOM   1030 N  N   . ALA   A 1 134 ? 48.88900 47.73100 23.39400 1.000 46.20049  ? 131 ALA   A N   1 
ATOM   1031 C  CA  . ALA   A 1 134 ? 47.62600 47.47300 22.72100 1.000 48.37706  ? 131 ALA   A CA  1 
ATOM   1032 C  C   . ALA   A 1 134 ? 47.52400 46.01400 22.29900 1.000 48.34375  ? 131 ALA   A C   1 
ATOM   1033 O  O   . ALA   A 1 134 ? 46.46000 45.40200 22.42500 1.000 39.19308  ? 131 ALA   A O   1 
ATOM   1034 C  CB  . ALA   A 1 134 ? 47.47800 48.39300 21.50700 1.000 47.25750  ? 131 ALA   A CB  1 
ATOM   1035 N  N   . LEU   A 1 135 ? 48.61700 45.45000 21.77400 1.000 36.34661  ? 132 LEU   A N   1 
ATOM   1036 C  CA  . LEU   A 1 135 ? 48.60100 44.05400 21.33700 1.000 47.35801  ? 132 LEU   A CA  1 
ATOM   1037 C  C   . LEU   A 1 135 ? 48.53000 43.09000 22.51700 1.000 47.77420  ? 132 LEU   A C   1 
ATOM   1038 O  O   . LEU   A 1 135 ? 47.78700 42.10300 22.47500 1.000 44.50338  ? 132 LEU   A O   1 
ATOM   1039 C  CB  . LEU   A 1 135 ? 49.84600 43.75500 20.51100 1.000 41.49950  ? 132 LEU   A CB  1 
ATOM   1040 C  CG  . LEU   A 1 135 ? 49.67000 43.66800 19.01200 1.000 41.25062  ? 132 LEU   A CG  1 
ATOM   1041 C  CD1 . LEU   A 1 135 ? 50.94700 43.12300 18.40700 1.000 40.18385  ? 132 LEU   A CD1 1 
ATOM   1042 C  CD2 . LEU   A 1 135 ? 48.44700 42.82400 18.64000 1.000 41.21177  ? 132 LEU   A CD2 1 
ATOM   1043 N  N   . GLN   A 1 136 ? 49.31000 43.35200 23.56900 1.000 41.23294  ? 133 GLN   A N   1 
ATOM   1044 C  CA  . GLN   A 1 136 ? 49.30700 42.47800 24.74000 1.000 47.86888  ? 133 GLN   A CA  1 
ATOM   1045 C  C   . GLN   A 1 136 ? 47.93700 42.45500 25.40400 1.000 49.16138  ? 133 GLN   A C   1 
ATOM   1046 O  O   . GLN   A 1 136 ? 47.39800 41.38000 25.69800 1.000 48.90640  ? 133 GLN   A O   1 
ATOM   1047 C  CB  . GLN   A 1 136 ? 50.38300 42.92400 25.73200 1.000 41.53586  ? 133 GLN   A CB  1 
ATOM   1048 C  CG  . GLN   A 1 136 ? 50.81600 41.84800 26.72500 1.000 45.98948  ? 133 GLN   A CG  1 
ATOM   1049 C  CD  . GLN   A 1 136 ? 50.97600 40.46700 26.08500 1.000 60.60266  ? 133 GLN   A CD  1 
ATOM   1050 O  OE1 . GLN   A 1 136 ? 51.80800 40.25600 25.18800 1.000 56.19291  ? 133 GLN   A OE1 1 
ATOM   1051 N  NE2 . GLN   A 1 136 ? 50.17800 39.51800 26.55100 1.000 57.12116  ? 133 GLN   A NE2 1 
ATOM   1052 N  N   . ASP   A 1 137 ? 47.34500 43.63400 25.62400 1.000 39.99294  ? 134 ASP   A N   1 
ATOM   1053 C  CA  . ASP   A 1 137 ? 46.03900 43.69000 26.27400 1.000 45.15954  ? 134 ASP   A CA  1 
ATOM   1054 C  C   . ASP   A 1 137 ? 44.99900 42.93200 25.46600 1.000 51.05375  ? 134 ASP   A C   1 
ATOM   1055 O  O   . ASP   A 1 137 ? 44.18900 42.18000 26.02500 1.000 38.83745  ? 134 ASP   A O   1 
ATOM   1056 C  CB  . ASP   A 1 137 ? 45.58400 45.14200 26.46800 1.000 51.13268  ? 134 ASP   A CB  1 
ATOM   1057 C  CG  . ASP   A 1 137 ? 46.42600 45.91300 27.47800 1.000 49.18997  ? 134 ASP   A CG  1 
ATOM   1058 O  OD1 . ASP   A 1 137 ? 47.28900 45.33000 28.16900 1.000 53.74143  ? 134 ASP   A OD1 1 
ATOM   1059 O  OD2 . ASP   A 1 137 ? 46.22500 47.14300 27.55400 1.000 59.42571  ? 134 ASP   A OD2 1 
ATOM   1060 N  N   . ALA   A 1 138 ? 45.00800 43.12400 24.14000 1.000 40.93200  ? 135 ALA   A N   1 
ATOM   1061 C  CA  . ALA   A 1 138 ? 44.01600 42.48300 23.28900 1.000 39.27438  ? 135 ALA   A CA  1 
ATOM   1062 C  C   . ALA   A 1 138 ? 44.24000 40.97900 23.24100 1.000 36.82000  ? 135 ALA   A C   1 
ATOM   1063 O  O   . ALA   A 1 138 ? 43.27900 40.20900 23.15800 1.000 39.77155  ? 135 ALA   A O   1 
ATOM   1064 C  CB  . ALA   A 1 138 ? 44.07200 43.08900 21.87200 1.000 35.81334  ? 135 ALA   A CB  1 
ATOM   1065 N  N   . TYR   A 1 139 ? 45.51200 40.56600 23.23400 1.000 35.43035  ? 136 TYR   A N   1 
ATOM   1066 C  CA  . TYR   A 1 139 ? 45.90100 39.15800 23.30100 1.000 43.32900  ? 136 TYR   A CA  1 
ATOM   1067 C  C   . TYR   A 1 139 ? 45.26200 38.47500 24.51000 1.000 50.98411  ? 136 TYR   A C   1 
ATOM   1068 O  O   . TYR   A 1 139 ? 44.60400 37.43400 24.38200 1.000 43.29537  ? 136 TYR   A O   1 
ATOM   1069 C  CB  . TYR   A 1 139 ? 47.42300 39.08100 23.40300 1.000 37.61591  ? 136 TYR   A CB  1 
ATOM   1070 C  CG  . TYR   A 1 139 ? 48.11000 37.75000 23.21200 1.000 54.72742  ? 136 TYR   A CG  1 
ATOM   1071 C  CD1 . TYR   A 1 139 ? 47.45500 36.62900 22.68000 1.000 48.03836  ? 136 TYR   A CD1 1 
ATOM   1072 C  CD2 . TYR   A 1 139 ? 49.43100 37.59800 23.64400 1.000 63.47512  ? 136 TYR   A CD2 1 
ATOM   1073 C  CE1 . TYR   A 1 139 ? 48.14000 35.41700 22.52600 1.000 47.31865  ? 136 TYR   A CE1 1 
ATOM   1074 C  CE2 . TYR   A 1 139 ? 50.11300 36.40700 23.50700 1.000 55.78232  ? 136 TYR   A CE2 1 
ATOM   1075 C  CZ  . TYR   A 1 139 ? 49.48200 35.32400 22.95400 1.000 63.61182  ? 136 TYR   A CZ  1 
ATOM   1076 O  OH  . TYR   A 1 139 ? 50.25100 34.18200 22.85800 1.000 55.07078  ? 136 TYR   A OH  1 
ATOM   1077 N  N   . TYR   A 1 140 ? 45.44400 39.07100 25.69500 1.000 41.20402  ? 137 TYR   A N   1 
ATOM   1078 C  CA  . TYR   A 1 140 ? 44.84100 38.53100 26.91400 1.000 42.68255  ? 137 TYR   A CA  1 
ATOM   1079 C  C   . TYR   A 1 140 ? 43.33100 38.41500 26.77900 1.000 49.06895  ? 137 TYR   A C   1 
ATOM   1080 O  O   . TYR   A 1 140 ? 42.75200 37.36300 27.07100 1.000 43.49454  ? 137 TYR   A O   1 
ATOM   1081 C  CB  . TYR   A 1 140 ? 45.17900 39.41000 28.11500 1.000 37.44546  ? 137 TYR   A CB  1 
ATOM   1082 C  CG  . TYR   A 1 140 ? 46.55600 39.21000 28.66600 1.000 36.18103  ? 137 TYR   A CG  1 
ATOM   1083 C  CD1 . TYR   A 1 140 ? 47.04500 37.94100 28.93600 1.000 41.72415  ? 137 TYR   A CD1 1 
ATOM   1084 C  CD2 . TYR   A 1 140 ? 47.36700 40.29400 28.94900 1.000 40.31400  ? 137 TYR   A CD2 1 
ATOM   1085 C  CE1 . TYR   A 1 140 ? 48.31900 37.75700 29.46900 1.000 38.28166  ? 137 TYR   A CE1 1 
ATOM   1086 C  CE2 . TYR   A 1 140 ? 48.64100 40.12100 29.48700 1.000 45.29656  ? 137 TYR   A CE2 1 
ATOM   1087 C  CZ  . TYR   A 1 140 ? 49.10900 38.85400 29.74800 1.000 47.64894  ? 137 TYR   A CZ  1 
ATOM   1088 O  OH  . TYR   A 1 140 ? 50.37700 38.69600 30.27500 1.000 47.86303  ? 137 TYR   A OH  1 
ATOM   1089 N  N   . ARG   A 1 141 ? 42.66700 39.50100 26.36800 1.000 44.83237  ? 138 ARG   A N   1 
ATOM   1090 C  CA  A ARG   A 1 141 ? 41.22100 39.44600 26.17600 0.520 45.63649  ? 138 ARG   A CA  1 
ATOM   1091 C  CA  B ARG   A 1 141 ? 41.22400 39.42400 26.20200 0.480 45.62277  ? 138 ARG   A CA  1 
ATOM   1092 C  C   . ARG   A 1 141 ? 40.84500 38.38900 25.14700 1.000 45.26414  ? 138 ARG   A C   1 
ATOM   1093 O  O   . ARG   A 1 141 ? 39.79200 37.74800 25.25800 1.000 48.98059  ? 138 ARG   A O   1 
ATOM   1094 C  CB  A ARG   A 1 141 ? 40.67700 40.81300 25.74100 0.520 45.35410  ? 138 ARG   A CB  1 
ATOM   1095 C  CB  B ARG   A 1 141 ? 40.65900 40.80800 25.86900 0.480 45.45445  ? 138 ARG   A CB  1 
ATOM   1096 C  CG  A ARG   A 1 141 ? 40.62200 41.88000 26.83400 0.520 51.52990  ? 138 ARG   A CG  1 
ATOM   1097 C  CG  B ARG   A 1 141 ? 40.78200 41.78400 27.04300 0.480 51.68733  ? 138 ARG   A CG  1 
ATOM   1098 C  CD  A ARG   A 1 141 ? 40.03600 41.35800 28.14700 0.520 58.05246  ? 138 ARG   A CD  1 
ATOM   1099 C  CD  B ARG   A 1 141 ? 40.04900 43.10100 26.82300 0.480 51.08852  ? 138 ARG   A CD  1 
ATOM   1100 N  NE  A ARG   A 1 141 ? 38.69300 40.80200 28.01100 0.520 57.23550  ? 138 ARG   A NE  1 
ATOM   1101 N  NE  B ARG   A 1 141 ? 40.96800 44.23500 26.87700 0.480 64.20961  ? 138 ARG   A NE  1 
ATOM   1102 C  CZ  A ARG   A 1 141 ? 38.17000 39.88500 28.82000 0.520 54.17962  ? 138 ARG   A CZ  1 
ATOM   1103 C  CZ  B ARG   A 1 141 ? 40.83000 45.29200 27.66800 0.480 55.40228  ? 138 ARG   A CZ  1 
ATOM   1104 N  NH1 A ARG   A 1 141 ? 38.85500 39.38300 29.83900 0.520 39.15314  ? 138 ARG   A NH1 1 
ATOM   1105 N  NH1 B ARG   A 1 141 ? 39.78300 45.43100 28.46600 0.480 48.90011  ? 138 ARG   A NH1 1 
ATOM   1106 N  NH2 A ARG   A 1 141 ? 36.93000 39.45800 28.59800 0.520 55.65421  ? 138 ARG   A NH2 1 
ATOM   1107 N  NH2 B ARG   A 1 141 ? 41.76700 46.23200 27.65700 0.480 45.71651  ? 138 ARG   A NH2 1 
ATOM   1108 N  N   . ALA   A 1 142 ? 41.69600 38.18100 24.14400 1.000 41.14128  ? 139 ALA   A N   1 
ATOM   1109 C  CA  . ALA   A 1 142 ? 41.40600 37.15700 23.14400 1.000 44.77314  ? 139 ALA   A CA  1 
ATOM   1110 C  C   . ALA   A 1 142 ? 41.42800 35.75500 23.74900 1.000 41.83705  ? 139 ALA   A C   1 
ATOM   1111 O  O   . ALA   A 1 142 ? 40.54300 34.94100 23.46600 1.000 44.62880  ? 139 ALA   A O   1 
ATOM   1112 C  CB  . ALA   A 1 142 ? 42.40100 37.24300 21.99600 1.000 36.41178  ? 139 ALA   A CB  1 
ATOM   1113 N  N   . ARG   A 1 143 ? 42.44800 35.45600 24.56200 1.000 48.47672  ? 140 ARG   A N   1 
ATOM   1114 C  CA  . ARG   A 1 143 ? 42.53500 34.16700 25.24400 1.000 56.97950  ? 140 ARG   A CA  1 
ATOM   1115 C  C   . ARG   A 1 143 ? 41.31300 33.90400 26.10600 1.000 53.54653  ? 140 ARG   A C   1 
ATOM   1116 O  O   . ARG   A 1 143 ? 40.93700 32.74300 26.31100 1.000 54.40136  ? 140 ARG   A O   1 
ATOM   1117 C  CB  . ARG   A 1 143 ? 43.80300 34.10500 26.09600 1.000 48.27539  ? 140 ARG   A CB  1 
ATOM   1118 C  CG  . ARG   A 1 143 ? 45.08100 34.04200 25.25300 1.000 69.45703  ? 140 ARG   A CG  1 
ATOM   1119 C  CD  . ARG   A 1 143 ? 46.34200 34.43400 26.02800 1.000 80.00954  ? 140 ARG   A CD  1 
ATOM   1120 N  NE  . ARG   A 1 143 ? 47.51900 33.67300 25.61000 1.000 90.34434  ? 140 ARG   A NE  1 
ATOM   1121 C  CZ  . ARG   A 1 143 ? 47.72100 32.38000 25.84500 1.000 85.02133  ? 140 ARG   A CZ  1 
ATOM   1122 N  NH1 . ARG   A 1 143 ? 46.84500 31.64900 26.52000 1.000 76.70117  ? 140 ARG   A NH1 1 
ATOM   1123 N  NH2 . ARG   A 1 143 ? 48.83500 31.80800 25.39600 1.000 84.45525  ? 140 ARG   A NH2 1 
ATOM   1124 N  N   . ALA   A 1 144 ? 40.67500 34.96100 26.60600 1.000 45.50319  ? 141 ALA   A N   1 
ATOM   1125 C  CA  . ALA   A 1 144 ? 39.46400 34.84700 27.40100 1.000 40.73396  ? 141 ALA   A CA  1 
ATOM   1126 C  C   . ALA   A 1 144 ? 38.20000 34.93600 26.55700 1.000 46.53938  ? 141 ALA   A C   1 
ATOM   1127 O  O   . ALA   A 1 144 ? 37.12400 35.19500 27.10400 1.000 64.06861  ? 141 ALA   A O   1 
ATOM   1128 C  CB  . ALA   A 1 144 ? 39.45000 35.92600 28.49200 1.000 37.88193  ? 141 ALA   A CB  1 
ATOM   1129 N  N   . GLY   A 1 145 ? 38.30100 34.76200 25.23900 1.000 54.61615  ? 142 GLY   A N   1 
ATOM   1130 C  CA  . GLY   A 1 145 ? 37.12600 34.62100 24.40000 1.000 49.27772  ? 142 GLY   A CA  1 
ATOM   1131 C  C   . GLY   A 1 145 ? 36.68000 35.86400 23.64900 1.000 59.17462  ? 142 GLY   A C   1 
ATOM   1132 O  O   . GLY   A 1 145 ? 35.83100 35.74400 22.75700 1.000 56.74125  ? 142 GLY   A O   1 
ATOM   1133 N  N   . GLU   A 1 146 ? 37.21300 37.04400 23.96800 1.000 55.44353  ? 143 GLU   A N   1 
ATOM   1134 C  CA  . GLU   A 1 146 ? 36.80300 38.30200 23.33600 1.000 57.54797  ? 143 GLU   A CA  1 
ATOM   1135 C  C   . GLU   A 1 146 ? 37.92900 38.76300 22.41000 1.000 47.21824  ? 143 GLU   A C   1 
ATOM   1136 O  O   . GLU   A 1 146 ? 38.79400 39.55300 22.79600 1.000 46.71878  ? 143 GLU   A O   1 
ATOM   1137 C  CB  . GLU   A 1 146 ? 36.47100 39.35000 24.38600 1.000 47.14949  ? 143 GLU   A CB  1 
ATOM   1138 C  CG  . GLU   A 1 146 ? 35.05800 39.21700 24.93700 1.000 71.69676  ? 143 GLU   A CG  1 
ATOM   1139 C  CD  . GLU   A 1 146 ? 34.70100 40.32500 25.92200 1.000 106.82068 ? 143 GLU   A CD  1 
ATOM   1140 O  OE1 . GLU   A 1 146 ? 35.58600 41.14900 26.25300 1.000 97.87116  ? 143 GLU   A OE1 1 
ATOM   1141 O  OE2 . GLU   A 1 146 ? 33.53400 40.36300 26.37700 1.000 110.40755 ? 143 GLU   A OE2 1 
ATOM   1142 N  N   . ALA   A 1 147 ? 37.89800 38.28000 21.17200 1.000 45.88788  ? 144 ALA   A N   1 
ATOM   1143 C  CA  . ALA   A 1 147 ? 39.03600 38.40600 20.27500 1.000 41.94699  ? 144 ALA   A CA  1 
ATOM   1144 C  C   . ALA   A 1 147 ? 38.83100 39.41200 19.14100 1.000 43.43876  ? 144 ALA   A C   1 
ATOM   1145 O  O   . ALA   A 1 147 ? 39.75600 39.60300 18.33700 1.000 45.19954  ? 144 ALA   A O   1 
ATOM   1146 C  CB  . ALA   A 1 147 ? 39.38100 37.02500 19.70600 1.000 42.51608  ? 144 ALA   A CB  1 
ATOM   1147 N  N   . ALA   A 1 148 ? 37.67100 40.08100 19.06800 1.000 41.81337  ? 145 ALA   A N   1 
ATOM   1148 C  CA  . ALA   A 1 148 ? 37.42900 41.05200 17.99300 1.000 42.12080  ? 145 ALA   A CA  1 
ATOM   1149 C  C   . ALA   A 1 148 ? 38.55500 42.08200 17.89800 1.000 43.76319  ? 145 ALA   A C   1 
ATOM   1150 O  O   . ALA   A 1 148 ? 39.10800 42.32200 16.81500 1.000 44.82521  ? 145 ALA   A O   1 
ATOM   1151 C  CB  . ALA   A 1 148 ? 36.08900 41.76200 18.21100 1.000 36.72557  ? 145 ALA   A CB  1 
ATOM   1152 N  N   . ASN   A 1 149 ? 38.90900 42.70200 19.02500 1.000 40.24618  ? 146 ASN   A N   1 
ATOM   1153 C  CA  . ASN   A 1 149 ? 39.92000 43.75500 19.00100 1.000 37.76894  ? 146 ASN   A CA  1 
ATOM   1154 C  C   . ASN   A 1 149 ? 41.28900 43.20600 18.63100 1.000 46.03671  ? 146 ASN   A C   1 
ATOM   1155 O  O   . ASN   A 1 149 ? 42.04500 43.84200 17.88400 1.000 43.94438  ? 146 ASN   A O   1 
ATOM   1156 C  CB  . ASN   A 1 149 ? 39.96700 44.44600 20.36500 1.000 47.74108  ? 146 ASN   A CB  1 
ATOM   1157 C  CG  . ASN   A 1 149 ? 39.29900 45.78000 20.34600 1.000 61.62937  ? 146 ASN   A CG  1 
ATOM   1158 O  OD1 . ASN   A 1 149 ? 39.74300 46.70500 19.66100 1.000 67.15404  ? 146 ASN   A OD1 1 
ATOM   1159 N  ND2 . ASN   A 1 149 ? 38.16600 45.87500 21.03400 1.000 68.51849  ? 146 ASN   A ND2 1 
ATOM   1160 N  N   . PHE   A 1 150 ? 41.63000 42.02700 19.14700 1.000 41.57356  ? 147 PHE   A N   1 
ATOM   1161 C  CA  . PHE   A 1 150 ? 42.90800 41.42500 18.79600 1.000 41.69865  ? 147 PHE   A CA  1 
ATOM   1162 C  C   . PHE   A 1 150 ? 43.00400 41.20500 17.29400 1.000 41.37879  ? 147 PHE   A C   1 
ATOM   1163 O  O   . PHE   A 1 150 ? 44.01100 41.56300 16.67100 1.000 42.51652  ? 147 PHE   A O   1 
ATOM   1164 C  CB  . PHE   A 1 150 ? 43.09500 40.10900 19.56800 1.000 38.65479  ? 147 PHE   A CB  1 
ATOM   1165 C  CG  . PHE   A 1 150 ? 44.46400 39.53300 19.46500 1.000 36.05729  ? 147 PHE   A CG  1 
ATOM   1166 C  CD1 . PHE   A 1 150 ? 45.58300 40.31000 19.75300 1.000 36.25630  ? 147 PHE   A CD1 1 
ATOM   1167 C  CD2 . PHE   A 1 150 ? 44.64200 38.21000 19.09200 1.000 42.35957  ? 147 PHE   A CD2 1 
ATOM   1168 C  CE1 . PHE   A 1 150 ? 46.85400 39.77300 19.66700 1.000 33.12325  ? 147 PHE   A CE1 1 
ATOM   1169 C  CE2 . PHE   A 1 150 ? 45.90900 37.66100 19.00400 1.000 38.04506  ? 147 PHE   A CE2 1 
ATOM   1170 C  CZ  . PHE   A 1 150 ? 47.01800 38.44400 19.28500 1.000 40.75690  ? 147 PHE   A CZ  1 
ATOM   1171 N  N   . CYS   A 1 151 ? 41.95000 40.64600 16.68700 1.000 40.52611  ? 148 CYS   A N   1 
ATOM   1172 C  CA  . CYS   A 1 151 ? 41.98000 40.36600 15.25000 1.000 39.84927  ? 148 CYS   A CA  1 
ATOM   1173 C  C   . CYS   A 1 151 ? 42.06700 41.64800 14.42600 1.000 40.27152  ? 148 CYS   A C   1 
ATOM   1174 O  O   . CYS   A 1 151 ? 42.79200 41.69800 13.42000 1.000 38.85371  ? 148 CYS   A O   1 
ATOM   1175 C  CB  . CYS   A 1 151 ? 40.74800 39.55700 14.84400 1.000 44.75046  ? 148 CYS   A CB  1 
ATOM   1176 S  SG  . CYS   A 1 151 ? 40.68400 37.89000 15.56900 1.000 42.35146  ? 148 CYS   A SG  1 
ATOM   1177 N  N   . ALA   A 1 152 ? 41.33500 42.68700 14.82800 1.000 34.79424  ? 149 ALA   A N   1 
ATOM   1178 C  CA  . ALA   A 1 152 ? 41.45300 43.97300 14.14700 1.000 40.97063  ? 149 ALA   A CA  1 
ATOM   1179 C  C   . ALA   A 1 152 ? 42.88400 44.47800 14.21000 1.000 46.58997  ? 149 ALA   A C   1 
ATOM   1180 O  O   . ALA   A 1 152 ? 43.44500 44.92700 13.20000 1.000 42.40398  ? 149 ALA   A O   1 
ATOM   1181 C  CB  . ALA   A 1 152 ? 40.50000 44.99800 14.77700 1.000 41.09641  ? 149 ALA   A CB  1 
ATOM   1182 N  N   . LEU   A 1 153 ? 43.49900 44.37600 15.39200 1.000 41.12483  ? 150 LEU   A N   1 
ATOM   1183 C  CA  . LEU   A 1 153 ? 44.87400 44.81800 15.57000 1.000 45.25008  ? 150 LEU   A CA  1 
ATOM   1184 C  C   . LEU   A 1 153 ? 45.82800 44.00800 14.70900 1.000 43.83483  ? 150 LEU   A C   1 
ATOM   1185 O  O   . LEU   A 1 153 ? 46.77700 44.55700 14.13700 1.000 45.77069  ? 150 LEU   A O   1 
ATOM   1186 C  CB  . LEU   A 1 153 ? 45.26700 44.72900 17.05300 1.000 36.64308  ? 150 LEU   A CB  1 
ATOM   1187 C  CG  . LEU   A 1 153 ? 44.77000 45.87700 17.94600 1.000 45.37996  ? 150 LEU   A CG  1 
ATOM   1188 C  CD1 . LEU   A 1 153 ? 45.15200 45.66800 19.41200 1.000 39.79621  ? 150 LEU   A CD1 1 
ATOM   1189 C  CD2 . LEU   A 1 153 ? 45.31600 47.21500 17.45900 1.000 37.04895  ? 150 LEU   A CD2 1 
ATOM   1190 N  N   . ILE   A 1 154 ? 45.59800 42.69700 14.59900 1.000 45.88309  ? 151 ILE   A N   1 
ATOM   1191 C  CA  . ILE   A 1 154 ? 46.46400 41.89300 13.74300 1.000 49.95670  ? 151 ILE   A CA  1 
ATOM   1192 C  C   . ILE   A 1 154 ? 46.41100 42.41100 12.30900 1.000 41.74117  ? 151 ILE   A C   1 
ATOM   1193 O  O   . ILE   A 1 154 ? 47.44900 42.59100 11.65800 1.000 41.42832  ? 151 ILE   A O   1 
ATOM   1194 C  CB  . ILE   A 1 154 ? 46.09200 40.39900 13.83200 1.000 44.43592  ? 151 ILE   A CB  1 
ATOM   1195 C  CG1 . ILE   A 1 154 ? 46.45300 39.86700 15.23300 1.000 45.96022  ? 151 ILE   A CG1 1 
ATOM   1196 C  CG2 . ILE   A 1 154 ? 46.82100 39.61300 12.71600 1.000 37.28811  ? 151 ILE   A CG2 1 
ATOM   1197 C  CD1 . ILE   A 1 154 ? 45.92400 38.49100 15.56600 1.000 37.32705  ? 151 ILE   A CD1 1 
ATOM   1198 N  N   . LEU   A 1 155 ? 45.20600 42.68900 11.80900 1.000 40.64420  ? 152 LEU   A N   1 
ATOM   1199 C  CA  . LEU   A 1 155 ? 45.07200 43.19300 10.44600 1.000 45.43905  ? 152 LEU   A CA  1 
ATOM   1200 C  C   . LEU   A 1 155 ? 45.83900 44.50500 10.27300 1.000 43.65255  ? 152 LEU   A C   1 
ATOM   1201 O  O   . LEU   A 1 155 ? 46.68600 44.62700 9.37600  1.000 42.61766  ? 152 LEU   A O   1 
ATOM   1202 C  CB  . LEU   A 1 155 ? 43.59100 43.34400 10.10100 1.000 41.40871  ? 152 LEU   A CB  1 
ATOM   1203 C  CG  . LEU   A 1 155 ? 42.87800 42.00900 9.82700  1.000 45.82527  ? 152 LEU   A CG  1 
ATOM   1204 C  CD1 . LEU   A 1 155 ? 41.38200 42.05500 10.13500 1.000 32.09130  ? 152 LEU   A CD1 1 
ATOM   1205 C  CD2 . LEU   A 1 155 ? 43.09200 41.55800 8.38400  1.000 39.35432  ? 152 LEU   A CD2 1 
ATOM   1206 N  N   . ALA   A 1 156 ? 45.62100 45.45900 11.18600 1.000 45.23149  ? 153 ALA   A N   1 
ATOM   1207 C  CA  . ALA   A 1 156 ? 46.28100 46.75900 11.09000 1.000 48.09745  ? 153 ALA   A CA  1 
ATOM   1208 C  C   . ALA   A 1 156 ? 47.79600 46.62800 11.18300 1.000 45.76792  ? 153 ALA   A C   1 
ATOM   1209 O  O   . ALA   A 1 156 ? 48.52900 47.26300 10.41600 1.000 45.72085  ? 153 ALA   A O   1 
ATOM   1210 C  CB  . ALA   A 1 156 ? 45.74900 47.69800 12.17800 1.000 43.31779  ? 153 ALA   A CB  1 
ATOM   1211 N  N   . TYR   A 1 157 ? 48.29000 45.80800 12.11200 1.000 39.93656  ? 154 TYR   A N   1 
ATOM   1212 C  CA  . TYR   A 1 157 ? 49.73700 45.65200 12.23300 1.000 46.03920  ? 154 TYR   A CA  1 
ATOM   1213 C  C   . TYR   A 1 157 ? 50.33700 44.94300 11.02100 1.000 47.13936  ? 154 TYR   A C   1 
ATOM   1214 O  O   . TYR   A 1 157 ? 51.50100 45.18200 10.67700 1.000 48.22503  ? 154 TYR   A O   1 
ATOM   1215 C  CB  . TYR   A 1 157 ? 50.08900 44.90100 13.52300 1.000 44.10429  ? 154 TYR   A CB  1 
ATOM   1216 C  CG  . TYR   A 1 157 ? 50.15200 45.79500 14.74400 1.000 47.73626  ? 154 TYR   A CG  1 
ATOM   1217 C  CD1 . TYR   A 1 157 ? 51.21200 46.67900 14.94100 1.000 38.31909  ? 154 TYR   A CD1 1 
ATOM   1218 C  CD2 . TYR   A 1 157 ? 49.13900 45.76000 15.69600 1.000 40.00945  ? 154 TYR   A CD2 1 
ATOM   1219 C  CE1 . TYR   A 1 157 ? 51.25400 47.51200 16.08100 1.000 42.49521  ? 154 TYR   A CE1 1 
ATOM   1220 C  CE2 . TYR   A 1 157 ? 49.16900 46.58100 16.81800 1.000 44.26561  ? 154 TYR   A CE2 1 
ATOM   1221 C  CZ  . TYR   A 1 157 ? 50.22000 47.44500 17.00400 1.000 38.89985  ? 154 TYR   A CZ  1 
ATOM   1222 O  OH  . TYR   A 1 157 ? 50.19900 48.22700 18.11500 1.000 40.11343  ? 154 TYR   A OH  1 
ATOM   1223 N  N   . CYS   A 1 158 ? 49.57800 44.06400 10.37100 1.000 44.89953  ? 155 CYS   A N   1 
ATOM   1224 C  CA  . CYS   A 1 158 ? 50.06000 43.38400 9.17300  1.000 50.80293  ? 155 CYS   A CA  1 
ATOM   1225 C  C   . CYS   A 1 158 ? 49.77100 44.16000 7.89000  1.000 47.85207  ? 155 CYS   A C   1 
ATOM   1226 O  O   . CYS   A 1 158 ? 50.10200 43.67100 6.80200  1.000 46.31487  ? 155 CYS   A O   1 
ATOM   1227 C  CB  . CYS   A 1 158 ? 49.44100 41.98700 9.07400  1.000 36.37987  ? 155 CYS   A CB  1 
ATOM   1228 S  SG  . CYS   A 1 158 ? 49.97500 40.85900 10.35700 1.000 46.50758  ? 155 CYS   A SG  1 
ATOM   1229 N  N   . ASN   A 1 159 ? 49.16100 45.34500 7.99500  1.000 46.21711  ? 156 ASN   A N   1 
ATOM   1230 C  CA  . ASN   A 1 159 ? 48.74700 46.14100 6.84300  1.000 49.41362  ? 156 ASN   A CA  1 
ATOM   1231 C  C   . ASN   A 1 159 ? 47.90300 45.30300 5.88000  1.000 51.27855  ? 156 ASN   A C   1 
ATOM   1232 O  O   . ASN   A 1 159 ? 48.13400 45.25700 4.66900  1.000 56.07035  ? 156 ASN   A O   1 
ATOM   1233 C  CB  . ASN   A 1 159 ? 49.95600 46.75900 6.13400  1.000 54.28851  ? 156 ASN   A CB  1 
ATOM   1234 C  CG  . ASN   A 1 159 ? 49.55900 47.89100 5.17100  1.000 85.55168  ? 156 ASN   A CG  1 
ATOM   1235 O  OD1 . ASN   A 1 159 ? 48.42000 48.37100 5.18000  1.000 67.62219  ? 156 ASN   A OD1 1 
ATOM   1236 N  ND2 . ASN   A 1 159 ? 50.49500 48.28700 4.30600  1.000 96.76533  ? 156 ASN   A ND2 1 
ATOM   1237 N  N   . LYS   A 1 160 ? 46.92000 44.62000 6.44000  1.000 46.90224  ? 157 LYS   A N   1 
ATOM   1238 C  CA  . LYS   A 1 160 ? 45.99600 43.80500 5.67700  1.000 45.67045  ? 157 LYS   A CA  1 
ATOM   1239 C  C   . LYS   A 1 160 ? 44.59600 44.31100 5.96100  1.000 43.09558  ? 157 LYS   A C   1 
ATOM   1240 O  O   . LYS   A 1 160 ? 44.33900 44.89000 7.01800  1.000 49.41556  ? 157 LYS   A O   1 
ATOM   1241 C  CB  . LYS   A 1 160 ? 46.12800 42.31200 6.04000  1.000 40.91211  ? 157 LYS   A CB  1 
ATOM   1242 C  CG  . LYS   A 1 160 ? 47.49700 41.70500 5.68500  1.000 56.46116  ? 157 LYS   A CG  1 
ATOM   1243 C  CD  . LYS   A 1 160 ? 47.45100 40.98700 4.32700  1.000 57.45505  ? 157 LYS   A CD  1 
ATOM   1244 C  CE  . LYS   A 1 160 ? 48.83200 40.87800 3.66700  1.000 75.65596  ? 157 LYS   A CE  1 
ATOM   1245 N  NZ  . LYS   A 1 160 ? 48.83500 40.00100 2.42200  1.000 81.40846  ? 157 LYS   A NZ  1 
ATOM   1246 N  N   . THR   A 1 161 ? 43.69200 44.12000 5.01100  1.000 44.92125  ? 158 THR   A N   1 
ATOM   1247 C  CA  . THR   A 1 161 ? 42.31900 44.55300 5.19500  1.000 43.13457  ? 158 THR   A CA  1 
ATOM   1248 C  C   . THR   A 1 161 ? 41.41700 43.33600 5.26000  1.000 38.83594  ? 158 THR   A C   1 
ATOM   1249 O  O   . THR   A 1 161 ? 41.75200 42.26600 4.74700  1.000 42.52734  ? 158 THR   A O   1 
ATOM   1250 C  CB  . THR   A 1 161 ? 41.86700 45.48900 4.05600  1.000 54.13553  ? 158 THR   A CB  1 
ATOM   1251 O  OG1 . THR   A 1 161 ? 42.08500 44.84900 2.79600  1.000 50.52049  ? 158 THR   A OG1 1 
ATOM   1252 C  CG2 . THR   A 1 161 ? 42.65600 46.80400 4.09100  1.000 43.92396  ? 158 THR   A CG2 1 
ATOM   1253 N  N   . VAL   A 1 162 ? 40.26800 43.51400 5.91500  1.000 39.06987  ? 159 VAL   A N   1 
ATOM   1254 C  CA  . VAL   A 1 162 ? 39.25900 42.46800 5.95000  1.000 36.98103  ? 159 VAL   A CA  1 
ATOM   1255 C  C   . VAL   A 1 162 ? 38.92800 42.05900 4.51800  1.000 43.34509  ? 159 VAL   A C   1 
ATOM   1256 O  O   . VAL   A 1 162 ? 38.74100 42.91000 3.63900  1.000 40.23103  ? 159 VAL   A O   1 
ATOM   1257 C  CB  . VAL   A 1 162 ? 38.01900 42.95900 6.71800  1.000 39.60098  ? 159 VAL   A CB  1 
ATOM   1258 C  CG1 . VAL   A 1 162 ? 36.88600 41.96900 6.59600  1.000 42.49963  ? 159 VAL   A CG1 1 
ATOM   1259 C  CG2 . VAL   A 1 162 ? 38.34900 43.18100 8.21400  1.000 42.27002  ? 159 VAL   A CG2 1 
ATOM   1260 N  N   . GLY   A 1 163 ? 38.86800 40.75100 4.27600  1.000 40.52832  ? 160 GLY   A N   1 
ATOM   1261 C  CA  . GLY   A 1 163 ? 38.62700 40.18000 2.97700  1.000 41.32183  ? 160 GLY   A CA  1 
ATOM   1262 C  C   . GLY   A 1 163 ? 39.88600 39.81400 2.21300  1.000 35.86470  ? 160 GLY   A C   1 
ATOM   1263 O  O   . GLY   A 1 163 ? 39.86200 38.87700 1.41100  1.000 43.97588  ? 160 GLY   A O   1 
ATOM   1264 N  N   . GLU   A 1 164 ? 40.97500 40.54200 2.42900  1.000 40.61294  ? 161 GLU   A N   1 
ATOM   1265 C  CA  . GLU   A 1 164 ? 42.23200 40.22100 1.76900  1.000 43.27374  ? 161 GLU   A CA  1 
ATOM   1266 C  C   . GLU   A 1 164 ? 42.69500 38.79900 2.13000  1.000 59.20290  ? 161 GLU   A C   1 
ATOM   1267 O  O   . GLU   A 1 164 ? 42.45900 38.29700 3.23800  1.000 47.30504  ? 161 GLU   A O   1 
ATOM   1268 C  CB  . GLU   A 1 164 ? 43.29100 41.25200 2.16400  1.000 41.86672  ? 161 GLU   A CB  1 
ATOM   1269 C  CG  . GLU   A 1 164 ? 44.52900 41.29000 1.30400  1.000 60.77380  ? 161 GLU   A CG  1 
ATOM   1270 C  CD  . GLU   A 1 164 ? 45.47000 42.41900 1.70200  1.000 73.37115  ? 161 GLU   A CD  1 
ATOM   1271 O  OE1 . GLU   A 1 164 ? 44.99600 43.39000 2.33100  1.000 65.10533  ? 161 GLU   A OE1 1 
ATOM   1272 O  OE2 . GLU   A 1 164 ? 46.68000 42.34300 1.37600  1.000 75.52641  ? 161 GLU   A OE2 1 
ATOM   1273 N  N   . LEU   A 1 165 ? 43.37400 38.16300 1.17300  1.000 46.78236  ? 162 LEU   A N   1 
ATOM   1274 C  CA  . LEU   A 1 165 ? 43.85200 36.78800 1.28800  1.000 55.72990  ? 162 LEU   A CA  1 
ATOM   1275 C  C   . LEU   A 1 165 ? 45.17700 36.76400 2.04800  1.000 44.13838  ? 162 LEU   A C   1 
ATOM   1276 O  O   . LEU   A 1 165 ? 46.15200 37.38900 1.61800  1.000 46.25958  ? 162 LEU   A O   1 
ATOM   1277 C  CB  . LEU   A 1 165 ? 44.02200 36.18400 -0.11400 1.000 52.79943  ? 162 LEU   A CB  1 
ATOM   1278 C  CG  . LEU   A 1 165 ? 42.76800 36.13000 -0.99300 1.000 54.85958  ? 162 LEU   A CG  1 
ATOM   1279 C  CD1 . LEU   A 1 165 ? 43.07300 35.53100 -2.37400 1.000 61.93227  ? 162 LEU   A CD1 1 
ATOM   1280 C  CD2 . LEU   A 1 165 ? 41.64700 35.34400 -0.28000 1.000 48.62165  ? 162 LEU   A CD2 1 
ATOM   1281 N  N   . GLY   A 1 166 ? 45.21900 36.07000 3.17700  1.000 45.47978  ? 163 GLY   A N   1 
ATOM   1282 C  CA  . GLY   A 1 166 ? 46.36700 36.12700 4.07700  1.000 41.54911  ? 163 GLY   A CA  1 
ATOM   1283 C  C   . GLY   A 1 166 ? 47.12400 34.81500 4.18100  1.000 41.19779  ? 163 GLY   A C   1 
ATOM   1284 O  O   . GLY   A 1 166 ? 46.52500 33.73900 4.17700  1.000 39.38508  ? 163 GLY   A O   1 
ATOM   1285 N  N   . ASP   A 1 167 ? 48.44600 34.91700 4.30200  1.000 37.29422  ? 164 ASP   A N   1 
ATOM   1286 C  CA  . ASP   A 1 167 ? 49.32800 33.78000 4.55200  1.000 38.26763  ? 164 ASP   A CA  1 
ATOM   1287 C  C   . ASP   A 1 167 ? 49.66000 33.69800 6.05200  1.000 39.43055  ? 164 ASP   A C   1 
ATOM   1288 O  O   . ASP   A 1 167 ? 50.14500 34.67600 6.63100  1.000 35.22931  ? 164 ASP   A O   1 
ATOM   1289 C  CB  . ASP   A 1 167 ? 50.60600 33.94200 3.72000  1.000 36.53052  ? 164 ASP   A CB  1 
ATOM   1290 C  CG  . ASP   A 1 167 ? 51.65300 32.85500 3.99300  1.000 44.20217  ? 164 ASP   A CG  1 
ATOM   1291 O  OD1 . ASP   A 1 167 ? 52.25100 32.82800 5.08800  1.000 53.31476  ? 164 ASP   A OD1 1 
ATOM   1292 O  OD2 . ASP   A 1 167 ? 51.90900 32.04300 3.08900  1.000 45.51156  ? 164 ASP   A OD2 1 
ATOM   1293 N  N   . VAL   A 1 168 ? 49.42200 32.52700 6.67100  1.000 38.76308  ? 165 VAL   A N   1 
ATOM   1294 C  CA  . VAL   A 1 168 ? 49.60900 32.38800 8.12700  1.000 36.94725  ? 165 VAL   A CA  1 
ATOM   1295 C  C   . VAL   A 1 168 ? 51.07000 32.60900 8.51900  1.000 40.28327  ? 165 VAL   A C   1 
ATOM   1296 O  O   . VAL   A 1 168 ? 51.37400 33.35200 9.46200  1.000 41.61352  ? 165 VAL   A O   1 
ATOM   1297 C  CB  . VAL   A 1 168 ? 49.09400 31.01900 8.62200  1.000 38.94112  ? 165 VAL   A CB  1 
ATOM   1298 C  CG1 . VAL   A 1 168 ? 49.59100 30.73400 10.05200 1.000 35.03499  ? 165 VAL   A CG1 1 
ATOM   1299 C  CG2 . VAL   A 1 168 ? 47.58200 30.96400 8.58800  1.000 35.83523  ? 165 VAL   A CG2 1 
ATOM   1300 N  N   . ARG   A 1 169 ? 51.99700 31.95500 7.81800  1.000 44.64841  ? 166 ARG   A N   1 
ATOM   1301 C  CA  . ARG   A 1 169 ? 53.41200 32.14300 8.12700  1.000 34.96779  ? 166 ARG   A CA  1 
ATOM   1302 C  C   . ARG   A 1 169 ? 53.81500 33.61500 8.07500  1.000 44.48790  ? 166 ARG   A C   1 
ATOM   1303 O  O   . ARG   A 1 169 ? 54.56600 34.09400 8.93900  1.000 42.37979  ? 166 ARG   A O   1 
ATOM   1304 C  CB  . ARG   A 1 169 ? 54.26500 31.31900 7.16000  1.000 38.76225  ? 166 ARG   A CB  1 
ATOM   1305 C  CG  . ARG   A 1 169 ? 55.75400 31.52300 7.34400  1.000 37.14613  ? 166 ARG   A CG  1 
ATOM   1306 C  CD  . ARG   A 1 169 ? 56.54700 30.89200 6.22200  1.000 41.23655  ? 166 ARG   A CD  1 
ATOM   1307 N  NE  . ARG   A 1 169 ? 56.32400 31.57400 4.95000  1.000 54.35934  ? 166 ARG   A NE  1 
ATOM   1308 C  CZ  . ARG   A 1 169 ? 57.05800 32.59100 4.52800  1.000 52.78151  ? 166 ARG   A CZ  1 
ATOM   1309 N  NH1 . ARG   A 1 169 ? 58.08700 33.03500 5.23400  1.000 44.65205  ? 166 ARG   A NH1 1 
ATOM   1310 N  NH2 . ARG   A 1 169 ? 56.74700 33.18000 3.37800  1.000 61.61208  ? 166 ARG   A NH2 1 
ATOM   1311 N  N   . GLU   A 1 170 ? 53.32700 34.35500 7.07300  1.000 39.53368  ? 167 GLU   A N   1 
ATOM   1312 C  CA  . GLU   A 1 170 ? 53.67400 35.77400 6.97900  1.000 38.01398  ? 167 GLU   A CA  1 
ATOM   1313 C  C   . GLU   A 1 170 ? 53.04100 36.57100 8.10600  1.000 38.56787  ? 167 GLU   A C   1 
ATOM   1314 O  O   . GLU   A 1 170 ? 53.65400 37.50100 8.64300  1.000 39.19647  ? 167 GLU   A O   1 
ATOM   1315 C  CB  . GLU   A 1 170 ? 53.24800 36.34900 5.61800  1.000 43.62672  ? 167 GLU   A CB  1 
ATOM   1316 C  CG  . GLU   A 1 170 ? 53.99800 35.75800 4.44400  1.000 35.21412  ? 167 GLU   A CG  1 
ATOM   1317 C  CD  . GLU   A 1 170 ? 53.61100 36.35000 3.08000  1.000 49.54628  ? 167 GLU   A CD  1 
ATOM   1318 O  OE1 . GLU   A 1 170 ? 52.75900 37.26800 3.00800  1.000 45.77702  ? 167 GLU   A OE1 1 
ATOM   1319 O  OE2 . GLU   A 1 170 ? 54.16700 35.87200 2.06800  1.000 46.43792  ? 167 GLU   A OE2 1 
ATOM   1320 N  N   . THR   A 1 171 ? 51.81400 36.22100 8.48100  1.000 41.80998  ? 168 THR   A N   1 
ATOM   1321 C  CA  . THR   A 1 171 ? 51.15800 36.90900 9.58300  1.000 43.18867  ? 168 THR   A CA  1 
ATOM   1322 C  C   . THR   A 1 171 ? 51.90200 36.68000 10.89100 1.000 52.12352  ? 168 THR   A C   1 
ATOM   1323 O  O   . THR   A 1 171 ? 52.14600 37.63000 11.65300 1.000 45.23789  ? 168 THR   A O   1 
ATOM   1324 C  CB  . THR   A 1 171 ? 49.72100 36.43400 9.68300  1.000 38.62546  ? 168 THR   A CB  1 
ATOM   1325 O  OG1 . THR   A 1 171 ? 49.12200 36.55900 8.39200  1.000 40.18221  ? 168 THR   A OG1 1 
ATOM   1326 C  CG2 . THR   A 1 171 ? 48.95300 37.25100 10.68900 1.000 33.31716  ? 168 THR   A CG2 1 
ATOM   1327 N  N   . MET   A 1 172 ? 52.29100 35.42400 11.16000 1.000 40.50624  ? 169 MET   A N   1 
ATOM   1328 C  CA  . MET   A 1 172 ? 53.02600 35.13100 12.38800 1.000 40.05053  ? 169 MET   A CA  1 
ATOM   1329 C  C   . MET   A 1 172 ? 54.34200 35.89400 12.41500 1.000 42.94605  ? 169 MET   A C   1 
ATOM   1330 O  O   . MET   A 1 172 ? 54.73400 36.44500 13.45500 1.000 38.27561  ? 169 MET   A O   1 
ATOM   1331 C  CB  . MET   A 1 172 ? 53.26600 33.61700 12.51900 1.000 34.10972  ? 169 MET   A CB  1 
ATOM   1332 C  CG  . MET   A 1 172 ? 51.95700 32.81000 12.52300 1.000 36.43812  ? 169 MET   A CG  1 
ATOM   1333 S  SD  . MET   A 1 172 ? 50.92300 33.04800 13.98500 1.000 42.93852  ? 169 MET   A SD  1 
ATOM   1334 C  CE  . MET   A 1 172 ? 52.10600 32.86000 15.31100 1.000 36.43354  ? 169 MET   A CE  1 
ATOM   1335 N  N   . SER   A 1 173 ? 55.02400 35.95700 11.26700 1.000 41.29249  ? 170 SER   A N   1 
ATOM   1336 C  CA  . SER   A 1 173 ? 56.31000 36.64100 11.20100 1.000 41.35668  ? 170 SER   A CA  1 
ATOM   1337 C  C   . SER   A 1 173 ? 56.16600 38.12100 11.53900 1.000 50.25242  ? 170 SER   A C   1 
ATOM   1338 O  O   . SER   A 1 173 ? 56.98000 38.68100 12.28400 1.000 46.02207  ? 170 SER   A O   1 
ATOM   1339 C  CB  . SER   A 1 173 ? 56.92500 36.46500 9.80500  1.000 45.98159  ? 170 SER   A CB  1 
ATOM   1340 O  OG  . SER   A 1 173 ? 58.06000 37.32000 9.66500  1.000 51.97152  ? 170 SER   A OG  1 
ATOM   1341 N  N   . TYR   A 1 174 ? 55.14900 38.77800 10.96500 1.000 49.37639  ? 171 TYR   A N   1 
ATOM   1342 C  CA  . TYR   A 1 174 ? 54.86100 40.17100 11.31100 1.000 44.75134  ? 171 TYR   A CA  1 
ATOM   1343 C  C   . TYR   A 1 174 ? 54.58100 40.31200 12.79800 1.000 44.87886  ? 171 TYR   A C   1 
ATOM   1344 O  O   . TYR   A 1 174 ? 55.05300 41.25200 13.45400 1.000 43.75774  ? 171 TYR   A O   1 
ATOM   1345 C  CB  . TYR   A 1 174 ? 53.65100 40.66900 10.51600 1.000 51.73459  ? 171 TYR   A CB  1 
ATOM   1346 C  CG  . TYR   A 1 174 ? 53.94600 41.61200 9.37600  1.000 63.19688  ? 171 TYR   A CG  1 
ATOM   1347 C  CD1 . TYR   A 1 174 ? 54.30700 42.93900 9.61400  1.000 67.51343  ? 171 TYR   A CD1 1 
ATOM   1348 C  CD2 . TYR   A 1 174 ? 53.83300 41.18700 8.05400  1.000 76.32693  ? 171 TYR   A CD2 1 
ATOM   1349 C  CE1 . TYR   A 1 174 ? 54.56100 43.81900 8.55800  1.000 85.30687  ? 171 TYR   A CE1 1 
ATOM   1350 C  CE2 . TYR   A 1 174 ? 54.08700 42.05600 6.98600  1.000 87.53101  ? 171 TYR   A CE2 1 
ATOM   1351 C  CZ  . TYR   A 1 174 ? 54.45100 43.37200 7.24700  1.000 98.47074  ? 171 TYR   A CZ  1 
ATOM   1352 O  OH  . TYR   A 1 174 ? 54.70300 44.23900 6.20000  1.000 106.73403 ? 171 TYR   A OH  1 
ATOM   1353 N  N   . LEU   A 1 175 ? 53.77000 39.40100 13.34000 1.000 41.81251  ? 172 LEU   A N   1 
ATOM   1354 C  CA  . LEU   A 1 175 ? 53.44400 39.45600 14.75600 1.000 40.67901  ? 172 LEU   A CA  1 
ATOM   1355 C  C   . LEU   A 1 175 ? 54.68900 39.25400 15.61500 1.000 45.45379  ? 172 LEU   A C   1 
ATOM   1356 O  O   . LEU   A 1 175 ? 54.90800 40.00000 16.58000 1.000 43.31322  ? 172 LEU   A O   1 
ATOM   1357 C  CB  . LEU   A 1 175 ? 52.37100 38.41500 15.07400 1.000 44.23256  ? 172 LEU   A CB  1 
ATOM   1358 C  CG  . LEU   A 1 175 ? 51.00300 38.71600 14.45800 1.000 44.90609  ? 172 LEU   A CG  1 
ATOM   1359 C  CD1 . LEU   A 1 175 ? 49.95200 37.67500 14.87700 1.000 32.62763  ? 172 LEU   A CD1 1 
ATOM   1360 C  CD2 . LEU   A 1 175 ? 50.56700 40.13600 14.83900 1.000 35.56888  ? 172 LEU   A CD2 1 
ATOM   1361 N  N   . PHE   A 1 176 ? 55.53400 38.27600 15.25100 1.000 43.35081  ? 173 PHE   A N   1 
ATOM   1362 C  CA  . PHE   A 1 176 ? 56.78100 38.03100 15.97500 1.000 43.00518  ? 173 PHE   A CA  1 
ATOM   1363 C  C   . PHE   A 1 176 ? 57.64500 39.28700 16.03800 1.000 45.44409  ? 173 PHE   A C   1 
ATOM   1364 O  O   . PHE   A 1 176 ? 58.30900 39.54400 17.04800 1.000 47.41379  ? 173 PHE   A O   1 
ATOM   1365 C  CB  . PHE   A 1 176 ? 57.56400 36.89500 15.30000 1.000 41.21624  ? 173 PHE   A CB  1 
ATOM   1366 C  CG  . PHE   A 1 176 ? 56.92200 35.54100 15.44300 1.000 35.99459  ? 173 PHE   A CG  1 
ATOM   1367 C  CD1 . PHE   A 1 176 ? 55.98600 35.30200 16.44500 1.000 42.15136  ? 173 PHE   A CD1 1 
ATOM   1368 C  CD2 . PHE   A 1 176 ? 57.24800 34.50700 14.58300 1.000 43.42604  ? 173 PHE   A CD2 1 
ATOM   1369 C  CE1 . PHE   A 1 176 ? 55.38200 34.06200 16.59000 1.000 35.90850  ? 173 PHE   A CE1 1 
ATOM   1370 C  CE2 . PHE   A 1 176 ? 56.65400 33.26100 14.73600 1.000 45.49554  ? 173 PHE   A CE2 1 
ATOM   1371 C  CZ  . PHE   A 1 176 ? 55.71600 33.04000 15.73500 1.000 44.28489  ? 173 PHE   A CZ  1 
ATOM   1372 N  N   . GLN   A 1 177 ? 57.65000 40.08000 14.96400 1.000 44.41609  ? 174 GLN   A N   1 
ATOM   1373 C  CA  . GLN   A 1 177 ? 58.47000 41.28700 14.93700 1.000 45.08604  ? 174 GLN   A CA  1 
ATOM   1374 C  C   . GLN   A 1 177 ? 57.99800 42.32000 15.94900 1.000 44.37244  ? 174 GLN   A C   1 
ATOM   1375 O  O   . GLN   A 1 177 ? 58.77800 43.19300 16.34200 1.000 51.56782  ? 174 GLN   A O   1 
ATOM   1376 C  CB  . GLN   A 1 177 ? 58.46900 41.88000 13.52500 1.000 45.32962  ? 174 GLN   A CB  1 
ATOM   1377 C  CG  . GLN   A 1 177 ? 59.49700 41.24800 12.59100 1.000 42.13564  ? 174 GLN   A CG  1 
ATOM   1378 C  CD  . GLN   A 1 177 ? 59.21400 41.53100 11.11300 1.000 60.25771  ? 174 GLN   A CD  1 
ATOM   1379 O  OE1 . GLN   A 1 177 ? 58.55500 40.75000 10.42500 1.000 70.14568  ? 174 GLN   A OE1 1 
ATOM   1380 N  NE2 . GLN   A 1 177 ? 59.70700 42.66500 10.62600 1.000 70.85747  ? 174 GLN   A NE2 1 
ATOM   1381 N  N   . HIS   A 1 178 ? 56.74000 42.23400 16.38700 1.000 41.84230  ? 175 HIS   A N   1 
ATOM   1382 C  CA  . HIS   A 1 178 ? 56.21600 43.09000 17.43600 1.000 44.32422  ? 175 HIS   A CA  1 
ATOM   1383 C  C   . HIS   A 1 178 ? 56.20600 42.40100 18.79800 1.000 48.64784  ? 175 HIS   A C   1 
ATOM   1384 O  O   . HIS   A 1 178 ? 55.44600 42.80600 19.68200 1.000 51.77799  ? 175 HIS   A O   1 
ATOM   1385 C  CB  . HIS   A 1 178 ? 54.81000 43.56400 17.08400 1.000 40.01071  ? 175 HIS   A CB  1 
ATOM   1386 C  CG  . HIS   A 1 178 ? 54.75400 44.41000 15.85500 1.000 68.14989  ? 175 HIS   A CG  1 
ATOM   1387 N  ND1 . HIS   A 1 178 ? 54.81400 43.88200 14.58100 1.000 53.13385  ? 175 HIS   A ND1 1 
ATOM   1388 C  CD2 . HIS   A 1 178 ? 54.65400 45.75300 15.70500 1.000 47.62893  ? 175 HIS   A CD2 1 
ATOM   1389 C  CE1 . HIS   A 1 178 ? 54.74600 44.86100 13.70100 1.000 61.32522  ? 175 HIS   A CE1 1 
ATOM   1390 N  NE2 . HIS   A 1 178 ? 54.65000 46.00500 14.35600 1.000 71.02255  ? 175 HIS   A NE2 1 
ATOM   1391 N  N   . ALA   A 1 179 ? 57.02500 41.36700 18.98000 1.000 44.96369  ? 176 ALA   A N   1 
ATOM   1392 C  CA  . ALA   A 1 179 ? 57.06200 40.61100 20.22000 1.000 46.89366  ? 176 ALA   A CA  1 
ATOM   1393 C  C   . ALA   A 1 179 ? 58.48600 40.58200 20.75600 1.000 44.87431  ? 176 ALA   A C   1 
ATOM   1394 O  O   . ALA   A 1 179 ? 59.44900 40.84200 20.02900 1.000 44.63684  ? 176 ALA   A O   1 
ATOM   1395 C  CB  . ALA   A 1 179 ? 56.53600 39.18300 20.01300 1.000 40.79295  ? 176 ALA   A CB  1 
ATOM   1396 N  N   . ASN   A 1 180 ? 58.61300 40.25800 22.04200 1.000 43.59735  ? 177 ASN   A N   1 
ATOM   1397 C  CA  . ASN   A 1 180 ? 59.92300 40.20000 22.69900 1.000 51.45276  ? 177 ASN   A CA  1 
ATOM   1398 C  C   . ASN   A 1 180 ? 60.55100 38.84000 22.43700 1.000 51.14355  ? 177 ASN   A C   1 
ATOM   1399 O  O   . ASN   A 1 180 ? 60.33200 37.87900 23.17400 1.000 50.72660  ? 177 ASN   A O   1 
ATOM   1400 C  CB  . ASN   A 1 180 ? 59.79900 40.44500 24.19600 1.000 47.93459  ? 177 ASN   A CB  1 
ATOM   1401 C  CG  . ASN   A 1 180 ? 61.15400 40.75300 24.87600 1.000 66.11526  ? 177 ASN   A CG  1 
ATOM   1402 O  OD1 . ASN   A 1 180 ? 61.17600 41.26700 25.99300 1.000 72.22214  ? 177 ASN   A OD1 1 
ATOM   1403 N  ND2 . ASN   A 1 180 ? 62.27300 40.44800 24.20000 1.000 50.53479  ? 177 ASN   A ND2 1 
ATOM   1404 N  N   . LEU   A 1 181 ? 61.37200 38.77200 21.39100 1.000 51.93620  ? 178 LEU   A N   1 
ATOM   1405 C  CA  . LEU   A 1 181 ? 62.11900 37.57100 21.04000 1.000 51.36871  ? 178 LEU   A CA  1 
ATOM   1406 C  C   . LEU   A 1 181 ? 63.62400 37.81100 21.11000 1.000 62.71459  ? 178 LEU   A C   1 
ATOM   1407 O  O   . LEU   A 1 181 ? 64.39800 37.14800 20.41600 1.000 63.60696  ? 178 LEU   A O   1 
ATOM   1408 C  CB  . LEU   A 1 181 ? 61.70400 37.06700 19.65700 1.000 47.56806  ? 178 LEU   A CB  1 
ATOM   1409 C  CG  . LEU   A 1 181 ? 60.21800 36.68200 19.59200 1.000 51.72957  ? 178 LEU   A CG  1 
ATOM   1410 C  CD1 . LEU   A 1 181 ? 59.79000 36.30400 18.19100 1.000 48.09228  ? 178 LEU   A CD1 1 
ATOM   1411 C  CD2 . LEU   A 1 181 ? 59.89300 35.54900 20.60500 1.000 46.57421  ? 178 LEU   A CD2 1 
ATOM   1412 N  N   . ASP   A 1 182 ? 64.04400 38.74800 21.96900 1.000 65.95274  ? 179 ASP   A N   1 
ATOM   1413 C  CA  . ASP   A 1 182 ? 65.46200 39.08000 22.11000 1.000 70.32856  ? 179 ASP   A CA  1 
ATOM   1414 C  C   . ASP   A 1 182 ? 66.25600 37.91100 22.68900 1.000 71.60928  ? 179 ASP   A C   1 
ATOM   1415 O  O   . ASP   A 1 182 ? 67.35600 37.60400 22.21800 1.000 73.17114  ? 179 ASP   A O   1 
ATOM   1416 C  CB  . ASP   A 1 182 ? 65.61300 40.31700 22.99800 1.000 68.83594  ? 179 ASP   A CB  1 
ATOM   1417 C  CG  . ASP   A 1 182 ? 65.20800 41.61400 22.29100 1.000 85.44776  ? 179 ASP   A CG  1 
ATOM   1418 O  OD1 . ASP   A 1 182 ? 64.89100 41.58300 21.07500 1.000 72.01790  ? 179 ASP   A OD1 1 
ATOM   1419 O  OD2 . ASP   A 1 182 ? 65.17800 42.66600 22.97300 1.000 80.57504  ? 179 ASP   A OD2 1 
ATOM   1420 N  N   . SER   A 1 183 ? 65.71300 37.24500 23.70700 1.000 77.31212  ? 180 SER   A N   1 
ATOM   1421 C  CA  . SER   A 1 183 ? 66.37000 36.08900 24.30500 1.000 67.92966  ? 180 SER   A CA  1 
ATOM   1422 C  C   . SER   A 1 183 ? 66.48300 34.91100 23.34700 1.000 79.30309  ? 180 SER   A C   1 
ATOM   1423 O  O   . SER   A 1 183 ? 67.05800 33.88700 23.73100 1.000 79.71461  ? 180 SER   A O   1 
ATOM   1424 C  CB  . SER   A 1 183 ? 65.60100 35.63600 25.55200 1.000 71.26908  ? 180 SER   A CB  1 
ATOM   1425 O  OG  . SER   A 1 183 ? 65.41900 36.70400 26.46800 1.000 87.47717  ? 180 SER   A OG  1 
ATOM   1426 N  N   . CYS   A 1 184 ? 65.93400 35.00800 22.13600 1.000 66.15070  ? 181 CYS   A N   1 
ATOM   1427 C  CA  . CYS   A 1 184 ? 65.90000 33.87600 21.22400 1.000 61.38193  ? 181 CYS   A CA  1 
ATOM   1428 C  C   . CYS   A 1 184 ? 67.16000 33.85200 20.38100 1.000 63.99444  ? 181 CYS   A C   1 
ATOM   1429 O  O   . CYS   A 1 184 ? 67.57100 34.87900 19.83800 1.000 68.37268  ? 181 CYS   A O   1 
ATOM   1430 C  CB  . CYS   A 1 184 ? 64.66600 33.91300 20.32600 1.000 58.14172  ? 181 CYS   A CB  1 
ATOM   1431 S  SG  . CYS   A 1 184 ? 63.15900 33.54900 21.21600 1.000 55.37839  ? 181 CYS   A SG  1 
ATOM   1432 N  N   . LYS   A 1 185 ? 67.75300 32.67000 20.25500 1.000 61.29123  ? 182 LYS   A N   1 
ATOM   1433 C  CA  . LYS   A 1 185 ? 69.07000 32.53300 19.66100 1.000 59.85767  ? 182 LYS   A CA  1 
ATOM   1434 C  C   . LYS   A 1 185 ? 69.14000 31.22100 18.89800 1.000 60.52822  ? 182 LYS   A C   1 
ATOM   1435 O  O   . LYS   A 1 185 ? 68.63700 30.19100 19.36200 1.000 63.35612  ? 182 LYS   A O   1 
ATOM   1436 C  CB  . LYS   A 1 185 ? 70.14700 32.61000 20.75600 1.000 72.54054  ? 182 LYS   A CB  1 
ATOM   1437 C  CG  . LYS   A 1 185 ? 71.53800 32.15700 20.35600 1.000 81.83484  ? 182 LYS   A CG  1 
ATOM   1438 C  CD  . LYS   A 1 185 ? 72.53800 32.51600 21.45600 1.000 85.11808  ? 182 LYS   A CD  1 
ATOM   1439 C  CE  . LYS   A 1 185 ? 73.25800 31.29100 21.99900 1.000 88.69525  ? 182 LYS   A CE  1 
ATOM   1440 N  NZ  . LYS   A 1 185 ? 74.09800 31.62500 23.18500 1.000 100.97937 ? 182 LYS   A NZ  1 
ATOM   1441 N  N   . ARG   A 1 186 ? 69.74900 31.26600 17.71600 1.000 60.38022  ? 183 ARG   A N   1 
ATOM   1442 C  CA  . ARG   A 1 186 ? 69.92900 30.07400 16.89900 1.000 64.45405  ? 183 ARG   A CA  1 
ATOM   1443 C  C   . ARG   A 1 186 ? 71.32700 30.09600 16.30600 1.000 72.16374  ? 183 ARG   A C   1 
ATOM   1444 O  O   . ARG   A 1 186 ? 71.68100 31.02400 15.57300 1.000 79.72082  ? 183 ARG   A O   1 
ATOM   1445 C  CB  . ARG   A 1 186 ? 68.88400 29.98200 15.78600 1.000 60.14892  ? 183 ARG   A CB  1 
ATOM   1446 C  CG  . ARG   A 1 186 ? 69.21000 28.91600 14.75500 1.000 62.02025  ? 183 ARG   A CG  1 
ATOM   1447 C  CD  . ARG   A 1 186 ? 68.11600 28.79600 13.69600 1.000 63.35658  ? 183 ARG   A CD  1 
ATOM   1448 N  NE  . ARG   A 1 186 ? 66.86400 28.30100 14.25900 1.000 58.37909  ? 183 ARG   A NE  1 
ATOM   1449 C  CZ  . ARG   A 1 186 ? 65.69500 28.32100 13.63300 1.000 64.03808  ? 183 ARG   A CZ  1 
ATOM   1450 N  NH1 . ARG   A 1 186 ? 65.56600 28.83200 12.41800 1.000 62.49522  ? 183 ARG   A NH1 1 
ATOM   1451 N  NH2 . ARG   A 1 186 ? 64.62900 27.81000 14.24000 1.000 63.29486  ? 183 ARG   A NH2 1 
ATOM   1452 N  N   . VAL   A 1 187 ? 72.11300 29.07600 16.61800 1.000 73.35708  ? 184 VAL   A N   1 
ATOM   1453 C  CA  . VAL   A 1 187 ? 73.45700 28.92300 16.08300 1.000 68.76415  ? 184 VAL   A CA  1 
ATOM   1454 C  C   . VAL   A 1 187 ? 73.41200 27.85500 15.00800 1.000 66.47633  ? 184 VAL   A C   1 
ATOM   1455 O  O   . VAL   A 1 187 ? 72.87300 26.76500 15.22900 1.000 68.43765  ? 184 VAL   A O   1 
ATOM   1456 C  CB  . VAL   A 1 187 ? 74.45800 28.56000 17.19100 1.000 80.39042  ? 184 VAL   A CB  1 
ATOM   1457 C  CG1 . VAL   A 1 187 ? 75.86500 28.63100 16.66500 1.000 73.84090  ? 184 VAL   A CG1 1 
ATOM   1458 C  CG2 . VAL   A 1 187 ? 74.29900 29.50900 18.36200 1.000 70.79919  ? 184 VAL   A CG2 1 
ATOM   1459 N  N   . LEU   A 1 188 ? 73.95800 28.17200 13.83800 1.000 76.95889  ? 185 LEU   A N   1 
ATOM   1460 C  CA  . LEU   A 1 188 ? 73.95000 27.26900 12.70100 1.000 76.69405  ? 185 LEU   A CA  1 
ATOM   1461 C  C   . LEU   A 1 188 ? 75.38000 26.94900 12.29300 1.000 83.18777  ? 185 LEU   A C   1 
ATOM   1462 O  O   . LEU   A 1 188 ? 76.32100 27.67300 12.62800 1.000 79.43426  ? 185 LEU   A O   1 
ATOM   1463 C  CB  . LEU   A 1 188 ? 73.19400 27.87900 11.51400 1.000 80.66799  ? 185 LEU   A CB  1 
ATOM   1464 C  CG  . LEU   A 1 188 ? 71.67100 27.95900 11.63900 1.000 82.09504  ? 185 LEU   A CG  1 
ATOM   1465 C  CD1 . LEU   A 1 188 ? 71.06400 28.42600 10.33200 1.000 84.41802  ? 185 LEU   A CD1 1 
ATOM   1466 C  CD2 . LEU   A 1 188 ? 71.08700 26.61800 12.04700 1.000 77.28700  ? 185 LEU   A CD2 1 
ATOM   1467 N  N   . ASN   A 1 189 ? 75.53600 25.85000 11.56300 1.000 84.20486  ? 186 ASN   A N   1 
ATOM   1468 C  CA  . ASN   A 1 189 ? 76.82500 25.48200 10.99600 1.000 99.32565  ? 186 ASN   A CA  1 
ATOM   1469 C  C   . ASN   A 1 189 ? 76.60200 25.00700 9.57100  1.000 103.33029 ? 186 ASN   A C   1 
ATOM   1470 O  O   . ASN   A 1 189 ? 75.71000 24.19200 9.31500  1.000 102.15265 ? 186 ASN   A O   1 
ATOM   1471 C  CB  . ASN   A 1 189 ? 77.52000 24.39200 11.82500 1.000 110.22428 ? 186 ASN   A CB  1 
ATOM   1472 C  CG  . ASN   A 1 189 ? 79.03000 24.59000 11.91600 1.000 111.76479 ? 186 ASN   A CG  1 
ATOM   1473 O  OD1 . ASN   A 1 189 ? 79.51500 25.70400 12.11600 1.000 109.39215 ? 186 ASN   A OD1 1 
ATOM   1474 N  ND2 . ASN   A 1 189 ? 79.77700 23.49900 11.78300 1.000 104.30315 ? 186 ASN   A ND2 1 
ATOM   1475 N  N   . VAL   A 1 190 ? 77.39500 25.53600 8.64500  1.000 105.22097 ? 187 VAL   A N   1 
ATOM   1476 C  CA  . VAL   A 1 190 ? 77.34100 25.14600 7.24400  1.000 104.61000 ? 187 VAL   A CA  1 
ATOM   1477 C  C   . VAL   A 1 190 ? 78.64000 24.43200 6.91100  1.000 103.49415 ? 187 VAL   A C   1 
ATOM   1478 O  O   . VAL   A 1 190 ? 79.72800 24.90800 7.26200  1.000 97.23283  ? 187 VAL   A O   1 
ATOM   1479 C  CB  . VAL   A 1 190 ? 77.11500 26.35700 6.32400  1.000 105.20047 ? 187 VAL   A CB  1 
ATOM   1480 C  CG1 . VAL   A 1 190 ? 76.53200 25.90200 4.99800  1.000 102.11856 ? 187 VAL   A CG1 1 
ATOM   1481 C  CG2 . VAL   A 1 190 ? 76.20000 27.36300 6.99800  1.000 99.25144  ? 187 VAL   A CG2 1 
ATOM   1482 N  N   . VAL   A 1 191 ? 78.52600 23.28800 6.24600  1.000 105.36387 ? 188 VAL   A N   1 
ATOM   1483 C  CA  . VAL   A 1 191 ? 79.66900 22.45200 5.90800  1.000 114.18284 ? 188 VAL   A CA  1 
ATOM   1484 C  C   . VAL   A 1 191 ? 79.75300 22.36800 4.39100  1.000 113.51956 ? 188 VAL   A C   1 
ATOM   1485 O  O   . VAL   A 1 191 ? 78.94500 21.68000 3.75100  1.000 103.38660 ? 188 VAL   A O   1 
ATOM   1486 C  CB  . VAL   A 1 191 ? 79.56700 21.05700 6.53700  1.000 109.29277 ? 188 VAL   A CB  1 
ATOM   1487 C  CG1 . VAL   A 1 191 ? 80.63700 20.13200 5.97400  1.000 120.68429 ? 188 VAL   A CG1 1 
ATOM   1488 C  CG2 . VAL   A 1 191 ? 79.70700 21.16400 8.04000  1.000 111.47135 ? 188 VAL   A CG2 1 
ATOM   1489 N  N   . CYS   A 1 192 ? 80.71900 23.07900 3.81600  1.000 105.09857 ? 189 CYS   A N   1 
ATOM   1490 C  CA  . CYS   A 1 192 ? 81.06200 22.95200 2.41000  1.000 114.67840 ? 189 CYS   A CA  1 
ATOM   1491 C  C   . CYS   A 1 192 ? 82.37800 22.20200 2.28100  1.000 115.09240 ? 189 CYS   A C   1 
ATOM   1492 O  O   . CYS   A 1 192 ? 83.32800 22.46100 3.02900  1.000 102.97526 ? 189 CYS   A O   1 
ATOM   1493 C  CB  . CYS   A 1 192 ? 81.18400 24.31700 1.72800  1.000 122.84533 ? 189 CYS   A CB  1 
ATOM   1494 S  SG  . CYS   A 1 192 ? 81.79700 24.20300 0.02900  1.000 123.20022 ? 189 CYS   A SG  1 
ATOM   1495 N  N   . LYS   A 1 193 ? 82.42400 21.27500 1.32100  1.000 114.26875 ? 190 LYS   A N   1 
ATOM   1496 C  CA  . LYS   A 1 193 ? 83.61100 20.44500 1.13800  1.000 114.83903 ? 190 LYS   A CA  1 
ATOM   1497 C  C   . LYS   A 1 193 ? 84.83200 21.28800 0.78900  1.000 115.61892 ? 190 LYS   A C   1 
ATOM   1498 O  O   . LYS   A 1 193 ? 85.93600 21.02900 1.28200  1.000 115.75202 ? 190 LYS   A O   1 
ATOM   1499 C  CB  . LYS   A 1 193 ? 83.34700 19.39900 0.05600  1.000 108.50404 ? 190 LYS   A CB  1 
ATOM   1500 C  CG  . LYS   A 1 193 ? 82.14700 18.51400 0.34900  1.000 108.95819 ? 190 LYS   A CG  1 
ATOM   1501 C  CD  . LYS   A 1 193 ? 81.97500 17.44800 -0.71800 1.000 112.97525 ? 190 LYS   A CD  1 
ATOM   1502 C  CE  . LYS   A 1 193 ? 80.93200 16.41900 -0.30500 1.000 124.03468 ? 190 LYS   A CE  1 
ATOM   1503 N  NZ  . LYS   A 1 193 ? 80.75900 15.35400 -1.33600 1.000 129.56638 ? 190 LYS   A NZ  1 
ATOM   1504 N  N   . THR   A 1 194 ? 84.65200 22.30900 -0.04800 1.000 114.20277 ? 191 THR   A N   1 
ATOM   1505 C  CA  . THR   A 1 194 ? 85.75800 23.16000 -0.46900 1.000 117.23913 ? 191 THR   A CA  1 
ATOM   1506 C  C   . THR   A 1 194 ? 85.98500 24.32000 0.49500  1.000 116.34168 ? 191 THR   A C   1 
ATOM   1507 O  O   . THR   A 1 194 ? 87.10300 24.51700 0.98400  1.000 109.16652 ? 191 THR   A O   1 
ATOM   1508 C  CB  . THR   A 1 194 ? 85.49700 23.69900 -1.88000 1.000 115.83846 ? 191 THR   A CB  1 
ATOM   1509 O  OG1 . THR   A 1 194 ? 85.14700 22.61400 -2.75100 1.000 109.08497 ? 191 THR   A OG1 1 
ATOM   1510 C  CG2 . THR   A 1 194 ? 86.73600 24.41200 -2.42000 1.000 107.40531 ? 191 THR   A CG2 1 
ATOM   1511 N  N   . CYS   A 1 195 ? 84.93000 25.09200 0.77500  1.000 116.14564 ? 192 CYS   A N   1 
ATOM   1512 C  CA  . CYS   A 1 195 ? 85.08200 26.29100 1.59300  1.000 118.32093 ? 192 CYS   A CA  1 
ATOM   1513 C  C   . CYS   A 1 195 ? 85.33200 25.93700 3.05400  1.000 116.95233 ? 192 CYS   A C   1 
ATOM   1514 O  O   . CYS   A 1 195 ? 86.14700 26.58300 3.72500  1.000 112.33008 ? 192 CYS   A O   1 
ATOM   1515 C  CB  . CYS   A 1 195 ? 83.84400 27.17800 1.45200  1.000 123.38762 ? 192 CYS   A CB  1 
ATOM   1516 S  SG  . CYS   A 1 195 ? 83.43700 27.65200 -0.25200 1.000 107.54710 ? 192 CYS   A SG  1 
ATOM   1517 N  N   . GLY   A 1 196 ? 84.63900 24.92000 3.56500  1.000 108.59834 ? 193 GLY   A N   1 
ATOM   1518 C  CA  . GLY   A 1 196 ? 84.89500 24.45200 4.91200  1.000 109.90599 ? 193 GLY   A CA  1 
ATOM   1519 C  C   . GLY   A 1 196 ? 83.71000 24.51100 5.85400  1.000 112.42349 ? 193 GLY   A C   1 
ATOM   1520 O  O   . GLY   A 1 196 ? 82.62400 24.00600 5.54500  1.000 107.85826 ? 193 GLY   A O   1 
ATOM   1521 N  N   . GLN   A 1 197 ? 83.92000 25.12400 7.01800  1.000 114.47317 ? 194 GLN   A N   1 
ATOM   1522 C  CA  . GLN   A 1 197 ? 82.91500 25.20700 8.07100  1.000 111.77818 ? 194 GLN   A CA  1 
ATOM   1523 C  C   . GLN   A 1 197 ? 82.72600 26.66500 8.45400  1.000 111.89054 ? 194 GLN   A C   1 
ATOM   1524 O  O   . GLN   A 1 197 ? 83.69100 27.34100 8.82900  1.000 105.17269 ? 194 GLN   A O   1 
ATOM   1525 C  CB  . GLN   A 1 197 ? 83.33000 24.39600 9.30100  1.000 113.69549 ? 194 GLN   A CB  1 
ATOM   1526 C  CG  . GLN   A 1 197 ? 82.51800 23.13800 9.54900  1.000 118.60107 ? 194 GLN   A CG  1 
ATOM   1527 C  CD  . GLN   A 1 197 ? 82.75900 22.56700 10.93900 1.000 127.01138 ? 194 GLN   A CD  1 
ATOM   1528 O  OE1 . GLN   A 1 197 ? 83.25700 23.25900 11.82900 1.000 119.44958 ? 194 GLN   A OE1 1 
ATOM   1529 N  NE2 . GLN   A 1 197 ? 82.40400 21.30200 11.13100 1.000 130.38506 ? 194 GLN   A NE2 1 
ATOM   1530 N  N   . GLN   A 1 198 ? 81.48900 27.14700 8.36900  1.000 115.85840 ? 195 GLN   A N   1 
ATOM   1531 C  CA  . GLN   A 1 198 ? 81.15300 28.50000 8.78900  1.000 124.39779 ? 195 GLN   A CA  1 
ATOM   1532 C  C   . GLN   A 1 198 ? 79.96700 28.44000 9.73900  1.000 111.65404 ? 195 GLN   A C   1 
ATOM   1533 O  O   . GLN   A 1 198 ? 78.99300 27.72500 9.48200  1.000 103.27674 ? 195 GLN   A O   1 
ATOM   1534 C  CB  . GLN   A 1 198 ? 80.83900 29.40500 7.58900  1.000 122.96888 ? 195 GLN   A CB  1 
ATOM   1535 C  CG  . GLN   A 1 198 ? 80.73300 30.89200 7.93300  1.000 118.74684 ? 195 GLN   A CG  1 
ATOM   1536 C  CD  . GLN   A 1 198 ? 81.91900 31.40700 8.73400  1.000 128.77415 ? 195 GLN   A CD  1 
ATOM   1537 O  OE1 . GLN   A 1 198 ? 81.91300 31.37900 9.96700  1.000 132.45089 ? 195 GLN   A OE1 1 
ATOM   1538 N  NE2 . GLN   A 1 198 ? 82.94300 31.88700 8.03500  1.000 126.70055 ? 195 GLN   A NE2 1 
ATOM   1539 N  N   . GLN   A 1 199 ? 80.05800 29.18800 10.83500 1.000 107.20347 ? 196 GLN   A N   1 
ATOM   1540 C  CA  . GLN   A 1 199 ? 79.05900 29.17200 11.89000 1.000 101.65914 ? 196 GLN   A CA  1 
ATOM   1541 C  C   . GLN   A 1 199 ? 78.46100 30.56100 12.04600 1.000 99.18579  ? 196 GLN   A C   1 
ATOM   1542 O  O   . GLN   A 1 199 ? 79.19100 31.53700 12.24400 1.000 102.53189 ? 196 GLN   A O   1 
ATOM   1543 C  CB  . GLN   A 1 199 ? 79.66500 28.70900 13.21900 1.000 96.17559  ? 196 GLN   A CB  1 
ATOM   1544 C  CG  . GLN   A 1 199 ? 78.69600 28.78600 14.38200 1.000 95.79266  ? 196 GLN   A CG  1 
ATOM   1545 C  CD  . GLN   A 1 199 ? 79.17800 28.04100 15.61200 1.000 90.66340  ? 196 GLN   A CD  1 
ATOM   1546 O  OE1 . GLN   A 1 199 ? 79.40000 28.64000 16.66500 1.000 84.27716  ? 196 GLN   A OE1 1 
ATOM   1547 N  NE2 . GLN   A 1 199 ? 79.33200 26.72600 15.48600 1.000 89.18585  ? 196 GLN   A NE2 1 
ATOM   1548 N  N   . THR   A 1 200 ? 77.13700 30.64200 11.96500 1.000 92.97647  ? 197 THR   A N   1 
ATOM   1549 C  CA  . THR   A 1 200 ? 76.41000 31.89300 12.11600 1.000 84.52514  ? 197 THR   A CA  1 
ATOM   1550 C  C   . THR   A 1 200 ? 75.44800 31.79400 13.29200 1.000 83.56929  ? 197 THR   A C   1 
ATOM   1551 O  O   . THR   A 1 200 ? 74.98800 30.70500 13.65300 1.000 78.30265  ? 197 THR   A O   1 
ATOM   1552 C  CB  . THR   A 1 200 ? 75.63100 32.24300 10.84200 1.000 91.53779  ? 197 THR   A CB  1 
ATOM   1553 O  OG1 . THR   A 1 200 ? 74.70300 31.19100 10.55000 1.000 89.09830  ? 197 THR   A OG1 1 
ATOM   1554 C  CG2 . THR   A 1 200 ? 76.57900 32.43000 9.65600  1.000 78.18371  ? 197 THR   A CG2 1 
ATOM   1555 N  N   . THR   A 1 201 ? 75.14900 32.94500 13.88800 1.000 78.84995  ? 198 THR   A N   1 
ATOM   1556 C  CA  . THR   A 1 201 ? 74.20400 33.03900 14.98900 1.000 75.75636  ? 198 THR   A CA  1 
ATOM   1557 C  C   . THR   A 1 201 ? 73.08300 33.99100 14.60600 1.000 76.02776  ? 198 THR   A C   1 
ATOM   1558 O  O   . THR   A 1 201 ? 73.34500 35.12100 14.17800 1.000 77.62641  ? 198 THR   A O   1 
ATOM   1559 C  CB  . THR   A 1 201 ? 74.89100 33.52200 16.27000 1.000 79.84282  ? 198 THR   A CB  1 
ATOM   1560 O  OG1 . THR   A 1 201 ? 75.58800 32.42700 16.87400 1.000 89.27742  ? 198 THR   A OG1 1 
ATOM   1561 C  CG2 . THR   A 1 201 ? 73.86300 34.05600 17.26300 1.000 71.14691  ? 198 THR   A CG2 1 
ATOM   1562 N  N   . LEU   A 1 202 ? 71.84100 33.53500 14.75800 1.000 75.32499  ? 199 LEU   A N   1 
ATOM   1563 C  CA  . LEU   A 1 202 ? 70.66500 34.35500 14.50900 1.000 71.41494  ? 199 LEU   A CA  1 
ATOM   1564 C  C   . LEU   A 1 202 ? 69.99500 34.71900 15.82800 1.000 69.02425  ? 199 LEU   A C   1 
ATOM   1565 O  O   . LEU   A 1 202 ? 70.02600 33.95200 16.79300 1.000 73.58409  ? 199 LEU   A O   1 
ATOM   1566 C  CB  . LEU   A 1 202 ? 69.66700 33.63300 13.59900 1.000 63.50054  ? 199 LEU   A CB  1 
ATOM   1567 C  CG  . LEU   A 1 202 ? 70.24600 33.06600 12.30700 1.000 63.52835  ? 199 LEU   A CG  1 
ATOM   1568 C  CD1 . LEU   A 1 202 ? 69.28600 32.09200 11.64000 1.000 59.51240  ? 199 LEU   A CD1 1 
ATOM   1569 C  CD2 . LEU   A 1 202 ? 70.59700 34.20000 11.36600 1.000 62.50750  ? 199 LEU   A CD2 1 
ATOM   1570 N  N   . LYS   A 1 203 ? 69.39800 35.90800 15.86500 1.000 71.45544  ? 200 LYS   A N   1 
ATOM   1571 C  CA  . LYS   A 1 203 ? 68.68000 36.38900 17.03500 1.000 60.94614  ? 200 LYS   A CA  1 
ATOM   1572 C  C   . LYS   A 1 203 ? 67.30300 36.88000 16.61200 1.000 57.01569  ? 200 LYS   A C   1 
ATOM   1573 O  O   . LYS   A 1 203 ? 67.07900 37.23800 15.45300 1.000 75.70766  ? 200 LYS   A O   1 
ATOM   1574 C  CB  . LYS   A 1 203 ? 69.44600 37.51300 17.75100 1.000 61.55317  ? 200 LYS   A CB  1 
ATOM   1575 C  CG  . LYS   A 1 203 ? 70.86100 37.12900 18.17300 1.000 74.40199  ? 200 LYS   A CG  1 
ATOM   1576 C  CD  . LYS   A 1 203 ? 71.07500 37.27500 19.68400 1.000 87.34440  ? 200 LYS   A CD  1 
ATOM   1577 C  CE  . LYS   A 1 203 ? 69.93000 36.65900 20.49000 1.000 77.97544  ? 200 LYS   A CE  1 
ATOM   1578 N  NZ  . LYS   A 1 203 ? 70.27400 36.38300 21.91800 1.000 82.87135  ? 200 LYS   A NZ  1 
ATOM   1579 N  N   . GLY   A 1 204 ? 66.37200 36.87800 17.56300 1.000 61.58837  ? 201 GLY   A N   1 
ATOM   1580 C  CA  . GLY   A 1 204 ? 65.05800 37.43000 17.28800 1.000 61.25683  ? 201 GLY   A CA  1 
ATOM   1581 C  C   . GLY   A 1 204 ? 64.22200 36.54600 16.37500 1.000 61.41048  ? 201 GLY   A C   1 
ATOM   1582 O  O   . GLY   A 1 204 ? 64.31700 35.31500 16.38900 1.000 63.61077  ? 201 GLY   A O   1 
ATOM   1583 N  N   . VAL   A 1 205 ? 63.40000 37.20500 15.55300 1.000 61.02822  ? 202 VAL   A N   1 
ATOM   1584 C  CA  . VAL   A 1 205 ? 62.43000 36.52000 14.69700 1.000 50.59869  ? 202 VAL   A CA  1 
ATOM   1585 C  C   . VAL   A 1 205 ? 63.09300 35.45300 13.84000 1.000 53.54952  ? 202 VAL   A C   1 
ATOM   1586 O  O   . VAL   A 1 205 ? 62.50900 34.39300 13.57600 1.000 53.68539  ? 202 VAL   A O   1 
ATOM   1587 C  CB  . VAL   A 1 205 ? 61.69400 37.54600 13.81700 1.000 52.68118  ? 202 VAL   A CB  1 
ATOM   1588 C  CG1 . VAL   A 1 205 ? 60.87100 36.83000 12.75300 1.000 48.06751  ? 202 VAL   A CG1 1 
ATOM   1589 C  CG2 . VAL   A 1 205 ? 60.81700 38.40600 14.66900 1.000 59.42706  ? 202 VAL   A CG2 1 
ATOM   1590 N  N   . GLU   A 1 206 ? 64.31000 35.72800 13.36600 1.000 53.43549  ? 203 GLU   A N   1 
ATOM   1591 C  CA  . GLU   A 1 206 ? 65.01400 34.78600 12.50600 1.000 54.10844  ? 203 GLU   A CA  1 
ATOM   1592 C  C   . GLU   A 1 206 ? 65.43300 33.52700 13.25200 1.000 51.96277  ? 203 GLU   A C   1 
ATOM   1593 O  O   . GLU   A 1 206 ? 65.69900 32.49700 12.62000 1.000 55.82496  ? 203 GLU   A O   1 
ATOM   1594 C  CB  . GLU   A 1 206 ? 66.25500 35.45500 11.91200 1.000 62.04594  ? 203 GLU   A CB  1 
ATOM   1595 C  CG  . GLU   A 1 206 ? 66.03300 36.33700 10.70600 1.000 68.63335  ? 203 GLU   A CG  1 
ATOM   1596 C  CD  . GLU   A 1 206 ? 67.34900 36.64100 9.99200  1.000 97.39418  ? 203 GLU   A CD  1 
ATOM   1597 O  OE1 . GLU   A 1 206 ? 68.15300 37.44300 10.52500 1.000 102.23700 ? 203 GLU   A OE1 1 
ATOM   1598 O  OE2 . GLU   A 1 206 ? 67.59100 36.05500 8.91400  1.000 93.55090  ? 203 GLU   A OE2 1 
ATOM   1599 N  N   . ALA   A 1 207 ? 65.52500 33.58700 14.57800 1.000 55.84870  ? 204 ALA   A N   1 
ATOM   1600 C  CA  . ALA   A 1 207 ? 65.90400 32.40300 15.32900 1.000 63.67129  ? 204 ALA   A CA  1 
ATOM   1601 C  C   . ALA   A 1 207 ? 64.75600 31.41800 15.49800 1.000 61.42115  ? 204 ALA   A C   1 
ATOM   1602 O  O   . ALA   A 1 207 ? 65.01400 30.23600 15.75000 1.000 52.80863  ? 204 ALA   A O   1 
ATOM   1603 C  CB  . ALA   A 1 207 ? 66.45900 32.79200 16.69700 1.000 51.57864  ? 204 ALA   A CB  1 
ATOM   1604 N  N   . VAL   A 1 208 ? 63.50200 31.84800 15.33500 1.000 57.57371  ? 205 VAL   A N   1 
ATOM   1605 C  CA  . VAL   A 1 208 ? 62.37400 30.96300 15.61600 1.000 48.04784  ? 205 VAL   A CA  1 
ATOM   1606 C  C   . VAL   A 1 208 ? 61.65800 30.48800 14.36700 1.000 49.28613  ? 205 VAL   A C   1 
ATOM   1607 O  O   . VAL   A 1 208 ? 60.75300 29.64800 14.48000 1.000 49.97275  ? 205 VAL   A O   1 
ATOM   1608 C  CB  . VAL   A 1 208 ? 61.38000 31.60900 16.60100 1.000 57.99614  ? 205 VAL   A CB  1 
ATOM   1609 C  CG1 . VAL   A 1 208 ? 62.12400 32.06300 17.85900 1.000 50.16963  ? 205 VAL   A CG1 1 
ATOM   1610 C  CG2 . VAL   A 1 208 ? 60.62800 32.76800 15.95900 1.000 48.50573  ? 205 VAL   A CG2 1 
ATOM   1611 N  N   . MET   A 1 209 ? 62.11000 30.94200 13.20400 1.000 49.68661  ? 206 MET   A N   1 
ATOM   1612 C  CA  . MET   A 1 209 ? 61.41000 30.58200 11.95100 1.000 45.42884  ? 206 MET   A CA  1 
ATOM   1613 C  C   . MET   A 1 209 ? 62.36800 29.97600 10.93200 1.000 52.87656  ? 206 MET   A C   1 
ATOM   1614 O  O   . MET   A 1 209 ? 63.49000 30.47400 10.81300 1.000 53.98311  ? 206 MET   A O   1 
ATOM   1615 C  CB  . MET   A 1 209 ? 60.76600 31.81600 11.31800 1.000 51.60241  ? 206 MET   A CB  1 
ATOM   1616 C  CG  . MET   A 1 209 ? 59.79900 32.54200 12.21800 1.000 57.19350  ? 206 MET   A CG  1 
ATOM   1617 S  SD  . MET   A 1 209 ? 58.99200 33.88100 11.32000 1.000 54.05895  ? 206 MET   A SD  1 
ATOM   1618 C  CE  . MET   A 1 209 ? 58.04200 32.94000 10.12900 1.000 59.43882  ? 206 MET   A CE  1 
ATOM   1619 N  N   . TYR   A 1 210 ? 61.94500 28.91200 10.26300 1.000 48.62244  ? 207 TYR   A N   1 
ATOM   1620 C  CA  . TYR   A 1 210 ? 62.69900 28.35500 9.16000  1.000 50.34326  ? 207 TYR   A CA  1 
ATOM   1621 C  C   . TYR   A 1 210 ? 61.72600 28.01800 8.03600  1.000 52.28740  ? 207 TYR   A C   1 
ATOM   1622 O  O   . TYR   A 1 210 ? 60.60700 27.55200 8.28900  1.000 46.89242  ? 207 TYR   A O   1 
ATOM   1623 C  CB  . TYR   A 1 210 ? 63.50600 27.11400 9.59900  1.000 55.86704  ? 207 TYR   A CB  1 
ATOM   1624 C  CG  . TYR   A 1 210 ? 64.34700 26.56100 8.47000  1.000 56.73380  ? 207 TYR   A CG  1 
ATOM   1625 C  CD1 . TYR   A 1 210 ? 65.55500 27.16000 8.12200  1.000 53.64740  ? 207 TYR   A CD1 1 
ATOM   1626 C  CD2 . TYR   A 1 210 ? 63.90700 25.48400 7.71600  1.000 46.27389  ? 207 TYR   A CD2 1 
ATOM   1627 C  CE1 . TYR   A 1 210 ? 66.31300 26.68600 7.06100  1.000 56.15833  ? 207 TYR   A CE1 1 
ATOM   1628 C  CE2 . TYR   A 1 210 ? 64.66500 24.99600 6.65000  1.000 56.12781  ? 207 TYR   A CE2 1 
ATOM   1629 C  CZ  . TYR   A 1 210 ? 65.87300 25.60700 6.33000  1.000 59.88607  ? 207 TYR   A CZ  1 
ATOM   1630 O  OH  . TYR   A 1 210 ? 66.65300 25.15200 5.28100  1.000 75.80787  ? 207 TYR   A OH  1 
ATOM   1631 N  N   . MET   A 1 211 ? 62.14300 28.29300 6.79900  1.000 51.60337  ? 208 MET   A N   1 
ATOM   1632 C  CA  . MET   A 1 211 ? 61.40800 27.91700 5.59500  1.000 49.18393  ? 208 MET   A CA  1 
ATOM   1633 C  C   . MET   A 1 211 ? 62.23200 26.91100 4.80300  1.000 48.60410  ? 208 MET   A C   1 
ATOM   1634 O  O   . MET   A 1 211 ? 63.40900 27.15600 4.52400  1.000 58.92257  ? 208 MET   A O   1 
ATOM   1635 C  CB  . MET   A 1 211 ? 61.09300 29.14700 4.72300  1.000 46.35479  ? 208 MET   A CB  1 
ATOM   1636 C  CG  . MET   A 1 211 ? 60.24800 28.87200 3.45700  1.000 43.29151  ? 208 MET   A CG  1 
ATOM   1637 S  SD  . MET   A 1 211 ? 58.57000 28.30900 3.87200  1.000 56.52074  ? 208 MET   A SD  1 
ATOM   1638 C  CE  . MET   A 1 211 ? 57.66000 28.39200 2.35400  1.000 55.06628  ? 208 MET   A CE  1 
ATOM   1639 N  N   . GLY   A 1 212 ? 61.60900 25.80200 4.42100  1.000 51.68379  ? 209 GLY   A N   1 
ATOM   1640 C  CA  . GLY   A 1 212 ? 62.33700 24.73000 3.76200  1.000 51.04047  ? 209 GLY   A CA  1 
ATOM   1641 C  C   . GLY   A 1 212 ? 61.90100 23.32600 4.15000  1.000 57.51141  ? 209 GLY   A C   1 
ATOM   1642 O  O   . GLY   A 1 212 ? 61.83600 22.43800 3.29700  1.000 52.87143  ? 209 GLY   A O   1 
ATOM   1643 N  N   . THR   A 1 213 ? 61.61700 23.09200 5.43000  1.000 58.18874  ? 210 THR   A N   1 
ATOM   1644 C  CA  . THR   A 1 213 ? 61.12400 21.78700 5.84700  1.000 63.66466  ? 210 THR   A CA  1 
ATOM   1645 C  C   . THR   A 1 213 ? 60.18300 21.96200 7.02400  1.000 55.45165  ? 210 THR   A C   1 
ATOM   1646 O  O   . THR   A 1 213 ? 60.31600 22.90200 7.81200  1.000 45.54525  ? 210 THR   A O   1 
ATOM   1647 C  CB  . THR   A 1 213 ? 62.24900 20.80800 6.23900  1.000 59.66151  ? 210 THR   A CB  1 
ATOM   1648 O  OG1 . THR   A 1 213 ? 61.66300 19.57200 6.66700  1.000 60.33264  ? 210 THR   A OG1 1 
ATOM   1649 C  CG2 . THR   A 1 213 ? 63.10300 21.35500 7.36700  1.000 49.31442  ? 210 THR   A CG2 1 
ATOM   1650 N  N   . LEU   A 1 214 ? 59.22500 21.04200 7.11700  1.000 51.36103  ? 211 LEU   A N   1 
ATOM   1651 C  CA  . LEU   A 1 214 ? 58.29500 20.98100 8.22800  1.000 44.41126  ? 211 LEU   A CA  1 
ATOM   1652 C  C   . LEU   A 1 214 ? 58.86200 20.26300 9.44800  1.000 51.84579  ? 211 LEU   A C   1 
ATOM   1653 O  O   . LEU   A 1 214 ? 58.30600 20.39800 10.54200 1.000 50.84670  ? 211 LEU   A O   1 
ATOM   1654 C  CB  . LEU   A 1 214 ? 57.02100 20.25800 7.80300  1.000 46.80343  ? 211 LEU   A CB  1 
ATOM   1655 C  CG  . LEU   A 1 214 ? 56.23300 20.82000 6.63300  1.000 51.40081  ? 211 LEU   A CG  1 
ATOM   1656 C  CD1 . LEU   A 1 214 ? 54.97600 19.96900 6.44700  1.000 50.11480  ? 211 LEU   A CD1 1 
ATOM   1657 C  CD2 . LEU   A 1 214 ? 55.90100 22.29600 6.88000  1.000 48.40620  ? 211 LEU   A CD2 1 
ATOM   1658 N  N   . SER   A 1 215 ? 59.93200 19.49100 9.28400  1.000 58.20477  ? 212 SER   A N   1 
ATOM   1659 C  CA  . SER   A 1 215 ? 60.40500 18.58500 10.32300 1.000 65.09906  ? 212 SER   A CA  1 
ATOM   1660 C  C   . SER   A 1 215 ? 61.51100 19.25500 11.12700 1.000 54.89753  ? 212 SER   A C   1 
ATOM   1661 O  O   . SER   A 1 215 ? 62.56000 19.59700 10.57800 1.000 57.31135  ? 212 SER   A O   1 
ATOM   1662 C  CB  . SER   A 1 215 ? 60.89500 17.27200 9.71000  1.000 63.30223  ? 212 SER   A CB  1 
ATOM   1663 O  OG  . SER   A 1 215 ? 61.65000 16.52400 10.64200 1.000 71.40676  ? 212 SER   A OG  1 
ATOM   1664 N  N   . TYR   A 1 216 ? 61.26300 19.45600 12.42700 1.000 55.98964  ? 213 TYR   A N   1 
ATOM   1665 C  CA  . TYR   A 1 216 ? 62.31700 19.93300 13.32100 1.000 58.19351  ? 213 TYR   A CA  1 
ATOM   1666 C  C   . TYR   A 1 216 ? 63.47500 18.93500 13.38200 1.000 66.53406  ? 213 TYR   A C   1 
ATOM   1667 O  O   . TYR   A 1 216 ? 64.64700 19.33200 13.37600 1.000 60.61487  ? 213 TYR   A O   1 
ATOM   1668 C  CB  . TYR   A 1 216 ? 61.74500 20.18200 14.72100 1.000 53.32810  ? 213 TYR   A CB  1 
ATOM   1669 C  CG  . TYR   A 1 216 ? 62.57400 21.10100 15.59900 1.000 52.74876  ? 213 TYR   A CG  1 
ATOM   1670 C  CD1 . TYR   A 1 216 ? 63.48900 21.99200 15.05600 1.000 59.52351  ? 213 TYR   A CD1 1 
ATOM   1671 C  CD2 . TYR   A 1 216 ? 62.43100 21.08000 16.98600 1.000 69.18663  ? 213 TYR   A CD2 1 
ATOM   1672 C  CE1 . TYR   A 1 216 ? 64.24200 22.84300 15.87500 1.000 53.35309  ? 213 TYR   A CE1 1 
ATOM   1673 C  CE2 . TYR   A 1 216 ? 63.17000 21.91200 17.80400 1.000 52.75684  ? 213 TYR   A CE2 1 
ATOM   1674 C  CZ  . TYR   A 1 216 ? 64.07300 22.78700 17.25100 1.000 64.29082  ? 213 TYR   A CZ  1 
ATOM   1675 O  OH  . TYR   A 1 216 ? 64.79600 23.60700 18.09000 1.000 62.59622  ? 213 TYR   A OH  1 
ATOM   1676 N  N   . GLU   A 1 217 ? 63.16700 17.63500 13.43200 1.000 66.14547  ? 214 GLU   A N   1 
ATOM   1677 C  CA  . GLU   A 1 217 ? 64.22700 16.62700 13.42900 1.000 74.63525  ? 214 GLU   A CA  1 
ATOM   1678 C  C   . GLU   A 1 217 ? 65.12400 16.78600 12.21100 1.000 75.97871  ? 214 GLU   A C   1 
ATOM   1679 O  O   . GLU   A 1 217 ? 66.35100 16.88000 12.33900 1.000 75.56401  ? 214 GLU   A O   1 
ATOM   1680 C  CB  . GLU   A 1 217 ? 63.63300 15.21900 13.47100 1.000 64.58348  ? 214 GLU   A CB  1 
ATOM   1681 C  CG  . GLU   A 1 217 ? 62.87900 14.88700 14.76100 1.000 91.79297  ? 214 GLU   A CG  1 
ATOM   1682 C  CD  . GLU   A 1 217 ? 63.78300 14.61400 15.96400 1.000 93.87793  ? 214 GLU   A CD  1 
ATOM   1683 O  OE1 . GLU   A 1 217 ? 64.97000 15.01400 15.95700 1.000 93.58741  ? 214 GLU   A OE1 1 
ATOM   1684 O  OE2 . GLU   A 1 217 ? 63.28700 14.00000 16.93300 1.000 101.35826 ? 214 GLU   A OE2 1 
ATOM   1685 N  N   . GLN   A 1 218 ? 64.52100 16.84300 11.02000 1.000 65.01286  ? 215 GLN   A N   1 
ATOM   1686 C  CA  . GLN   A 1 218 ? 65.30200 17.01000 9.79800  1.000 67.02889  ? 215 GLN   A CA  1 
ATOM   1687 C  C   . GLN   A 1 218 ? 66.17900 18.25100 9.86700  1.000 73.26151  ? 215 GLN   A C   1 
ATOM   1688 O  O   . GLN   A 1 218 ? 67.31900 18.24500 9.38900  1.000 69.59527  ? 215 GLN   A O   1 
ATOM   1689 C  CB  . GLN   A 1 218 ? 64.37300 17.07500 8.58900  1.000 72.02995  ? 215 GLN   A CB  1 
ATOM   1690 C  CG  . GLN   A 1 218 ? 65.06600 16.76800 7.27100  1.000 87.52623  ? 215 GLN   A CG  1 
ATOM   1691 C  CD  . GLN   A 1 218 ? 65.75400 15.41200 7.28100  1.000 98.76285  ? 215 GLN   A CD  1 
ATOM   1692 O  OE1 . GLN   A 1 218 ? 66.95200 15.31100 7.56100  1.000 97.85958  ? 215 GLN   A OE1 1 
ATOM   1693 N  NE2 . GLN   A 1 218 ? 64.99700 14.36000 6.97700  1.000 95.34517  ? 215 GLN   A NE2 1 
ATOM   1694 N  N   . PHE   A 1 219 ? 65.66800 19.32500 10.46900 1.000 66.47764  ? 216 PHE   A N   1 
ATOM   1695 C  CA  . PHE   A 1 219 ? 66.47900 20.52300 10.64700 1.000 69.02669  ? 216 PHE   A CA  1 
ATOM   1696 C  C   . PHE   A 1 219 ? 67.67700 20.24000 11.55000 1.000 72.31598  ? 216 PHE   A C   1 
ATOM   1697 O  O   . PHE   A 1 219 ? 68.78000 20.74400 11.30900 1.000 82.10230  ? 216 PHE   A O   1 
ATOM   1698 C  CB  . PHE   A 1 219 ? 65.60400 21.64200 11.21500 1.000 66.09025  ? 216 PHE   A CB  1 
ATOM   1699 C  CG  . PHE   A 1 219 ? 66.22800 23.00300 11.16800 1.000 63.57220  ? 216 PHE   A CG  1 
ATOM   1700 C  CD1 . PHE   A 1 219 ? 66.86700 23.45700 10.02500 1.000 72.97986  ? 216 PHE   A CD1 1 
ATOM   1701 C  CD2 . PHE   A 1 219 ? 66.15100 23.84600 12.26600 1.000 63.14051  ? 216 PHE   A CD2 1 
ATOM   1702 C  CE1 . PHE   A 1 219 ? 67.43300 24.71900 9.98400  1.000 61.74851  ? 216 PHE   A CE1 1 
ATOM   1703 C  CE2 . PHE   A 1 219 ? 66.70900 25.10300 12.22900 1.000 67.03611  ? 216 PHE   A CE2 1 
ATOM   1704 C  CZ  . PHE   A 1 219 ? 67.35300 25.54100 11.08400 1.000 66.11950  ? 216 PHE   A CZ  1 
ATOM   1705 N  N   . LYS   A 1 220 ? 67.48100 19.42800 12.59300 1.000 72.74427  ? 217 LYS   A N   1 
ATOM   1706 C  CA  . LYS   A 1 220 ? 68.58700 19.09300 13.48500 1.000 81.20465  ? 217 LYS   A CA  1 
ATOM   1707 C  C   . LYS   A 1 220 ? 69.60700 18.20100 12.78700 1.000 79.42012  ? 217 LYS   A C   1 
ATOM   1708 O  O   . LYS   A 1 220 ? 70.81700 18.35800 12.98400 1.000 86.63425  ? 217 LYS   A O   1 
ATOM   1709 C  CB  . LYS   A 1 220 ? 68.06100 18.41200 14.74800 1.000 72.49630  ? 217 LYS   A CB  1 
ATOM   1710 C  CG  . LYS   A 1 220 ? 67.38800 19.34400 15.73500 1.000 67.12936  ? 217 LYS   A CG  1 
ATOM   1711 C  CD  . LYS   A 1 220 ? 66.47700 18.57700 16.67900 1.000 65.82855  ? 217 LYS   A CD  1 
ATOM   1712 C  CE  . LYS   A 1 220 ? 65.89900 19.48700 17.74300 1.000 66.97375  ? 217 LYS   A CE  1 
ATOM   1713 N  NZ  . LYS   A 1 220 ? 65.07500 18.74200 18.74300 1.000 75.56023  ? 217 LYS   A NZ  1 
ATOM   1714 N  N   . LYS   A 1 221 ? 69.13400 17.26000 11.96800 1.000 76.43125  ? 218 LYS   A N   1 
ATOM   1715 C  CA  . LYS   A 1 221 ? 70.02800 16.36500 11.24500 1.000 86.68172  ? 218 LYS   A CA  1 
ATOM   1716 C  C   . LYS   A 1 221 ? 70.73700 17.05300 10.08200 1.000 87.66873  ? 218 LYS   A C   1 
ATOM   1717 O  O   . LYS   A 1 221 ? 71.75600 16.54300 9.61000  1.000 83.32304  ? 218 LYS   A O   1 
ATOM   1718 C  CB  . LYS   A 1 221 ? 69.24600 15.14700 10.74100 1.000 76.37908  ? 218 LYS   A CB  1 
ATOM   1719 C  CG  . LYS   A 1 221 ? 69.18300 14.00200 11.74500 1.000 88.74899  ? 218 LYS   A CG  1 
ATOM   1720 C  CD  . LYS   A 1 221 ? 67.76500 13.47800 11.91800 1.000 91.36446  ? 218 LYS   A CD  1 
ATOM   1721 C  CE  . LYS   A 1 221 ? 67.33700 12.63700 10.72600 1.000 101.37713 ? 218 LYS   A CE  1 
ATOM   1722 N  NZ  . LYS   A 1 221 ? 66.01100 11.98200 10.94100 1.000 100.26823 ? 218 LYS   A NZ  1 
ATOM   1723 N  N   . GLY   A 1 222 ? 70.23500 18.19400 9.61500  1.000 86.07913  ? 219 GLY   A N   1 
ATOM   1724 C  CA  . GLY   A 1 222 ? 70.87000 18.88700 8.51300  1.000 84.05290  ? 219 GLY   A CA  1 
ATOM   1725 C  C   . GLY   A 1 222 ? 70.02500 18.93800 7.25600  1.000 84.39525  ? 219 GLY   A C   1 
ATOM   1726 O  O   . GLY   A 1 222 ? 69.26500 18.00800 6.96400  1.000 77.35171  ? 219 GLY   A O   1 
ATOM   1727 N  N   . VAL   A 1 223 ? 70.14900 20.03200 6.50500  1.000 85.56925  ? 220 VAL   A N   1 
ATOM   1728 C  CA  . VAL   A 1 223 ? 69.41200 20.22900 5.26600  1.000 95.10532  ? 220 VAL   A CA  1 
ATOM   1729 C  C   . VAL   A 1 223 ? 70.38200 20.71600 4.20200  1.000 92.90288  ? 220 VAL   A C   1 
ATOM   1730 O  O   . VAL   A 1 223 ? 71.41900 21.31700 4.49700  1.000 85.25172  ? 220 VAL   A O   1 
ATOM   1731 C  CB  . VAL   A 1 223 ? 68.23900 21.22800 5.41300  1.000 84.34034  ? 220 VAL   A CB  1 
ATOM   1732 C  CG1 . VAL   A 1 223 ? 67.03500 20.54200 6.03300  1.000 77.18870  ? 220 VAL   A CG1 1 
ATOM   1733 C  CG2 . VAL   A 1 223 ? 68.66400 22.44200 6.23500  1.000 77.44761  ? 220 VAL   A CG2 1 
ATOM   1734 N  N   . GLN   A 1 224 ? 70.01300 20.46300 2.94800  1.000 96.87708  ? 221 GLN   A N   1 
ATOM   1735 C  CA  . GLN   A 1 224 ? 70.87900 20.72500 1.80300  1.000 101.13376 ? 221 GLN   A CA  1 
ATOM   1736 C  C   . GLN   A 1 224 ? 70.62600 22.13600 1.28200  1.000 94.37697  ? 221 GLN   A C   1 
ATOM   1737 O  O   . GLN   A 1 224 ? 69.56300 22.42100 0.72500  1.000 97.27597  ? 221 GLN   A O   1 
ATOM   1738 C  CB  . GLN   A 1 224 ? 70.64700 19.68200 0.71200  1.000 99.39893  ? 221 GLN   A CB  1 
ATOM   1739 C  CG  . GLN   A 1 224 ? 71.08400 18.27700 1.11200  1.000 94.62840  ? 221 GLN   A CG  1 
ATOM   1740 C  CD  . GLN   A 1 224 ? 72.36800 18.27400 1.93500  1.000 99.77139  ? 221 GLN   A CD  1 
ATOM   1741 O  OE1 . GLN   A 1 224 ? 73.39000 18.82800 1.52200  1.000 101.41242 ? 221 GLN   A OE1 1 
ATOM   1742 N  NE2 . GLN   A 1 224 ? 72.31800 17.64600 3.10800  1.000 97.37794  ? 221 GLN   A NE2 1 
ATOM   1743 N  N   . ILE   A 1 225 ? 71.60300 23.01700 1.46800  1.000 98.65500  ? 222 ILE   A N   1 
ATOM   1744 C  CA  . ILE   A 1 225 ? 71.52000 24.38400 0.96000  1.000 104.96796 ? 222 ILE   A CA  1 
ATOM   1745 C  C   . ILE   A 1 225 ? 72.71400 24.63500 0.04400  1.000 117.61861 ? 222 ILE   A C   1 
ATOM   1746 O  O   . ILE   A 1 225 ? 73.83000 24.17600 0.33600  1.000 118.66535 ? 222 ILE   A O   1 
ATOM   1747 C  CB  . ILE   A 1 225 ? 71.44900 25.40900 2.10700  1.000 106.04776 ? 222 ILE   A CB  1 
ATOM   1748 C  CG1 . ILE   A 1 225 ? 72.80800 25.57200 2.80300  1.000 105.14762 ? 222 ILE   A CG1 1 
ATOM   1749 C  CG2 . ILE   A 1 225 ? 70.37000 25.01100 3.10900  1.000 101.38668 ? 222 ILE   A CG2 1 
ATOM   1750 C  CD1 . ILE   A 1 225 ? 73.15800 27.01200 3.17100  1.000 94.29006  ? 222 ILE   A CD1 1 
ATOM   1751 N  N   . PRO   A 1 226 ? 72.52500 25.31700 -1.08400 1.000 122.54115 ? 223 PRO   A N   1 
ATOM   1752 C  CA  . PRO   A 1 226 ? 73.66400 25.60800 -1.96600 1.000 119.73984 ? 223 PRO   A CA  1 
ATOM   1753 C  C   . PRO   A 1 226 ? 74.65700 26.54800 -1.30000 1.000 115.22820 ? 223 PRO   A C   1 
ATOM   1754 O  O   . PRO   A 1 226 ? 74.27700 27.46600 -0.57000 1.000 115.99026 ? 223 PRO   A O   1 
ATOM   1755 C  CB  . PRO   A 1 226 ? 73.00800 26.25900 -3.18900 1.000 120.41412 ? 223 PRO   A CB  1 
ATOM   1756 C  CG  . PRO   A 1 226 ? 71.57100 25.81800 -3.14100 1.000 112.60917 ? 223 PRO   A CG  1 
ATOM   1757 C  CD  . PRO   A 1 226 ? 71.23700 25.69800 -1.68900 1.000 115.09590 ? 223 PRO   A CD  1 
ATOM   1758 N  N   . CYS   A 1 227 ? 75.94000 26.30700 -1.55400 1.000 121.75947 ? 224 CYS   A N   1 
ATOM   1759 C  CA  . CYS   A 1 227 ? 76.99300 27.13900 -0.98800 1.000 128.11153 ? 224 CYS   A CA  1 
ATOM   1760 C  C   . CYS   A 1 227 ? 77.34400 28.28900 -1.92800 1.000 127.44360 ? 224 CYS   A C   1 
ATOM   1761 O  O   . CYS   A 1 227 ? 77.01700 28.27200 -3.11800 1.000 121.20014 ? 224 CYS   A O   1 
ATOM   1762 C  CB  . CYS   A 1 227 ? 78.24700 26.31300 -0.69700 1.000 118.87018 ? 224 CYS   A CB  1 
ATOM   1763 S  SG  . CYS   A 1 227 ? 79.63900 27.30600 -0.09400 1.000 112.87499 ? 224 CYS   A SG  1 
ATOM   1764 N  N   . THR   A 1 228 ? 78.02400 29.29800 -1.36800 1.000 129.18515 ? 225 THR   A N   1 
ATOM   1765 C  CA  . THR   A 1 228 ? 78.51800 30.41200 -2.17800 1.000 129.19715 ? 225 THR   A CA  1 
ATOM   1766 C  C   . THR   A 1 228 ? 79.40500 29.91300 -3.31400 1.000 125.25697 ? 225 THR   A C   1 
ATOM   1767 O  O   . THR   A 1 228 ? 79.31900 30.40900 -4.44300 1.000 125.96734 ? 225 THR   A O   1 
ATOM   1768 C  CB  . THR   A 1 228 ? 79.28800 31.40900 -1.30300 1.000 127.81647 ? 225 THR   A CB  1 
ATOM   1769 O  OG1 . THR   A 1 228 ? 78.46300 31.84400 -0.21400 1.000 128.67866 ? 225 THR   A OG1 1 
ATOM   1770 C  CG2 . THR   A 1 228 ? 79.72200 32.62200 -2.11900 1.000 113.11701 ? 225 THR   A CG2 1 
ATOM   1771 N  N   . CYS   A 1 229 ? 80.26300 28.92900 -3.03400 1.000 131.73892 ? 226 CYS   A N   1 
ATOM   1772 C  CA  . CYS   A 1 229 ? 81.08600 28.31600 -4.07100 1.000 126.13503 ? 226 CYS   A CA  1 
ATOM   1773 C  C   . CYS   A 1 229 ? 80.26000 27.53900 -5.08800 1.000 129.06116 ? 226 CYS   A C   1 
ATOM   1774 O  O   . CYS   A 1 229 ? 80.71500 27.35300 -6.22100 1.000 129.16234 ? 226 CYS   A O   1 
ATOM   1775 C  CB  . CYS   A 1 229 ? 82.11600 27.37700 -3.44000 1.000 130.52084 ? 226 CYS   A CB  1 
ATOM   1776 S  SG  . CYS   A 1 229 ? 81.48800 25.69400 -3.12600 1.000 128.25852 ? 226 CYS   A SG  1 
ATOM   1777 N  N   . GLY   A 1 230 ? 79.07600 27.06700 -4.70800 1.000 128.02049 ? 227 GLY   A N   1 
ATOM   1778 C  CA  . GLY   A 1 230 ? 78.25900 26.24800 -5.58500 1.000 122.08119 ? 227 GLY   A CA  1 
ATOM   1779 C  C   . GLY   A 1 230 ? 78.67800 24.78800 -5.61600 1.000 124.66401 ? 227 GLY   A C   1 
ATOM   1780 O  O   . GLY   A 1 230 ? 78.57400 24.06900 -4.61600 1.000 121.42039 ? 227 GLY   A O   1 
ATOM   1781 N  N   . GLN   A 1 232 ? 76.31500 22.70500 -3.19400 1.000 111.69072 ? 229 GLN   A N   1 
ATOM   1782 C  CA  . GLN   A 1 232 ? 75.29100 22.17000 -2.30000 1.000 116.56407 ? 229 GLN   A CA  1 
ATOM   1783 C  C   . GLN   A 1 232 ? 75.88900 21.76900 -0.95600 1.000 123.93509 ? 229 GLN   A C   1 
ATOM   1784 O  O   . GLN   A 1 232 ? 76.21300 20.60000 -0.74200 1.000 124.96378 ? 229 GLN   A O   1 
ATOM   1785 C  CB  . GLN   A 1 232 ? 74.58800 20.96200 -2.93100 1.000 109.47290 ? 229 GLN   A CB  1 
ATOM   1786 C  CG  . GLN   A 1 232 ? 73.71800 21.28800 -4.13600 1.000 119.15285 ? 229 GLN   A CG  1 
ATOM   1787 C  CD  . GLN   A 1 232 ? 72.53200 22.17700 -3.79200 1.000 123.13023 ? 229 GLN   A CD  1 
ATOM   1788 O  OE1 . GLN   A 1 232 ? 72.14400 23.03900 -4.58000 1.000 124.67940 ? 229 GLN   A OE1 1 
ATOM   1789 N  NE2 . GLN   A 1 232 ? 71.94800 21.96800 -2.61600 1.000 114.22142 ? 229 GLN   A NE2 1 
ATOM   1790 N  N   . ALA   A 1 233 ? 76.02500 22.73900 -0.05200 1.000 124.44184 ? 230 ALA   A N   1 
ATOM   1791 C  CA  . ALA   A 1 233 ? 76.56300 22.48900 1.27900  1.000 112.49228 ? 230 ALA   A CA  1 
ATOM   1792 C  C   . ALA   A 1 233 ? 75.47200 21.90600 2.17800  1.000 109.81649 ? 230 ALA   A C   1 
ATOM   1793 O  O   . ALA   A 1 233 ? 74.36800 21.57700 1.73300  1.000 107.42720 ? 230 ALA   A O   1 
ATOM   1794 C  CB  . ALA   A 1 233 ? 77.15400 23.77000 1.86300  1.000 101.17479 ? 230 ALA   A CB  1 
ATOM   1795 N  N   . THR   A 1 234 ? 75.77400 21.76500 3.46500  1.000 110.54308 ? 231 THR   A N   1 
ATOM   1796 C  CA  . THR   A 1 234 ? 74.81300 21.25900 4.43500  1.000 104.26386 ? 231 THR   A CA  1 
ATOM   1797 C  C   . THR   A 1 234 ? 74.75500 22.21300 5.61900  1.000 103.75398 ? 231 THR   A C   1 
ATOM   1798 O  O   . THR   A 1 234 ? 75.79400 22.59700 6.16800  1.000 94.29080  ? 231 THR   A O   1 
ATOM   1799 C  CB  . THR   A 1 234 ? 75.17700 19.84100 4.89300  1.000 99.94593  ? 231 THR   A CB  1 
ATOM   1800 O  OG1 . THR   A 1 234 ? 74.71600 18.89700 3.91800  1.000 101.78018 ? 231 THR   A OG1 1 
ATOM   1801 C  CG2 . THR   A 1 234 ? 74.53000 19.51800 6.23100  1.000 94.07111  ? 231 THR   A CG2 1 
ATOM   1802 N  N   . LYS   A 1 235 ? 73.54200 22.61900 5.98200  1.000 97.89603  ? 232 LYS   A N   1 
ATOM   1803 C  CA  . LYS   A 1 235 ? 73.29800 23.43800 7.16000  1.000 101.48998 ? 232 LYS   A CA  1 
ATOM   1804 C  C   . LYS   A 1 235 ? 72.53700 22.60700 8.18400  1.000 97.68306  ? 232 LYS   A C   1 
ATOM   1805 O  O   . LYS   A 1 235 ? 71.58100 21.90800 7.83500  1.000 96.82811  ? 232 LYS   A O   1 
ATOM   1806 C  CB  . LYS   A 1 235 ? 72.51300 24.70200 6.79500  1.000 97.96108  ? 232 LYS   A CB  1 
ATOM   1807 C  CG  . LYS   A 1 235 ? 71.54400 25.18000 7.87200  1.000 94.98860  ? 232 LYS   A CG  1 
ATOM   1808 C  CD  . LYS   A 1 235 ? 70.72000 26.36600 7.39400  1.000 93.92318  ? 232 LYS   A CD  1 
ATOM   1809 C  CE  . LYS   A 1 235 ? 71.60400 27.49800 6.89900  1.000 81.56786  ? 232 LYS   A CE  1 
ATOM   1810 N  NZ  . LYS   A 1 235 ? 70.79400 28.56300 6.25100  1.000 84.90155  ? 232 LYS   A NZ  1 
ATOM   1811 N  N   . TYR   A 1 236 ? 72.97200 22.66700 9.43800  1.000 94.51958  ? 233 TYR   A N   1 
ATOM   1812 C  CA  . TYR   A 1 236 ? 72.30400 21.93400 10.50100 1.000 94.50640  ? 233 TYR   A CA  1 
ATOM   1813 C  C   . TYR   A 1 236 ? 72.25400 22.80100 11.75000 1.000 96.19760  ? 233 TYR   A C   1 
ATOM   1814 O  O   . TYR   A 1 236 ? 73.05300 23.72400 11.93300 1.000 87.60613  ? 233 TYR   A O   1 
ATOM   1815 C  CB  . TYR   A 1 236 ? 72.99800 20.59200 10.79700 1.000 101.51951 ? 233 TYR   A CB  1 
ATOM   1816 C  CG  . TYR   A 1 236 ? 74.39700 20.72900 11.35700 1.000 117.95797 ? 233 TYR   A CG  1 
ATOM   1817 C  CD1 . TYR   A 1 236 ? 75.49700 20.83800 10.51300 1.000 118.45417 ? 233 TYR   A CD1 1 
ATOM   1818 C  CD2 . TYR   A 1 236 ? 74.62200 20.74100 12.73100 1.000 122.53745 ? 233 TYR   A CD2 1 
ATOM   1819 C  CE1 . TYR   A 1 236 ? 76.78400 20.96700 11.02300 1.000 131.99932 ? 233 TYR   A CE1 1 
ATOM   1820 C  CE2 . TYR   A 1 236 ? 75.90500 20.86900 13.25100 1.000 128.10407 ? 233 TYR   A CE2 1 
ATOM   1821 C  CZ  . TYR   A 1 236 ? 76.98300 20.98100 12.39300 1.000 133.75372 ? 233 TYR   A CZ  1 
ATOM   1822 O  OH  . TYR   A 1 236 ? 78.25600 21.10900 12.90800 1.000 125.27041 ? 233 TYR   A OH  1 
ATOM   1823 N  N   . LEU   A 1 237 ? 71.30000 22.48500 12.61300 1.000 83.94522  ? 234 LEU   A N   1 
ATOM   1824 C  CA  . LEU   A 1 237 ? 71.09200 23.25600 13.82600 1.000 82.13086  ? 234 LEU   A CA  1 
ATOM   1825 C  C   . LEU   A 1 237 ? 72.14300 22.87300 14.86200 1.000 89.02390  ? 234 LEU   A C   1 
ATOM   1826 O  O   . LEU   A 1 237 ? 72.27900 21.69600 15.21400 1.000 84.34488  ? 234 LEU   A O   1 
ATOM   1827 C  CB  . LEU   A 1 237 ? 69.68000 23.02100 14.34900 1.000 72.58619  ? 234 LEU   A CB  1 
ATOM   1828 C  CG  . LEU   A 1 237 ? 69.30600 23.75000 15.63200 1.000 74.44906  ? 234 LEU   A CG  1 
ATOM   1829 C  CD1 . LEU   A 1 237 ? 69.37800 25.26200 15.43400 1.000 66.44239  ? 234 LEU   A CD1 1 
ATOM   1830 C  CD2 . LEU   A 1 237 ? 67.91800 23.30700 16.09400 1.000 76.82939  ? 234 LEU   A CD2 1 
ATOM   1831 N  N   . VAL   A 1 238 ? 72.88900 23.86600 15.33600 1.000 81.16627  ? 235 VAL   A N   1 
ATOM   1832 C  CA  . VAL   A 1 238 ? 73.89100 23.65600 16.37500 1.000 78.96914  ? 235 VAL   A CA  1 
ATOM   1833 C  C   . VAL   A 1 238 ? 73.29600 23.85600 17.76000 1.000 83.46382  ? 235 VAL   A C   1 
ATOM   1834 O  O   . VAL   A 1 238 ? 73.40900 22.98400 18.62600 1.000 84.08249  ? 235 VAL   A O   1 
ATOM   1835 C  CB  . VAL   A 1 238 ? 75.09900 24.59200 16.14000 1.000 85.27130  ? 235 VAL   A CB  1 
ATOM   1836 C  CG1 . VAL   A 1 238 ? 75.83900 24.87800 17.44900 1.000 73.53999  ? 235 VAL   A CG1 1 
ATOM   1837 C  CG2 . VAL   A 1 238 ? 76.03700 23.99400 15.10800 1.000 84.68729  ? 235 VAL   A CG2 1 
ATOM   1838 N  N   . GLN   A 1 239 ? 72.65200 25.00100 17.98900 1.000 79.49202  ? 236 GLN   A N   1 
ATOM   1839 C  CA  . GLN   A 1 239 ? 72.03100 25.29600 19.27300 1.000 81.51980  ? 236 GLN   A CA  1 
ATOM   1840 C  C   . GLN   A 1 239 ? 70.77800 26.12900 19.02900 1.000 81.80066  ? 236 GLN   A C   1 
ATOM   1841 O  O   . GLN   A 1 239 ? 70.77700 27.02200 18.17700 1.000 75.30480  ? 236 GLN   A O   1 
ATOM   1842 C  CB  . GLN   A 1 239 ? 72.99700 26.03400 20.21800 1.000 68.26933  ? 236 GLN   A CB  1 
ATOM   1843 C  CG  . GLN   A 1 239 ? 72.31800 26.66200 21.43300 1.000 86.20449  ? 236 GLN   A CG  1 
ATOM   1844 C  CD  . GLN   A 1 239 ? 73.20900 27.63300 22.18600 1.000 102.01866 ? 236 GLN   A CD  1 
ATOM   1845 O  OE1 . GLN   A 1 239 ? 72.74000 28.38000 23.04800 1.000 103.90576 ? 236 GLN   A OE1 1 
ATOM   1846 N  NE2 . GLN   A 1 239 ? 74.49800 27.64000 21.85500 1.000 103.96986 ? 236 GLN   A NE2 1 
ATOM   1847 N  N   . GLN   A 1 240 ? 69.71300 25.82300 19.77100 1.000 78.98399  ? 237 GLN   A N   1 
ATOM   1848 C  CA  . GLN   A 1 240 ? 68.45100 26.54300 19.68000 1.000 71.29526  ? 237 GLN   A CA  1 
ATOM   1849 C  C   . GLN   A 1 240 ? 68.03600 27.00600 21.06700 1.000 72.71839  ? 237 GLN   A C   1 
ATOM   1850 O  O   . GLN   A 1 240 ? 68.08600 26.23600 22.03000 1.000 80.05187  ? 237 GLN   A O   1 
ATOM   1851 C  CB  . GLN   A 1 240 ? 67.34400 25.67300 19.06000 1.000 75.18874  ? 237 GLN   A CB  1 
ATOM   1852 C  CG  . GLN   A 1 240 ? 66.01400 26.40400 18.87100 1.000 72.26781  ? 237 GLN   A CG  1 
ATOM   1853 C  CD  . GLN   A 1 240 ? 66.07900 27.46500 17.78600 1.000 64.00147  ? 237 GLN   A CD  1 
ATOM   1854 O  OE1 . GLN   A 1 240 ? 66.50300 27.19100 16.66500 1.000 69.69499  ? 237 GLN   A OE1 1 
ATOM   1855 N  NE2 . GLN   A 1 240 ? 65.65600 28.68600 18.11600 1.000 54.48121  ? 237 GLN   A NE2 1 
ATOM   1856 N  N   . GLU   A 1 241 ? 67.61200 28.26300 21.16700 1.000 65.49623  ? 238 GLU   A N   1 
ATOM   1857 C  CA  . GLU   A 1 241 ? 67.29500 28.86900 22.45900 1.000 68.54298  ? 238 GLU   A CA  1 
ATOM   1858 C  C   . GLU   A 1 241 ? 66.03400 29.71800 22.29100 1.000 74.85134  ? 238 GLU   A C   1 
ATOM   1859 O  O   . GLU   A 1 241 ? 66.11400 30.92700 22.05800 1.000 74.75142  ? 238 GLU   A O   1 
ATOM   1860 C  CB  . GLU   A 1 241 ? 68.47600 29.69300 22.94700 1.000 73.67725  ? 238 GLU   A CB  1 
ATOM   1861 C  CG  . GLU   A 1 241 ? 68.48300 30.00900 24.41200 1.000 84.37096  ? 238 GLU   A CG  1 
ATOM   1862 C  CD  . GLU   A 1 241 ? 69.41800 29.11300 25.18900 1.000 100.45308 ? 238 GLU   A CD  1 
ATOM   1863 O  OE1 . GLU   A 1 241 ? 70.27700 28.44900 24.56200 1.000 97.71632  ? 238 GLU   A OE1 1 
ATOM   1864 O  OE2 . GLU   A 1 241 ? 69.28200 29.07600 26.43100 1.000 95.71276  ? 238 GLU   A OE2 1 
ATOM   1865 N  N   . SER   A 1 242 ? 64.87100 29.08600 22.42500 1.000 66.94190  ? 239 SER   A N   1 
ATOM   1866 C  CA  . SER   A 1 242 ? 63.60300 29.77900 22.24200 1.000 63.42464  ? 239 SER   A CA  1 
ATOM   1867 C  C   . SER   A 1 242 ? 62.49900 28.93600 22.86200 1.000 59.27053  ? 239 SER   A C   1 
ATOM   1868 O  O   . SER   A 1 242 ? 62.65400 27.71900 23.00300 1.000 57.45949  ? 239 SER   A O   1 
ATOM   1869 C  CB  . SER   A 1 242 ? 63.32200 30.01900 20.75200 1.000 46.18308  ? 239 SER   A CB  1 
ATOM   1870 O  OG  . SER   A 1 242 ? 63.36100 28.79700 20.04400 1.000 44.81971  ? 239 SER   A OG  1 
ATOM   1871 N  N   . PRO   A 1 243 ? 61.36500 29.54800 23.22600 1.000 54.31812  ? 240 PRO   A N   1 
ATOM   1872 C  CA  . PRO   A 1 243 ? 60.23800 28.76200 23.75800 1.000 45.68707  ? 240 PRO   A CA  1 
ATOM   1873 C  C   . PRO   A 1 243 ? 59.52800 27.92200 22.71400 1.000 45.74332  ? 240 PRO   A C   1 
ATOM   1874 O  O   . PRO   A 1 243 ? 58.71400 27.06600 23.08800 1.000 55.66922  ? 240 PRO   A O   1 
ATOM   1875 C  CB  . PRO   A 1 243 ? 59.28500 29.83200 24.31600 1.000 53.60938  ? 240 PRO   A CB  1 
ATOM   1876 C  CG  . PRO   A 1 243 ? 60.03200 31.12800 24.27400 1.000 49.28826  ? 240 PRO   A CG  1 
ATOM   1877 C  CD  . PRO   A 1 243 ? 61.06200 30.98700 23.19500 1.000 45.73118  ? 240 PRO   A CD  1 
ATOM   1878 N  N   . PHE   A 1 244 ? 59.78500 28.15500 21.43100 1.000 46.44153  ? 241 PHE   A N   1 
ATOM   1879 C  CA  . PHE   A 1 244 ? 59.12700 27.45300 20.33100 1.000 43.15791  ? 241 PHE   A CA  1 
ATOM   1880 C  C   . PHE   A 1 244 ? 59.96100 27.68600 19.08300 1.000 45.61371  ? 241 PHE   A C   1 
ATOM   1881 O  O   . PHE   A 1 244 ? 60.83200 28.56000 19.05300 1.000 47.06399  ? 241 PHE   A O   1 
ATOM   1882 C  CB  . PHE   A 1 244 ? 57.68600 27.94700 20.10800 1.000 45.08720  ? 241 PHE   A CB  1 
ATOM   1883 C  CG  . PHE   A 1 244 ? 57.61600 29.37700 19.63500 1.000 48.99196  ? 241 PHE   A CG  1 
ATOM   1884 C  CD1 . PHE   A 1 244 ? 57.72000 29.68700 18.27300 1.000 44.13418  ? 241 PHE   A CD1 1 
ATOM   1885 C  CD2 . PHE   A 1 244 ? 57.49600 30.41900 20.55600 1.000 42.31073  ? 241 PHE   A CD2 1 
ATOM   1886 C  CE1 . PHE   A 1 244 ? 57.70700 31.00700 17.84300 1.000 46.29817  ? 241 PHE   A CE1 1 
ATOM   1887 C  CE2 . PHE   A 1 244 ? 57.46800 31.74800 20.13000 1.000 44.20094  ? 241 PHE   A CE2 1 
ATOM   1888 C  CZ  . PHE   A 1 244 ? 57.57100 32.04000 18.76700 1.000 47.11314  ? 241 PHE   A CZ  1 
ATOM   1889 N  N   . VAL   A 1 245 ? 59.68200 26.88800 18.04900 1.000 43.09675  ? 242 VAL   A N   1 
ATOM   1890 C  CA  . VAL   A 1 245 ? 60.17300 27.12600 16.70000 1.000 46.38368  ? 242 VAL   A CA  1 
ATOM   1891 C  C   . VAL   A 1 245 ? 59.00300 26.90700 15.74400 1.000 54.10525  ? 242 VAL   A C   1 
ATOM   1892 O  O   . VAL   A 1 245 ? 58.09200 26.12000 16.02200 1.000 47.68302  ? 242 VAL   A O   1 
ATOM   1893 C  CB  . VAL   A 1 245 ? 61.37300 26.21000 16.33100 1.000 57.18260  ? 242 VAL   A CB  1 
ATOM   1894 C  CG1 . VAL   A 1 245 ? 62.56200 26.46900 17.25900 1.000 54.69296  ? 242 VAL   A CG1 1 
ATOM   1895 C  CG2 . VAL   A 1 245 ? 60.97400 24.74400 16.36500 1.000 50.82549  ? 242 VAL   A CG2 1 
ATOM   1896 N  N   . MET   A 1 246 ? 59.05100 27.64500 14.62800 1.000 54.27631  ? 243 MET   A N   1 
ATOM   1897 C  CA  . MET   A 1 246 ? 58.05300 27.45600 13.54700 1.000 53.50058  ? 243 MET   A CA  1 
ATOM   1898 C  C   . MET   A 1 246 ? 58.79200 26.95800 12.30700 1.000 47.60962  ? 243 MET   A C   1 
ATOM   1899 O  O   . MET   A 1 246 ? 59.70200 27.64800 11.84100 1.000 49.06124  ? 243 MET   A O   1 
ATOM   1900 C  CB  . MET   A 1 246 ? 57.29200 28.72300 13.15400 1.000 46.01190  ? 243 MET   A CB  1 
ATOM   1901 C  CG  . MET   A 1 246 ? 56.40400 28.47800 11.94000 1.000 49.69512  ? 243 MET   A CG  1 
ATOM   1902 S  SD  . MET   A 1 246 ? 55.49600 29.90200 11.30400 1.000 51.09143  ? 243 MET   A SD  1 
ATOM   1903 C  CE  . MET   A 1 246 ? 55.95600 31.12100 12.52200 1.000 41.19992  ? 243 MET   A CE  1 
ATOM   1904 N  N   . MET   A 1 247 ? 58.41700 25.78900 11.82600 1.000 44.36928  ? 244 MET   A N   1 
ATOM   1905 C  CA  . MET   A 1 247 ? 58.98000 25.20200 10.61900 1.000 45.08778  ? 244 MET   A CA  1 
ATOM   1906 C  C   . MET   A 1 247 ? 57.93600 25.29000 9.52200  1.000 45.85821  ? 244 MET   A C   1 
ATOM   1907 O  O   . MET   A 1 247 ? 56.79700 24.85600 9.72000  1.000 49.22535  ? 244 MET   A O   1 
ATOM   1908 C  CB  . MET   A 1 247 ? 59.37600 23.73600 10.83300 1.000 50.55411  ? 244 MET   A CB  1 
ATOM   1909 C  CG  . MET   A 1 247 ? 60.28500 23.43200 12.02400 1.000 40.97171  ? 244 MET   A CG  1 
ATOM   1910 S  SD  . MET   A 1 247 ? 61.86900 24.29100 12.01100 1.000 53.26892  ? 244 MET   A SD  1 
ATOM   1911 C  CE  . MET   A 1 247 ? 62.65900 23.47200 10.63600 1.000 53.18870  ? 244 MET   A CE  1 
ATOM   1912 N  N   . SER   A 1 248 ? 58.32400 25.83300 8.36500  1.000 44.57656  ? 245 SER   A N   1 
ATOM   1913 C  CA  . SER   A 1 248 ? 57.40400 25.98100 7.24700  1.000 49.91571  ? 245 SER   A CA  1 
ATOM   1914 C  C   . SER   A 1 248 ? 58.00800 25.40000 5.97400  1.000 52.18606  ? 245 SER   A C   1 
ATOM   1915 O  O   . SER   A 1 248 ? 59.23000 25.29200 5.81900  1.000 48.92777  ? 245 SER   A O   1 
ATOM   1916 C  CB  . SER   A 1 248 ? 57.03000 27.45200 7.01000  1.000 47.59255  ? 245 SER   A CB  1 
ATOM   1917 O  OG  . SER   A 1 248 ? 56.58800 28.06700 8.20900  1.000 46.19912  ? 245 SER   A OG  1 
ATOM   1918 N  N   . ALA   A 1 249 ? 57.11200 25.04100 5.05300  1.000 49.09587  ? 246 ALA   A N   1 
ATOM   1919 C  CA  . ALA   A 1 249 ? 57.45300 24.57900 3.71700  1.000 45.20687  ? 246 ALA   A CA  1 
ATOM   1920 C  C   . ALA   A 1 249 ? 56.23000 24.76900 2.84100  1.000 51.20511  ? 246 ALA   A C   1 
ATOM   1921 O  O   . ALA   A 1 249 ? 55.10800 24.73900 3.35700  1.000 47.31781  ? 246 ALA   A O   1 
ATOM   1922 C  CB  . ALA   A 1 249 ? 57.87200 23.10000 3.72200  1.000 45.85477  ? 246 ALA   A CB  1 
ATOM   1923 N  N   . PRO   A 1 250 ? 56.39900 24.93500 1.52600  1.000 48.96013  ? 247 PRO   A N   1 
ATOM   1924 C  CA  . PRO   A 1 250 ? 55.24000 24.98600 0.64200  1.000 44.19066  ? 247 PRO   A CA  1 
ATOM   1925 C  C   . PRO   A 1 250 ? 54.35600 23.78100 0.88800  1.000 46.45114  ? 247 PRO   A C   1 
ATOM   1926 O  O   . PRO   A 1 250 ? 54.86700 22.68700 1.16100  1.000 54.52926  ? 247 PRO   A O   1 
ATOM   1927 C  CB  . PRO   A 1 250 ? 55.85500 24.95100 -0.77300 1.000 45.39237  ? 247 PRO   A CB  1 
ATOM   1928 C  CG  . PRO   A 1 250 ? 57.21700 25.49300 -0.60800 1.000 43.82298  ? 247 PRO   A CG  1 
ATOM   1929 C  CD  . PRO   A 1 250 ? 57.66700 25.05600 0.77900  1.000 44.87769  ? 247 PRO   A CD  1 
ATOM   1930 N  N   . PRO   A 1 251 ? 53.03800 23.93800 0.79200  1.000 43.18962  ? 248 PRO   A N   1 
ATOM   1931 C  CA  . PRO   A 1 251 ? 52.13200 22.84500 1.15500  1.000 40.30038  ? 248 PRO   A CA  1 
ATOM   1932 C  C   . PRO   A 1 251 ? 52.50100 21.55000 0.44000  1.000 56.55984  ? 248 PRO   A C   1 
ATOM   1933 O  O   . PRO   A 1 251 ? 52.85500 21.55300 -0.73900 1.000 52.82004  ? 248 PRO   A O   1 
ATOM   1934 C  CB  . PRO   A 1 251 ? 50.76000 23.36400 0.71600  1.000 45.80767  ? 248 PRO   A CB  1 
ATOM   1935 C  CG  . PRO   A 1 251 ? 50.89400 24.87400 0.72800  1.000 38.40204  ? 248 PRO   A CG  1 
ATOM   1936 C  CD  . PRO   A 1 251 ? 52.32500 25.17300 0.40900  1.000 38.87912  ? 248 PRO   A CD  1 
ATOM   1937 N  N   . ALA   A 1 252 ? 52.43900 20.44500 1.18300  1.000 57.36824  ? 249 ALA   A N   1 
ATOM   1938 C  CA  . ALA   A 1 252 ? 52.74400 19.10300 0.70100  1.000 52.48651  ? 249 ALA   A CA  1 
ATOM   1939 C  C   . ALA   A 1 252 ? 52.15500 18.11000 1.69300  1.000 62.35016  ? 249 ALA   A C   1 
ATOM   1940 O  O   . ALA   A 1 252 ? 52.05000 18.40800 2.88600  1.000 57.74200  ? 249 ALA   A O   1 
ATOM   1941 C  CB  . ALA   A 1 252 ? 54.25800 18.87700 0.55300  1.000 39.08313  ? 249 ALA   A CB  1 
ATOM   1942 N  N   . GLN   A 1 253 ? 51.77100 16.93300 1.19400  1.000 60.37195  ? 250 GLN   A N   1 
ATOM   1943 C  CA  . GLN   A 1 253 ? 51.22600 15.90000 2.07000  1.000 51.75546  ? 250 GLN   A CA  1 
ATOM   1944 C  C   . GLN   A 1 253 ? 52.25900 15.49100 3.11000  1.000 58.08451  ? 250 GLN   A C   1 
ATOM   1945 O  O   . GLN   A 1 253 ? 53.45300 15.38000 2.81900  1.000 54.33636  ? 250 GLN   A O   1 
ATOM   1946 C  CB  . GLN   A 1 253 ? 50.77900 14.69300 1.25900  1.000 58.14156  ? 250 GLN   A CB  1 
ATOM   1947 C  CG  . GLN   A 1 253 ? 49.53000 14.98900 0.45300  1.000 57.91882  ? 250 GLN   A CG  1 
ATOM   1948 C  CD  . GLN   A 1 253 ? 48.26800 14.84900 1.27300  1.000 61.39587  ? 250 GLN   A CD  1 
ATOM   1949 O  OE1 . GLN   A 1 253 ? 48.15600 13.95900 2.11800  1.000 68.80226  ? 250 GLN   A OE1 1 
ATOM   1950 N  NE2 . GLN   A 1 253 ? 47.30600 15.72400 1.02700  1.000 71.68955  ? 250 GLN   A NE2 1 
ATOM   1951 N  N   . TYR   A 1 254 ? 51.79300 15.29900 4.34000  1.000 54.55965  ? 251 TYR   A N   1 
ATOM   1952 C  CA  . TYR   A 1 254 ? 52.68500 15.16500 5.47900  1.000 59.03972  ? 251 TYR   A CA  1 
ATOM   1953 C  C   . TYR   A 1 254 ? 51.94600 14.45200 6.59500  1.000 53.21658  ? 251 TYR   A C   1 
ATOM   1954 O  O   . TYR   A 1 254 ? 50.74200 14.65100 6.78400  1.000 55.73319  ? 251 TYR   A O   1 
ATOM   1955 C  CB  . TYR   A 1 254 ? 53.16300 16.53200 5.94900  1.000 47.13430  ? 251 TYR   A CB  1 
ATOM   1956 C  CG  . TYR   A 1 254 ? 54.25000 16.51400 6.97300  1.000 51.87426  ? 251 TYR   A CG  1 
ATOM   1957 C  CD1 . TYR   A 1 254 ? 55.57400 16.32200 6.60100  1.000 48.82836  ? 251 TYR   A CD1 1 
ATOM   1958 C  CD2 . TYR   A 1 254 ? 53.96700 16.75000 8.31800  1.000 47.93760  ? 251 TYR   A CD2 1 
ATOM   1959 C  CE1 . TYR   A 1 254 ? 56.58800 16.34000 7.54400  1.000 51.58060  ? 251 TYR   A CE1 1 
ATOM   1960 C  CE2 . TYR   A 1 254 ? 54.97700 16.76000 9.27100  1.000 43.65590  ? 251 TYR   A CE2 1 
ATOM   1961 C  CZ  . TYR   A 1 254 ? 56.27900 16.55300 8.87800  1.000 52.78922  ? 251 TYR   A CZ  1 
ATOM   1962 O  OH  . TYR   A 1 254 ? 57.28000 16.57400 9.81600  1.000 54.34196  ? 251 TYR   A OH  1 
ATOM   1963 N  N   . GLU   A 1 255 ? 52.66700 13.61500 7.32100  1.000 62.48788  ? 252 GLU   A N   1 
ATOM   1964 C  CA  . GLU   A 1 255 ? 52.08800 12.86000 8.41700  1.000 66.21085  ? 252 GLU   A CA  1 
ATOM   1965 C  C   . GLU   A 1 255 ? 52.38300 13.59100 9.71900  1.000 61.57942  ? 252 GLU   A C   1 
ATOM   1966 O  O   . GLU   A 1 255 ? 53.53700 13.94800 9.98700  1.000 53.83818  ? 252 GLU   A O   1 
ATOM   1967 C  CB  . GLU   A 1 255 ? 52.64500 11.44000 8.44900  1.000 73.65227  ? 252 GLU   A CB  1 
ATOM   1968 C  CG  . GLU   A 1 255 ? 51.58400 10.37100 8.64900  1.000 89.67220  ? 252 GLU   A CG  1 
ATOM   1969 C  CD  . GLU   A 1 255 ? 52.14700 9.09300  9.24200  1.000 98.54541  ? 252 GLU   A CD  1 
ATOM   1970 O  OE1 . GLU   A 1 255 ? 53.39000 8.95600  9.30500  1.000 97.07799  ? 252 GLU   A OE1 1 
ATOM   1971 O  OE2 . GLU   A 1 255 ? 51.34100 8.22900  9.64900  1.000 104.73141 ? 252 GLU   A OE2 1 
ATOM   1972 N  N   . LEU   A 1 256 ? 51.33900 13.84500 10.50000 1.000 53.29216  ? 253 LEU   A N   1 
ATOM   1973 C  CA  . LEU   A 1 256 ? 51.47400 14.45000 11.82200 1.000 55.84638  ? 253 LEU   A CA  1 
ATOM   1974 C  C   . LEU   A 1 256 ? 51.19400 13.38000 12.86800 1.000 49.99962  ? 253 LEU   A C   1 
ATOM   1975 O  O   . LEU   A 1 256 ? 50.13600 12.73900 12.83400 1.000 51.99149  ? 253 LEU   A O   1 
ATOM   1976 C  CB  . LEU   A 1 256 ? 50.51600 15.63100 11.99100 1.000 47.64116  ? 253 LEU   A CB  1 
ATOM   1977 C  CG  . LEU   A 1 256 ? 50.81000 16.89400 11.18500 1.000 51.14441  ? 253 LEU   A CG  1 
ATOM   1978 C  CD1 . LEU   A 1 256 ? 49.61400 17.84400 11.26900 1.000 46.33701  ? 253 LEU   A CD1 1 
ATOM   1979 C  CD2 . LEU   A 1 256 ? 52.10300 17.55500 11.66800 1.000 42.09742  ? 253 LEU   A CD2 1 
ATOM   1980 N  N   . LYS   A 1 257 ? 52.13400 13.18500 13.78800 1.000 58.79325  ? 254 LYS   A N   1 
ATOM   1981 C  CA  . LYS   A 1 257 ? 52.02300 12.15100 14.81200 1.000 59.56130  ? 254 LYS   A CA  1 
ATOM   1982 C  C   . LYS   A 1 257 ? 51.74100 12.78100 16.16900 1.000 49.52963  ? 254 LYS   A C   1 
ATOM   1983 O  O   . LYS   A 1 257 ? 52.44600 13.70600 16.58600 1.000 50.09266  ? 254 LYS   A O   1 
ATOM   1984 C  CB  . LYS   A 1 257 ? 53.30300 11.31100 14.88200 1.000 54.91819  ? 254 LYS   A CB  1 
ATOM   1985 C  CG  . LYS   A 1 257 ? 53.59900 10.50600 13.61300 1.000 67.82321  ? 254 LYS   A CG  1 
ATOM   1986 C  CD  . LYS   A 1 257 ? 53.35800 9.01200  13.80800 1.000 84.95771  ? 254 LYS   A CD  1 
ATOM   1987 C  CE  . LYS   A 1 257 ? 51.95300 8.73000  14.31800 1.000 92.75342  ? 254 LYS   A CE  1 
ATOM   1988 N  NZ  . LYS   A 1 257 ? 51.77100 7.33700  14.81700 1.000 101.12493 ? 254 LYS   A NZ  1 
ATOM   1989 N  N   . HIS   A 1 258 ? 50.72000 12.26500 16.85700 1.000 50.41367  ? 255 HIS   A N   1 
ATOM   1990 C  CA  . HIS   A 1 258 ? 50.34500 12.75700 18.17700 1.000 52.32345  ? 255 HIS   A CA  1 
ATOM   1991 C  C   . HIS   A 1 258 ? 51.55400 12.81600 19.10200 1.000 51.97245  ? 255 HIS   A C   1 
ATOM   1992 O  O   . HIS   A 1 258 ? 52.37700 11.90000 19.12300 1.000 54.98895  ? 255 HIS   A O   1 
ATOM   1993 C  CB  . HIS   A 1 258 ? 49.26600 11.85500 18.77200 1.000 54.60906  ? 255 HIS   A CB  1 
ATOM   1994 C  CG  . HIS   A 1 258 ? 49.05100 12.05400 20.24000 1.000 59.15748  ? 255 HIS   A CG  1 
ATOM   1995 N  ND1 . HIS   A 1 258 ? 49.59200 11.21600 21.19200 1.000 77.52957  ? 255 HIS   A ND1 1 
ATOM   1996 C  CD2 . HIS   A 1 258 ? 48.34000 12.98300 20.92000 1.000 64.70773  ? 255 HIS   A CD2 1 
ATOM   1997 C  CE1 . HIS   A 1 258 ? 49.23800 11.63000 22.39600 1.000 73.69981  ? 255 HIS   A CE1 1 
ATOM   1998 N  NE2 . HIS   A 1 258 ? 48.47900 12.70100 22.26000 1.000 72.27706  ? 255 HIS   A NE2 1 
ATOM   1999 N  N   . GLY   A 1 259 ? 51.68700 13.92600 19.82700 1.000 48.04903  ? 256 GLY   A N   1 
ATOM   2000 C  CA  . GLY   A 1 259 ? 52.76600 14.09000 20.78500 1.000 44.97959  ? 256 GLY   A CA  1 
ATOM   2001 C  C   . GLY   A 1 259 ? 54.10600 14.51600 20.22100 1.000 47.42591  ? 256 GLY   A C   1 
ATOM   2002 O  O   . GLY   A 1 259 ? 55.05400 14.70800 20.99800 1.000 47.15176  ? 256 GLY   A O   1 
ATOM   2003 N  N   . THR   A 1 260 ? 54.23100 14.68900 18.90500 1.000 48.65243  ? 257 THR   A N   1 
ATOM   2004 C  CA  . THR   A 1 260 ? 55.51300 15.07100 18.31500 1.000 48.88203  ? 257 THR   A CA  1 
ATOM   2005 C  C   . THR   A 1 260 ? 55.58100 16.53500 17.87800 1.000 54.77667  ? 257 THR   A C   1 
ATOM   2006 O  O   . THR   A 1 260 ? 56.62900 16.97500 17.39500 1.000 48.40115  ? 257 THR   A O   1 
ATOM   2007 C  CB  . THR   A 1 260 ? 55.82100 14.16000 17.12700 1.000 56.35937  ? 257 THR   A CB  1 
ATOM   2008 O  OG1 . THR   A 1 260 ? 54.80200 14.32800 16.13700 1.000 56.94732  ? 257 THR   A OG1 1 
ATOM   2009 C  CG2 . THR   A 1 260 ? 55.83600 12.68400 17.58300 1.000 46.78983  ? 257 THR   A CG2 1 
ATOM   2010 N  N   . PHE   A 1 261 ? 54.50900 17.30300 18.05300 1.000 46.98877  ? 258 PHE   A N   1 
ATOM   2011 C  CA  . PHE   A 1 261 ? 54.46800 18.69700 17.62900 1.000 56.91427  ? 258 PHE   A CA  1 
ATOM   2012 C  C   . PHE   A 1 261 ? 53.40600 19.38000 18.47600 1.000 43.76207  ? 258 PHE   A C   1 
ATOM   2013 O  O   . PHE   A 1 261 ? 52.53400 18.72400 19.04200 1.000 43.30237  ? 258 PHE   A O   1 
ATOM   2014 C  CB  . PHE   A 1 261 ? 54.15500 18.82100 16.11300 1.000 41.19812  ? 258 PHE   A CB  1 
ATOM   2015 C  CG  . PHE   A 1 261 ? 52.75500 18.37100 15.76000 1.000 46.14890  ? 258 PHE   A CG  1 
ATOM   2016 C  CD1 . PHE   A 1 261 ? 52.42100 17.01600 15.77000 1.000 41.27213  ? 258 PHE   A CD1 1 
ATOM   2017 C  CD2 . PHE   A 1 261 ? 51.75700 19.29900 15.47300 1.000 41.59708  ? 258 PHE   A CD2 1 
ATOM   2018 C  CE1 . PHE   A 1 261 ? 51.11800 16.59500 15.49300 1.000 41.79441  ? 258 PHE   A CE1 1 
ATOM   2019 C  CE2 . PHE   A 1 261 ? 50.45100 18.88100 15.17800 1.000 40.19662  ? 258 PHE   A CE2 1 
ATOM   2020 C  CZ  . PHE   A 1 261 ? 50.13500 17.53200 15.19100 1.000 45.39642  ? 258 PHE   A CZ  1 
ATOM   2021 N  N   . THR   A 1 262 ? 53.46100 20.70600 18.53200 1.000 52.97667  ? 259 THR   A N   1 
ATOM   2022 C  CA  . THR   A 1 262 ? 52.40200 21.43000 19.22800 1.000 43.33094  ? 259 THR   A CA  1 
ATOM   2023 C  C   . THR   A 1 262 ? 51.15300 21.58300 18.35900 1.000 37.44511  ? 259 THR   A C   1 
ATOM   2024 O  O   . THR   A 1 262 ? 50.04800 21.20300 18.76200 1.000 42.08341  ? 259 THR   A O   1 
ATOM   2025 C  CB  . THR   A 1 262 ? 52.93000 22.79100 19.66800 1.000 43.19916  ? 259 THR   A CB  1 
ATOM   2026 O  OG1 . THR   A 1 262 ? 54.06800 22.58400 20.50300 1.000 54.20538  ? 259 THR   A OG1 1 
ATOM   2027 C  CG2 . THR   A 1 262 ? 51.88400 23.55900 20.42700 1.000 42.09205  ? 259 THR   A CG2 1 
ATOM   2028 N  N   . CYS   A 1 263 ? 51.31000 22.12700 17.15700 1.000 42.53969  ? 260 CYS   A N   1 
ATOM   2029 C  CA  . CYS   A 1 263 ? 50.17100 22.45900 16.30700 1.000 37.87755  ? 260 CYS   A CA  1 
ATOM   2030 C  C   . CYS   A 1 263 ? 50.71000 22.79200 14.92300 1.000 41.68733  ? 260 CYS   A C   1 
ATOM   2031 O  O   . CYS   A 1 263 ? 51.91100 23.00900 14.75300 1.000 43.75565  ? 260 CYS   A O   1 
ATOM   2032 C  CB  . CYS   A 1 263 ? 49.34300 23.62500 16.88200 1.000 40.98301  ? 260 CYS   A CB  1 
ATOM   2033 S  SG  . CYS   A 1 263 ? 50.23400 25.20600 16.97500 1.000 42.16130  ? 260 CYS   A SG  1 
ATOM   2034 N  N   . ALA   A 1 264 ? 49.80300 22.84600 13.93500 1.000 36.57745  ? 261 ALA   A N   1 
ATOM   2035 C  CA  . ALA   A 1 264 ? 50.19100 22.89800 12.52700 1.000 43.59754  ? 261 ALA   A CA  1 
ATOM   2036 C  C   . ALA   A 1 264 ? 49.11000 23.57900 11.67900 1.000 46.03435  ? 261 ALA   A C   1 
ATOM   2037 O  O   . ALA   A 1 264 ? 47.91600 23.50700 11.98800 1.000 41.14541  ? 261 ALA   A O   1 
ATOM   2038 C  CB  . ALA   A 1 264 ? 50.46300 21.47600 11.98700 1.000 39.38325  ? 261 ALA   A CB  1 
ATOM   2039 N  N   . SER   A 1 265 ? 49.54700 24.21100 10.57800 1.000 47.89992  ? 262 SER   A N   1 
ATOM   2040 C  CA  . SER   A 1 265 ? 48.65900 24.81500 9.58100  1.000 45.75097  ? 262 SER   A CA  1 
ATOM   2041 C  C   . SER   A 1 265 ? 48.47100 23.85700 8.41000  1.000 42.58425  ? 262 SER   A C   1 
ATOM   2042 O  O   . SER   A 1 265 ? 49.44100 23.50000 7.73200  1.000 42.59103  ? 262 SER   A O   1 
ATOM   2043 C  CB  . SER   A 1 265 ? 49.21500 26.13900 9.04000  1.000 34.83021  ? 262 SER   A CB  1 
ATOM   2044 O  OG  . SER   A 1 265 ? 49.62900 27.03800 10.05700 1.000 43.14063  ? 262 SER   A OG  1 
ATOM   2045 N  N   . GLU   A 1 266 ? 47.20700 23.54500 8.13400  1.000 41.43536  ? 263 GLU   A N   1 
ATOM   2046 C  CA  . GLU   A 1 266 ? 46.86400 22.75000 6.93500  1.000 49.20406  ? 263 GLU   A CA  1 
ATOM   2047 C  C   . GLU   A 1 266 ? 46.36200 23.72900 5.87400  1.000 46.72826  ? 263 GLU   A C   1 
ATOM   2048 O  O   . GLU   A 1 266 ? 45.53300 24.57600 6.20400  1.000 48.24229  ? 263 GLU   A O   1 
ATOM   2049 C  CB  . GLU   A 1 266 ? 45.76000 21.73900 7.22400  1.000 46.26046  ? 263 GLU   A CB  1 
ATOM   2050 C  CG  . GLU   A 1 266 ? 45.22000 21.08500 5.96700  1.000 58.92956  ? 263 GLU   A CG  1 
ATOM   2051 C  CD  . GLU   A 1 266 ? 43.84300 20.46300 6.08700  1.000 64.68251  ? 263 GLU   A CD  1 
ATOM   2052 O  OE1 . GLU   A 1 266 ? 43.75000 19.34600 6.60300  1.000 62.32115  ? 263 GLU   A OE1 1 
ATOM   2053 O  OE2 . GLU   A 1 266 ? 42.87300 21.09500 5.65300  1.000 85.34518  ? 263 GLU   A OE2 1 
ATOM   2054 N  N   . TYR   A 1 267 ? 46.86100 23.60700 4.65100  1.000 46.76642  ? 264 TYR   A N   1 
ATOM   2055 C  CA  . TYR   A 1 267 ? 46.45700 24.49100 3.56300  1.000 52.85680  ? 264 TYR   A CA  1 
ATOM   2056 C  C   . TYR   A 1 267 ? 46.04000 23.66200 2.36000  1.000 51.20861  ? 264 TYR   A C   1 
ATOM   2057 O  O   . TYR   A 1 267 ? 46.84700 22.90100 1.81900  1.000 52.77290  ? 264 TYR   A O   1 
ATOM   2058 C  CB  . TYR   A 1 267 ? 47.57900 25.45600 3.17300  1.000 43.89525  ? 264 TYR   A CB  1 
ATOM   2059 C  CG  . TYR   A 1 267 ? 47.13500 26.48800 2.16000  1.000 50.79966  ? 264 TYR   A CG  1 
ATOM   2060 C  CD1 . TYR   A 1 267 ? 46.47400 27.65000 2.56200  1.000 45.71898  ? 264 TYR   A CD1 1 
ATOM   2061 C  CD2 . TYR   A 1 267 ? 47.35200 26.29100 0.79100  1.000 47.13496  ? 264 TYR   A CD2 1 
ATOM   2062 C  CE1 . TYR   A 1 267 ? 46.05600 28.60500 1.63000  1.000 46.41374  ? 264 TYR   A CE1 1 
ATOM   2063 C  CE2 . TYR   A 1 267 ? 46.94400 27.23400 -0.15000 1.000 49.89361  ? 264 TYR   A CE2 1 
ATOM   2064 C  CZ  . TYR   A 1 267 ? 46.29900 28.38800 0.27100  1.000 59.46048  ? 264 TYR   A CZ  1 
ATOM   2065 O  OH  . TYR   A 1 267 ? 45.90000 29.31900 -0.66200 1.000 45.24209  ? 264 TYR   A OH  1 
ATOM   2066 N  N   . THR   A 1 268 ? 44.79300 23.83900 1.93200  1.000 52.63453  ? 265 THR   A N   1 
ATOM   2067 C  CA  . THR   A 1 268 ? 44.20500 23.12500 0.80900  1.000 49.85269  ? 265 THR   A CA  1 
ATOM   2068 C  C   . THR   A 1 268 ? 43.85500 24.11400 -0.29800 1.000 55.44579  ? 265 THR   A C   1 
ATOM   2069 O  O   . THR   A 1 268 ? 43.35200 25.20800 -0.02500 1.000 52.40556  ? 265 THR   A O   1 
ATOM   2070 C  CB  . THR   A 1 268 ? 42.94000 22.37100 1.24900  1.000 49.67596  ? 265 THR   A CB  1 
ATOM   2071 O  OG1 . THR   A 1 268 ? 43.28600 21.37400 2.21500  1.000 61.28287  ? 265 THR   A OG1 1 
ATOM   2072 C  CG2 . THR   A 1 268 ? 42.27900 21.69400 0.06800  1.000 57.04753  ? 265 THR   A CG2 1 
ATOM   2073 N  N   . GLY   A 1 269 ? 44.13300 23.74200 -1.54100 1.000 55.07373  ? 266 GLY   A N   1 
ATOM   2074 C  CA  . GLY   A 1 269 ? 43.66600 24.49600 -2.68600 1.000 52.29536  ? 266 GLY   A CA  1 
ATOM   2075 C  C   . GLY   A 1 269 ? 44.75900 25.29700 -3.37000 1.000 55.72967  ? 266 GLY   A C   1 
ATOM   2076 O  O   . GLY   A 1 269 ? 45.95800 25.05900 -3.20300 1.000 47.37833  ? 266 GLY   A O   1 
ATOM   2077 N  N   . ASN   A 1 270 ? 44.32400 26.27300 -4.15700 1.000 59.13383  ? 267 ASN   A N   1 
ATOM   2078 C  CA  . ASN   A 1 270 ? 45.25400 27.02800 -4.97800 1.000 48.99741  ? 267 ASN   A CA  1 
ATOM   2079 C  C   . ASN   A 1 270 ? 46.00200 28.05200 -4.14500 1.000 49.54684  ? 267 ASN   A C   1 
ATOM   2080 O  O   . ASN   A 1 270 ? 45.48700 28.56500 -3.14800 1.000 45.64943  ? 267 ASN   A O   1 
ATOM   2081 C  CB  . ASN   A 1 270 ? 44.51900 27.73400 -6.10700 1.000 58.38709  ? 267 ASN   A CB  1 
ATOM   2082 C  CG  . ASN   A 1 270 ? 44.07000 26.76900 -7.18400 1.000 67.45615  ? 267 ASN   A CG  1 
ATOM   2083 O  OD1 . ASN   A 1 270 ? 44.86500 25.97500 -7.69500 1.000 67.49077  ? 267 ASN   A OD1 1 
ATOM   2084 N  ND2 . ASN   A 1 270 ? 42.78700 26.80700 -7.50600 1.000 63.71568  ? 267 ASN   A ND2 1 
ATOM   2085 N  N   . TYR   A 1 271 ? 47.23500 28.32700 -4.56400 1.000 44.58524  ? 268 TYR   A N   1 
ATOM   2086 C  CA  . TYR   A 1 271 ? 48.00200 29.46900 -4.09500 1.000 46.90647  ? 268 TYR   A CA  1 
ATOM   2087 C  C   . TYR   A 1 271 ? 47.10100 30.68100 -3.87800 1.000 48.46033  ? 268 TYR   A C   1 
ATOM   2088 O  O   . TYR   A 1 271 ? 46.29700 31.03800 -4.74500 1.000 44.73659  ? 268 TYR   A O   1 
ATOM   2089 C  CB  . TYR   A 1 271 ? 49.08800 29.78100 -5.12500 1.000 38.84269  ? 268 TYR   A CB  1 
ATOM   2090 C  CG  . TYR   A 1 271 ? 50.06300 30.85700 -4.73200 1.000 47.95878  ? 268 TYR   A CG  1 
ATOM   2091 C  CD1 . TYR   A 1 271 ? 50.80900 30.75600 -3.56400 1.000 49.42053  ? 268 TYR   A CD1 1 
ATOM   2092 C  CD2 . TYR   A 1 271 ? 50.26400 31.97200 -5.54600 1.000 48.07150  ? 268 TYR   A CD2 1 
ATOM   2093 C  CE1 . TYR   A 1 271 ? 51.72400 31.74900 -3.20800 1.000 42.40667  ? 268 TYR   A CE1 1 
ATOM   2094 C  CE2 . TYR   A 1 271 ? 51.17200 32.95400 -5.20500 1.000 49.03350  ? 268 TYR   A CE2 1 
ATOM   2095 C  CZ  . TYR   A 1 271 ? 51.89500 32.84400 -4.03400 1.000 44.56708  ? 268 TYR   A CZ  1 
ATOM   2096 O  OH  . TYR   A 1 271 ? 52.79300 33.83800 -3.70300 1.000 52.55536  ? 268 TYR   A OH  1 
ATOM   2097 N  N   . GLN   A 1 272 ? 47.18800 31.25900 -2.67800 1.000 48.63850  ? 269 GLN   A N   1 
ATOM   2098 C  CA  . GLN   A 1 272 ? 46.50100 32.48700 -2.27700 1.000 48.09628  ? 269 GLN   A CA  1 
ATOM   2099 C  C   . GLN   A 1 272 ? 44.99300 32.37900 -2.06300 1.000 49.07205  ? 269 GLN   A C   1 
ATOM   2100 O  O   . GLN   A 1 272 ? 44.48200 32.98700 -1.12000 1.000 63.92698  ? 269 GLN   A O   1 
ATOM   2101 C  CB  . GLN   A 1 272 ? 46.81300 33.60100 -3.26800 1.000 39.83553  ? 269 GLN   A CB  1 
ATOM   2102 C  CG  . GLN   A 1 272 ? 48.26700 34.03600 -3.13300 1.000 44.43013  ? 269 GLN   A CG  1 
ATOM   2103 C  CD  . GLN   A 1 272 ? 48.63700 35.17100 -4.06100 1.000 49.94746  ? 269 GLN   A CD  1 
ATOM   2104 O  OE1 . GLN   A 1 272 ? 48.05900 35.33000 -5.14700 1.000 46.80459  ? 269 GLN   A OE1 1 
ATOM   2105 N  NE2 . GLN   A 1 272 ? 49.61900 35.96500 -3.64600 1.000 41.15670  ? 269 GLN   A NE2 1 
ATOM   2106 N  N   . CYS   A 1 273 ? 44.24700 31.62600 -2.87000 1.000 48.52844  ? 270 CYS   A N   1 
ATOM   2107 C  CA  . CYS   A 1 273 ? 42.79900 31.58200 -2.66500 1.000 51.32224  ? 270 CYS   A CA  1 
ATOM   2108 C  C   . CYS   A 1 273 ? 42.32100 30.22000 -2.15800 1.000 48.94688  ? 270 CYS   A C   1 
ATOM   2109 O  O   . CYS   A 1 273 ? 41.16600 29.84900 -2.37300 1.000 45.45034  ? 270 CYS   A O   1 
ATOM   2110 C  CB  . CYS   A 1 273 ? 42.03200 31.97700 -3.94100 1.000 47.92514  ? 270 CYS   A CB  1 
ATOM   2111 S  SG  . CYS   A 1 273 ? 42.53400 31.14100 -5.45100 1.000 55.58946  ? 270 CYS   A SG  1 
ATOM   2112 N  N   . GLY   A 1 274 ? 43.18600 29.48000 -1.46500 1.000 58.23288  ? 271 GLY   A N   1 
ATOM   2113 C  CA  . GLY   A 1 274 ? 42.79300 28.25200 -0.79900 1.000 39.67336  ? 271 GLY   A CA  1 
ATOM   2114 C  C   . GLY   A 1 274 ? 42.18300 28.49200 0.56500  1.000 50.66128  ? 271 GLY   A C   1 
ATOM   2115 O  O   . GLY   A 1 274 ? 41.61200 29.55400 0.84000  1.000 47.15023  ? 271 GLY   A O   1 
ATOM   2116 N  N   . HIS   A 1 275 ? 42.30300 27.49300 1.44400  1.000 42.28616  ? 272 HIS   A N   1 
ATOM   2117 C  CA  . HIS   A 1 275 ? 41.70200 27.57300 2.77000  1.000 45.98750  ? 272 HIS   A CA  1 
ATOM   2118 C  C   . HIS   A 1 275 ? 42.58700 26.87900 3.80000  1.000 54.83748  ? 272 HIS   A C   1 
ATOM   2119 O  O   . HIS   A 1 275 ? 43.09900 25.77600 3.57400  1.000 45.08823  ? 272 HIS   A O   1 
ATOM   2120 C  CB  . HIS   A 1 275 ? 40.30100 26.94300 2.76700  1.000 43.54831  ? 272 HIS   A CB  1 
ATOM   2121 C  CG  . HIS   A 1 275 ? 39.51600 27.14900 4.03100  1.000 51.72242  ? 272 HIS   A CG  1 
ATOM   2122 N  ND1 . HIS   A 1 275 ? 39.02400 28.38400 4.42300  1.000 58.73281  ? 272 HIS   A ND1 1 
ATOM   2123 C  CD2 . HIS   A 1 275 ? 39.11000 26.26000 4.97700  1.000 48.03420  ? 272 HIS   A CD2 1 
ATOM   2124 C  CE1 . HIS   A 1 275 ? 38.35100 28.23800 5.55200  1.000 66.61117  ? 272 HIS   A CE1 1 
ATOM   2125 N  NE2 . HIS   A 1 275 ? 38.38900 26.96100 5.91100  1.000 48.32513  ? 272 HIS   A NE2 1 
ATOM   2126 N  N   . TYR   A 1 276 ? 42.75300 27.53900 4.93200  1.000 47.30707  ? 273 TYR   A N   1 
ATOM   2127 C  CA  . TYR   A 1 276 ? 43.53300 27.02400 6.04000  1.000 40.48495  ? 273 TYR   A CA  1 
ATOM   2128 C  C   . TYR   A 1 276 ? 42.65000 26.26400 7.02200  1.000 44.26089  ? 273 TYR   A C   1 
ATOM   2129 O  O   . TYR   A 1 276 ? 41.49900 26.63600 7.26800  1.000 42.30469  ? 273 TYR   A O   1 
ATOM   2130 C  CB  . TYR   A 1 276 ? 44.19000 28.17100 6.78600  1.000 36.12685  ? 273 TYR   A CB  1 
ATOM   2131 C  CG  . TYR   A 1 276 ? 45.48500 28.69000 6.23100  1.000 43.78260  ? 273 TYR   A CG  1 
ATOM   2132 C  CD1 . TYR   A 1 276 ? 46.68500 28.04100 6.50100  1.000 38.89417  ? 273 TYR   A CD1 1 
ATOM   2133 C  CD2 . TYR   A 1 276 ? 45.51900 29.86200 5.46300  1.000 35.78934  ? 273 TYR   A CD2 1 
ATOM   2134 C  CE1 . TYR   A 1 276 ? 47.88800 28.53400 6.02300  1.000 39.29544  ? 273 TYR   A CE1 1 
ATOM   2135 C  CE2 . TYR   A 1 276 ? 46.71700 30.36200 4.97700  1.000 32.96124  ? 273 TYR   A CE2 1 
ATOM   2136 C  CZ  . TYR   A 1 276 ? 47.90400 29.69700 5.27300  1.000 36.96361  ? 273 TYR   A CZ  1 
ATOM   2137 O  OH  . TYR   A 1 276 ? 49.11600 30.17900 4.82300  1.000 38.14869  ? 273 TYR   A OH  1 
ATOM   2138 N  N   . LYS   A 1 277 ? 43.22100 25.21600 7.61200  1.000 45.34084  ? 274 LYS   A N   1 
ATOM   2139 C  CA  . LYS   A 1 277 ? 42.69000 24.58100 8.81400  1.000 44.25184  ? 274 LYS   A CA  1 
ATOM   2140 C  C   . LYS   A 1 277 ? 43.82600 24.43900 9.81900  1.000 38.62371  ? 274 LYS   A C   1 
ATOM   2141 O  O   . LYS   A 1 277 ? 45.00700 24.53200 9.46600  1.000 43.38356  ? 274 LYS   A O   1 
ATOM   2142 C  CB  . LYS   A 1 277 ? 42.09400 23.20100 8.51200  1.000 48.03846  ? 274 LYS   A CB  1 
ATOM   2143 C  CG  . LYS   A 1 277 ? 40.78600 23.23000 7.74700  1.000 50.32150  ? 274 LYS   A CG  1 
ATOM   2144 C  CD  . LYS   A 1 277 ? 40.21600 21.82100 7.60900  1.000 55.65127  ? 274 LYS   A CD  1 
ATOM   2145 C  CE  . LYS   A 1 277 ? 39.42900 21.66000 6.32200  1.000 54.16892  ? 274 LYS   A CE  1 
ATOM   2146 N  NZ  . LYS   A 1 277 ? 38.86000 20.29000 6.20800  1.000 60.31826  ? 274 LYS   A NZ  1 
ATOM   2147 N  N   . HIS   A 1 278 ? 43.46800 24.16900 11.07100 1.000 39.52946  ? 275 HIS   A N   1 
ATOM   2148 C  CA  . HIS   A 1 278 ? 44.41700 24.12100 12.17500 1.000 41.48258  ? 275 HIS   A CA  1 
ATOM   2149 C  C   . HIS   A 1 278 ? 44.39800 22.73900 12.82600 1.000 46.92935  ? 275 HIS   A C   1 
ATOM   2150 O  O   . HIS   A 1 278 ? 43.33500 22.24500 13.22300 1.000 39.87607  ? 275 HIS   A O   1 
ATOM   2151 C  CB  . HIS   A 1 278 ? 44.08800 25.22000 13.20300 1.000 33.52411  ? 275 HIS   A CB  1 
ATOM   2152 C  CG  . HIS   A 1 278 ? 45.00000 25.24000 14.38500 1.000 38.10537  ? 275 HIS   A CG  1 
ATOM   2153 N  ND1 . HIS   A 1 278 ? 46.24400 25.83500 14.36000 1.000 40.89074  ? 275 HIS   A ND1 1 
ATOM   2154 C  CD2 . HIS   A 1 278 ? 44.84600 24.74400 15.63300 1.000 41.28694  ? 275 HIS   A CD2 1 
ATOM   2155 C  CE1 . HIS   A 1 278 ? 46.81800 25.70300 15.54000 1.000 43.84770  ? 275 HIS   A CE1 1 
ATOM   2156 N  NE2 . HIS   A 1 278 ? 45.98800 25.04700 16.33100 1.000 42.29470  ? 275 HIS   A NE2 1 
ATOM   2157 N  N   . ILE   A 1 279 ? 45.57000 22.12200 12.93900 1.000 43.97466  ? 276 ILE   A N   1 
ATOM   2158 C  CA  . ILE   A 1 279 ? 45.73100 20.83300 13.60900 1.000 39.57194  ? 276 ILE   A CA  1 
ATOM   2159 C  C   . ILE   A 1 279 ? 46.51000 21.05600 14.89300 1.000 42.43383  ? 276 ILE   A C   1 
ATOM   2160 O  O   . ILE   A 1 279 ? 47.58400 21.67200 14.87200 1.000 39.59683  ? 276 ILE   A O   1 
ATOM   2161 C  CB  . ILE   A 1 279 ? 46.46300 19.80600 12.73000 1.000 43.40974  ? 276 ILE   A CB  1 
ATOM   2162 C  CG1 . ILE   A 1 279 ? 45.96600 19.85600 11.27100 1.000 40.28860  ? 276 ILE   A CG1 1 
ATOM   2163 C  CG2 . ILE   A 1 279 ? 46.38800 18.44500 13.38300 1.000 42.52017  ? 276 ILE   A CG2 1 
ATOM   2164 C  CD1 . ILE   A 1 279 ? 44.48800 19.61600 11.10300 1.000 45.23766  ? 276 ILE   A CD1 1 
ATOM   2165 N  N   . THR   A 1 280 ? 45.98900 20.53300 16.00100 1.000 35.60419  ? 277 THR   A N   1 
ATOM   2166 C  CA  . THR   A 1 280 ? 46.63400 20.66800 17.29900 1.000 40.04013  ? 277 THR   A CA  1 
ATOM   2167 C  C   . THR   A 1 280 ? 46.70100 19.30300 17.98300 1.000 42.88013  ? 277 THR   A C   1 
ATOM   2168 O  O   . THR   A 1 280 ? 45.76200 18.50500 17.89000 1.000 44.60770  ? 277 THR   A O   1 
ATOM   2169 C  CB  . THR   A 1 280 ? 45.88700 21.70200 18.18000 1.000 39.34276  ? 277 THR   A CB  1 
ATOM   2170 O  OG1 . THR   A 1 280 ? 46.45500 21.72400 19.49000 1.000 42.33176  ? 277 THR   A OG1 1 
ATOM   2171 C  CG2 . THR   A 1 280 ? 44.40000 21.36400 18.28600 1.000 36.01480  ? 277 THR   A CG2 1 
ATOM   2172 N  N   . SER   A 1 281 ? 47.82800 19.03800 18.66600 1.000 46.41506  ? 278 SER   A N   1 
ATOM   2173 C  CA  . SER   A 1 281 ? 48.10000 17.75300 19.32300 1.000 35.88293  ? 278 SER   A CA  1 
ATOM   2174 C  C   . SER   A 1 281 ? 47.75900 17.86100 20.80500 1.000 39.82909  ? 278 SER   A C   1 
ATOM   2175 O  O   . SER   A 1 281 ? 48.51900 18.44100 21.58200 1.000 44.48528  ? 278 SER   A O   1 
ATOM   2176 C  CB  . SER   A 1 281 ? 49.55500 17.34200 19.14700 1.000 42.02670  ? 278 SER   A CB  1 
ATOM   2177 O  OG  . SER   A 1 281 ? 49.81100 16.07500 19.74300 1.000 47.21371  ? 278 SER   A OG  1 
ATOM   2178 N  N   . LYS   A 1 282 ? 46.62800 17.29100 21.19500 1.000 42.91833  ? 279 LYS   A N   1 
ATOM   2179 C  CA  . LYS   A 1 282 ? 46.20700 17.21800 22.59300 1.000 38.74343  ? 279 LYS   A CA  1 
ATOM   2180 C  C   . LYS   A 1 282 ? 46.37200 15.77000 23.07000 1.000 45.94222  ? 279 LYS   A C   1 
ATOM   2181 O  O   . LYS   A 1 282 ? 47.44200 15.19500 22.83800 1.000 44.49940  ? 279 LYS   A O   1 
ATOM   2182 C  CB  . LYS   A 1 282 ? 44.78900 17.75900 22.74700 1.000 43.76374  ? 279 LYS   A CB  1 
ATOM   2183 C  CG  . LYS   A 1 282 ? 44.57000 19.16400 22.21100 1.000 45.07507  ? 279 LYS   A CG  1 
ATOM   2184 C  CD  . LYS   A 1 282 ? 45.57100 20.14800 22.83900 1.000 47.86401  ? 279 LYS   A CD  1 
ATOM   2185 C  CE  . LYS   A 1 282 ? 45.16000 21.58100 22.59200 1.000 49.93543  ? 279 LYS   A CE  1 
ATOM   2186 N  NZ  . LYS   A 1 282 ? 43.72600 21.81700 22.94600 1.000 50.24782  ? 279 LYS   A NZ  1 
ATOM   2187 N  N   . GLU   A 1 283 ? 45.38200 15.18400 23.73600 1.000 38.90435  ? 280 GLU   A N   1 
ATOM   2188 C  CA  . GLU   A 1 283 ? 45.45500 13.77000 24.05500 1.000 53.10555  ? 280 GLU   A CA  1 
ATOM   2189 C  C   . GLU   A 1 283 ? 45.23600 12.94100 22.80500 1.000 56.30387  ? 280 GLU   A C   1 
ATOM   2190 O  O   . GLU   A 1 283 ? 45.61800 11.76700 22.77300 1.000 54.39050  ? 280 GLU   A O   1 
ATOM   2191 C  CB  . GLU   A 1 283 ? 44.43000 13.42100 25.14800 1.000 42.51947  ? 280 GLU   A CB  1 
ATOM   2192 C  CG  . GLU   A 1 283 ? 43.01700 13.21300 24.65200 1.000 43.09529  ? 280 GLU   A CG  1 
ATOM   2193 C  CD  . GLU   A 1 283 ? 42.29300 14.50900 24.29200 1.000 52.97948  ? 280 GLU   A CD  1 
ATOM   2194 O  OE1 . GLU   A 1 283 ? 42.90400 15.60100 24.36100 1.000 46.74717  ? 280 GLU   A OE1 1 
ATOM   2195 O  OE2 . GLU   A 1 283 ? 41.09600 14.43200 23.93900 1.000 49.67582  ? 280 GLU   A OE2 1 
ATOM   2196 N  N   . THR   A 1 284 ? 44.64000 13.55000 21.77600 1.000 51.59064  ? 281 THR   A N   1 
ATOM   2197 C  CA  . THR   A 1 284 ? 44.58600 13.02000 20.42600 1.000 48.85653  ? 281 THR   A CA  1 
ATOM   2198 C  C   . THR   A 1 284 ? 44.71300 14.21100 19.46400 1.000 59.15037  ? 281 THR   A C   1 
ATOM   2199 O  O   . THR   A 1 284 ? 44.87200 15.36000 19.89200 1.000 51.98924  ? 281 THR   A O   1 
ATOM   2200 C  CB  . THR   A 1 284 ? 43.30600 12.18200 20.22900 1.000 48.25201  ? 281 THR   A CB  1 
ATOM   2201 O  OG1 . THR   A 1 284 ? 43.41200 11.42600 19.01700 1.000 52.87032  ? 281 THR   A OG1 1 
ATOM   2202 C  CG2 . THR   A 1 284 ? 42.06700 13.05800 20.16200 1.000 41.97670  ? 281 THR   A CG2 1 
ATOM   2203 N  N   . LEU   A 1 285 ? 44.68200 13.94500 18.15800 1.000 49.19465  ? 282 LEU   A N   1 
ATOM   2204 C  CA  . LEU   A 1 285 ? 44.84200 15.01600 17.17500 1.000 54.54883  ? 282 LEU   A CA  1 
ATOM   2205 C  C   . LEU   A 1 285 ? 43.49200 15.64300 16.87700 1.000 47.36601  ? 282 LEU   A C   1 
ATOM   2206 O  O   . LEU   A 1 285 ? 42.53600 14.94300 16.54000 1.000 51.27111  ? 282 LEU   A O   1 
ATOM   2207 C  CB  . LEU   A 1 285 ? 45.47100 14.49800 15.88500 1.000 40.11767  ? 282 LEU   A CB  1 
ATOM   2208 C  CG  . LEU   A 1 285 ? 46.89900 13.96700 16.02300 1.000 57.71477  ? 282 LEU   A CG  1 
ATOM   2209 C  CD1 . LEU   A 1 285 ? 47.50500 13.64600 14.67200 1.000 50.61916  ? 282 LEU   A CD1 1 
ATOM   2210 C  CD2 . LEU   A 1 285 ? 47.77000 14.95600 16.76400 1.000 52.64517  ? 282 LEU   A CD2 1 
ATOM   2211 N  N   . TYR   A 1 286 ? 43.40400 16.95900 17.03000 1.000 49.51521  ? 283 TYR   A N   1 
ATOM   2212 C  CA  . TYR   A 1 286 ? 42.18200 17.69800 16.75300 1.000 42.21929  ? 283 TYR   A CA  1 
ATOM   2213 C  C   . TYR   A 1 286 ? 42.38900 18.58100 15.52700 1.000 44.25873  ? 283 TYR   A C   1 
ATOM   2214 O  O   . TYR   A 1 286 ? 43.48100 19.12600 15.31600 1.000 42.07816  ? 283 TYR   A O   1 
ATOM   2215 C  CB  . TYR   A 1 286 ? 41.78500 18.55700 17.95400 1.000 46.16442  ? 283 TYR   A CB  1 
ATOM   2216 C  CG  . TYR   A 1 286 ? 41.17900 17.78700 19.09900 1.000 49.58623  ? 283 TYR   A CG  1 
ATOM   2217 C  CD1 . TYR   A 1 286 ? 39.82400 17.50700 19.12300 1.000 54.83956  ? 283 TYR   A CD1 1 
ATOM   2218 C  CD2 . TYR   A 1 286 ? 41.96100 17.34100 20.16000 1.000 52.09855  ? 283 TYR   A CD2 1 
ATOM   2219 C  CE1 . TYR   A 1 286 ? 39.25900 16.81100 20.16200 1.000 52.03206  ? 283 TYR   A CE1 1 
ATOM   2220 C  CE2 . TYR   A 1 286 ? 41.39900 16.63400 21.22100 1.000 45.55717  ? 283 TYR   A CE2 1 
ATOM   2221 C  CZ  . TYR   A 1 286 ? 40.05100 16.37700 21.20400 1.000 55.60117  ? 283 TYR   A CZ  1 
ATOM   2222 O  OH  . TYR   A 1 286 ? 39.46400 15.69500 22.22600 1.000 58.25840  ? 283 TYR   A OH  1 
ATOM   2223 N  N   . CYS   A 1 287 ? 41.34700 18.70000 14.70900 1.000 44.24195  ? 284 CYS   A N   1 
ATOM   2224 C  CA  . CYS   A 1 287 ? 41.35000 19.58600 13.55100 1.000 37.30266  ? 284 CYS   A CA  1 
ATOM   2225 C  C   . CYS   A 1 287 ? 40.27800 20.64000 13.76400 1.000 45.40428  ? 284 CYS   A C   1 
ATOM   2226 O  O   . CYS   A 1 287 ? 39.09900 20.30900 13.94500 1.000 45.10354  ? 284 CYS   A O   1 
ATOM   2227 C  CB  . CYS   A 1 287 ? 41.09800 18.82900 12.25000 1.000 47.88382  ? 284 CYS   A CB  1 
ATOM   2228 S  SG  . CYS   A 1 287 ? 40.95800 19.91800 10.78200 1.000 51.90956  ? 284 CYS   A SG  1 
ATOM   2229 N  N   . ILE   A 1 288 ? 40.69300 21.90100 13.78200 1.000 47.48300  ? 285 ILE   A N   1 
ATOM   2230 C  CA  . ILE   A 1 288 ? 39.79800 23.02500 14.02000 1.000 40.95646  ? 285 ILE   A CA  1 
ATOM   2231 C  C   . ILE   A 1 288 ? 39.66300 23.77500 12.70800 1.000 47.24176  ? 285 ILE   A C   1 
ATOM   2232 O  O   . ILE   A 1 288 ? 40.65600 24.28100 12.16700 1.000 50.42925  ? 285 ILE   A O   1 
ATOM   2233 C  CB  . ILE   A 1 288 ? 40.32300 23.93400 15.14000 1.000 41.67557  ? 285 ILE   A CB  1 
ATOM   2234 C  CG1 . ILE   A 1 288 ? 40.48500 23.11800 16.42200 1.000 38.64696  ? 285 ILE   A CG1 1 
ATOM   2235 C  CG2 . ILE   A 1 288 ? 39.41300 25.12700 15.33500 1.000 42.99343  ? 285 ILE   A CG2 1 
ATOM   2236 C  CD1 . ILE   A 1 288 ? 40.93500 23.92500 17.61800 1.000 39.29036  ? 285 ILE   A CD1 1 
ATOM   2237 N  N   . ASP   A 1 289 ? 38.44600 23.80700 12.17900 1.000 46.19065  ? 286 ASP   A N   1 
ATOM   2238 C  CA  . ASP   A 1 289 ? 38.11300 24.50100 10.93900 1.000 41.98546  ? 286 ASP   A CA  1 
ATOM   2239 C  C   . ASP   A 1 289 ? 37.09000 25.57200 11.28800 1.000 45.12258  ? 286 ASP   A C   1 
ATOM   2240 O  O   . ASP   A 1 289 ? 35.88700 25.34300 11.19600 1.000 50.75585  ? 286 ASP   A O   1 
ATOM   2241 C  CB  . ASP   A 1 289 ? 37.57300 23.51900 9.87100  1.000 46.89722  ? 286 ASP   A CB  1 
ATOM   2242 C  CG  . ASP   A 1 289 ? 37.36900 24.18100 8.50900  1.000 60.45862  ? 286 ASP   A CG  1 
ATOM   2243 O  OD1 . ASP   A 1 289 ? 37.75000 25.36000 8.34200  1.000 55.26530  ? 286 ASP   A OD1 1 
ATOM   2244 O  OD2 . ASP   A 1 289 ? 36.84300 23.50400 7.59400  1.000 69.40814  ? 286 ASP   A OD2 1 
ATOM   2245 N  N   . GLY   A 1 290 ? 37.57400 26.74700 11.68600 1.000 44.56827  ? 287 GLY   A N   1 
ATOM   2246 C  CA  . GLY   A 1 290 ? 36.68800 27.77200 12.20600 1.000 40.40296  ? 287 GLY   A CA  1 
ATOM   2247 C  C   . GLY   A 1 290 ? 35.87300 27.31000 13.40100 1.000 44.91332  ? 287 GLY   A C   1 
ATOM   2248 O  O   . GLY   A 1 290 ? 36.41600 27.18000 14.50000 1.000 52.85058  ? 287 GLY   A O   1 
ATOM   2249 N  N   . ALA   A 1 291 ? 34.57500 27.05200 13.21000 1.000 46.98414  ? 288 ALA   A N   1 
ATOM   2250 C  CA  . ALA   A 1 291 ? 33.71600 26.57100 14.28900 1.000 57.83829  ? 288 ALA   A CA  1 
ATOM   2251 C  C   . ALA   A 1 291 ? 33.61700 25.05100 14.34700 1.000 49.16818  ? 288 ALA   A C   1 
ATOM   2252 O  O   . ALA   A 1 291 ? 33.01400 24.52700 15.28700 1.000 63.35182  ? 288 ALA   A O   1 
ATOM   2253 C  CB  . ALA   A 1 291 ? 32.30100 27.15500 14.15900 1.000 43.67357  ? 288 ALA   A CB  1 
ATOM   2254 N  N   . LEU   A 1 292 ? 34.19600 24.34300 13.38000 1.000 48.90871  ? 289 LEU   A N   1 
ATOM   2255 C  CA  . LEU   A 1 292 ? 34.07300 22.89700 13.24400 1.000 53.38783  ? 289 LEU   A CA  1 
ATOM   2256 C  C   . LEU   A 1 292 ? 35.26500 22.18900 13.87200 1.000 52.98223  ? 289 LEU   A C   1 
ATOM   2257 O  O   . LEU   A 1 292 ? 36.41100 22.62300 13.71900 1.000 48.54706  ? 289 LEU   A O   1 
ATOM   2258 C  CB  . LEU   A 1 292 ? 33.98800 22.49300 11.76800 1.000 48.64119  ? 289 LEU   A CB  1 
ATOM   2259 C  CG  . LEU   A 1 292 ? 32.91300 23.15700 10.92500 1.000 56.87623  ? 289 LEU   A CG  1 
ATOM   2260 C  CD1 . LEU   A 1 292 ? 33.00800 22.65300 9.50000  1.000 56.58877  ? 289 LEU   A CD1 1 
ATOM   2261 C  CD2 . LEU   A 1 292 ? 31.55500 22.87600 11.53600 1.000 61.23273  ? 289 LEU   A CD2 1 
ATOM   2262 N  N   . LEU   A 1 293 ? 34.98800 21.06800 14.53200 1.000 51.23292  ? 290 LEU   A N   1 
ATOM   2263 C  CA  . LEU   A 1 293 ? 35.98400 20.30800 15.27800 1.000 52.84780  ? 290 LEU   A CA  1 
ATOM   2264 C  C   . LEU   A 1 293 ? 35.86700 18.83600 14.90800 1.000 57.49722  ? 290 LEU   A C   1 
ATOM   2265 O  O   . LEU   A 1 293 ? 34.78400 18.25400 15.02800 1.000 55.59389  ? 290 LEU   A O   1 
ATOM   2266 C  CB  . LEU   A 1 293 ? 35.78800 20.48700 16.79200 1.000 46.63208  ? 290 LEU   A CB  1 
ATOM   2267 C  CG  . LEU   A 1 293 ? 36.79200 19.76300 17.69000 1.000 47.72733  ? 290 LEU   A CG  1 
ATOM   2268 C  CD1 . LEU   A 1 293 ? 38.19700 20.23300 17.37400 1.000 46.79616  ? 290 LEU   A CD1 1 
ATOM   2269 C  CD2 . LEU   A 1 293 ? 36.47400 19.98200 19.14900 1.000 42.44112  ? 290 LEU   A CD2 1 
ATOM   2270 N  N   . THR   A 1 294 ? 36.96800 18.24400 14.44300 1.000 49.59517  ? 291 THR   A N   1 
ATOM   2271 C  CA  . THR   A 1 294 ? 37.06100 16.80600 14.22400 1.000 49.96013  ? 291 THR   A CA  1 
ATOM   2272 C  C   . THR   A 1 294 ? 38.30900 16.29200 14.93500 1.000 57.15243  ? 291 THR   A C   1 
ATOM   2273 O  O   . THR   A 1 294 ? 39.23100 17.05600 15.23000 1.000 58.67916  ? 291 THR   A O   1 
ATOM   2274 C  CB  . THR   A 1 294 ? 37.10100 16.44000 12.72000 1.000 57.77157  ? 291 THR   A CB  1 
ATOM   2275 O  OG1 . THR   A 1 294 ? 38.20000 17.09400 12.07900 1.000 54.62484  ? 291 THR   A OG1 1 
ATOM   2276 C  CG2 . THR   A 1 294 ? 35.81300 16.86700 12.02400 1.000 47.60782  ? 291 THR   A CG2 1 
ATOM   2277 N  N   . LYS   A 1 295 ? 38.31900 14.99100 15.24200 1.000 56.98752  ? 292 LYS   A N   1 
ATOM   2278 C  CA  . LYS   A 1 295 ? 39.42000 14.36000 15.95800 1.000 54.55132  ? 292 LYS   A CA  1 
ATOM   2279 C  C   . LYS   A 1 295 ? 39.78200 13.05000 15.28200 1.000 51.60743  ? 292 LYS   A C   1 
ATOM   2280 O  O   . LYS   A 1 295 ? 38.94200 12.41500 14.64000 1.000 59.73114  ? 292 LYS   A O   1 
ATOM   2281 C  CB  . LYS   A 1 295 ? 39.08300 14.08900 17.43800 1.000 62.24078  ? 292 LYS   A CB  1 
ATOM   2282 C  CG  . LYS   A 1 295 ? 37.62900 13.77700 17.69500 1.000 64.39632  ? 292 LYS   A CG  1 
ATOM   2283 C  CD  . LYS   A 1 295 ? 37.35400 13.59600 19.18400 1.000 73.27985  ? 292 LYS   A CD  1 
ATOM   2284 C  CE  . LYS   A 1 295 ? 38.08500 12.39600 19.75700 1.000 69.79341  ? 292 LYS   A CE  1 
ATOM   2285 N  NZ  . LYS   A 1 295 ? 37.58700 12.06900 21.13800 1.000 79.73000  ? 292 LYS   A NZ  1 
ATOM   2286 N  N   . SER   A 1 296 ? 41.04000 12.64800 15.44200 1.000 49.47165  ? 293 SER   A N   1 
ATOM   2287 C  CA  . SER   A 1 296 ? 41.53100 11.41700 14.83500 1.000 55.95929  ? 293 SER   A CA  1 
ATOM   2288 C  C   . SER   A 1 296 ? 42.88500 11.08700 15.45100 1.000 59.10006  ? 293 SER   A C   1 
ATOM   2289 O  O   . SER   A 1 296 ? 43.60800 11.98100 15.89900 1.000 56.77642  ? 293 SER   A O   1 
ATOM   2290 C  CB  . SER   A 1 296 ? 41.64400 11.54700 13.30500 1.000 51.03091  ? 293 SER   A CB  1 
ATOM   2291 O  OG  . SER   A 1 296 ? 42.75400 12.35200 12.93000 1.000 56.48454  ? 293 SER   A OG  1 
ATOM   2292 N  N   . SER   A 1 297 ? 43.22000 9.79700  15.47300 1.000 55.36256  ? 294 SER   A N   1 
ATOM   2293 C  CA  . SER   A 1 297 ? 44.44200 9.38900  16.15400 1.000 57.01894  ? 294 SER   A CA  1 
ATOM   2294 C  C   . SER   A 1 297 ? 45.67500 9.65000  15.30900 1.000 56.61465  ? 294 SER   A C   1 
ATOM   2295 O  O   . SER   A 1 297 ? 46.76300 9.87300  15.85800 1.000 59.46397  ? 294 SER   A O   1 
ATOM   2296 C  CB  . SER   A 1 297 ? 44.36700 7.91100  16.54400 1.000 61.14097  ? 294 SER   A CB  1 
ATOM   2297 O  OG  . SER   A 1 297 ? 44.16900 7.09200  15.41000 1.000 83.79496  ? 294 SER   A OG  1 
ATOM   2298 N  N   . GLU   A 1 298 ? 45.53000 9.62700  13.98800 1.000 61.33356  ? 295 GLU   A N   1 
ATOM   2299 C  CA  . GLU   A 1 298 ? 46.60700 9.95300  13.06600 1.000 60.48305  ? 295 GLU   A CA  1 
ATOM   2300 C  C   . GLU   A 1 298 ? 46.11700 11.03500 12.11800 1.000 55.66991  ? 295 GLU   A C   1 
ATOM   2301 O  O   . GLU   A 1 298 ? 44.92100 11.32600 12.03500 1.000 53.89743  ? 295 GLU   A O   1 
ATOM   2302 C  CB  . GLU   A 1 298 ? 47.07800 8.72200  12.27700 1.000 68.01615  ? 295 GLU   A CB  1 
ATOM   2303 C  CG  . GLU   A 1 298 ? 47.17900 7.45300  13.10300 1.000 78.87911  ? 295 GLU   A CG  1 
ATOM   2304 C  CD  . GLU   A 1 298 ? 48.47400 6.71600  12.85800 1.000 101.15226 ? 295 GLU   A CD  1 
ATOM   2305 O  OE1 . GLU   A 1 298 ? 49.54100 7.35300  12.96800 1.000 102.02245 ? 295 GLU   A OE1 1 
ATOM   2306 O  OE2 . GLU   A 1 298 ? 48.42700 5.50400  12.54900 1.000 116.88890 ? 295 GLU   A OE2 1 
ATOM   2307 N  N   . TYR   A 1 299 ? 47.05900 11.64500 11.40800 1.000 55.88120  ? 296 TYR   A N   1 
ATOM   2308 C  CA  . TYR   A 1 299 ? 46.70800 12.67400 10.44500 1.000 54.30137  ? 296 TYR   A CA  1 
ATOM   2309 C  C   . TYR   A 1 299 ? 47.68400 12.64400 9.27900  1.000 61.12202  ? 296 TYR   A C   1 
ATOM   2310 O  O   . TYR   A 1 299 ? 48.90500 12.68700 9.47600  1.000 61.43943  ? 296 TYR   A O   1 
ATOM   2311 C  CB  . TYR   A 1 299 ? 46.70800 14.06500 11.08400 1.000 63.11706  ? 296 TYR   A CB  1 
ATOM   2312 C  CG  . TYR   A 1 299 ? 46.42200 15.14700 10.07900 1.000 63.27759  ? 296 TYR   A CG  1 
ATOM   2313 C  CD1 . TYR   A 1 299 ? 47.44700 15.70000 9.32500  1.000 62.42842  ? 296 TYR   A CD1 1 
ATOM   2314 C  CD2 . TYR   A 1 299 ? 45.12300 15.60100 9.86500  1.000 60.80284  ? 296 TYR   A CD2 1 
ATOM   2315 C  CE1 . TYR   A 1 299 ? 47.19800 16.67000 8.39000  1.000 61.79658  ? 296 TYR   A CE1 1 
ATOM   2316 C  CE2 . TYR   A 1 299 ? 44.86300 16.58200 8.92300  1.000 53.15882  ? 296 TYR   A CE2 1 
ATOM   2317 C  CZ  . TYR   A 1 299 ? 45.91100 17.11100 8.19300  1.000 58.18915  ? 296 TYR   A CZ  1 
ATOM   2318 O  OH  . TYR   A 1 299 ? 45.70000 18.08800 7.25200  1.000 74.80290  ? 296 TYR   A OH  1 
ATOM   2319 N  N   . LYS   A 1 300 ? 47.13800 12.60300 8.06800  1.000 55.72810  ? 297 LYS   A N   1 
ATOM   2320 C  CA  . LYS   A 1 300 ? 47.92300 12.80200 6.86000  1.000 61.71279  ? 297 LYS   A CA  1 
ATOM   2321 C  C   . LYS   A 1 300 ? 47.20400 13.83700 6.00100  1.000 60.56014  ? 297 LYS   A C   1 
ATOM   2322 O  O   . LYS   A 1 300 ? 45.99300 13.73500 5.77900  1.000 57.38290  ? 297 LYS   A O   1 
ATOM   2323 C  CB  . LYS   A 1 300 ? 48.12900 11.47700 6.11300  1.000 70.39671  ? 297 LYS   A CB  1 
ATOM   2324 C  CG  . LYS   A 1 300 ? 48.86600 11.60600 4.78300  1.000 88.32723  ? 297 LYS   A CG  1 
ATOM   2325 C  CD  . LYS   A 1 300 ? 50.27300 11.00600 4.82500  1.000 85.27707  ? 297 LYS   A CD  1 
ATOM   2326 C  CE  . LYS   A 1 300 ? 50.63800 10.35800 3.49000  1.000 88.97440  ? 297 LYS   A CE  1 
ATOM   2327 N  NZ  . LYS   A 1 300 ? 50.00800 11.05700 2.32100  1.000 81.59512  ? 297 LYS   A NZ  1 
ATOM   2328 N  N   . GLY   A 1 301 ? 47.93100 14.85500 5.55900  1.000 51.09681  ? 298 GLY   A N   1 
ATOM   2329 C  CA  . GLY   A 1 301 ? 47.31200 15.94100 4.84100  1.000 48.30572  ? 298 GLY   A CA  1 
ATOM   2330 C  C   . GLY   A 1 301 ? 48.30700 16.99900 4.41100  1.000 52.61231  ? 298 GLY   A C   1 
ATOM   2331 O  O   . GLY   A 1 301 ? 49.50200 16.93600 4.73200  1.000 48.79645  ? 298 GLY   A O   1 
ATOM   2332 N  N   . PRO   A 1 302 ? 47.82500 18.00800 3.67300  1.000 49.83398  ? 299 PRO   A N   1 
ATOM   2333 C  CA  . PRO   A 1 302 ? 48.72000 19.04800 3.14400  1.000 44.77721  ? 299 PRO   A CA  1 
ATOM   2334 C  C   . PRO   A 1 302 ? 49.01400 20.08000 4.22100  1.000 52.72598  ? 299 PRO   A C   1 
ATOM   2335 O  O   . PRO   A 1 302 ? 48.14300 20.86100 4.61700  1.000 52.45808  ? 299 PRO   A O   1 
ATOM   2336 C  CB  . PRO   A 1 302 ? 47.91500 19.63700 1.97600  1.000 43.00800  ? 299 PRO   A CB  1 
ATOM   2337 C  CG  . PRO   A 1 302 ? 46.48300 19.44200 2.37500  1.000 49.81836  ? 299 PRO   A CG  1 
ATOM   2338 C  CD  . PRO   A 1 302 ? 46.41300 18.24900 3.32800  1.000 48.75395  ? 299 PRO   A CD  1 
ATOM   2339 N  N   . ILE   A 1 303 ? 50.24500 20.06400 4.71800  1.000 40.84429  ? 300 ILE   A N   1 
ATOM   2340 C  CA  . ILE   A 1 303 ? 50.67100 20.86600 5.85800  1.000 45.02767  ? 300 ILE   A CA  1 
ATOM   2341 C  C   . ILE   A 1 303 ? 51.70400 21.85700 5.36100  1.000 45.87592  ? 300 ILE   A C   1 
ATOM   2342 O  O   . ILE   A 1 303 ? 52.54200 21.51600 4.51800  1.000 46.11283  ? 300 ILE   A O   1 
ATOM   2343 C  CB  . ILE   A 1 303 ? 51.24700 19.98000 6.98700  1.000 46.56596  ? 300 ILE   A CB  1 
ATOM   2344 C  CG1 . ILE   A 1 303 ? 50.17000 19.03300 7.53200  1.000 47.60531  ? 300 ILE   A CG1 1 
ATOM   2345 C  CG2 . ILE   A 1 303 ? 51.85200 20.81900 8.09800  1.000 41.95662  ? 300 ILE   A CG2 1 
ATOM   2346 C  CD1 . ILE   A 1 303 ? 48.95500 19.73500 8.10900  1.000 44.03944  ? 300 ILE   A CD1 1 
ATOM   2347 N  N   . THR   A 1 304 ? 51.65800 23.08100 5.89300  1.000 44.80351  ? 301 THR   A N   1 
ATOM   2348 C  CA  . THR   A 1 304 ? 52.59900 24.11000 5.48000  1.000 38.03289  ? 301 THR   A CA  1 
ATOM   2349 C  C   . THR   A 1 304 ? 53.32900 24.80100 6.62100  1.000 38.09194  ? 301 THR   A C   1 
ATOM   2350 O  O   . THR   A 1 304 ? 54.41100 25.35200 6.37600  1.000 46.16495  ? 301 THR   A O   1 
ATOM   2351 C  CB  . THR   A 1 304 ? 51.88800 25.15200 4.58900  1.000 46.54240  ? 301 THR   A CB  1 
ATOM   2352 O  OG1 . THR   A 1 304 ? 52.86300 26.02000 4.00600  1.000 38.99846  ? 301 THR   A OG1 1 
ATOM   2353 C  CG2 . THR   A 1 304 ? 50.85200 25.96600 5.36600  1.000 33.27315  ? 301 THR   A CG2 1 
ATOM   2354 N  N   . ASP   A 1 305 ? 52.81600 24.75800 7.85500  1.000 40.80039  ? 302 ASP   A N   1 
ATOM   2355 C  CA  . ASP   A 1 305 ? 53.53500 25.19200 9.05400  1.000 42.33644  ? 302 ASP   A CA  1 
ATOM   2356 C  C   . ASP   A 1 305 ? 53.39800 24.13500 10.14400 1.000 43.83496  ? 302 ASP   A C   1 
ATOM   2357 O  O   . ASP   A 1 305 ? 52.32400 23.55000 10.31500 1.000 46.84561  ? 302 ASP   A O   1 
ATOM   2358 C  CB  . ASP   A 1 305 ? 52.99300 26.51700 9.65700  1.000 39.72448  ? 302 ASP   A CB  1 
ATOM   2359 C  CG  . ASP   A 1 305 ? 52.78600 27.61600 8.60600  1.000 46.94557  ? 302 ASP   A CG  1 
ATOM   2360 O  OD1 . ASP   A 1 305 ? 53.75100 28.00100 7.90900  1.000 42.51203  ? 302 ASP   A OD1 1 
ATOM   2361 O  OD2 . ASP   A 1 305 ? 51.64800 28.11700 8.51100  1.000 46.46602  ? 302 ASP   A OD2 1 
ATOM   2362 N  N   . VAL   A 1 306 ? 54.46100 23.92800 10.91500 1.000 43.02481  ? 303 VAL   A N   1 
ATOM   2363 C  CA  . VAL   A 1 306 ? 54.40200 23.10300 12.11800 1.000 47.34429  ? 303 VAL   A CA  1 
ATOM   2364 C  C   . VAL   A 1 306 ? 55.12100 23.85000 13.23000 1.000 40.69471  ? 303 VAL   A C   1 
ATOM   2365 O  O   . VAL   A 1 306 ? 56.24200 24.33300 13.03100 1.000 47.44864  ? 303 VAL   A O   1 
ATOM   2366 C  CB  . VAL   A 1 306 ? 55.03200 21.70800 11.90800 1.000 49.33067  ? 303 VAL   A CB  1 
ATOM   2367 C  CG1 . VAL   A 1 306 ? 54.85000 20.85800 13.15100 1.000 45.20923  ? 303 VAL   A CG1 1 
ATOM   2368 C  CG2 . VAL   A 1 306 ? 54.42200 21.00100 10.69600 1.000 33.79001  ? 303 VAL   A CG2 1 
ATOM   2369 N  N   . PHE   A 1 307 ? 54.47300 23.95300 14.39400 1.000 39.73339  ? 304 PHE   A N   1 
ATOM   2370 C  CA  . PHE   A 1 307 ? 55.03300 24.59300 15.57900 1.000 48.41919  ? 304 PHE   A CA  1 
ATOM   2371 C  C   . PHE   A 1 307 ? 55.49000 23.53300 16.58100 1.000 45.39052  ? 304 PHE   A C   1 
ATOM   2372 O  O   . PHE   A 1 307 ? 54.80500 22.52700 16.78700 1.000 45.94453  ? 304 PHE   A O   1 
ATOM   2373 C  CB  . PHE   A 1 307 ? 54.00400 25.55200 16.20600 1.000 39.74904  ? 304 PHE   A CB  1 
ATOM   2374 C  CG  . PHE   A 1 307 ? 53.64500 26.70100 15.28900 1.000 47.98582  ? 304 PHE   A CG  1 
ATOM   2375 C  CD1 . PHE   A 1 307 ? 52.75000 26.51400 14.23100 1.000 46.85860  ? 304 PHE   A CD1 1 
ATOM   2376 C  CD2 . PHE   A 1 307 ? 54.26100 27.94200 15.42600 1.000 47.98379  ? 304 PHE   A CD2 1 
ATOM   2377 C  CE1 . PHE   A 1 307 ? 52.44300 27.55600 13.35200 1.000 47.24062  ? 304 PHE   A CE1 1 
ATOM   2378 C  CE2 . PHE   A 1 307 ? 53.96100 28.98800 14.55400 1.000 45.78405  ? 304 PHE   A CE2 1 
ATOM   2379 C  CZ  . PHE   A 1 307 ? 53.04500 28.78600 13.51300 1.000 47.23322  ? 304 PHE   A CZ  1 
ATOM   2380 N  N   . TYR   A 1 308 ? 56.67400 23.73800 17.16500 1.000 42.26208  ? 305 TYR   A N   1 
ATOM   2381 C  CA  . TYR   A 1 308 ? 57.22400 22.82800 18.16700 1.000 47.22776  ? 305 TYR   A CA  1 
ATOM   2382 C  C   . TYR   A 1 308 ? 57.61500 23.61300 19.40400 1.000 52.63558  ? 305 TYR   A C   1 
ATOM   2383 O  O   . TYR   A 1 308 ? 58.06600 24.75700 19.31200 1.000 47.72074  ? 305 TYR   A O   1 
ATOM   2384 C  CB  . TYR   A 1 308 ? 58.47600 22.06300 17.68000 1.000 45.27552  ? 305 TYR   A CB  1 
ATOM   2385 C  CG  . TYR   A 1 308 ? 58.29800 21.29400 16.39500 1.000 54.12706  ? 305 TYR   A CG  1 
ATOM   2386 C  CD1 . TYR   A 1 308 ? 58.38300 21.94100 15.15400 1.000 40.19110  ? 305 TYR   A CD1 1 
ATOM   2387 C  CD2 . TYR   A 1 308 ? 58.07100 19.92100 16.40700 1.000 51.18368  ? 305 TYR   A CD2 1 
ATOM   2388 C  CE1 . TYR   A 1 308 ? 58.23000 21.23900 13.96700 1.000 38.73848  ? 305 TYR   A CE1 1 
ATOM   2389 C  CE2 . TYR   A 1 308 ? 57.92800 19.20300 15.21500 1.000 45.63734  ? 305 TYR   A CE2 1 
ATOM   2390 C  CZ  . TYR   A 1 308 ? 58.00700 19.86900 14.00100 1.000 48.05063  ? 305 TYR   A CZ  1 
ATOM   2391 O  OH  . TYR   A 1 308 ? 57.85500 19.15800 12.82800 1.000 48.32540  ? 305 TYR   A OH  1 
ATOM   2392 N  N   . LYS   A 1 309 ? 57.45500 22.98100 20.56300 1.000 54.46105  ? 306 LYS   A N   1 
ATOM   2393 C  CA  . LYS   A 1 309 ? 57.96500 23.54400 21.80200 1.000 49.00697  ? 306 LYS   A CA  1 
ATOM   2394 C  C   . LYS   A 1 309 ? 59.47900 23.36300 21.89300 1.000 52.48546  ? 306 LYS   A C   1 
ATOM   2395 O  O   . LYS   A 1 309 ? 60.06100 22.45000 21.29900 1.000 51.23280  ? 306 LYS   A O   1 
ATOM   2396 C  CB  . LYS   A 1 309 ? 57.26800 22.90500 23.00400 1.000 46.32227  ? 306 LYS   A CB  1 
ATOM   2397 C  CG  . LYS   A 1 309 ? 56.01100 23.67900 23.42700 1.000 55.62796  ? 306 LYS   A CG  1 
ATOM   2398 C  CD  . LYS   A 1 309 ? 54.80200 22.75500 23.62100 1.000 62.75395  ? 306 LYS   A CD  1 
ATOM   2399 C  CE  . LYS   A 1 309 ? 53.66500 23.45700 24.34900 1.000 53.46219  ? 306 LYS   A CE  1 
ATOM   2400 N  NZ  . LYS   A 1 309 ? 53.65400 24.89000 23.95700 1.000 68.30560  ? 306 LYS   A NZ  1 
ATOM   2401 N  N   . GLU   A 1 310 ? 60.11600 24.28000 22.61400 1.000 56.32841  ? 307 GLU   A N   1 
ATOM   2402 C  CA  . GLU   A 1 310 ? 61.56300 24.29100 22.76600 1.000 63.00414  ? 307 GLU   A CA  1 
ATOM   2403 C  C   . GLU   A 1 310 ? 61.89900 25.00700 24.07000 1.000 63.97260  ? 307 GLU   A C   1 
ATOM   2404 O  O   . GLU   A 1 310 ? 61.05600 25.67600 24.67100 1.000 62.35074  ? 307 GLU   A O   1 
ATOM   2405 C  CB  . GLU   A 1 310 ? 62.24600 24.96200 21.55700 1.000 63.68316  ? 307 GLU   A CB  1 
ATOM   2406 C  CG  . GLU   A 1 310 ? 63.78000 24.87500 21.51900 1.000 61.47524  ? 307 GLU   A CG  1 
ATOM   2407 C  CD  . GLU   A 1 310 ? 64.30500 23.44700 21.68200 1.000 77.57677  ? 307 GLU   A CD  1 
ATOM   2408 O  OE1 . GLU   A 1 310 ? 64.49500 23.00500 22.84000 1.000 75.93463  ? 307 GLU   A OE1 1 
ATOM   2409 O  OE2 . GLU   A 1 310 ? 64.53100 22.76700 20.65400 1.000 69.41058  ? 307 GLU   A OE2 1 
ATOM   2410 N  N   . ASN   A 1 311 ? 63.13900 24.83800 24.51000 1.000 59.97659  ? 308 ASN   A N   1 
ATOM   2411 C  CA  . ASN   A 1 311 ? 63.65500 25.59500 25.64100 1.000 70.06643  ? 308 ASN   A CA  1 
ATOM   2412 C  C   . ASN   A 1 311 ? 65.11500 25.91500 25.36900 1.000 66.96188  ? 308 ASN   A C   1 
ATOM   2413 O  O   . ASN   A 1 311 ? 65.48700 27.07200 25.15100 1.000 68.43282  ? 308 ASN   A O   1 
ATOM   2414 C  CB  . ASN   A 1 311 ? 63.48300 24.81200 26.95900 1.000 76.89304  ? 308 ASN   A CB  1 
ATOM   2415 C  CG  . ASN   A 1 311 ? 63.89300 23.33400 26.83800 1.000 84.71038  ? 308 ASN   A CG  1 
ATOM   2416 O  OD1 . ASN   A 1 311 ? 65.07100 23.00700 26.66000 1.000 90.52184  ? 308 ASN   A OD1 1 
ATOM   2417 N  ND2 . ASN   A 1 311 ? 62.91300 22.44200 26.92600 1.000 77.22723  ? 308 ASN   A ND2 1 
ATOM   2418 N  N   . SER   A 1 312 ? 65.93300 24.87000 25.36000 1.000 75.99372  ? 309 SER   A N   1 
ATOM   2419 C  CA  . SER   A 1 312 ? 67.36400 24.96400 25.12100 1.000 80.81216  ? 309 SER   A CA  1 
ATOM   2420 C  C   . SER   A 1 312 ? 67.77700 23.64300 24.50000 1.000 68.99896  ? 309 SER   A C   1 
ATOM   2421 O  O   . SER   A 1 312 ? 67.53900 22.58200 25.08500 1.000 84.30268  ? 309 SER   A O   1 
ATOM   2422 C  CB  . SER   A 1 312 ? 68.13200 25.22800 26.41800 1.000 75.12627  ? 309 SER   A CB  1 
ATOM   2423 O  OG  . SER   A 1 312 ? 69.44700 25.67900 26.14900 1.000 80.66791  ? 309 SER   A OG  1 
ATOM   2424 N  N   . TYR   A 1 313 ? 68.35100 23.70300 23.30900 1.000 69.57264  ? 310 TYR   A N   1 
ATOM   2425 C  CA  . TYR   A 1 313 ? 68.81000 22.51600 22.61100 1.000 66.70911  ? 310 TYR   A CA  1 
ATOM   2426 C  C   . TYR   A 1 313 ? 70.22700 22.76700 22.13300 1.000 78.90846  ? 310 TYR   A C   1 
ATOM   2427 O  O   . TYR   A 1 313 ? 70.51400 23.81600 21.55000 1.000 76.35475  ? 310 TYR   A O   1 
ATOM   2428 C  CB  . TYR   A 1 313 ? 67.89200 22.16700 21.43800 1.000 68.00995  ? 310 TYR   A CB  1 
ATOM   2429 C  CG  . TYR   A 1 313 ? 68.49400 21.19800 20.44600 1.000 72.57062  ? 310 TYR   A CG  1 
ATOM   2430 C  CD1 . TYR   A 1 313 ? 68.32200 19.82500 20.59300 1.000 68.85858  ? 310 TYR   A CD1 1 
ATOM   2431 C  CD2 . TYR   A 1 313 ? 69.22700 21.65500 19.35200 1.000 74.87333  ? 310 TYR   A CD2 1 
ATOM   2432 C  CE1 . TYR   A 1 313 ? 68.86700 18.93100 19.68100 1.000 71.02473  ? 310 TYR   A CE1 1 
ATOM   2433 C  CE2 . TYR   A 1 313 ? 69.77900 20.76900 18.43900 1.000 78.89286  ? 310 TYR   A CE2 1 
ATOM   2434 C  CZ  . TYR   A 1 313 ? 69.59600 19.41100 18.61000 1.000 73.97547  ? 310 TYR   A CZ  1 
ATOM   2435 O  OH  . TYR   A 1 313 ? 70.14200 18.53300 17.70500 1.000 85.66331  ? 310 TYR   A OH  1 
ATOM   2436 N  N   . THR   A 1 314 ? 71.11100 21.81600 22.40600 1.000 82.84967  ? 311 THR   A N   1 
ATOM   2437 C  CA  . THR   A 1 314 ? 72.46800 21.82500 21.88700 1.000 76.25882  ? 311 THR   A CA  1 
ATOM   2438 C  C   . THR   A 1 314 ? 72.69000 20.50700 21.16500 1.000 84.62591  ? 311 THR   A C   1 
ATOM   2439 O  O   . THR   A 1 314 ? 72.32200 19.44500 21.68000 1.000 79.40037  ? 311 THR   A O   1 
ATOM   2440 C  CB  . THR   A 1 314 ? 73.49900 22.01300 23.00300 1.000 68.21467  ? 311 THR   A CB  1 
ATOM   2441 O  OG1 . THR   A 1 314 ? 73.29200 23.27900 23.64600 1.000 80.51071  ? 311 THR   A OG1 1 
ATOM   2442 C  CG2 . THR   A 1 314 ? 74.90500 21.95900 22.43600 1.000 79.27689  ? 311 THR   A CG2 1 
ATOM   2443 N  N   . THR   A 1 315 ? 73.25700 20.58100 19.96400 1.000 91.72426  ? 312 THR   A N   1 
ATOM   2444 C  CA  . THR   A 1 315 ? 73.46300 19.38800 19.16000 1.000 96.08848  ? 312 THR   A CA  1 
ATOM   2445 C  C   . THR   A 1 315 ? 74.58600 18.53400 19.74500 1.000 103.39030 ? 312 THR   A C   1 
ATOM   2446 O  O   . THR   A 1 315 ? 75.42800 19.00100 20.52100 1.000 91.31477  ? 312 THR   A O   1 
ATOM   2447 C  CB  . THR   A 1 315 ? 73.78100 19.76500 17.70800 1.000 93.27551  ? 312 THR   A CB  1 
ATOM   2448 O  OG1 . THR   A 1 315 ? 73.56900 18.63400 16.85100 1.000 100.12306 ? 312 THR   A OG1 1 
ATOM   2449 C  CG2 . THR   A 1 315 ? 75.22300 20.23700 17.57400 1.000 94.93642  ? 312 THR   A CG2 1 
ATOM   2450 N  N   . THR   A 1 316 ? 74.57700 17.25400 19.36900 1.000 115.03934 ? 313 THR   A N   1 
ATOM   2451 C  CA  . THR   A 1 316 ? 75.62400 16.30900 19.73500 1.000 114.57881 ? 313 THR   A CA  1 
ATOM   2452 C  C   . THR   A 1 316 ? 76.48100 15.91800 18.53300 1.000 118.54070 ? 313 THR   A C   1 
ATOM   2453 O  O   . THR   A 1 316 ? 77.10300 14.85100 18.53700 1.000 124.15426 ? 313 THR   A O   1 
ATOM   2454 C  CB  . THR   A 1 316 ? 75.01500 15.06400 20.38400 1.000 101.66855 ? 313 THR   A CB  1 
ATOM   2455 O  OG1 . THR   A 1 316 ? 74.11700 14.43700 19.46200 1.000 110.01122 ? 313 THR   A OG1 1 
ATOM   2456 C  CG2 . THR   A 1 316 ? 74.25300 15.43700 21.64900 1.000 93.17755  ? 313 THR   A CG2 1 
ATOM   2457 N  N   . ILE   A 1 317 ? 76.51400 16.75700 17.50000 1.000 120.44189 ? 314 ILE   A N   1 
ATOM   2458 C  CA  . ILE   A 1 317 ? 77.35800 16.53800 16.33100 1.000 128.62703 ? 314 ILE   A CA  1 
ATOM   2459 C  C   . ILE   A 1 317 ? 78.71500 17.17600 16.59100 1.000 134.06824 ? 314 ILE   A C   1 
ATOM   2460 O  O   . ILE   A 1 317 ? 78.79600 18.35400 16.96300 1.000 126.58919 ? 314 ILE   A O   1 
ATOM   2461 C  CB  . ILE   A 1 317 ? 76.70600 17.11800 15.06400 1.000 130.54269 ? 314 ILE   A CB  1 
ATOM   2462 C  CG1 . ILE   A 1 317 ? 75.44000 16.33700 14.70000 1.000 123.69936 ? 314 ILE   A CG1 1 
ATOM   2463 C  CG2 . ILE   A 1 317 ? 77.69100 17.11500 13.90300 1.000 126.65871 ? 314 ILE   A CG2 1 
ATOM   2464 C  CD1 . ILE   A 1 317 ? 74.57100 17.02800 13.66700 1.000 109.62676 ? 314 ILE   A CD1 1 
ATOM   2465 N  N   . LYS   A 1 318 ? 79.78000 16.40100 16.40400 1.000 144.45453 ? 315 LYS   A N   1 
ATOM   2466 C  CA  . LYS   A 1 318 ? 81.13500 16.87800 16.66400 1.000 139.56136 ? 315 LYS   A CA  1 
ATOM   2467 C  C   . LYS   A 1 318 ? 81.64500 17.73900 15.51000 1.000 138.99258 ? 315 LYS   A C   1 
ATOM   2468 O  O   . LYS   A 1 318 ? 82.20400 18.81600 15.72500 1.000 131.55170 ? 315 LYS   A O   1 
ATOM   2469 C  CB  . LYS   A 1 318 ? 82.08200 15.69700 16.90800 1.000 127.01033 ? 315 LYS   A CB  1 
ATOM   2470 O  OXT . LYS   A 1 318 ? 81.50200 17.38400 14.33800 1.000 139.19595 ? 315 LYS   A OXT 1 
HETATM 2471 C  C21 . A1BEG B 2 .   ? 53.29800 36.34200 -1.23800 1.000 45.51138  ? 401 A1BEG A C21 1 
HETATM 2472 N  N3  . A1BEG B 2 .   ? 57.13700 30.94200 0.24000  1.000 58.31514  ? 401 A1BEG A N3  1 
HETATM 2473 C  C20 . A1BEG B 2 .   ? 52.36100 35.25700 -0.74500 1.000 39.97024  ? 401 A1BEG A C20 1 
HETATM 2474 C  C18 . A1BEG B 2 .   ? 50.06600 34.88400 -0.08700 1.000 41.61963  ? 401 A1BEG A C18 1 
HETATM 2475 C  C17 . A1BEG B 2 .   ? 48.85500 35.32000 0.43600  1.000 34.10442  ? 401 A1BEG A C17 1 
HETATM 2476 C  C16 . A1BEG B 2 .   ? 47.90700 34.40600 0.85900  1.000 37.69546  ? 401 A1BEG A C16 1 
HETATM 2477 C  C15 . A1BEG B 2 .   ? 47.07700 32.07300 1.30400  1.000 34.88233  ? 401 A1BEG A C15 1 
HETATM 2478 C  C14 . A1BEG B 2 .   ? 48.12000 33.03000 0.78300  1.000 35.16686  ? 401 A1BEG A C14 1 
HETATM 2479 C  C13 . A1BEG B 2 .   ? 49.33500 32.58100 0.25500  1.000 38.18412  ? 401 A1BEG A C13 1 
HETATM 2480 C  C1  . A1BEG B 2 .   ? 58.93900 30.28000 -1.25800 1.000 77.52768  ? 401 A1BEG A C1  1 
HETATM 2481 C  C4  . A1BEG B 2 .   ? 55.86400 30.60600 0.39300  1.000 52.22677  ? 401 A1BEG A C4  1 
HETATM 2482 C  C5  . A1BEG B 2 .   ? 55.44000 29.66700 -0.56200 1.000 47.26560  ? 401 A1BEG A C5  1 
HETATM 2483 C  C7  . A1BEG B 2 .   ? 53.08400 29.31400 0.21300  1.000 40.22842  ? 401 A1BEG A C7  1 
HETATM 2484 N  N2  . A1BEG B 2 .   ? 57.55000 30.21300 -0.82400 1.000 59.68932  ? 401 A1BEG A N2  1 
HETATM 2485 C  C8  . A1BEG B 2 .   ? 51.81700 28.82400 0.01000  1.000 38.91214  ? 401 A1BEG A C8  1 
HETATM 2486 C  C12 . A1BEG B 2 .   ? 49.59400 31.11600 0.11400  1.000 43.39398  ? 401 A1BEG A C12 1 
HETATM 2487 C  C9  . A1BEG B 2 .   ? 50.69900 29.11700 0.99800  1.000 43.40318  ? 401 A1BEG A C9  1 
HETATM 2488 C  C10 . A1BEG B 2 .   ? 50.96300 28.67200 2.43700  1.000 38.97294  ? 401 A1BEG A C10 1 
HETATM 2489 C  C6  . A1BEG B 2 .   ? 54.08200 29.07600 -0.72900 1.000 42.14503  ? 401 A1BEG A C6  1 
HETATM 2490 C  C22 . A1BEG B 2 .   ? 52.72800 37.13100 -2.42800 1.000 40.29174  ? 401 A1BEG A C22 1 
HETATM 2491 C  C23 . A1BEG B 2 .   ? 51.87000 38.24400 -1.78900 1.000 44.19836  ? 401 A1BEG A C23 1 
HETATM 2492 C  C24 . A1BEG B 2 .   ? 52.01000 38.03600 -0.27200 1.000 39.18175  ? 401 A1BEG A C24 1 
HETATM 2493 C  C25 . A1BEG B 2 .   ? 51.00900 37.04700 0.28100  1.000 33.40369  ? 401 A1BEG A C25 1 
HETATM 2494 C  C27 . A1BEG B 2 .   ? 54.50100 38.34600 -0.32200 1.000 42.36609  ? 401 A1BEG A C27 1 
HETATM 2495 C  C28 . A1BEG B 2 .   ? 50.29900 33.50600 -0.17500 1.000 31.45734  ? 401 A1BEG A C28 1 
HETATM 2496 C  C30 . A1BEG B 2 .   ? 51.56700 28.06600 -1.17800 1.000 39.12584  ? 401 A1BEG A C30 1 
HETATM 2497 C  C31 . A1BEG B 2 .   ? 50.30200 27.52700 -1.52000 1.000 40.13595  ? 401 A1BEG A C31 1 
HETATM 2498 C  C32 . A1BEG B 2 .   ? 50.12700 26.83500 -2.68600 1.000 56.47283  ? 401 A1BEG A C32 1 
HETATM 2499 C  C33 . A1BEG B 2 .   ? 51.18600 26.64700 -3.56100 1.000 42.35265  ? 401 A1BEG A C33 1 
HETATM 2500 C  C34 . A1BEG B 2 .   ? 52.42600 27.15100 -3.27200 1.000 45.27051  ? 401 A1BEG A C34 1 
HETATM 2501 C  C35 . A1BEG B 2 .   ? 52.64600 27.87100 -2.07400 1.000 38.48207  ? 401 A1BEG A C35 1 
HETATM 2502 C  C37 . A1BEG B 2 .   ? 56.56900 29.44900 -1.32200 1.000 48.27537  ? 401 A1BEG A C37 1 
HETATM 2503 N  N11 . A1BEG B 2 .   ? 50.43000 30.55700 1.00200  1.000 44.60122  ? 401 A1BEG A N11 1 
HETATM 2504 N  N19 . A1BEG B 2 .   ? 51.02500 35.79900 -0.48500 1.000 40.06635  ? 401 A1BEG A N19 1 
HETATM 2505 N  N26 . A1BEG B 2 .   ? 53.37000 37.39300 -0.15900 1.000 40.16357  ? 401 A1BEG A N26 1 
HETATM 2506 N  N36 . A1BEG B 2 .   ? 53.90100 28.37800 -1.83800 1.000 46.14558  ? 401 A1BEG A N36 1 
HETATM 2507 O  O29 . A1BEG B 2 .   ? 48.99100 30.45500 -0.72300 1.000 39.14747  ? 401 A1BEG A O29 1 
HETATM 2508 C  C   . ACT   C 3 .   ? 51.51100 5.19500  9.28200  1.000 107.27517 ? 402 ACT   A C   1 
HETATM 2509 O  O   . ACT   C 3 .   ? 50.46000 5.03500  9.97200  1.000 109.27658 ? 402 ACT   A O   1 
HETATM 2510 O  OXT . ACT   C 3 .   ? 52.70000 5.35200  9.68200  1.000 103.66447 ? 402 ACT   A OXT 1 
HETATM 2511 C  CH3 . ACT   C 3 .   ? 51.33100 5.20600  7.72000  1.000 92.70078  ? 402 ACT   A CH3 1 
HETATM 2512 ZN ZN  . ZN    D 4 .   ? 81.61400 26.32800 -0.88000 1.000 146.01879 ? 403 ZN    A ZN  1 
HETATM 2513 ZN ZN  . ZN    E 4 .   ? 57.62800 48.43200 19.94000 1.000 42.46270  ? 404 ZN    A ZN  1 
HETATM 2514 ZN ZN  . ZN    F 4 .   ? 39.52300 30.64600 3.96300  1.000 65.46134  ? 405 ZN    A ZN  1 
HETATM 2515 ZN ZN  A ZN    G 4 .   ? 32.72200 41.95000 7.08900  0.730 43.95552  ? 406 ZN    A ZN  1 
HETATM 2516 ZN ZN  B ZN    G 4 .   ? 31.43200 43.43100 7.56700  0.270 46.88034  ? 406 ZN    A ZN  1 
HETATM 2517 ZN ZN  . ZN    H 4 .   ? 55.04700 47.47800 12.62700 1.000 94.42085  ? 407 ZN    A ZN  1 
HETATM 2518 ZN ZN  . ZN    I 4 .   ? 83.29100 29.57900 0.99900  1.000 167.84834 ? 408 ZN    A ZN  1 
HETATM 2519 ZN ZN  . ZN    J 4 .   ? 49.92200 8.95400  20.92600 1.000 127.31934 ? 409 ZN    A ZN  1 
HETATM 2520 ZN ZN  . ZN    K 4 .   ? 45.81400 62.44600 28.46600 1.000 200.11557 ? 410 ZN    A ZN  1 
HETATM 2521 CL CL  . CL    L 5 .   ? 56.79400 46.79700 18.63200 1.000 43.43605  ? 411 CL    A CL  1 
HETATM 2522 CL CL  . CL    M 5 .   ? 58.52200 49.99900 18.55900 1.000 45.53334  ? 412 CL    A CL  1 
HETATM 2523 CL CL  . CL    N 5 .   ? 37.48200 31.31000 5.10600  1.000 57.85641  ? 413 CL    A CL  1 
HETATM 2524 CL CL  . CL    O 5 .   ? 31.59500 41.57900 8.78300  1.000 65.26586  ? 414 CL    A CL  1 
HETATM 2525 C  C1  . EDO   P 6 .   ? 30.04300 54.39400 5.81100  1.000 72.37040  ? 415 EDO   A C1  1 
HETATM 2526 O  O1  . EDO   P 6 .   ? 30.81200 54.83000 6.94300  1.000 85.93198  ? 415 EDO   A O1  1 
HETATM 2527 C  C2  . EDO   P 6 .   ? 29.05000 53.33100 6.28000  1.000 70.23769  ? 415 EDO   A C2  1 
HETATM 2528 O  O2  . EDO   P 6 .   ? 27.95300 53.94400 6.97600  1.000 81.06299  ? 415 EDO   A O2  1 
HETATM 2529 O  O   . HOH   Q 7 .   ? 56.90700 35.17800 27.64300 1.000 76.21369  ? 501 HOH   A O   1 
HETATM 2530 O  O   . HOH   Q 7 .   ? 38.59700 53.68300 8.76400  1.000 62.53025  ? 502 HOH   A O   1 
HETATM 2531 O  O   . HOH   Q 7 .   ? 55.57600 16.21500 3.16500  1.000 58.85688  ? 503 HOH   A O   1 
HETATM 2532 O  O   . HOH   Q 7 .   ? 59.01100 44.67700 18.95300 1.000 67.32988  ? 504 HOH   A O   1 
HETATM 2533 O  O   . HOH   Q 7 .   ? 42.37300 18.03300 8.06400  1.000 66.67443  ? 505 HOH   A O   1 
HETATM 2534 O  O   . HOH   Q 7 .   ? 34.76000 33.00800 22.72900 1.000 53.74997  ? 506 HOH   A O   1 
HETATM 2535 O  O   . HOH   Q 7 .   ? 37.58000 19.29200 23.21300 1.000 62.36273  ? 507 HOH   A O   1 
HETATM 2536 O  O   . HOH   Q 7 .   ? 36.26000 24.35300 24.54300 1.000 56.37773  ? 508 HOH   A O   1 
HETATM 2537 O  O   . HOH   Q 7 .   ? 42.46200 23.21300 4.47800  1.000 52.38316  ? 509 HOH   A O   1 
HETATM 2538 O  O   . HOH   Q 7 .   ? 52.64300 39.65900 3.56100  1.000 58.10448  ? 510 HOH   A O   1 
HETATM 2539 O  O   . HOH   Q 7 .   ? 37.29000 42.75100 25.47000 1.000 82.40279  ? 511 HOH   A O   1 
HETATM 2540 O  O   . HOH   Q 7 .   ? 49.60300 61.14200 28.72900 1.000 60.21253  ? 512 HOH   A O   1 
HETATM 2541 O  O   . HOH   Q 7 .   ? 52.46800 59.31200 28.11600 1.000 80.92084  ? 513 HOH   A O   1 
HETATM 2542 O  O   . HOH   Q 7 .   ? 51.14600 29.57800 6.10200  1.000 38.14166  ? 514 HOH   A O   1 
HETATM 2543 O  O   . HOH   Q 7 .   ? 36.64900 32.23100 1.78700  1.000 61.86135  ? 515 HOH   A O   1 
HETATM 2544 O  O   . HOH   Q 7 .   ? 57.71100 36.65100 23.65600 1.000 57.40421  ? 516 HOH   A O   1 
HETATM 2545 O  O   . HOH   Q 7 .   ? 30.79100 38.61800 5.96100  1.000 74.37266  ? 517 HOH   A O   1 
HETATM 2546 O  O   . HOH   Q 7 .   ? 52.80400 47.15500 11.58200 1.000 65.90537  ? 518 HOH   A O   1 
HETATM 2547 O  O   . HOH   Q 7 .   ? 47.96500 23.98900 -2.05200 1.000 51.88078  ? 519 HOH   A O   1 
HETATM 2548 O  O   . HOH   Q 7 .   ? 39.66400 43.56300 1.35200  1.000 50.73756  ? 520 HOH   A O   1 
HETATM 2549 O  O   . HOH   Q 7 .   ? 44.76900 47.33000 7.63500  1.000 48.96888  ? 521 HOH   A O   1 
HETATM 2550 O  O   . HOH   Q 7 .   ? 54.19500 33.32700 1.83900  1.000 45.94846  ? 522 HOH   A O   1 
HETATM 2551 O  O   . HOH   Q 7 .   ? 35.07900 22.25500 21.69100 1.000 61.80786  ? 523 HOH   A O   1 
HETATM 2552 O  O   . HOH   Q 7 .   ? 37.82300 51.20200 5.38300  1.000 54.48708  ? 524 HOH   A O   1 
HETATM 2553 O  O   . HOH   Q 7 .   ? 40.85400 19.05800 5.17200  1.000 75.63395  ? 525 HOH   A O   1 
HETATM 2554 O  O   . HOH   Q 7 .   ? 61.08900 20.04800 2.73200  1.000 70.43294  ? 526 HOH   A O   1 
HETATM 2555 O  O   . HOH   Q 7 .   ? 64.11300 29.91200 6.49000  1.000 60.19131  ? 527 HOH   A O   1 
HETATM 2556 O  O   . HOH   Q 7 .   ? 36.52200 54.28100 27.77900 1.000 80.72978  ? 528 HOH   A O   1 
HETATM 2557 O  O   . HOH   Q 7 .   ? 51.86100 33.30100 24.74200 1.000 59.47560  ? 529 HOH   A O   1 
HETATM 2558 O  O   . HOH   Q 7 .   ? 40.16400 30.26200 26.27500 1.000 82.20097  ? 530 HOH   A O   1 
HETATM 2559 O  O   . HOH   Q 7 .   ? 55.53800 29.62300 28.71100 1.000 66.48590  ? 531 HOH   A O   1 
HETATM 2560 O  O   . HOH   Q 7 .   ? 49.34700 10.17900 15.72300 1.000 60.50980  ? 532 HOH   A O   1 
HETATM 2561 O  O   . HOH   Q 7 .   ? 39.18800 29.73700 1.78900  1.000 52.21648  ? 533 HOH   A O   1 
HETATM 2562 O  O   . HOH   Q 7 .   ? 62.41300 27.25000 12.97600 1.000 55.90373  ? 534 HOH   A O   1 
HETATM 2563 O  O   . HOH   Q 7 .   ? 56.91000 21.54600 -0.02700 1.000 56.57461  ? 535 HOH   A O   1 
HETATM 2564 O  O   . HOH   Q 7 .   ? 49.96000 15.83700 22.41500 1.000 45.48876  ? 536 HOH   A O   1 
HETATM 2565 O  O   . HOH   Q 7 .   ? 58.63600 29.46600 9.09900  1.000 55.31441  ? 537 HOH   A O   1 
HETATM 2566 O  O   . HOH   Q 7 .   ? 30.18100 30.98000 9.01300  1.000 75.37322  ? 538 HOH   A O   1 
HETATM 2567 O  O   . HOH   Q 7 .   ? 44.27700 46.61300 23.29000 1.000 45.40910  ? 539 HOH   A O   1 
HETATM 2568 O  O   . HOH   Q 7 .   ? 50.27200 29.60600 25.10400 1.000 70.55656  ? 540 HOH   A O   1 
HETATM 2569 O  O   . HOH   Q 7 .   ? 40.72200 41.09200 21.83200 1.000 43.38723  ? 541 HOH   A O   1 
HETATM 2570 O  O   . HOH   Q 7 .   ? 44.04100 57.01500 10.60500 1.000 55.86347  ? 542 HOH   A O   1 
HETATM 2571 O  O   . HOH   Q 7 .   ? 45.79200 47.97500 5.21000  1.000 57.01745  ? 543 HOH   A O   1 
HETATM 2572 O  O   . HOH   Q 7 .   ? 68.37400 27.04900 4.56600  1.000 83.64263  ? 544 HOH   A O   1 
HETATM 2573 O  O   . HOH   Q 7 .   ? 39.60600 39.04800 6.61600  1.000 43.06749  ? 545 HOH   A O   1 
HETATM 2574 O  O   . HOH   Q 7 .   ? 38.17000 47.45600 5.61600  1.000 55.15192  ? 546 HOH   A O   1 
HETATM 2575 O  O   . HOH   Q 7 .   ? 49.73900 20.81400 21.62800 1.000 45.26112  ? 547 HOH   A O   1 
HETATM 2576 O  O   . HOH   Q 7 .   ? 29.71200 55.36800 9.94400  1.000 80.36928  ? 548 HOH   A O   1 
HETATM 2577 O  O   . HOH   Q 7 .   ? 42.15700 45.39500 24.77400 1.000 63.72505  ? 549 HOH   A O   1 
HETATM 2578 O  O   . HOH   Q 7 .   ? 42.00800 64.59100 14.77400 1.000 66.08655  ? 550 HOH   A O   1 
HETATM 2579 O  O   . HOH   Q 7 .   ? 65.40500 23.19800 3.89300  1.000 74.03243  ? 551 HOH   A O   1 
HETATM 2580 O  O   . HOH   Q 7 .   ? 63.90800 20.17000 21.06900 1.000 61.63611  ? 552 HOH   A O   1 
HETATM 2581 O  O   . HOH   Q 7 .   ? 30.96100 37.98000 18.51300 1.000 63.86970  ? 553 HOH   A O   1 
HETATM 2582 O  O   . HOH   Q 7 .   ? 53.53100 28.40000 5.22600  1.000 39.73063  ? 554 HOH   A O   1 
HETATM 2583 O  O   . HOH   Q 7 .   ? 54.83000 59.52800 29.02800 1.000 79.66415  ? 555 HOH   A O   1 
HETATM 2584 O  O   . HOH   Q 7 .   ? 55.07300 21.30200 3.49700  1.000 50.64632  ? 556 HOH   A O   1 
HETATM 2585 O  O   . HOH   Q 7 .   ? 62.87800 40.64300 19.49900 1.000 53.16428  ? 557 HOH   A O   1 
HETATM 2586 O  O   . HOH   Q 7 .   ? 48.55200 22.97100 22.57500 1.000 55.06273  ? 558 HOH   A O   1 
HETATM 2587 O  O   . HOH   Q 7 .   ? 41.44800 38.81600 30.48700 1.000 47.94681  ? 559 HOH   A O   1 
HETATM 2588 O  O   . HOH   Q 7 .   ? 32.44000 34.92600 12.22500 1.000 47.45467  ? 560 HOH   A O   1 
HETATM 2589 O  O   . HOH   Q 7 .   ? 54.18800 30.45800 3.62100  1.000 39.87771  ? 561 HOH   A O   1 
HETATM 2590 O  O   . HOH   Q 7 .   ? 63.31100 39.92000 16.01700 1.000 84.37696  ? 562 HOH   A O   1 
HETATM 2591 O  O   . HOH   Q 7 .   ? 35.06700 34.29400 3.05700  1.000 68.41296  ? 563 HOH   A O   1 
HETATM 2592 O  O   . HOH   Q 7 .   ? 30.75500 46.07800 7.71900  1.000 54.81585  ? 564 HOH   A O   1 
HETATM 2593 O  O   . HOH   Q 7 .   ? 49.07200 55.30400 26.01200 1.000 48.24987  ? 565 HOH   A O   1 
HETATM 2594 O  O   . HOH   Q 7 .   ? 34.36600 48.78900 20.19500 1.000 81.56282  ? 566 HOH   A O   1 
HETATM 2595 O  O   . HOH   Q 7 .   ? 50.34500 52.53900 6.45900  1.000 65.08327  ? 567 HOH   A O   1 
HETATM 2596 O  O   . HOH   Q 7 .   ? 52.84500 51.41100 9.71500  1.000 77.56752  ? 568 HOH   A O   1 
HETATM 2597 O  O   . HOH   Q 7 .   ? 48.79500 43.45600 29.54500 1.000 63.14280  ? 569 HOH   A O   1 
HETATM 2598 O  O   . HOH   Q 7 .   ? 44.39500 12.23500 7.90900  1.000 65.30789  ? 570 HOH   A O   1 
HETATM 2599 O  O   . HOH   Q 7 .   ? 42.16700 39.65900 5.71600  1.000 40.12281  ? 571 HOH   A O   1 
HETATM 2600 O  O   . HOH   Q 7 .   ? 44.26700 58.91400 24.94700 1.000 58.35669  ? 572 HOH   A O   1 
HETATM 2601 O  O   . HOH   Q 7 .   ? 52.71000 23.54000 -2.68200 1.000 54.77849  ? 573 HOH   A O   1 
HETATM 2602 O  O   . HOH   Q 7 .   ? 45.34500 21.29300 -2.10900 1.000 64.22641  ? 574 HOH   A O   1 
HETATM 2603 O  O   . HOH   Q 7 .   ? 48.87400 26.57700 12.90000 1.000 41.46477  ? 575 HOH   A O   1 
HETATM 2604 O  O   . HOH   Q 7 .   ? 31.41200 35.05100 19.68600 1.000 60.48034  ? 576 HOH   A O   1 
HETATM 2605 O  O   . HOH   Q 7 .   ? 54.99800 51.21000 25.73000 1.000 52.18201  ? 577 HOH   A O   1 
HETATM 2606 O  O   . HOH   Q 7 .   ? 46.17300 45.91800 2.03400  1.000 66.57819  ? 578 HOH   A O   1 
HETATM 2607 O  O   . HOH   Q 7 .   ? 40.30100 27.24900 12.12200 1.000 47.48709  ? 579 HOH   A O   1 
HETATM 2608 O  O   . HOH   Q 7 .   ? 49.55000 38.65900 6.57800  1.000 46.62096  ? 580 HOH   A O   1 
HETATM 2609 O  O   . HOH   Q 7 .   ? 39.65000 12.04800 23.57900 1.000 68.79671  ? 581 HOH   A O   1 
HETATM 2610 O  O   . HOH   Q 7 .   ? 66.00100 16.47300 20.12500 1.000 74.84055  ? 582 HOH   A O   1 
HETATM 2611 O  O   . HOH   Q 7 .   ? 42.27500 47.90100 7.77100  1.000 40.83972  ? 583 HOH   A O   1 
HETATM 2612 O  O   . HOH   Q 7 .   ? 43.01300 36.71700 29.80000 1.000 51.14281  ? 584 HOH   A O   1 
HETATM 2613 O  O   . HOH   Q 7 .   ? 44.97800 44.97800 0.00000  0.50  70.31511  ? 585 HOH   A O   1 
HETATM 2614 O  O   . HOH   Q 7 .   ? 37.58600 31.04100 10.29000 1.000 40.48678  ? 586 HOH   A O   1 
HETATM 2615 O  O   . HOH   Q 7 .   ? 49.17000 65.07300 15.14700 1.000 62.43126  ? 587 HOH   A O   1 
HETATM 2616 O  O   . HOH   Q 7 .   ? 58.95100 19.07200 5.10000  1.000 54.65453  ? 588 HOH   A O   1 
HETATM 2617 O  O   . HOH   Q 7 .   ? 35.06100 49.02500 7.86400  1.000 49.99727  ? 589 HOH   A O   1 
HETATM 2618 O  O   . HOH   Q 7 .   ? 52.055   30.248   27.340   1.000 78.04653  ? 590 HOH   A O   1 
HETATM 2619 O  O   . HOH   Q 7 .   ? 43.37500 31.71400 1.37200  1.000 51.47214  ? 591 HOH   A O   1 
HETATM 2620 O  O   . HOH   Q 7 .   ? 49.85200 37.37700 4.07600  1.000 42.55325  ? 592 HOH   A O   1 
HETATM 2621 O  O   . HOH   Q 7 .   ? 52.37500 61.04500 13.27600 1.000 70.71522  ? 593 HOH   A O   1 
HETATM 2622 O  O   . HOH   Q 7 .   ? 55.84300 28.01200 23.51700 1.000 43.32469  ? 594 HOH   A O   1 
HETATM 2623 O  O   . HOH   Q 7 .   ? 51.93200 58.74600 17.52900 1.000 58.54657  ? 595 HOH   A O   1 
HETATM 2624 O  O   . HOH   Q 7 .   ? 40.12500 27.47600 9.62900  1.000 60.01135  ? 596 HOH   A O   1 
HETATM 2625 O  O   . HOH   Q 7 .   ? 60.42600 16.89200 13.78100 1.000 54.46243  ? 597 HOH   A O   1 
HETATM 2626 O  O   . HOH   Q 7 .   ? 31.80700 25.88500 17.50000 1.000 63.69954  ? 598 HOH   A O   1 
HETATM 2627 O  O   . HOH   Q 7 .   ? 31.94900 36.07200 4.50500  1.000 62.12140  ? 599 HOH   A O   1 
HETATM 2628 O  O   . HOH   Q 7 .   ? 55.52200 48.77400 15.98900 1.000 62.99564  ? 600 HOH   A O   1 
HETATM 2629 O  O   . HOH   Q 7 .   ? 50.67600 24.61000 23.98000 1.000 52.94023  ? 601 HOH   A O   1 
HETATM 2630 O  O   . HOH   Q 7 .   ? 34.04900 24.46000 23.56100 1.000 73.58585  ? 602 HOH   A O   1 
HETATM 2631 O  O   . HOH   Q 7 .   ? 64.07700 29.44200 25.94400 1.000 60.01351  ? 603 HOH   A O   1 
HETATM 2632 O  O   . HOH   Q 7 .   ? 40.28700 31.79500 -0.45600 1.000 64.59210  ? 604 HOH   A O   1 
HETATM 2633 O  O   . HOH   Q 7 .   ? 62.909   43.646   20.762   1.000 67.48814  ? 605 HOH   A O   1 
HETATM 2634 O  O   . HOH   Q 7 .   ? 47.40700 21.72800 -0.75000 1.000 57.30053  ? 606 HOH   A O   1 
HETATM 2635 O  O   . HOH   Q 7 .   ? 40.88600 10.19600 18.34600 1.000 64.89114  ? 607 HOH   A O   1 
HETATM 2636 O  O   . HOH   Q 7 .   ? 47.20400 9.72800  24.06900 1.000 70.56193  ? 608 HOH   A O   1 
HETATM 2637 O  O   . HOH   Q 7 .   ? 64.06600 45.17500 23.88700 1.000 62.27320  ? 609 HOH   A O   1 
HETATM 2638 O  O   . HOH   Q 7 .   ? 49.37500 58.27000 30.94400 1.000 81.59973  ? 610 HOH   A O   1 
HETATM 2639 O  O   . HOH   Q 7 .   ? 51.02000 48.98700 10.22900 1.000 61.97956  ? 611 HOH   A O   1 
HETATM 2640 O  O   . HOH   Q 7 .   ? 54.36200 43.10200 27.30200 1.000 65.74798  ? 612 HOH   A O   1 
HETATM 2641 O  O   . HOH   Q 7 .   ? 65.07700 20.36400 23.89000 1.000 77.56230  ? 613 HOH   A O   1 
HETATM 2642 O  O   . HOH   Q 7 .   ? 57.54200 52.30600 15.49100 1.000 62.68596  ? 614 HOH   A O   1 
HETATM 2643 O  O   . HOH   Q 7 .   ? 46.88100 56.58000 13.66200 1.000 60.10445  ? 615 HOH   A O   1 
HETATM 2644 O  O   . HOH   Q 7 .   ? 35.71800 13.76900 14.75100 1.000 63.12435  ? 616 HOH   A O   1 
HETATM 2645 O  O   . HOH   Q 7 .   ? 61.36300 43.78100 15.12000 1.000 67.25844  ? 617 HOH   A O   1 
HETATM 2646 O  O   . HOH   Q 7 .   ? 56.33400 16.67200 12.61500 1.000 61.56486  ? 618 HOH   A O   1 
HETATM 2647 O  O   . HOH   Q 7 .   ? 42.45100 29.82100 25.19400 1.000 56.66645  ? 619 HOH   A O   1 
HETATM 2648 O  O   . HOH   Q 7 .   ? 40.289   29.281   -5.103   1.000 72.45016  ? 620 HOH   A O   1 
HETATM 2649 O  O   . HOH   Q 7 .   ? 42.61800 34.78100 2.79700  1.000 64.37320  ? 621 HOH   A O   1 
HETATM 2650 O  O   . HOH   Q 7 .   ? 39.24200 56.43600 8.03500  1.000 67.53692  ? 622 HOH   A O   1 
HETATM 2651 O  O   . HOH   Q 7 .   ? 42.50500 49.83500 21.69000 1.000 64.02692  ? 623 HOH   A O   1 
HETATM 2652 O  O   . HOH   Q 7 .   ? 37.54700 19.96100 11.48300 1.000 62.97446  ? 624 HOH   A O   1 
HETATM 2653 O  O   . HOH   Q 7 .   ? 61.20300 41.21600 17.70900 1.000 58.21885  ? 625 HOH   A O   1 
HETATM 2654 O  O   . HOH   Q 7 .   ? 46.14800 10.38000 18.76500 1.000 65.77448  ? 626 HOH   A O   1 
HETATM 2655 O  O   . HOH   Q 7 .   ? 37.07500 35.22900 -1.51900 1.000 53.06490  ? 627 HOH   A O   1 
HETATM 2656 O  O   . HOH   Q 7 .   ? 55.66900 17.56200 21.35800 1.000 59.16840  ? 628 HOH   A O   1 
HETATM 2657 O  O   . HOH   Q 7 .   ? 54.90100 14.89000 13.25000 1.000 52.72211  ? 629 HOH   A O   1 
HETATM 2658 O  O   . HOH   Q 7 .   ? 43.81400 32.70800 3.64900  1.000 51.85485  ? 630 HOH   A O   1 
HETATM 2659 O  O   . HOH   Q 7 .   ? 36.22800 53.06300 10.10400 1.000 56.53431  ? 631 HOH   A O   1 
HETATM 2660 O  O   . HOH   Q 7 .   ? 55.32000 12.64800 6.46200  1.000 68.53163  ? 632 HOH   A O   1 
HETATM 2661 O  O   . HOH   Q 7 .   ? 35.84500 24.43400 4.97500  1.000 59.06233  ? 633 HOH   A O   1 
HETATM 2662 O  O   . HOH   Q 7 .   ? 53.70700 66.34500 25.36500 1.000 55.92603  ? 634 HOH   A O   1 
HETATM 2663 O  O   . HOH   Q 7 .   ? 57.514   59.614   13.723   1.000 54.22951  ? 635 HOH   A O   1 
HETATM 2664 O  O   . HOH   Q 7 .   ? 56.29900 13.11200 9.32800  1.000 71.07236  ? 636 HOH   A O   1 
HETATM 2665 O  O   . HOH   Q 7 .   ? 31.56500 29.13100 22.32200 1.000 67.27426  ? 637 HOH   A O   1 
HETATM 2666 O  O   . HOH   Q 7 .   ? 62.375   19.594   27.561   1.000 79.01791  ? 638 HOH   A O   1 
HETATM 2667 O  O   . HOH   Q 7 .   ? 47.83200 27.12300 -7.21100 1.000 69.83438  ? 639 HOH   A O   1 
HETATM 2668 O  O   . HOH   Q 7 .   ? 37.65600 45.67100 3.75200  1.000 46.91442  ? 640 HOH   A O   1 
HETATM 2669 O  O   . HOH   Q 7 .   ? 37.32700 42.36300 21.52700 1.000 49.16205  ? 641 HOH   A O   1 
HETATM 2670 O  O   . HOH   Q 7 .   ? 35.00100 53.98000 20.23300 1.000 66.64378  ? 642 HOH   A O   1 
HETATM 2671 O  O   . HOH   Q 7 .   ? 33.24500 28.16500 10.77000 1.000 54.71747  ? 643 HOH   A O   1 
HETATM 2672 O  O   . HOH   Q 7 .   ? 51.21900 36.51300 26.86000 1.000 64.93203  ? 644 HOH   A O   1 
HETATM 2673 O  O   . HOH   Q 7 .   ? 47.751   48.938   29.401   1.000 70.39820  ? 645 HOH   A O   1 
HETATM 2674 O  O   . HOH   Q 7 .   ? 36.52000 20.57200 8.13900  1.000 70.15550  ? 646 HOH   A O   1 
HETATM 2675 O  O   . HOH   Q 7 .   ? 35.31100 40.03300 20.92100 1.000 52.12789  ? 647 HOH   A O   1 
HETATM 2676 O  O   . HOH   Q 7 .   ? 57.14800 36.14100 1.76800  1.000 69.14821  ? 648 HOH   A O   1 
HETATM 2677 O  O   . HOH   Q 7 .   ? 49.09400 44.26200 1.99600  1.000 73.18504  ? 649 HOH   A O   1 
HETATM 2678 O  O   . HOH   Q 7 .   ? 62.71600 36.50200 24.40900 1.000 66.46976  ? 650 HOH   A O   1 
HETATM 2679 O  O   . HOH   Q 7 .   ? 40.41900 54.83000 32.51800 1.000 74.97415  ? 651 HOH   A O   1 
HETATM 2680 O  O   . HOH   Q 7 .   ? 51.83300 33.30000 27.11100 1.000 65.54549  ? 652 HOH   A O   1 
HETATM 2681 O  O   . HOH   Q 7 .   ? 41.84200 18.82000 3.05500  1.000 72.54752  ? 653 HOH   A O   1 
HETATM 2682 O  O   . HOH   Q 7 .   ? 51.26900 62.14600 26.63600 1.000 61.16955  ? 654 HOH   A O   1 
HETATM 2683 O  O   . HOH   Q 7 .   ? 41.31600 26.82100 -4.36600 1.000 68.43306  ? 655 HOH   A O   1 
HETATM 2684 O  O   . HOH   Q 7 .   ? 32.09700 52.92200 8.97100  1.000 71.89564  ? 656 HOH   A O   1 
HETATM 2685 O  O   . HOH   Q 7 .   ? 40.09800 17.74800 7.45000  1.000 81.13600  ? 657 HOH   A O   1 
HETATM 2686 O  O   . HOH   Q 7 .   ? 53.64800 48.91000 13.87100 1.000 55.62271  ? 658 HOH   A O   1 
HETATM 2687 O  O   . HOH   Q 7 .   ? 52.15300 16.52200 -1.86600 1.000 71.59696  ? 659 HOH   A O   1 
HETATM 2688 O  O   . HOH   Q 7 .   ? 51.33100 36.08300 31.67100 1.000 60.71952  ? 660 HOH   A O   1 
HETATM 2689 O  O   . HOH   Q 7 .   ? 31.95800 20.38900 14.76600 1.000 73.18582  ? 661 HOH   A O   1 
HETATM 2690 O  O   . HOH   Q 7 .   ? 40.00500 46.38600 7.10900  1.000 41.84887  ? 662 HOH   A O   1 
HETATM 2691 O  O   . HOH   Q 7 .   ? 38.38900 46.90700 23.97900 1.000 75.19505  ? 663 HOH   A O   1 
HETATM 2692 O  O   . HOH   Q 7 .   ? 48.30500 17.51800 -1.33700 1.000 67.28786  ? 664 HOH   A O   1 
HETATM 2693 O  O   . HOH   Q 7 .   ? 59.62100 31.32200 7.36500  1.000 48.92540  ? 665 HOH   A O   1 
HETATM 2694 O  O   . HOH   Q 7 .   ? 33.595   38.830   2.124    1.000 65.82557  ? 666 HOH   A O   1 
HETATM 2695 O  O   . HOH   Q 7 .   ? 40.94500 65.31700 19.99100 1.000 74.45407  ? 667 HOH   A O   1 
HETATM 2696 O  O   . HOH   Q 7 .   ? 40.92500 8.13300  14.10800 1.000 76.37088  ? 668 HOH   A O   1 
HETATM 2697 O  O   . HOH   Q 7 .   ? 40.39000 43.85700 23.80200 1.000 61.61087  ? 669 HOH   A O   1 
HETATM 2698 O  O   . HOH   Q 7 .   ? 56.31800 20.03600 20.45200 1.000 43.53947  ? 670 HOH   A O   1 
HETATM 2699 O  O   . HOH   Q 7 .   ? 55.97800 38.95100 7.05000  1.000 57.96310  ? 671 HOH   A O   1 
HETATM 2700 O  O   . HOH   Q 7 .   ? 50.22800 69.64200 17.19100 1.000 75.22629  ? 672 HOH   A O   1 
HETATM 2701 O  O   . HOH   Q 7 .   ? 58.220   26.462   26.178   1.000 62.46286  ? 673 HOH   A O   1 
HETATM 2702 O  O   . HOH   Q 7 .   ? 59.66000 14.91300 12.54100 1.000 77.75231  ? 674 HOH   A O   1 
HETATM 2703 O  O   . HOH   Q 7 .   ? 52.75600 50.32400 11.70500 1.000 65.27957  ? 675 HOH   A O   1 
HETATM 2704 O  O   . HOH   Q 7 .   ? 69.60300 37.89800 13.33000 1.000 74.24343  ? 676 HOH   A O   1 
HETATM 2705 O  O   . HOH   Q 7 .   ? 49.16700 55.60100 30.13500 1.000 71.51479  ? 677 HOH   A O   1 
HETATM 2706 O  O   . HOH   Q 7 .   ? 61.53100 43.35000 22.66900 1.000 69.30852  ? 678 HOH   A O   1 
HETATM 2707 O  O   . HOH   Q 7 .   ? 64.52000 32.19100 24.77800 1.000 80.26699  ? 679 HOH   A O   1 
HETATM 2708 O  O   . HOH   Q 7 .   ? 37.97500 49.46000 20.96000 1.000 67.58934  ? 680 HOH   A O   1 
HETATM 2709 O  O   . HOH   Q 7 .   ? 40.44500 31.72600 3.02400  1.000 40.38897  ? 681 HOH   A O   1 
HETATM 2710 O  O   . HOH   Q 7 .   ? 41.10200 15.53100 12.40000 1.000 61.25824  ? 682 HOH   A O   1 
HETATM 2711 O  O   . HOH   Q 7 .   ? 55.39500 33.49300 -0.97400 1.000 65.65053  ? 683 HOH   A O   1 
HETATM 2712 O  O   . HOH   Q 7 .   ? 44.22800 66.25400 24.83700 1.000 75.96013  ? 684 HOH   A O   1 
HETATM 2713 O  O   . HOH   Q 7 .   ? 40.20000 48.61500 24.33700 1.000 67.39029  ? 685 HOH   A O   1 
HETATM 2714 O  O   . HOH   Q 7 .   ? 41.36300 52.69600 6.41500  1.000 64.69903  ? 686 HOH   A O   1 
HETATM 2715 O  O   . HOH   Q 7 .   ? 73.07900 30.13300 26.03600 1.000 90.30427  ? 687 HOH   A O   1 
HETATM 2716 O  O   . HOH   Q 7 .   ? 35.08900 27.45500 8.29500  1.000 63.18832  ? 688 HOH   A O   1 
HETATM 2717 O  O   . HOH   Q 7 .   ? 58.78500 34.03600 25.13600 1.000 81.74568  ? 689 HOH   A O   1 
HETATM 2718 O  O   . HOH   Q 7 .   ? 52.93400 44.97900 26.85100 1.000 58.55469  ? 690 HOH   A O   1 
HETATM 2719 O  O   . HOH   Q 7 .   ? 55.20700 56.37700 10.58300 1.000 77.38922  ? 691 HOH   A O   1 
HETATM 2720 O  O   . HOH   Q 7 .   ? 37.76800 28.74800 8.91200  1.000 53.10252  ? 692 HOH   A O   1 
HETATM 2721 O  O   . HOH   Q 7 .   ? 45.83900 9.00000  20.75300 1.000 73.71016  ? 693 HOH   A O   1 
HETATM 2722 O  O   . HOH   Q 7 .   ? 61.24000 21.01500 24.21600 1.000 72.94990  ? 694 HOH   A O   1 
HETATM 2723 O  O   . HOH   Q 7 .   ? 57.44200 48.06000 14.33100 1.000 83.44866  ? 695 HOH   A O   1 
HETATM 2724 O  O   . HOH   Q 7 .   ? 51.93300 28.09800 25.64900 1.000 65.60229  ? 696 HOH   A O   1 
HETATM 2725 O  O   . HOH   Q 7 .   ? 34.72200 45.70600 20.32000 1.000 65.09151  ? 697 HOH   A O   1 
HETATM 2726 O  O   . HOH   Q 7 .   ? 50.80200 45.21300 28.38900 1.000 61.95805  ? 698 HOH   A O   1 
HETATM 2727 O  O   . HOH   Q 7 .   ? 53.78800 56.05500 7.76800  1.000 89.49243  ? 699 HOH   A O   1 
HETATM 2728 O  O   . HOH   Q 7 .   ? 49.838   47.256   29.695   1.000 75.16664  ? 700 HOH   A O   1 
HETATM 2729 O  O   . HOH   Q 7 .   ? 54.548   66.730   15.218   1.000 68.79000  ? 701 HOH   A O   1 
HETATM 2730 O  O   . HOH   Q 7 .   ? 39.69800 49.36700 4.13000  1.000 63.22218  ? 702 HOH   A O   1 
HETATM 2731 O  O   . HOH   Q 7 .   ? 30.96600 32.44000 21.91500 1.000 78.60247  ? 703 HOH   A O   1 
HETATM 2732 O  O   . HOH   Q 7 .   ? 51.35800 44.88800 3.20000  1.000 76.14183  ? 704 HOH   A O   1 
HETATM 2733 O  O   . HOH   Q 7 .   ? 32.47800 47.56000 18.81800 1.000 79.21438  ? 705 HOH   A O   1 
HETATM 2734 O  O   . HOH   Q 7 .   ? 42.04900 16.70800 4.86800  1.000 79.95322  ? 706 HOH   A O   1 
HETATM 2735 O  O   . HOH   Q 7 .   ? 63.98300 33.73900 9.36200  1.000 65.46176  ? 707 HOH   A O   1 
HETATM 2736 O  O   . HOH   Q 7 .   ? 49.70100 26.68900 25.86000 1.000 63.96309  ? 708 HOH   A O   1 
HETATM 2737 O  O   . HOH   Q 7 .   ? 42.99400 55.69400 7.68600  1.000 64.09739  ? 709 HOH   A O   1 
HETATM 2738 O  O   . HOH   Q 7 .   ? 34.56500 51.67300 8.33500  1.000 51.24971  ? 710 HOH   A O   1 
HETATM 2739 O  O   . HOH   Q 7 .   ? 49.56600 19.82100 -1.02800 1.000 66.04445  ? 711 HOH   A O   1 
HETATM 2740 O  O   . HOH   Q 7 .   ? 52.045   68.852   25.027   1.000 59.89881  ? 712 HOH   A O   1 
HETATM 2741 O  O   . HOH   Q 7 .   ? 52.67900 9.14000  21.56500 1.000 85.13501  ? 713 HOH   A O   1 
HETATM 2742 O  O   . HOH   Q 7 .   ? 62.56400 32.13800 7.64300  1.000 55.28668  ? 714 HOH   A O   1 
HETATM 2743 O  O   . HOH   Q 7 .   ? 35.26800 27.12300 3.92900  1.000 66.68841  ? 715 HOH   A O   1 
HETATM 2744 O  O   . HOH   Q 7 .   ? 36.05600 50.91900 20.60300 1.000 74.94432  ? 716 HOH   A O   1 
HETATM 2745 O  O   . HOH   Q 7 .   ? 52.70300 52.62400 27.97700 1.000 66.57935  ? 717 HOH   A O   1 
HETATM 2746 O  O   . HOH   Q 7 .   ? 51.44400 40.20600 6.34100  1.000 71.56451  ? 718 HOH   A O   1 
HETATM 2747 O  O   . HOH   Q 7 .   ? 57.51000 36.90800 5.95500  1.000 61.59635  ? 719 HOH   A O   1 
HETATM 2748 O  O   . HOH   Q 7 .   ? 47.85200 8.23700  19.17200 1.000 72.51585  ? 720 HOH   A O   1 
HETATM 2749 O  O   . HOH   Q 7 .   ? 50.18000 52.84300 27.31500 1.000 57.13169  ? 721 HOH   A O   1 
HETATM 2750 O  O   . HOH   Q 7 .   ? 48.54800 8.09200  23.28100 1.000 70.65699  ? 722 HOH   A O   1 
HETATM 2751 O  O   . HOH   Q 7 .   ? 29.91900 31.96800 19.19100 1.000 70.13128  ? 723 HOH   A O   1 
HETATM 2752 O  O   . HOH   Q 7 .   ? 41.73000 49.91000 5.82900  1.000 55.53469  ? 724 HOH   A O   1 
HETATM 2753 O  O   . HOH   Q 7 .   ? 50.45500 23.30600 -3.31800 1.000 54.18626  ? 725 HOH   A O   1 
HETATM 2754 O  O   . HOH   Q 7 .   ? 51.450   14.006   24.502   1.000 61.67852  ? 726 HOH   A O   1 
HETATM 2755 O  O   . HOH   Q 7 .   ? 35.97200 27.84000 1.89800  1.000 82.66316  ? 727 HOH   A O   1 
HETATM 2756 O  O   . HOH   Q 7 .   ? 55.48000 46.19700 10.43000 1.000 75.78379  ? 728 HOH   A O   1 
HETATM 2757 O  O   . HOH   Q 7 .   ? 49.14000 57.96800 15.65800 1.000 70.26194  ? 729 HOH   A O   1 
HETATM 2758 O  O   . HOH   Q 7 .   ? 44.04000 54.30500 5.93200  1.000 83.75710  ? 730 HOH   A O   1 
HETATM 2759 O  O   . HOH   Q 7 .   ? 45.63800 53.18700 4.56300  1.000 63.53932  ? 731 HOH   A O   1 
HETATM 2760 O  O   . HOH   Q 7 .   ? 51.07500 34.84500 28.81900 1.000 60.76979  ? 732 HOH   A O   1 
HETATM 2761 O  O   . HOH   Q 7 .   ? 46.61500 46.61500 0.00000  0.50  87.08131  ? 733 HOH   A O   1 
HETATM 2762 O  O   . HOH   Q 7 .   ? 58.11700 19.87900 1.30700  1.000 68.15959  ? 734 HOH   A O   1 
HETATM 2763 O  O   . HOH   Q 7 .   ? 53.71300 61.13500 16.02500 1.000 62.18822  ? 735 HOH   A O   1 
HETATM 2764 O  O   . HOH   Q 7 .   ? 53.21400 63.99900 26.65400 1.000 55.12560  ? 736 HOH   A O   1 
HETATM 2765 O  O   . HOH   Q 7 .   ? 30.20500 38.66100 8.89500  1.000 71.78715  ? 737 HOH   A O   1 
HETATM 2766 O  O   . HOH   Q 7 .   ? 56.22500 49.98000 12.08700 1.000 76.33325  ? 738 HOH   A O   1 
HETATM 2767 O  O   . HOH   Q 7 .   ? 44.20700 50.10100 4.39100  1.000 53.72946  ? 739 HOH   A O   1 
HETATM 2768 O  O   . HOH   Q 7 .   ? 50.93100 59.91900 30.47200 1.000 81.98055  ? 740 HOH   A O   1 
HETATM 2769 O  O   . HOH   Q 7 .   ? 24.170   54.883   4.294    1.000 69.02781  ? 741 HOH   A O   1 
HETATM 2770 O  O   . HOH   Q 7 .   ? 56.83700 18.91000 3.45800  1.000 54.30041  ? 742 HOH   A O   1 
HETATM 2771 O  O   . HOH   Q 7 .   ? 29.61900 29.01900 20.36700 1.000 74.32700  ? 743 HOH   A O   1 
HETATM 2772 O  O   . HOH   Q 7 .   ? 29.76800 27.62800 17.22600 1.000 74.27134  ? 744 HOH   A O   1 
HETATM 2773 O  O   . HOH   Q 7 .   ? 49.13500 50.95500 28.78100 1.000 63.67984  ? 745 HOH   A O   1 
HETATM 2774 O  O   . HOH   Q 7 .   ? 29.85300 29.93800 15.74100 1.000 70.93963  ? 746 HOH   A O   1 
HETATM 2775 O  O   . HOH   Q 7 .   ? 33.85200 27.42400 1.31000  1.000 82.68317  ? 747 HOH   A O   1 
HETATM 2776 O  O   . HOH   Q 7 .   ? 32.34500 26.52800 2.65700  1.000 88.81031  ? 748 HOH   A O   1 
# 
