data_9DO1
# 
_entry.id   9DO1 
# 
_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   9DO1         pdb_00009do1 10.2210/pdb9do1/pdb 
WWPDB D_1000288539 ?            ?                   
# 
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                        9DO1 
_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-N-{(1R)-1-[(2M)-2-(1-methyl-1H-pyrazol-4-yl)quinolin-4-yl]ethyl}-5-{[(2R)-1-methylpyrrolidin-2-yl]methoxy}benzamide' 
483.605   1   ?                  ? ? ? 
3 non-polymer syn 'DI(HYDROXYETHYL)ETHER' 106.120   1   ?                  ? ? ? 
4 non-polymer syn 'ZINC ION' 65.409    6   ?                  ? ? ? 
5 non-polymer syn 'CHLORIDE ION' 35.453    5   ?                  ? ? ? 
6 water       nat water 18.015    206 ?                  ? ? ? 
# 
_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-N-{(1R)-1-[(2M)-2-(1-methyl-1H-pyrazol-4-yl)quinolin-4-yl]ethyl}-5-{[(2R)-1-methylpyrrolidin-2-yl]methoxy}benzamide' 
A1BF2 
3 'DI(HYDROXYETHYL)ETHER'                                                                                                        
PEG   
4 'ZINC ION'                                                                                                                     
ZN    
5 'CHLORIDE ION'                                                                                                                 
CL    
6 water                                                                                                                          
HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   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 
A1BF2 non-polymer         . 
'2-methyl-N-{(1R)-1-[(2M)-2-(1-methyl-1H-pyrazol-4-yl)quinolin-4-yl]ethyl}-5-{[(2R)-1-methylpyrrolidin-2-yl]methoxy}benzamide' ? 
'C29 H33 N5 O2'  483.605 
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 
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 
PEG   non-polymer         . 'DI(HYDROXYETHYL)ETHER' ? 'C4 H10 O3'      106.120 
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 231 228 228 LYS LYS 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        A1BF2 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BF2 
_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 A1BF2 1   401 402 A1BF2 LIG A . 
C 3 PEG   1   402 403 PEG   PEG A . 
D 4 ZN    1   403 1   ZN    ZN  A . 
E 4 ZN    1   404 2   ZN    ZN  A . 
F 4 ZN    1   405 3   ZN    ZN  A . 
G 4 ZN    1   406 6   ZN    ZN  A . 
H 4 ZN    1   407 7   ZN    ZN  A . 
I 4 ZN    1   408 8   ZN    ZN  A . 
J 5 CL    1   409 1   CL    CL  A . 
K 5 CL    1   410 2   CL    CL  A . 
L 5 CL    1   411 4   CL    CL  A . 
M 5 CL    1   412 5   CL    CL  A . 
N 5 CL    1   413 6   CL    CL  A . 
O 6 HOH   1   501 5   HOH   HOH A . 
O 6 HOH   2   502 4   HOH   HOH A . 
O 6 HOH   3   503 10  HOH   HOH A . 
O 6 HOH   4   504 12  HOH   HOH A . 
O 6 HOH   5   505 159 HOH   HOH A . 
O 6 HOH   6   506 28  HOH   HOH A . 
O 6 HOH   7   507 192 HOH   HOH A . 
O 6 HOH   8   508 154 HOH   HOH A . 
O 6 HOH   9   509 126 HOH   HOH A . 
O 6 HOH   10  510 20  HOH   HOH A . 
O 6 HOH   11  511 229 HOH   HOH A . 
O 6 HOH   12  512 45  HOH   HOH A . 
O 6 HOH   13  513 36  HOH   HOH A . 
O 6 HOH   14  514 119 HOH   HOH A . 
O 6 HOH   15  515 37  HOH   HOH A . 
O 6 HOH   16  516 11  HOH   HOH A . 
O 6 HOH   17  517 27  HOH   HOH A . 
O 6 HOH   18  518 193 HOH   HOH A . 
O 6 HOH   19  519 208 HOH   HOH A . 
O 6 HOH   20  520 7   HOH   HOH A . 
O 6 HOH   21  521 39  HOH   HOH A . 
O 6 HOH   22  522 67  HOH   HOH A . 
O 6 HOH   23  523 198 HOH   HOH A . 
O 6 HOH   24  524 1   HOH   HOH A . 
O 6 HOH   25  525 199 HOH   HOH A . 
O 6 HOH   26  526 78  HOH   HOH A . 
O 6 HOH   27  527 200 HOH   HOH A . 
O 6 HOH   28  528 35  HOH   HOH A . 
O 6 HOH   29  529 22  HOH   HOH A . 
O 6 HOH   30  530 56  HOH   HOH A . 
O 6 HOH   31  531 8   HOH   HOH A . 
O 6 HOH   32  532 88  HOH   HOH A . 
O 6 HOH   33  533 182 HOH   HOH A . 
O 6 HOH   34  534 185 HOH   HOH A . 
O 6 HOH   35  535 197 HOH   HOH A . 
O 6 HOH   36  536 41  HOH   HOH A . 
O 6 HOH   37  537 220 HOH   HOH A . 
O 6 HOH   38  538 62  HOH   HOH A . 
O 6 HOH   39  539 26  HOH   HOH A . 
O 6 HOH   40  540 141 HOH   HOH A . 
O 6 HOH   41  541 194 HOH   HOH A . 
O 6 HOH   42  542 151 HOH   HOH A . 
O 6 HOH   43  543 123 HOH   HOH A . 
O 6 HOH   44  544 2   HOH   HOH A . 
O 6 HOH   45  545 43  HOH   HOH A . 
O 6 HOH   46  546 235 HOH   HOH A . 
O 6 HOH   47  547 223 HOH   HOH A . 
O 6 HOH   48  548 21  HOH   HOH A . 
O 6 HOH   49  549 155 HOH   HOH A . 
O 6 HOH   50  550 153 HOH   HOH A . 
O 6 HOH   51  551 63  HOH   HOH A . 
O 6 HOH   52  552 231 HOH   HOH A . 
O 6 HOH   53  553 134 HOH   HOH A . 
O 6 HOH   54  554 18  HOH   HOH A . 
O 6 HOH   55  555 142 HOH   HOH A . 
O 6 HOH   56  556 64  HOH   HOH A . 
O 6 HOH   57  557 24  HOH   HOH A . 
O 6 HOH   58  558 40  HOH   HOH A . 
O 6 HOH   59  559 124 HOH   HOH A . 
O 6 HOH   60  560 25  HOH   HOH A . 
O 6 HOH   61  561 114 HOH   HOH A . 
O 6 HOH   62  562 30  HOH   HOH A . 
O 6 HOH   63  563 54  HOH   HOH A . 
O 6 HOH   64  564 125 HOH   HOH A . 
O 6 HOH   65  565 60  HOH   HOH A . 
O 6 HOH   66  566 204 HOH   HOH A . 
O 6 HOH   67  567 135 HOH   HOH A . 
O 6 HOH   68  568 74  HOH   HOH A . 
O 6 HOH   69  569 14  HOH   HOH A . 
O 6 HOH   70  570 23  HOH   HOH A . 
O 6 HOH   71  571 33  HOH   HOH A . 
O 6 HOH   72  572 129 HOH   HOH A . 
O 6 HOH   73  573 165 HOH   HOH A . 
O 6 HOH   74  574 127 HOH   HOH A . 
O 6 HOH   75  575 49  HOH   HOH A . 
O 6 HOH   76  576 51  HOH   HOH A . 
O 6 HOH   77  577 76  HOH   HOH A . 
O 6 HOH   78  578 133 HOH   HOH A . 
O 6 HOH   79  579 190 HOH   HOH A . 
O 6 HOH   80  580 180 HOH   HOH A . 
O 6 HOH   81  581 213 HOH   HOH A . 
O 6 HOH   82  582 101 HOH   HOH A . 
O 6 HOH   83  583 42  HOH   HOH A . 
O 6 HOH   84  584 150 HOH   HOH A . 
O 6 HOH   85  585 19  HOH   HOH A . 
O 6 HOH   86  586 52  HOH   HOH A . 
O 6 HOH   87  587 121 HOH   HOH A . 
O 6 HOH   88  588 181 HOH   HOH A . 
O 6 HOH   89  589 75  HOH   HOH A . 
O 6 HOH   90  590 94  HOH   HOH A . 
O 6 HOH   91  591 6   HOH   HOH A . 
O 6 HOH   92  592 73  HOH   HOH A . 
O 6 HOH   93  593 17  HOH   HOH A . 
O 6 HOH   94  594 207 HOH   HOH A . 
O 6 HOH   95  595 77  HOH   HOH A . 
O 6 HOH   96  596 221 HOH   HOH A . 
O 6 HOH   97  597 140 HOH   HOH A . 
O 6 HOH   98  598 183 HOH   HOH A . 
O 6 HOH   99  599 66  HOH   HOH A . 
O 6 HOH   100 600 228 HOH   HOH A . 
O 6 HOH   101 601 224 HOH   HOH A . 
O 6 HOH   102 602 61  HOH   HOH A . 
O 6 HOH   103 603 57  HOH   HOH A . 
O 6 HOH   104 604 80  HOH   HOH A . 
O 6 HOH   105 605 164 HOH   HOH A . 
O 6 HOH   106 606 91  HOH   HOH A . 
O 6 HOH   107 607 203 HOH   HOH A . 
O 6 HOH   108 608 230 HOH   HOH A . 
O 6 HOH   109 609 83  HOH   HOH A . 
O 6 HOH   110 610 48  HOH   HOH A . 
O 6 HOH   111 611 29  HOH   HOH A . 
O 6 HOH   112 612 215 HOH   HOH A . 
O 6 HOH   113 613 89  HOH   HOH A . 
O 6 HOH   114 614 131 HOH   HOH A . 
O 6 HOH   115 615 219 HOH   HOH A . 
O 6 HOH   116 616 132 HOH   HOH A . 
O 6 HOH   117 617 167 HOH   HOH A . 
O 6 HOH   118 618 68  HOH   HOH A . 
O 6 HOH   119 619 3   HOH   HOH A . 
O 6 HOH   120 620 87  HOH   HOH A . 
O 6 HOH   121 621 70  HOH   HOH A . 
O 6 HOH   122 622 38  HOH   HOH A . 
O 6 HOH   123 623 58  HOH   HOH A . 
O 6 HOH   124 624 122 HOH   HOH A . 
O 6 HOH   125 625 81  HOH   HOH A . 
O 6 HOH   126 626 156 HOH   HOH A . 
O 6 HOH   127 627 34  HOH   HOH A . 
O 6 HOH   128 628 216 HOH   HOH A . 
O 6 HOH   129 629 144 HOH   HOH A . 
O 6 HOH   130 630 108 HOH   HOH A . 
O 6 HOH   131 631 53  HOH   HOH A . 
O 6 HOH   132 632 31  HOH   HOH A . 
O 6 HOH   133 633 202 HOH   HOH A . 
O 6 HOH   134 634 222 HOH   HOH A . 
O 6 HOH   135 635 82  HOH   HOH A . 
O 6 HOH   136 636 212 HOH   HOH A . 
O 6 HOH   137 637 92  HOH   HOH A . 
O 6 HOH   138 638 218 HOH   HOH A . 
O 6 HOH   139 639 160 HOH   HOH A . 
O 6 HOH   140 640 157 HOH   HOH A . 
O 6 HOH   141 641 205 HOH   HOH A . 
O 6 HOH   142 642 189 HOH   HOH A . 
O 6 HOH   143 643 46  HOH   HOH A . 
O 6 HOH   144 644 149 HOH   HOH A . 
O 6 HOH   145 645 84  HOH   HOH A . 
O 6 HOH   146 646 85  HOH   HOH A . 
O 6 HOH   147 647 178 HOH   HOH A . 
O 6 HOH   148 648 112 HOH   HOH A . 
O 6 HOH   149 649 211 HOH   HOH A . 
O 6 HOH   150 650 186 HOH   HOH A . 
O 6 HOH   151 651 115 HOH   HOH A . 
O 6 HOH   152 652 104 HOH   HOH A . 
O 6 HOH   153 653 79  HOH   HOH A . 
O 6 HOH   154 654 226 HOH   HOH A . 
O 6 HOH   155 655 161 HOH   HOH A . 
O 6 HOH   156 656 128 HOH   HOH A . 
O 6 HOH   157 657 50  HOH   HOH A . 
O 6 HOH   158 658 206 HOH   HOH A . 
O 6 HOH   159 659 232 HOH   HOH A . 
O 6 HOH   160 660 102 HOH   HOH A . 
O 6 HOH   161 661 177 HOH   HOH A . 
O 6 HOH   162 662 113 HOH   HOH A . 
O 6 HOH   163 663 175 HOH   HOH A . 
O 6 HOH   164 664 136 HOH   HOH A . 
O 6 HOH   165 665 137 HOH   HOH A . 
O 6 HOH   166 666 158 HOH   HOH A . 
O 6 HOH   167 667 225 HOH   HOH A . 
O 6 HOH   168 668 71  HOH   HOH A . 
O 6 HOH   169 669 188 HOH   HOH A . 
O 6 HOH   170 670 72  HOH   HOH A . 
O 6 HOH   171 671 110 HOH   HOH A . 
O 6 HOH   172 672 196 HOH   HOH A . 
O 6 HOH   173 673 237 HOH   HOH A . 
O 6 HOH   174 674 234 HOH   HOH A . 
O 6 HOH   175 675 109 HOH   HOH A . 
O 6 HOH   176 676 173 HOH   HOH A . 
O 6 HOH   177 677 98  HOH   HOH A . 
O 6 HOH   178 678 209 HOH   HOH A . 
O 6 HOH   179 679 95  HOH   HOH A . 
O 6 HOH   180 680 195 HOH   HOH A . 
O 6 HOH   181 681 201 HOH   HOH A . 
O 6 HOH   182 682 179 HOH   HOH A . 
O 6 HOH   183 683 55  HOH   HOH A . 
O 6 HOH   184 684 191 HOH   HOH A . 
O 6 HOH   185 685 100 HOH   HOH A . 
O 6 HOH   186 686 152 HOH   HOH A . 
O 6 HOH   187 687 130 HOH   HOH A . 
O 6 HOH   188 688 59  HOH   HOH A . 
O 6 HOH   189 689 99  HOH   HOH A . 
O 6 HOH   190 690 172 HOH   HOH A . 
O 6 HOH   191 691 174 HOH   HOH A . 
O 6 HOH   192 692 214 HOH   HOH A . 
O 6 HOH   193 693 97  HOH   HOH A . 
O 6 HOH   194 694 171 HOH   HOH A . 
O 6 HOH   195 695 217 HOH   HOH A . 
O 6 HOH   196 696 176 HOH   HOH A . 
O 6 HOH   197 697 210 HOH   HOH A . 
O 6 HOH   198 698 236 HOH   HOH A . 
O 6 HOH   199 699 106 HOH   HOH A . 
O 6 HOH   200 700 169 HOH   HOH A . 
O 6 HOH   201 701 163 HOH   HOH A . 
O 6 HOH   202 702 187 HOH   HOH A . 
O 6 HOH   203 703 168 HOH   HOH A . 
O 6 HOH   204 704 86  HOH   HOH A . 
O 6 HOH   205 705 107 HOH   HOH A . 
O 6 HOH   206 706 111 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 6   ? CG  ? A LYS 9   CG  
5  1 Y 1 A LYS 6   ? CD  ? A LYS 9   CD  
6  1 Y 1 A LYS 6   ? CE  ? A LYS 9   CE  
7  1 Y 1 A LYS 6   ? NZ  ? A LYS 9   NZ  
8  1 Y 1 A LYS 45  ? CG  ? A LYS 48  CG  
9  1 Y 1 A LYS 45  ? CD  ? A LYS 48  CD  
10 1 Y 1 A LYS 45  ? CE  ? A LYS 48  CE  
11 1 Y 1 A LYS 45  ? NZ  ? A LYS 48  NZ  
12 1 Y 1 A LYS 190 ? CG  ? A LYS 193 CG  
13 1 Y 1 A LYS 190 ? CD  ? A LYS 193 CD  
14 1 Y 1 A LYS 190 ? CE  ? A LYS 193 CE  
15 1 Y 1 A LYS 190 ? NZ  ? A LYS 193 NZ  
16 1 Y 1 A LYS 228 ? CG  ? A LYS 231 CG  
17 1 Y 1 A LYS 228 ? CD  ? A LYS 231 CD  
18 1 Y 1 A LYS 228 ? CE  ? A LYS 231 CE  
19 1 Y 1 A LYS 228 ? NZ  ? A LYS 231 NZ  
20 1 Y 1 A LYS 315 ? CG  ? A LYS 318 CG  
21 1 Y 1 A LYS 315 ? CD  ? A LYS 318 CD  
22 1 Y 1 A LYS 315 ? CE  ? A LYS 318 CE  
23 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   ? ? ? 1.21.2_5419 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                     9DO1 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     114.121 
_cell.length_a_esd                 ? 
_cell.length_b                     114.121 
_cell.length_b_esd                 ? 
_cell.length_c                     219.729 
_cell.length_c_esd                 ? 
_cell.volume                       2861663.185 
_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                         9DO1 
_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                   9DO1 
_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             4.98 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          75.28 
_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              5.8 
_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   5.6-6.5 
_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                          59.51 
_reflns.entry_id                                       9DO1 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.4 
_reflns.d_resolution_low                               34.29 
_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                                     28788 
_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                                15 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.6 
_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                                0.115 
_reflns.pdbx_Rpim_I_all                                0.041 
_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                              0.108 
_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                                    2.4 
_reflns_shell.d_res_low                                     2.49 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.3 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2974 
_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                               14.8 
_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                               2.14 
_reflns_shell.pdbx_Rpim_I_all                               0.766 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.640 
_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                                  1.99 
_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                               75.19 
_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                                 9DO1 
_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                            2.40 
_refine.ls_d_res_low                             34.29 
_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                     28749 
_refine.ls_number_reflns_R_free                  1424 
_refine.ls_number_reflns_R_work                  27325 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.94 
_refine.ls_percent_reflns_R_free                 4.95 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2099 
_refine.ls_R_factor_R_free                       0.2378 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2085 
_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                          1.33 
_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                 27.4349 
_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                            0.3301 
_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                       2.40 
_refine_hist.d_res_low                        34.29 
_refine_hist.number_atoms_solvent             206 
_refine_hist.number_atoms_total               2712 
_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        2452 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         54 
_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' ? 0.0029  ? 2584 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.5202  ? 3517 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0384  ? 386  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0034  ? 448  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 17.9851 ? 927  ? 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' 2.40 2.49  . . 143 2678 99.96  . . . . 0.3241 . . . . . . . . . . . 0.3430 
'X-RAY DIFFRACTION' 2.49 2.59  . . 147 2668 99.86  . . . . 0.3122 . . . . . . . . . . . 0.3393 
'X-RAY DIFFRACTION' 2.59 2.70  . . 140 2693 99.96  . . . . 0.2843 . . . . . . . . . . . 0.3284 
'X-RAY DIFFRACTION' 2.70 2.85  . . 154 2691 99.93  . . . . 0.2695 . . . . . . . . . . . 0.2813 
'X-RAY DIFFRACTION' 2.85 3.02  . . 136 2705 99.96  . . . . 0.2473 . . . . . . . . . . . 0.2884 
'X-RAY DIFFRACTION' 3.02 3.26  . . 134 2722 99.93  . . . . 0.2340 . . . . . . . . . . . 0.2674 
'X-RAY DIFFRACTION' 3.26 3.58  . . 141 2731 100.00 . . . . 0.2117 . . . . . . . . . . . 0.2617 
'X-RAY DIFFRACTION' 3.58 4.10  . . 127 2752 100.00 . . . . 0.1846 . . . . . . . . . . . 0.1853 
'X-RAY DIFFRACTION' 4.10 5.16  . . 148 2775 100.00 . . . . 0.1769 . . . . . . . . . . . 0.2084 
'X-RAY DIFFRACTION' 5.17 34.29 . . 154 2910 99.84  . . . . 0.1892 . . . . . . . . . . . 0.2241 
# 
_struct.entry_id                     9DO1 
_struct.title                        'SARS-CoV-2 papain-like protease (PLpro) with inhibitor Jun13307' 
_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        9DO1 
_struct_keywords.text            
'SARS CoV-2 Papain Like Protease (PLpro), complex, inhibitor, Jun13307, 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 5 ? 
K N N 5 ? 
L N N 5 ? 
M N N 5 ? 
N N N 5 ? 
O N N 6 ? 
# 
_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              9DO1 
_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 9DO1 SER A 1 ? UNP P0DTD1 ? ? 'expression tag' -2 1 
1 9DO1 ASN A 2 ? UNP P0DTD1 ? ? 'expression tag' -1 2 
1 9DO1 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 
# 
_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 ? CYS A 158 ? ALA A 144 CYS A 155 1 ? 12 
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 ASP 65  OD1 ? ? ? 1_555 E ZN  . ZN ? ? A ASP 62  A ZN  404 10_665 ? ? ? ? ? ? ? 1.929 ? ? 
metalc2  metalc ? ? A HIS 76  ND1 ? ? ? 1_555 E ZN  . ZN ? ? A HIS 73  A ZN  404 1_555  ? ? ? ? ? ? ? 2.283 ? ? 
metalc3  metalc ? ? A HIS 92  ND1 ? ? ? 1_555 F ZN  . ZN ? ? A HIS 89  A ZN  405 1_555  ? ? ? ? ? ? ? 2.296 ? ? 
metalc4  metalc ? ? A ASP 111 OD2 ? ? ? 1_555 F ZN  . ZN ? ? A ASP 108 A ZN  405 1_555  ? ? ? ? ? ? ? 2.272 ? ? 
metalc5  metalc ? ? A CYS 114 SG  ? ? ? 1_555 I ZN  . ZN ? ? A CYS 111 A ZN  408 1_555  ? ? ? ? ? ? ? 2.312 ? ? 
metalc6  metalc ? ? A HIS 178 NE2 ? ? ? 1_555 G ZN  . ZN ? ? A HIS 175 A ZN  406 1_555  ? ? ? ? ? ? ? 2.300 ? ? 
metalc7  metalc ? ? A CYS 192 SG  ? ? ? 1_555 D ZN  . ZN ? ? A CYS 189 A ZN  403 1_555  ? ? ? ? ? ? ? 2.329 ? ? 
metalc8  metalc ? ? A CYS 195 SG  ? ? ? 1_555 D ZN  . ZN ? ? A CYS 192 A ZN  403 1_555  ? ? ? ? ? ? ? 2.329 ? ? 
metalc9  metalc ? ? A CYS 195 SG  ? ? ? 1_555 H ZN  . ZN ? ? A CYS 192 A ZN  407 1_555  ? ? ? ? ? ? ? 2.303 ? ? 
metalc10 metalc ? ? A CYS 195 SG  ? ? ? 1_555 H ZN  . ZN ? ? A CYS 192 A ZN  407 8_665  ? ? ? ? ? ? ? 2.993 ? ? 
metalc11 metalc ? ? A CYS 227 SG  ? ? ? 1_555 D ZN  . ZN ? ? A CYS 224 A ZN  403 1_555  ? ? ? ? ? ? ? 2.333 ? ? 
metalc12 metalc ? ? A CYS 229 SG  ? ? ? 1_555 D ZN  . ZN ? ? A CYS 226 A ZN  403 1_555  ? ? ? ? ? ? ? 2.332 ? ? 
metalc13 metalc ? ? A CYS 273 SG  ? ? ? 1_555 F ZN  . ZN ? ? A CYS 270 A ZN  405 15_555 ? ? ? ? ? ? ? 2.258 ? ? 
metalc14 metalc ? ? A HIS 275 ND1 ? ? ? 1_555 I ZN  . ZN ? ? A HIS 272 A ZN  408 1_555  ? ? ? ? ? ? ? 2.317 ? ? 
metalc15 metalc ? ? F ZN  .   ZN  ? ? ? 1_555 O HOH . O  ? ? A ZN  405 A HOH 668 1_555  ? ? ? ? ? ? ? 2.306 ? ? 
# 
_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  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_555 116.3 ? 
2  ND1 ? A HIS 92  ? A HIS 89  ? 1_555 ZN ? F ZN . ? A ZN 405 ? 1_555  OD2 ? A ASP 111 ? A ASP 108 ? 1_555 114.6 ? 
3  ND1 ? A HIS 92  ? A HIS 89  ? 1_555 ZN ? F ZN . ? A ZN 405 ? 1_555  SG  ? A CYS 273 ? A CYS 270 ? 1_555 101.1 ? 
4  OD2 ? A ASP 111 ? A ASP 108 ? 1_555 ZN ? F ZN . ? A ZN 405 ? 1_555  SG  ? A CYS 273 ? A CYS 270 ? 1_555 29.4  ? 
5  ND1 ? A HIS 92  ? A HIS 89  ? 1_555 ZN ? F ZN . ? A ZN 405 ? 1_555  O   ? O HOH .   ? A HOH 668 ? 1_555 129.8 ? 
6  OD2 ? A ASP 111 ? A ASP 108 ? 1_555 ZN ? F ZN . ? A ZN 405 ? 1_555  O   ? O HOH .   ? A HOH 668 ? 1_555 100.3 ? 
7  SG  ? A CYS 273 ? A CYS 270 ? 1_555 ZN ? F ZN . ? A ZN 405 ? 1_555  O   ? O HOH .   ? A HOH 668 ? 1_555 124.9 ? 
8  SG  ? A CYS 114 ? A CYS 111 ? 1_555 ZN ? I ZN . ? A ZN 408 ? 1_555  ND1 ? A HIS 275 ? A HIS 272 ? 1_555 97.4  ? 
9  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_555 111.1 ? 
10 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_555 111.9 ? 
11 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_555 106.0 ? 
12 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_555 105.8 ? 
13 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_555 110.7 ? 
14 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_555 111.5 ? 
15 SG  ? A CYS 195 ? A CYS 192 ? 1_555 ZN ? H ZN . ? A ZN 407 ? 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 GLN A 232 ? GLU A 241 ? GLN A 229 GLU A 238 
AA3 4 VAL A 223 ? PRO A 226 ? VAL A 220 PRO A 223 
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 GLN A 232 ? GLU A 241 ? GLN A 229 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 ? LEU A 256 ? PHE A 241 LEU A 253 
AA5 3 TYR A 299 ? LYS A 309 ? TYR A 296 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 HIS A 20  ? O HIS A 17  N THR A 12  ? N THR A 9   
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 LYS A 185 ? N LYS A 182 O GLU A 241 ? O GLU A 238 
AA3 3 4 O ALA A 233 ? O ALA A 230 N ILE A 225 ? N ILE A 222 
AA4 1 2 O LEU A 202 ? O LEU A 199 N ARG A 186 ? N ARG A 183 
AA4 2 3 N LYS A 185 ? N LYS A 182 O GLU A 241 ? O GLU A 238 
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 ALA A 264 ? N ALA A 261 O ILE A 279 ? O ILE A 276 
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                   9DO1 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ILE A 14  ? ? -123.26 -65.83  
2 1 ALA A 107 ? ? -175.90 138.88  
3 1 GLN A 269 ? ? 67.27   -32.05  
4 1 LYS A 279 ? ? -115.25 -132.52 
5 1 ASN A 308 ? ? -140.09 -59.51  
# 
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 
# 
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 
A1BF2 C13  C  Y N 1   
A1BF2 C15  C  Y N 2   
A1BF2 C21  C  N N 3   
A1BF2 C22  C  N N 4   
A1BF2 C24  C  N N 5   
A1BF2 C26  C  N N 6   
A1BF2 C28  C  N N 7   
A1BF2 C01  C  N N 8   
A1BF2 C04  C  Y N 9   
A1BF2 C05  C  Y N 10  
A1BF2 C06  C  Y N 11  
A1BF2 C07  C  Y N 12  
A1BF2 C08  C  Y N 13  
A1BF2 C09  C  N R 14  
A1BF2 C11  C  N N 15  
A1BF2 C12  C  Y N 16  
A1BF2 C14  C  Y N 17  
A1BF2 C16  C  Y N 18  
A1BF2 C18  C  N N 19  
A1BF2 C19  C  N R 20  
A1BF2 C23  C  N N 21  
A1BF2 C25  C  Y N 22  
A1BF2 C29  C  Y N 23  
A1BF2 C30  C  Y N 24  
A1BF2 C31  C  Y N 25  
A1BF2 C32  C  Y N 26  
A1BF2 C33  C  Y N 27  
A1BF2 C34  C  Y N 28  
A1BF2 C36  C  Y N 29  
A1BF2 N02  N  Y N 30  
A1BF2 N03  N  Y N 31  
A1BF2 N10  N  N N 32  
A1BF2 N20  N  N N 33  
A1BF2 N35  N  Y N 34  
A1BF2 O17  O  N N 35  
A1BF2 O27  O  N N 36  
A1BF2 H151 H  N N 37  
A1BF2 H211 H  N N 38  
A1BF2 H212 H  N N 39  
A1BF2 H221 H  N N 40  
A1BF2 H222 H  N N 41  
A1BF2 H241 H  N N 42  
A1BF2 H242 H  N N 43  
A1BF2 H243 H  N N 44  
A1BF2 H262 H  N N 45  
A1BF2 H261 H  N N 46  
A1BF2 H263 H  N N 47  
A1BF2 H281 H  N N 48  
A1BF2 H283 H  N N 49  
A1BF2 H282 H  N N 50  
A1BF2 H013 H  N N 51  
A1BF2 H011 H  N N 52  
A1BF2 H012 H  N N 53  
A1BF2 H041 H  N N 54  
A1BF2 H071 H  N N 55  
A1BF2 H091 H  N N 56  
A1BF2 H141 H  N N 57  
A1BF2 H181 H  N N 58  
A1BF2 H182 H  N N 59  
A1BF2 H191 H  N N 60  
A1BF2 H231 H  N N 61  
A1BF2 H232 H  N N 62  
A1BF2 H251 H  N N 63  
A1BF2 H301 H  N N 64  
A1BF2 H311 H  N N 65  
A1BF2 H321 H  N N 66  
A1BF2 H331 H  N N 67  
A1BF2 H361 H  N N 68  
A1BF2 H101 H  N N 69  
ALA   N    N  N N 70  
ALA   CA   C  N S 71  
ALA   C    C  N N 72  
ALA   O    O  N N 73  
ALA   CB   C  N N 74  
ALA   OXT  O  N N 75  
ALA   H    H  N N 76  
ALA   H2   H  N N 77  
ALA   HA   H  N N 78  
ALA   HB1  H  N N 79  
ALA   HB2  H  N N 80  
ALA   HB3  H  N N 81  
ALA   HXT  H  N N 82  
ARG   N    N  N N 83  
ARG   CA   C  N S 84  
ARG   C    C  N N 85  
ARG   O    O  N N 86  
ARG   CB   C  N N 87  
ARG   CG   C  N N 88  
ARG   CD   C  N N 89  
ARG   NE   N  N N 90  
ARG   CZ   C  N N 91  
ARG   NH1  N  N N 92  
ARG   NH2  N  N N 93  
ARG   OXT  O  N N 94  
ARG   H    H  N N 95  
ARG   H2   H  N N 96  
ARG   HA   H  N N 97  
ARG   HB2  H  N N 98  
ARG   HB3  H  N N 99  
ARG   HG2  H  N N 100 
ARG   HG3  H  N N 101 
ARG   HD2  H  N N 102 
ARG   HD3  H  N N 103 
ARG   HE   H  N N 104 
ARG   HH11 H  N N 105 
ARG   HH12 H  N N 106 
ARG   HH21 H  N N 107 
ARG   HH22 H  N N 108 
ARG   HXT  H  N N 109 
ASN   N    N  N N 110 
ASN   CA   C  N S 111 
ASN   C    C  N N 112 
ASN   O    O  N N 113 
ASN   CB   C  N N 114 
ASN   CG   C  N N 115 
ASN   OD1  O  N N 116 
ASN   ND2  N  N N 117 
ASN   OXT  O  N N 118 
ASN   H    H  N N 119 
ASN   H2   H  N N 120 
ASN   HA   H  N N 121 
ASN   HB2  H  N N 122 
ASN   HB3  H  N N 123 
ASN   HD21 H  N N 124 
ASN   HD22 H  N N 125 
ASN   HXT  H  N N 126 
ASP   N    N  N N 127 
ASP   CA   C  N S 128 
ASP   C    C  N N 129 
ASP   O    O  N N 130 
ASP   CB   C  N N 131 
ASP   CG   C  N N 132 
ASP   OD1  O  N N 133 
ASP   OD2  O  N N 134 
ASP   OXT  O  N N 135 
ASP   H    H  N N 136 
ASP   H2   H  N N 137 
ASP   HA   H  N N 138 
ASP   HB2  H  N N 139 
ASP   HB3  H  N N 140 
ASP   HD2  H  N N 141 
ASP   HXT  H  N N 142 
CL    CL   CL N N 143 
CYS   N    N  N N 144 
CYS   CA   C  N R 145 
CYS   C    C  N N 146 
CYS   O    O  N N 147 
CYS   CB   C  N N 148 
CYS   SG   S  N N 149 
CYS   OXT  O  N N 150 
CYS   H    H  N N 151 
CYS   H2   H  N N 152 
CYS   HA   H  N N 153 
CYS   HB2  H  N N 154 
CYS   HB3  H  N N 155 
CYS   HG   H  N N 156 
CYS   HXT  H  N N 157 
GLN   N    N  N N 158 
GLN   CA   C  N S 159 
GLN   C    C  N N 160 
GLN   O    O  N N 161 
GLN   CB   C  N N 162 
GLN   CG   C  N N 163 
GLN   CD   C  N N 164 
GLN   OE1  O  N N 165 
GLN   NE2  N  N N 166 
GLN   OXT  O  N N 167 
GLN   H    H  N N 168 
GLN   H2   H  N N 169 
GLN   HA   H  N N 170 
GLN   HB2  H  N N 171 
GLN   HB3  H  N N 172 
GLN   HG2  H  N N 173 
GLN   HG3  H  N N 174 
GLN   HE21 H  N N 175 
GLN   HE22 H  N N 176 
GLN   HXT  H  N N 177 
GLU   N    N  N N 178 
GLU   CA   C  N S 179 
GLU   C    C  N N 180 
GLU   O    O  N N 181 
GLU   CB   C  N N 182 
GLU   CG   C  N N 183 
GLU   CD   C  N N 184 
GLU   OE1  O  N N 185 
GLU   OE2  O  N N 186 
GLU   OXT  O  N N 187 
GLU   H    H  N N 188 
GLU   H2   H  N N 189 
GLU   HA   H  N N 190 
GLU   HB2  H  N N 191 
GLU   HB3  H  N N 192 
GLU   HG2  H  N N 193 
GLU   HG3  H  N N 194 
GLU   HE2  H  N N 195 
GLU   HXT  H  N N 196 
GLY   N    N  N N 197 
GLY   CA   C  N N 198 
GLY   C    C  N N 199 
GLY   O    O  N N 200 
GLY   OXT  O  N N 201 
GLY   H    H  N N 202 
GLY   H2   H  N N 203 
GLY   HA2  H  N N 204 
GLY   HA3  H  N N 205 
GLY   HXT  H  N N 206 
HIS   N    N  N N 207 
HIS   CA   C  N S 208 
HIS   C    C  N N 209 
HIS   O    O  N N 210 
HIS   CB   C  N N 211 
HIS   CG   C  Y N 212 
HIS   ND1  N  Y N 213 
HIS   CD2  C  Y N 214 
HIS   CE1  C  Y N 215 
HIS   NE2  N  Y N 216 
HIS   OXT  O  N N 217 
HIS   H    H  N N 218 
HIS   H2   H  N N 219 
HIS   HA   H  N N 220 
HIS   HB2  H  N N 221 
HIS   HB3  H  N N 222 
HIS   HD1  H  N N 223 
HIS   HD2  H  N N 224 
HIS   HE1  H  N N 225 
HIS   HE2  H  N N 226 
HIS   HXT  H  N N 227 
HOH   O    O  N N 228 
HOH   H1   H  N N 229 
HOH   H2   H  N N 230 
ILE   N    N  N N 231 
ILE   CA   C  N S 232 
ILE   C    C  N N 233 
ILE   O    O  N N 234 
ILE   CB   C  N S 235 
ILE   CG1  C  N N 236 
ILE   CG2  C  N N 237 
ILE   CD1  C  N N 238 
ILE   OXT  O  N N 239 
ILE   H    H  N N 240 
ILE   H2   H  N N 241 
ILE   HA   H  N N 242 
ILE   HB   H  N N 243 
ILE   HG12 H  N N 244 
ILE   HG13 H  N N 245 
ILE   HG21 H  N N 246 
ILE   HG22 H  N N 247 
ILE   HG23 H  N N 248 
ILE   HD11 H  N N 249 
ILE   HD12 H  N N 250 
ILE   HD13 H  N N 251 
ILE   HXT  H  N N 252 
LEU   N    N  N N 253 
LEU   CA   C  N S 254 
LEU   C    C  N N 255 
LEU   O    O  N N 256 
LEU   CB   C  N N 257 
LEU   CG   C  N N 258 
LEU   CD1  C  N N 259 
LEU   CD2  C  N N 260 
LEU   OXT  O  N N 261 
LEU   H    H  N N 262 
LEU   H2   H  N N 263 
LEU   HA   H  N N 264 
LEU   HB2  H  N N 265 
LEU   HB3  H  N N 266 
LEU   HG   H  N N 267 
LEU   HD11 H  N N 268 
LEU   HD12 H  N N 269 
LEU   HD13 H  N N 270 
LEU   HD21 H  N N 271 
LEU   HD22 H  N N 272 
LEU   HD23 H  N N 273 
LEU   HXT  H  N N 274 
LYS   N    N  N N 275 
LYS   CA   C  N S 276 
LYS   C    C  N N 277 
LYS   O    O  N N 278 
LYS   CB   C  N N 279 
LYS   CG   C  N N 280 
LYS   CD   C  N N 281 
LYS   CE   C  N N 282 
LYS   NZ   N  N N 283 
LYS   OXT  O  N N 284 
LYS   H    H  N N 285 
LYS   H2   H  N N 286 
LYS   HA   H  N N 287 
LYS   HB2  H  N N 288 
LYS   HB3  H  N N 289 
LYS   HG2  H  N N 290 
LYS   HG3  H  N N 291 
LYS   HD2  H  N N 292 
LYS   HD3  H  N N 293 
LYS   HE2  H  N N 294 
LYS   HE3  H  N N 295 
LYS   HZ1  H  N N 296 
LYS   HZ2  H  N N 297 
LYS   HZ3  H  N N 298 
LYS   HXT  H  N N 299 
MET   N    N  N N 300 
MET   CA   C  N S 301 
MET   C    C  N N 302 
MET   O    O  N N 303 
MET   CB   C  N N 304 
MET   CG   C  N N 305 
MET   SD   S  N N 306 
MET   CE   C  N N 307 
MET   OXT  O  N N 308 
MET   H    H  N N 309 
MET   H2   H  N N 310 
MET   HA   H  N N 311 
MET   HB2  H  N N 312 
MET   HB3  H  N N 313 
MET   HG2  H  N N 314 
MET   HG3  H  N N 315 
MET   HE1  H  N N 316 
MET   HE2  H  N N 317 
MET   HE3  H  N N 318 
MET   HXT  H  N N 319 
PEG   C1   C  N N 320 
PEG   O1   O  N N 321 
PEG   C2   C  N N 322 
PEG   O2   O  N N 323 
PEG   C3   C  N N 324 
PEG   C4   C  N N 325 
PEG   O4   O  N N 326 
PEG   H11  H  N N 327 
PEG   H12  H  N N 328 
PEG   HO1  H  N N 329 
PEG   H21  H  N N 330 
PEG   H22  H  N N 331 
PEG   H31  H  N N 332 
PEG   H32  H  N N 333 
PEG   H41  H  N N 334 
PEG   H42  H  N N 335 
PEG   HO4  H  N N 336 
PHE   N    N  N N 337 
PHE   CA   C  N S 338 
PHE   C    C  N N 339 
PHE   O    O  N N 340 
PHE   CB   C  N N 341 
PHE   CG   C  Y N 342 
PHE   CD1  C  Y N 343 
PHE   CD2  C  Y N 344 
PHE   CE1  C  Y N 345 
PHE   CE2  C  Y N 346 
PHE   CZ   C  Y N 347 
PHE   OXT  O  N N 348 
PHE   H    H  N N 349 
PHE   H2   H  N N 350 
PHE   HA   H  N N 351 
PHE   HB2  H  N N 352 
PHE   HB3  H  N N 353 
PHE   HD1  H  N N 354 
PHE   HD2  H  N N 355 
PHE   HE1  H  N N 356 
PHE   HE2  H  N N 357 
PHE   HZ   H  N N 358 
PHE   HXT  H  N N 359 
PRO   N    N  N N 360 
PRO   CA   C  N S 361 
PRO   C    C  N N 362 
PRO   O    O  N N 363 
PRO   CB   C  N N 364 
PRO   CG   C  N N 365 
PRO   CD   C  N N 366 
PRO   OXT  O  N N 367 
PRO   H    H  N N 368 
PRO   HA   H  N N 369 
PRO   HB2  H  N N 370 
PRO   HB3  H  N N 371 
PRO   HG2  H  N N 372 
PRO   HG3  H  N N 373 
PRO   HD2  H  N N 374 
PRO   HD3  H  N N 375 
PRO   HXT  H  N N 376 
SER   N    N  N N 377 
SER   CA   C  N S 378 
SER   C    C  N N 379 
SER   O    O  N N 380 
SER   CB   C  N N 381 
SER   OG   O  N N 382 
SER   OXT  O  N N 383 
SER   H    H  N N 384 
SER   H2   H  N N 385 
SER   HA   H  N N 386 
SER   HB2  H  N N 387 
SER   HB3  H  N N 388 
SER   HG   H  N N 389 
SER   HXT  H  N N 390 
THR   N    N  N N 391 
THR   CA   C  N S 392 
THR   C    C  N N 393 
THR   O    O  N N 394 
THR   CB   C  N R 395 
THR   OG1  O  N N 396 
THR   CG2  C  N N 397 
THR   OXT  O  N N 398 
THR   H    H  N N 399 
THR   H2   H  N N 400 
THR   HA   H  N N 401 
THR   HB   H  N N 402 
THR   HG1  H  N N 403 
THR   HG21 H  N N 404 
THR   HG22 H  N N 405 
THR   HG23 H  N N 406 
THR   HXT  H  N N 407 
TRP   N    N  N N 408 
TRP   CA   C  N S 409 
TRP   C    C  N N 410 
TRP   O    O  N N 411 
TRP   CB   C  N N 412 
TRP   CG   C  Y N 413 
TRP   CD1  C  Y N 414 
TRP   CD2  C  Y N 415 
TRP   NE1  N  Y N 416 
TRP   CE2  C  Y N 417 
TRP   CE3  C  Y N 418 
TRP   CZ2  C  Y N 419 
TRP   CZ3  C  Y N 420 
TRP   CH2  C  Y N 421 
TRP   OXT  O  N N 422 
TRP   H    H  N N 423 
TRP   H2   H  N N 424 
TRP   HA   H  N N 425 
TRP   HB2  H  N N 426 
TRP   HB3  H  N N 427 
TRP   HD1  H  N N 428 
TRP   HE1  H  N N 429 
TRP   HE3  H  N N 430 
TRP   HZ2  H  N N 431 
TRP   HZ3  H  N N 432 
TRP   HH2  H  N N 433 
TRP   HXT  H  N N 434 
TYR   N    N  N N 435 
TYR   CA   C  N S 436 
TYR   C    C  N N 437 
TYR   O    O  N N 438 
TYR   CB   C  N N 439 
TYR   CG   C  Y N 440 
TYR   CD1  C  Y N 441 
TYR   CD2  C  Y N 442 
TYR   CE1  C  Y N 443 
TYR   CE2  C  Y N 444 
TYR   CZ   C  Y N 445 
TYR   OH   O  N N 446 
TYR   OXT  O  N N 447 
TYR   H    H  N N 448 
TYR   H2   H  N N 449 
TYR   HA   H  N N 450 
TYR   HB2  H  N N 451 
TYR   HB3  H  N N 452 
TYR   HD1  H  N N 453 
TYR   HD2  H  N N 454 
TYR   HE1  H  N N 455 
TYR   HE2  H  N N 456 
TYR   HH   H  N N 457 
TYR   HXT  H  N N 458 
VAL   N    N  N N 459 
VAL   CA   C  N S 460 
VAL   C    C  N N 461 
VAL   O    O  N N 462 
VAL   CB   C  N N 463 
VAL   CG1  C  N N 464 
VAL   CG2  C  N N 465 
VAL   OXT  O  N N 466 
VAL   H    H  N N 467 
VAL   H2   H  N N 468 
VAL   HA   H  N N 469 
VAL   HB   H  N N 470 
VAL   HG11 H  N N 471 
VAL   HG12 H  N N 472 
VAL   HG13 H  N N 473 
VAL   HG21 H  N N 474 
VAL   HG22 H  N N 475 
VAL   HG23 H  N N 476 
VAL   HXT  H  N N 477 
ZN    ZN   ZN N N 478 
# 
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 
A1BF2 N02 C01  sing N N 1   
A1BF2 N03 N02  sing Y N 2   
A1BF2 C04 N03  doub Y N 3   
A1BF2 C05 C04  sing Y N 4   
A1BF2 C07 C06  doub Y N 5   
A1BF2 C08 C07  sing Y N 6   
A1BF2 C11 N10  sing N N 7   
A1BF2 C13 C12  doub Y N 8   
A1BF2 C15 C14  doub Y N 9   
A1BF2 C16 C15  sing Y N 10  
A1BF2 C18 O17  sing N N 11  
A1BF2 C19 C18  sing N N 12  
A1BF2 N20 C19  sing N N 13  
A1BF2 C22 C21  sing N N 14  
A1BF2 C23 C22  sing N N 15  
A1BF2 C21 N20  sing N N 16  
A1BF2 C24 N20  sing N N 17  
A1BF2 O17 C16  sing N N 18  
A1BF2 C25 C16  doub Y N 19  
A1BF2 C14 C13  sing Y N 20  
A1BF2 C26 C13  sing N N 21  
A1BF2 C12 C11  sing N N 22  
A1BF2 O27 C11  doub N N 23  
A1BF2 N10 C09  sing N N 24  
A1BF2 C28 C09  sing N N 25  
A1BF2 C09 C08  sing N N 26  
A1BF2 C29 C08  doub Y N 27  
A1BF2 C30 C29  sing Y N 28  
A1BF2 C31 C30  doub Y N 29  
A1BF2 C32 C31  sing Y N 30  
A1BF2 C33 C32  doub Y N 31  
A1BF2 C34 C33  sing Y N 32  
A1BF2 N35 C34  doub Y N 33  
A1BF2 C06 C05  sing N N 34  
A1BF2 C36 C05  doub Y N 35  
A1BF2 N02 C36  sing Y N 36  
A1BF2 C06 N35  sing Y N 37  
A1BF2 C12 C25  sing Y N 38  
A1BF2 C19 C23  sing N N 39  
A1BF2 C29 C34  sing Y N 40  
A1BF2 C15 H151 sing N N 41  
A1BF2 C21 H211 sing N N 42  
A1BF2 C21 H212 sing N N 43  
A1BF2 C22 H221 sing N N 44  
A1BF2 C22 H222 sing N N 45  
A1BF2 C24 H241 sing N N 46  
A1BF2 C24 H242 sing N N 47  
A1BF2 C24 H243 sing N N 48  
A1BF2 C26 H262 sing N N 49  
A1BF2 C26 H261 sing N N 50  
A1BF2 C26 H263 sing N N 51  
A1BF2 C28 H281 sing N N 52  
A1BF2 C28 H283 sing N N 53  
A1BF2 C28 H282 sing N N 54  
A1BF2 C01 H013 sing N N 55  
A1BF2 C01 H011 sing N N 56  
A1BF2 C01 H012 sing N N 57  
A1BF2 C04 H041 sing N N 58  
A1BF2 C07 H071 sing N N 59  
A1BF2 C09 H091 sing N N 60  
A1BF2 C14 H141 sing N N 61  
A1BF2 C18 H181 sing N N 62  
A1BF2 C18 H182 sing N N 63  
A1BF2 C19 H191 sing N N 64  
A1BF2 C23 H231 sing N N 65  
A1BF2 C23 H232 sing N N 66  
A1BF2 C25 H251 sing N N 67  
A1BF2 C30 H301 sing N N 68  
A1BF2 C31 H311 sing N N 69  
A1BF2 C32 H321 sing N N 70  
A1BF2 C33 H331 sing N N 71  
A1BF2 C36 H361 sing N N 72  
A1BF2 N10 H101 sing N N 73  
ALA   N   CA   sing N N 74  
ALA   N   H    sing N N 75  
ALA   N   H2   sing N N 76  
ALA   CA  C    sing N N 77  
ALA   CA  CB   sing N N 78  
ALA   CA  HA   sing N N 79  
ALA   C   O    doub N N 80  
ALA   C   OXT  sing N N 81  
ALA   CB  HB1  sing N N 82  
ALA   CB  HB2  sing N N 83  
ALA   CB  HB3  sing N N 84  
ALA   OXT HXT  sing N N 85  
ARG   N   CA   sing N N 86  
ARG   N   H    sing N N 87  
ARG   N   H2   sing N N 88  
ARG   CA  C    sing N N 89  
ARG   CA  CB   sing N N 90  
ARG   CA  HA   sing N N 91  
ARG   C   O    doub N N 92  
ARG   C   OXT  sing N N 93  
ARG   CB  CG   sing N N 94  
ARG   CB  HB2  sing N N 95  
ARG   CB  HB3  sing N N 96  
ARG   CG  CD   sing N N 97  
ARG   CG  HG2  sing N N 98  
ARG   CG  HG3  sing N N 99  
ARG   CD  NE   sing N N 100 
ARG   CD  HD2  sing N N 101 
ARG   CD  HD3  sing N N 102 
ARG   NE  CZ   sing N N 103 
ARG   NE  HE   sing N N 104 
ARG   CZ  NH1  sing N N 105 
ARG   CZ  NH2  doub N N 106 
ARG   NH1 HH11 sing N N 107 
ARG   NH1 HH12 sing N N 108 
ARG   NH2 HH21 sing N N 109 
ARG   NH2 HH22 sing N N 110 
ARG   OXT HXT  sing N N 111 
ASN   N   CA   sing N N 112 
ASN   N   H    sing N N 113 
ASN   N   H2   sing N N 114 
ASN   CA  C    sing N N 115 
ASN   CA  CB   sing N N 116 
ASN   CA  HA   sing N N 117 
ASN   C   O    doub N N 118 
ASN   C   OXT  sing N N 119 
ASN   CB  CG   sing N N 120 
ASN   CB  HB2  sing N N 121 
ASN   CB  HB3  sing N N 122 
ASN   CG  OD1  doub N N 123 
ASN   CG  ND2  sing N N 124 
ASN   ND2 HD21 sing N N 125 
ASN   ND2 HD22 sing N N 126 
ASN   OXT HXT  sing N N 127 
ASP   N   CA   sing N N 128 
ASP   N   H    sing N N 129 
ASP   N   H2   sing N N 130 
ASP   CA  C    sing N N 131 
ASP   CA  CB   sing N N 132 
ASP   CA  HA   sing N N 133 
ASP   C   O    doub N N 134 
ASP   C   OXT  sing N N 135 
ASP   CB  CG   sing N N 136 
ASP   CB  HB2  sing N N 137 
ASP   CB  HB3  sing N N 138 
ASP   CG  OD1  doub N N 139 
ASP   CG  OD2  sing N N 140 
ASP   OD2 HD2  sing N N 141 
ASP   OXT HXT  sing N N 142 
CYS   N   CA   sing N N 143 
CYS   N   H    sing N N 144 
CYS   N   H2   sing N N 145 
CYS   CA  C    sing N N 146 
CYS   CA  CB   sing N N 147 
CYS   CA  HA   sing N N 148 
CYS   C   O    doub N N 149 
CYS   C   OXT  sing N N 150 
CYS   CB  SG   sing N N 151 
CYS   CB  HB2  sing N N 152 
CYS   CB  HB3  sing N N 153 
CYS   SG  HG   sing N N 154 
CYS   OXT HXT  sing N N 155 
GLN   N   CA   sing N N 156 
GLN   N   H    sing N N 157 
GLN   N   H2   sing N N 158 
GLN   CA  C    sing N N 159 
GLN   CA  CB   sing N N 160 
GLN   CA  HA   sing N N 161 
GLN   C   O    doub N N 162 
GLN   C   OXT  sing N N 163 
GLN   CB  CG   sing N N 164 
GLN   CB  HB2  sing N N 165 
GLN   CB  HB3  sing N N 166 
GLN   CG  CD   sing N N 167 
GLN   CG  HG2  sing N N 168 
GLN   CG  HG3  sing N N 169 
GLN   CD  OE1  doub N N 170 
GLN   CD  NE2  sing N N 171 
GLN   NE2 HE21 sing N N 172 
GLN   NE2 HE22 sing N N 173 
GLN   OXT HXT  sing N N 174 
GLU   N   CA   sing N N 175 
GLU   N   H    sing N N 176 
GLU   N   H2   sing N N 177 
GLU   CA  C    sing N N 178 
GLU   CA  CB   sing N N 179 
GLU   CA  HA   sing N N 180 
GLU   C   O    doub N N 181 
GLU   C   OXT  sing N N 182 
GLU   CB  CG   sing N N 183 
GLU   CB  HB2  sing N N 184 
GLU   CB  HB3  sing N N 185 
GLU   CG  CD   sing N N 186 
GLU   CG  HG2  sing N N 187 
GLU   CG  HG3  sing N N 188 
GLU   CD  OE1  doub N N 189 
GLU   CD  OE2  sing N N 190 
GLU   OE2 HE2  sing N N 191 
GLU   OXT HXT  sing N N 192 
GLY   N   CA   sing N N 193 
GLY   N   H    sing N N 194 
GLY   N   H2   sing N N 195 
GLY   CA  C    sing N N 196 
GLY   CA  HA2  sing N N 197 
GLY   CA  HA3  sing N N 198 
GLY   C   O    doub N N 199 
GLY   C   OXT  sing N N 200 
GLY   OXT HXT  sing N N 201 
HIS   N   CA   sing N N 202 
HIS   N   H    sing N N 203 
HIS   N   H2   sing N N 204 
HIS   CA  C    sing N N 205 
HIS   CA  CB   sing N N 206 
HIS   CA  HA   sing N N 207 
HIS   C   O    doub N N 208 
HIS   C   OXT  sing N N 209 
HIS   CB  CG   sing N N 210 
HIS   CB  HB2  sing N N 211 
HIS   CB  HB3  sing N N 212 
HIS   CG  ND1  sing Y N 213 
HIS   CG  CD2  doub Y N 214 
HIS   ND1 CE1  doub Y N 215 
HIS   ND1 HD1  sing N N 216 
HIS   CD2 NE2  sing Y N 217 
HIS   CD2 HD2  sing N N 218 
HIS   CE1 NE2  sing Y N 219 
HIS   CE1 HE1  sing N N 220 
HIS   NE2 HE2  sing N N 221 
HIS   OXT HXT  sing N N 222 
HOH   O   H1   sing N N 223 
HOH   O   H2   sing N N 224 
ILE   N   CA   sing N N 225 
ILE   N   H    sing N N 226 
ILE   N   H2   sing N N 227 
ILE   CA  C    sing N N 228 
ILE   CA  CB   sing N N 229 
ILE   CA  HA   sing N N 230 
ILE   C   O    doub N N 231 
ILE   C   OXT  sing N N 232 
ILE   CB  CG1  sing N N 233 
ILE   CB  CG2  sing N N 234 
ILE   CB  HB   sing N N 235 
ILE   CG1 CD1  sing N N 236 
ILE   CG1 HG12 sing N N 237 
ILE   CG1 HG13 sing N N 238 
ILE   CG2 HG21 sing N N 239 
ILE   CG2 HG22 sing N N 240 
ILE   CG2 HG23 sing N N 241 
ILE   CD1 HD11 sing N N 242 
ILE   CD1 HD12 sing N N 243 
ILE   CD1 HD13 sing N N 244 
ILE   OXT HXT  sing N N 245 
LEU   N   CA   sing N N 246 
LEU   N   H    sing N N 247 
LEU   N   H2   sing N N 248 
LEU   CA  C    sing N N 249 
LEU   CA  CB   sing N N 250 
LEU   CA  HA   sing N N 251 
LEU   C   O    doub N N 252 
LEU   C   OXT  sing N N 253 
LEU   CB  CG   sing N N 254 
LEU   CB  HB2  sing N N 255 
LEU   CB  HB3  sing N N 256 
LEU   CG  CD1  sing N N 257 
LEU   CG  CD2  sing N N 258 
LEU   CG  HG   sing N N 259 
LEU   CD1 HD11 sing N N 260 
LEU   CD1 HD12 sing N N 261 
LEU   CD1 HD13 sing N N 262 
LEU   CD2 HD21 sing N N 263 
LEU   CD2 HD22 sing N N 264 
LEU   CD2 HD23 sing N N 265 
LEU   OXT HXT  sing N N 266 
LYS   N   CA   sing N N 267 
LYS   N   H    sing N N 268 
LYS   N   H2   sing N N 269 
LYS   CA  C    sing N N 270 
LYS   CA  CB   sing N N 271 
LYS   CA  HA   sing N N 272 
LYS   C   O    doub N N 273 
LYS   C   OXT  sing N N 274 
LYS   CB  CG   sing N N 275 
LYS   CB  HB2  sing N N 276 
LYS   CB  HB3  sing N N 277 
LYS   CG  CD   sing N N 278 
LYS   CG  HG2  sing N N 279 
LYS   CG  HG3  sing N N 280 
LYS   CD  CE   sing N N 281 
LYS   CD  HD2  sing N N 282 
LYS   CD  HD3  sing N N 283 
LYS   CE  NZ   sing N N 284 
LYS   CE  HE2  sing N N 285 
LYS   CE  HE3  sing N N 286 
LYS   NZ  HZ1  sing N N 287 
LYS   NZ  HZ2  sing N N 288 
LYS   NZ  HZ3  sing N N 289 
LYS   OXT HXT  sing N N 290 
MET   N   CA   sing N N 291 
MET   N   H    sing N N 292 
MET   N   H2   sing N N 293 
MET   CA  C    sing N N 294 
MET   CA  CB   sing N N 295 
MET   CA  HA   sing N N 296 
MET   C   O    doub N N 297 
MET   C   OXT  sing N N 298 
MET   CB  CG   sing N N 299 
MET   CB  HB2  sing N N 300 
MET   CB  HB3  sing N N 301 
MET   CG  SD   sing N N 302 
MET   CG  HG2  sing N N 303 
MET   CG  HG3  sing N N 304 
MET   SD  CE   sing N N 305 
MET   CE  HE1  sing N N 306 
MET   CE  HE2  sing N N 307 
MET   CE  HE3  sing N N 308 
MET   OXT HXT  sing N N 309 
PEG   C1  O1   sing N N 310 
PEG   C1  C2   sing N N 311 
PEG   C1  H11  sing N N 312 
PEG   C1  H12  sing N N 313 
PEG   O1  HO1  sing N N 314 
PEG   C2  O2   sing N N 315 
PEG   C2  H21  sing N N 316 
PEG   C2  H22  sing N N 317 
PEG   O2  C3   sing N N 318 
PEG   C3  C4   sing N N 319 
PEG   C3  H31  sing N N 320 
PEG   C3  H32  sing N N 321 
PEG   C4  O4   sing N N 322 
PEG   C4  H41  sing N N 323 
PEG   C4  H42  sing N N 324 
PEG   O4  HO4  sing N N 325 
PHE   N   CA   sing N N 326 
PHE   N   H    sing N N 327 
PHE   N   H2   sing N N 328 
PHE   CA  C    sing N N 329 
PHE   CA  CB   sing N N 330 
PHE   CA  HA   sing N N 331 
PHE   C   O    doub N N 332 
PHE   C   OXT  sing N N 333 
PHE   CB  CG   sing N N 334 
PHE   CB  HB2  sing N N 335 
PHE   CB  HB3  sing N N 336 
PHE   CG  CD1  doub Y N 337 
PHE   CG  CD2  sing Y N 338 
PHE   CD1 CE1  sing Y N 339 
PHE   CD1 HD1  sing N N 340 
PHE   CD2 CE2  doub Y N 341 
PHE   CD2 HD2  sing N N 342 
PHE   CE1 CZ   doub Y N 343 
PHE   CE1 HE1  sing N N 344 
PHE   CE2 CZ   sing Y N 345 
PHE   CE2 HE2  sing N N 346 
PHE   CZ  HZ   sing N N 347 
PHE   OXT HXT  sing N N 348 
PRO   N   CA   sing N N 349 
PRO   N   CD   sing N N 350 
PRO   N   H    sing N N 351 
PRO   CA  C    sing N N 352 
PRO   CA  CB   sing N N 353 
PRO   CA  HA   sing N N 354 
PRO   C   O    doub N N 355 
PRO   C   OXT  sing N N 356 
PRO   CB  CG   sing N N 357 
PRO   CB  HB2  sing N N 358 
PRO   CB  HB3  sing N N 359 
PRO   CG  CD   sing N N 360 
PRO   CG  HG2  sing N N 361 
PRO   CG  HG3  sing N N 362 
PRO   CD  HD2  sing N N 363 
PRO   CD  HD3  sing N N 364 
PRO   OXT HXT  sing N N 365 
SER   N   CA   sing N N 366 
SER   N   H    sing N N 367 
SER   N   H2   sing N N 368 
SER   CA  C    sing N N 369 
SER   CA  CB   sing N N 370 
SER   CA  HA   sing N N 371 
SER   C   O    doub N N 372 
SER   C   OXT  sing N N 373 
SER   CB  OG   sing N N 374 
SER   CB  HB2  sing N N 375 
SER   CB  HB3  sing N N 376 
SER   OG  HG   sing N N 377 
SER   OXT HXT  sing N N 378 
THR   N   CA   sing N N 379 
THR   N   H    sing N N 380 
THR   N   H2   sing N N 381 
THR   CA  C    sing N N 382 
THR   CA  CB   sing N N 383 
THR   CA  HA   sing N N 384 
THR   C   O    doub N N 385 
THR   C   OXT  sing N N 386 
THR   CB  OG1  sing N N 387 
THR   CB  CG2  sing N N 388 
THR   CB  HB   sing N N 389 
THR   OG1 HG1  sing N N 390 
THR   CG2 HG21 sing N N 391 
THR   CG2 HG22 sing N N 392 
THR   CG2 HG23 sing N N 393 
THR   OXT HXT  sing N N 394 
TRP   N   CA   sing N N 395 
TRP   N   H    sing N N 396 
TRP   N   H2   sing N N 397 
TRP   CA  C    sing N N 398 
TRP   CA  CB   sing N N 399 
TRP   CA  HA   sing N N 400 
TRP   C   O    doub N N 401 
TRP   C   OXT  sing N N 402 
TRP   CB  CG   sing N N 403 
TRP   CB  HB2  sing N N 404 
TRP   CB  HB3  sing N N 405 
TRP   CG  CD1  doub Y N 406 
TRP   CG  CD2  sing Y N 407 
TRP   CD1 NE1  sing Y N 408 
TRP   CD1 HD1  sing N N 409 
TRP   CD2 CE2  doub Y N 410 
TRP   CD2 CE3  sing Y N 411 
TRP   NE1 CE2  sing Y N 412 
TRP   NE1 HE1  sing N N 413 
TRP   CE2 CZ2  sing Y N 414 
TRP   CE3 CZ3  doub Y N 415 
TRP   CE3 HE3  sing N N 416 
TRP   CZ2 CH2  doub Y N 417 
TRP   CZ2 HZ2  sing N N 418 
TRP   CZ3 CH2  sing Y N 419 
TRP   CZ3 HZ3  sing N N 420 
TRP   CH2 HH2  sing N N 421 
TRP   OXT HXT  sing N N 422 
TYR   N   CA   sing N N 423 
TYR   N   H    sing N N 424 
TYR   N   H2   sing N N 425 
TYR   CA  C    sing N N 426 
TYR   CA  CB   sing N N 427 
TYR   CA  HA   sing N N 428 
TYR   C   O    doub N N 429 
TYR   C   OXT  sing N N 430 
TYR   CB  CG   sing N N 431 
TYR   CB  HB2  sing N N 432 
TYR   CB  HB3  sing N N 433 
TYR   CG  CD1  doub Y N 434 
TYR   CG  CD2  sing Y N 435 
TYR   CD1 CE1  sing Y N 436 
TYR   CD1 HD1  sing N N 437 
TYR   CD2 CE2  doub Y N 438 
TYR   CD2 HD2  sing N N 439 
TYR   CE1 CZ   doub Y N 440 
TYR   CE1 HE1  sing N N 441 
TYR   CE2 CZ   sing Y N 442 
TYR   CE2 HE2  sing N N 443 
TYR   CZ  OH   sing N N 444 
TYR   OH  HH   sing N N 445 
TYR   OXT HXT  sing N N 446 
VAL   N   CA   sing N N 447 
VAL   N   H    sing N N 448 
VAL   N   H2   sing N N 449 
VAL   CA  C    sing N N 450 
VAL   CA  CB   sing N N 451 
VAL   CA  HA   sing N N 452 
VAL   C   O    doub N N 453 
VAL   C   OXT  sing N N 454 
VAL   CB  CG1  sing N N 455 
VAL   CB  CG2  sing N N 456 
VAL   CB  HB   sing N N 457 
VAL   CG1 HG11 sing N N 458 
VAL   CG1 HG12 sing N N 459 
VAL   CG1 HG13 sing N N 460 
VAL   CG2 HG21 sing N N 461 
VAL   CG2 HG22 sing N N 462 
VAL   CG2 HG23 sing N N 463 
VAL   OXT HXT  sing N N 464 
# 
_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                    9DO1 
_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]   0.008763 
_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]   0.008763 
_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]   0.004551 
_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   ? 24.06900 71.05800 23.80800 1.000 124.38664 ? 4   THR   A N   1 
ATOM   2    C  CA  . THR   A 1 7   ? 25.43300 70.54700 23.73900 1.000 124.64800 ? 4   THR   A CA  1 
ATOM   3    C  C   . THR   A 1 7   ? 25.57600 69.26700 24.55700 1.000 134.17529 ? 4   THR   A C   1 
ATOM   4    O  O   . THR   A 1 7   ? 24.79900 69.01800 25.47900 1.000 140.56789 ? 4   THR   A O   1 
ATOM   5    C  CB  . THR   A 1 7   ? 26.45200 71.58700 24.23800 1.000 119.43825 ? 4   THR   A CB  1 
ATOM   6    O  OG1 . THR   A 1 7   ? 26.32800 71.74100 25.65700 1.000 108.60985 ? 4   THR   A OG1 1 
ATOM   7    C  CG2 . THR   A 1 7   ? 26.21500 72.93000 23.56300 1.000 117.34623 ? 4   THR   A CG2 1 
ATOM   8    N  N   . ILE   A 1 8   ? 26.57800 68.45800 24.21500 1.000 132.26122 ? 5   ILE   A N   1 
ATOM   9    C  CA  . ILE   A 1 8   ? 26.81500 67.17900 24.87100 1.000 128.17203 ? 5   ILE   A CA  1 
ATOM   10   C  C   . ILE   A 1 8   ? 28.27000 67.10500 25.30800 1.000 126.98068 ? 5   ILE   A C   1 
ATOM   11   O  O   . ILE   A 1 8   ? 29.15500 67.71600 24.70100 1.000 124.01699 ? 5   ILE   A O   1 
ATOM   12   C  CB  . ILE   A 1 8   ? 26.46400 65.98900 23.95100 1.000 115.51618 ? 5   ILE   A CB  1 
ATOM   13   N  N   . LYS   A 1 9   ? 28.51400 66.34600 26.37400 1.000 128.56469 ? 6   LYS   A N   1 
ATOM   14   C  CA  . LYS   A 1 9   ? 29.85200 66.12700 26.90600 1.000 129.42070 ? 6   LYS   A CA  1 
ATOM   15   C  C   . LYS   A 1 9   ? 30.30200 64.71300 26.56600 1.000 129.80205 ? 6   LYS   A C   1 
ATOM   16   O  O   . LYS   A 1 9   ? 29.59600 63.74400 26.86700 1.000 129.05073 ? 6   LYS   A O   1 
ATOM   17   C  CB  . LYS   A 1 9   ? 29.88400 66.34500 28.42100 1.000 108.21722 ? 6   LYS   A CB  1 
ATOM   18   N  N   . VAL   A 1 10  ? 31.47100 64.59700 25.93800 1.000 119.71541 ? 7   VAL   A N   1 
ATOM   19   C  CA  . VAL   A 1 10  ? 32.01700 63.32200 25.50000 1.000 114.20462 ? 7   VAL   A CA  1 
ATOM   20   C  C   . VAL   A 1 10  ? 33.44500 63.18900 26.02200 1.000 109.86418 ? 7   VAL   A C   1 
ATOM   21   O  O   . VAL   A 1 10  ? 33.97600 64.08200 26.68100 1.000 105.21639 ? 7   VAL   A O   1 
ATOM   22   C  CB  . VAL   A 1 10  ? 31.98200 63.16500 23.96500 1.000 114.25561 ? 7   VAL   A CB  1 
ATOM   23   C  CG1 . VAL   A 1 10  ? 30.57700 63.40100 23.43100 1.000 116.36616 ? 7   VAL   A CG1 1 
ATOM   24   C  CG2 . VAL   A 1 10  ? 32.97700 64.11200 23.31200 1.000 109.98187 ? 7   VAL   A CG2 1 
ATOM   25   N  N   . PHE   A 1 11  ? 34.06300 62.05000 25.71000 1.000 113.07030 ? 8   PHE   A N   1 
ATOM   26   C  CA  . PHE   A 1 11  ? 35.45000 61.77300 26.06000 1.000 98.88233  ? 8   PHE   A CA  1 
ATOM   27   C  C   . PHE   A 1 11  ? 36.20900 61.39400 24.79800 1.000 95.96477  ? 8   PHE   A C   1 
ATOM   28   O  O   . PHE   A 1 11  ? 35.74900 60.54700 24.02500 1.000 90.38806  ? 8   PHE   A O   1 
ATOM   29   C  CB  . PHE   A 1 11  ? 35.55000 60.64300 27.09200 1.000 100.33469 ? 8   PHE   A CB  1 
ATOM   30   C  CG  . PHE   A 1 11  ? 35.16600 61.05300 28.48500 1.000 105.55227 ? 8   PHE   A CG  1 
ATOM   31   C  CD1 . PHE   A 1 11  ? 35.75700 62.15200 29.08700 1.000 106.43510 ? 8   PHE   A CD1 1 
ATOM   32   C  CD2 . PHE   A 1 11  ? 34.21600 60.33600 29.19500 1.000 101.11704 ? 8   PHE   A CD2 1 
ATOM   33   C  CE1 . PHE   A 1 11  ? 35.40600 62.53000 30.37000 1.000 111.67230 ? 8   PHE   A CE1 1 
ATOM   34   C  CE2 . PHE   A 1 11  ? 33.86100 60.70900 30.47800 1.000 105.04610 ? 8   PHE   A CE2 1 
ATOM   35   C  CZ  . PHE   A 1 11  ? 34.45700 61.80800 31.06700 1.000 110.86079 ? 8   PHE   A CZ  1 
ATOM   36   N  N   . THR   A 1 12  ? 37.36300 62.02000 24.58700 1.000 85.96497  ? 9   THR   A N   1 
ATOM   37   C  CA  . THR   A 1 12  ? 38.24700 61.68000 23.48400 1.000 85.90133  ? 9   THR   A CA  1 
ATOM   38   C  C   . THR   A 1 12  ? 39.45000 60.90900 24.00900 1.000 79.71671  ? 9   THR   A C   1 
ATOM   39   O  O   . THR   A 1 12  ? 39.89200 61.11400 25.14400 1.000 76.10126  ? 9   THR   A O   1 
ATOM   40   C  CB  . THR   A 1 12  ? 38.72400 62.92800 22.73300 1.000 78.94783  ? 9   THR   A CB  1 
ATOM   41   O  OG1 . THR   A 1 12  ? 39.27500 63.87100 23.66200 1.000 86.97350  ? 9   THR   A OG1 1 
ATOM   42   C  CG2 . THR   A 1 12  ? 37.57000 63.57000 21.98300 1.000 81.62517  ? 9   THR   A CG2 1 
ATOM   43   N  N   . THR   A 1 13  ? 39.97900 60.02000 23.17200 1.000 67.64085  ? 10  THR   A N   1 
ATOM   44   C  CA  . THR   A 1 13  ? 41.10700 59.19500 23.57600 1.000 71.53485  ? 10  THR   A CA  1 
ATOM   45   C  C   . THR   A 1 13  ? 41.76800 58.61300 22.33600 1.000 71.36319  ? 10  THR   A C   1 
ATOM   46   O  O   . THR   A 1 13  ? 41.19800 58.61600 21.24200 1.000 64.09692  ? 10  THR   A O   1 
ATOM   47   C  CB  . THR   A 1 13  ? 40.67000 58.07100 24.52500 1.000 74.67188  ? 10  THR   A CB  1 
ATOM   48   O  OG1 . THR   A 1 13  ? 41.80800 57.57200 25.23800 1.000 73.23713  ? 10  THR   A OG1 1 
ATOM   49   C  CG2 . THR   A 1 13  ? 40.02900 56.93100 23.74400 1.000 66.97302  ? 10  THR   A CG2 1 
ATOM   50   N  N   . VAL   A 1 14  ? 42.99100 58.12400 22.52500 1.000 70.39098  ? 11  VAL   A N   1 
ATOM   51   C  CA  . VAL   A 1 14  ? 43.66700 57.33600 21.50500 1.000 72.68016  ? 11  VAL   A CA  1 
ATOM   52   C  C   . VAL   A 1 14  ? 44.00800 55.93200 21.98100 1.000 68.46769  ? 11  VAL   A C   1 
ATOM   53   O  O   . VAL   A 1 14  ? 44.30100 55.06700 21.14000 1.000 67.37894  ? 11  VAL   A O   1 
ATOM   54   C  CB  . VAL   A 1 14  ? 44.94100 58.04500 20.99700 1.000 68.97206  ? 11  VAL   A CB  1 
ATOM   55   C  CG1 . VAL   A 1 14  ? 44.61100 59.43700 20.48700 1.000 69.51435  ? 11  VAL   A CG1 1 
ATOM   56   C  CG2 . VAL   A 1 14  ? 45.99500 58.10600 22.09200 1.000 67.87232  ? 11  VAL   A CG2 1 
ATOM   57   N  N   . ASP   A 1 15  ? 43.96700 55.66300 23.28900 1.000 63.44899  ? 12  ASP   A N   1 
ATOM   58   C  CA  . ASP   A 1 15  ? 44.35000 54.36900 23.83200 1.000 66.28185  ? 12  ASP   A CA  1 
ATOM   59   C  C   . ASP   A 1 15  ? 43.28000 53.73100 24.70600 1.000 78.65466  ? 12  ASP   A C   1 
ATOM   60   O  O   . ASP   A 1 15  ? 43.51300 52.63900 25.23800 1.000 85.50805  ? 12  ASP   A O   1 
ATOM   61   C  CB  . ASP   A 1 15  ? 45.64700 54.49600 24.65000 1.000 71.94025  ? 12  ASP   A CB  1 
ATOM   62   C  CG  . ASP   A 1 15  ? 45.57600 55.59400 25.70100 1.000 68.74359  ? 12  ASP   A CG  1 
ATOM   63   O  OD1 . ASP   A 1 15  ? 44.46200 56.07500 26.00000 1.000 65.92575  ? 12  ASP   A OD1 1 
ATOM   64   O  OD2 . ASP   A 1 15  ? 46.63900 55.97600 26.23400 1.000 63.72351  ? 12  ASP   A OD2 1 
ATOM   65   N  N   . ASN   A 1 16  ? 42.12800 54.37900 24.88200 1.000 76.07885  ? 13  ASN   A N   1 
ATOM   66   C  CA  . ASN   A 1 16  ? 41.07000 53.92800 25.78500 1.000 84.80997  ? 13  ASN   A CA  1 
ATOM   67   C  C   . ASN   A 1 16  ? 41.55500 53.80300 27.22700 1.000 71.43436  ? 13  ASN   A C   1 
ATOM   68   O  O   . ASN   A 1 16  ? 40.97400 53.05300 28.01800 1.000 84.34774  ? 13  ASN   A O   1 
ATOM   69   C  CB  . ASN   A 1 16  ? 40.45900 52.60100 25.31900 1.000 85.74516  ? 13  ASN   A CB  1 
ATOM   70   C  CG  . ASN   A 1 16  ? 38.99400 52.47600 25.68100 1.000 92.03720  ? 13  ASN   A CG  1 
ATOM   71   O  OD1 . ASN   A 1 16  ? 38.33000 53.46800 25.98400 1.000 85.94486  ? 13  ASN   A OD1 1 
ATOM   72   N  ND2 . ASN   A 1 16  ? 38.48000 51.25100 25.65400 1.000 96.40518  ? 13  ASN   A ND2 1 
ATOM   73   N  N   . ILE   A 1 17  ? 42.61600 54.52500 27.58400 1.000 77.98543  ? 14  ILE   A N   1 
ATOM   74   C  CA  . ILE   A 1 17  ? 43.11200 54.55700 28.95600 1.000 74.65178  ? 14  ILE   A CA  1 
ATOM   75   C  C   . ILE   A 1 17  ? 43.13500 56.00100 29.43400 1.000 73.25746  ? 14  ILE   A C   1 
ATOM   76   O  O   . ILE   A 1 17  ? 42.39300 56.37700 30.34900 1.000 91.44307  ? 14  ILE   A O   1 
ATOM   77   C  CB  . ILE   A 1 17  ? 44.50700 53.91600 29.07200 1.000 77.93364  ? 14  ILE   A CB  1 
ATOM   78   C  CG1 . ILE   A 1 17  ? 44.44100 52.42900 28.73100 1.000 72.82965  ? 14  ILE   A CG1 1 
ATOM   79   C  CG2 . ILE   A 1 17  ? 45.07600 54.11900 30.47000 1.000 70.98583  ? 14  ILE   A CG2 1 
ATOM   80   C  CD1 . ILE   A 1 17  ? 45.72300 51.89100 28.16000 1.000 80.30828  ? 14  ILE   A CD1 1 
ATOM   81   N  N   . ASN   A 1 18  ? 43.98500 56.81900 28.82200 1.000 77.03671  ? 15  ASN   A N   1 
ATOM   82   C  CA  . ASN   A 1 18  ? 44.04600 58.24400 29.13500 1.000 79.85129  ? 15  ASN   A CA  1 
ATOM   83   C  C   . ASN   A 1 18  ? 42.87400 58.92900 28.44400 1.000 71.62515  ? 15  ASN   A C   1 
ATOM   84   O  O   . ASN   A 1 18  ? 42.94800 59.27400 27.26400 1.000 80.03754  ? 15  ASN   A O   1 
ATOM   85   C  CB  . ASN   A 1 18  ? 45.38200 58.83200 28.69600 1.000 75.86400  ? 15  ASN   A CB  1 
ATOM   86   C  CG  . ASN   A 1 18  ? 46.56600 58.13000 29.33500 1.000 82.52204  ? 15  ASN   A CG  1 
ATOM   87   O  OD1 . ASN   A 1 18  ? 46.78200 58.22700 30.54300 1.000 86.18841  ? 15  ASN   A OD1 1 
ATOM   88   N  ND2 . ASN   A 1 18  ? 47.33600 57.40900 28.52700 1.000 74.85108  ? 15  ASN   A ND2 1 
ATOM   89   N  N   . LEU   A 1 19  ? 41.78200 59.12100 29.17700 1.000 79.29603  ? 16  LEU   A N   1 
ATOM   90   C  CA  . LEU   A 1 19  ? 40.58900 59.75300 28.63200 1.000 88.63250  ? 16  LEU   A CA  1 
ATOM   91   C  C   . LEU   A 1 19  ? 40.63400 61.25600 28.87300 1.000 89.57195  ? 16  LEU   A C   1 
ATOM   92   O  O   . LEU   A 1 19  ? 41.01600 61.71400 29.95400 1.000 80.00549  ? 16  LEU   A O   1 
ATOM   93   C  CB  . LEU   A 1 19  ? 39.32400 59.15800 29.25600 1.000 92.98171  ? 16  LEU   A CB  1 
ATOM   94   C  CG  . LEU   A 1 19  ? 39.14400 57.63500 29.27000 1.000 92.01239  ? 16  LEU   A CG  1 
ATOM   95   C  CD1 . LEU   A 1 19  ? 37.66700 57.28900 29.32800 1.000 99.89797  ? 16  LEU   A CD1 1 
ATOM   96   C  CD2 . LEU   A 1 19  ? 39.78700 56.97500 28.06000 1.000 82.44354  ? 16  LEU   A CD2 1 
ATOM   97   N  N   . HIS   A 1 20  ? 40.24000 62.02300 27.85900 1.000 86.32401  ? 17  HIS   A N   1 
ATOM   98   C  CA  . HIS   A 1 20  ? 40.28400 63.47800 27.90600 1.000 92.41431  ? 17  HIS   A CA  1 
ATOM   99   C  C   . HIS   A 1 20  ? 38.87000 64.02700 27.79200 1.000 91.69429  ? 17  HIS   A C   1 
ATOM   100  O  O   . HIS   A 1 20  ? 38.13000 63.65800 26.87400 1.000 93.59562  ? 17  HIS   A O   1 
ATOM   101  C  CB  . HIS   A 1 20  ? 41.17300 64.03300 26.78600 1.000 88.36590  ? 17  HIS   A CB  1 
ATOM   102  C  CG  . HIS   A 1 20  ? 42.58500 63.53500 26.83600 1.000 91.07736  ? 17  HIS   A CG  1 
ATOM   103  N  ND1 . HIS   A 1 20  ? 43.58100 64.19400 27.52400 1.000 98.95092  ? 17  HIS   A ND1 1 
ATOM   104  C  CD2 . HIS   A 1 20  ? 43.16700 62.44400 26.28500 1.000 75.40687  ? 17  HIS   A CD2 1 
ATOM   105  C  CE1 . HIS   A 1 20  ? 44.71600 63.53000 27.39600 1.000 79.27301  ? 17  HIS   A CE1 1 
ATOM   106  N  NE2 . HIS   A 1 20  ? 44.49300 62.46400 26.64800 1.000 83.33557  ? 17  HIS   A NE2 1 
ATOM   107  N  N   . THR   A 1 21  ? 38.49600 64.89800 28.72500 1.000 102.39158 ? 18  THR   A N   1 
ATOM   108  C  CA  . THR   A 1 21  ? 37.14600 65.44100 28.74200 1.000 105.73452 ? 18  THR   A CA  1 
ATOM   109  C  C   . THR   A 1 21  ? 37.01000 66.56800 27.72300 1.000 106.57635 ? 18  THR   A C   1 
ATOM   110  O  O   . THR   A 1 21  ? 37.91000 67.39700 27.55700 1.000 102.31652 ? 18  THR   A O   1 
ATOM   111  C  CB  . THR   A 1 21  ? 36.77100 65.91500 30.15300 1.000 97.54235  ? 18  THR   A CB  1 
ATOM   112  O  OG1 . THR   A 1 21  ? 35.34400 66.01000 30.27100 1.000 115.37535 ? 18  THR   A OG1 1 
ATOM   113  C  CG2 . THR   A 1 21  ? 37.42000 67.25200 30.51300 1.000 104.77033 ? 18  THR   A CG2 1 
ATOM   114  N  N   . GLN   A 1 22  ? 35.89700 66.55100 26.99100 1.000 98.37042  ? 19  GLN   A N   1 
ATOM   115  C  CA  . GLN   A 1 22  ? 35.63000 67.54600 25.96200 1.000 105.69890 ? 19  GLN   A CA  1 
ATOM   116  C  C   . GLN   A 1 22  ? 34.13400 67.82000 25.92000 1.000 113.47774 ? 19  GLN   A C   1 
ATOM   117  O  O   . GLN   A 1 22  ? 33.31600 66.93300 26.18000 1.000 110.85714 ? 19  GLN   A O   1 
ATOM   118  C  CB  . GLN   A 1 22  ? 36.11300 67.09700 24.57200 1.000 101.67289 ? 19  GLN   A CB  1 
ATOM   119  C  CG  . GLN   A 1 22  ? 37.54300 66.56900 24.50200 1.000 96.92268  ? 19  GLN   A CG  1 
ATOM   120  C  CD  . GLN   A 1 22  ? 38.57600 67.67500 24.39300 1.000 99.49500  ? 19  GLN   A CD  1 
ATOM   121  O  OE1 . GLN   A 1 22  ? 38.44200 68.58500 23.57700 1.000 106.44198 ? 19  GLN   A OE1 1 
ATOM   122  N  NE2 . GLN   A 1 22  ? 39.61300 67.60200 25.22200 1.000 98.75300  ? 19  GLN   A NE2 1 
ATOM   123  N  N   . VAL   A 1 23  ? 33.78500 69.06100 25.59000 1.000 114.40041 ? 20  VAL   A N   1 
ATOM   124  C  CA  . VAL   A 1 23  ? 32.40100 69.47400 25.39900 1.000 119.53897 ? 20  VAL   A CA  1 
ATOM   125  C  C   . VAL   A 1 23  ? 32.22400 69.87300 23.94100 1.000 114.91784 ? 20  VAL   A C   1 
ATOM   126  O  O   . VAL   A 1 23  ? 32.98900 70.69200 23.41800 1.000 108.08695 ? 20  VAL   A O   1 
ATOM   127  C  CB  . VAL   A 1 23  ? 32.01200 70.62500 26.34700 1.000 112.68214 ? 20  VAL   A CB  1 
ATOM   128  C  CG1 . VAL   A 1 23  ? 33.09500 71.69700 26.37400 1.000 107.54511 ? 20  VAL   A CG1 1 
ATOM   129  C  CG2 . VAL   A 1 23  ? 30.67200 71.21700 25.93800 1.000 111.16266 ? 20  VAL   A CG2 1 
ATOM   130  N  N   . VAL   A 1 24  ? 31.22800 69.28400 23.28500 1.000 115.15626 ? 21  VAL   A N   1 
ATOM   131  C  CA  . VAL   A 1 24  ? 31.02100 69.47000 21.85700 1.000 122.50866 ? 21  VAL   A CA  1 
ATOM   132  C  C   . VAL   A 1 24  ? 29.75200 70.27800 21.62500 1.000 124.43176 ? 21  VAL   A C   1 
ATOM   133  O  O   . VAL   A 1 24  ? 28.88600 70.40400 22.49600 1.000 129.45530 ? 21  VAL   A O   1 
ATOM   134  C  CB  . VAL   A 1 24  ? 30.95000 68.12400 21.10400 1.000 112.93986 ? 21  VAL   A CB  1 
ATOM   135  C  CG1 . VAL   A 1 24  ? 32.02900 67.18500 21.60000 1.000 108.85227 ? 21  VAL   A CG1 1 
ATOM   136  C  CG2 . VAL   A 1 24  ? 29.57400 67.49200 21.26100 1.000 114.73396 ? 21  VAL   A CG2 1 
ATOM   137  N  N   . ASP   A 1 25  ? 29.65200 70.83400 20.42200 1.000 122.32462 ? 22  ASP   A N   1 
ATOM   138  C  CA  . ASP   A 1 25  ? 28.45900 71.53300 19.96800 1.000 129.81523 ? 22  ASP   A CA  1 
ATOM   139  C  C   . ASP   A 1 25  ? 27.70900 70.63900 18.99100 1.000 131.10738 ? 22  ASP   A C   1 
ATOM   140  O  O   . ASP   A 1 25  ? 28.29700 70.13500 18.02800 1.000 129.52048 ? 22  ASP   A O   1 
ATOM   141  C  CB  . ASP   A 1 25  ? 28.82300 72.86100 19.30300 1.000 131.12665 ? 22  ASP   A CB  1 
ATOM   142  C  CG  . ASP   A 1 25  ? 27.61500 73.57800 18.72500 1.000 136.58393 ? 22  ASP   A CG  1 
ATOM   143  O  OD1 . ASP   A 1 25  ? 26.48900 73.35300 19.21700 1.000 144.84008 ? 22  ASP   A OD1 1 
ATOM   144  O  OD2 . ASP   A 1 25  ? 27.79400 74.36700 17.77400 1.000 132.74200 ? 22  ASP   A OD2 1 
ATOM   145  N  N   . MET   A 1 26  ? 26.41200 70.44600 19.23900 1.000 126.11281 ? 23  MET   A N   1 
ATOM   146  C  CA  . MET   A 1 26  ? 25.61200 69.56200 18.40200 1.000 131.66987 ? 23  MET   A CA  1 
ATOM   147  C  C   . MET   A 1 26  ? 25.41200 70.10400 16.99200 1.000 129.16192 ? 23  MET   A C   1 
ATOM   148  O  O   . MET   A 1 26  ? 24.96400 69.35400 16.11800 1.000 116.99925 ? 23  MET   A O   1 
ATOM   149  C  CB  . MET   A 1 26  ? 24.25200 69.30800 19.05700 1.000 133.29600 ? 23  MET   A CB  1 
ATOM   150  C  CG  . MET   A 1 26  ? 24.30900 69.14400 20.57300 1.000 126.72353 ? 23  MET   A CG  1 
ATOM   151  S  SD  . MET   A 1 26  ? 23.34600 67.75600 21.21400 1.000 147.76231 ? 23  MET   A SD  1 
ATOM   152  C  CE  . MET   A 1 26  ? 24.38500 66.36900 20.76900 1.000 118.20334 ? 23  MET   A CE  1 
ATOM   153  N  N   . SER   A 1 27  ? 25.72500 71.38000 16.75000 1.000 128.82362 ? 24  SER   A N   1 
ATOM   154  C  CA  . SER   A 1 27  ? 25.59200 71.93900 15.40900 1.000 134.17104 ? 24  SER   A CA  1 
ATOM   155  C  C   . SER   A 1 27  ? 26.74200 71.49500 14.51200 1.000 134.59417 ? 24  SER   A C   1 
ATOM   156  O  O   . SER   A 1 27  ? 26.51700 70.98800 13.40700 1.000 125.54173 ? 24  SER   A O   1 
ATOM   157  C  CB  . SER   A 1 27  ? 25.52200 73.46700 15.47700 1.000 130.05425 ? 24  SER   A CB  1 
ATOM   158  O  OG  . SER   A 1 27  ? 26.79700 74.05200 15.26800 1.000 129.39273 ? 24  SER   A OG  1 
ATOM   159  N  N   . MET   A 1 28  ? 27.97800 71.67300 14.97300 1.000 138.21389 ? 25  MET   A N   1 
ATOM   160  C  CA  . MET   A 1 28  ? 29.14000 71.26600 14.19900 1.000 125.19367 ? 25  MET   A CA  1 
ATOM   161  C  C   . MET   A 1 28  ? 29.37900 69.76900 14.33600 1.000 123.15498 ? 25  MET   A C   1 
ATOM   162  O  O   . MET   A 1 28  ? 29.23200 69.19600 15.41900 1.000 121.57169 ? 25  MET   A O   1 
ATOM   163  C  CB  . MET   A 1 28  ? 30.39000 72.02500 14.64600 1.000 118.70533 ? 25  MET   A CB  1 
ATOM   164  C  CG  . MET   A 1 28  ? 30.13500 73.42800 15.16000 1.000 119.36146 ? 25  MET   A CG  1 
ATOM   165  S  SD  . MET   A 1 28  ? 31.62500 74.17500 15.85300 1.000 129.65668 ? 25  MET   A SD  1 
ATOM   166  C  CE  . MET   A 1 28  ? 30.98000 74.94800 17.33500 1.000 101.40067 ? 25  MET   A CE  1 
ATOM   167  N  N   . THR   A 1 29  ? 29.76100 69.14100 13.22800 1.000 118.22596 ? 26  THR   A N   1 
ATOM   168  C  CA  . THR   A 1 29  ? 30.04200 67.71700 13.23000 1.000 114.46664 ? 26  THR   A CA  1 
ATOM   169  C  C   . THR   A 1 29  ? 31.36700 67.44300 13.94200 1.000 111.38585 ? 26  THR   A C   1 
ATOM   170  O  O   . THR   A 1 29  ? 32.14800 68.35300 14.23400 1.000 111.40294 ? 26  THR   A O   1 
ATOM   171  C  CB  . THR   A 1 29  ? 30.05400 67.18000 11.79700 1.000 114.82858 ? 26  THR   A CB  1 
ATOM   172  O  OG1 . THR   A 1 29  ? 31.04800 67.87000 11.03100 1.000 111.00092 ? 26  THR   A OG1 1 
ATOM   173  C  CG2 . THR   A 1 29  ? 28.69900 67.35200 11.13500 1.000 119.66727 ? 26  THR   A CG2 1 
ATOM   174  N  N   . TYR   A 1 30  ? 31.61100 66.15900 14.22500 1.000 108.12488 ? 27  TYR   A N   1 
ATOM   175  C  CA  . TYR   A 1 30  ? 32.79100 65.77300 14.99400 1.000 105.24036 ? 27  TYR   A CA  1 
ATOM   176  C  C   . TYR   A 1 30  ? 34.08400 66.11800 14.26800 1.000 95.76842  ? 27  TYR   A C   1 
ATOM   177  O  O   . TYR   A 1 30  ? 35.08400 66.45800 14.91100 1.000 91.76208  ? 27  TYR   A O   1 
ATOM   178  C  CB  . TYR   A 1 30  ? 32.74600 64.27700 15.30700 1.000 94.21043  ? 27  TYR   A CB  1 
ATOM   179  C  CG  . TYR   A 1 30  ? 31.75800 63.91100 16.39100 1.000 94.28414  ? 27  TYR   A CG  1 
ATOM   180  C  CD1 . TYR   A 1 30  ? 31.84500 64.47800 17.65600 1.000 95.77675  ? 27  TYR   A CD1 1 
ATOM   181  C  CD2 . TYR   A 1 30  ? 30.73400 63.00400 16.14800 1.000 92.58861  ? 27  TYR   A CD2 1 
ATOM   182  C  CE1 . TYR   A 1 30  ? 30.94200 64.15100 18.65200 1.000 97.69089  ? 27  TYR   A CE1 1 
ATOM   183  C  CE2 . TYR   A 1 30  ? 29.82600 62.67000 17.13900 1.000 106.73682 ? 27  TYR   A CE2 1 
ATOM   184  C  CZ  . TYR   A 1 30  ? 29.93500 63.24700 18.38700 1.000 100.83988 ? 27  TYR   A CZ  1 
ATOM   185  O  OH  . TYR   A 1 30  ? 29.03300 62.91700 19.37200 1.000 102.12351 ? 27  TYR   A OH  1 
ATOM   186  N  N   . GLY   A 1 31  ? 34.08600 66.03900 12.93500 1.000 96.51055  ? 28  GLY   A N   1 
ATOM   187  C  CA  . GLY   A 1 31  ? 35.30700 66.28800 12.18800 1.000 89.16613  ? 28  GLY   A CA  1 
ATOM   188  C  C   . GLY   A 1 31  ? 35.78700 67.72200 12.26700 1.000 100.44654 ? 28  GLY   A C   1 
ATOM   189  O  O   . GLY   A 1 31  ? 36.98800 67.98400 12.15300 1.000 96.67655  ? 28  GLY   A O   1 
ATOM   190  N  N   . GLN   A 1 32  ? 34.86100 68.64300 12.52000 1.000 105.63516 ? 29  GLN   A N   1 
ATOM   191  C  CA  . GLN   A 1 32  ? 35.22900 70.08000 12.53900 1.000 108.54363 ? 29  GLN   A CA  1 
ATOM   192  C  C   . GLN   A 1 32  ? 35.81300 70.43400 13.90500 1.000 104.21736 ? 29  GLN   A C   1 
ATOM   193  O  O   . GLN   A 1 32  ? 36.64800 71.34900 13.96400 1.000 113.94896 ? 29  GLN   A O   1 
ATOM   194  C  CB  . GLN   A 1 32  ? 33.98800 70.91500 12.22800 1.000 122.16116 ? 29  GLN   A CB  1 
ATOM   195  C  CG  . GLN   A 1 32  ? 33.39100 70.62100 10.85800 1.000 125.02355 ? 29  GLN   A CG  1 
ATOM   196  C  CD  . GLN   A 1 32  ? 32.51300 71.73600 10.34300 1.000 140.50523 ? 29  GLN   A CD  1 
ATOM   197  O  OE1 . GLN   A 1 32  ? 31.40200 71.94400 10.82500 1.000 132.19586 ? 29  GLN   A OE1 1 
ATOM   198  N  NE2 . GLN   A 1 32  ? 33.00700 72.46000 9.35200  1.000 148.20062 ? 29  GLN   A NE2 1 
ATOM   199  N  N   . GLN   A 1 33  ? 35.40600 69.72400 14.95100 1.000 99.22836  ? 30  GLN   A N   1 
ATOM   200  C  CA  . GLN   A 1 33  ? 35.84700 70.01900 16.30900 1.000 101.09121 ? 30  GLN   A CA  1 
ATOM   201  C  C   . GLN   A 1 33  ? 37.02200 69.15800 16.75300 1.000 98.37278  ? 30  GLN   A C   1 
ATOM   202  O  O   . GLN   A 1 33  ? 37.97300 69.67700 17.34600 1.000 93.17521  ? 30  GLN   A O   1 
ATOM   203  C  CB  . GLN   A 1 33  ? 34.68500 69.84100 17.29200 1.000 104.22977 ? 30  GLN   A CB  1 
ATOM   204  C  CG  . GLN   A 1 33  ? 33.30800 69.99600 16.66500 1.000 103.25360 ? 30  GLN   A CG  1 
ATOM   205  C  CD  . GLN   A 1 33  ? 32.21000 70.16900 17.69700 1.000 111.37883 ? 30  GLN   A CD  1 
ATOM   206  O  OE1 . GLN   A 1 33  ? 32.40400 70.81600 18.72600 1.000 100.58154 ? 30  GLN   A OE1 1 
ATOM   207  N  NE2 . GLN   A 1 33  ? 31.04800 69.58300 17.42700 1.000 107.91713 ? 30  GLN   A NE2 1 
ATOM   208  N  N   . PHE   A 1 34  ? 36.98500 67.85200 16.47800 1.000 97.97914  ? 31  PHE   A N   1 
ATOM   209  C  CA  . PHE   A 1 34  ? 38.04200 66.94300 16.90100 1.000 88.50532  ? 31  PHE   A CA  1 
ATOM   210  C  C   . PHE   A 1 34  ? 38.94000 66.46900 15.77100 1.000 79.60069  ? 31  PHE   A C   1 
ATOM   211  O  O   . PHE   A 1 34  ? 40.08200 66.08000 16.03600 1.000 76.18483  ? 31  PHE   A O   1 
ATOM   212  C  CB  . PHE   A 1 34  ? 37.44500 65.70400 17.58300 1.000 83.61687  ? 31  PHE   A CB  1 
ATOM   213  C  CG  . PHE   A 1 34  ? 36.73500 66.00200 18.86600 1.000 90.34580  ? 31  PHE   A CG  1 
ATOM   214  C  CD1 . PHE   A 1 34  ? 37.14100 67.05200 19.67100 1.000 86.64958  ? 31  PHE   A CD1 1 
ATOM   215  C  CD2 . PHE   A 1 34  ? 35.66000 65.22900 19.26800 1.000 92.80607  ? 31  PHE   A CD2 1 
ATOM   216  C  CE1 . PHE   A 1 34  ? 36.48600 67.32500 20.85300 1.000 91.99278  ? 31  PHE   A CE1 1 
ATOM   217  C  CE2 . PHE   A 1 34  ? 35.00200 65.49700 20.44900 1.000 91.02466  ? 31  PHE   A CE2 1 
ATOM   218  C  CZ  . PHE   A 1 34  ? 35.41700 66.54600 21.24200 1.000 94.09503  ? 31  PHE   A CZ  1 
ATOM   219  N  N   . GLY   A 1 35  ? 38.46200 66.49100 14.53200 1.000 83.68575  ? 32  GLY   A N   1 
ATOM   220  C  CA  . GLY   A 1 35  ? 39.14500 65.83600 13.44600 1.000 67.34952  ? 32  GLY   A CA  1 
ATOM   221  C  C   . GLY   A 1 35  ? 38.52300 64.47900 13.20100 1.000 75.45454  ? 32  GLY   A C   1 
ATOM   222  O  O   . GLY   A 1 35  ? 37.37200 64.23000 13.57400 1.000 77.37615  ? 32  GLY   A O   1 
ATOM   223  N  N   . PRO   A 1 36  ? 39.26800 63.57300 12.57000 1.000 74.22212  ? 33  PRO   A N   1 
ATOM   224  C  CA  . PRO   A 1 36  ? 38.75900 62.20500 12.37700 1.000 70.89299  ? 33  PRO   A CA  1 
ATOM   225  C  C   . PRO   A 1 36  ? 38.41800 61.55900 13.71300 1.000 78.45770  ? 33  PRO   A C   1 
ATOM   226  O  O   . PRO   A 1 36  ? 39.28200 61.36800 14.57200 1.000 65.19090  ? 33  PRO   A O   1 
ATOM   227  C  CB  . PRO   A 1 36  ? 39.91900 61.49200 11.67200 1.000 72.71444  ? 33  PRO   A CB  1 
ATOM   228  C  CG  . PRO   A 1 36  ? 40.69800 62.59400 11.01700 1.000 65.84340  ? 33  PRO   A CG  1 
ATOM   229  C  CD  . PRO   A 1 36  ? 40.58200 63.77500 11.93800 1.000 64.39040  ? 33  PRO   A CD  1 
ATOM   230  N  N   . THR   A 1 37  ? 37.13700 61.23900 13.88800 1.000 68.29283  ? 34  THR   A N   1 
ATOM   231  C  CA  . THR   A 1 37  ? 36.61200 60.69000 15.12900 1.000 76.64781  ? 34  THR   A CA  1 
ATOM   232  C  C   . THR   A 1 37  ? 35.90600 59.37100 14.84400 1.000 86.25225  ? 34  THR   A C   1 
ATOM   233  O  O   . THR   A 1 37  ? 35.34000 59.17400 13.76400 1.000 84.25476  ? 34  THR   A O   1 
ATOM   234  C  CB  . THR   A 1 37  ? 35.64200 61.67200 15.80000 1.000 74.24779  ? 34  THR   A CB  1 
ATOM   235  O  OG1 . THR   A 1 37  ? 36.15400 63.00500 15.68000 1.000 78.60336  ? 34  THR   A OG1 1 
ATOM   236  C  CG2 . THR   A 1 37  ? 35.47100 61.34300 17.27100 1.000 82.88433  ? 34  THR   A CG2 1 
ATOM   237  N  N   . TYR   A 1 38  ? 35.94500 58.46300 15.81900 1.000 70.59125  ? 35  TYR   A N   1 
ATOM   238  C  CA  . TYR   A 1 38  ? 35.38600 57.13000 15.64900 1.000 76.61543  ? 35  TYR   A CA  1 
ATOM   239  C  C   . TYR   A 1 38  ? 34.64300 56.70800 16.90700 1.000 80.25219  ? 35  TYR   A C   1 
ATOM   240  O  O   . TYR   A 1 38  ? 34.99800 57.10000 18.02200 1.000 86.99257  ? 35  TYR   A O   1 
ATOM   241  C  CB  . TYR   A 1 38  ? 36.47200 56.09300 15.32900 1.000 65.87864  ? 35  TYR   A CB  1 
ATOM   242  C  CG  . TYR   A 1 38  ? 37.32500 56.42800 14.12600 1.000 68.49486  ? 35  TYR   A CG  1 
ATOM   243  C  CD1 . TYR   A 1 38  ? 38.48400 57.18400 14.26100 1.000 63.19547  ? 35  TYR   A CD1 1 
ATOM   244  C  CD2 . TYR   A 1 38  ? 36.97700 55.98100 12.85700 1.000 64.14840  ? 35  TYR   A CD2 1 
ATOM   245  C  CE1 . TYR   A 1 38  ? 39.26900 57.49100 13.16600 1.000 62.67320  ? 35  TYR   A CE1 1 
ATOM   246  C  CE2 . TYR   A 1 38  ? 37.75700 56.28200 11.75400 1.000 58.07457  ? 35  TYR   A CE2 1 
ATOM   247  C  CZ  . TYR   A 1 38  ? 38.90100 57.03700 11.91500 1.000 72.81944  ? 35  TYR   A CZ  1 
ATOM   248  O  OH  . TYR   A 1 38  ? 39.68200 57.34000 10.82400 1.000 68.31934  ? 35  TYR   A OH  1 
ATOM   249  N  N   . LEU   A 1 39  ? 33.60200 55.90000 16.71000 1.000 87.22067  ? 36  LEU   A N   1 
ATOM   250  C  CA  . LEU   A 1 39  ? 32.86800 55.25500 17.79700 1.000 103.97444 ? 36  LEU   A CA  1 
ATOM   251  C  C   . LEU   A 1 39  ? 32.75400 53.77100 17.48000 1.000 103.62832 ? 36  LEU   A C   1 
ATOM   252  O  O   . LEU   A 1 39  ? 32.02900 53.38700 16.55500 1.000 96.77480  ? 36  LEU   A O   1 
ATOM   253  C  CB  . LEU   A 1 39  ? 31.48200 55.86800 17.98800 1.000 98.63204  ? 36  LEU   A CB  1 
ATOM   254  C  CG  . LEU   A 1 39  ? 31.20100 56.51700 19.34400 1.000 96.62985  ? 36  LEU   A CG  1 
ATOM   255  C  CD1 . LEU   A 1 39  ? 29.75400 56.99200 19.42000 1.000 97.49089  ? 36  LEU   A CD1 1 
ATOM   256  C  CD2 . LEU   A 1 39  ? 31.52100 55.55700 20.47500 1.000 98.59084  ? 36  LEU   A CD2 1 
ATOM   257  N  N   . ASP   A 1 40  ? 33.46800 52.94800 18.24600 1.000 95.09587  ? 37  ASP   A N   1 
ATOM   258  C  CA  . ASP   A 1 40  ? 33.41300 51.49300 18.11900 1.000 96.44272  ? 37  ASP   A CA  1 
ATOM   259  C  C   . ASP   A 1 40  ? 33.71600 51.05600 16.68700 1.000 99.73654  ? 37  ASP   A C   1 
ATOM   260  O  O   . ASP   A 1 40  ? 33.03500 50.20600 16.10800 1.000 106.33833 ? 37  ASP   A O   1 
ATOM   261  C  CB  . ASP   A 1 40  ? 32.05900 50.95900 18.58800 1.000 98.72386  ? 37  ASP   A CB  1 
ATOM   262  C  CG  . ASP   A 1 40  ? 31.59100 51.61000 19.87700 1.000 115.51437 ? 37  ASP   A CG  1 
ATOM   263  O  OD1 . ASP   A 1 40  ? 32.41400 51.75900 20.80500 1.000 115.87530 ? 37  ASP   A OD1 1 
ATOM   264  O  OD2 . ASP   A 1 40  ? 30.40000 51.97700 19.96100 1.000 124.64454 ? 37  ASP   A OD2 1 
ATOM   265  N  N   . GLY   A 1 41  ? 34.75800 51.65500 16.11100 1.000 94.09226  ? 38  GLY   A N   1 
ATOM   266  C  CA  . GLY   A 1 41  ? 35.16100 51.35700 14.75300 1.000 83.54593  ? 38  GLY   A CA  1 
ATOM   267  C  C   . GLY   A 1 41  ? 34.39500 52.08700 13.67200 1.000 83.99418  ? 38  GLY   A C   1 
ATOM   268  O  O   . GLY   A 1 41  ? 34.80000 52.02500 12.50300 1.000 98.35126  ? 38  GLY   A O   1 
ATOM   269  N  N   . ALA   A 1 42  ? 33.30900 52.77800 14.01000 1.000 89.90568  ? 39  ALA   A N   1 
ATOM   270  C  CA  . ALA   A 1 42  ? 32.49400 53.46700 13.01900 1.000 93.67203  ? 39  ALA   A CA  1 
ATOM   271  C  C   . ALA   A 1 42  ? 32.95700 54.91100 12.87100 1.000 89.98461  ? 39  ALA   A C   1 
ATOM   272  O  O   . ALA   A 1 42  ? 33.10700 55.62800 13.86600 1.000 93.08853  ? 39  ALA   A O   1 
ATOM   273  C  CB  . ALA   A 1 42  ? 31.01600 53.42200 13.40900 1.000 101.36045 ? 39  ALA   A CB  1 
ATOM   274  N  N   . ASP   A 1 43  ? 33.17400 55.33200 11.62700 1.000 93.48186  ? 40  ASP   A N   1 
ATOM   275  C  CA  . ASP   A 1 43  ? 33.62700 56.69000 11.34200 1.000 86.74993  ? 40  ASP   A CA  1 
ATOM   276  C  C   . ASP   A 1 43  ? 32.49500 57.67400 11.61200 1.000 84.14240  ? 40  ASP   A C   1 
ATOM   277  O  O   . ASP   A 1 43  ? 31.50300 57.70800 10.87800 1.000 102.36139 ? 40  ASP   A O   1 
ATOM   278  C  CB  . ASP   A 1 43  ? 34.10500 56.78900 9.89700  1.000 71.74506  ? 40  ASP   A CB  1 
ATOM   279  C  CG  . ASP   A 1 43  ? 35.10200 57.91000 9.68900  1.000 78.16242  ? 40  ASP   A CG  1 
ATOM   280  O  OD1 . ASP   A 1 43  ? 35.01900 58.91800 10.42000 1.000 86.66952  ? 40  ASP   A OD1 1 
ATOM   281  O  OD2 . ASP   A 1 43  ? 35.96800 57.78400 8.79700  1.000 79.15691  ? 40  ASP   A OD2 1 
ATOM   282  N  N   . VAL   A 1 44  ? 32.64100 58.47800 12.66400 1.000 85.53756  ? 41  VAL   A N   1 
ATOM   283  C  CA  . VAL   A 1 44  ? 31.62900 59.46400 13.02900 1.000 89.55402  ? 41  VAL   A CA  1 
ATOM   284  C  C   . VAL   A 1 44  ? 32.15800 60.86300 12.74500 1.000 91.37385  ? 41  VAL   A C   1 
ATOM   285  O  O   . VAL   A 1 44  ? 31.74100 61.83900 13.38000 1.000 96.95610  ? 41  VAL   A O   1 
ATOM   286  C  CB  . VAL   A 1 44  ? 31.21300 59.31800 14.50400 1.000 80.32321  ? 41  VAL   A CB  1 
ATOM   287  C  CG1 . VAL   A 1 44  ? 30.50000 57.99400 14.72100 1.000 91.24357  ? 41  VAL   A CG1 1 
ATOM   288  C  CG2 . VAL   A 1 44  ? 32.42700 59.42900 15.41300 1.000 90.11281  ? 41  VAL   A CG2 1 
ATOM   289  N  N   . THR   A 1 45  ? 33.08200 60.97000 11.78700 1.000 82.91021  ? 42  THR   A N   1 
ATOM   290  C  CA  . THR   A 1 45  ? 33.63700 62.27200 11.43000 1.000 93.65055  ? 42  THR   A CA  1 
ATOM   291  C  C   . THR   A 1 45  ? 32.57200 63.17700 10.82200 1.000 105.20865 ? 42  THR   A C   1 
ATOM   292  O  O   . THR   A 1 45  ? 32.36000 64.30200 11.28700 1.000 107.41500 ? 42  THR   A O   1 
ATOM   293  C  CB  . THR   A 1 45  ? 34.80800 62.09500 10.46200 1.000 94.55541  ? 42  THR   A CB  1 
ATOM   294  O  OG1 . THR   A 1 45  ? 35.88000 61.41400 11.12500 1.000 89.96673  ? 42  THR   A OG1 1 
ATOM   295  C  CG2 . THR   A 1 45  ? 35.30100 63.44300 9.96000  1.000 92.54998  ? 42  THR   A CG2 1 
ATOM   296  N  N   . LYS   A 1 46  ? 31.89000 62.70100 9.78100  1.000 105.86543 ? 43  LYS   A N   1 
ATOM   297  C  CA  . LYS   A 1 46  ? 30.84800 63.46800 9.11000  1.000 100.57406 ? 43  LYS   A CA  1 
ATOM   298  C  C   . LYS   A 1 46  ? 29.49200 63.35600 9.79700  1.000 109.19015 ? 43  LYS   A C   1 
ATOM   299  O  O   . LYS   A 1 46  ? 28.49300 63.82800 9.24200  1.000 117.51526 ? 43  LYS   A O   1 
ATOM   300  C  CB  . LYS   A 1 46  ? 30.72500 63.02000 7.65100  1.000 95.05779  ? 43  LYS   A CB  1 
ATOM   301  C  CG  . LYS   A 1 46  ? 32.04200 63.01600 6.89000  1.000 103.45469 ? 43  LYS   A CG  1 
ATOM   302  C  CD  . LYS   A 1 46  ? 31.81700 62.91700 5.38900  1.000 107.11390 ? 43  LYS   A CD  1 
ATOM   303  C  CE  . LYS   A 1 46  ? 32.92600 63.61300 4.61500  1.000 119.29005 ? 43  LYS   A CE  1 
ATOM   304  N  NZ  . LYS   A 1 46  ? 33.95700 64.19700 5.51800  1.000 113.64046 ? 43  LYS   A NZ  1 
ATOM   305  N  N   . ILE   A 1 47  ? 29.43200 62.75000 10.98000 1.000 109.64190 ? 44  ILE   A N   1 
ATOM   306  C  CA  . ILE   A 1 47  ? 28.18600 62.55800 11.71300 1.000 109.20210 ? 44  ILE   A CA  1 
ATOM   307  C  C   . ILE   A 1 47  ? 28.10000 63.62200 12.79900 1.000 106.24209 ? 44  ILE   A C   1 
ATOM   308  O  O   . ILE   A 1 47  ? 29.07500 63.86200 13.52300 1.000 111.14312 ? 44  ILE   A O   1 
ATOM   309  C  CB  . ILE   A 1 47  ? 28.10200 61.13700 12.30300 1.000 108.36480 ? 44  ILE   A CB  1 
ATOM   310  C  CG1 . ILE   A 1 47  ? 27.27500 60.21900 11.39700 1.000 112.82853 ? 44  ILE   A CG1 1 
ATOM   311  C  CG2 . ILE   A 1 47  ? 27.50800 61.14600 13.70300 1.000 102.40099 ? 44  ILE   A CG2 1 
ATOM   312  C  CD1 . ILE   A 1 47  ? 27.71000 60.21000 9.94700  1.000 110.70602 ? 44  ILE   A CD1 1 
ATOM   313  N  N   . LYS   A 1 48  ? 26.95200 64.28900 12.88500 1.000 115.58891 ? 45  LYS   A N   1 
ATOM   314  C  CA  . LYS   A 1 48  ? 26.75300 65.30400 13.90300 1.000 117.45431 ? 45  LYS   A CA  1 
ATOM   315  C  C   . LYS   A 1 48  ? 26.61600 64.64600 15.27400 1.000 112.99191 ? 45  LYS   A C   1 
ATOM   316  O  O   . LYS   A 1 48  ? 26.25900 63.47100 15.37400 1.000 113.75448 ? 45  LYS   A O   1 
ATOM   317  C  CB  . LYS   A 1 48  ? 25.51400 66.13800 13.58300 1.000 108.73009 ? 45  LYS   A CB  1 
ATOM   318  N  N   . PRO   A 1 49  ? 26.91600 65.37500 16.34900 1.000 111.77123 ? 46  PRO   A N   1 
ATOM   319  C  CA  . PRO   A 1 49  ? 26.73500 64.79700 17.68900 1.000 111.23216 ? 46  PRO   A CA  1 
ATOM   320  C  C   . PRO   A 1 49  ? 25.26200 64.51900 17.95800 1.000 113.17423 ? 46  PRO   A C   1 
ATOM   321  O  O   . PRO   A 1 49  ? 24.39400 65.34300 17.66200 1.000 118.52037 ? 46  PRO   A O   1 
ATOM   322  C  CB  . PRO   A 1 49  ? 27.29400 65.87000 18.63500 1.000 104.40606 ? 46  PRO   A CB  1 
ATOM   323  C  CG  . PRO   A 1 49  ? 28.02000 66.84700 17.78600 1.000 113.23717 ? 46  PRO   A CG  1 
ATOM   324  C  CD  . PRO   A 1 49  ? 27.56600 66.69500 16.37300 1.000 110.76193 ? 46  PRO   A CD  1 
ATOM   325  N  N   . HIS   A 1 50  ? 24.98700 63.33700 18.50100 1.000 120.69253 ? 47  HIS   A N   1 
ATOM   326  C  CA  . HIS   A 1 50  ? 23.64300 62.90500 18.86000 1.000 121.90461 ? 47  HIS   A CA  1 
ATOM   327  C  C   . HIS   A 1 50  ? 23.50700 62.84200 20.38000 1.000 121.44847 ? 47  HIS   A C   1 
ATOM   328  O  O   . HIS   A 1 50  ? 24.45300 63.10000 21.13000 1.000 126.28402 ? 47  HIS   A O   1 
ATOM   329  C  CB  . HIS   A 1 50  ? 23.31400 61.55000 18.22400 1.000 115.40400 ? 47  HIS   A CB  1 
ATOM   330  C  CG  . HIS   A 1 50  ? 23.25500 61.56900 16.72500 1.000 122.27967 ? 47  HIS   A CG  1 
ATOM   331  N  ND1 . HIS   A 1 50  ? 23.96500 62.46400 15.95200 1.000 134.76692 ? 47  HIS   A ND1 1 
ATOM   332  C  CD2 . HIS   A 1 50  ? 22.56800 60.79000 15.85600 1.000 124.31133 ? 47  HIS   A CD2 1 
ATOM   333  C  CE1 . HIS   A 1 50  ? 23.71300 62.23900 14.67500 1.000 129.65515 ? 47  HIS   A CE1 1 
ATOM   334  N  NE2 . HIS   A 1 50  ? 22.87000 61.22700 14.58900 1.000 134.99056 ? 47  HIS   A NE2 1 
ATOM   335  N  N   . ASN   A 1 51  ? 22.30300 62.48600 20.83500 1.000 122.39232 ? 48  ASN   A N   1 
ATOM   336  C  CA  . ASN   A 1 51  ? 22.05300 62.39900 22.27000 1.000 123.91493 ? 48  ASN   A CA  1 
ATOM   337  C  C   . ASN   A 1 51  ? 22.60600 61.10800 22.86000 1.000 125.48816 ? 48  ASN   A C   1 
ATOM   338  O  O   . ASN   A 1 51  ? 23.11900 61.10900 23.98600 1.000 124.09543 ? 48  ASN   A O   1 
ATOM   339  C  CB  . ASN   A 1 51  ? 20.55500 62.51800 22.55000 1.000 122.26018 ? 48  ASN   A CB  1 
ATOM   340  C  CG  . ASN   A 1 51  ? 19.91000 63.65700 21.78600 1.000 123.93853 ? 48  ASN   A CG  1 
ATOM   341  O  OD1 . ASN   A 1 51  ? 19.20600 63.43800 20.80000 1.000 123.23739 ? 48  ASN   A OD1 1 
ATOM   342  N  ND2 . ASN   A 1 51  ? 20.15000 64.88400 22.23700 1.000 106.37415 ? 48  ASN   A ND2 1 
ATOM   343  N  N   . SER   A 1 52  ? 22.51300 59.99900 22.12100 1.000 129.42959 ? 49  SER   A N   1 
ATOM   344  C  CA  . SER   A 1 52  ? 23.10000 58.74500 22.57900 1.000 130.28481 ? 49  SER   A CA  1 
ATOM   345  C  C   . SER   A 1 52  ? 24.62100 58.80300 22.61900 1.000 135.07161 ? 49  SER   A C   1 
ATOM   346  O  O   . SER   A 1 52  ? 25.24400 57.97500 23.29200 1.000 132.21668 ? 49  SER   A O   1 
ATOM   347  C  CB  . SER   A 1 52  ? 22.64600 57.59100 21.68300 1.000 131.47607 ? 49  SER   A CB  1 
ATOM   348  O  OG  . SER   A 1 52  ? 23.64300 57.25700 20.73100 1.000 133.70625 ? 49  SER   A OG  1 
ATOM   349  N  N   . HIS   A 1 53  ? 25.22800 59.76100 21.91500 1.000 133.82746 ? 50  HIS   A N   1 
ATOM   350  C  CA  . HIS   A 1 53  ? 26.67700 59.90900 21.91600 1.000 127.50133 ? 50  HIS   A CA  1 
ATOM   351  C  C   . HIS   A 1 53  ? 27.20300 60.56000 23.18800 1.000 132.40599 ? 50  HIS   A C   1 
ATOM   352  O  O   . HIS   A 1 53  ? 28.40600 60.47300 23.45800 1.000 139.01747 ? 50  HIS   A O   1 
ATOM   353  C  CB  . HIS   A 1 53  ? 27.12000 60.73000 20.70300 1.000 112.23395 ? 50  HIS   A CB  1 
ATOM   354  C  CG  . HIS   A 1 53  ? 26.92600 60.03000 19.39400 1.000 119.14566 ? 50  HIS   A CG  1 
ATOM   355  N  ND1 . HIS   A 1 53  ? 27.24500 60.61100 18.18600 1.000 122.07799 ? 50  HIS   A ND1 1 
ATOM   356  C  CD2 . HIS   A 1 53  ? 26.44700 58.79700 19.10400 1.000 117.47405 ? 50  HIS   A CD2 1 
ATOM   357  C  CE1 . HIS   A 1 53  ? 26.97100 59.76600 17.20800 1.000 126.13534 ? 50  HIS   A CE1 1 
ATOM   358  N  NE2 . HIS   A 1 53  ? 26.48500 58.65800 17.73800 1.000 119.99537 ? 50  HIS   A NE2 1 
ATOM   359  N  N   . GLU   A 1 54  ? 26.33900 61.20800 23.96600 1.000 130.79177 ? 51  GLU   A N   1 
ATOM   360  C  CA  . GLU   A 1 54  ? 26.77800 61.87500 25.18400 1.000 131.76418 ? 51  GLU   A CA  1 
ATOM   361  C  C   . GLU   A 1 54  ? 27.26700 60.84900 26.19900 1.000 129.63286 ? 51  GLU   A C   1 
ATOM   362  O  O   . GLU   A 1 54  ? 26.60100 59.83900 26.44900 1.000 124.13671 ? 51  GLU   A O   1 
ATOM   363  C  CB  . GLU   A 1 54  ? 25.63900 62.70800 25.77200 1.000 134.67407 ? 51  GLU   A CB  1 
ATOM   364  C  CG  . GLU   A 1 54  ? 26.07900 63.72500 26.81600 1.000 129.69155 ? 51  GLU   A CG  1 
ATOM   365  C  CD  . GLU   A 1 54  ? 26.17100 63.13500 28.20900 1.000 138.49223 ? 51  GLU   A CD  1 
ATOM   366  O  OE1 . GLU   A 1 54  ? 25.44400 62.16000 28.49200 1.000 154.29489 ? 51  GLU   A OE1 1 
ATOM   367  O  OE2 . GLU   A 1 54  ? 26.97300 63.64600 29.01900 1.000 132.24643 ? 51  GLU   A OE2 1 
ATOM   368  N  N   . GLY   A 1 55  ? 28.43600 61.10900 26.78300 1.000 126.68326 ? 52  GLY   A N   1 
ATOM   369  C  CA  . GLY   A 1 55  ? 29.04400 60.21200 27.73700 1.000 124.74210 ? 52  GLY   A CA  1 
ATOM   370  C  C   . GLY   A 1 55  ? 29.92400 59.13700 27.13500 1.000 114.34214 ? 52  GLY   A C   1 
ATOM   371  O  O   . GLY   A 1 55  ? 30.81100 58.62300 27.82600 1.000 101.17908 ? 52  GLY   A O   1 
ATOM   372  N  N   . LYS   A 1 56  ? 29.70800 58.78300 25.87100 1.000 125.53898 ? 53  LYS   A N   1 
ATOM   373  C  CA  . LYS   A 1 56  ? 30.51000 57.75400 25.22900 1.000 121.30781 ? 53  LYS   A CA  1 
ATOM   374  C  C   . LYS   A 1 56  ? 31.93600 58.24800 24.99700 1.000 111.44839 ? 53  LYS   A C   1 
ATOM   375  O  O   . LYS   A 1 56  ? 32.20900 59.45000 24.93200 1.000 112.48676 ? 53  LYS   A O   1 
ATOM   376  C  CB  . LYS   A 1 56  ? 29.87900 57.33200 23.90100 1.000 116.88677 ? 53  LYS   A CB  1 
ATOM   377  C  CG  . LYS   A 1 56  ? 28.51800 56.66900 24.04200 1.000 126.76502 ? 53  LYS   A CG  1 
ATOM   378  C  CD  . LYS   A 1 56  ? 28.49900 55.30000 23.37900 1.000 126.04439 ? 53  LYS   A CD  1 
ATOM   379  C  CE  . LYS   A 1 56  ? 27.10000 54.93200 22.91000 1.000 121.42486 ? 53  LYS   A CE  1 
ATOM   380  N  NZ  . LYS   A 1 56  ? 26.08100 55.15300 23.97300 1.000 121.98762 ? 53  LYS   A NZ  1 
ATOM   381  N  N   . THR   A 1 57  ? 32.85300 57.29300 24.87200 1.000 100.52493 ? 54  THR   A N   1 
ATOM   382  C  CA  . THR   A 1 57  ? 34.26200 57.57700 24.64000 1.000 89.76697  ? 54  THR   A CA  1 
ATOM   383  C  C   . THR   A 1 57  ? 34.56000 57.46500 23.15000 1.000 93.69049  ? 54  THR   A C   1 
ATOM   384  O  O   . THR   A 1 57  ? 34.20700 56.46500 22.51400 1.000 86.91006  ? 54  THR   A O   1 
ATOM   385  C  CB  . THR   A 1 57  ? 35.14800 56.62000 25.44100 1.000 100.34105 ? 54  THR   A CB  1 
ATOM   386  O  OG1 . THR   A 1 57  ? 35.21300 57.05600 26.80500 1.000 99.61547  ? 54  THR   A OG1 1 
ATOM   387  C  CG2 . THR   A 1 57  ? 36.55500 56.57400 24.86400 1.000 97.96933  ? 54  THR   A CG2 1 
ATOM   388  N  N   . PHE   A 1 58  ? 35.20200 58.49100 22.59800 1.000 93.16906  ? 55  PHE   A N   1 
ATOM   389  C  CA  . PHE   A 1 58  ? 35.49900 58.56700 21.17600 1.000 84.97358  ? 55  PHE   A CA  1 
ATOM   390  C  C   . PHE   A 1 58  ? 36.98900 58.37700 20.93500 1.000 74.42637  ? 55  PHE   A C   1 
ATOM   391  O  O   . PHE   A 1 58  ? 37.82100 58.91300 21.67400 1.000 76.13639  ? 55  PHE   A O   1 
ATOM   392  C  CB  . PHE   A 1 58  ? 35.06400 59.91600 20.59800 1.000 94.45829  ? 55  PHE   A CB  1 
ATOM   393  C  CG  . PHE   A 1 58  ? 33.58300 60.04900 20.40500 1.000 96.66317  ? 55  PHE   A CG  1 
ATOM   394  C  CD1 . PHE   A 1 58  ? 32.77300 60.47400 21.44500 1.000 102.05921 ? 55  PHE   A CD1 1 
ATOM   395  C  CD2 . PHE   A 1 58  ? 33.00200 59.77100 19.18000 1.000 95.96238  ? 55  PHE   A CD2 1 
ATOM   396  C  CE1 . PHE   A 1 58  ? 31.41100 60.60700 21.27000 1.000 101.69472 ? 55  PHE   A CE1 1 
ATOM   397  C  CE2 . PHE   A 1 58  ? 31.64200 59.90800 18.99700 1.000 102.59960 ? 55  PHE   A CE2 1 
ATOM   398  C  CZ  . PHE   A 1 58  ? 30.84500 60.32200 20.04400 1.000 98.07614  ? 55  PHE   A CZ  1 
ATOM   399  N  N   . TYR   A 1 59  ? 37.32000 57.61900 19.89400 1.000 62.57443  ? 56  TYR   A N   1 
ATOM   400  C  CA  . TYR   A 1 59  ? 38.68900 57.52200 19.40800 1.000 69.24979  ? 56  TYR   A CA  1 
ATOM   401  C  C   . TYR   A 1 59  ? 38.94300 58.64900 18.41300 1.000 79.41276  ? 56  TYR   A C   1 
ATOM   402  O  O   . TYR   A 1 59  ? 38.16300 58.84300 17.47500 1.000 67.65560  ? 56  TYR   A O   1 
ATOM   403  C  CB  . TYR   A 1 59  ? 38.93700 56.16900 18.74200 1.000 79.81329  ? 56  TYR   A CB  1 
ATOM   404  C  CG  . TYR   A 1 59  ? 39.33000 55.05500 19.68500 1.000 77.98449  ? 56  TYR   A CG  1 
ATOM   405  C  CD1 . TYR   A 1 59  ? 38.61700 54.81400 20.85200 1.000 96.56405  ? 56  TYR   A CD1 1 
ATOM   406  C  CD2 . TYR   A 1 59  ? 40.41300 54.23500 19.39900 1.000 76.34857  ? 56  TYR   A CD2 1 
ATOM   407  C  CE1 . TYR   A 1 59  ? 38.97700 53.79000 21.71000 1.000 88.48815  ? 56  TYR   A CE1 1 
ATOM   408  C  CE2 . TYR   A 1 59  ? 40.77800 53.21100 20.24700 1.000 75.65973  ? 56  TYR   A CE2 1 
ATOM   409  C  CZ  . TYR   A 1 59  ? 40.05900 52.99100 21.40100 1.000 87.55380  ? 56  TYR   A CZ  1 
ATOM   410  O  OH  . TYR   A 1 59  ? 40.42600 51.96900 22.24500 1.000 90.00915  ? 56  TYR   A OH  1 
ATOM   411  N  N   . VAL   A 1 60  ? 40.03200 59.38900 18.61600 1.000 68.95094  ? 57  VAL   A N   1 
ATOM   412  C  CA  . VAL   A 1 60  ? 40.37900 60.50400 17.74500 1.000 67.40199  ? 57  VAL   A CA  1 
ATOM   413  C  C   . VAL   A 1 60  ? 41.80000 60.32100 17.23400 1.000 62.02690  ? 57  VAL   A C   1 
ATOM   414  O  O   . VAL   A 1 60  ? 42.66100 59.76100 17.91800 1.000 69.30187  ? 57  VAL   A O   1 
ATOM   415  C  CB  . VAL   A 1 60  ? 40.24300 61.86700 18.45900 1.000 69.35427  ? 57  VAL   A CB  1 
ATOM   416  C  CG1 . VAL   A 1 60  ? 38.77800 62.22800 18.64600 1.000 61.39387  ? 57  VAL   A CG1 1 
ATOM   417  C  CG2 . VAL   A 1 60  ? 40.97300 61.84400 19.79200 1.000 66.95129  ? 57  VAL   A CG2 1 
ATOM   418  N  N   . LEU   A 1 61  ? 42.03800 60.79500 16.01700 1.000 65.04310  ? 58  LEU   A N   1 
ATOM   419  C  CA  . LEU   A 1 61  ? 43.39600 60.83900 15.50100 1.000 65.00252  ? 58  LEU   A CA  1 
ATOM   420  C  C   . LEU   A 1 61  ? 44.19600 61.88100 16.28000 1.000 67.40287  ? 58  LEU   A C   1 
ATOM   421  O  O   . LEU   A 1 61  ? 43.67700 62.96100 16.58100 1.000 80.15780  ? 58  LEU   A O   1 
ATOM   422  C  CB  . LEU   A 1 61  ? 43.39200 61.17200 14.00800 1.000 66.80327  ? 58  LEU   A CB  1 
ATOM   423  C  CG  . LEU   A 1 61  ? 44.68600 61.66900 13.35800 1.000 85.75456  ? 58  LEU   A CG  1 
ATOM   424  C  CD1 . LEU   A 1 61  ? 45.53800 60.50100 12.87300 1.000 68.58865  ? 58  LEU   A CD1 1 
ATOM   425  C  CD2 . LEU   A 1 61  ? 44.37500 62.61500 12.21100 1.000 76.95993  ? 58  LEU   A CD2 1 
ATOM   426  N  N   . PRO   A 1 62  ? 45.44100 61.58000 16.64700 1.000 67.33189  ? 59  PRO   A N   1 
ATOM   427  C  CA  . PRO   A 1 62  ? 46.22800 62.52600 17.45700 1.000 75.46069  ? 59  PRO   A CA  1 
ATOM   428  C  C   . PRO   A 1 62  ? 46.36400 63.87900 16.77400 1.000 69.02529  ? 59  PRO   A C   1 
ATOM   429  O  O   . PRO   A 1 62  ? 46.85600 63.98100 15.64800 1.000 69.06517  ? 59  PRO   A O   1 
ATOM   430  C  CB  . PRO   A 1 62  ? 47.58200 61.82100 17.59900 1.000 61.61946  ? 59  PRO   A CB  1 
ATOM   431  C  CG  . PRO   A 1 62  ? 47.26600 60.36900 17.44800 1.000 59.63306  ? 59  PRO   A CG  1 
ATOM   432  C  CD  . PRO   A 1 62  ? 46.14000 60.29800 16.45400 1.000 59.32953  ? 59  PRO   A CD  1 
ATOM   433  N  N   . ASN   A 1 63  ? 45.91400 64.92500 17.47000 1.000 70.15355  ? 60  ASN   A N   1 
ATOM   434  C  CA  . ASN   A 1 63  ? 45.97100 66.28900 16.96300 1.000 78.71095  ? 60  ASN   A CA  1 
ATOM   435  C  C   . ASN   A 1 63  ? 46.87000 67.20400 17.78400 1.000 77.14454  ? 60  ASN   A C   1 
ATOM   436  O  O   . ASN   A 1 63  ? 47.02900 68.37600 17.42000 1.000 81.46875  ? 60  ASN   A O   1 
ATOM   437  C  CB  . ASN   A 1 63  ? 44.56000 66.89300 16.89400 1.000 79.46294  ? 60  ASN   A CB  1 
ATOM   438  C  CG  . ASN   A 1 63  ? 43.77100 66.68000 18.17300 1.000 86.66060  ? 60  ASN   A CG  1 
ATOM   439  O  OD1 . ASN   A 1 63  ? 44.16700 67.14000 19.24400 1.000 96.47112  ? 60  ASN   A OD1 1 
ATOM   440  N  ND2 . ASN   A 1 63  ? 42.64400 65.98400 18.06500 1.000 89.77717  ? 60  ASN   A ND2 1 
ATOM   441  N  N   . ASP   A 1 64  ? 47.45200 66.71600 18.87900 1.000 67.89261  ? 61  ASP   A N   1 
ATOM   442  C  CA  . ASP   A 1 64  ? 48.40400 67.48400 19.67100 1.000 61.84640  ? 61  ASP   A CA  1 
ATOM   443  C  C   . ASP   A 1 64  ? 49.51700 66.55100 20.13300 1.000 66.18676  ? 61  ASP   A C   1 
ATOM   444  O  O   . ASP   A 1 64  ? 49.46200 65.33400 19.93000 1.000 61.76726  ? 61  ASP   A O   1 
ATOM   445  C  CB  . ASP   A 1 64  ? 47.71700 68.18800 20.85100 1.000 64.71902  ? 61  ASP   A CB  1 
ATOM   446  C  CG  . ASP   A 1 64  ? 47.03100 67.22100 21.81000 1.000 67.01802  ? 61  ASP   A CG  1 
ATOM   447  O  OD1 . ASP   A 1 64  ? 47.59500 66.15200 22.12700 1.000 71.21345  ? 61  ASP   A OD1 1 
ATOM   448  O  OD2 . ASP   A 1 64  ? 45.90900 67.54000 22.25300 1.000 80.58002  ? 61  ASP   A OD2 1 
ATOM   449  N  N   . ASP   A 1 65  ? 50.53000 67.13100 20.78000 1.000 58.36204  ? 62  ASP   A N   1 
ATOM   450  C  CA  . ASP   A 1 65  ? 51.68400 66.34100 21.19300 1.000 55.84528  ? 62  ASP   A CA  1 
ATOM   451  C  C   . ASP   A 1 65  ? 51.34100 65.35900 22.30500 1.000 59.55334  ? 62  ASP   A C   1 
ATOM   452  O  O   . ASP   A 1 65  ? 51.91500 64.26600 22.35700 1.000 60.31126  ? 62  ASP   A O   1 
ATOM   453  C  CB  . ASP   A 1 65  ? 52.82000 67.26100 21.63000 1.000 53.38951  ? 62  ASP   A CB  1 
ATOM   454  C  CG  . ASP   A 1 65  ? 54.17300 66.60400 21.49800 1.000 53.32728  ? 62  ASP   A CG  1 
ATOM   455  O  OD1 . ASP   A 1 65  ? 54.57300 66.30000 20.35300 1.000 48.54369  ? 62  ASP   A OD1 1 
ATOM   456  O  OD2 . ASP   A 1 65  ? 54.83600 66.39200 22.53500 1.000 47.63605  ? 62  ASP   A OD2 1 
ATOM   457  N  N   . THR   A 1 66  ? 50.42300 65.72400 23.20300 1.000 60.64147  ? 63  THR   A N   1 
ATOM   458  C  CA  . THR   A 1 66  ? 50.02600 64.79800 24.26100 1.000 61.78850  ? 63  THR   A CA  1 
ATOM   459  C  C   . THR   A 1 66  ? 49.36800 63.55300 23.67800 1.000 62.68551  ? 63  THR   A C   1 
ATOM   460  O  O   . THR   A 1 66  ? 49.67800 62.42600 24.08300 1.000 59.58240  ? 63  THR   A O   1 
ATOM   461  C  CB  . THR   A 1 66  ? 49.08600 65.49300 25.24900 1.000 63.08403  ? 63  THR   A CB  1 
ATOM   462  O  OG1 . THR   A 1 66  ? 49.82000 66.45600 26.01400 1.000 64.73679  ? 63  THR   A OG1 1 
ATOM   463  C  CG2 . THR   A 1 66  ? 48.46600 64.48000 26.20100 1.000 59.28267  ? 63  THR   A CG2 1 
ATOM   464  N  N   . LEU   A 1 67  ? 48.46500 63.73800 22.71300 1.000 63.16328  ? 64  LEU   A N   1 
ATOM   465  C  CA  . LEU   A 1 67  ? 47.83800 62.59700 22.05500 1.000 57.62532  ? 64  LEU   A CA  1 
ATOM   466  C  C   . LEU   A 1 67  ? 48.84600 61.82500 21.21300 1.000 62.39583  ? 64  LEU   A C   1 
ATOM   467  O  O   . LEU   A 1 67  ? 48.76700 60.59500 21.11600 1.000 60.73978  ? 64  LEU   A O   1 
ATOM   468  C  CB  . LEU   A 1 67  ? 46.66800 63.07100 21.19300 1.000 67.23638  ? 64  LEU   A CB  1 
ATOM   469  C  CG  . LEU   A 1 67  ? 45.43700 63.60100 21.93300 1.000 72.21318  ? 64  LEU   A CG  1 
ATOM   470  C  CD1 . LEU   A 1 67  ? 44.22200 63.60000 21.01900 1.000 75.87503  ? 64  LEU   A CD1 1 
ATOM   471  C  CD2 . LEU   A 1 67  ? 45.16500 62.79000 23.19100 1.000 63.80561  ? 64  LEU   A CD2 1 
ATOM   472  N  N   . ARG   A 1 68  ? 49.79800 62.52900 20.59200 1.000 60.34200  ? 65  ARG   A N   1 
ATOM   473  C  CA  . ARG   A 1 68  ? 50.81300 61.85500 19.78900 1.000 54.09862  ? 65  ARG   A CA  1 
ATOM   474  C  C   . ARG   A 1 68  ? 51.68000 60.95000 20.65700 1.000 56.78364  ? 65  ARG   A C   1 
ATOM   475  O  O   . ARG   A 1 68  ? 51.93100 59.78900 20.31100 1.000 50.27593  ? 65  ARG   A O   1 
ATOM   476  C  CB  . ARG   A 1 68  ? 51.67600 62.88400 19.05500 1.000 54.12199  ? 65  ARG   A CB  1 
ATOM   477  C  CG  . ARG   A 1 68  ? 51.07100 63.41600 17.76100 1.000 60.32352  ? 65  ARG   A CG  1 
ATOM   478  C  CD  . ARG   A 1 68  ? 52.12800 64.08700 16.89000 1.000 55.88394  ? 65  ARG   A CD  1 
ATOM   479  N  NE  . ARG   A 1 68  ? 52.70500 65.25900 17.53900 1.000 61.83704  ? 65  ARG   A NE  1 
ATOM   480  C  CZ  . ARG   A 1 68  ? 52.17100 66.47300 17.51000 1.000 64.23016  ? 65  ARG   A CZ  1 
ATOM   481  N  NH1 . ARG   A 1 68  ? 51.04700 66.72000 16.85700 1.000 50.54168  ? 65  ARG   A NH1 1 
ATOM   482  N  NH2 . ARG   A 1 68  ? 52.77800 67.46500 18.15600 1.000 51.86573  ? 65  ARG   A NH2 1 
ATOM   483  N  N   . VAL   A 1 69  ? 52.14100 61.46800 21.79800 1.000 52.60407  ? 66  VAL   A N   1 
ATOM   484  C  CA  . VAL   A 1 69  ? 52.97800 60.67200 22.69100 1.000 55.40595  ? 66  VAL   A CA  1 
ATOM   485  C  C   . VAL   A 1 69  ? 52.19100 59.48900 23.23900 1.000 57.79977  ? 66  VAL   A C   1 
ATOM   486  O  O   . VAL   A 1 69  ? 52.66900 58.35000 23.23700 1.000 47.61133  ? 66  VAL   A O   1 
ATOM   487  C  CB  . VAL   A 1 69  ? 53.54500 61.54700 23.82200 1.000 51.70023  ? 66  VAL   A CB  1 
ATOM   488  C  CG1 . VAL   A 1 69  ? 54.16800 60.67300 24.90300 1.000 42.72733  ? 66  VAL   A CG1 1 
ATOM   489  C  CG2 . VAL   A 1 69  ? 54.56900 62.52400 23.26600 1.000 40.59428  ? 66  VAL   A CG2 1 
ATOM   490  N  N   . GLU   A 1 70  ? 50.96500 59.73900 23.70700 1.000 56.53473  ? 67  GLU   A N   1 
ATOM   491  C  CA  . GLU   A 1 70  ? 50.12900 58.65200 24.20900 1.000 59.00959  ? 67  GLU   A CA  1 
ATOM   492  C  C   . GLU   A 1 70  ? 49.90900 57.58700 23.14000 1.000 63.09508  ? 67  GLU   A C   1 
ATOM   493  O  O   . GLU   A 1 70  ? 49.89400 56.38800 23.44200 1.000 65.11040  ? 67  GLU   A O   1 
ATOM   494  C  CB  . GLU   A 1 70  ? 48.79000 59.20400 24.70000 1.000 55.96000  ? 67  GLU   A CB  1 
ATOM   495  C  CG  . GLU   A 1 70  ? 48.83900 59.83200 26.08400 1.000 66.40854  ? 67  GLU   A CG  1 
ATOM   496  C  CD  . GLU   A 1 70  ? 47.60400 60.66100 26.38800 1.000 69.64526  ? 67  GLU   A CD  1 
ATOM   497  O  OE1 . GLU   A 1 70  ? 46.66200 60.64800 25.56600 1.000 64.26237  ? 67  GLU   A OE1 1 
ATOM   498  O  OE2 . GLU   A 1 70  ? 47.57400 61.32400 27.44600 1.000 70.91851  ? 67  GLU   A OE2 1 
ATOM   499  N  N   . ALA   A 1 71  ? 49.75200 58.00700 21.88200 1.000 59.41702  ? 68  ALA   A N   1 
ATOM   500  C  CA  . ALA   A 1 71  ? 49.52600 57.05300 20.80000 1.000 54.05773  ? 68  ALA   A CA  1 
ATOM   501  C  C   . ALA   A 1 71  ? 50.72700 56.13800 20.60400 1.000 52.48154  ? 68  ALA   A C   1 
ATOM   502  O  O   . ALA   A 1 71  ? 50.56400 54.93500 20.36700 1.000 48.98835  ? 68  ALA   A O   1 
ATOM   503  C  CB  . ALA   A 1 71  ? 49.20000 57.79400 19.50400 1.000 48.11936  ? 68  ALA   A CB  1 
ATOM   504  N  N   . PHE   A 1 72  ? 51.94200 56.68100 20.70000 1.000 47.25408  ? 69  PHE   A N   1 
ATOM   505  C  CA  . PHE   A 1 72  ? 53.11800 55.83200 20.54000 1.000 56.20233  ? 69  PHE   A CA  1 
ATOM   506  C  C   . PHE   A 1 72  ? 53.28600 54.87800 21.71700 1.000 53.22465  ? 69  PHE   A C   1 
ATOM   507  O  O   . PHE   A 1 72  ? 53.64200 53.71100 21.52200 1.000 53.70857  ? 69  PHE   A O   1 
ATOM   508  C  CB  . PHE   A 1 72  ? 54.38300 56.67000 20.36600 1.000 42.96589  ? 69  PHE   A CB  1 
ATOM   509  C  CG  . PHE   A 1 72  ? 55.63000 55.83800 20.26000 1.000 52.87914  ? 69  PHE   A CG  1 
ATOM   510  C  CD1 . PHE   A 1 72  ? 56.02600 55.32300 19.03900 1.000 45.54862  ? 69  PHE   A CD1 1 
ATOM   511  C  CD2 . PHE   A 1 72  ? 56.38800 55.54200 21.38400 1.000 49.94891  ? 69  PHE   A CD2 1 
ATOM   512  C  CE1 . PHE   A 1 72  ? 57.16200 54.54600 18.93400 1.000 49.81661  ? 69  PHE   A CE1 1 
ATOM   513  C  CE2 . PHE   A 1 72  ? 57.52400 54.76600 21.28500 1.000 51.89709  ? 69  PHE   A CE2 1 
ATOM   514  C  CZ  . PHE   A 1 72  ? 57.91100 54.26400 20.05800 1.000 47.37805  ? 69  PHE   A CZ  1 
ATOM   515  N  N   . GLU   A 1 73  ? 53.06300 55.35400 22.94600 1.000 47.58645  ? 70  GLU   A N   1 
ATOM   516  C  CA  . GLU   A 1 73  ? 53.27800 54.48800 24.10300 1.000 60.99086  ? 70  GLU   A CA  1 
ATOM   517  C  C   . GLU   A 1 73  ? 52.36900 53.26700 24.06700 1.000 53.86670  ? 70  GLU   A C   1 
ATOM   518  O  O   . GLU   A 1 73  ? 52.76000 52.19200 24.53600 1.000 61.29937  ? 70  GLU   A O   1 
ATOM   519  C  CB  . GLU   A 1 73  ? 53.07100 55.25500 25.41300 1.000 56.76738  ? 70  GLU   A CB  1 
ATOM   520  C  CG  . GLU   A 1 73  ? 53.63800 56.65900 25.43200 1.000 67.03582  ? 70  GLU   A CG  1 
ATOM   521  C  CD  . GLU   A 1 73  ? 54.97200 56.76700 26.14400 1.000 91.33941  ? 70  GLU   A CD  1 
ATOM   522  O  OE1 . GLU   A 1 73  ? 55.88000 55.96200 25.84400 1.000 76.29365  ? 70  GLU   A OE1 1 
ATOM   523  O  OE2 . GLU   A 1 73  ? 55.11500 57.67000 26.99800 1.000 87.95938  ? 70  GLU   A OE2 1 
ATOM   524  N  N   . TYR   A 1 74  ? 51.16500 53.40400 23.51000 1.000 46.68978  ? 71  TYR   A N   1 
ATOM   525  C  CA  . TYR   A 1 74  ? 50.23000 52.28600 23.46400 1.000 60.67190  ? 71  TYR   A CA  1 
ATOM   526  C  C   . TYR   A 1 74  ? 50.41900 51.40600 22.23200 1.000 58.35343  ? 71  TYR   A C   1 
ATOM   527  O  O   . TYR   A 1 74  ? 50.34300 50.17800 22.33700 1.000 54.19522  ? 71  TYR   A O   1 
ATOM   528  C  CB  . TYR   A 1 74  ? 48.78800 52.79600 23.51100 1.000 55.04534  ? 71  TYR   A CB  1 
ATOM   529  C  CG  . TYR   A 1 74  ? 47.80100 51.75300 23.98600 1.000 69.18334  ? 71  TYR   A CG  1 
ATOM   530  C  CD1 . TYR   A 1 74  ? 48.04200 51.01900 25.14100 1.000 59.89864  ? 71  TYR   A CD1 1 
ATOM   531  C  CD2 . TYR   A 1 74  ? 46.63400 51.49300 23.27500 1.000 63.42368  ? 71  TYR   A CD2 1 
ATOM   532  C  CE1 . TYR   A 1 74  ? 47.14800 50.06000 25.58000 1.000 53.57656  ? 71  TYR   A CE1 1 
ATOM   533  C  CE2 . TYR   A 1 74  ? 45.73000 50.53700 23.70800 1.000 61.49156  ? 71  TYR   A CE2 1 
ATOM   534  C  CZ  . TYR   A 1 74  ? 45.99500 49.82300 24.86200 1.000 71.41291  ? 71  TYR   A CZ  1 
ATOM   535  O  OH  . TYR   A 1 74  ? 45.10600 48.86800 25.30100 1.000 78.11692  ? 71  TYR   A OH  1 
ATOM   536  N  N   . TYR   A 1 75  ? 50.66400 52.00600 21.06500 1.000 48.34968  ? 72  TYR   A N   1 
ATOM   537  C  CA  . TYR   A 1 75  ? 50.72500 51.25600 19.81600 1.000 46.71924  ? 72  TYR   A CA  1 
ATOM   538  C  C   . TYR   A 1 75  ? 52.13600 51.06200 19.28200 1.000 50.23732  ? 72  TYR   A C   1 
ATOM   539  O  O   . TYR   A 1 75  ? 52.33900 50.18500 18.43500 1.000 50.78527  ? 72  TYR   A O   1 
ATOM   540  C  CB  . TYR   A 1 75  ? 49.88600 51.95100 18.73600 1.000 44.23946  ? 72  TYR   A CB  1 
ATOM   541  C  CG  . TYR   A 1 75  ? 48.42600 52.10800 19.08900 1.000 48.72904  ? 72  TYR   A CG  1 
ATOM   542  C  CD1 . TYR   A 1 75  ? 47.55300 51.03200 18.99900 1.000 46.09104  ? 72  TYR   A CD1 1 
ATOM   543  C  CD2 . TYR   A 1 75  ? 47.91700 53.33400 19.49900 1.000 55.38507  ? 72  TYR   A CD2 1 
ATOM   544  C  CE1 . TYR   A 1 75  ? 46.21400 51.16800 19.31600 1.000 50.51716  ? 72  TYR   A CE1 1 
ATOM   545  C  CE2 . TYR   A 1 75  ? 46.57800 53.48000 19.81800 1.000 53.38053  ? 72  TYR   A CE2 1 
ATOM   546  C  CZ  . TYR   A 1 75  ? 45.73200 52.39300 19.72400 1.000 59.49028  ? 72  TYR   A CZ  1 
ATOM   547  O  OH  . TYR   A 1 75  ? 44.40000 52.53100 20.04100 1.000 66.93234  ? 72  TYR   A OH  1 
ATOM   548  N  N   . HIS   A 1 76  ? 53.09900 51.86000 19.74400 1.000 49.58806  ? 73  HIS   A N   1 
ATOM   549  C  CA  . HIS   A 1 76  ? 54.48300 51.80300 19.26400 1.000 58.31887  ? 73  HIS   A CA  1 
ATOM   550  C  C   . HIS   A 1 76  ? 54.57100 52.09200 17.76500 1.000 51.39863  ? 73  HIS   A C   1 
ATOM   551  O  O   . HIS   A 1 76  ? 55.38100 51.50600 17.04600 1.000 57.99373  ? 73  HIS   A O   1 
ATOM   552  C  CB  . HIS   A 1 76  ? 55.13900 50.46400 19.61600 1.000 48.24042  ? 73  HIS   A CB  1 
ATOM   553  C  CG  . HIS   A 1 76  ? 55.46400 50.32500 21.07200 1.000 57.39854  ? 73  HIS   A CG  1 
ATOM   554  N  ND1 . HIS   A 1 76  ? 56.57500 49.65100 21.52900 1.000 45.18493  ? 73  HIS   A ND1 1 
ATOM   555  C  CD2 . HIS   A 1 76  ? 54.82600 50.79000 22.17300 1.000 47.14572  ? 73  HIS   A CD2 1 
ATOM   556  C  CE1 . HIS   A 1 76  ? 56.60500 49.70100 22.84900 1.000 59.74298  ? 73  HIS   A CE1 1 
ATOM   557  N  NE2 . HIS   A 1 76  ? 55.55400 50.38500 23.26500 1.000 54.75584  ? 73  HIS   A NE2 1 
ATOM   558  N  N   . THR   A 1 77  ? 53.73600 53.01500 17.29300 1.000 51.13437  ? 74  THR   A N   1 
ATOM   559  C  CA  . THR   A 1 77  ? 53.80400 53.47000 15.91400 1.000 61.18378  ? 74  THR   A CA  1 
ATOM   560  C  C   . THR   A 1 77  ? 53.40800 54.93900 15.85000 1.000 64.40147  ? 74  THR   A C   1 
ATOM   561  O  O   . THR   A 1 77  ? 52.59800 55.41700 16.65100 1.000 53.85897  ? 74  THR   A O   1 
ATOM   562  C  CB  . THR   A 1 77  ? 52.90400 52.63700 14.98800 1.000 67.01413  ? 74  THR   A CB  1 
ATOM   563  O  OG1 . THR   A 1 77  ? 53.08000 53.06600 13.63000 1.000 61.83019  ? 74  THR   A OG1 1 
ATOM   564  C  CG2 . THR   A 1 77  ? 51.43600 52.78500 15.37600 1.000 50.57678  ? 74  THR   A CG2 1 
ATOM   565  N  N   . THR   A 1 78  ? 54.00100 55.65700 14.89600 1.000 59.52723  ? 75  THR   A N   1 
ATOM   566  C  CA  . THR   A 1 78  ? 53.63100 57.03800 14.61700 1.000 61.23687  ? 75  THR   A CA  1 
ATOM   567  C  C   . THR   A 1 78  ? 52.91700 57.17900 13.28000 1.000 68.92108  ? 75  THR   A C   1 
ATOM   568  O  O   . THR   A 1 78  ? 52.69000 58.30400 12.82300 1.000 74.36343  ? 75  THR   A O   1 
ATOM   569  C  CB  . THR   A 1 78  ? 54.86400 57.94400 14.65000 1.000 57.23105  ? 75  THR   A CB  1 
ATOM   570  O  OG1 . THR   A 1 78  ? 55.84000 57.46500 13.71700 1.000 61.56169  ? 75  THR   A OG1 1 
ATOM   571  C  CG2 . THR   A 1 78  ? 55.46900 57.96300 16.04500 1.000 57.43602  ? 75  THR   A CG2 1 
ATOM   572  N  N   . ASP   A 1 79  ? 52.56600 56.06500 12.64700 1.000 61.94772  ? 76  ASP   A N   1 
ATOM   573  C  CA  . ASP   A 1 79  ? 51.85500 56.07100 11.37700 1.000 51.55748  ? 76  ASP   A CA  1 
ATOM   574  C  C   . ASP   A 1 79  ? 50.50300 56.75800 11.53200 1.000 56.00888  ? 76  ASP   A C   1 
ATOM   575  O  O   . ASP   A 1 79  ? 49.64300 56.25900 12.27500 1.000 55.68512  ? 76  ASP   A O   1 
ATOM   576  C  CB  . ASP   A 1 79  ? 51.67700 54.63400 10.88600 1.000 62.71533  ? 76  ASP   A CB  1 
ATOM   577  C  CG  . ASP   A 1 79  ? 51.13400 54.54900 9.46800  1.000 63.18082  ? 76  ASP   A CG  1 
ATOM   578  O  OD1 . ASP   A 1 79  ? 50.73800 55.58500 8.89200  1.000 65.78737  ? 76  ASP   A OD1 1 
ATOM   579  O  OD2 . ASP   A 1 79  ? 51.10900 53.42600 8.92400  1.000 68.97247  ? 76  ASP   A OD2 1 
ATOM   580  N  N   . PRO   A 1 80  ? 50.26500 57.88600 10.85400 1.000 65.33043  ? 77  PRO   A N   1 
ATOM   581  C  CA  . PRO   A 1 80  ? 48.96200 58.56000 10.97200 1.000 61.67163  ? 77  PRO   A CA  1 
ATOM   582  C  C   . PRO   A 1 80  ? 47.80900 57.77200 10.37500 1.000 58.97408  ? 77  PRO   A C   1 
ATOM   583  O  O   . PRO   A 1 80  ? 46.65000 58.09200 10.67000 1.000 68.99632  ? 77  PRO   A O   1 
ATOM   584  C  CB  . PRO   A 1 80  ? 49.17100 59.88300 10.21900 1.000 61.40099  ? 77  PRO   A CB  1 
ATOM   585  C  CG  . PRO   A 1 80  ? 50.64400 59.96500 9.91000  1.000 59.64998  ? 77  PRO   A CG  1 
ATOM   586  C  CD  . PRO   A 1 80  ? 51.17400 58.57500 9.92400  1.000 58.44574  ? 77  PRO   A CD  1 
ATOM   587  N  N   . SER   A 1 81  ? 48.08100 56.76300 9.54900  1.000 54.86740  ? 78  SER   A N   1 
ATOM   588  C  CA  . SER   A 1 81  ? 47.03500 55.92900 8.97400  1.000 58.11523  ? 78  SER   A CA  1 
ATOM   589  C  C   . SER   A 1 81  ? 46.70300 54.71400 9.83100  1.000 65.00388  ? 78  SER   A C   1 
ATOM   590  O  O   . SER   A 1 81  ? 45.76600 53.98100 9.49600  1.000 64.83739  ? 78  SER   A O   1 
ATOM   591  C  CB  . SER   A 1 81  ? 47.43800 55.46800 7.56900  1.000 57.53113  ? 78  SER   A CB  1 
ATOM   592  O  OG  . SER   A 1 81  ? 48.32300 54.36000 7.61800  1.000 59.42314  ? 78  SER   A OG  1 
ATOM   593  N  N   . PHE   A 1 82  ? 47.43800 54.48500 10.92500 1.000 57.08926  ? 79  PHE   A N   1 
ATOM   594  C  CA  . PHE   A 1 82  ? 47.23100 53.27300 11.71500 1.000 63.79620  ? 79  PHE   A CA  1 
ATOM   595  C  C   . PHE   A 1 82  ? 45.84700 53.25500 12.35100 1.000 54.97038  ? 79  PHE   A C   1 
ATOM   596  O  O   . PHE   A 1 82  ? 45.12800 52.25200 12.26300 1.000 54.84154  ? 79  PHE   A O   1 
ATOM   597  C  CB  . PHE   A 1 82  ? 48.31400 53.14400 12.78900 1.000 58.65737  ? 79  PHE   A CB  1 
ATOM   598  C  CG  . PHE   A 1 82  ? 48.26900 51.83600 13.53900 1.000 60.19436  ? 79  PHE   A CG  1 
ATOM   599  C  CD1 . PHE   A 1 82  ? 48.97500 50.73400 13.07900 1.000 57.39374  ? 79  PHE   A CD1 1 
ATOM   600  C  CD2 . PHE   A 1 82  ? 47.50900 51.70400 14.69300 1.000 51.99735  ? 79  PHE   A CD2 1 
ATOM   601  C  CE1 . PHE   A 1 82  ? 48.93200 49.52800 13.76100 1.000 63.01312  ? 79  PHE   A CE1 1 
ATOM   602  C  CE2 . PHE   A 1 82  ? 47.45800 50.50200 15.37500 1.000 52.01898  ? 79  PHE   A CE2 1 
ATOM   603  C  CZ  . PHE   A 1 82  ? 48.17300 49.41300 14.91000 1.000 56.94014  ? 79  PHE   A CZ  1 
ATOM   604  N  N   . LEU   A 1 83  ? 45.45600 54.35500 12.99600 1.000 55.27305  ? 80  LEU   A N   1 
ATOM   605  C  CA  . LEU   A 1 83  ? 44.18300 54.38900 13.71100 1.000 55.19156  ? 80  LEU   A CA  1 
ATOM   606  C  C   . LEU   A 1 83  ? 43.01200 54.11800 12.77400 1.000 62.97699  ? 80  LEU   A C   1 
ATOM   607  O  O   . LEU   A 1 83  ? 42.11800 53.32600 13.09400 1.000 62.17375  ? 80  LEU   A O   1 
ATOM   608  C  CB  . LEU   A 1 83  ? 44.01300 55.73600 14.41200 1.000 60.52618  ? 80  LEU   A CB  1 
ATOM   609  C  CG  . LEU   A 1 83  ? 42.79300 55.84400 15.32900 1.000 67.24151  ? 80  LEU   A CG  1 
ATOM   610  C  CD1 . LEU   A 1 83  ? 43.16800 55.47200 16.75400 1.000 80.39984  ? 80  LEU   A CD1 1 
ATOM   611  C  CD2 . LEU   A 1 83  ? 42.19800 57.24400 15.27100 1.000 76.36923  ? 80  LEU   A CD2 1 
ATOM   612  N  N   . GLY   A 1 84  ? 43.00300 54.76500 11.60800 1.000 60.95142  ? 81  GLY   A N   1 
ATOM   613  C  CA  . GLY   A 1 84  ? 41.91800 54.54400 10.66500 1.000 52.14597  ? 81  GLY   A CA  1 
ATOM   614  C  C   . GLY   A 1 84  ? 41.87700 53.12000 10.14700 1.000 50.08514  ? 81  GLY   A C   1 
ATOM   615  O  O   . GLY   A 1 84  ? 40.81200 52.50100 10.08600 1.000 51.32856  ? 81  GLY   A O   1 
ATOM   616  N  N   . ARG   A 1 85  ? 43.03800 52.57900 9.76900  1.000 46.36548  ? 82  ARG   A N   1 
ATOM   617  C  CA  . ARG   A 1 85  ? 43.09700 51.18400 9.34700  1.000 58.03129  ? 82  ARG   A CA  1 
ATOM   618  C  C   . ARG   A 1 85  ? 42.68000 50.25100 10.47900 1.000 63.86485  ? 82  ARG   A C   1 
ATOM   619  O  O   . ARG   A 1 85  ? 42.00900 49.23800 10.24600 1.000 54.15958  ? 82  ARG   A O   1 
ATOM   620  C  CB  . ARG   A 1 85  ? 44.50300 50.85000 8.84800  1.000 53.94409  ? 82  ARG   A CB  1 
ATOM   621  C  CG  . ARG   A 1 85  ? 44.76100 51.32800 7.42400  1.000 61.52840  ? 82  ARG   A CG  1 
ATOM   622  C  CD  . ARG   A 1 85  ? 46.15900 50.98400 6.93700  1.000 60.23707  ? 82  ARG   A CD  1 
ATOM   623  N  NE  . ARG   A 1 85  ? 47.20300 51.51200 7.80600  1.000 64.52875  ? 82  ARG   A NE  1 
ATOM   624  C  CZ  . ARG   A 1 85  ? 48.00100 50.76000 8.55200  1.000 73.07778  ? 82  ARG   A CZ  1 
ATOM   625  N  NH1 . ARG   A 1 85  ? 47.88300 49.44200 8.57900  1.000 62.64579  ? 82  ARG   A NH1 1 
ATOM   626  N  NH2 . ARG   A 1 85  ? 48.93900 51.34400 9.29200  1.000 66.27396  ? 82  ARG   A NH2 1 
ATOM   627  N  N   . TYR   A 1 86  ? 43.05100 50.58600 11.71600 1.000 57.62706  ? 83  TYR   A N   1 
ATOM   628  C  CA  . TYR   A 1 86  ? 42.62300 49.79300 12.86300 1.000 54.56648  ? 83  TYR   A CA  1 
ATOM   629  C  C   . TYR   A 1 86  ? 41.11000 49.85400 13.02800 1.000 54.51286  ? 83  TYR   A C   1 
ATOM   630  O  O   . TYR   A 1 86  ? 40.44300 48.81600 13.12800 1.000 51.44046  ? 83  TYR   A O   1 
ATOM   631  C  CB  . TYR   A 1 86  ? 43.33700 50.28600 14.12500 1.000 60.33086  ? 83  TYR   A CB  1 
ATOM   632  C  CG  . TYR   A 1 86  ? 42.83700 49.71900 15.44100 1.000 63.52918  ? 83  TYR   A CG  1 
ATOM   633  C  CD1 . TYR   A 1 86  ? 42.43900 48.39100 15.55600 1.000 52.68191  ? 83  TYR   A CD1 1 
ATOM   634  C  CD2 . TYR   A 1 86  ? 42.79400 50.51400 16.57900 1.000 75.23315  ? 83  TYR   A CD2 1 
ATOM   635  C  CE1 . TYR   A 1 86  ? 41.99200 47.88200 16.76100 1.000 58.74173  ? 83  TYR   A CE1 1 
ATOM   636  C  CE2 . TYR   A 1 86  ? 42.35400 50.01300 17.78700 1.000 72.02812  ? 83  TYR   A CE2 1 
ATOM   637  C  CZ  . TYR   A 1 86  ? 41.95500 48.69800 17.87500 1.000 77.96355  ? 83  TYR   A CZ  1 
ATOM   638  O  OH  . TYR   A 1 86  ? 41.51600 48.20400 19.08200 1.000 61.76110  ? 83  TYR   A OH  1 
ATOM   639  N  N   . MET   A 1 87  ? 40.54900 51.06400 13.03900 1.000 60.50845  ? 84  MET   A N   1 
ATOM   640  C  CA  . MET   A 1 87  ? 39.10800 51.20600 13.20900 1.000 63.13007  ? 84  MET   A CA  1 
ATOM   641  C  C   . MET   A 1 87  ? 38.34000 50.58000 12.05300 1.000 55.78735  ? 84  MET   A C   1 
ATOM   642  O  O   . MET   A 1 87  ? 37.25000 50.03500 12.25900 1.000 60.48677  ? 84  MET   A O   1 
ATOM   643  C  CB  . MET   A 1 87  ? 38.74000 52.68100 13.35800 1.000 60.51293  ? 84  MET   A CB  1 
ATOM   644  C  CG  . MET   A 1 87  ? 39.22600 53.28600 14.66000 1.000 59.89738  ? 84  MET   A CG  1 
ATOM   645  S  SD  . MET   A 1 87  ? 38.15500 52.86900 16.04700 1.000 69.19509  ? 84  MET   A SD  1 
ATOM   646  C  CE  . MET   A 1 87  ? 39.18700 51.70600 16.93600 1.000 71.55414  ? 84  MET   A CE  1 
ATOM   647  N  N   . SER   A 1 88  ? 38.89000 50.64000 10.83800 1.000 54.61554  ? 85  SER   A N   1 
ATOM   648  C  CA  . SER   A 1 88  ? 38.21700 50.03300 9.69400  1.000 61.81619  ? 85  SER   A CA  1 
ATOM   649  C  C   . SER   A 1 88  ? 38.15100 48.51700 9.83500  1.000 56.74976  ? 85  SER   A C   1 
ATOM   650  O  O   . SER   A 1 88  ? 37.12500 47.90300 9.51900  1.000 52.95614  ? 85  SER   A O   1 
ATOM   651  C  CB  . SER   A 1 88  ? 38.92700 50.42300 8.39600  1.000 51.51988  ? 85  SER   A CB  1 
ATOM   652  O  OG  . SER   A 1 88  ? 38.19700 49.98400 7.26500  1.000 71.88174  ? 85  SER   A OG  1 
ATOM   653  N  N   . ALA   A 1 89  ? 39.23500 47.89700 10.30600 1.000 56.92123  ? 86  ALA   A N   1 
ATOM   654  C  CA  . ALA   A 1 89  ? 39.21600 46.45700 10.53600 1.000 56.27228  ? 86  ALA   A CA  1 
ATOM   655  C  C   . ALA   A 1 89  ? 38.30200 46.09500 11.70000 1.000 53.11765  ? 86  ALA   A C   1 
ATOM   656  O  O   . ALA   A 1 89  ? 37.55600 45.11100 11.62500 1.000 53.05441  ? 86  ALA   A O   1 
ATOM   657  C  CB  . ALA   A 1 89  ? 40.63300 45.94200 10.78800 1.000 58.72675  ? 86  ALA   A CB  1 
ATOM   658  N  N   . LEU   A 1 90  ? 38.34300 46.87800 12.78400 1.000 54.57032  ? 87  LEU   A N   1 
ATOM   659  C  CA  . LEU   A 1 90  ? 37.51400 46.57000 13.94500 1.000 54.03738  ? 87  LEU   A CA  1 
ATOM   660  C  C   . LEU   A 1 90  ? 36.04000 46.51200 13.56800 1.000 62.06826  ? 87  LEU   A C   1 
ATOM   661  O  O   . LEU   A 1 90  ? 35.30400 45.65600 14.06900 1.000 58.69071  ? 87  LEU   A O   1 
ATOM   662  C  CB  . LEU   A 1 90  ? 37.74800 47.59700 15.05700 1.000 49.60228  ? 87  LEU   A CB  1 
ATOM   663  C  CG  . LEU   A 1 90  ? 37.00600 47.35000 16.37600 1.000 63.96990  ? 87  LEU   A CG  1 
ATOM   664  C  CD1 . LEU   A 1 90  ? 37.44300 46.04400 17.03600 1.000 51.43162  ? 87  LEU   A CD1 1 
ATOM   665  C  CD2 . LEU   A 1 90  ? 37.18600 48.51900 17.33200 1.000 57.03883  ? 87  LEU   A CD2 1 
ATOM   666  N  N   . ASN   A 1 91  ? 35.60500 47.39300 12.65900 1.000 65.57618  ? 88  ASN   A N   1 
ATOM   667  C  CA  . ASN   A 1 91  ? 34.21000 47.42600 12.22500 1.000 67.42045  ? 88  ASN   A CA  1 
ATOM   668  C  C   . ASN   A 1 91  ? 33.72300 46.06600 11.74200 1.000 63.44038  ? 88  ASN   A C   1 
ATOM   669  O  O   . ASN   A 1 91  ? 32.55100 45.72100 11.93400 1.000 59.33314  ? 88  ASN   A O   1 
ATOM   670  C  CB  . ASN   A 1 91  ? 34.03700 48.46200 11.11400 1.000 73.26651  ? 88  ASN   A CB  1 
ATOM   671  C  CG  . ASN   A 1 91  ? 32.78200 49.29000 11.27800 1.000 75.50903  ? 88  ASN   A CG  1 
ATOM   672  O  OD1 . ASN   A 1 91  ? 32.20000 49.34700 12.36200 1.000 86.00160  ? 88  ASN   A OD1 1 
ATOM   673  N  ND2 . ASN   A 1 91  ? 32.34900 49.92800 10.19700 1.000 93.76228  ? 88  ASN   A ND2 1 
ATOM   674  N  N   . HIS   A 1 92  ? 34.59800 45.28600 11.11000 1.000 60.75912  ? 89  HIS   A N   1 
ATOM   675  C  CA  . HIS   A 1 92  ? 34.24200 43.94200 10.67700 1.000 59.90286  ? 89  HIS   A CA  1 
ATOM   676  C  C   . HIS   A 1 92  ? 34.41900 42.92500 11.80200 1.000 66.02543  ? 89  HIS   A C   1 
ATOM   677  O  O   . HIS   A 1 92  ? 33.52000 42.12000 12.06300 1.000 61.92194  ? 89  HIS   A O   1 
ATOM   678  C  CB  . HIS   A 1 92  ? 35.08600 43.53500 9.46500  1.000 56.50399  ? 89  HIS   A CB  1 
ATOM   679  C  CG  . HIS   A 1 92  ? 34.82600 44.35800 8.24200  1.000 69.14760  ? 89  HIS   A CG  1 
ATOM   680  N  ND1 . HIS   A 1 92  ? 33.82500 44.06400 7.34200  1.000 69.24301  ? 89  HIS   A ND1 1 
ATOM   681  C  CD2 . HIS   A 1 92  ? 35.44000 45.46900 7.77100  1.000 62.04834  ? 89  HIS   A CD2 1 
ATOM   682  C  CE1 . HIS   A 1 92  ? 33.83400 44.95700 6.36800  1.000 73.49495  ? 89  HIS   A CE1 1 
ATOM   683  N  NE2 . HIS   A 1 92  ? 34.80400 45.82000 6.60400  1.000 65.52226  ? 89  HIS   A NE2 1 
ATOM   684  N  N   . THR   A 1 93  ? 35.56500 42.96000 12.48700 1.000 49.85946  ? 90  THR   A N   1 
ATOM   685  C  CA  . THR   A 1 93  ? 35.88200 41.91500 13.45400 1.000 61.88222  ? 90  THR   A CA  1 
ATOM   686  C  C   . THR   A 1 93  ? 34.91900 41.88500 14.63600 1.000 60.82516  ? 90  THR   A C   1 
ATOM   687  O  O   . THR   A 1 93  ? 34.76700 40.82900 15.25900 1.000 60.75449  ? 90  THR   A O   1 
ATOM   688  C  CB  . THR   A 1 93  ? 37.31700 42.07700 13.96000 1.000 45.96854  ? 90  THR   A CB  1 
ATOM   689  O  OG1 . THR   A 1 93  ? 37.41900 43.26600 14.75100 1.000 51.60457  ? 90  THR   A OG1 1 
ATOM   690  C  CG2 . THR   A 1 93  ? 38.29200 42.15600 12.79000 1.000 46.87151  ? 90  THR   A CG2 1 
ATOM   691  N  N   . LYS   A 1 94  ? 34.22700 42.98700 14.90100 1.000 64.63180  ? 91  LYS   A N   1 
ATOM   692  C  CA  . LYS   A 1 94  ? 33.27400 43.03100 16.03900 1.000 54.32357  ? 91  LYS   A CA  1 
ATOM   693  C  C   . LYS   A 1 94  ? 32.04400 42.19000 15.69600 1.000 60.51550  ? 91  LYS   A C   1 
ATOM   694  O  O   . LYS   A 1 94  ? 31.34400 41.78100 16.62600 1.000 69.90667  ? 91  LYS   A O   1 
ATOM   695  C  CB  . LYS   A 1 94  ? 32.91700 44.48000 16.36900 1.000 60.16004  ? 91  LYS   A CB  1 
ATOM   696  C  CG  . LYS   A 1 94  ? 32.23000 45.24900 15.25000 1.000 95.54711  ? 91  LYS   A CG  1 
ATOM   697  C  CD  . LYS   A 1 94  ? 32.23100 46.74500 15.45800 1.000 102.77310 ? 91  LYS   A CD  1 
ATOM   698  C  CE  . LYS   A 1 94  ? 30.98700 47.41100 14.90900 1.000 99.25403  ? 91  LYS   A CE  1 
ATOM   699  N  NZ  . LYS   A 1 94  ? 31.15100 48.88000 14.80300 1.000 92.04514  ? 91  LYS   A NZ  1 
ATOM   700  N  N   . LYS   A 1 95  ? 31.80700 41.93400 14.41300 1.000 64.19614  ? 92  LYS   A N   1 
ATOM   701  C  CA  . LYS   A 1 95  ? 30.66600 41.14700 13.97200 1.000 66.61305  ? 92  LYS   A CA  1 
ATOM   702  C  C   . LYS   A 1 95  ? 31.01000 39.68800 13.71100 1.000 62.10776  ? 92  LYS   A C   1 
ATOM   703  O  O   . LYS   A 1 95  ? 30.09700 38.88500 13.48600 1.000 61.43766  ? 92  LYS   A O   1 
ATOM   704  C  CB  . LYS   A 1 95  ? 30.04300 41.76300 12.70800 1.000 66.90919  ? 92  LYS   A CB  1 
ATOM   705  C  CG  . LYS   A 1 95  ? 29.66900 43.23500 12.85700 1.000 74.97505  ? 92  LYS   A CG  1 
ATOM   706  C  CD  . LYS   A 1 95  ? 29.12200 43.83000 11.55900 1.000 84.05131  ? 92  LYS   A CD  1 
ATOM   707  C  CE  . LYS   A 1 95  ? 29.82100 43.26100 10.33200 1.000 97.48965  ? 92  LYS   A CE  1 
ATOM   708  N  NZ  . LYS   A 1 95  ? 30.11900 44.29200 9.29300  1.000 80.33573  ? 92  LYS   A NZ  1 
ATOM   709  N  N   . TRP   A 1 96  ? 32.29000 39.32600 13.73100 1.000 67.13760  ? 93  TRP   A N   1 
ATOM   710  C  CA  . TRP   A 1 96  ? 32.67600 37.92900 13.61900 1.000 63.48698  ? 93  TRP   A CA  1 
ATOM   711  C  C   . TRP   A 1 96  ? 32.30000 37.16700 14.88900 1.000 62.80463  ? 93  TRP   A C   1 
ATOM   712  O  O   . TRP   A 1 96  ? 32.08600 37.74900 15.95600 1.000 64.11931  ? 93  TRP   A O   1 
ATOM   713  C  CB  . TRP   A 1 96  ? 34.17900 37.79800 13.37400 1.000 52.18231  ? 93  TRP   A CB  1 
ATOM   714  C  CG  . TRP   A 1 96  ? 34.65200 38.35300 12.07000 1.000 58.94067  ? 93  TRP   A CG  1 
ATOM   715  C  CD1 . TRP   A 1 96  ? 33.88100 38.83600 11.05200 1.000 59.91862  ? 93  TRP   A CD1 1 
ATOM   716  C  CD2 . TRP   A 1 96  ? 36.01200 38.47800 11.63800 1.000 50.65578  ? 93  TRP   A CD2 1 
ATOM   717  N  NE1 . TRP   A 1 96  ? 34.67800 39.25600 10.01300 1.000 58.24535  ? 93  TRP   A NE1 1 
ATOM   718  C  CE2 . TRP   A 1 96  ? 35.99000 39.04700 10.34900 1.000 53.97380  ? 93  TRP   A CE2 1 
ATOM   719  C  CE3 . TRP   A 1 96  ? 37.24600 38.16600 12.21800 1.000 53.85853  ? 93  TRP   A CE3 1 
ATOM   720  C  CZ2 . TRP   A 1 96  ? 37.15400 39.30800 9.63000  1.000 52.40760  ? 93  TRP   A CZ2 1 
ATOM   721  C  CZ3 . TRP   A 1 96  ? 38.40100 38.42700 11.50200 1.000 56.73988  ? 93  TRP   A CZ3 1 
ATOM   722  C  CH2 . TRP   A 1 96  ? 38.34700 38.99200 10.22200 1.000 58.88729  ? 93  TRP   A CH2 1 
ATOM   723  N  N   . LYS   A 1 97  ? 32.22600 35.84600 14.76500 1.000 68.70659  ? 94  LYS   A N   1 
ATOM   724  C  CA  . LYS   A 1 97  ? 31.96800 34.97000 15.90000 1.000 77.28750  ? 94  LYS   A CA  1 
ATOM   725  C  C   . LYS   A 1 97  ? 33.26500 34.30800 16.34600 1.000 66.91351  ? 94  LYS   A C   1 
ATOM   726  O  O   . LYS   A 1 97  ? 34.07200 33.87600 15.51700 1.000 65.96179  ? 94  LYS   A O   1 
ATOM   727  C  CB  . LYS   A 1 97  ? 30.92700 33.90600 15.54900 1.000 69.85547  ? 94  LYS   A CB  1 
ATOM   728  C  CG  . LYS   A 1 97  ? 29.57400 34.47300 15.14900 1.000 81.27219  ? 94  LYS   A CG  1 
ATOM   729  C  CD  . LYS   A 1 97  ? 29.02500 35.39600 16.22500 1.000 85.33528  ? 94  LYS   A CD  1 
ATOM   730  C  CE  . LYS   A 1 97  ? 27.69400 36.00100 15.81000 1.000 83.99823  ? 94  LYS   A CE  1 
ATOM   731  N  NZ  . LYS   A 1 97  ? 27.18700 36.96500 16.82600 1.000 99.63937  ? 94  LYS   A NZ  1 
ATOM   732  N  N   . TYR   A 1 98  ? 33.46100 34.22900 17.66400 1.000 62.97258  ? 95  TYR   A N   1 
ATOM   733  C  CA  . TYR   A 1 98  ? 34.68700 33.70200 18.26000 1.000 59.89998  ? 95  TYR   A CA  1 
ATOM   734  C  C   . TYR   A 1 98  ? 34.33400 32.54100 19.18300 1.000 59.89541  ? 95  TYR   A C   1 
ATOM   735  O  O   . TYR   A 1 98  ? 34.34400 32.68700 20.41500 1.000 68.92594  ? 95  TYR   A O   1 
ATOM   736  C  CB  . TYR   A 1 98  ? 35.44500 34.79800 19.00700 1.000 52.63696  ? 95  TYR   A CB  1 
ATOM   737  C  CG  . TYR   A 1 98  ? 35.83800 35.95700 18.11700 1.000 70.77160  ? 95  TYR   A CG  1 
ATOM   738  C  CD1 . TYR   A 1 98  ? 36.99200 35.90500 17.34600 1.000 56.97346  ? 95  TYR   A CD1 1 
ATOM   739  C  CD2 . TYR   A 1 98  ? 35.04800 37.09700 18.03800 1.000 65.09483  ? 95  TYR   A CD2 1 
ATOM   740  C  CE1 . TYR   A 1 98  ? 37.35200 36.95700 16.52700 1.000 64.29013  ? 95  TYR   A CE1 1 
ATOM   741  C  CE2 . TYR   A 1 98  ? 35.40000 38.15600 17.22100 1.000 65.54088  ? 95  TYR   A CE2 1 
ATOM   742  C  CZ  . TYR   A 1 98  ? 36.55300 38.08000 16.46800 1.000 64.20071  ? 95  TYR   A CZ  1 
ATOM   743  O  OH  . TYR   A 1 98  ? 36.91200 39.13000 15.65200 1.000 54.41187  ? 95  TYR   A OH  1 
ATOM   744  N  N   . PRO   A 1 99  ? 34.03400 31.37100 18.62600 1.000 65.09025  ? 96  PRO   A N   1 
ATOM   745  C  CA  . PRO   A 1 99  ? 33.64700 30.23300 19.46300 1.000 52.23097  ? 96  PRO   A CA  1 
ATOM   746  C  C   . PRO   A 1 99  ? 34.84500 29.56400 20.11700 1.000 66.42054  ? 96  PRO   A C   1 
ATOM   747  O  O   . PRO   A 1 99  ? 35.94600 29.51500 19.56300 1.000 58.46079  ? 96  PRO   A O   1 
ATOM   748  C  CB  . PRO   A 1 99  ? 32.97000 29.28600 18.46600 1.000 56.40569  ? 96  PRO   A CB  1 
ATOM   749  C  CG  . PRO   A 1 99  ? 33.67400 29.56200 17.17600 1.000 58.77905  ? 96  PRO   A CG  1 
ATOM   750  C  CD  . PRO   A 1 99  ? 34.03200 31.03000 17.19100 1.000 57.36169  ? 96  PRO   A CD  1 
ATOM   751  N  N   . GLN   A 1 100 ? 34.61200 29.04700 21.32200 1.000 62.75883  ? 97  GLN   A N   1 
ATOM   752  C  CA  . GLN   A 1 100 ? 35.60100 28.22400 22.00700 1.000 65.50889  ? 97  GLN   A CA  1 
ATOM   753  C  C   . GLN   A 1 100 ? 35.59300 26.82900 21.39200 1.000 62.32258  ? 97  GLN   A C   1 
ATOM   754  O  O   . GLN   A 1 100 ? 34.55400 26.16100 21.37200 1.000 63.88922  ? 97  GLN   A O   1 
ATOM   755  C  CB  . GLN   A 1 100 ? 35.30300 28.15200 23.50300 1.000 64.91464  ? 97  GLN   A CB  1 
ATOM   756  C  CG  . GLN   A 1 100 ? 35.45400 29.46700 24.24900 1.000 65.99782  ? 97  GLN   A CG  1 
ATOM   757  C  CD  . GLN   A 1 100 ? 36.84000 30.06300 24.11000 1.000 73.23006  ? 97  GLN   A CD  1 
ATOM   758  O  OE1 . GLN   A 1 100 ? 37.82400 29.49600 24.58700 1.000 74.28807  ? 97  GLN   A OE1 1 
ATOM   759  N  NE2 . GLN   A 1 100 ? 36.92300 31.22000 23.46200 1.000 81.96108  ? 97  GLN   A NE2 1 
ATOM   760  N  N   . VAL   A 1 101 ? 36.74400 26.39300 20.88600 1.000 59.76539  ? 98  VAL   A N   1 
ATOM   761  C  CA  . VAL   A 1 101 ? 36.88300 25.09600 20.23600 1.000 50.04562  ? 98  VAL   A CA  1 
ATOM   762  C  C   . VAL   A 1 101 ? 38.06200 24.37700 20.87500 1.000 62.22940  ? 98  VAL   A C   1 
ATOM   763  O  O   . VAL   A 1 101 ? 39.20600 24.83400 20.75600 1.000 63.81238  ? 98  VAL   A O   1 
ATOM   764  C  CB  . VAL   A 1 101 ? 37.09200 25.22900 18.71700 1.000 67.46716  ? 98  VAL   A CB  1 
ATOM   765  C  CG1 . VAL   A 1 101 ? 37.35400 23.86400 18.09000 1.000 67.30135  ? 98  VAL   A CG1 1 
ATOM   766  C  CG2 . VAL   A 1 101 ? 35.89100 25.89900 18.06800 1.000 66.49509  ? 98  VAL   A CG2 1 
ATOM   767  N  N   . ASN   A 1 102 ? 37.78500 23.25800 21.54900 1.000 60.53604  ? 99  ASN   A N   1 
ATOM   768  C  CA  . ASN   A 1 102 ? 38.82100 22.45500 22.20300 1.000 58.44686  ? 99  ASN   A CA  1 
ATOM   769  C  C   . ASN   A 1 102 ? 39.62800 23.29600 23.19100 1.000 59.42416  ? 99  ASN   A C   1 
ATOM   770  O  O   . ASN   A 1 102 ? 40.85700 23.21300 23.25100 1.000 53.23310  ? 99  ASN   A O   1 
ATOM   771  C  CB  . ASN   A 1 102 ? 39.73800 21.79200 21.16900 1.000 60.15096  ? 99  ASN   A CB  1 
ATOM   772  C  CG  . ASN   A 1 102 ? 40.54100 20.64100 21.74800 1.000 77.42052  ? 99  ASN   A CG  1 
ATOM   773  O  OD1 . ASN   A 1 102 ? 41.75100 20.54800 21.54000 1.000 79.37604  ? 99  ASN   A OD1 1 
ATOM   774  N  ND2 . ASN   A 1 102 ? 39.87000 19.76000 22.48200 1.000 71.87488  ? 99  ASN   A ND2 1 
ATOM   775  N  N   . GLY   A 1 103 ? 38.92900 24.12700 23.96400 1.000 54.57127  ? 100 GLY   A N   1 
ATOM   776  C  CA  . GLY   A 1 103 ? 39.58100 25.01200 24.90700 1.000 54.51464  ? 100 GLY   A CA  1 
ATOM   777  C  C   . GLY   A 1 103 ? 40.35100 26.16100 24.29600 1.000 65.94476  ? 100 GLY   A C   1 
ATOM   778  O  O   . GLY   A 1 103 ? 41.12100 26.81400 25.00600 1.000 68.33091  ? 100 GLY   A O   1 
ATOM   779  N  N   . LEU   A 1 104 ? 40.17000 26.43400 23.00300 1.000 63.90357  ? 101 LEU   A N   1 
ATOM   780  C  CA  . LEU   A 1 104 ? 40.87300 27.50800 22.31600 1.000 61.29455  ? 101 LEU   A CA  1 
ATOM   781  C  C   . LEU   A 1 104 ? 39.87500 28.43600 21.63900 1.000 61.34307  ? 101 LEU   A C   1 
ATOM   782  O  O   . LEU   A 1 104 ? 38.82000 28.00300 21.16500 1.000 58.31100  ? 101 LEU   A O   1 
ATOM   783  C  CB  . LEU   A 1 104 ? 41.84600 26.96300 21.26500 1.000 52.26087  ? 101 LEU   A CB  1 
ATOM   784  C  CG  . LEU   A 1 104 ? 42.98900 26.09000 21.77900 1.000 52.77862  ? 101 LEU   A CG  1 
ATOM   785  C  CD1 . LEU   A 1 104 ? 43.50600 25.18200 20.67100 1.000 47.23789  ? 101 LEU   A CD1 1 
ATOM   786  C  CD2 . LEU   A 1 104 ? 44.10500 26.95500 22.33900 1.000 48.84508  ? 101 LEU   A CD2 1 
ATOM   787  N  N   . THR   A 1 105 ? 40.22200 29.72100 21.59100 1.000 55.94768  ? 102 THR   A N   1 
ATOM   788  C  CA  . THR   A 1 105 ? 39.39700 30.70900 20.90500 1.000 52.63546  ? 102 THR   A CA  1 
ATOM   789  C  C   . THR   A 1 105 ? 39.69000 30.66000 19.40900 1.000 57.04079  ? 102 THR   A C   1 
ATOM   790  O  O   . THR   A 1 105 ? 40.82600 30.90200 18.98500 1.000 50.94227  ? 102 THR   A O   1 
ATOM   791  C  CB  . THR   A 1 105 ? 39.66100 32.11000 21.45300 1.000 57.04379  ? 102 THR   A CB  1 
ATOM   792  O  OG1 . THR   A 1 105 ? 39.61500 32.08500 22.88400 1.000 55.44368  ? 102 THR   A OG1 1 
ATOM   793  C  CG2 . THR   A 1 105 ? 38.61400 33.08800 20.93600 1.000 51.27543  ? 102 THR   A CG2 1 
ATOM   794  N  N   . SER   A 1 106 ? 38.67300 30.34100 18.61600 1.000 49.87125  ? 103 SER   A N   1 
ATOM   795  C  CA  . SER   A 1 106 ? 38.76700 30.30200 17.16600 1.000 55.82297  ? 103 SER   A CA  1 
ATOM   796  C  C   . SER   A 1 106 ? 37.91100 31.41800 16.56700 1.000 51.93549  ? 103 SER   A C   1 
ATOM   797  O  O   . SER   A 1 106 ? 37.40300 32.29000 17.28100 1.000 53.75467  ? 103 SER   A O   1 
ATOM   798  C  CB  . SER   A 1 106 ? 38.35100 28.92300 16.65300 1.000 51.73498  ? 103 SER   A CB  1 
ATOM   799  O  OG  . SER   A 1 106 ? 38.70100 28.76500 15.28900 1.000 58.74507  ? 103 SER   A OG  1 
ATOM   800  N  N   . ILE   A 1 107 ? 37.75200 31.39300 15.24400 1.000 57.12743  ? 104 ILE   A N   1 
ATOM   801  C  CA  . ILE   A 1 107 ? 36.94200 32.37000 14.52400 1.000 55.31139  ? 104 ILE   A CA  1 
ATOM   802  C  C   . ILE   A 1 107 ? 36.03100 31.62900 13.55900 1.000 55.26568  ? 104 ILE   A C   1 
ATOM   803  O  O   . ILE   A 1 107 ? 36.50200 30.80300 12.76900 1.000 50.02787  ? 104 ILE   A O   1 
ATOM   804  C  CB  . ILE   A 1 107 ? 37.79800 33.38100 13.73600 1.000 48.82153  ? 104 ILE   A CB  1 
ATOM   805  C  CG1 . ILE   A 1 107 ? 39.00500 33.84900 14.54900 1.000 51.01804  ? 104 ILE   A CG1 1 
ATOM   806  C  CG2 . ILE   A 1 107 ? 36.94700 34.57800 13.34800 1.000 59.74629  ? 104 ILE   A CG2 1 
ATOM   807  C  CD1 . ILE   A 1 107 ? 39.73000 35.03000 13.92700 1.000 46.72354  ? 104 ILE   A CD1 1 
ATOM   808  N  N   . LYS   A 1 108 ? 34.73800 31.93700 13.60300 1.000 51.73720  ? 105 LYS   A N   1 
ATOM   809  C  CA  . LYS   A 1 108 ? 33.83700 31.45300 12.56800 1.000 66.34023  ? 105 LYS   A CA  1 
ATOM   810  C  C   . LYS   A 1 108 ? 34.20800 32.08700 11.23100 1.000 64.05012  ? 105 LYS   A C   1 
ATOM   811  O  O   . LYS   A 1 108 ? 34.48300 33.28800 11.15000 1.000 64.18414  ? 105 LYS   A O   1 
ATOM   812  C  CB  . LYS   A 1 108 ? 32.38600 31.76800 12.93400 1.000 65.32727  ? 105 LYS   A CB  1 
ATOM   813  C  CG  . LYS   A 1 108 ? 31.36100 31.25000 11.93500 1.000 83.11755  ? 105 LYS   A CG  1 
ATOM   814  C  CD  . LYS   A 1 108 ? 29.94900 31.64600 12.34000 1.000 88.51335  ? 105 LYS   A CD  1 
ATOM   815  C  CE  . LYS   A 1 108 ? 28.94400 31.24800 11.27100 1.000 78.78016  ? 105 LYS   A CE  1 
ATOM   816  N  NZ  . LYS   A 1 108 ? 27.55700 31.65400 11.62600 1.000 97.54500  ? 105 LYS   A NZ  1 
ATOM   817  N  N   . TRP   A 1 109 ? 34.22800 31.26400 10.18400 1.000 70.70391  ? 106 TRP   A N   1 
ATOM   818  C  CA  . TRP   A 1 109 ? 34.74500 31.70000 8.89400  1.000 69.29626  ? 106 TRP   A CA  1 
ATOM   819  C  C   . TRP   A 1 109 ? 33.92000 32.85400 8.34500  1.000 68.27565  ? 106 TRP   A C   1 
ATOM   820  O  O   . TRP   A 1 109 ? 32.68500 32.83200 8.38200  1.000 70.25552  ? 106 TRP   A O   1 
ATOM   821  C  CB  . TRP   A 1 109 ? 34.77200 30.52300 7.91100  1.000 71.96796  ? 106 TRP   A CB  1 
ATOM   822  C  CG  . TRP   A 1 109 ? 33.47800 30.25600 7.19900  1.000 106.82215 ? 106 TRP   A CG  1 
ATOM   823  C  CD1 . TRP   A 1 109 ? 32.53200 29.33300 7.53700  1.000 109.49600 ? 106 TRP   A CD1 1 
ATOM   824  C  CD2 . TRP   A 1 109 ? 33.00100 30.90500 6.01400  1.000 114.30621 ? 106 TRP   A CD2 1 
ATOM   825  N  NE1 . TRP   A 1 109 ? 31.48900 29.37600 6.64400  1.000 117.33966 ? 106 TRP   A NE1 1 
ATOM   826  C  CE2 . TRP   A 1 109 ? 31.75200 30.33400 5.70000  1.000 108.47415 ? 106 TRP   A CE2 1 
ATOM   827  C  CE3 . TRP   A 1 109 ? 33.50400 31.92100 5.19500  1.000 96.90584  ? 106 TRP   A CE3 1 
ATOM   828  C  CZ2 . TRP   A 1 109 ? 31.00100 30.74200 4.60100  1.000 107.60884 ? 106 TRP   A CZ2 1 
ATOM   829  C  CZ3 . TRP   A 1 109 ? 32.75700 32.32600 4.10600  1.000 95.72181  ? 106 TRP   A CZ3 1 
ATOM   830  C  CH2 . TRP   A 1 109 ? 31.51900 31.73700 3.81800  1.000 109.05560 ? 106 TRP   A CH2 1 
ATOM   831  N  N   . ALA   A 1 110 ? 34.61700 33.87100 7.84500  1.000 67.44923  ? 107 ALA   A N   1 
ATOM   832  C  CA  . ALA   A 1 110 ? 34.00700 35.06400 7.28300  1.000 58.96614  ? 107 ALA   A CA  1 
ATOM   833  C  C   . ALA   A 1 110 ? 35.11600 35.94200 6.72800  1.000 63.67614  ? 107 ALA   A C   1 
ATOM   834  O  O   . ALA   A 1 110 ? 36.17700 36.06400 7.34200  1.000 56.36904  ? 107 ALA   A O   1 
ATOM   835  C  CB  . ALA   A 1 110 ? 33.19300 35.83300 8.33500  1.000 52.86201  ? 107 ALA   A CB  1 
ATOM   836  N  N   . ASP   A 1 111 ? 34.86900 36.52900 5.55800  1.000 67.30749  ? 108 ASP   A N   1 
ATOM   837  C  CA  . ASP   A 1 111 ? 35.76500 37.52200 4.96500  1.000 52.71772  ? 108 ASP   A CA  1 
ATOM   838  C  C   . ASP   A 1 111 ? 37.18900 36.99000 4.80100  1.000 57.20930  ? 108 ASP   A C   1 
ATOM   839  O  O   . ASP   A 1 111 ? 38.16500 37.72500 4.97000  1.000 58.59935  ? 108 ASP   A O   1 
ATOM   840  C  CB  . ASP   A 1 111 ? 35.75700 38.81500 5.78200  1.000 46.94249  ? 108 ASP   A CB  1 
ATOM   841  C  CG  . ASP   A 1 111 ? 34.35300 39.34200 6.02500  1.000 66.15510  ? 108 ASP   A CG  1 
ATOM   842  O  OD1 . ASP   A 1 111 ? 33.40500 38.83500 5.38700  1.000 78.25380  ? 108 ASP   A OD1 1 
ATOM   843  O  OD2 . ASP   A 1 111 ? 34.20000 40.27100 6.84400  1.000 58.92715  ? 108 ASP   A OD2 1 
ATOM   844  N  N   . ASN   A 1 112 ? 37.30700 35.70200 4.46400  1.000 54.02352  ? 109 ASN   A N   1 
ATOM   845  C  CA  . ASN   A 1 112 ? 38.60000 35.05700 4.21500  1.000 56.93086  ? 109 ASN   A CA  1 
ATOM   846  C  C   . ASN   A 1 112 ? 39.51700 35.11900 5.43700  1.000 58.02135  ? 109 ASN   A C   1 
ATOM   847  O  O   . ASN   A 1 112 ? 40.73000 35.29700 5.31000  1.000 60.08263  ? 109 ASN   A O   1 
ATOM   848  C  CB  . ASN   A 1 112 ? 39.29800 35.66700 2.99600  1.000 46.70314  ? 109 ASN   A CB  1 
ATOM   849  C  CG  . ASN   A 1 112 ? 38.59400 35.34700 1.68800  1.000 68.76706  ? 109 ASN   A CG  1 
ATOM   850  O  OD1 . ASN   A 1 112 ? 38.07600 34.24600 1.49800  1.000 72.09110  ? 109 ASN   A OD1 1 
ATOM   851  N  ND2 . ASN   A 1 112 ? 38.57900 36.31200 0.77600  1.000 57.01058  ? 109 ASN   A ND2 1 
ATOM   852  N  N   . ASN   A 1 113 ? 38.94500 34.96300 6.63400  1.000 51.49413  ? 110 ASN   A N   1 
ATOM   853  C  CA  . ASN   A 1 113 ? 39.71800 35.06500 7.86700  1.000 62.50262  ? 110 ASN   A CA  1 
ATOM   854  C  C   . ASN   A 1 113 ? 40.33900 33.74000 8.29800  1.000 57.05731  ? 110 ASN   A C   1 
ATOM   855  O  O   . ASN   A 1 113 ? 40.71800 33.60200 9.46600  1.000 65.53282  ? 110 ASN   A O   1 
ATOM   856  C  CB  . ASN   A 1 113 ? 38.85500 35.62600 9.00300  1.000 53.68225  ? 110 ASN   A CB  1 
ATOM   857  C  CG  . ASN   A 1 113 ? 37.70300 34.70500 9.39500  1.000 57.31744  ? 110 ASN   A CG  1 
ATOM   858  O  OD1 . ASN   A 1 113 ? 37.61100 33.55900 8.95100  1.000 54.70822  ? 110 ASN   A OD1 1 
ATOM   859  N  ND2 . ASN   A 1 113 ? 36.80500 35.22100 10.22800 1.000 46.35712  ? 110 ASN   A ND2 1 
ATOM   860  N  N   . CYS   A 1 114 ? 40.44900 32.76400 7.39200  1.000 66.27977  ? 111 CYS   A N   1 
ATOM   861  C  CA  . CYS   A 1 114 ? 40.96500 31.45800 7.79200  1.000 62.08636  ? 111 CYS   A CA  1 
ATOM   862  C  C   . CYS   A 1 114 ? 42.41500 31.55300 8.25100  1.000 62.37177  ? 111 CYS   A C   1 
ATOM   863  O  O   . CYS   A 1 114 ? 42.82800 30.84300 9.17400  1.000 63.90854  ? 111 CYS   A O   1 
ATOM   864  C  CB  . CYS   A 1 114 ? 40.83000 30.45300 6.64700  1.000 51.67290  ? 111 CYS   A CB  1 
ATOM   865  S  SG  . CYS   A 1 114 ? 41.86800 30.74500 5.19500  1.000 63.32026  ? 111 CYS   A SG  1 
ATOM   866  N  N   . TYR   A 1 115 ? 43.20300 32.42800 7.62400  1.000 52.24258  ? 112 TYR   A N   1 
ATOM   867  C  CA  . TYR   A 1 115 ? 44.58300 32.59100 8.06300  1.000 54.92910  ? 112 TYR   A CA  1 
ATOM   868  C  C   . TYR   A 1 115 ? 44.65900 33.32500 9.39700  1.000 47.62315  ? 112 TYR   A C   1 
ATOM   869  O  O   . TYR   A 1 115 ? 45.57800 33.07700 10.18600 1.000 50.44777  ? 112 TYR   A O   1 
ATOM   870  C  CB  . TYR   A 1 115 ? 45.39900 33.31300 6.98700  1.000 52.16745  ? 112 TYR   A CB  1 
ATOM   871  C  CG  . TYR   A 1 115 ? 45.22500 34.81400 6.96100  1.000 52.17936  ? 112 TYR   A CG  1 
ATOM   872  C  CD1 . TYR   A 1 115 ? 44.09100 35.39300 6.40500  1.000 57.50573  ? 112 TYR   A CD1 1 
ATOM   873  C  CD2 . TYR   A 1 115 ? 46.19800 35.65500 7.49100  1.000 46.85581  ? 112 TYR   A CD2 1 
ATOM   874  C  CE1 . TYR   A 1 115 ? 43.92800 36.76800 6.37700  1.000 56.84488  ? 112 TYR   A CE1 1 
ATOM   875  C  CE2 . TYR   A 1 115 ? 46.04500 37.02900 7.46800  1.000 55.69359  ? 112 TYR   A CE2 1 
ATOM   876  C  CZ  . TYR   A 1 115 ? 44.90900 37.58100 6.91000  1.000 57.35919  ? 112 TYR   A CZ  1 
ATOM   877  O  OH  . TYR   A 1 115 ? 44.75500 38.94900 6.88700  1.000 56.94964  ? 112 TYR   A OH  1 
ATOM   878  N  N   . LEU   A 1 116 ? 43.70100 34.21400 9.67300  1.000 56.74885  ? 113 LEU   A N   1 
ATOM   879  C  CA  . LEU   A 1 116 ? 43.66600 34.88900 10.96700 1.000 51.98830  ? 113 LEU   A CA  1 
ATOM   880  C  C   . LEU   A 1 116 ? 43.29400 33.92600 12.08600 1.000 55.16989  ? 113 LEU   A C   1 
ATOM   881  O  O   . LEU   A 1 116 ? 43.86200 33.99100 13.18200 1.000 52.27347  ? 113 LEU   A O   1 
ATOM   882  C  CB  . LEU   A 1 116 ? 42.68200 36.05800 10.93200 1.000 54.04990  ? 113 LEU   A CB  1 
ATOM   883  C  CG  . LEU   A 1 116 ? 43.06100 37.24800 10.05200 1.000 67.22619  ? 113 LEU   A CG  1 
ATOM   884  C  CD1 . LEU   A 1 116 ? 41.91400 38.24500 9.98800  1.000 63.22943  ? 113 LEU   A CD1 1 
ATOM   885  C  CD2 . LEU   A 1 116 ? 44.32500 37.90900 10.58100 1.000 51.43413  ? 113 LEU   A CD2 1 
ATOM   886  N  N   . ALA   A 1 117 ? 42.33200 33.03600 11.83600 1.000 53.80671  ? 114 ALA   A N   1 
ATOM   887  C  CA  . ALA   A 1 117 ? 41.96800 32.05400 12.85100 1.000 55.15294  ? 114 ALA   A CA  1 
ATOM   888  C  C   . ALA   A 1 117 ? 43.12500 31.10700 13.13400 1.000 52.25199  ? 114 ALA   A C   1 
ATOM   889  O  O   . ALA   A 1 117 ? 43.38100 30.75800 14.29200 1.000 52.76627  ? 114 ALA   A O   1 
ATOM   890  C  CB  . ALA   A 1 117 ? 40.72600 31.27900 12.41500 1.000 52.17445  ? 114 ALA   A CB  1 
ATOM   891  N  N   . THR   A 1 118 ? 43.84800 30.69500 12.08900 1.000 43.13423  ? 115 THR   A N   1 
ATOM   892  C  CA  . THR   A 1 118 ? 44.99000 29.80700 12.28600 1.000 54.35517  ? 115 THR   A CA  1 
ATOM   893  C  C   . THR   A 1 118 ? 46.08000 30.48700 13.10600 1.000 52.17971  ? 115 THR   A C   1 
ATOM   894  O  O   . THR   A 1 118 ? 46.63000 29.88900 14.03800 1.000 55.91065  ? 115 THR   A O   1 
ATOM   895  C  CB  . THR   A 1 118 ? 45.54200 29.34700 10.93500 1.000 47.95114  ? 115 THR   A CB  1 
ATOM   896  O  OG1 . THR   A 1 118 ? 44.57000 28.52800 10.27500 1.000 57.99142  ? 115 THR   A OG1 1 
ATOM   897  C  CG2 . THR   A 1 118 ? 46.82100 28.54500 11.12500 1.000 54.92123  ? 115 THR   A CG2 1 
ATOM   898  N  N   . ALA   A 1 119 ? 46.39800 31.74300 12.78000 1.000 48.30137  ? 116 ALA   A N   1 
ATOM   899  C  CA  . ALA   A 1 119 ? 47.37900 32.48200 13.57000 1.000 55.76073  ? 116 ALA   A CA  1 
ATOM   900  C  C   . ALA   A 1 119 ? 46.89100 32.69700 14.99900 1.000 52.45640  ? 116 ALA   A C   1 
ATOM   901  O  O   . ALA   A 1 119 ? 47.67800 32.60700 15.94900 1.000 46.88112  ? 116 ALA   A O   1 
ATOM   902  C  CB  . ALA   A 1 119 ? 47.69200 33.82100 12.90400 1.000 43.20282  ? 116 ALA   A CB  1 
ATOM   903  N  N   . LEU   A 1 120 ? 45.59600 32.97800 15.17100 1.000 48.64039  ? 117 LEU   A N   1 
ATOM   904  C  CA  . LEU   A 1 120 ? 45.05700 33.19700 16.50900 1.000 46.14069  ? 117 LEU   A CA  1 
ATOM   905  C  C   . LEU   A 1 120 ? 45.15200 31.93200 17.35200 1.000 62.81057  ? 117 LEU   A C   1 
ATOM   906  O  O   . LEU   A 1 120 ? 45.49700 31.99100 18.53900 1.000 52.43071  ? 117 LEU   A O   1 
ATOM   907  C  CB  . LEU   A 1 120 ? 43.60800 33.67400 16.41500 1.000 47.84679  ? 117 LEU   A CB  1 
ATOM   908  C  CG  . LEU   A 1 120 ? 42.81300 33.81100 17.71500 1.000 52.08421  ? 117 LEU   A CG  1 
ATOM   909  C  CD1 . LEU   A 1 120 ? 43.41500 34.88600 18.60500 1.000 48.60622  ? 117 LEU   A CD1 1 
ATOM   910  C  CD2 . LEU   A 1 120 ? 41.35100 34.11300 17.41300 1.000 44.57427  ? 117 LEU   A CD2 1 
ATOM   911  N  N   . LEU   A 1 121 ? 44.85600 30.77600 16.75300 1.000 59.51109  ? 118 LEU   A N   1 
ATOM   912  C  CA  . LEU   A 1 121 ? 44.96700 29.51800 17.48200 1.000 57.33984  ? 118 LEU   A CA  1 
ATOM   913  C  C   . LEU   A 1 121 ? 46.42100 29.19800 17.80900 1.000 52.80196  ? 118 LEU   A C   1 
ATOM   914  O  O   . LEU   A 1 121 ? 46.71700 28.65800 18.88100 1.000 49.01627  ? 118 LEU   A O   1 
ATOM   915  C  CB  . LEU   A 1 121 ? 44.33100 28.38900 16.67100 1.000 45.97799  ? 118 LEU   A CB  1 
ATOM   916  C  CG  . LEU   A 1 121 ? 42.81700 28.49200 16.46500 1.000 52.47891  ? 118 LEU   A CG  1 
ATOM   917  C  CD1 . LEU   A 1 121 ? 42.37600 27.68100 15.24800 1.000 48.39324  ? 118 LEU   A CD1 1 
ATOM   918  C  CD2 . LEU   A 1 121 ? 42.06400 28.05000 17.70800 1.000 50.51774  ? 118 LEU   A CD2 1 
ATOM   919  N  N   . THR   A 1 122 ? 47.34200 29.53300 16.90200 1.000 45.98944  ? 119 THR   A N   1 
ATOM   920  C  CA  . THR   A 1 122 ? 48.75400 29.25900 17.14800 1.000 43.52379  ? 119 THR   A CA  1 
ATOM   921  C  C   . THR   A 1 122 ? 49.28800 30.10000 18.30000 1.000 55.36775  ? 119 THR   A C   1 
ATOM   922  O  O   . THR   A 1 122 ? 50.07300 29.61100 19.12200 1.000 47.82712  ? 119 THR   A O   1 
ATOM   923  C  CB  . THR   A 1 122 ? 49.56700 29.51600 15.88000 1.000 48.05199  ? 119 THR   A CB  1 
ATOM   924  O  OG1 . THR   A 1 122 ? 49.01100 28.76400 14.79500 1.000 46.82433  ? 119 THR   A OG1 1 
ATOM   925  C  CG2 . THR   A 1 122 ? 51.02200 29.11000 16.08000 1.000 38.30719  ? 119 THR   A CG2 1 
ATOM   926  N  N   . LEU   A 1 123 ? 48.86400 31.36400 18.38600 1.000 49.02346  ? 120 LEU   A N   1 
ATOM   927  C  CA  . LEU   A 1 123 ? 49.40400 32.25600 19.40600 1.000 51.98647  ? 120 LEU   A CA  1 
ATOM   928  C  C   . LEU   A 1 123 ? 49.00100 31.82100 20.81000 1.000 53.17916  ? 120 LEU   A C   1 
ATOM   929  O  O   . LEU   A 1 123 ? 49.72200 32.10300 21.77300 1.000 57.17585  ? 120 LEU   A O   1 
ATOM   930  C  CB  . LEU   A 1 123 ? 48.95200 33.69100 19.13800 1.000 54.99116  ? 120 LEU   A CB  1 
ATOM   931  C  CG  . LEU   A 1 123 ? 49.62000 34.36300 17.93600 1.000 57.76370  ? 120 LEU   A CG  1 
ATOM   932  C  CD1 . LEU   A 1 123 ? 48.80100 35.55100 17.45800 1.000 56.42261  ? 120 LEU   A CD1 1 
ATOM   933  C  CD2 . LEU   A 1 123 ? 51.03600 34.78600 18.28300 1.000 59.47240  ? 120 LEU   A CD2 1 
ATOM   934  N  N   . GLN   A 1 124 ? 47.86800 31.13200 20.94600 1.000 52.61091  ? 121 GLN   A N   1 
ATOM   935  C  CA  . GLN   A 1 124 ? 47.42900 30.62000 22.23800 1.000 56.37067  ? 121 GLN   A CA  1 
ATOM   936  C  C   . GLN   A 1 124 ? 48.19600 29.38000 22.67900 1.000 51.57253  ? 121 GLN   A C   1 
ATOM   937  O  O   . GLN   A 1 124 ? 47.95900 28.89200 23.78900 1.000 62.30937  ? 121 GLN   A O   1 
ATOM   938  C  CB  . GLN   A 1 124 ? 45.93000 30.30900 22.20200 1.000 50.97229  ? 121 GLN   A CB  1 
ATOM   939  C  CG  . GLN   A 1 124 ? 45.04600 31.54200 22.13600 1.000 57.63960  ? 121 GLN   A CG  1 
ATOM   940  C  CD  . GLN   A 1 124 ? 43.65100 31.23700 21.62200 1.000 53.71807  ? 121 GLN   A CD  1 
ATOM   941  O  OE1 . GLN   A 1 124 ? 42.74600 30.92200 22.39600 1.000 52.07815  ? 121 GLN   A OE1 1 
ATOM   942  N  NE2 . GLN   A 1 124 ? 43.47100 31.33100 20.31000 1.000 51.81436  ? 121 GLN   A NE2 1 
ATOM   943  N  N   . GLN   A 1 125 ? 49.11000 28.86700 21.85400 1.000 54.48836  ? 122 GLN   A N   1 
ATOM   944  C  CA  . GLN   A 1 125 ? 49.84300 27.65100 22.16900 1.000 50.97960  ? 122 GLN   A CA  1 
ATOM   945  C  C   . GLN   A 1 125 ? 51.35300 27.84100 22.21400 1.000 55.65381  ? 122 GLN   A C   1 
ATOM   946  O  O   . GLN   A 1 125 ? 52.07400 26.87000 22.47100 1.000 52.80163  ? 122 GLN   A O   1 
ATOM   947  C  CB  . GLN   A 1 125 ? 49.49400 26.55000 21.15800 1.000 55.28763  ? 122 GLN   A CB  1 
ATOM   948  C  CG  . GLN   A 1 125 ? 48.03300 26.13500 21.19200 1.000 44.20334  ? 122 GLN   A CG  1 
ATOM   949  C  CD  . GLN   A 1 125 ? 47.64600 25.26600 20.01300 1.000 52.58574  ? 122 GLN   A CD  1 
ATOM   950  O  OE1 . GLN   A 1 125 ? 47.89500 24.06100 20.00500 1.000 50.82689  ? 122 GLN   A OE1 1 
ATOM   951  N  NE2 . GLN   A 1 125 ? 47.03400 25.87500 19.00800 1.000 49.18438  ? 122 GLN   A NE2 1 
ATOM   952  N  N   . ILE   A 1 126 ? 51.85700 29.05000 21.97100 1.000 55.04393  ? 123 ILE   A N   1 
ATOM   953  C  CA  . ILE   A 1 126 ? 53.28200 29.33500 22.07700 1.000 51.01024  ? 123 ILE   A CA  1 
ATOM   954  C  C   . ILE   A 1 126 ? 53.48000 30.50800 23.02600 1.000 52.27792  ? 123 ILE   A C   1 
ATOM   955  O  O   . ILE   A 1 126 ? 52.57600 31.32500 23.23400 1.000 52.10988  ? 123 ILE   A O   1 
ATOM   956  C  CB  . ILE   A 1 126 ? 53.92300 29.62300 20.70000 1.000 58.92234  ? 123 ILE   A CB  1 
ATOM   957  C  CG1 . ILE   A 1 126 ? 53.27200 30.84200 20.04600 1.000 56.56849  ? 123 ILE   A CG1 1 
ATOM   958  C  CG2 . ILE   A 1 126 ? 53.80700 28.40700 19.79200 1.000 45.69264  ? 123 ILE   A CG2 1 
ATOM   959  C  CD1 . ILE   A 1 126 ? 53.93900 31.25800 18.75800 1.000 47.11151  ? 123 ILE   A CD1 1 
ATOM   960  N  N   . GLU   A 1 127 ? 54.67200 30.58100 23.61600 1.000 50.45769  ? 124 GLU   A N   1 
ATOM   961  C  CA  . GLU   A 1 127 ? 54.99200 31.61300 24.59500 1.000 55.55650  ? 124 GLU   A CA  1 
ATOM   962  C  C   . GLU   A 1 127 ? 55.51800 32.85000 23.87700 1.000 52.17695  ? 124 GLU   A C   1 
ATOM   963  O  O   . GLU   A 1 127 ? 56.53100 32.78100 23.17200 1.000 58.19360  ? 124 GLU   A O   1 
ATOM   964  C  CB  . GLU   A 1 127 ? 56.01600 31.10600 25.61100 1.000 54.63069  ? 124 GLU   A CB  1 
ATOM   965  C  CG  . GLU   A 1 127 ? 56.43800 32.15800 26.63400 1.000 52.57633  ? 124 GLU   A CG  1 
ATOM   966  C  CD  . GLU   A 1 127 ? 55.28900 32.64500 27.50900 1.000 68.94482  ? 124 GLU   A CD  1 
ATOM   967  O  OE1 . GLU   A 1 127 ? 54.29400 31.90700 27.67500 1.000 72.33557  ? 124 GLU   A OE1 1 
ATOM   968  O  OE2 . GLU   A 1 127 ? 55.40900 33.75500 28.07300 1.000 70.22025  ? 124 GLU   A OE2 1 
ATOM   969  N  N   . LEU   A 1 128 ? 54.83900 33.98000 24.06700 1.000 59.13046  ? 125 LEU   A N   1 
ATOM   970  C  CA  . LEU   A 1 128 ? 55.17100 35.20300 23.35200 1.000 58.01483  ? 125 LEU   A CA  1 
ATOM   971  C  C   . LEU   A 1 128 ? 54.71700 36.40300 24.16900 1.000 56.87077  ? 125 LEU   A C   1 
ATOM   972  O  O   . LEU   A 1 128 ? 53.65500 36.37000 24.79700 1.000 60.72585  ? 125 LEU   A O   1 
ATOM   973  C  CB  . LEU   A 1 128 ? 54.51300 35.22800 21.96600 1.000 54.50109  ? 125 LEU   A CB  1 
ATOM   974  C  CG  . LEU   A 1 128 ? 55.18600 36.04000 20.86000 1.000 62.45591  ? 125 LEU   A CG  1 
ATOM   975  C  CD1 . LEU   A 1 128 ? 56.53000 35.43900 20.48600 1.000 58.52245  ? 125 LEU   A CD1 1 
ATOM   976  C  CD2 . LEU   A 1 128 ? 54.27800 36.12000 19.64500 1.000 61.50715  ? 125 LEU   A CD2 1 
ATOM   977  N  N   . LYS   A 1 129 ? 55.52500 37.46000 24.15200 1.000 52.55451  ? 126 LYS   A N   1 
ATOM   978  C  CA  . LYS   A 1 129 ? 55.20100 38.71300 24.82400 1.000 53.72728  ? 126 LYS   A CA  1 
ATOM   979  C  C   . LYS   A 1 129 ? 55.30600 39.84600 23.81500 1.000 60.13196  ? 126 LYS   A C   1 
ATOM   980  O  O   . LYS   A 1 129 ? 56.37200 40.06200 23.23100 1.000 54.33120  ? 126 LYS   A O   1 
ATOM   981  C  CB  . LYS   A 1 129 ? 56.13200 38.95900 26.01400 1.000 60.60502  ? 126 LYS   A CB  1 
ATOM   982  C  CG  . LYS   A 1 129 ? 55.72500 40.13300 26.88600 1.000 67.70154  ? 126 LYS   A CG  1 
ATOM   983  C  CD  . LYS   A 1 129 ? 56.87500 40.58700 27.77000 1.000 86.04993  ? 126 LYS   A CD  1 
ATOM   984  C  CE  . LYS   A 1 129 ? 57.01200 39.69900 29.00100 1.000 98.33162  ? 126 LYS   A CE  1 
ATOM   985  N  NZ  . LYS   A 1 129 ? 57.70100 40.39700 30.12400 1.000 89.04968  ? 126 LYS   A NZ  1 
ATOM   986  N  N   . PHE   A 1 130 ? 54.20500 40.56400 23.61200 1.000 62.12759  ? 127 PHE   A N   1 
ATOM   987  C  CA  . PHE   A 1 130 ? 54.16300 41.65800 22.65100 1.000 55.59608  ? 127 PHE   A CA  1 
ATOM   988  C  C   . PHE   A 1 130 ? 54.65700 42.95000 23.28900 1.000 54.18804  ? 127 PHE   A C   1 
ATOM   989  O  O   . PHE   A 1 130 ? 54.35900 43.23900 24.45100 1.000 58.01383  ? 127 PHE   A O   1 
ATOM   990  C  CB  . PHE   A 1 130 ? 52.74400 41.84400 22.11500 1.000 48.63264  ? 127 PHE   A CB  1 
ATOM   991  C  CG  . PHE   A 1 130 ? 52.32600 40.78400 21.13400 1.000 54.34143  ? 127 PHE   A CG  1 
ATOM   992  C  CD1 . PHE   A 1 130 ? 53.01500 40.61500 19.94500 1.000 47.86659  ? 127 PHE   A CD1 1 
ATOM   993  C  CD2 . PHE   A 1 130 ? 51.24700 39.95600 21.40300 1.000 50.81387  ? 127 PHE   A CD2 1 
ATOM   994  C  CE1 . PHE   A 1 130 ? 52.63600 39.64100 19.03900 1.000 53.62246  ? 127 PHE   A CE1 1 
ATOM   995  C  CE2 . PHE   A 1 130 ? 50.86200 38.98100 20.50100 1.000 58.26141  ? 127 PHE   A CE2 1 
ATOM   996  C  CZ  . PHE   A 1 130 ? 51.55700 38.82300 19.31700 1.000 49.45539  ? 127 PHE   A CZ  1 
ATOM   997  N  N   . ASN   A 1 131 ? 55.41400 43.72900 22.51500 1.000 51.59547  ? 128 ASN   A N   1 
ATOM   998  C  CA  . ASN   A 1 131 ? 55.99400 44.98000 22.99300 1.000 51.27789  ? 128 ASN   A CA  1 
ATOM   999  C  C   . ASN   A 1 131 ? 54.96300 46.10800 23.07600 1.000 53.76471  ? 128 ASN   A C   1 
ATOM   1000 O  O   . ASN   A 1 131 ? 54.91900 46.80600 24.09700 1.000 56.98182  ? 128 ASN   A O   1 
ATOM   1001 C  CB  . ASN   A 1 131 ? 57.17400 45.39400 22.10700 1.000 56.61506  ? 128 ASN   A CB  1 
ATOM   1002 C  CG  . ASN   A 1 131 ? 58.32400 44.40400 22.16300 1.000 67.14226  ? 128 ASN   A CG  1 
ATOM   1003 O  OD1 . ASN   A 1 131 ? 58.72200 43.95500 23.24000 1.000 61.69064  ? 128 ASN   A OD1 1 
ATOM   1004 N  ND2 . ASN   A 1 131 ? 58.86300 44.05800 21.00000 1.000 59.76373  ? 128 ASN   A ND2 1 
ATOM   1005 N  N   . PRO   A 1 132 ? 54.13300 46.34300 22.05700 1.000 54.84303  ? 129 PRO   A N   1 
ATOM   1006 C  CA  . PRO   A 1 132 ? 53.10500 47.38600 22.18200 1.000 52.87355  ? 129 PRO   A CA  1 
ATOM   1007 C  C   . PRO   A 1 132 ? 52.05600 46.99000 23.20300 1.000 50.18260  ? 129 PRO   A C   1 
ATOM   1008 O  O   . PRO   A 1 132 ? 51.45100 45.91300 23.09400 1.000 55.21441  ? 129 PRO   A O   1 
ATOM   1009 C  CB  . PRO   A 1 132 ? 52.50200 47.46900 20.77000 1.000 50.91316  ? 129 PRO   A CB  1 
ATOM   1010 C  CG  . PRO   A 1 132 ? 53.52200 46.85800 19.87600 1.000 45.75188  ? 129 PRO   A CG  1 
ATOM   1011 C  CD  . PRO   A 1 132 ? 54.14000 45.77400 20.69500 1.000 50.43931  ? 129 PRO   A CD  1 
ATOM   1012 N  N   . PRO   A 1 133 ? 51.81900 47.83000 24.21600 1.000 53.75986  ? 130 PRO   A N   1 
ATOM   1013 C  CA  . PRO   A 1 133 ? 50.76300 47.51900 25.19500 1.000 53.27965  ? 130 PRO   A CA  1 
ATOM   1014 C  C   . PRO   A 1 133 ? 49.40500 47.26000 24.56800 1.000 57.21370  ? 130 PRO   A C   1 
ATOM   1015 O  O   . PRO   A 1 133 ? 48.63200 46.45300 25.10000 1.000 60.81287  ? 130 PRO   A O   1 
ATOM   1016 C  CB  . PRO   A 1 133 ? 50.74300 48.76600 26.09100 1.000 53.13859  ? 130 PRO   A CB  1 
ATOM   1017 C  CG  . PRO   A 1 133 ? 52.12600 49.31600 25.99500 1.000 49.39296  ? 130 PRO   A CG  1 
ATOM   1018 C  CD  . PRO   A 1 133 ? 52.59500 49.02400 24.59100 1.000 54.10883  ? 130 PRO   A CD  1 
ATOM   1019 N  N   . ALA   A 1 134 ? 49.08900 47.92100 23.45100 1.000 53.16913  ? 131 ALA   A N   1 
ATOM   1020 C  CA  . ALA   A 1 134 ? 47.83300 47.64400 22.76200 1.000 67.12574  ? 131 ALA   A CA  1 
ATOM   1021 C  C   . ALA   A 1 134 ? 47.76100 46.19100 22.31200 1.000 56.67151  ? 131 ALA   A C   1 
ATOM   1022 O  O   . ALA   A 1 134 ? 46.70300 45.55700 22.40000 1.000 50.36710  ? 131 ALA   A O   1 
ATOM   1023 C  CB  . ALA   A 1 134 ? 47.67000 48.58100 21.56400 1.000 58.09232  ? 131 ALA   A CB  1 
ATOM   1024 N  N   . LEU   A 1 135 ? 48.87900 45.64700 21.82400 1.000 47.76257  ? 132 LEU   A N   1 
ATOM   1025 C  CA  . LEU   A 1 135 ? 48.89300 44.25900 21.37300 1.000 52.59493  ? 132 LEU   A CA  1 
ATOM   1026 C  C   . LEU   A 1 135 ? 48.80900 43.29500 22.54700 1.000 59.07187  ? 132 LEU   A C   1 
ATOM   1027 O  O   . LEU   A 1 135 ? 48.09600 42.28800 22.48000 1.000 57.75343  ? 132 LEU   A O   1 
ATOM   1028 C  CB  . LEU   A 1 135 ? 50.15400 43.98300 20.55400 1.000 50.51025  ? 132 LEU   A CB  1 
ATOM   1029 C  CG  . LEU   A 1 135 ? 50.00100 43.88600 19.03800 1.000 54.24871  ? 132 LEU   A CG  1 
ATOM   1030 C  CD1 . LEU   A 1 135 ? 51.28900 43.37600 18.40700 1.000 57.78623  ? 132 LEU   A CD1 1 
ATOM   1031 C  CD2 . LEU   A 1 135 ? 48.82300 42.99700 18.66400 1.000 50.10940  ? 132 LEU   A CD2 1 
ATOM   1032 N  N   . GLN   A 1 136 ? 49.53600 43.58500 23.63000 1.000 52.49724  ? 133 GLN   A N   1 
ATOM   1033 C  CA  . GLN   A 1 136 ? 49.53600 42.69400 24.78500 1.000 60.45298  ? 133 GLN   A CA  1 
ATOM   1034 C  C   . GLN   A 1 136 ? 48.17600 42.66500 25.46700 1.000 55.81489  ? 133 GLN   A C   1 
ATOM   1035 O  O   . GLN   A 1 136 ? 47.69300 41.59300 25.85000 1.000 59.94711  ? 133 GLN   A O   1 
ATOM   1036 C  CB  . GLN   A 1 136 ? 50.62300 43.11800 25.77100 1.000 58.86626  ? 133 GLN   A CB  1 
ATOM   1037 C  CG  . GLN   A 1 136 ? 50.97900 42.06000 26.79800 1.000 62.24980  ? 133 GLN   A CG  1 
ATOM   1038 C  CD  . GLN   A 1 136 ? 51.21300 40.69400 26.17800 1.000 75.60931  ? 133 GLN   A CD  1 
ATOM   1039 O  OE1 . GLN   A 1 136 ? 51.92500 40.56200 25.17900 1.000 64.75513  ? 133 GLN   A OE1 1 
ATOM   1040 N  NE2 . GLN   A 1 136 ? 50.61500 39.66600 26.77300 1.000 66.89062  ? 133 GLN   A NE2 1 
ATOM   1041 N  N   . ASP   A 1 137 ? 47.54300 43.82900 25.62900 1.000 54.58853  ? 134 ASP   A N   1 
ATOM   1042 C  CA  . ASP   A 1 137 ? 46.23900 43.88100 26.28600 1.000 59.18600  ? 134 ASP   A CA  1 
ATOM   1043 C  C   . ASP   A 1 137 ? 45.18900 43.12900 25.48000 1.000 60.40622  ? 134 ASP   A C   1 
ATOM   1044 O  O   . ASP   A 1 137 ? 44.40000 42.35400 26.03400 1.000 51.89098  ? 134 ASP   A O   1 
ATOM   1045 C  CB  . ASP   A 1 137 ? 45.81000 45.33300 26.49800 1.000 62.36095  ? 134 ASP   A CB  1 
ATOM   1046 C  CG  . ASP   A 1 137 ? 46.63400 46.03700 27.55400 1.000 59.68914  ? 134 ASP   A CG  1 
ATOM   1047 O  OD1 . ASP   A 1 137 ? 47.41000 45.35800 28.26000 1.000 61.01839  ? 134 ASP   A OD1 1 
ATOM   1048 O  OD2 . ASP   A 1 137 ? 46.50900 47.27300 27.67400 1.000 73.03623  ? 134 ASP   A OD2 1 
ATOM   1049 N  N   . ALA   A 1 138 ? 45.16000 43.35600 24.16400 1.000 52.64135  ? 135 ALA   A N   1 
ATOM   1050 C  CA  . ALA   A 1 138 ? 44.21500 42.64500 23.31100 1.000 53.50899  ? 135 ALA   A CA  1 
ATOM   1051 C  C   . ALA   A 1 138 ? 44.53300 41.15800 23.25200 1.000 49.77730  ? 135 ALA   A C   1 
ATOM   1052 O  O   . ALA   A 1 138 ? 43.61500 40.33400 23.16000 1.000 48.91358  ? 135 ALA   A O   1 
ATOM   1053 C  CB  . ALA   A 1 138 ? 44.21800 43.24800 21.90500 1.000 51.60880  ? 135 ALA   A CB  1 
ATOM   1054 N  N   . TYR   A 1 139 ? 45.82100 40.80200 23.28800 1.000 47.32568  ? 136 TYR   A N   1 
ATOM   1055 C  CA  . TYR   A 1 139 ? 46.22200 39.40000 23.36000 1.000 50.16499  ? 136 TYR   A CA  1 
ATOM   1056 C  C   . TYR   A 1 139 ? 45.57500 38.71600 24.55800 1.000 61.38873  ? 136 TYR   A C   1 
ATOM   1057 O  O   . TYR   A 1 139 ? 44.96600 37.64800 24.42600 1.000 48.48447  ? 136 TYR   A O   1 
ATOM   1058 C  CB  . TYR   A 1 139 ? 47.74800 39.31000 23.44000 1.000 50.45979  ? 136 TYR   A CB  1 
ATOM   1059 C  CG  . TYR   A 1 139 ? 48.35200 37.93100 23.27000 1.000 60.96233  ? 136 TYR   A CG  1 
ATOM   1060 C  CD1 . TYR   A 1 139 ? 47.59500 36.85200 22.82700 1.000 61.35605  ? 136 TYR   A CD1 1 
ATOM   1061 C  CD2 . TYR   A 1 139 ? 49.69200 37.70900 23.57400 1.000 75.38746  ? 136 TYR   A CD2 1 
ATOM   1062 C  CE1 . TYR   A 1 139 ? 48.16200 35.59300 22.68100 1.000 66.91071  ? 136 TYR   A CE1 1 
ATOM   1063 C  CE2 . TYR   A 1 139 ? 50.26500 36.46000 23.43300 1.000 67.35005  ? 136 TYR   A CE2 1 
ATOM   1064 C  CZ  . TYR   A 1 139 ? 49.49900 35.40600 22.98700 1.000 79.67324  ? 136 TYR   A CZ  1 
ATOM   1065 O  OH  . TYR   A 1 139 ? 50.08000 34.16600 22.85000 1.000 79.94883  ? 136 TYR   A OH  1 
ATOM   1066 N  N   . TYR   A 1 140 ? 45.68200 39.33600 25.73800 1.000 52.82923  ? 137 TYR   A N   1 
ATOM   1067 C  CA  . TYR   A 1 140 ? 45.09500 38.76100 26.94400 1.000 51.51100  ? 137 TYR   A CA  1 
ATOM   1068 C  C   . TYR   A 1 140 ? 43.58700 38.59700 26.79600 1.000 57.98520  ? 137 TYR   A C   1 
ATOM   1069 O  O   . TYR   A 1 140 ? 43.03300 37.53300 27.09800 1.000 57.42406  ? 137 TYR   A O   1 
ATOM   1070 C  CB  . TYR   A 1 140 ? 45.42300 39.63600 28.15300 1.000 51.59711  ? 137 TYR   A CB  1 
ATOM   1071 C  CG  . TYR   A 1 140 ? 46.80800 39.42300 28.71800 1.000 50.57606  ? 137 TYR   A CG  1 
ATOM   1072 C  CD1 . TYR   A 1 140 ? 47.27800 38.14600 29.00100 1.000 50.31973  ? 137 TYR   A CD1 1 
ATOM   1073 C  CD2 . TYR   A 1 140 ? 47.64700 40.50000 28.96900 1.000 52.09387  ? 137 TYR   A CD2 1 
ATOM   1074 C  CE1 . TYR   A 1 140 ? 48.54400 37.95000 29.52100 1.000 42.85880  ? 137 TYR   A CE1 1 
ATOM   1075 C  CE2 . TYR   A 1 140 ? 48.91300 40.31400 29.49100 1.000 56.88377  ? 137 TYR   A CE2 1 
ATOM   1076 C  CZ  . TYR   A 1 140 ? 49.35700 39.03800 29.76600 1.000 56.98055  ? 137 TYR   A CZ  1 
ATOM   1077 O  OH  . TYR   A 1 140 ? 50.61900 38.84900 30.28500 1.000 53.03809  ? 137 TYR   A OH  1 
ATOM   1078 N  N   . ARG   A 1 141 ? 42.90200 39.64500 26.32800 1.000 50.66811  ? 138 ARG   A N   1 
ATOM   1079 C  CA  A ARG   A 1 141 ? 41.45500 39.56400 26.15600 0.507 56.80272  ? 138 ARG   A CA  1 
ATOM   1080 C  CA  B ARG   A 1 141 ? 41.45600 39.55100 26.17100 0.493 56.00867  ? 138 ARG   A CA  1 
ATOM   1081 C  C   . ARG   A 1 141 ? 41.07300 38.53000 25.10800 1.000 61.95507  ? 138 ARG   A C   1 
ATOM   1082 O  O   . ARG   A 1 141 ? 39.98500 37.94600 25.17900 1.000 57.92891  ? 138 ARG   A O   1 
ATOM   1083 C  CB  A ARG   A 1 141 ? 40.88800 40.93400 25.77800 0.507 56.47235  ? 138 ARG   A CB  1 
ATOM   1084 C  CB  B ARG   A 1 141 ? 40.87400 40.92600 25.84500 0.493 55.67449  ? 138 ARG   A CB  1 
ATOM   1085 C  CG  A ARG   A 1 141 ? 40.96500 41.97100 26.88800 0.507 63.19454  ? 138 ARG   A CG  1 
ATOM   1086 C  CG  B ARG   A 1 141 ? 41.01800 41.92300 26.98800 0.493 63.16287  ? 138 ARG   A CG  1 
ATOM   1087 C  CD  A ARG   A 1 141 ? 40.44600 41.41800 28.20900 0.507 63.85441  ? 138 ARG   A CD  1 
ATOM   1088 C  CD  B ARG   A 1 141 ? 40.45100 43.28500 26.63300 0.493 65.89188  ? 138 ARG   A CD  1 
ATOM   1089 N  NE  A ARG   A 1 141 ? 39.05900 40.97700 28.12500 0.507 70.94833  ? 138 ARG   A NE  1 
ATOM   1090 N  NE  B ARG   A 1 141 ? 41.42800 44.34800 26.83400 0.493 72.24634  ? 138 ARG   A NE  1 
ATOM   1091 C  CZ  A ARG   A 1 141 ? 38.50300 40.09000 28.94000 0.507 63.35216  ? 138 ARG   A CZ  1 
ATOM   1092 C  CZ  B ARG   A 1 141 ? 41.23600 45.40900 27.60700 0.493 60.49651  ? 138 ARG   A CZ  1 
ATOM   1093 N  NH1 A ARG   A 1 141 ? 39.19200 39.52100 29.91600 0.507 49.43499  ? 138 ARG   A NH1 1 
ATOM   1094 N  NH1 B ARG   A 1 141 ? 40.10400 45.58800 28.26700 0.493 57.21627  ? 138 ARG   A NH1 1 
ATOM   1095 N  NH2 A ARG   A 1 141 ? 37.22400 39.76600 28.77200 0.507 65.81706  ? 138 ARG   A NH2 1 
ATOM   1096 N  NH2 B ARG   A 1 141 ? 42.20600 46.31100 27.72100 0.493 51.29001  ? 138 ARG   A NH2 1 
ATOM   1097 N  N   . ALA   A 1 142 ? 41.95100 38.28900 24.13000 1.000 51.32895  ? 139 ALA   A N   1 
ATOM   1098 C  CA  . ALA   A 1 142 ? 41.67000 37.27100 23.12300 1.000 57.99937  ? 139 ALA   A CA  1 
ATOM   1099 C  C   . ALA   A 1 142 ? 41.70300 35.87400 23.73100 1.000 51.29346  ? 139 ALA   A C   1 
ATOM   1100 O  O   . ALA   A 1 142 ? 40.86700 35.02600 23.40000 1.000 58.15746  ? 139 ALA   A O   1 
ATOM   1101 C  CB  . ALA   A 1 142 ? 42.66700 37.38200 21.97000 1.000 49.02228  ? 139 ALA   A CB  1 
ATOM   1102 N  N   . ARG   A 1 143 ? 42.66800 35.61500 24.61900 1.000 53.43947  ? 140 ARG   A N   1 
ATOM   1103 C  CA  A ARG   A 1 143 ? 42.72200 34.31800 25.28400 0.586 65.23268  ? 140 ARG   A CA  1 
ATOM   1104 C  CA  B ARG   A 1 143 ? 42.72900 34.32200 25.29500 0.414 59.45755  ? 140 ARG   A CA  1 
ATOM   1105 C  C   . ARG   A 1 143 ? 41.49600 34.08500 26.15700 1.000 65.22762  ? 140 ARG   A C   1 
ATOM   1106 O  O   . ARG   A 1 143 ? 41.04100 32.94300 26.29300 1.000 66.63106  ? 140 ARG   A O   1 
ATOM   1107 C  CB  A ARG   A 1 143 ? 44.00300 34.20700 26.10900 0.586 58.82221  ? 140 ARG   A CB  1 
ATOM   1108 C  CB  B ARG   A 1 143 ? 43.99700 34.23400 26.14500 0.414 58.16645  ? 140 ARG   A CB  1 
ATOM   1109 C  CG  A ARG   A 1 143 ? 45.26400 34.45500 25.29900 0.586 57.05086  ? 140 ARG   A CG  1 
ATOM   1110 C  CG  B ARG   A 1 143 ? 44.10600 32.96000 26.97100 0.414 60.78617  ? 140 ARG   A CG  1 
ATOM   1111 C  CD  A ARG   A 1 143 ? 46.42700 34.89500 26.17300 0.586 70.13553  ? 140 ARG   A CD  1 
ATOM   1112 C  CD  B ARG   A 1 143 ? 44.51100 31.77800 26.11100 0.414 68.13625  ? 140 ARG   A CD  1 
ATOM   1113 N  NE  A ARG   A 1 143 ? 47.69200 34.31900 25.73000 0.586 80.20732  ? 140 ARG   A NE  1 
ATOM   1114 N  NE  B ARG   A 1 143 ? 45.79800 32.01100 25.46800 0.414 76.61541  ? 140 ARG   A NE  1 
ATOM   1115 C  CZ  A ARG   A 1 143 ? 48.05600 33.05800 25.92000 0.586 77.60424  ? 140 ARG   A CZ  1 
ATOM   1116 C  CZ  B ARG   A 1 143 ? 46.94200 31.47300 25.86800 0.414 74.84776  ? 140 ARG   A CZ  1 
ATOM   1117 N  NH1 A ARG   A 1 143 ? 47.28700 32.20600 26.57900 0.586 68.59011  ? 140 ARG   A NH1 1 
ATOM   1118 N  NH1 B ARG   A 1 143 ? 46.99100 30.62900 26.88500 0.414 68.03605  ? 140 ARG   A NH1 1 
ATOM   1119 N  NH2 A ARG   A 1 143 ? 49.22600 32.64200 25.44300 0.586 74.67078  ? 140 ARG   A NH2 1 
ATOM   1120 N  NH2 B ARG   A 1 143 ? 48.06600 31.79500 25.23400 0.414 76.14321  ? 140 ARG   A NH2 1 
ATOM   1121 N  N   . ALA   A 1 144 ? 40.94300 35.14600 26.74100 1.000 65.13070  ? 141 ALA   A N   1 
ATOM   1122 C  CA  . ALA   A 1 144 ? 39.73700 35.04400 27.55100 1.000 54.63339  ? 141 ALA   A CA  1 
ATOM   1123 C  C   . ALA   A 1 144 ? 38.46400 34.95700 26.71900 1.000 60.17716  ? 141 ALA   A C   1 
ATOM   1124 O  O   . ALA   A 1 144 ? 37.37600 34.87700 27.29700 1.000 72.75227  ? 141 ALA   A O   1 
ATOM   1125 C  CB  . ALA   A 1 144 ? 39.64200 36.23600 28.50600 1.000 59.53061  ? 141 ALA   A CB  1 
ATOM   1126 N  N   . GLY   A 1 145 ? 38.56300 34.98600 25.38800 1.000 56.90115  ? 142 GLY   A N   1 
ATOM   1127 C  CA  . GLY   A 1 145 ? 37.40900 34.81500 24.52500 1.000 56.25726  ? 142 GLY   A CA  1 
ATOM   1128 C  C   . GLY   A 1 145 ? 36.95600 36.04100 23.75400 1.000 62.92115  ? 142 GLY   A C   1 
ATOM   1129 O  O   . GLY   A 1 145 ? 36.04800 35.91600 22.92400 1.000 67.87054  ? 142 GLY   A O   1 
ATOM   1130 N  N   . GLU   A 1 146 ? 37.54100 37.21500 23.98800 1.000 65.71382  ? 143 GLU   A N   1 
ATOM   1131 C  CA  . GLU   A 1 146 ? 37.13400 38.45500 23.32000 1.000 63.75306  ? 143 GLU   A CA  1 
ATOM   1132 C  C   . GLU   A 1 146 ? 38.26800 38.89800 22.39500 1.000 56.52945  ? 143 GLU   A C   1 
ATOM   1133 O  O   . GLU   A 1 146 ? 39.11500 39.71000 22.77000 1.000 57.99143  ? 143 GLU   A O   1 
ATOM   1134 C  CB  . GLU   A 1 146 ? 36.78800 39.53400 24.33900 1.000 69.85866  ? 143 GLU   A CB  1 
ATOM   1135 C  CG  . GLU   A 1 146 ? 35.33500 39.52900 24.78000 1.000 76.54019  ? 143 GLU   A CG  1 
ATOM   1136 C  CD  . GLU   A 1 146 ? 35.06300 40.53800 25.88000 1.000 112.14291 ? 143 GLU   A CD  1 
ATOM   1137 O  OE1 . GLU   A 1 146 ? 35.87300 41.47700 26.04100 1.000 107.22044 ? 143 GLU   A OE1 1 
ATOM   1138 O  OE2 . GLU   A 1 146 ? 34.04500 40.38800 26.58700 1.000 121.43905 ? 143 GLU   A OE2 1 
ATOM   1139 N  N   . ALA   A 1 147 ? 38.26100 38.37500 21.16700 1.000 52.22499  ? 144 ALA   A N   1 
ATOM   1140 C  CA  . ALA   A 1 147 ? 39.38400 38.52800 20.25100 1.000 57.77025  ? 144 ALA   A CA  1 
ATOM   1141 C  C   . ALA   A 1 147 ? 39.08700 39.48000 19.09400 1.000 54.94857  ? 144 ALA   A C   1 
ATOM   1142 O  O   . ALA   A 1 147 ? 39.84800 39.51300 18.12200 1.000 57.04698  ? 144 ALA   A O   1 
ATOM   1143 C  CB  . ALA   A 1 147 ? 39.80700 37.16200 19.71000 1.000 44.19626  ? 144 ALA   A CB  1 
ATOM   1144 N  N   . ALA   A 1 148 ? 38.00600 40.26100 19.17800 1.000 57.29380  ? 145 ALA   A N   1 
ATOM   1145 C  CA  . ALA   A 1 148 ? 37.68700 41.19500 18.10100 1.000 58.92971  ? 145 ALA   A CA  1 
ATOM   1146 C  C   . ALA   A 1 148 ? 38.75200 42.28000 17.97600 1.000 55.23964  ? 145 ALA   A C   1 
ATOM   1147 O  O   . ALA   A 1 148 ? 39.24600 42.55300 16.87500 1.000 58.01255  ? 145 ALA   A O   1 
ATOM   1148 C  CB  . ALA   A 1 148 ? 36.30800 41.81600 18.32900 1.000 51.79926  ? 145 ALA   A CB  1 
ATOM   1149 N  N   . ASN   A 1 149 ? 39.12100 42.90900 19.09500 1.000 51.98609  ? 146 ASN   A N   1 
ATOM   1150 C  CA  . ASN   A 1 149 ? 40.12900 43.96400 19.04400 1.000 56.28583  ? 146 ASN   A CA  1 
ATOM   1151 C  C   . ASN   A 1 149 ? 41.49300 43.41000 18.65300 1.000 58.03664  ? 146 ASN   A C   1 
ATOM   1152 O  O   . ASN   A 1 149 ? 42.25500 44.07100 17.93700 1.000 58.84063  ? 146 ASN   A O   1 
ATOM   1153 C  CB  . ASN   A 1 149 ? 40.20700 44.68300 20.39000 1.000 56.08735  ? 146 ASN   A CB  1 
ATOM   1154 C  CG  . ASN   A 1 149 ? 39.32500 45.91300 20.44400 1.000 70.36463  ? 146 ASN   A CG  1 
ATOM   1155 O  OD1 . ASN   A 1 149 ? 39.67900 46.96900 19.91900 1.000 79.32644  ? 146 ASN   A OD1 1 
ATOM   1156 N  ND2 . ASN   A 1 149 ? 38.16200 45.78000 21.07200 1.000 69.75789  ? 146 ASN   A ND2 1 
ATOM   1157 N  N   . PHE   A 1 150 ? 41.81800 42.19900 19.10900 1.000 51.73810  ? 147 PHE   A N   1 
ATOM   1158 C  CA  . PHE   A 1 150 ? 43.10600 41.60400 18.76900 1.000 53.86925  ? 147 PHE   A CA  1 
ATOM   1159 C  C   . PHE   A 1 150 ? 43.20700 41.32600 17.27400 1.000 54.21149  ? 147 PHE   A C   1 
ATOM   1160 O  O   . PHE   A 1 150 ? 44.25400 41.56900 16.66200 1.000 48.37745  ? 147 PHE   A O   1 
ATOM   1161 C  CB  . PHE   A 1 150 ? 43.31900 40.31900 19.57200 1.000 43.61926  ? 147 PHE   A CB  1 
ATOM   1162 C  CG  . PHE   A 1 150 ? 44.71100 39.75800 19.46700 1.000 45.66969  ? 147 PHE   A CG  1 
ATOM   1163 C  CD1 . PHE   A 1 150 ? 45.81200 40.52900 19.80900 1.000 46.24893  ? 147 PHE   A CD1 1 
ATOM   1164 C  CD2 . PHE   A 1 150 ? 44.91700 38.45800 19.03800 1.000 46.66324  ? 147 PHE   A CD2 1 
ATOM   1165 C  CE1 . PHE   A 1 150 ? 47.09400 40.01200 19.71700 1.000 39.49664  ? 147 PHE   A CE1 1 
ATOM   1166 C  CE2 . PHE   A 1 150 ? 46.19800 37.93400 18.94500 1.000 45.83807  ? 147 PHE   A CE2 1 
ATOM   1167 C  CZ  . PHE   A 1 150 ? 47.28700 38.71400 19.28200 1.000 45.01339  ? 147 PHE   A CZ  1 
ATOM   1168 N  N   . CYS   A 1 151 ? 42.12800 40.82500 16.67000 1.000 48.66129  ? 148 CYS   A N   1 
ATOM   1169 C  CA  . CYS   A 1 151 ? 42.15800 40.50600 15.24700 1.000 50.86744  ? 148 CYS   A CA  1 
ATOM   1170 C  C   . CYS   A 1 151 ? 42.26200 41.76700 14.39800 1.000 52.35283  ? 148 CYS   A C   1 
ATOM   1171 O  O   . CYS   A 1 151 ? 42.93800 41.77100 13.36400 1.000 48.24753  ? 148 CYS   A O   1 
ATOM   1172 C  CB  . CYS   A 1 151 ? 40.91800 39.69700 14.86600 1.000 46.47023  ? 148 CYS   A CB  1 
ATOM   1173 S  SG  . CYS   A 1 151 ? 40.90000 38.01100 15.53100 1.000 52.73651  ? 148 CYS   A SG  1 
ATOM   1174 N  N   . ALA   A 1 152 ? 41.60000 42.84700 14.81700 1.000 51.77678  ? 149 ALA   A N   1 
ATOM   1175 C  CA  . ALA   A 1 152 ? 41.73600 44.10800 14.09600 1.000 47.02084  ? 149 ALA   A CA  1 
ATOM   1176 C  C   . ALA   A 1 152 ? 43.15500 44.64900 14.20200 1.000 60.83401  ? 149 ALA   A C   1 
ATOM   1177 O  O   . ALA   A 1 152 ? 43.70300 45.16500 13.22100 1.000 52.66409  ? 149 ALA   A O   1 
ATOM   1178 C  CB  . ALA   A 1 152 ? 40.73200 45.13100 14.62300 1.000 43.49554  ? 149 ALA   A CB  1 
ATOM   1179 N  N   . LEU   A 1 153 ? 43.76900 44.53300 15.38300 1.000 50.15960  ? 150 LEU   A N   1 
ATOM   1180 C  CA  . LEU   A 1 153 ? 45.13500 45.01500 15.54800 1.000 51.13487  ? 150 LEU   A CA  1 
ATOM   1181 C  C   . LEU   A 1 153 ? 46.10200 44.23500 14.66600 1.000 54.73313  ? 150 LEU   A C   1 
ATOM   1182 O  O   . LEU   A 1 153 ? 47.00200 44.82100 14.05300 1.000 55.60542  ? 150 LEU   A O   1 
ATOM   1183 C  CB  . LEU   A 1 153 ? 45.54900 44.93200 17.01600 1.000 52.56129  ? 150 LEU   A CB  1 
ATOM   1184 C  CG  . LEU   A 1 153 ? 45.05700 46.07500 17.90800 1.000 54.56760  ? 150 LEU   A CG  1 
ATOM   1185 C  CD1 . LEU   A 1 153 ? 45.49800 45.85500 19.34600 1.000 55.78366  ? 150 LEU   A CD1 1 
ATOM   1186 C  CD2 . LEU   A 1 153 ? 45.55700 47.41500 17.39300 1.000 49.90993  ? 150 LEU   A CD2 1 
ATOM   1187 N  N   . ILE   A 1 154 ? 45.92200 42.91500 14.57700 1.000 51.52600  ? 151 ILE   A N   1 
ATOM   1188 C  CA  . ILE   A 1 154 ? 46.78000 42.10300 13.71600 1.000 59.06694  ? 151 ILE   A CA  1 
ATOM   1189 C  C   . ILE   A 1 154 ? 46.73600 42.61600 12.28000 1.000 58.25368  ? 151 ILE   A C   1 
ATOM   1190 O  O   . ILE   A 1 154 ? 47.77800 42.77300 11.62800 1.000 53.14264  ? 151 ILE   A O   1 
ATOM   1191 C  CB  . ILE   A 1 154 ? 46.37400 40.62000 13.80300 1.000 54.61871  ? 151 ILE   A CB  1 
ATOM   1192 C  CG1 . ILE   A 1 154 ? 46.74700 40.05000 15.17300 1.000 59.39016  ? 151 ILE   A CG1 1 
ATOM   1193 C  CG2 . ILE   A 1 154 ? 47.04500 39.81200 12.69800 1.000 45.25924  ? 151 ILE   A CG2 1 
ATOM   1194 C  CD1 . ILE   A 1 154 ? 46.08700 38.72800 15.48500 1.000 48.23168  ? 151 ILE   A CD1 1 
ATOM   1195 N  N   . LEU   A 1 155 ? 45.53400 42.90300 11.77100 1.000 48.46563  ? 152 LEU   A N   1 
ATOM   1196 C  CA  . LEU   A 1 155 ? 45.40600 43.38700 10.40000 1.000 55.61759  ? 152 LEU   A CA  1 
ATOM   1197 C  C   . LEU   A 1 155 ? 46.08900 44.73900 10.22500 1.000 51.20329  ? 152 LEU   A C   1 
ATOM   1198 O  O   . LEU   A 1 155 ? 46.81300 44.95600 9.24600  1.000 53.43484  ? 152 LEU   A O   1 
ATOM   1199 C  CB  . LEU   A 1 155 ? 43.92900 43.47000 10.01200 1.000 45.32048  ? 152 LEU   A CB  1 
ATOM   1200 C  CG  . LEU   A 1 155 ? 43.19700 42.13600 9.83000  1.000 52.02140  ? 152 LEU   A CG  1 
ATOM   1201 C  CD1 . LEU   A 1 155 ? 41.72000 42.27100 10.17100 1.000 43.41669  ? 152 LEU   A CD1 1 
ATOM   1202 C  CD2 . LEU   A 1 155 ? 43.37400 41.60900 8.41500  1.000 47.86790  ? 152 LEU   A CD2 1 
ATOM   1203 N  N   . ALA   A 1 156 ? 45.87800 45.65800 11.17100 1.000 49.65413  ? 153 ALA   A N   1 
ATOM   1204 C  CA  . ALA   A 1 156 ? 46.51100 46.97100 11.08800 1.000 50.34723  ? 153 ALA   A CA  1 
ATOM   1205 C  C   . ALA   A 1 156 ? 48.03100 46.86500 11.15100 1.000 58.53313  ? 153 ALA   A C   1 
ATOM   1206 O  O   . ALA   A 1 156 ? 48.73500 47.52100 10.37300 1.000 54.65498  ? 153 ALA   A O   1 
ATOM   1207 C  CB  . ALA   A 1 156 ? 45.98800 47.87700 12.20300 1.000 47.97972  ? 153 ALA   A CB  1 
ATOM   1208 N  N   . TYR   A 1 157 ? 48.55700 46.04300 12.06200 1.000 46.41431  ? 154 TYR   A N   1 
ATOM   1209 C  CA  . TYR   A 1 157 ? 50.00600 45.91300 12.17700 1.000 53.88825  ? 154 TYR   A CA  1 
ATOM   1210 C  C   . TYR   A 1 157 ? 50.61200 45.23000 10.95700 1.000 50.42942  ? 154 TYR   A C   1 
ATOM   1211 O  O   . TYR   A 1 157 ? 51.77100 45.49200 10.61500 1.000 61.23705  ? 154 TYR   A O   1 
ATOM   1212 C  CB  . TYR   A 1 157 ? 50.37100 45.14900 13.45200 1.000 50.93515  ? 154 TYR   A CB  1 
ATOM   1213 C  CG  . TYR   A 1 157 ? 50.36200 46.00800 14.69700 1.000 51.26000  ? 154 TYR   A CG  1 
ATOM   1214 C  CD1 . TYR   A 1 157 ? 51.30800 47.00700 14.88500 1.000 55.06128  ? 154 TYR   A CD1 1 
ATOM   1215 C  CD2 . TYR   A 1 157 ? 49.40100 45.82300 15.68200 1.000 47.67842  ? 154 TYR   A CD2 1 
ATOM   1216 C  CE1 . TYR   A 1 157 ? 51.29700 47.79700 16.02600 1.000 55.74859  ? 154 TYR   A CE1 1 
ATOM   1217 C  CE2 . TYR   A 1 157 ? 49.38000 46.60700 16.81700 1.000 54.56805  ? 154 TYR   A CE2 1 
ATOM   1218 C  CZ  . TYR   A 1 157 ? 50.32900 47.59000 16.98600 1.000 53.25957  ? 154 TYR   A CZ  1 
ATOM   1219 O  OH  . TYR   A 1 157 ? 50.30000 48.36600 18.12000 1.000 45.47311  ? 154 TYR   A OH  1 
ATOM   1220 N  N   . CYS   A 1 158 ? 49.85500 44.36100 10.29000 1.000 53.77784  ? 155 CYS   A N   1 
ATOM   1221 C  CA  . CYS   A 1 158 ? 50.32600 43.66200 9.10000  1.000 62.19947  ? 155 CYS   A CA  1 
ATOM   1222 C  C   . CYS   A 1 158 ? 50.00700 44.39900 7.80400  1.000 60.05796  ? 155 CYS   A C   1 
ATOM   1223 O  O   . CYS   A 1 158 ? 50.30300 43.87100 6.72600  1.000 58.14438  ? 155 CYS   A O   1 
ATOM   1224 C  CB  . CYS   A 1 158 ? 49.72200 42.25600 9.03400  1.000 55.87764  ? 155 CYS   A CB  1 
ATOM   1225 S  SG  . CYS   A 1 158 ? 50.28100 41.12500 10.31600 1.000 59.98553  ? 155 CYS   A SG  1 
ATOM   1226 N  N   A ASN   A 1 159 ? 49.42200 45.59700 7.88400  0.495 59.81717  ? 156 ASN   A N   1 
ATOM   1227 N  N   B ASN   A 1 159 ? 49.41100 45.59000 7.88500  0.505 59.62225  ? 156 ASN   A N   1 
ATOM   1228 C  CA  A ASN   A 1 159 ? 49.02200 46.36600 6.70300  0.495 62.96042  ? 156 ASN   A CA  1 
ATOM   1229 C  CA  B ASN   A 1 159 ? 49.03200 46.36600 6.70300  0.505 62.04584  ? 156 ASN   A CA  1 
ATOM   1230 C  C   A ASN   A 1 159 ? 48.12400 45.53900 5.78700  0.495 63.28099  ? 156 ASN   A C   1 
ATOM   1231 C  C   B ASN   A 1 159 ? 48.11100 45.56000 5.78800  0.505 63.12396  ? 156 ASN   A C   1 
ATOM   1232 O  O   A ASN   A 1 159 ? 48.25400 45.56100 4.56100  0.495 62.31313  ? 156 ASN   A O   1 
ATOM   1233 O  O   B ASN   A 1 159 ? 48.21400 45.61900 4.56100  0.505 63.23348  ? 156 ASN   A O   1 
ATOM   1234 C  CB  A ASN   A 1 159 ? 50.24100 46.89600 5.94400  0.495 58.17772  ? 156 ASN   A CB  1 
ATOM   1235 C  CB  B ASN   A 1 159 ? 50.26800 46.86100 5.94600  0.505 58.02262  ? 156 ASN   A CB  1 
ATOM   1236 C  CG  A ASN   A 1 159 ? 49.91700 48.11900 5.10300  0.495 66.82983  ? 156 ASN   A CG  1 
ATOM   1237 C  CG  B ASN   A 1 159 ? 51.21400 47.65800 6.83000  0.505 62.80546  ? 156 ASN   A CG  1 
ATOM   1238 O  OD1 A ASN   A 1 159 ? 49.09700 48.95400 5.48800  0.495 56.17194  ? 156 ASN   A OD1 1 
ATOM   1239 O  OD1 B ASN   A 1 159 ? 52.35500 47.25600 7.06000  0.505 67.13205  ? 156 ASN   A OD1 1 
ATOM   1240 N  ND2 A ASN   A 1 159 ? 50.56200 48.22900 3.94600  0.495 66.45443  ? 156 ASN   A ND2 1 
ATOM   1241 N  ND2 B ASN   A 1 159 ? 50.74200 48.79600 7.32500  0.505 59.21288  ? 156 ASN   A ND2 1 
ATOM   1242 N  N   . LYS   A 1 160 ? 47.20800 44.79300 6.39300  1.000 58.00898  ? 157 LYS   A N   1 
ATOM   1243 C  CA  . LYS   A 1 160 ? 46.23500 43.99400 5.66800  1.000 59.01542  ? 157 LYS   A CA  1 
ATOM   1244 C  C   . LYS   A 1 160 ? 44.83600 44.50100 5.98600  1.000 59.92803  ? 157 LYS   A C   1 
ATOM   1245 O  O   . LYS   A 1 160 ? 44.57500 44.99500 7.08700  1.000 56.39498  ? 157 LYS   A O   1 
ATOM   1246 C  CB  . LYS   A 1 160 ? 46.35200 42.50500 6.02700  1.000 49.86110  ? 157 LYS   A CB  1 
ATOM   1247 C  CG  . LYS   A 1 160 ? 47.69900 41.88700 5.68300  1.000 64.40711  ? 157 LYS   A CG  1 
ATOM   1248 C  CD  . LYS   A 1 160 ? 47.61300 41.06300 4.40900  1.000 67.89700  ? 157 LYS   A CD  1 
ATOM   1249 C  CE  . LYS   A 1 160 ? 48.96000 40.98000 3.70700  1.000 81.64957  ? 157 LYS   A CE  1 
ATOM   1250 N  NZ  . LYS   A 1 160 ? 49.31900 42.25300 3.01800  1.000 97.31951  ? 157 LYS   A NZ  1 
ATOM   1251 N  N   . THR   A 1 161 ? 43.94300 44.38900 5.01000  1.000 54.42805  ? 158 THR   A N   1 
ATOM   1252 C  CA  . THR   A 1 161 ? 42.55600 44.79400 5.17100  1.000 52.10750  ? 158 THR   A CA  1 
ATOM   1253 C  C   . THR   A 1 161 ? 41.66000 43.56500 5.21900  1.000 50.81916  ? 158 THR   A C   1 
ATOM   1254 O  O   . THR   A 1 161 ? 42.03700 42.47400 4.78200  1.000 57.85788  ? 158 THR   A O   1 
ATOM   1255 C  CB  . THR   A 1 161 ? 42.10400 45.71900 4.03200  1.000 60.23771  ? 158 THR   A CB  1 
ATOM   1256 O  OG1 . THR   A 1 161 ? 42.42700 45.12600 2.76800  1.000 62.40513  ? 158 THR   A OG1 1 
ATOM   1257 C  CG2 . THR   A 1 161 ? 42.79000 47.07400 4.14000  1.000 58.09871  ? 158 THR   A CG2 1 
ATOM   1258 N  N   . VAL   A 1 162 ? 40.45700 43.76200 5.76000  1.000 51.59155  ? 159 VAL   A N   1 
ATOM   1259 C  CA  . VAL   A 1 162 ? 39.48700 42.67800 5.83000  1.000 60.04201  ? 159 VAL   A CA  1 
ATOM   1260 C  C   . VAL   A 1 162 ? 39.15600 42.20800 4.42100  1.000 55.34085  ? 159 VAL   A C   1 
ATOM   1261 O  O   . VAL   A 1 162 ? 38.89300 43.01700 3.52300  1.000 56.33761  ? 159 VAL   A O   1 
ATOM   1262 C  CB  . VAL   A 1 162 ? 38.23400 43.14100 6.58800  1.000 53.27337  ? 159 VAL   A CB  1 
ATOM   1263 C  CG1 . VAL   A 1 162 ? 37.10100 42.13700 6.42200  1.000 57.60668  ? 159 VAL   A CG1 1 
ATOM   1264 C  CG2 . VAL   A 1 162 ? 38.55900 43.35300 8.05900  1.000 54.92376  ? 159 VAL   A CG2 1 
ATOM   1265 N  N   . GLY   A 1 163 ? 39.18000 40.89200 4.21900  1.000 51.41741  ? 160 GLY   A N   1 
ATOM   1266 C  CA  . GLY   A 1 163 ? 38.92500 40.29200 2.93200  1.000 46.73616  ? 160 GLY   A CA  1 
ATOM   1267 C  C   . GLY   A 1 163 ? 40.17000 39.96200 2.13700  1.000 53.36438  ? 160 GLY   A C   1 
ATOM   1268 O  O   . GLY   A 1 163 ? 40.11600 39.09400 1.25700  1.000 58.00368  ? 160 GLY   A O   1 
ATOM   1269 N  N   . GLU   A 1 164 ? 41.28400 40.63100 2.42100  1.000 49.10965  ? 161 GLU   A N   1 
ATOM   1270 C  CA  . GLU   A 1 164 ? 42.53700 40.34400 1.74000  1.000 51.75107  ? 161 GLU   A CA  1 
ATOM   1271 C  C   . GLU   A 1 164 ? 43.00200 38.92000 2.03900  1.000 64.82295  ? 161 GLU   A C   1 
ATOM   1272 O  O   . GLU   A 1 164 ? 42.78300 38.38400 3.13000  1.000 56.77960  ? 161 GLU   A O   1 
ATOM   1273 C  CB  . GLU   A 1 164 ? 43.61000 41.34600 2.16900  1.000 51.88603  ? 161 GLU   A CB  1 
ATOM   1274 C  CG  . GLU   A 1 164 ? 44.74600 41.52100 1.18100  1.000 75.84073  ? 161 GLU   A CG  1 
ATOM   1275 C  CD  . GLU   A 1 164 ? 45.63200 42.70100 1.52700  1.000 88.23197  ? 161 GLU   A CD  1 
ATOM   1276 O  OE1 . GLU   A 1 164 ? 45.22600 43.51500 2.38400  1.000 75.96612  ? 161 GLU   A OE1 1 
ATOM   1277 O  OE2 . GLU   A 1 164 ? 46.73000 42.81700 0.94200  1.000 96.26804  ? 161 GLU   A OE2 1 
ATOM   1278 N  N   . LEU   A 1 165 ? 43.64800 38.30800 1.04800  1.000 64.15854  ? 162 LEU   A N   1 
ATOM   1279 C  CA  . LEU   A 1 165 ? 44.18900 36.96100 1.19100  1.000 69.76362  ? 162 LEU   A CA  1 
ATOM   1280 C  C   . LEU   A 1 165 ? 45.48300 37.02000 1.99600  1.000 57.12504  ? 162 LEU   A C   1 
ATOM   1281 O  O   . LEU   A 1 165 ? 46.41800 37.73800 1.62500  1.000 55.61734  ? 162 LEU   A O   1 
ATOM   1282 C  CB  . LEU   A 1 165 ? 44.42900 36.33800 -0.18400 1.000 68.21182  ? 162 LEU   A CB  1 
ATOM   1283 C  CG  . LEU   A 1 165 ? 43.27800 36.42000 -1.19300 1.000 59.61337  ? 162 LEU   A CG  1 
ATOM   1284 C  CD1 . LEU   A 1 165 ? 43.66800 35.77600 -2.51600 1.000 69.77133  ? 162 LEU   A CD1 1 
ATOM   1285 C  CD2 . LEU   A 1 165 ? 42.01100 35.77700 -0.63700 1.000 59.15778  ? 162 LEU   A CD2 1 
ATOM   1286 N  N   . GLY   A 1 166 ? 45.54200 36.26600 3.09000  1.000 60.14774  ? 163 GLY   A N   1 
ATOM   1287 C  CA  . GLY   A 1 166 ? 46.64700 36.35000 4.02600  1.000 47.27644  ? 163 GLY   A CA  1 
ATOM   1288 C  C   . GLY   A 1 166 ? 47.41100 35.04500 4.15000  1.000 57.05786  ? 163 GLY   A C   1 
ATOM   1289 O  O   . GLY   A 1 166 ? 46.83400 33.95800 4.07700  1.000 56.15061  ? 163 GLY   A O   1 
ATOM   1290 N  N   . ASP   A 1 167 ? 48.72200 35.16800 4.34200  1.000 51.26177  ? 164 ASP   A N   1 
ATOM   1291 C  CA  . ASP   A 1 167 ? 49.61400 34.03600 4.55800  1.000 56.29665  ? 164 ASP   A CA  1 
ATOM   1292 C  C   . ASP   A 1 167 ? 49.96400 33.95100 6.04200  1.000 54.51715  ? 164 ASP   A C   1 
ATOM   1293 O  O   . ASP   A 1 167 ? 50.38800 34.94600 6.64200  1.000 48.28993  ? 164 ASP   A O   1 
ATOM   1294 C  CB  . ASP   A 1 167 ? 50.88000 34.18900 3.71100  1.000 47.99632  ? 164 ASP   A CB  1 
ATOM   1295 C  CG  . ASP   A 1 167 ? 51.85500 33.03400 3.88600  1.000 62.76315  ? 164 ASP   A CG  1 
ATOM   1296 O  OD1 . ASP   A 1 167 ? 52.54100 32.97700 4.93000  1.000 58.30921  ? 164 ASP   A OD1 1 
ATOM   1297 O  OD2 . ASP   A 1 167 ? 51.95100 32.19500 2.96600  1.000 58.65217  ? 164 ASP   A OD2 1 
ATOM   1298 N  N   . VAL   A 1 168 ? 49.79000 32.76100 6.62800  1.000 51.80505  ? 165 VAL   A N   1 
ATOM   1299 C  CA  . VAL   A 1 168 ? 49.98700 32.59400 8.06800  1.000 53.32981  ? 165 VAL   A CA  1 
ATOM   1300 C  C   . VAL   A 1 168 ? 51.44600 32.82300 8.45100  1.000 52.47247  ? 165 VAL   A C   1 
ATOM   1301 O  O   . VAL   A 1 168 ? 51.74200 33.50300 9.44100  1.000 45.48977  ? 165 VAL   A O   1 
ATOM   1302 C  CB  . VAL   A 1 168 ? 49.49700 31.20600 8.51900  1.000 53.52858  ? 165 VAL   A CB  1 
ATOM   1303 C  CG1 . VAL   A 1 168 ? 50.00400 30.88600 9.92400  1.000 52.17436  ? 165 VAL   A CG1 1 
ATOM   1304 C  CG2 . VAL   A 1 168 ? 47.97900 31.13600 8.47700  1.000 44.55131  ? 165 VAL   A CG2 1 
ATOM   1305 N  N   . ARG   A 1 169 ? 52.37900 32.25600 7.68200  1.000 56.17699  ? 166 ARG   A N   1 
ATOM   1306 C  CA  . ARG   A 1 169 ? 53.79600 32.42500 7.99000  1.000 48.38397  ? 166 ARG   A CA  1 
ATOM   1307 C  C   . ARG   A 1 169 ? 54.20000 33.89300 7.96700  1.000 51.90098  ? 166 ARG   A C   1 
ATOM   1308 O  O   . ARG   A 1 169 ? 55.01000 34.33600 8.79000  1.000 54.58828  ? 166 ARG   A O   1 
ATOM   1309 C  CB  . ARG   A 1 169 ? 54.64500 31.62200 7.00400  1.000 50.85911  ? 166 ARG   A CB  1 
ATOM   1310 C  CG  . ARG   A 1 169 ? 56.14700 31.77700 7.20400  1.000 52.42913  ? 166 ARG   A CG  1 
ATOM   1311 C  CD  . ARG   A 1 169 ? 56.92100 31.18300 6.04000  1.000 50.53955  ? 166 ARG   A CD  1 
ATOM   1312 N  NE  . ARG   A 1 169 ? 56.64400 31.88400 4.79200  1.000 70.88436  ? 166 ARG   A NE  1 
ATOM   1313 C  CZ  . ARG   A 1 169 ? 57.30900 32.95100 4.37200  1.000 70.18969  ? 166 ARG   A CZ  1 
ATOM   1314 N  NH1 . ARG   A 1 169 ? 58.32300 33.44800 5.06200  1.000 57.56753  ? 166 ARG   A NH1 1 
ATOM   1315 N  NH2 . ARG   A 1 169 ? 56.94900 33.53300 3.23200  1.000 78.48139  ? 166 ARG   A NH2 1 
ATOM   1316 N  N   . GLU   A 1 170 ? 53.64400 34.66600 7.03000  1.000 49.28897  ? 167 GLU   A N   1 
ATOM   1317 C  CA  . GLU   A 1 170 ? 53.98400 36.08200 6.94800  1.000 50.85491  ? 167 GLU   A CA  1 
ATOM   1318 C  C   . GLU   A 1 170 ? 53.32500 36.87800 8.06400  1.000 51.46668  ? 167 GLU   A C   1 
ATOM   1319 O  O   . GLU   A 1 170 ? 53.92100 37.83200 8.58000  1.000 47.86898  ? 167 GLU   A O   1 
ATOM   1320 C  CB  . GLU   A 1 170 ? 53.59600 36.63100 5.57300  1.000 47.93061  ? 167 GLU   A CB  1 
ATOM   1321 C  CG  . GLU   A 1 170 ? 54.16100 35.79900 4.43400  1.000 52.84373  ? 167 GLU   A CG  1 
ATOM   1322 C  CD  . GLU   A 1 170 ? 53.73700 36.27400 3.05500  1.000 72.97190  ? 167 GLU   A CD  1 
ATOM   1323 O  OE1 . GLU   A 1 170 ? 52.96900 37.25800 2.95100  1.000 54.44829  ? 167 GLU   A OE1 1 
ATOM   1324 O  OE2 . GLU   A 1 170 ? 54.18300 35.65000 2.06900  1.000 73.47941  ? 167 GLU   A OE2 1 
ATOM   1325 N  N   . THR   A 1 171 ? 52.11100 36.49400 8.46100  1.000 46.89165  ? 168 THR   A N   1 
ATOM   1326 C  CA  . THR   A 1 171 ? 51.46100 37.15400 9.58700  1.000 46.62308  ? 168 THR   A CA  1 
ATOM   1327 C  C   . THR   A 1 171 ? 52.20800 36.88700 10.88900 1.000 58.41893  ? 168 THR   A C   1 
ATOM   1328 O  O   . THR   A 1 171 ? 52.41900 37.80700 11.68900 1.000 50.05359  ? 168 THR   A O   1 
ATOM   1329 C  CB  . THR   A 1 171 ? 50.00900 36.69200 9.68900  1.000 53.35823  ? 168 THR   A CB  1 
ATOM   1330 O  OG1 . THR   A 1 171 ? 49.39700 36.76500 8.39500  1.000 51.09256  ? 168 THR   A OG1 1 
ATOM   1331 C  CG2 . THR   A 1 171 ? 49.23600 37.56700 10.66400 1.000 44.87059  ? 168 THR   A CG2 1 
ATOM   1332 N  N   . MET   A 1 172 ? 52.62800 35.63700 11.11600 1.000 49.81078  ? 169 MET   A N   1 
ATOM   1333 C  CA  . MET   A 1 172 ? 53.37600 35.32500 12.33000 1.000 56.81799  ? 169 MET   A CA  1 
ATOM   1334 C  C   . MET   A 1 172 ? 54.69200 36.08900 12.37300 1.000 58.75363  ? 169 MET   A C   1 
ATOM   1335 O  O   . MET   A 1 172 ? 55.10400 36.57500 13.43400 1.000 51.29863  ? 169 MET   A O   1 
ATOM   1336 C  CB  . MET   A 1 172 ? 53.63000 33.81900 12.42700 1.000 46.24187  ? 169 MET   A CB  1 
ATOM   1337 C  CG  . MET   A 1 172 ? 52.36300 32.97700 12.50400 1.000 45.27789  ? 169 MET   A CG  1 
ATOM   1338 S  SD  . MET   A 1 172 ? 51.36100 33.30100 13.97000 1.000 50.01113  ? 169 MET   A SD  1 
ATOM   1339 C  CE  . MET   A 1 172 ? 52.60100 33.25500 15.26300 1.000 51.15241  ? 169 MET   A CE  1 
ATOM   1340 N  N   . SER   A 1 173 ? 55.35900 36.21600 11.22200 1.000 58.27402  ? 170 SER   A N   1 
ATOM   1341 C  CA  . SER   A 1 173 ? 56.61900 36.94900 11.17200 1.000 60.44863  ? 170 SER   A CA  1 
ATOM   1342 C  C   . SER   A 1 173 ? 56.41500 38.42000 11.50800 1.000 61.51744  ? 170 SER   A C   1 
ATOM   1343 O  O   . SER   A 1 173 ? 57.21900 39.01500 12.23800 1.000 54.16983  ? 170 SER   A O   1 
ATOM   1344 C  CB  . SER   A 1 173 ? 57.25700 36.79700 9.79200  1.000 52.46794  ? 170 SER   A CB  1 
ATOM   1345 O  OG  . SER   A 1 173 ? 58.36200 37.67200 9.65300  1.000 50.97688  ? 170 SER   A OG  1 
ATOM   1346 N  N   . TYR   A 1 174 ? 55.34700 39.02700 10.98300 1.000 54.22505  ? 171 TYR   A N   1 
ATOM   1347 C  CA  . TYR   A 1 174 ? 55.04000 40.41200 11.32600 1.000 60.65906  ? 171 TYR   A CA  1 
ATOM   1348 C  C   . TYR   A 1 174 ? 54.78300 40.56200 12.81900 1.000 56.21779  ? 171 TYR   A C   1 
ATOM   1349 O  O   . TYR   A 1 174 ? 55.26500 41.51000 13.44900 1.000 59.98189  ? 171 TYR   A O   1 
ATOM   1350 C  CB  . TYR   A 1 174 ? 53.83000 40.89500 10.53000 1.000 66.48876  ? 171 TYR   A CB  1 
ATOM   1351 C  CG  . TYR   A 1 174 ? 54.16900 41.79700 9.36700  1.000 72.63591  ? 171 TYR   A CG  1 
ATOM   1352 C  CD1 . TYR   A 1 174 ? 54.68400 43.07000 9.57500  1.000 82.25161  ? 171 TYR   A CD1 1 
ATOM   1353 C  CD2 . TYR   A 1 174 ? 53.96900 41.37500 8.05800  1.000 80.17094  ? 171 TYR   A CD2 1 
ATOM   1354 C  CE1 . TYR   A 1 174 ? 54.99400 43.89700 8.50900  1.000 102.69486 ? 171 TYR   A CE1 1 
ATOM   1355 C  CE2 . TYR   A 1 174 ? 54.27500 42.19300 6.98800  1.000 88.82411  ? 171 TYR   A CE2 1 
ATOM   1356 C  CZ  . TYR   A 1 174 ? 54.78700 43.45200 7.21800  1.000 97.92654  ? 171 TYR   A CZ  1 
ATOM   1357 O  OH  . TYR   A 1 174 ? 55.09200 44.26700 6.15300  1.000 106.80053 ? 171 TYR   A OH  1 
ATOM   1358 N  N   . LEU   A 1 175 ? 54.02400 39.63300 13.40400 1.000 55.54854  ? 172 LEU   A N   1 
ATOM   1359 C  CA  . LEU   A 1 175 ? 53.75300 39.70000 14.83400 1.000 57.21934  ? 172 LEU   A CA  1 
ATOM   1360 C  C   . LEU   A 1 175 ? 55.01700 39.44900 15.64800 1.000 56.90691  ? 172 LEU   A C   1 
ATOM   1361 O  O   . LEU   A 1 175 ? 55.22600 40.08500 16.68800 1.000 50.60986  ? 172 LEU   A O   1 
ATOM   1362 C  CB  . LEU   A 1 175 ? 52.65500 38.70300 15.20500 1.000 51.96871  ? 172 LEU   A CB  1 
ATOM   1363 C  CG  . LEU   A 1 175 ? 51.28100 38.97400 14.58300 1.000 58.26742  ? 172 LEU   A CG  1 
ATOM   1364 C  CD1 . LEU   A 1 175 ? 50.32500 37.81600 14.83700 1.000 47.40624  ? 172 LEU   A CD1 1 
ATOM   1365 C  CD2 . LEU   A 1 175 ? 50.69600 40.27700 15.11300 1.000 50.86456  ? 172 LEU   A CD2 1 
ATOM   1366 N  N   . PHE   A 1 176 ? 55.87700 38.53500 15.18600 1.000 55.28720  ? 173 PHE   A N   1 
ATOM   1367 C  CA  . PHE   A 1 176 ? 57.11800 38.25800 15.90300 1.000 48.94395  ? 173 PHE   A CA  1 
ATOM   1368 C  C   . PHE   A 1 176 ? 57.98700 39.50600 15.99800 1.000 57.60317  ? 173 PHE   A C   1 
ATOM   1369 O  O   . PHE   A 1 176 ? 58.64900 39.73700 17.01700 1.000 58.67486  ? 173 PHE   A O   1 
ATOM   1370 C  CB  . PHE   A 1 176 ? 57.88800 37.12700 15.21600 1.000 54.04618  ? 173 PHE   A CB  1 
ATOM   1371 C  CG  . PHE   A 1 176 ? 57.27000 35.76600 15.39600 1.000 50.33421  ? 173 PHE   A CG  1 
ATOM   1372 C  CD1 . PHE   A 1 176 ? 56.35000 35.53100 16.40500 1.000 51.61370  ? 173 PHE   A CD1 1 
ATOM   1373 C  CD2 . PHE   A 1 176 ? 57.60800 34.72200 14.54800 1.000 53.63251  ? 173 PHE   A CD2 1 
ATOM   1374 C  CE1 . PHE   A 1 176 ? 55.78000 34.27800 16.56600 1.000 45.19724  ? 173 PHE   A CE1 1 
ATOM   1375 C  CE2 . PHE   A 1 176 ? 57.04200 33.46800 14.70500 1.000 48.99692  ? 173 PHE   A CE2 1 
ATOM   1376 C  CZ  . PHE   A 1 176 ? 56.12900 33.24600 15.71700 1.000 48.89771  ? 173 PHE   A CZ  1 
ATOM   1377 N  N   . GLN   A 1 177 ? 57.99200 40.32700 14.94400 1.000 59.58806  ? 174 GLN   A N   1 
ATOM   1378 C  CA  . GLN   A 1 177 ? 58.79500 41.54400 14.95100 1.000 61.87345  ? 174 GLN   A CA  1 
ATOM   1379 C  C   . GLN   A 1 177 ? 58.30800 42.55200 15.98400 1.000 57.00557  ? 174 GLN   A C   1 
ATOM   1380 O  O   . GLN   A 1 177 ? 59.07900 43.43100 16.38500 1.000 58.10814  ? 174 GLN   A O   1 
ATOM   1381 C  CB  . GLN   A 1 177 ? 58.80400 42.17300 13.55500 1.000 62.11693  ? 174 GLN   A CB  1 
ATOM   1382 C  CG  . GLN   A 1 177 ? 59.85200 41.58300 12.61700 1.000 57.11890  ? 174 GLN   A CG  1 
ATOM   1383 C  CD  . GLN   A 1 177 ? 59.54400 41.83200 11.14800 1.000 79.44939  ? 174 GLN   A CD  1 
ATOM   1384 O  OE1 . GLN   A 1 177 ? 58.85200 41.04400 10.50000 1.000 81.02769  ? 174 GLN   A OE1 1 
ATOM   1385 N  NE2 . GLN   A 1 177 ? 60.05400 42.93700 10.61900 1.000 91.21408  ? 174 GLN   A NE2 1 
ATOM   1386 N  N   . HIS   A 1 178 ? 57.05600 42.44000 16.42800 1.000 52.53624  ? 175 HIS   A N   1 
ATOM   1387 C  CA  . HIS   A 1 178 ? 56.50600 43.29400 17.47200 1.000 49.52822  ? 175 HIS   A CA  1 
ATOM   1388 C  C   . HIS   A 1 178 ? 56.48200 42.60300 18.83000 1.000 59.81746  ? 175 HIS   A C   1 
ATOM   1389 O  O   . HIS   A 1 178 ? 55.72800 43.01700 19.71800 1.000 59.71159  ? 175 HIS   A O   1 
ATOM   1390 C  CB  . HIS   A 1 178 ? 55.09900 43.75600 17.09000 1.000 54.07309  ? 175 HIS   A CB  1 
ATOM   1391 C  CG  . HIS   A 1 178 ? 55.05900 44.62400 15.87200 1.000 75.45021  ? 175 HIS   A CG  1 
ATOM   1392 N  ND1 . HIS   A 1 178 ? 55.28100 44.13600 14.60200 1.000 63.91590  ? 175 HIS   A ND1 1 
ATOM   1393 C  CD2 . HIS   A 1 178 ? 54.82200 45.94900 15.72900 1.000 56.76396  ? 175 HIS   A CD2 1 
ATOM   1394 C  CE1 . HIS   A 1 178 ? 55.18300 45.12300 13.73000 1.000 73.22264  ? 175 HIS   A CE1 1 
ATOM   1395 N  NE2 . HIS   A 1 178 ? 54.90600 46.23400 14.38800 1.000 87.52005  ? 175 HIS   A NE2 1 
ATOM   1396 N  N   . ALA   A 1 179 ? 57.28900 41.56000 19.00800 1.000 53.47000  ? 176 ALA   A N   1 
ATOM   1397 C  CA  . ALA   A 1 179 ? 57.36800 40.82500 20.26000 1.000 62.78462  ? 176 ALA   A CA  1 
ATOM   1398 C  C   . ALA   A 1 179 ? 58.80200 40.83200 20.77300 1.000 55.87269  ? 176 ALA   A C   1 
ATOM   1399 O  O   . ALA   A 1 179 ? 59.74700 41.12300 20.03500 1.000 63.98675  ? 176 ALA   A O   1 
ATOM   1400 C  CB  . ALA   A 1 179 ? 56.87400 39.38200 20.08900 1.000 59.23935  ? 176 ALA   A CB  1 
ATOM   1401 N  N   . ASN   A 1 180 ? 58.95600 40.50800 22.05600 1.000 61.40368  ? 177 ASN   A N   1 
ATOM   1402 C  CA  . ASN   A 1 180 ? 60.27000 40.47200 22.70000 1.000 62.59721  ? 177 ASN   A CA  1 
ATOM   1403 C  C   . ASN   A 1 180 ? 60.89600 39.10800 22.44600 1.000 62.19207  ? 177 ASN   A C   1 
ATOM   1404 O  O   . ASN   A 1 180 ? 60.64900 38.14100 23.16700 1.000 60.13964  ? 177 ASN   A O   1 
ATOM   1405 C  CB  . ASN   A 1 180 ? 60.15400 40.75800 24.19300 1.000 64.89877  ? 177 ASN   A CB  1 
ATOM   1406 C  CG  . ASN   A 1 180 ? 61.51100 40.90100 24.87200 1.000 70.05293  ? 177 ASN   A CG  1 
ATOM   1407 O  OD1 . ASN   A 1 180 ? 62.56100 40.76300 24.24100 1.000 65.19362  ? 177 ASN   A OD1 1 
ATOM   1408 N  ND2 . ASN   A 1 180 ? 61.49100 41.17900 26.17000 1.000 74.04954  ? 177 ASN   A ND2 1 
ATOM   1409 N  N   . LEU   A 1 181 ? 61.72100 39.03500 21.40200 1.000 58.62727  ? 178 LEU   A N   1 
ATOM   1410 C  CA  . LEU   A 1 181 ? 62.46600 37.82900 21.06400 1.000 59.85500  ? 178 LEU   A CA  1 
ATOM   1411 C  C   . LEU   A 1 181 ? 63.96900 38.08000 21.12400 1.000 68.86591  ? 178 LEU   A C   1 
ATOM   1412 O  O   . LEU   A 1 181 ? 64.74400 37.42500 20.42400 1.000 69.67290  ? 178 LEU   A O   1 
ATOM   1413 C  CB  . LEU   A 1 181 ? 62.05700 37.31000 19.68600 1.000 61.75210  ? 178 LEU   A CB  1 
ATOM   1414 C  CG  . LEU   A 1 181 ? 60.59200 36.90300 19.52500 1.000 61.28118  ? 178 LEU   A CG  1 
ATOM   1415 C  CD1 . LEU   A 1 181 ? 60.26900 36.60000 18.06900 1.000 61.17635  ? 178 LEU   A CD1 1 
ATOM   1416 C  CD2 . LEU   A 1 181 ? 60.27600 35.70600 20.40900 1.000 53.21352  ? 178 LEU   A CD2 1 
ATOM   1417 N  N   . ASP   A 1 182 ? 64.38700 39.03200 21.96200 1.000 71.77780  ? 179 ASP   A N   1 
ATOM   1418 C  CA  . ASP   A 1 182 ? 65.80300 39.37600 22.05500 1.000 73.73079  ? 179 ASP   A CA  1 
ATOM   1419 C  C   . ASP   A 1 182 ? 66.62000 38.21900 22.61400 1.000 78.06531  ? 179 ASP   A C   1 
ATOM   1420 O  O   . ASP   A 1 182 ? 67.74900 37.97800 22.17200 1.000 87.59823  ? 179 ASP   A O   1 
ATOM   1421 C  CB  . ASP   A 1 182 ? 65.98200 40.62300 22.92100 1.000 84.29386  ? 179 ASP   A CB  1 
ATOM   1422 C  CG  . ASP   A 1 182 ? 65.51200 41.88900 22.22800 1.000 92.56811  ? 179 ASP   A CG  1 
ATOM   1423 O  OD1 . ASP   A 1 182 ? 65.34400 41.86700 20.99100 1.000 76.12549  ? 179 ASP   A OD1 1 
ATOM   1424 O  OD2 . ASP   A 1 182 ? 65.30400 42.90500 22.92600 1.000 92.65414  ? 179 ASP   A OD2 1 
ATOM   1425 N  N   . SER   A 1 183 ? 66.06600 37.49000 23.58400 1.000 82.19247  ? 180 SER   A N   1 
ATOM   1426 C  CA  . SER   A 1 183 ? 66.77100 36.36100 24.17500 1.000 81.53311  ? 180 SER   A CA  1 
ATOM   1427 C  C   . SER   A 1 183 ? 66.87400 35.17000 23.23300 1.000 79.04437  ? 180 SER   A C   1 
ATOM   1428 O  O   . SER   A 1 183 ? 67.63800 34.24200 23.52000 1.000 85.51833  ? 180 SER   A O   1 
ATOM   1429 C  CB  . SER   A 1 183 ? 66.07600 35.93300 25.47000 1.000 75.81926  ? 180 SER   A CB  1 
ATOM   1430 O  OG  . SER   A 1 183 ? 66.08900 36.98300 26.42100 1.000 86.02134  ? 180 SER   A OG  1 
ATOM   1431 N  N   . CYS   A 1 184 ? 66.13500 35.17000 22.12700 1.000 69.90261  ? 181 CYS   A N   1 
ATOM   1432 C  CA  . CYS   A 1 184 ? 66.12500 34.03200 21.21800 1.000 74.21255  ? 181 CYS   A CA  1 
ATOM   1433 C  C   . CYS   A 1 184 ? 67.39000 34.03400 20.37200 1.000 80.67023  ? 181 CYS   A C   1 
ATOM   1434 O  O   . CYS   A 1 184 ? 67.63400 34.97400 19.60900 1.000 84.66395  ? 181 CYS   A O   1 
ATOM   1435 C  CB  . CYS   A 1 184 ? 64.87900 34.06600 20.33900 1.000 61.38885  ? 181 CYS   A CB  1 
ATOM   1436 S  SG  . CYS   A 1 184 ? 63.35600 33.90900 21.28900 1.000 64.72790  ? 181 CYS   A SG  1 
ATOM   1437 N  N   . LYS   A 1 185 ? 68.18700 32.97600 20.50300 1.000 82.56088  ? 182 LYS   A N   1 
ATOM   1438 C  CA  . LYS   A 1 185 ? 69.46200 32.85100 19.81400 1.000 76.23739  ? 182 LYS   A CA  1 
ATOM   1439 C  C   . LYS   A 1 185 ? 69.49300 31.54400 19.03800 1.000 71.73079  ? 182 LYS   A C   1 
ATOM   1440 O  O   . LYS   A 1 185 ? 69.00100 30.51700 19.51500 1.000 77.69995  ? 182 LYS   A O   1 
ATOM   1441 C  CB  . LYS   A 1 185 ? 70.63300 32.90900 20.81100 1.000 82.10545  ? 182 LYS   A CB  1 
ATOM   1442 C  CG  . LYS   A 1 185 ? 71.90100 32.20300 20.35100 1.000 95.59841  ? 182 LYS   A CG  1 
ATOM   1443 C  CD  . LYS   A 1 185 ? 72.83200 31.90600 21.51900 1.000 98.31189  ? 182 LYS   A CD  1 
ATOM   1444 C  CE  . LYS   A 1 185 ? 73.22800 33.17900 22.25300 1.000 107.78434 ? 182 LYS   A CE  1 
ATOM   1445 N  NZ  . LYS   A 1 185 ? 73.72400 32.89500 23.62900 1.000 122.84820 ? 182 LYS   A NZ  1 
ATOM   1446 N  N   . ARG   A 1 186 ? 70.06200 31.58900 17.83600 1.000 76.38458  ? 183 ARG   A N   1 
ATOM   1447 C  CA  . ARG   A 1 186 ? 70.23700 30.39800 17.01300 1.000 76.66356  ? 183 ARG   A CA  1 
ATOM   1448 C  C   . ARG   A 1 186 ? 71.63300 30.42400 16.41400 1.000 81.43036  ? 183 ARG   A C   1 
ATOM   1449 O  O   . ARG   A 1 186 ? 71.99200 31.37800 15.71800 1.000 91.66934  ? 183 ARG   A O   1 
ATOM   1450 C  CB  . ARG   A 1 186 ? 69.18100 30.31900 15.90700 1.000 70.60953  ? 183 ARG   A CB  1 
ATOM   1451 C  CG  . ARG   A 1 186 ? 69.53300 29.34300 14.79500 1.000 67.84607  ? 183 ARG   A CG  1 
ATOM   1452 C  CD  . ARG   A 1 186 ? 68.38300 29.17900 13.81800 1.000 70.62117  ? 183 ARG   A CD  1 
ATOM   1453 N  NE  . ARG   A 1 186 ? 67.21100 28.58700 14.45100 1.000 71.11762  ? 183 ARG   A NE  1 
ATOM   1454 C  CZ  . ARG   A 1 186 ? 66.06200 28.35300 13.83200 1.000 68.70434  ? 183 ARG   A CZ  1 
ATOM   1455 N  NH1 . ARG   A 1 186 ? 65.89100 28.65300 12.55400 1.000 69.88360  ? 183 ARG   A NH1 1 
ATOM   1456 N  NH2 . ARG   A 1 186 ? 65.05900 27.80400 14.51100 1.000 69.76653  ? 183 ARG   A NH2 1 
ATOM   1457 N  N   . VAL   A 1 187 ? 72.41400 29.38400 16.68500 1.000 80.79917  ? 184 VAL   A N   1 
ATOM   1458 C  CA  . VAL   A 1 187 ? 73.76200 29.24300 16.14700 1.000 84.23313  ? 184 VAL   A CA  1 
ATOM   1459 C  C   . VAL   A 1 187 ? 73.72800 28.14100 15.09900 1.000 83.34223  ? 184 VAL   A C   1 
ATOM   1460 O  O   . VAL   A 1 187 ? 73.30300 27.01400 15.38500 1.000 84.83548  ? 184 VAL   A O   1 
ATOM   1461 C  CB  . VAL   A 1 187 ? 74.78600 28.93000 17.24700 1.000 80.17639  ? 184 VAL   A CB  1 
ATOM   1462 C  CG1 . VAL   A 1 187 ? 76.11700 28.54200 16.63100 1.000 80.17477  ? 184 VAL   A CG1 1 
ATOM   1463 C  CG2 . VAL   A 1 187 ? 74.95200 30.12700 18.17100 1.000 84.85332  ? 184 VAL   A CG2 1 
ATOM   1464 N  N   . LEU   A 1 188 ? 74.16600 28.46500 13.88900 1.000 83.76856  ? 185 LEU   A N   1 
ATOM   1465 C  CA  . LEU   A 1 188 ? 74.16900 27.53000 12.77500 1.000 85.54405  ? 185 LEU   A CA  1 
ATOM   1466 C  C   . LEU   A 1 188 ? 75.59800 27.21400 12.35800 1.000 89.42438  ? 185 LEU   A C   1 
ATOM   1467 O  O   . LEU   A 1 188 ? 76.55500 27.88400 12.75400 1.000 87.75161  ? 185 LEU   A O   1 
ATOM   1468 C  CB  . LEU   A 1 188 ? 73.38300 28.09600 11.58700 1.000 86.02485  ? 185 LEU   A CB  1 
ATOM   1469 C  CG  . LEU   A 1 188 ? 71.86200 28.12200 11.72300 1.000 91.51528  ? 185 LEU   A CG  1 
ATOM   1470 C  CD1 . LEU   A 1 188 ? 71.24700 28.94100 10.59800 1.000 88.24162  ? 185 LEU   A CD1 1 
ATOM   1471 C  CD2 . LEU   A 1 188 ? 71.29600 26.71000 11.74200 1.000 87.54990  ? 185 LEU   A CD2 1 
ATOM   1472 N  N   . ASN   A 1 189 ? 75.73000 26.17700 11.53600 1.000 96.60177  ? 186 ASN   A N   1 
ATOM   1473 C  CA  . ASN   A 1 189 ? 77.02500 25.78200 11.00200 1.000 105.31609 ? 186 ASN   A CA  1 
ATOM   1474 C  C   . ASN   A 1 189 ? 76.82600 25.23100 9.60000  1.000 108.19247 ? 186 ASN   A C   1 
ATOM   1475 O  O   . ASN   A 1 189 ? 76.00900 24.32800 9.39700  1.000 109.08377 ? 186 ASN   A O   1 
ATOM   1476 C  CB  . ASN   A 1 189 ? 77.70000 24.73600 11.89600 1.000 113.79947 ? 186 ASN   A CB  1 
ATOM   1477 C  CG  . ASN   A 1 189 ? 79.20700 24.70300 11.72000 1.000 116.06927 ? 186 ASN   A CG  1 
ATOM   1478 O  OD1 . ASN   A 1 189 ? 79.88800 25.71500 11.89200 1.000 111.20286 ? 186 ASN   A OD1 1 
ATOM   1479 N  ND2 . ASN   A 1 189 ? 79.73600 23.53500 11.37100 1.000 112.60048 ? 186 ASN   A ND2 1 
ATOM   1480 N  N   . VAL   A 1 190 ? 77.56300 25.78300 8.64000  1.000 112.63545 ? 187 VAL   A N   1 
ATOM   1481 C  CA  . VAL   A 1 190 ? 77.55700 25.29800 7.26700  1.000 112.70615 ? 187 VAL   A CA  1 
ATOM   1482 C  C   . VAL   A 1 190 ? 78.85000 24.53300 7.02300  1.000 108.83162 ? 187 VAL   A C   1 
ATOM   1483 O  O   . VAL   A 1 190 ? 79.90300 24.85200 7.58600  1.000 104.73311 ? 187 VAL   A O   1 
ATOM   1484 C  CB  . VAL   A 1 190 ? 77.37600 26.44400 6.24600  1.000 115.06397 ? 187 VAL   A CB  1 
ATOM   1485 C  CG1 . VAL   A 1 190 ? 76.29700 27.40700 6.72200  1.000 107.55048 ? 187 VAL   A CG1 1 
ATOM   1486 C  CG2 . VAL   A 1 190 ? 78.68700 27.18500 6.01200  1.000 117.94321 ? 187 VAL   A CG2 1 
ATOM   1487 N  N   . VAL   A 1 191 ? 78.76100 23.49600 6.19300  1.000 112.66850 ? 188 VAL   A N   1 
ATOM   1488 C  CA  . VAL   A 1 191 ? 79.89500 22.62900 5.89500  1.000 118.86284 ? 188 VAL   A CA  1 
ATOM   1489 C  C   . VAL   A 1 191 ? 80.00000 22.49700 4.38300  1.000 118.75747 ? 188 VAL   A C   1 
ATOM   1490 O  O   . VAL   A 1 191 ? 79.04200 22.07300 3.72500  1.000 119.12613 ? 188 VAL   A O   1 
ATOM   1491 C  CB  . VAL   A 1 191 ? 79.75600 21.24800 6.56100  1.000 119.26044 ? 188 VAL   A CB  1 
ATOM   1492 C  CG1 . VAL   A 1 191 ? 80.48900 20.17800 5.75900  1.000 123.45519 ? 188 VAL   A CG1 1 
ATOM   1493 C  CG2 . VAL   A 1 191 ? 80.27800 21.30000 7.98800  1.000 116.15116 ? 188 VAL   A CG2 1 
ATOM   1494 N  N   . CYS   A 1 192 ? 81.15500 22.86800 3.83500  1.000 117.74989 ? 189 CYS   A N   1 
ATOM   1495 C  CA  . CYS   A 1 192 ? 81.41800 22.78400 2.40700  1.000 123.33314 ? 189 CYS   A CA  1 
ATOM   1496 C  C   . CYS   A 1 192 ? 82.71000 22.01300 2.18400  1.000 120.15030 ? 189 CYS   A C   1 
ATOM   1497 O  O   . CYS   A 1 192 ? 83.67300 22.17000 2.94100  1.000 112.47471 ? 189 CYS   A O   1 
ATOM   1498 C  CB  . CYS   A 1 192 ? 81.51700 24.17700 1.77300  1.000 123.03154 ? 189 CYS   A CB  1 
ATOM   1499 S  SG  . CYS   A 1 192 ? 81.99100 24.17500 0.03000  1.000 129.33259 ? 189 CYS   A SG  1 
ATOM   1500 N  N   . LYS   A 1 193 ? 82.72400 21.18000 1.14000  1.000 123.87382 ? 190 LYS   A N   1 
ATOM   1501 C  CA  . LYS   A 1 193 ? 83.89400 20.35000 0.87100  1.000 123.34063 ? 190 LYS   A CA  1 
ATOM   1502 C  C   . LYS   A 1 193 ? 85.11800 21.18600 0.51500  1.000 129.54793 ? 190 LYS   A C   1 
ATOM   1503 O  O   . LYS   A 1 193 ? 86.24700 20.78800 0.82000  1.000 127.48984 ? 190 LYS   A O   1 
ATOM   1504 C  CB  . LYS   A 1 193 ? 83.58500 19.35900 -0.25100 1.000 110.07385 ? 190 LYS   A CB  1 
ATOM   1505 N  N   . THR   A 1 194 ? 84.91800 22.34200 -0.11900 1.000 126.32518 ? 191 THR   A N   1 
ATOM   1506 C  CA  . THR   A 1 194 ? 86.02000 23.20400 -0.53800 1.000 118.46733 ? 191 THR   A CA  1 
ATOM   1507 C  C   . THR   A 1 194 ? 86.28900 24.31800 0.47000  1.000 118.93895 ? 191 THR   A C   1 
ATOM   1508 O  O   . THR   A 1 194 ? 87.41500 24.46200 0.95600  1.000 114.10532 ? 191 THR   A O   1 
ATOM   1509 C  CB  . THR   A 1 194 ? 85.72600 23.80200 -1.92100 1.000 119.27875 ? 191 THR   A CB  1 
ATOM   1510 O  OG1 . THR   A 1 194 ? 85.57900 22.74800 -2.88000 1.000 117.92839 ? 191 THR   A OG1 1 
ATOM   1511 C  CG2 . THR   A 1 194 ? 86.85700 24.72500 -2.35700 1.000 115.55468 ? 191 THR   A CG2 1 
ATOM   1512 N  N   . CYS   A 1 195 ? 85.26600 25.11200 0.79300  1.000 122.60580 ? 192 CYS   A N   1 
ATOM   1513 C  CA  . CYS   A 1 195 ? 85.46900 26.26300 1.66700  1.000 118.85972 ? 192 CYS   A CA  1 
ATOM   1514 C  C   . CYS   A 1 195 ? 85.68400 25.83500 3.11400  1.000 120.34967 ? 192 CYS   A C   1 
ATOM   1515 O  O   . CYS   A 1 195 ? 86.49000 26.44000 3.83100  1.000 115.53337 ? 192 CYS   A O   1 
ATOM   1516 C  CB  . CYS   A 1 195 ? 84.28100 27.21700 1.55700  1.000 128.90758 ? 192 CYS   A CB  1 
ATOM   1517 S  SG  . CYS   A 1 195 ? 83.77500 27.57300 -0.14200 1.000 101.19505 ? 192 CYS   A SG  1 
ATOM   1518 N  N   . GLY   A 1 196 ? 84.97200 24.80500 3.56300  1.000 115.16584 ? 193 GLY   A N   1 
ATOM   1519 C  CA  . GLY   A 1 196 ? 85.15400 24.30800 4.91300  1.000 115.13979 ? 193 GLY   A CA  1 
ATOM   1520 C  C   . GLY   A 1 196 ? 83.93200 24.45600 5.79500  1.000 116.25719 ? 193 GLY   A C   1 
ATOM   1521 O  O   . GLY   A 1 196 ? 82.82000 24.10000 5.39400  1.000 109.48181 ? 193 GLY   A O   1 
ATOM   1522 N  N   . GLN   A 1 197 ? 84.12700 24.98500 7.00200  1.000 119.67907 ? 194 GLN   A N   1 
ATOM   1523 C  CA  . GLN   A 1 197 ? 83.06100 25.11500 7.98600  1.000 120.67594 ? 194 GLN   A CA  1 
ATOM   1524 C  C   . GLN   A 1 197 ? 82.98100 26.56000 8.45600  1.000 118.28586 ? 194 GLN   A C   1 
ATOM   1525 O  O   . GLN   A 1 197 ? 84.00700 27.17500 8.76300  1.000 106.03756 ? 194 GLN   A O   1 
ATOM   1526 C  CB  . GLN   A 1 197 ? 83.29400 24.17000 9.17300  1.000 113.94931 ? 194 GLN   A CB  1 
ATOM   1527 C  CG  . GLN   A 1 197 ? 82.97300 24.76300 10.53600 1.000 127.74564 ? 194 GLN   A CG  1 
ATOM   1528 C  CD  . GLN   A 1 197 ? 83.19900 23.77700 11.66600 1.000 128.72868 ? 194 GLN   A CD  1 
ATOM   1529 O  OE1 . GLN   A 1 197 ? 83.81300 22.72700 11.47600 1.000 121.04760 ? 194 GLN   A OE1 1 
ATOM   1530 N  NE2 . GLN   A 1 197 ? 82.70300 24.11300 12.85200 1.000 118.63328 ? 194 GLN   A NE2 1 
ATOM   1531 N  N   . GLN   A 1 198 ? 81.76200 27.09700 8.50500  1.000 121.83661 ? 195 GLN   A N   1 
ATOM   1532 C  CA  . GLN   A 1 198 ? 81.52800 28.46800 8.93500  1.000 125.27722 ? 195 GLN   A CA  1 
ATOM   1533 C  C   . GLN   A 1 198 ? 80.33600 28.50400 9.87900  1.000 114.39518 ? 195 GLN   A C   1 
ATOM   1534 O  O   . GLN   A 1 198 ? 79.33500 27.81800 9.65600  1.000 104.69012 ? 195 GLN   A O   1 
ATOM   1535 C  CB  . GLN   A 1 198 ? 81.28700 29.39800 7.73500  1.000 129.84361 ? 195 GLN   A CB  1 
ATOM   1536 C  CG  . GLN   A 1 198 ? 80.89200 30.81800 8.11400  1.000 132.30235 ? 195 GLN   A CG  1 
ATOM   1537 C  CD  . GLN   A 1 198 ? 82.09200 31.71200 8.36800  1.000 129.85907 ? 195 GLN   A CD  1 
ATOM   1538 O  OE1 . GLN   A 1 198 ? 83.23800 31.29100 8.21000  1.000 127.43361 ? 195 GLN   A OE1 1 
ATOM   1539 N  NE2 . GLN   A 1 198 ? 81.83300 32.95200 8.76900  1.000 124.66293 ? 195 GLN   A NE2 1 
ATOM   1540 N  N   . GLN   A 1 199 ? 80.45300 29.30800 10.93300 1.000 105.66283 ? 196 GLN   A N   1 
ATOM   1541 C  CA  . GLN   A 1 199 ? 79.44500 29.40100 11.97900 1.000 103.29798 ? 196 GLN   A CA  1 
ATOM   1542 C  C   . GLN   A 1 199 ? 78.77700 30.76900 11.94600 1.000 104.88650 ? 196 GLN   A C   1 
ATOM   1543 O  O   . GLN   A 1 199 ? 79.44700 31.79400 11.78500 1.000 110.94819 ? 196 GLN   A O   1 
ATOM   1544 C  CB  . GLN   A 1 199 ? 80.06900 29.16000 13.35700 1.000 102.02230 ? 196 GLN   A CB  1 
ATOM   1545 C  CG  . GLN   A 1 199 ? 79.06300 28.99400 14.48300 1.000 96.95021  ? 196 GLN   A CG  1 
ATOM   1546 C  CD  . GLN   A 1 199 ? 79.46700 27.91800 15.47400 1.000 102.60208 ? 196 GLN   A CD  1 
ATOM   1547 O  OE1 . GLN   A 1 199 ? 79.46900 26.72900 15.15200 1.000 100.17380 ? 196 GLN   A OE1 1 
ATOM   1548 N  NE2 . GLN   A 1 199 ? 79.81100 28.33100 16.68900 1.000 75.72614  ? 196 GLN   A NE2 1 
ATOM   1549 N  N   . THR   A 1 200 ? 77.45500 30.77800 12.10100 1.000 98.34979  ? 197 THR   A N   1 
ATOM   1550 C  CA  . THR   A 1 200 ? 76.67800 32.00700 12.14500 1.000 91.88371  ? 197 THR   A CA  1 
ATOM   1551 C  C   . THR   A 1 200 ? 75.75300 31.98000 13.35300 1.000 89.68673  ? 197 THR   A C   1 
ATOM   1552 O  O   . THR   A 1 200 ? 75.28400 30.91800 13.77300 1.000 91.83842  ? 197 THR   A O   1 
ATOM   1553 C  CB  . THR   A 1 200 ? 75.85200 32.20700 10.86500 1.000 93.01614  ? 197 THR   A CB  1 
ATOM   1554 O  OG1 . THR   A 1 200 ? 75.33500 30.94500 10.42400 1.000 96.45591  ? 197 THR   A OG1 1 
ATOM   1555 C  CG2 . THR   A 1 200 ? 76.71000 32.81500 9.76400  1.000 81.47428  ? 197 THR   A CG2 1 
ATOM   1556 N  N   . THR   A 1 201 ? 75.49500 33.16100 13.90800 1.000 83.58777  ? 198 THR   A N   1 
ATOM   1557 C  CA  . THR   A 1 201 ? 74.61700 33.31900 15.06100 1.000 85.73621  ? 198 THR   A CA  1 
ATOM   1558 C  C   . THR   A 1 201 ? 73.48500 34.26600 14.69200 1.000 89.61912  ? 198 THR   A C   1 
ATOM   1559 O  O   . THR   A 1 201 ? 73.72900 35.43000 14.35600 1.000 100.29797 ? 198 THR   A O   1 
ATOM   1560 C  CB  . THR   A 1 201 ? 75.38400 33.84800 16.27400 1.000 91.70035  ? 198 THR   A CB  1 
ATOM   1561 O  OG1 . THR   A 1 201 ? 76.50200 32.99300 16.54700 1.000 101.91227 ? 198 THR   A OG1 1 
ATOM   1562 C  CG2 . THR   A 1 201 ? 74.47900 33.90100 17.49600 1.000 76.89400  ? 198 THR   A CG2 1 
ATOM   1563 N  N   . LEU   A 1 202 ? 72.25400 33.76700 14.75400 1.000 86.96388  ? 199 LEU   A N   1 
ATOM   1564 C  CA  . LEU   A 1 202 ? 71.07000 34.56100 14.46400 1.000 76.06182  ? 199 LEU   A CA  1 
ATOM   1565 C  C   . LEU   A 1 202 ? 70.38700 34.98300 15.76000 1.000 83.30532  ? 199 LEU   A C   1 
ATOM   1566 O  O   . LEU   A 1 202 ? 70.47000 34.29600 16.78100 1.000 86.27948  ? 199 LEU   A O   1 
ATOM   1567 C  CB  . LEU   A 1 202 ? 70.08800 33.78200 13.58700 1.000 71.84995  ? 199 LEU   A CB  1 
ATOM   1568 C  CG  . LEU   A 1 202 ? 70.63900 33.27800 12.25200 1.000 79.60840  ? 199 LEU   A CG  1 
ATOM   1569 C  CD1 . LEU   A 1 202 ? 69.61100 32.42000 11.53000 1.000 70.24702  ? 199 LEU   A CD1 1 
ATOM   1570 C  CD2 . LEU   A 1 202 ? 71.07900 34.44400 11.38100 1.000 74.39629  ? 199 LEU   A CD2 1 
ATOM   1571 N  N   . LYS   A 1 203 ? 69.70900 36.12600 15.70400 1.000 83.54219  ? 200 LYS   A N   1 
ATOM   1572 C  CA  . LYS   A 1 203 ? 69.05400 36.71100 16.86300 1.000 66.31188  ? 200 LYS   A CA  1 
ATOM   1573 C  C   . LYS   A 1 203 ? 67.64300 37.13900 16.48900 1.000 74.43750  ? 200 LYS   A C   1 
ATOM   1574 O  O   . LYS   A 1 203 ? 67.37000 37.50400 15.34200 1.000 83.23111  ? 200 LYS   A O   1 
ATOM   1575 C  CB  . LYS   A 1 203 ? 69.83700 37.92400 17.39400 1.000 62.39522  ? 200 LYS   A CB  1 
ATOM   1576 C  CG  . LYS   A 1 203 ? 70.82100 37.62400 18.51700 1.000 81.70821  ? 200 LYS   A CG  1 
ATOM   1577 C  CD  . LYS   A 1 203 ? 70.32100 36.51500 19.42100 1.000 99.33965  ? 200 LYS   A CD  1 
ATOM   1578 C  CE  . LYS   A 1 203 ? 70.61900 36.81300 20.88000 1.000 91.65119  ? 200 LYS   A CE  1 
ATOM   1579 N  NZ  . LYS   A 1 203 ? 69.78000 35.98800 21.79100 1.000 90.40657  ? 200 LYS   A NZ  1 
ATOM   1580 N  N   . GLY   A 1 204 ? 66.74500 37.08700 17.47100 1.000 72.61681  ? 201 GLY   A N   1 
ATOM   1581 C  CA  . GLY   A 1 204 ? 65.41200 37.63300 17.27100 1.000 62.96738  ? 201 GLY   A CA  1 
ATOM   1582 C  C   . GLY   A 1 204 ? 64.54400 36.75200 16.39100 1.000 69.77239  ? 201 GLY   A C   1 
ATOM   1583 O  O   . GLY   A 1 204 ? 64.52500 35.52300 16.51700 1.000 73.67350  ? 201 GLY   A O   1 
ATOM   1584 N  N   . VAL   A 1 205 ? 63.81300 37.40000 15.48000 1.000 64.05163  ? 202 VAL   A N   1 
ATOM   1585 C  CA  . VAL   A 1 205 ? 62.83400 36.69900 14.65100 1.000 58.65093  ? 202 VAL   A CA  1 
ATOM   1586 C  C   . VAL   A 1 205 ? 63.50900 35.63600 13.79400 1.000 61.93466  ? 202 VAL   A C   1 
ATOM   1587 O  O   . VAL   A 1 205 ? 62.94000 34.56600 13.54500 1.000 66.59177  ? 202 VAL   A O   1 
ATOM   1588 C  CB  . VAL   A 1 205 ? 62.05400 37.71000 13.79100 1.000 63.27963  ? 202 VAL   A CB  1 
ATOM   1589 C  CG1 . VAL   A 1 205 ? 61.06900 36.99500 12.87800 1.000 54.47538  ? 202 VAL   A CG1 1 
ATOM   1590 C  CG2 . VAL   A 1 205 ? 61.33500 38.71100 14.68300 1.000 71.23921  ? 202 VAL   A CG2 1 
ATOM   1591 N  N   . GLU   A 1 206 ? 64.73200 35.90900 13.33400 1.000 69.50956  ? 203 GLU   A N   1 
ATOM   1592 C  CA  . GLU   A 1 206 ? 65.44000 34.95400 12.49000 1.000 67.12510  ? 203 GLU   A CA  1 
ATOM   1593 C  C   . GLU   A 1 206 ? 65.83800 33.69200 13.24400 1.000 67.15978  ? 203 GLU   A C   1 
ATOM   1594 O  O   . GLU   A 1 206 ? 66.07200 32.65600 12.61200 1.000 69.10179  ? 203 GLU   A O   1 
ATOM   1595 C  CB  . GLU   A 1 206 ? 66.68400 35.60800 11.88700 1.000 81.49167  ? 203 GLU   A CB  1 
ATOM   1596 C  CG  . GLU   A 1 206 ? 66.43600 36.33400 10.57700 1.000 93.53931  ? 203 GLU   A CG  1 
ATOM   1597 C  CD  . GLU   A 1 206 ? 67.35600 37.52500 10.39200 1.000 116.86931 ? 203 GLU   A CD  1 
ATOM   1598 O  OE1 . GLU   A 1 206 ? 67.26600 38.47600 11.19800 1.000 123.81197 ? 203 GLU   A OE1 1 
ATOM   1599 O  OE2 . GLU   A 1 206 ? 68.17100 37.50900 9.44600  1.000 115.98172 ? 203 GLU   A OE2 1 
ATOM   1600 N  N   . ALA   A 1 207 ? 65.91900 33.75200 14.57300 1.000 65.31214  ? 204 ALA   A N   1 
ATOM   1601 C  CA  . ALA   A 1 207 ? 66.32100 32.59400 15.36000 1.000 76.66590  ? 204 ALA   A CA  1 
ATOM   1602 C  C   . ALA   A 1 207 ? 65.19200 31.59600 15.58000 1.000 73.25552  ? 204 ALA   A C   1 
ATOM   1603 O  O   . ALA   A 1 207 ? 65.46800 30.45700 15.97200 1.000 70.39614  ? 204 ALA   A O   1 
ATOM   1604 C  CB  . ALA   A 1 207 ? 66.87500 33.04500 16.71300 1.000 62.87419  ? 204 ALA   A CB  1 
ATOM   1605 N  N   . VAL   A 1 208 ? 63.93900 31.98000 15.33600 1.000 57.88770  ? 205 VAL   A N   1 
ATOM   1606 C  CA  . VAL   A 1 208 ? 62.79700 31.11700 15.60800 1.000 62.02851  ? 205 VAL   A CA  1 
ATOM   1607 C  C   . VAL   A 1 208 ? 62.06400 30.68300 14.35000 1.000 60.88214  ? 205 VAL   A C   1 
ATOM   1608 O  O   . VAL   A 1 208 ? 61.11700 29.89300 14.44300 1.000 63.94333  ? 205 VAL   A O   1 
ATOM   1609 C  CB  . VAL   A 1 208 ? 61.81300 31.78200 16.59400 1.000 63.56854  ? 205 VAL   A CB  1 
ATOM   1610 C  CG1 . VAL   A 1 208 ? 62.53200 32.16800 17.88000 1.000 53.26229  ? 205 VAL   A CG1 1 
ATOM   1611 C  CG2 . VAL   A 1 208 ? 61.15300 32.99600 15.95800 1.000 56.34507  ? 205 VAL   A CG2 1 
ATOM   1612 N  N   . MET   A 1 209 ? 62.47100 31.16200 13.17500 1.000 63.86402  ? 206 MET   A N   1 
ATOM   1613 C  CA  . MET   A 1 209 ? 61.80800 30.83300 11.92000 1.000 61.17427  ? 206 MET   A CA  1 
ATOM   1614 C  C   . MET   A 1 209 ? 62.80300 30.21600 10.94800 1.000 63.80395  ? 206 MET   A C   1 
ATOM   1615 O  O   . MET   A 1 209 ? 63.96600 30.62700 10.88900 1.000 67.24041  ? 206 MET   A O   1 
ATOM   1616 C  CB  . MET   A 1 209 ? 61.17800 32.07600 11.28000 1.000 62.98763  ? 206 MET   A CB  1 
ATOM   1617 C  CG  . MET   A 1 209 ? 60.13300 32.77400 12.13800 1.000 74.54083  ? 206 MET   A CG  1 
ATOM   1618 S  SD  . MET   A 1 209 ? 59.28800 34.10100 11.25000 1.000 63.64246  ? 206 MET   A SD  1 
ATOM   1619 C  CE  . MET   A 1 209 ? 58.30500 33.15000 10.09300 1.000 65.76448  ? 206 MET   A CE  1 
ATOM   1620 N  N   . TYR   A 1 210 ? 62.33800 29.23000 10.18300 1.000 56.76427  ? 207 TYR   A N   1 
ATOM   1621 C  CA  . TYR   A 1 210 ? 63.12200 28.65900 9.09900  1.000 64.92400  ? 207 TYR   A CA  1 
ATOM   1622 C  C   . TYR   A 1 210 ? 62.19600 28.30700 7.94500  1.000 69.30088  ? 207 TYR   A C   1 
ATOM   1623 O  O   . TYR   A 1 210 ? 61.05400 27.88700 8.14900  1.000 72.69300  ? 207 TYR   A O   1 
ATOM   1624 C  CB  . TYR   A 1 210 ? 63.90500 27.41300 9.53500  1.000 73.49664  ? 207 TYR   A CB  1 
ATOM   1625 C  CG  . TYR   A 1 210 ? 64.77800 26.85000 8.43400  1.000 70.36075  ? 207 TYR   A CG  1 
ATOM   1626 C  CD1 . TYR   A 1 210 ? 66.01100 27.41700 8.14200  1.000 69.67311  ? 207 TYR   A CD1 1 
ATOM   1627 C  CD2 . TYR   A 1 210 ? 64.35800 25.76600 7.67200  1.000 64.28547  ? 207 TYR   A CD2 1 
ATOM   1628 C  CE1 . TYR   A 1 210 ? 66.80700 26.91400 7.13000  1.000 74.86014  ? 207 TYR   A CE1 1 
ATOM   1629 C  CE2 . TYR   A 1 210 ? 65.14600 25.25600 6.66000  1.000 66.43714  ? 207 TYR   A CE2 1 
ATOM   1630 C  CZ  . TYR   A 1 210 ? 66.37100 25.83400 6.39300  1.000 79.84440  ? 207 TYR   A CZ  1 
ATOM   1631 O  OH  . TYR   A 1 210 ? 67.16300 25.33200 5.38500  1.000 90.18665  ? 207 TYR   A OH  1 
ATOM   1632 N  N   . MET   A 1 211 ? 62.70700 28.48000 6.72900  1.000 69.98913  ? 208 MET   A N   1 
ATOM   1633 C  CA  . MET   A 1 211 ? 61.97300 28.19500 5.50200  1.000 65.92014  ? 208 MET   A CA  1 
ATOM   1634 C  C   . MET   A 1 211 ? 62.73600 27.14300 4.71100  1.000 67.83177  ? 208 MET   A C   1 
ATOM   1635 O  O   . MET   A 1 211 ? 63.91900 27.32800 4.40800  1.000 80.35981  ? 208 MET   A O   1 
ATOM   1636 C  CB  . MET   A 1 211 ? 61.79100 29.46700 4.67200  1.000 69.34474  ? 208 MET   A CB  1 
ATOM   1637 C  CG  . MET   A 1 211 ? 60.89900 29.30800 3.45300  1.000 63.07407  ? 208 MET   A CG  1 
ATOM   1638 S  SD  . MET   A 1 211 ? 59.16500 29.13800 3.90800  1.000 77.91649  ? 208 MET   A SD  1 
ATOM   1639 C  CE  . MET   A 1 211 ? 58.60100 27.98500 2.67600  1.000 70.07525  ? 208 MET   A CE  1 
ATOM   1640 N  N   . GLY   A 1 212 ? 62.06100 26.04400 4.37900  1.000 62.80447  ? 209 GLY   A N   1 
ATOM   1641 C  CA  . GLY   A 1 212 ? 62.69900 24.96700 3.64800  1.000 70.39919  ? 209 GLY   A CA  1 
ATOM   1642 C  C   . GLY   A 1 212 ? 62.19600 23.58200 4.00300  1.000 75.20100  ? 209 GLY   A C   1 
ATOM   1643 O  O   . GLY   A 1 212 ? 61.91300 22.77600 3.11300  1.000 71.86086  ? 209 GLY   A O   1 
ATOM   1644 N  N   . THR   A 1 213 ? 62.08600 23.28500 5.29700  1.000 72.24717  ? 210 THR   A N   1 
ATOM   1645 C  CA  . THR   A 1 213 ? 61.63400 21.97500 5.74400  1.000 69.59613  ? 210 THR   A CA  1 
ATOM   1646 C  C   . THR   A 1 213 ? 60.66000 22.12900 6.90300  1.000 70.19729  ? 210 THR   A C   1 
ATOM   1647 O  O   . THR   A 1 213 ? 60.71900 23.09800 7.66400  1.000 59.09491  ? 210 THR   A O   1 
ATOM   1648 C  CB  . THR   A 1 213 ? 62.80600 21.07500 6.17100  1.000 78.52967  ? 210 THR   A CB  1 
ATOM   1649 O  OG1 . THR   A 1 213 ? 62.29600 19.86200 6.74100  1.000 70.37254  ? 210 THR   A OG1 1 
ATOM   1650 C  CG2 . THR   A 1 213 ? 63.69000 21.78100 7.19000  1.000 67.33922  ? 210 THR   A CG2 1 
ATOM   1651 N  N   . LEU   A 1 214 ? 59.76200 21.15400 7.02400  1.000 61.64557  ? 211 LEU   A N   1 
ATOM   1652 C  CA  . LEU   A 1 214 ? 58.78900 21.13000 8.10600  1.000 53.29718  ? 211 LEU   A CA  1 
ATOM   1653 C  C   . LEU   A 1 214 ? 59.29800 20.41700 9.34900  1.000 67.98579  ? 211 LEU   A C   1 
ATOM   1654 O  O   . LEU   A 1 214 ? 58.74900 20.62900 10.43600 1.000 68.58596  ? 211 LEU   A O   1 
ATOM   1655 C  CB  . LEU   A 1 214 ? 57.50100 20.44300 7.64600  1.000 57.77737  ? 211 LEU   A CB  1 
ATOM   1656 C  CG  . LEU   A 1 214 ? 56.67800 21.09600 6.54000  1.000 57.07044  ? 211 LEU   A CG  1 
ATOM   1657 C  CD1 . LEU   A 1 214 ? 55.46400 20.23200 6.24700  1.000 54.17723  ? 211 LEU   A CD1 1 
ATOM   1658 C  CD2 . LEU   A 1 214 ? 56.26400 22.50700 6.92800  1.000 58.52109  ? 211 LEU   A CD2 1 
ATOM   1659 N  N   . SER   A 1 215 ? 60.32300 19.58000 9.21600  1.000 66.90361  ? 212 SER   A N   1 
ATOM   1660 C  CA  . SER   A 1 215 ? 60.77400 18.72000 10.30100 1.000 70.85097  ? 212 SER   A CA  1 
ATOM   1661 C  C   . SER   A 1 215 ? 61.85700 19.42500 11.10800 1.000 68.74579  ? 212 SER   A C   1 
ATOM   1662 O  O   . SER   A 1 215 ? 62.91000 19.77900 10.56700 1.000 66.94087  ? 212 SER   A O   1 
ATOM   1663 C  CB  . SER   A 1 215 ? 61.29100 17.39200 9.74800  1.000 72.10361  ? 212 SER   A CB  1 
ATOM   1664 O  OG  . SER   A 1 215 ? 62.08000 16.70600 10.70500 1.000 84.23877  ? 212 SER   A OG  1 
ATOM   1665 N  N   . TYR   A 1 216 ? 61.59500 19.62800 12.40300 1.000 69.19671  ? 213 TYR   A N   1 
ATOM   1666 C  CA  . TYR   A 1 216 ? 62.62700 20.15000 13.29200 1.000 68.90532  ? 213 TYR   A CA  1 
ATOM   1667 C  C   . TYR   A 1 216 ? 63.78400 19.17100 13.43200 1.000 78.64800  ? 213 TYR   A C   1 
ATOM   1668 O  O   . TYR   A 1 216 ? 64.93300 19.59100 13.61600 1.000 74.15524  ? 213 TYR   A O   1 
ATOM   1669 C  CB  . TYR   A 1 216 ? 62.02800 20.46200 14.66400 1.000 72.70163  ? 213 TYR   A CB  1 
ATOM   1670 C  CG  . TYR   A 1 216 ? 62.89200 21.33100 15.55400 1.000 63.51862  ? 213 TYR   A CG  1 
ATOM   1671 C  CD1 . TYR   A 1 216 ? 63.77700 22.25800 15.01600 1.000 66.73734  ? 213 TYR   A CD1 1 
ATOM   1672 C  CD2 . TYR   A 1 216 ? 62.81300 21.23000 16.93800 1.000 67.79746  ? 213 TYR   A CD2 1 
ATOM   1673 C  CE1 . TYR   A 1 216 ? 64.56200 23.05700 15.83500 1.000 64.60489  ? 213 TYR   A CE1 1 
ATOM   1674 C  CE2 . TYR   A 1 216 ? 63.58900 22.02300 17.76200 1.000 56.18707  ? 213 TYR   A CE2 1 
ATOM   1675 C  CZ  . TYR   A 1 216 ? 64.46200 22.93300 17.20700 1.000 66.05386  ? 213 TYR   A CZ  1 
ATOM   1676 O  OH  . TYR   A 1 216 ? 65.23300 23.72000 18.03300 1.000 66.53520  ? 213 TYR   A OH  1 
ATOM   1677 N  N   . GLU   A 1 217 ? 63.50300 17.86800 13.34700 1.000 74.72283  ? 214 GLU   A N   1 
ATOM   1678 C  CA  . GLU   A 1 217 ? 64.56800 16.87400 13.40400 1.000 85.82261  ? 214 GLU   A CA  1 
ATOM   1679 C  C   . GLU   A 1 217 ? 65.48200 16.97900 12.19100 1.000 91.35677  ? 214 GLU   A C   1 
ATOM   1680 O  O   . GLU   A 1 217 ? 66.71000 16.90600 12.32300 1.000 91.64339  ? 214 GLU   A O   1 
ATOM   1681 C  CB  . GLU   A 1 217 ? 63.97200 15.46900 13.50600 1.000 78.83407  ? 214 GLU   A CB  1 
ATOM   1682 C  CG  . GLU   A 1 217 ? 63.64500 15.02900 14.92800 1.000 100.22479 ? 214 GLU   A CG  1 
ATOM   1683 C  CD  . GLU   A 1 217 ? 64.87200 14.88300 15.81300 1.000 101.76897 ? 214 GLU   A CD  1 
ATOM   1684 O  OE1 . GLU   A 1 217 ? 66.00300 14.80000 15.28300 1.000 107.47138 ? 214 GLU   A OE1 1 
ATOM   1685 O  OE2 . GLU   A 1 217 ? 64.70200 14.86300 17.04900 1.000 95.70455  ? 214 GLU   A OE2 1 
ATOM   1686 N  N   . GLN   A 1 218 ? 64.90100 17.14800 11.00000 1.000 83.00505  ? 215 GLN   A N   1 
ATOM   1687 C  CA  . GLN   A 1 218 ? 65.70900 17.29900 9.79500  1.000 81.97670  ? 215 GLN   A CA  1 
ATOM   1688 C  C   . GLN   A 1 218 ? 66.60100 18.53000 9.88300  1.000 83.56481  ? 215 GLN   A C   1 
ATOM   1689 O  O   . GLN   A 1 218 ? 67.75000 18.50900 9.42800  1.000 88.58160  ? 215 GLN   A O   1 
ATOM   1690 C  CB  . GLN   A 1 218 ? 64.80500 17.37400 8.56400  1.000 82.26778  ? 215 GLN   A CB  1 
ATOM   1691 C  CG  . GLN   A 1 218 ? 65.50300 17.04900 7.25300  1.000 97.69500  ? 215 GLN   A CG  1 
ATOM   1692 C  CD  . GLN   A 1 218 ? 66.50200 15.91600 7.38500  1.000 104.20304 ? 215 GLN   A CD  1 
ATOM   1693 O  OE1 . GLN   A 1 218 ? 66.12500 14.74700 7.46800  1.000 104.44294 ? 215 GLN   A OE1 1 
ATOM   1694 N  NE2 . GLN   A 1 218 ? 67.78600 16.25700 7.40200  1.000 105.19603 ? 215 GLN   A NE2 1 
ATOM   1695 N  N   . PHE   A 1 219 ? 66.08900 19.61300 10.47100 1.000 81.04856  ? 216 PHE   A N   1 
ATOM   1696 C  CA  . PHE   A 1 219 ? 66.91000 20.80300 10.66900 1.000 82.59668  ? 216 PHE   A CA  1 
ATOM   1697 C  C   . PHE   A 1 219 ? 68.08400 20.50900 11.59500 1.000 87.47219  ? 216 PHE   A C   1 
ATOM   1698 O  O   . PHE   A 1 219 ? 69.18400 21.04200 11.40600 1.000 91.64298  ? 216 PHE   A O   1 
ATOM   1699 C  CB  . PHE   A 1 219 ? 66.05000 21.94000 11.22400 1.000 79.61476  ? 216 PHE   A CB  1 
ATOM   1700 C  CG  . PHE   A 1 219 ? 66.69600 23.29300 11.13100 1.000 78.73513  ? 216 PHE   A CG  1 
ATOM   1701 C  CD1 . PHE   A 1 219 ? 67.31400 23.70200 9.96100  1.000 83.64967  ? 216 PHE   A CD1 1 
ATOM   1702 C  CD2 . PHE   A 1 219 ? 66.68100 24.15600 12.21300 1.000 76.24942  ? 216 PHE   A CD2 1 
ATOM   1703 C  CE1 . PHE   A 1 219 ? 67.90800 24.94700 9.87300  1.000 78.56387  ? 216 PHE   A CE1 1 
ATOM   1704 C  CE2 . PHE   A 1 219 ? 67.27200 25.40200 12.13300 1.000 84.96255  ? 216 PHE   A CE2 1 
ATOM   1705 C  CZ  . PHE   A 1 219 ? 67.88600 25.79900 10.96100 1.000 87.76486  ? 216 PHE   A CZ  1 
ATOM   1706 N  N   . LYS   A 1 220 ? 67.87100 19.65400 12.59900 1.000 97.24984  ? 217 LYS   A N   1 
ATOM   1707 C  CA  . LYS   A 1 220 ? 68.95600 19.28900 13.50500 1.000 87.72554  ? 217 LYS   A CA  1 
ATOM   1708 C  C   . LYS   A 1 220 ? 69.97200 18.38800 12.81500 1.000 90.57426  ? 217 LYS   A C   1 
ATOM   1709 O  O   . LYS   A 1 220 ? 71.18000 18.51200 13.05000 1.000 90.79912  ? 217 LYS   A O   1 
ATOM   1710 C  CB  . LYS   A 1 220 ? 68.39200 18.60200 14.74900 1.000 88.40454  ? 217 LYS   A CB  1 
ATOM   1711 C  CG  . LYS   A 1 220 ? 67.63200 19.52600 15.68700 1.000 89.15919  ? 217 LYS   A CG  1 
ATOM   1712 C  CD  . LYS   A 1 220 ? 66.79900 18.73400 16.68200 1.000 73.16475  ? 217 LYS   A CD  1 
ATOM   1713 C  CE  . LYS   A 1 220 ? 66.22700 19.63600 17.76200 1.000 76.50161  ? 217 LYS   A CE  1 
ATOM   1714 N  NZ  . LYS   A 1 220 ? 65.42200 18.87500 18.75800 1.000 81.44983  ? 217 LYS   A NZ  1 
ATOM   1715 N  N   . LYS   A 1 221 ? 69.50200 17.47500 11.96300 1.000 90.52810  ? 218 LYS   A N   1 
ATOM   1716 C  CA  . LYS   A 1 221 ? 70.41500 16.58200 11.25700 1.000 98.25056  ? 218 LYS   A CA  1 
ATOM   1717 C  C   . LYS   A 1 221 ? 71.16600 17.30700 10.14600 1.000 99.22584  ? 218 LYS   A C   1 
ATOM   1718 O  O   . LYS   A 1 221 ? 72.32400 16.97800 9.86600  1.000 96.22173  ? 218 LYS   A O   1 
ATOM   1719 C  CB  . LYS   A 1 221 ? 69.64600 15.38800 10.69000 1.000 88.42533  ? 218 LYS   A CB  1 
ATOM   1720 C  CG  . LYS   A 1 221 ? 69.31000 14.31400 11.71800 1.000 96.54702  ? 218 LYS   A CG  1 
ATOM   1721 C  CD  . LYS   A 1 221 ? 70.39500 14.19200 12.78100 1.000 110.95642 ? 218 LYS   A CD  1 
ATOM   1722 C  CE  . LYS   A 1 221 ? 69.83600 13.64800 14.08700 1.000 114.93912 ? 218 LYS   A CE  1 
ATOM   1723 N  NZ  . LYS   A 1 221 ? 70.54000 14.21200 15.27500 1.000 106.54262 ? 218 LYS   A NZ  1 
ATOM   1724 N  N   . GLY   A 1 222 ? 70.53300 18.28800 9.50800  1.000 100.62996 ? 219 GLY   A N   1 
ATOM   1725 C  CA  . GLY   A 1 222 ? 71.18600 19.04300 8.45900  1.000 93.94140  ? 219 GLY   A CA  1 
ATOM   1726 C  C   . GLY   A 1 222 ? 70.39500 19.08500 7.16900  1.000 96.67199  ? 219 GLY   A C   1 
ATOM   1727 O  O   . GLY   A 1 222 ? 69.73100 18.10900 6.80600  1.000 94.52119  ? 219 GLY   A O   1 
ATOM   1728 N  N   . VAL   A 1 223 ? 70.45500 20.21500 6.46900  1.000 99.20022  ? 220 VAL   A N   1 
ATOM   1729 C  CA  . VAL   A 1 223 ? 69.76700 20.38500 5.19700  1.000 106.16922 ? 220 VAL   A CA  1 
ATOM   1730 C  C   . VAL   A 1 223 ? 70.77000 20.86500 4.16000  1.000 103.48400 ? 220 VAL   A C   1 
ATOM   1731 O  O   . VAL   A 1 223 ? 71.76700 21.51800 4.48600  1.000 97.53713  ? 220 VAL   A O   1 
ATOM   1732 C  CB  . VAL   A 1 223 ? 68.58100 21.37000 5.30300  1.000 99.41443  ? 220 VAL   A CB  1 
ATOM   1733 C  CG1 . VAL   A 1 223 ? 67.35400 20.66400 5.86100  1.000 91.13874  ? 220 VAL   A CG1 1 
ATOM   1734 C  CG2 . VAL   A 1 223 ? 68.95900 22.56700 6.16100  1.000 83.46365  ? 220 VAL   A CG2 1 
ATOM   1735 N  N   . GLN   A 1 224 ? 70.49700 20.53700 2.89900  1.000 104.87513 ? 221 GLN   A N   1 
ATOM   1736 C  CA  . GLN   A 1 224 ? 71.39300 20.86400 1.79700  1.000 110.02989 ? 221 GLN   A CA  1 
ATOM   1737 C  C   . GLN   A 1 224 ? 71.09400 22.27000 1.29100  1.000 105.44509 ? 221 GLN   A C   1 
ATOM   1738 O  O   . GLN   A 1 224 ? 70.00600 22.52600 0.76600  1.000 108.09837 ? 221 GLN   A O   1 
ATOM   1739 C  CB  . GLN   A 1 224 ? 71.24700 19.84600 0.66700  1.000 106.92033 ? 221 GLN   A CB  1 
ATOM   1740 C  CG  . GLN   A 1 224 ? 71.68400 18.44000 1.03500  1.000 106.49459 ? 221 GLN   A CG  1 
ATOM   1741 C  CD  . GLN   A 1 224 ? 72.91700 18.41800 1.91800  1.000 110.73500 ? 221 GLN   A CD  1 
ATOM   1742 O  OE1 . GLN   A 1 224 ? 74.01800 18.74800 1.47800  1.000 111.65512 ? 221 GLN   A OE1 1 
ATOM   1743 N  NE2 . GLN   A 1 224 ? 72.73900 18.02200 3.17300  1.000 112.43084 ? 221 GLN   A NE2 1 
ATOM   1744 N  N   . ILE   A 1 225 ? 72.05700 23.17400 1.45400  1.000 106.75413 ? 222 ILE   A N   1 
ATOM   1745 C  CA  . ILE   A 1 225 ? 71.93600 24.54700 0.96900  1.000 113.07254 ? 222 ILE   A CA  1 
ATOM   1746 C  C   . ILE   A 1 225 ? 73.10200 24.82300 0.02400  1.000 124.41924 ? 222 ILE   A C   1 
ATOM   1747 O  O   . ILE   A 1 225 ? 74.19700 24.27300 0.21200  1.000 125.31540 ? 222 ILE   A O   1 
ATOM   1748 C  CB  . ILE   A 1 225 ? 71.85600 25.55100 2.13900  1.000 111.55618 ? 222 ILE   A CB  1 
ATOM   1749 C  CG1 . ILE   A 1 225 ? 73.22000 25.81300 2.80400  1.000 111.97314 ? 222 ILE   A CG1 1 
ATOM   1750 C  CG2 . ILE   A 1 225 ? 70.84000 25.09100 3.17500  1.000 115.08612 ? 222 ILE   A CG2 1 
ATOM   1751 C  CD1 . ILE   A 1 225 ? 74.01500 26.97300 2.21700  1.000 117.36314 ? 222 ILE   A CD1 1 
ATOM   1752 N  N   . PRO   A 1 226 ? 72.91400 25.64000 -1.01100 1.000 124.26647 ? 223 PRO   A N   1 
ATOM   1753 C  CA  . PRO   A 1 226 ? 74.01600 25.91800 -1.93900 1.000 119.65874 ? 223 PRO   A CA  1 
ATOM   1754 C  C   . PRO   A 1 226 ? 75.01200 26.91000 -1.35700 1.000 120.89282 ? 223 PRO   A C   1 
ATOM   1755 O  O   . PRO   A 1 226 ? 74.64000 27.93900 -0.78700 1.000 123.97624 ? 223 PRO   A O   1 
ATOM   1756 C  CB  . PRO   A 1 226 ? 73.30300 26.50200 -3.16500 1.000 123.49509 ? 223 PRO   A CB  1 
ATOM   1757 C  CG  . PRO   A 1 226 ? 72.06600 27.12100 -2.60800 1.000 118.21116 ? 223 PRO   A CG  1 
ATOM   1758 C  CD  . PRO   A 1 226 ? 71.64600 26.24800 -1.45500 1.000 120.66304 ? 223 PRO   A CD  1 
ATOM   1759 N  N   . CYS   A 1 227 ? 76.29300 26.59100 -1.51700 1.000 125.66811 ? 224 CYS   A N   1 
ATOM   1760 C  CA  . CYS   A 1 227 ? 77.37100 27.43000 -1.01800 1.000 127.00868 ? 224 CYS   A CA  1 
ATOM   1761 C  C   . CYS   A 1 227 ? 77.72800 28.51200 -2.03600 1.000 134.47873 ? 224 CYS   A C   1 
ATOM   1762 O  O   . CYS   A 1 227 ? 77.32800 28.46900 -3.20200 1.000 133.58897 ? 224 CYS   A O   1 
ATOM   1763 C  CB  . CYS   A 1 227 ? 78.59600 26.57800 -0.68700 1.000 120.35589 ? 224 CYS   A CB  1 
ATOM   1764 S  SG  . CYS   A 1 227 ? 80.05300 27.51000 -0.16900 1.000 121.35998 ? 224 CYS   A SG  1 
ATOM   1765 N  N   . THR   A 1 228 ? 78.50500 29.49600 -1.57600 1.000 134.87111 ? 225 THR   A N   1 
ATOM   1766 C  CA  . THR   A 1 228 ? 78.91600 30.60300 -2.43200 1.000 138.86200 ? 225 THR   A CA  1 
ATOM   1767 C  C   . THR   A 1 228 ? 79.88500 30.17900 -3.52900 1.000 135.59324 ? 225 THR   A C   1 
ATOM   1768 O  O   . THR   A 1 228 ? 80.10900 30.95400 -4.46500 1.000 134.73026 ? 225 THR   A O   1 
ATOM   1769 C  CB  . THR   A 1 228 ? 79.54700 31.71400 -1.58700 1.000 131.29776 ? 225 THR   A CB  1 
ATOM   1770 O  OG1 . THR   A 1 228 ? 79.40000 32.97200 -2.25800 1.000 122.68512 ? 225 THR   A OG1 1 
ATOM   1771 C  CG2 . THR   A 1 228 ? 81.02600 31.43800 -1.35500 1.000 132.06146 ? 225 THR   A CG2 1 
ATOM   1772 N  N   . CYS   A 1 229 ? 80.45700 28.97900 -3.44200 1.000 136.52117 ? 226 CYS   A N   1 
ATOM   1773 C  CA  . CYS   A 1 229 ? 81.38900 28.48600 -4.44600 1.000 132.80561 ? 226 CYS   A CA  1 
ATOM   1774 C  C   . CYS   A 1 229 ? 80.72100 27.62900 -5.51200 1.000 131.80380 ? 226 CYS   A C   1 
ATOM   1775 O  O   . CYS   A 1 229 ? 81.38300 27.25400 -6.48700 1.000 133.75345 ? 226 CYS   A O   1 
ATOM   1776 C  CB  . CYS   A 1 229 ? 82.50700 27.68000 -3.77600 1.000 133.76834 ? 226 CYS   A CB  1 
ATOM   1777 S  SG  . CYS   A 1 229 ? 81.98300 26.05800 -3.17500 1.000 123.98944 ? 226 CYS   A SG  1 
ATOM   1778 N  N   . GLY   A 1 230 ? 79.44000 27.30900 -5.35500 1.000 128.94710 ? 227 GLY   A N   1 
ATOM   1779 C  CA  . GLY   A 1 230 ? 78.74100 26.49300 -6.32700 1.000 132.08667 ? 227 GLY   A CA  1 
ATOM   1780 C  C   . GLY   A 1 230 ? 78.40000 25.11000 -5.81200 1.000 144.11163 ? 227 GLY   A C   1 
ATOM   1781 O  O   . GLY   A 1 230 ? 77.30700 24.59600 -6.07300 1.000 140.79484 ? 227 GLY   A O   1 
ATOM   1782 N  N   . LYS   A 1 231 ? 79.32700 24.49700 -5.08100 1.000 140.64690 ? 228 LYS   A N   1 
ATOM   1783 C  CA  . LYS   A 1 231 ? 79.09300 23.16600 -4.53800 1.000 134.19253 ? 228 LYS   A CA  1 
ATOM   1784 C  C   . LYS   A 1 231 ? 78.05600 23.21900 -3.42300 1.000 142.11235 ? 228 LYS   A C   1 
ATOM   1785 O  O   . LYS   A 1 231 ? 78.00100 24.17800 -2.64800 1.000 135.84863 ? 228 LYS   A O   1 
ATOM   1786 C  CB  . LYS   A 1 231 ? 80.39800 22.56900 -4.01400 1.000 116.74931 ? 228 LYS   A CB  1 
ATOM   1787 N  N   . GLN   A 1 232 ? 77.22700 22.18100 -3.34600 1.000 142.40256 ? 229 GLN   A N   1 
ATOM   1788 C  CA  . GLN   A 1 232 ? 76.19500 22.12400 -2.32100 1.000 132.40679 ? 229 GLN   A CA  1 
ATOM   1789 C  C   . GLN   A 1 232 ? 76.81900 21.92900 -0.94400 1.000 133.38853 ? 229 GLN   A C   1 
ATOM   1790 O  O   . GLN   A 1 232 ? 77.77800 21.17100 -0.78000 1.000 139.42655 ? 229 GLN   A O   1 
ATOM   1791 C  CB  . GLN   A 1 232 ? 75.21000 20.99200 -2.61800 1.000 119.57118 ? 229 GLN   A CB  1 
ATOM   1792 C  CG  . GLN   A 1 232 ? 74.40700 21.18500 -3.89400 1.000 121.95585 ? 229 GLN   A CG  1 
ATOM   1793 C  CD  . GLN   A 1 232 ? 73.09600 21.91000 -3.65700 1.000 131.92544 ? 229 GLN   A CD  1 
ATOM   1794 O  OE1 . GLN   A 1 232 ? 73.07500 23.02200 -3.12900 1.000 131.10630 ? 229 GLN   A OE1 1 
ATOM   1795 N  NE2 . GLN   A 1 232 ? 71.99300 21.28200 -4.04900 1.000 130.70771 ? 229 GLN   A NE2 1 
ATOM   1796 N  N   . ALA   A 1 233 ? 76.26800 22.62100 0.04600  1.000 131.18617 ? 230 ALA   A N   1 
ATOM   1797 C  CA  . ALA   A 1 233 ? 76.75000 22.57100 1.41800  1.000 123.32112 ? 230 ALA   A CA  1 
ATOM   1798 C  C   . ALA   A 1 233 ? 75.69500 21.93200 2.31600  1.000 119.50176 ? 230 ALA   A C   1 
ATOM   1799 O  O   . ALA   A 1 233 ? 74.62800 21.50700 1.86400  1.000 113.92936 ? 230 ALA   A O   1 
ATOM   1800 C  CB  . ALA   A 1 233 ? 77.12000 23.97200 1.91100  1.000 112.21099 ? 230 ALA   A CB  1 
ATOM   1801 N  N   . THR   A 1 234 ? 76.00600 21.86700 3.60900  1.000 116.64531 ? 231 THR   A N   1 
ATOM   1802 C  CA  . THR   A 1 234 ? 75.11400 21.28900 4.60600  1.000 114.25043 ? 231 THR   A CA  1 
ATOM   1803 C  C   . THR   A 1 234 ? 75.00900 22.24800 5.78100  1.000 111.09577 ? 231 THR   A C   1 
ATOM   1804 O  O   . THR   A 1 234 ? 76.02800 22.62600 6.36900  1.000 104.22803 ? 231 THR   A O   1 
ATOM   1805 C  CB  . THR   A 1 234 ? 75.61400 19.91700 5.07000  1.000 111.73769 ? 231 THR   A CB  1 
ATOM   1806 O  OG1 . THR   A 1 234 ? 75.37400 18.94800 4.04200  1.000 106.53280 ? 231 THR   A OG1 1 
ATOM   1807 C  CG2 . THR   A 1 234 ? 74.89700 19.48500 6.34100  1.000 113.67387 ? 231 THR   A CG2 1 
ATOM   1808 N  N   . LYS   A 1 235 ? 73.78400 22.64300 6.11700  1.000 103.75128 ? 232 LYS   A N   1 
ATOM   1809 C  CA  . LYS   A 1 235 ? 73.51400 23.54400 7.22800  1.000 107.90066 ? 232 LYS   A CA  1 
ATOM   1810 C  C   . LYS   A 1 235 ? 72.70000 22.80400 8.27800  1.000 105.26552 ? 232 LYS   A C   1 
ATOM   1811 O  O   . LYS   A 1 235 ? 71.64600 22.24000 7.96500  1.000 107.27918 ? 232 LYS   A O   1 
ATOM   1812 C  CB  . LYS   A 1 235 ? 72.76500 24.79300 6.75100  1.000 106.57134 ? 232 LYS   A CB  1 
ATOM   1813 C  CG  . LYS   A 1 235 ? 72.21900 25.66400 7.87100  1.000 108.32589 ? 232 LYS   A CG  1 
ATOM   1814 C  CD  . LYS   A 1 235 ? 71.23600 26.69700 7.33800  1.000 106.75954 ? 232 LYS   A CD  1 
ATOM   1815 C  CE  . LYS   A 1 235 ? 71.94800 27.95400 6.86000  1.000 101.51182 ? 232 LYS   A CE  1 
ATOM   1816 N  NZ  . LYS   A 1 235 ? 71.02500 28.87100 6.13500  1.000 97.50454  ? 232 LYS   A NZ  1 
ATOM   1817 N  N   . TYR   A 1 236 ? 73.18800 22.80100 9.51700  1.000 96.29403  ? 233 TYR   A N   1 
ATOM   1818 C  CA  . TYR   A 1 236 ? 72.49400 22.15100 10.61800 1.000 103.52393 ? 233 TYR   A CA  1 
ATOM   1819 C  C   . TYR   A 1 236 ? 72.45300 23.07800 11.82500 1.000 99.50396  ? 233 TYR   A C   1 
ATOM   1820 O  O   . TYR   A 1 236 ? 73.20100 24.05500 11.91500 1.000 91.97009  ? 233 TYR   A O   1 
ATOM   1821 C  CB  . TYR   A 1 236 ? 73.14400 20.80100 10.98700 1.000 107.65336 ? 233 TYR   A CB  1 
ATOM   1822 C  CG  . TYR   A 1 236 ? 74.60900 20.85300 11.39300 1.000 121.97335 ? 233 TYR   A CG  1 
ATOM   1823 C  CD1 . TYR   A 1 236 ? 75.02700 21.54500 12.52400 1.000 124.23467 ? 233 TYR   A CD1 1 
ATOM   1824 C  CD2 . TYR   A 1 236 ? 75.57300 20.19400 10.64100 1.000 127.52936 ? 233 TYR   A CD2 1 
ATOM   1825 C  CE1 . TYR   A 1 236 ? 76.35600 21.58600 12.89100 1.000 125.66306 ? 233 TYR   A CE1 1 
ATOM   1826 C  CE2 . TYR   A 1 236 ? 76.90900 20.23000 11.00200 1.000 136.59855 ? 233 TYR   A CE2 1 
ATOM   1827 C  CZ  . TYR   A 1 236 ? 77.29400 20.92800 12.12700 1.000 135.23840 ? 233 TYR   A CZ  1 
ATOM   1828 O  OH  . TYR   A 1 236 ? 78.61900 20.97100 12.49500 1.000 128.97904 ? 233 TYR   A OH  1 
ATOM   1829 N  N   . LEU   A 1 237 ? 71.57100 22.74600 12.76400 1.000 91.38882  ? 234 LEU   A N   1 
ATOM   1830 C  CA  . LEU   A 1 237 ? 71.41400 23.53500 13.97700 1.000 86.86257  ? 234 LEU   A CA  1 
ATOM   1831 C  C   . LEU   A 1 237 ? 72.47400 23.15200 15.00000 1.000 89.71565  ? 234 LEU   A C   1 
ATOM   1832 O  O   . LEU   A 1 237 ? 72.64100 21.97200 15.32400 1.000 94.12437  ? 234 LEU   A O   1 
ATOM   1833 C  CB  . LEU   A 1 237 ? 70.01700 23.33200 14.56300 1.000 81.59866  ? 234 LEU   A CB  1 
ATOM   1834 C  CG  . LEU   A 1 237 ? 69.58500 24.26600 15.69700 1.000 88.33667  ? 234 LEU   A CG  1 
ATOM   1835 C  CD1 . LEU   A 1 237 ? 70.00800 25.70300 15.42600 1.000 77.30747  ? 234 LEU   A CD1 1 
ATOM   1836 C  CD2 . LEU   A 1 237 ? 68.08300 24.17300 15.92400 1.000 89.05952  ? 234 LEU   A CD2 1 
ATOM   1837 N  N   . VAL   A 1 238 ? 73.19100 24.15000 15.50800 1.000 87.87543  ? 235 VAL   A N   1 
ATOM   1838 C  CA  . VAL   A 1 238 ? 74.18600 23.91200 16.54800 1.000 80.20902  ? 235 VAL   A CA  1 
ATOM   1839 C  C   . VAL   A 1 238 ? 73.59900 24.15300 17.93100 1.000 89.74080  ? 235 VAL   A C   1 
ATOM   1840 O  O   . VAL   A 1 238 ? 73.65800 23.28400 18.80500 1.000 91.88308  ? 235 VAL   A O   1 
ATOM   1841 C  CB  . VAL   A 1 238 ? 75.43300 24.78900 16.30800 1.000 78.49211  ? 235 VAL   A CB  1 
ATOM   1842 C  CG1 . VAL   A 1 238 ? 76.24000 24.93600 17.59100 1.000 79.54297  ? 235 VAL   A CG1 1 
ATOM   1843 C  CG2 . VAL   A 1 238 ? 76.29200 24.18700 15.21100 1.000 92.17171  ? 235 VAL   A CG2 1 
ATOM   1844 N  N   . GLN   A 1 239 ? 73.01100 25.33100 18.14100 1.000 78.41497  ? 236 GLN   A N   1 
ATOM   1845 C  CA  . GLN   A 1 239 ? 72.42200 25.69700 19.42000 1.000 85.64539  ? 236 GLN   A CA  1 
ATOM   1846 C  C   . GLN   A 1 239 ? 71.14200 26.48100 19.17500 1.000 90.81442  ? 236 GLN   A C   1 
ATOM   1847 O  O   . GLN   A 1 239 ? 71.06700 27.28400 18.24100 1.000 88.45149  ? 236 GLN   A O   1 
ATOM   1848 C  CB  . GLN   A 1 239 ? 73.39200 26.52500 20.27000 1.000 76.52256  ? 236 GLN   A CB  1 
ATOM   1849 C  CG  . GLN   A 1 239 ? 73.06100 26.52900 21.75400 1.000 80.07327  ? 236 GLN   A CG  1 
ATOM   1850 C  CD  . GLN   A 1 239 ? 73.75000 27.65200 22.50500 1.000 96.25739  ? 236 GLN   A CD  1 
ATOM   1851 O  OE1 . GLN   A 1 239 ? 74.74700 28.20500 22.04000 1.000 104.81846 ? 236 GLN   A OE1 1 
ATOM   1852 N  NE2 . GLN   A 1 239 ? 73.21800 27.99500 23.67300 1.000 102.23873 ? 236 GLN   A NE2 1 
ATOM   1853 N  N   . GLN   A 1 240 ? 70.13900 26.24300 20.01800 1.000 81.95980  ? 237 GLN   A N   1 
ATOM   1854 C  CA  . GLN   A 1 240 ? 68.85300 26.92500 19.91400 1.000 80.03893  ? 237 GLN   A CA  1 
ATOM   1855 C  C   . GLN   A 1 240 ? 68.39400 27.31100 21.31000 1.000 86.63084  ? 237 GLN   A C   1 
ATOM   1856 O  O   . GLN   A 1 240 ? 68.26300 26.44600 22.18100 1.000 89.73088  ? 237 GLN   A O   1 
ATOM   1857 C  CB  . GLN   A 1 240 ? 67.80700 26.03900 19.23000 1.000 75.71050  ? 237 GLN   A CB  1 
ATOM   1858 C  CG  . GLN   A 1 240 ? 66.46800 26.72400 19.00300 1.000 78.41341  ? 237 GLN   A CG  1 
ATOM   1859 C  CD  . GLN   A 1 240 ? 66.53000 27.78100 17.91600 1.000 78.67042  ? 237 GLN   A CD  1 
ATOM   1860 O  OE1 . GLN   A 1 240 ? 67.06000 27.54200 16.83100 1.000 77.65290  ? 237 GLN   A OE1 1 
ATOM   1861 N  NE2 . GLN   A 1 240 ? 65.98800 28.96000 18.20500 1.000 65.63042  ? 237 GLN   A NE2 1 
ATOM   1862 N  N   . GLU   A 1 241 ? 68.15100 28.60400 21.52100 1.000 71.29250  ? 238 GLU   A N   1 
ATOM   1863 C  CA  . GLU   A 1 241 ? 67.69700 29.13500 22.80700 1.000 86.16227  ? 238 GLU   A CA  1 
ATOM   1864 C  C   . GLU   A 1 241 ? 66.44600 29.96800 22.55000 1.000 89.99499  ? 238 GLU   A C   1 
ATOM   1865 O  O   . GLU   A 1 241 ? 66.52800 31.18700 22.38600 1.000 85.13385  ? 238 GLU   A O   1 
ATOM   1866 C  CB  . GLU   A 1 241 ? 68.79300 29.95600 23.48200 1.000 84.18527  ? 238 GLU   A CB  1 
ATOM   1867 C  CG  . GLU   A 1 241 ? 70.01600 29.15100 23.88200 1.000 94.54508  ? 238 GLU   A CG  1 
ATOM   1868 C  CD  . GLU   A 1 241 ? 70.30900 29.24200 25.36500 1.000 108.89329 ? 238 GLU   A CD  1 
ATOM   1869 O  OE1 . GLU   A 1 241 ? 70.71600 30.33000 25.82600 1.000 116.47059 ? 238 GLU   A OE1 1 
ATOM   1870 O  OE2 . GLU   A 1 241 ? 70.13200 28.22500 26.07000 1.000 110.83538 ? 238 GLU   A OE2 1 
ATOM   1871 N  N   . SER   A 1 242 ? 65.28700 29.31200 22.52000 1.000 79.07774  ? 239 SER   A N   1 
ATOM   1872 C  CA  . SER   A 1 242 ? 64.02600 29.99800 22.27700 1.000 77.13136  ? 239 SER   A CA  1 
ATOM   1873 C  C   . SER   A 1 242 ? 62.90000 29.15700 22.85400 1.000 76.67495  ? 239 SER   A C   1 
ATOM   1874 O  O   . SER   A 1 242 ? 63.01800 27.92800 22.90400 1.000 65.91034  ? 239 SER   A O   1 
ATOM   1875 C  CB  . SER   A 1 242 ? 63.80100 30.23300 20.77600 1.000 63.41228  ? 239 SER   A CB  1 
ATOM   1876 O  OG  . SER   A 1 242 ? 63.55000 29.01300 20.09900 1.000 49.72182  ? 239 SER   A OG  1 
ATOM   1877 N  N   . PRO   A 1 243 ? 61.80100 29.78000 23.29200 1.000 74.76773  ? 240 PRO   A N   1 
ATOM   1878 C  CA  . PRO   A 1 243 ? 60.66600 28.99700 23.81200 1.000 62.31779  ? 240 PRO   A CA  1 
ATOM   1879 C  C   . PRO   A 1 243 ? 59.92100 28.20900 22.74700 1.000 58.80818  ? 240 PRO   A C   1 
ATOM   1880 O  O   . PRO   A 1 243 ? 59.09600 27.35800 23.10200 1.000 61.72851  ? 240 PRO   A O   1 
ATOM   1881 C  CB  . PRO   A 1 243 ? 59.76000 30.06200 24.44300 1.000 58.22182  ? 240 PRO   A CB  1 
ATOM   1882 C  CG  . PRO   A 1 243 ? 60.12600 31.33400 23.76300 1.000 71.10697  ? 240 PRO   A CG  1 
ATOM   1883 C  CD  . PRO   A 1 243 ? 61.57400 31.23200 23.38900 1.000 65.00582  ? 240 PRO   A CD  1 
ATOM   1884 N  N   . PHE   A 1 244 ? 60.17500 28.45900 21.46700 1.000 62.01806  ? 241 PHE   A N   1 
ATOM   1885 C  CA  . PHE   A 1 244 ? 59.50400 27.72700 20.40200 1.000 57.06743  ? 241 PHE   A CA  1 
ATOM   1886 C  C   . PHE   A 1 244 ? 60.32800 27.85000 19.13100 1.000 59.00834  ? 241 PHE   A C   1 
ATOM   1887 O  O   . PHE   A 1 244 ? 61.29900 28.60700 19.06200 1.000 64.28496  ? 241 PHE   A O   1 
ATOM   1888 C  CB  . PHE   A 1 244 ? 58.07500 28.23700 20.17100 1.000 50.90441  ? 241 PHE   A CB  1 
ATOM   1889 C  CG  . PHE   A 1 244 ? 58.01100 29.66000 19.70300 1.000 58.66713  ? 241 PHE   A CG  1 
ATOM   1890 C  CD1 . PHE   A 1 244 ? 58.06200 29.96700 18.35000 1.000 47.81419  ? 241 PHE   A CD1 1 
ATOM   1891 C  CD2 . PHE   A 1 244 ? 57.90100 30.69400 20.61900 1.000 52.60129  ? 241 PHE   A CD2 1 
ATOM   1892 C  CE1 . PHE   A 1 244 ? 58.01300 31.28000 17.92100 1.000 49.00458  ? 241 PHE   A CE1 1 
ATOM   1893 C  CE2 . PHE   A 1 244 ? 57.84400 32.01100 20.19600 1.000 53.38305  ? 241 PHE   A CE2 1 
ATOM   1894 C  CZ  . PHE   A 1 244 ? 57.90100 32.30300 18.84300 1.000 60.98094  ? 241 PHE   A CZ  1 
ATOM   1895 N  N   . VAL   A 1 245 ? 59.91000 27.10000 18.11900 1.000 62.18954  ? 242 VAL   A N   1 
ATOM   1896 C  CA  . VAL   A 1 245 ? 60.53800 27.11900 16.80500 1.000 53.72006  ? 242 VAL   A CA  1 
ATOM   1897 C  C   . VAL   A 1 245 ? 59.43900 26.93800 15.76900 1.000 64.39839  ? 242 VAL   A C   1 
ATOM   1898 O  O   . VAL   A 1 245 ? 58.50900 26.15000 15.96800 1.000 54.35596  ? 242 VAL   A O   1 
ATOM   1899 C  CB  . VAL   A 1 245 ? 61.63200 26.03200 16.69600 1.000 54.43858  ? 242 VAL   A CB  1 
ATOM   1900 C  CG1 . VAL   A 1 245 ? 61.80500 25.56600 15.26300 1.000 75.11750  ? 242 VAL   A CG1 1 
ATOM   1901 C  CG2 . VAL   A 1 245 ? 62.95600 26.55600 17.24500 1.000 67.32765  ? 242 VAL   A CG2 1 
ATOM   1902 N  N   . MET   A 1 246 ? 59.46500 27.78000 14.70700 1.000 64.61212  ? 243 MET   A N   1 
ATOM   1903 C  CA  . MET   A 1 246 ? 58.50500 27.65600 13.56200 1.000 63.68418  ? 243 MET   A CA  1 
ATOM   1904 C  C   . MET   A 1 246 ? 59.25100 27.12000 12.33800 1.000 61.09263  ? 243 MET   A C   1 
ATOM   1905 O  O   . MET   A 1 246 ? 60.21000 27.76600 11.90100 1.000 55.28678  ? 243 MET   A O   1 
ATOM   1906 C  CB  . MET   A 1 246 ? 57.78200 28.95100 13.14700 1.000 50.58733  ? 243 MET   A CB  1 
ATOM   1907 C  CG  . MET   A 1 246 ? 56.69900 28.74900 12.03700 1.000 67.51857  ? 243 MET   A CG  1 
ATOM   1908 S  SD  . MET   A 1 246 ? 56.08300 30.20100 11.16200 1.000 73.72864  ? 243 MET   A SD  1 
ATOM   1909 C  CE  . MET   A 1 246 ? 56.09700 31.39100 12.49200 1.000 56.36029  ? 243 MET   A CE  1 
ATOM   1910 N  N   . MET   A 1 247 ? 58.82100 25.97700 11.82700 1.000 55.18790  ? 244 MET   A N   1 
ATOM   1911 C  CA  . MET   A 1 247 ? 59.39600 25.34200 10.64800 1.000 57.89368  ? 244 MET   A CA  1 
ATOM   1912 C  C   . MET   A 1 247 ? 58.37900 25.43900 9.51900  1.000 63.48490  ? 244 MET   A C   1 
ATOM   1913 O  O   . MET   A 1 247 ? 57.24100 24.97700 9.66500  1.000 61.68956  ? 244 MET   A O   1 
ATOM   1914 C  CB  . MET   A 1 247 ? 59.74700 23.87800 10.92500 1.000 64.07373  ? 244 MET   A CB  1 
ATOM   1915 C  CG  . MET   A 1 247 ? 60.71800 23.65400 12.07600 1.000 54.49516  ? 244 MET   A CG  1 
ATOM   1916 S  SD  . MET   A 1 247 ? 62.34000 24.40300 11.84000 1.000 67.16672  ? 244 MET   A SD  1 
ATOM   1917 C  CE  . MET   A 1 247 ? 62.75600 23.77200 10.21300 1.000 68.26952  ? 244 MET   A CE  1 
ATOM   1918 N  N   . SER   A 1 248 ? 58.78400 26.03400 8.40100  1.000 63.25111  ? 245 SER   A N   1 
ATOM   1919 C  CA  . SER   A 1 248 ? 57.88500 26.26800 7.28100  1.000 63.21298  ? 245 SER   A CA  1 
ATOM   1920 C  C   . SER   A 1 248 ? 58.43600 25.64800 6.00400  1.000 72.66844  ? 245 SER   A C   1 
ATOM   1921 O  O   . SER   A 1 248 ? 59.65100 25.51600 5.82700  1.000 62.95868  ? 245 SER   A O   1 
ATOM   1922 C  CB  . SER   A 1 248 ? 57.64900 27.76400 7.05900  1.000 56.83764  ? 245 SER   A CB  1 
ATOM   1923 O  OG  . SER   A 1 248 ? 56.91200 28.32800 8.12700  1.000 68.98501  ? 245 SER   A OG  1 
ATOM   1924 N  N   . ALA   A 1 249 ? 57.51700 25.27900 5.11600  1.000 65.31597  ? 246 ALA   A N   1 
ATOM   1925 C  CA  . ALA   A 1 249 ? 57.84200 24.73600 3.80600  1.000 54.81464  ? 246 ALA   A CA  1 
ATOM   1926 C  C   . ALA   A 1 249 ? 56.63800 24.94200 2.90000  1.000 71.22942  ? 246 ALA   A C   1 
ATOM   1927 O  O   . ALA   A 1 249 ? 55.51300 25.10300 3.39100  1.000 60.54329  ? 246 ALA   A O   1 
ATOM   1928 C  CB  . ALA   A 1 249 ? 58.21000 23.24600 3.89400  1.000 64.95949  ? 246 ALA   A CB  1 
ATOM   1929 N  N   . PRO   A 1 250 ? 56.83900 24.96800 1.58200  1.000 58.50789  ? 247 PRO   A N   1 
ATOM   1930 C  CA  . PRO   A 1 250 ? 55.69600 25.07000 0.67900  1.000 57.73499  ? 247 PRO   A CA  1 
ATOM   1931 C  C   . PRO   A 1 250 ? 54.75500 23.90100 0.88000  1.000 56.40611  ? 247 PRO   A C   1 
ATOM   1932 O  O   . PRO   A 1 250 ? 55.19000 22.78200 1.21300  1.000 64.85597  ? 247 PRO   A O   1 
ATOM   1933 C  CB  . PRO   A 1 250 ? 56.34300 25.04300 -0.71400 1.000 61.07350  ? 247 PRO   A CB  1 
ATOM   1934 C  CG  . PRO   A 1 250 ? 57.73900 25.51300 -0.49400 1.000 62.12182  ? 247 PRO   A CG  1 
ATOM   1935 C  CD  . PRO   A 1 250 ? 58.12100 24.98000 0.85600  1.000 65.62481  ? 247 PRO   A CD  1 
ATOM   1936 N  N   . PRO   A 1 251 ? 53.45300 24.11400 0.69500  1.000 57.98780  ? 248 PRO   A N   1 
ATOM   1937 C  CA  . PRO   A 1 251 ? 52.47100 23.06100 0.99100  1.000 56.75395  ? 248 PRO   A CA  1 
ATOM   1938 C  C   . PRO   A 1 251 ? 52.80000 21.75000 0.29300  1.000 68.02743  ? 248 PRO   A C   1 
ATOM   1939 O  O   . PRO   A 1 251 ? 52.98100 21.69700 -0.92600 1.000 69.81542  ? 248 PRO   A O   1 
ATOM   1940 C  CB  . PRO   A 1 251 ? 51.15600 23.65700 0.47900  1.000 61.77615  ? 248 PRO   A CB  1 
ATOM   1941 C  CG  . PRO   A 1 251 ? 51.35400 25.13000 0.55300  1.000 54.85104  ? 248 PRO   A CG  1 
ATOM   1942 C  CD  . PRO   A 1 251 ? 52.81500 25.37700 0.28800  1.000 53.98548  ? 248 PRO   A CD  1 
ATOM   1943 N  N   . ALA   A 1 252 ? 52.89000 20.68500 1.08700  1.000 71.15245  ? 249 ALA   A N   1 
ATOM   1944 C  CA  . ALA   A 1 252 ? 53.19700 19.35600 0.58400  1.000 72.77755  ? 249 ALA   A CA  1 
ATOM   1945 C  C   . ALA   A 1 252 ? 52.60400 18.33200 1.53700  1.000 78.48390  ? 249 ALA   A C   1 
ATOM   1946 O  O   . ALA   A 1 252 ? 52.37000 18.61700 2.71500  1.000 71.44801  ? 249 ALA   A O   1 
ATOM   1947 C  CB  . ALA   A 1 252 ? 54.70800 19.13900 0.43500  1.000 59.87803  ? 249 ALA   A CB  1 
ATOM   1948 N  N   . GLN   A 1 253 ? 52.36000 17.13200 1.01300  1.000 78.79132  ? 250 GLN   A N   1 
ATOM   1949 C  CA  . GLN   A 1 253 ? 51.83300 16.05800 1.84500  1.000 64.29673  ? 250 GLN   A CA  1 
ATOM   1950 C  C   . GLN   A 1 253 ? 52.83000 15.70400 2.93900  1.000 69.25098  ? 250 GLN   A C   1 
ATOM   1951 O  O   . GLN   A 1 253 ? 54.03600 15.59500 2.69700  1.000 59.41779  ? 250 GLN   A O   1 
ATOM   1952 C  CB  . GLN   A 1 253 ? 51.51500 14.82800 0.99700  1.000 70.52445  ? 250 GLN   A CB  1 
ATOM   1953 C  CG  . GLN   A 1 253 ? 50.24200 14.11400 1.41600  1.000 77.56085  ? 250 GLN   A CG  1 
ATOM   1954 C  CD  . GLN   A 1 253 ? 48.99800 14.94300 1.15800  1.000 73.47181  ? 250 GLN   A CD  1 
ATOM   1955 O  OE1 . GLN   A 1 253 ? 49.02900 15.91000 0.39900  1.000 81.14219  ? 250 GLN   A OE1 1 
ATOM   1956 N  NE2 . GLN   A 1 253 ? 47.89300 14.56400 1.78800  1.000 76.71065  ? 250 GLN   A NE2 1 
ATOM   1957 N  N   . TYR   A 1 254 ? 52.31400 15.52900 4.15300  1.000 71.74616  ? 251 TYR   A N   1 
ATOM   1958 C  CA  . TYR   A 1 254 ? 53.14800 15.38700 5.33600  1.000 64.43529  ? 251 TYR   A CA  1 
ATOM   1959 C  C   . TYR   A 1 254 ? 52.34300 14.66500 6.40500  1.000 71.98526  ? 251 TYR   A C   1 
ATOM   1960 O  O   . TYR   A 1 254 ? 51.13000 14.86900 6.51600  1.000 68.52064  ? 251 TYR   A O   1 
ATOM   1961 C  CB  . TYR   A 1 254 ? 53.61200 16.76000 5.83500  1.000 60.11167  ? 251 TYR   A CB  1 
ATOM   1962 C  CG  . TYR   A 1 254 ? 54.70700 16.74200 6.87800  1.000 64.93320  ? 251 TYR   A CG  1 
ATOM   1963 C  CD1 . TYR   A 1 254 ? 56.03300 16.54000 6.51800  1.000 51.11541  ? 251 TYR   A CD1 1 
ATOM   1964 C  CD2 . TYR   A 1 254 ? 54.41800 16.96400 8.22000  1.000 54.18606  ? 251 TYR   A CD2 1 
ATOM   1965 C  CE1 . TYR   A 1 254 ? 57.04100 16.53900 7.47000  1.000 53.50821  ? 251 TYR   A CE1 1 
ATOM   1966 C  CE2 . TYR   A 1 254 ? 55.41600 16.96300 9.17700  1.000 55.03209  ? 251 TYR   A CE2 1 
ATOM   1967 C  CZ  . TYR   A 1 254 ? 56.72400 16.75200 8.79800  1.000 58.10868  ? 251 TYR   A CZ  1 
ATOM   1968 O  OH  . TYR   A 1 254 ? 57.71500 16.75100 9.75200  1.000 67.27002  ? 251 TYR   A OH  1 
ATOM   1969 N  N   . GLU   A 1 255 ? 53.01600 13.81600 7.17400  1.000 72.99799  ? 252 GLU   A N   1 
ATOM   1970 C  CA  . GLU   A 1 255 ? 52.38600 13.08000 8.26100  1.000 76.71727  ? 252 GLU   A CA  1 
ATOM   1971 C  C   . GLU   A 1 255 ? 52.73300 13.73900 9.58800  1.000 68.34144  ? 252 GLU   A C   1 
ATOM   1972 O  O   . GLU   A 1 255 ? 53.90400 14.03000 9.85600  1.000 65.75038  ? 252 GLU   A O   1 
ATOM   1973 C  CB  . GLU   A 1 255 ? 52.82600 11.61500 8.26500  1.000 87.63944  ? 252 GLU   A CB  1 
ATOM   1974 C  CG  . GLU   A 1 255 ? 51.72800 10.65400 8.69800  1.000 100.54902 ? 252 GLU   A CG  1 
ATOM   1975 C  CD  . GLU   A 1 255 ? 52.17300 9.20500  8.68500  1.000 114.12755 ? 252 GLU   A CD  1 
ATOM   1976 O  OE1 . GLU   A 1 255 ? 53.39700 8.95300  8.69600  1.000 113.47281 ? 252 GLU   A OE1 1 
ATOM   1977 O  OE2 . GLU   A 1 255 ? 51.29600 8.31500  8.66100  1.000 112.36714 ? 252 GLU   A OE2 1 
ATOM   1978 N  N   . LEU   A 1 256 ? 51.71600 13.97300 10.41200 1.000 60.87030  ? 253 LEU   A N   1 
ATOM   1979 C  CA  . LEU   A 1 256 ? 51.88400 14.58000 11.72600 1.000 72.47414  ? 253 LEU   A CA  1 
ATOM   1980 C  C   . LEU   A 1 256 ? 51.67600 13.50900 12.78900 1.000 67.75905  ? 253 LEU   A C   1 
ATOM   1981 O  O   . LEU   A 1 256 ? 50.60300 12.89900 12.85900 1.000 65.40450  ? 253 LEU   A O   1 
ATOM   1982 C  CB  . LEU   A 1 256 ? 50.90800 15.74100 11.92100 1.000 60.95484  ? 253 LEU   A CB  1 
ATOM   1983 C  CG  . LEU   A 1 256 ? 51.20800 17.00400 11.11000 1.000 59.38942  ? 253 LEU   A CG  1 
ATOM   1984 C  CD1 . LEU   A 1 256 ? 50.08100 18.01400 11.23600 1.000 49.54674  ? 253 LEU   A CD1 1 
ATOM   1985 C  CD2 . LEU   A 1 256 ? 52.53400 17.62000 11.53300 1.000 48.10599  ? 253 LEU   A CD2 1 
ATOM   1986 N  N   . LYS   A 1 257 ? 52.70200 13.27900 13.60300 1.000 66.02233  ? 254 LYS   A N   1 
ATOM   1987 C  CA  . LYS   A 1 257 ? 52.64100 12.28600 14.66700 1.000 75.20609  ? 254 LYS   A CA  1 
ATOM   1988 C  C   . LYS   A 1 257 ? 52.20000 12.93300 15.97300 1.000 67.32456  ? 254 LYS   A C   1 
ATOM   1989 O  O   . LYS   A 1 257 ? 52.67800 14.01100 16.33800 1.000 70.11449  ? 254 LYS   A O   1 
ATOM   1990 C  CB  . LYS   A 1 257 ? 54.00100 11.61400 14.85600 1.000 79.61349  ? 254 LYS   A CB  1 
ATOM   1991 C  CG  . LYS   A 1 257 ? 54.03600 10.13600 14.50700 1.000 84.53571  ? 254 LYS   A CG  1 
ATOM   1992 C  CD  . LYS   A 1 257 ? 54.12700 9.90900  13.01100 1.000 80.17190  ? 254 LYS   A CD  1 
ATOM   1993 C  CE  . LYS   A 1 257 ? 53.50900 8.57800  12.62200 1.000 99.88214  ? 254 LYS   A CE  1 
ATOM   1994 N  NZ  . LYS   A 1 257 ? 53.65800 8.30100  11.16900 1.000 116.14181 ? 254 LYS   A NZ  1 
ATOM   1995 N  N   . HIS   A 1 258 ? 51.29300 12.26300 16.68000 1.000 70.52646  ? 255 HIS   A N   1 
ATOM   1996 C  CA  . HIS   A 1 258 ? 50.80400 12.78000 17.95200 1.000 64.88727  ? 255 HIS   A CA  1 
ATOM   1997 C  C   . HIS   A 1 258 ? 51.93300 12.84700 18.97300 1.000 68.38428  ? 255 HIS   A C   1 
ATOM   1998 O  O   . HIS   A 1 258 ? 52.65900 11.87100 19.18100 1.000 74.61014  ? 255 HIS   A O   1 
ATOM   1999 C  CB  . HIS   A 1 258 ? 49.66800 11.90300 18.47900 1.000 65.29087  ? 255 HIS   A CB  1 
ATOM   2000 C  CG  . HIS   A 1 258 ? 49.46600 12.00100 19.96000 1.000 72.28950  ? 255 HIS   A CG  1 
ATOM   2001 N  ND1 . HIS   A 1 258 ? 49.78900 10.97800 20.82600 1.000 80.48635  ? 255 HIS   A ND1 1 
ATOM   2002 C  CD2 . HIS   A 1 258 ? 48.97300 13.00100 20.72800 1.000 71.98404  ? 255 HIS   A CD2 1 
ATOM   2003 C  CE1 . HIS   A 1 258 ? 49.50400 11.34400 22.06300 1.000 88.77015  ? 255 HIS   A CE1 1 
ATOM   2004 N  NE2 . HIS   A 1 258 ? 49.00700 12.56700 22.03100 1.000 78.72666  ? 255 HIS   A NE2 1 
ATOM   2005 N  N   . GLY   A 1 259 ? 52.08400 14.01000 19.60500 1.000 68.24756  ? 256 GLY   A N   1 
ATOM   2006 C  CA  . GLY   A 1 259 ? 53.08700 14.20500 20.62800 1.000 56.01773  ? 256 GLY   A CA  1 
ATOM   2007 C  C   . GLY   A 1 259 ? 54.44900 14.64200 20.13000 1.000 59.57238  ? 256 GLY   A C   1 
ATOM   2008 O  O   . GLY   A 1 259 ? 55.32700 14.92500 20.95500 1.000 58.80302  ? 256 GLY   A O   1 
ATOM   2009 N  N   . THR   A 1 260 ? 54.65900 14.70900 18.81700 1.000 63.38041  ? 257 THR   A N   1 
ATOM   2010 C  CA  . THR   A 1 260 ? 55.94200 15.11300 18.25700 1.000 64.88237  ? 257 THR   A CA  1 
ATOM   2011 C  C   . THR   A 1 260 ? 55.98500 16.58500 17.86800 1.000 63.10937  ? 257 THR   A C   1 
ATOM   2012 O  O   . THR   A 1 260 ? 57.03800 17.06800 17.43900 1.000 59.12791  ? 257 THR   A O   1 
ATOM   2013 C  CB  . THR   A 1 260 ? 56.28100 14.25200 17.03600 1.000 74.66094  ? 257 THR   A CB  1 
ATOM   2014 O  OG1 . THR   A 1 260 ? 55.21500 14.33600 16.08200 1.000 66.66814  ? 257 THR   A OG1 1 
ATOM   2015 C  CG2 . THR   A 1 260 ? 56.47200 12.80200 17.44800 1.000 63.18089  ? 257 THR   A CG2 1 
ATOM   2016 N  N   . PHE   A 1 261 ? 54.87500 17.30500 18.01000 1.000 68.61907  ? 258 PHE   A N   1 
ATOM   2017 C  CA  . PHE   A 1 261 ? 54.80300 18.71000 17.64000 1.000 62.99035  ? 258 PHE   A CA  1 
ATOM   2018 C  C   . PHE   A 1 261 ? 53.71100 19.37300 18.46700 1.000 45.85899  ? 258 PHE   A C   1 
ATOM   2019 O  O   . PHE   A 1 261 ? 52.89800 18.70400 19.10900 1.000 56.82128  ? 258 PHE   A O   1 
ATOM   2020 C  CB  . PHE   A 1 261 ? 54.52800 18.88200 16.13900 1.000 53.54688  ? 258 PHE   A CB  1 
ATOM   2021 C  CG  . PHE   A 1 261 ? 53.12200 18.52900 15.73900 1.000 51.13144  ? 258 PHE   A CG  1 
ATOM   2022 C  CD1 . PHE   A 1 261 ? 52.70800 17.20500 15.70500 1.000 48.55711  ? 258 PHE   A CD1 1 
ATOM   2023 C  CD2 . PHE   A 1 261 ? 52.21100 19.51900 15.40800 1.000 49.25043  ? 258 PHE   A CD2 1 
ATOM   2024 C  CE1 . PHE   A 1 261 ? 51.41400 16.87500 15.34300 1.000 55.64314  ? 258 PHE   A CE1 1 
ATOM   2025 C  CE2 . PHE   A 1 261 ? 50.91300 19.19500 15.04300 1.000 49.44506  ? 258 PHE   A CE2 1 
ATOM   2026 C  CZ  . PHE   A 1 261 ? 50.51600 17.87200 15.01100 1.000 53.65477  ? 258 PHE   A CZ  1 
ATOM   2027 N  N   . THR   A 1 262 ? 53.69300 20.70600 18.43500 1.000 56.23797  ? 259 THR   A N   1 
ATOM   2028 C  CA  . THR   A 1 262 ? 52.67900 21.47600 19.15000 1.000 47.52266  ? 259 THR   A CA  1 
ATOM   2029 C  C   . THR   A 1 262 ? 51.45000 21.72500 18.27900 1.000 52.23727  ? 259 THR   A C   1 
ATOM   2030 O  O   . THR   A 1 262 ? 50.33900 21.31300 18.62900 1.000 50.28851  ? 259 THR   A O   1 
ATOM   2031 C  CB  . THR   A 1 262 ? 53.26600 22.80800 19.63400 1.000 58.65576  ? 259 THR   A CB  1 
ATOM   2032 O  OG1 . THR   A 1 262 ? 54.37300 22.55900 20.51000 1.000 62.85957  ? 259 THR   A OG1 1 
ATOM   2033 C  CG2 . THR   A 1 262 ? 52.21100 23.61700 20.37400 1.000 50.75905  ? 259 THR   A CG2 1 
ATOM   2034 N  N   . CYS   A 1 263 ? 51.63600 22.39700 17.14400 1.000 46.85348  ? 260 CYS   A N   1 
ATOM   2035 C  CA  . CYS   A 1 263 ? 50.52700 22.71400 16.25500 1.000 49.44136  ? 260 CYS   A CA  1 
ATOM   2036 C  C   . CYS   A 1 263 ? 51.07700 22.96000 14.85700 1.000 56.63185  ? 260 CYS   A C   1 
ATOM   2037 O  O   . CYS   A 1 263 ? 52.27900 23.17400 14.67300 1.000 53.32639  ? 260 CYS   A O   1 
ATOM   2038 C  CB  . CYS   A 1 263 ? 49.73100 23.92400 16.76000 1.000 50.01828  ? 260 CYS   A CB  1 
ATOM   2039 S  SG  . CYS   A 1 263 ? 50.69000 25.44900 16.90500 1.000 51.94284  ? 260 CYS   A SG  1 
ATOM   2040 N  N   . ALA   A 1 264 ? 50.18000 22.92500 13.86900 1.000 51.28533  ? 261 ALA   A N   1 
ATOM   2041 C  CA  . ALA   A 1 264 ? 50.59700 22.99100 12.47400 1.000 59.44997  ? 261 ALA   A CA  1 
ATOM   2042 C  C   . ALA   A 1 264 ? 49.52400 23.66700 11.62900 1.000 55.05102  ? 261 ALA   A C   1 
ATOM   2043 O  O   . ALA   A 1 264 ? 48.34400 23.70000 11.98900 1.000 54.26325  ? 261 ALA   A O   1 
ATOM   2044 C  CB  . ALA   A 1 264 ? 50.90500 21.59300 11.91900 1.000 57.28533  ? 261 ALA   A CB  1 
ATOM   2045 N  N   . SER   A 1 265 ? 49.95400 24.19300 10.48200 1.000 59.10103  ? 262 SER   A N   1 
ATOM   2046 C  CA  . SER   A 1 265 ? 49.08400 24.88200 9.53300  1.000 58.86514  ? 262 SER   A CA  1 
ATOM   2047 C  C   . SER   A 1 265 ? 48.87300 24.00300 8.30600  1.000 54.14708  ? 262 SER   A C   1 
ATOM   2048 O  O   . SER   A 1 265 ? 49.84000 23.62600 7.63500  1.000 53.41117  ? 262 SER   A O   1 
ATOM   2049 C  CB  . SER   A 1 265 ? 49.68300 26.22700 9.11500  1.000 54.32174  ? 262 SER   A CB  1 
ATOM   2050 O  OG  . SER   A 1 265 ? 49.88700 27.07700 10.22900 1.000 64.52910  ? 262 SER   A OG  1 
ATOM   2051 N  N   . GLU   A 1 266 ? 47.61400 23.69100 8.01000  1.000 50.27852  ? 263 GLU   A N   1 
ATOM   2052 C  CA  . GLU   A 1 266 ? 47.25200 22.95200 6.80700  1.000 60.39690  ? 263 GLU   A CA  1 
ATOM   2053 C  C   . GLU   A 1 266 ? 46.74000 23.92400 5.75100  1.000 62.78258  ? 263 GLU   A C   1 
ATOM   2054 O  O   . GLU   A 1 266 ? 45.85900 24.74400 6.03100  1.000 53.27474  ? 263 GLU   A O   1 
ATOM   2055 C  CB  . GLU   A 1 266 ? 46.18700 21.89500 7.10600  1.000 52.02483  ? 263 GLU   A CB  1 
ATOM   2056 C  CG  . GLU   A 1 266 ? 45.72400 21.12600 5.87000  1.000 69.48346  ? 263 GLU   A CG  1 
ATOM   2057 C  CD  . GLU   A 1 266 ? 44.37100 20.46300 6.05700  1.000 76.91821  ? 263 GLU   A CD  1 
ATOM   2058 O  OE1 . GLU   A 1 266 ? 44.31900 19.36200 6.64500  1.000 81.01338  ? 263 GLU   A OE1 1 
ATOM   2059 O  OE2 . GLU   A 1 266 ? 43.35900 21.04000 5.60800  1.000 78.97614  ? 263 GLU   A OE2 1 
ATOM   2060 N  N   . TYR   A 1 267 ? 47.28800 23.82700 4.54000  1.000 60.36431  ? 264 TYR   A N   1 
ATOM   2061 C  CA  . TYR   A 1 267 ? 46.89500 24.69100 3.43300  1.000 70.35233  ? 264 TYR   A CA  1 
ATOM   2062 C  C   . TYR   A 1 267 ? 46.48900 23.83300 2.24600  1.000 63.51012  ? 264 TYR   A C   1 
ATOM   2063 O  O   . TYR   A 1 267 ? 47.31400 23.09300 1.70000  1.000 64.70520  ? 264 TYR   A O   1 
ATOM   2064 C  CB  . TYR   A 1 267 ? 48.02800 25.64200 3.03400  1.000 57.50780  ? 264 TYR   A CB  1 
ATOM   2065 C  CG  . TYR   A 1 267 ? 47.59500 26.70800 2.05300  1.000 78.67463  ? 264 TYR   A CG  1 
ATOM   2066 C  CD1 . TYR   A 1 267 ? 46.95700 27.86300 2.48900  1.000 64.82845  ? 264 TYR   A CD1 1 
ATOM   2067 C  CD2 . TYR   A 1 267 ? 47.80700 26.55000 0.68800  1.000 67.12987  ? 264 TYR   A CD2 1 
ATOM   2068 C  CE1 . TYR   A 1 267 ? 46.55400 28.83800 1.59500  1.000 69.67383  ? 264 TYR   A CE1 1 
ATOM   2069 C  CE2 . TYR   A 1 267 ? 47.40600 27.52000 -0.21500 1.000 69.95134  ? 264 TYR   A CE2 1 
ATOM   2070 C  CZ  . TYR   A 1 267 ? 46.78200 28.66200 0.24400  1.000 78.05207  ? 264 TYR   A CZ  1 
ATOM   2071 O  OH  . TYR   A 1 267 ? 46.38400 29.62900 -0.64900 1.000 54.22809  ? 264 TYR   A OH  1 
ATOM   2072 N  N   . THR   A 1 268 ? 45.22400 23.93600 1.84900  1.000 65.85105  ? 265 THR   A N   1 
ATOM   2073 C  CA  . THR   A 1 268 ? 44.69700 23.25400 0.67600  1.000 73.27624  ? 265 THR   A CA  1 
ATOM   2074 C  C   . THR   A 1 268 ? 44.16800 24.28200 -0.31300 1.000 79.58084  ? 265 THR   A C   1 
ATOM   2075 O  O   . THR   A 1 268 ? 43.54700 25.27400 0.08000  1.000 76.63524  ? 265 THR   A O   1 
ATOM   2076 C  CB  . THR   A 1 268 ? 43.57700 22.27400 1.04700  1.000 69.09068  ? 265 THR   A CB  1 
ATOM   2077 O  OG1 . THR   A 1 268 ? 42.34200 22.98800 1.18200  1.000 77.69846  ? 265 THR   A OG1 1 
ATOM   2078 C  CG2 . THR   A 1 268 ? 43.89400 21.55800 2.34900  1.000 80.69386  ? 265 THR   A CG2 1 
ATOM   2079 N  N   . GLY   A 1 269 ? 44.41900 24.04400 -1.59300 1.000 78.94612  ? 266 GLY   A N   1 
ATOM   2080 C  CA  . GLY   A 1 269 ? 43.93900 24.90400 -2.65600 1.000 81.90205  ? 266 GLY   A CA  1 
ATOM   2081 C  C   . GLY   A 1 269 ? 45.07500 25.57900 -3.39300 1.000 78.09491  ? 266 GLY   A C   1 
ATOM   2082 O  O   . GLY   A 1 269 ? 46.25400 25.25200 -3.22200 1.000 62.95382  ? 266 GLY   A O   1 
ATOM   2083 N  N   . ASN   A 1 270 ? 44.70600 26.54300 -4.23000 1.000 73.68115  ? 267 ASN   A N   1 
ATOM   2084 C  CA  . ASN   A 1 270 ? 45.67500 27.22800 -5.06600 1.000 76.96571  ? 267 ASN   A CA  1 
ATOM   2085 C  C   . ASN   A 1 270 ? 46.40200 28.31500 -4.28000 1.000 69.88263  ? 267 ASN   A C   1 
ATOM   2086 O  O   . ASN   A 1 270 ? 45.97400 28.74000 -3.20300 1.000 70.50702  ? 267 ASN   A O   1 
ATOM   2087 C  CB  . ASN   A 1 270 ? 44.99400 27.83300 -6.29100 1.000 86.33140  ? 267 ASN   A CB  1 
ATOM   2088 C  CG  . ASN   A 1 270 ? 44.60800 26.79100 -7.31600 1.000 82.13083  ? 267 ASN   A CG  1 
ATOM   2089 O  OD1 . ASN   A 1 270 ? 45.44400 26.00300 -7.76200 1.000 89.05769  ? 267 ASN   A OD1 1 
ATOM   2090 N  ND2 . ASN   A 1 270 ? 43.33500 26.77600 -7.69300 1.000 72.90153  ? 267 ASN   A ND2 1 
ATOM   2091 N  N   . TYR   A 1 271 ? 47.52200 28.75900 -4.84700 1.000 69.37786  ? 268 TYR   A N   1 
ATOM   2092 C  CA  . TYR   A 1 271 ? 48.30400 29.84900 -4.28000 1.000 60.82911  ? 268 TYR   A CA  1 
ATOM   2093 C  C   . TYR   A 1 271 ? 47.41700 31.05000 -3.97600 1.000 64.31541  ? 268 TYR   A C   1 
ATOM   2094 O  O   . TYR   A 1 271 ? 46.63300 31.49100 -4.82200 1.000 72.43390  ? 268 TYR   A O   1 
ATOM   2095 C  CB  . TYR   A 1 271 ? 49.41600 30.23100 -5.26000 1.000 47.99126  ? 268 TYR   A CB  1 
ATOM   2096 C  CG  . TYR   A 1 271 ? 50.45100 31.19100 -4.72800 1.000 62.48277  ? 268 TYR   A CG  1 
ATOM   2097 C  CD1 . TYR   A 1 271 ? 51.28800 30.83400 -3.67700 1.000 70.71154  ? 268 TYR   A CD1 1 
ATOM   2098 C  CD2 . TYR   A 1 271 ? 50.62600 32.44100 -5.30800 1.000 61.02277  ? 268 TYR   A CD2 1 
ATOM   2099 C  CE1 . TYR   A 1 271 ? 52.24800 31.70700 -3.19900 1.000 67.47907  ? 268 TYR   A CE1 1 
ATOM   2100 C  CE2 . TYR   A 1 271 ? 51.58300 33.31900 -4.83900 1.000 76.20596  ? 268 TYR   A CE2 1 
ATOM   2101 C  CZ  . TYR   A 1 271 ? 52.39200 32.94800 -3.78600 1.000 74.29082  ? 268 TYR   A CZ  1 
ATOM   2102 O  OH  . TYR   A 1 271 ? 53.34500 33.82600 -3.32300 1.000 79.17507  ? 268 TYR   A OH  1 
ATOM   2103 N  N   . GLN   A 1 272 ? 47.51800 31.54300 -2.73900 1.000 68.38116  ? 269 GLN   A N   1 
ATOM   2104 C  CA  . GLN   A 1 272 ? 46.77700 32.70000 -2.24300 1.000 67.61186  ? 269 GLN   A CA  1 
ATOM   2105 C  C   . GLN   A 1 272 ? 45.27300 32.45600 -2.13100 1.000 66.92859  ? 269 GLN   A C   1 
ATOM   2106 O  O   . GLN   A 1 272 ? 44.62300 33.00600 -1.23600 1.000 70.89329  ? 269 GLN   A O   1 
ATOM   2107 C  CB  . GLN   A 1 272 ? 47.05300 33.92400 -3.11900 1.000 55.47672  ? 269 GLN   A CB  1 
ATOM   2108 C  CG  . GLN   A 1 272 ? 48.52500 34.30000 -3.17400 1.000 62.81676  ? 269 GLN   A CG  1 
ATOM   2109 C  CD  . GLN   A 1 272 ? 48.83000 35.32600 -4.24400 1.000 66.13424  ? 269 GLN   A CD  1 
ATOM   2110 O  OE1 . GLN   A 1 272 ? 48.05300 35.51500 -5.17900 1.000 72.69606  ? 269 GLN   A OE1 1 
ATOM   2111 N  NE2 . GLN   A 1 272 ? 49.97300 35.99100 -4.11600 1.000 67.96088  ? 269 GLN   A NE2 1 
ATOM   2112 N  N   . CYS   A 1 273 ? 44.71200 31.62900 -3.00900 1.000 77.59463  ? 270 CYS   A N   1 
ATOM   2113 C  CA  . CYS   A 1 273 ? 43.27400 31.39900 -3.04300 1.000 80.96086  ? 270 CYS   A CA  1 
ATOM   2114 C  C   . CYS   A 1 273 ? 42.83800 30.19000 -2.23700 1.000 72.30325  ? 270 CYS   A C   1 
ATOM   2115 O  O   . CYS   A 1 273 ? 41.64700 29.86200 -2.23500 1.000 66.45518  ? 270 CYS   A O   1 
ATOM   2116 C  CB  . CYS   A 1 273 ? 42.80500 31.23900 -4.48600 1.000 81.72617  ? 270 CYS   A CB  1 
ATOM   2117 S  SG  . CYS   A 1 273 ? 42.70300 32.81700 -5.28500 1.000 100.91336 ? 270 CYS   A SG  1 
ATOM   2118 N  N   . GLY   A 1 274 ? 43.76400 29.52100 -1.56400 1.000 79.02051  ? 271 GLY   A N   1 
ATOM   2119 C  CA  . GLY   A 1 274 ? 43.44800 28.32400 -0.82200 1.000 73.81839  ? 271 GLY   A CA  1 
ATOM   2120 C  C   . GLY   A 1 274 ? 42.73600 28.62700 0.48100  1.000 72.06505  ? 271 GLY   A C   1 
ATOM   2121 O  O   . GLY   A 1 274 ? 42.19200 29.71200 0.70900  1.000 61.71563  ? 271 GLY   A O   1 
ATOM   2122 N  N   . HIS   A 1 275 ? 42.75100 27.62500 1.35100  1.000 64.55477  ? 272 HIS   A N   1 
ATOM   2123 C  CA  . HIS   A 1 275 ? 42.09200 27.71500 2.63900  1.000 67.64260  ? 272 HIS   A CA  1 
ATOM   2124 C  C   . HIS   A 1 275 ? 42.98500 27.08400 3.69300  1.000 77.53852  ? 272 HIS   A C   1 
ATOM   2125 O  O   . HIS   A 1 275 ? 43.65700 26.08200 3.43300  1.000 62.35823  ? 272 HIS   A O   1 
ATOM   2126 C  CB  . HIS   A 1 275 ? 40.72800 27.03000 2.60300  1.000 57.20875  ? 272 HIS   A CB  1 
ATOM   2127 C  CG  . HIS   A 1 275 ? 39.89000 27.28800 3.81600  1.000 73.18336  ? 272 HIS   A CG  1 
ATOM   2128 N  ND1 . HIS   A 1 275 ? 39.39900 28.53800 4.13200  1.000 89.10996  ? 272 HIS   A ND1 1 
ATOM   2129 C  CD2 . HIS   A 1 275 ? 39.44600 26.45200 4.78500  1.000 66.18124  ? 272 HIS   A CD2 1 
ATOM   2130 C  CE1 . HIS   A 1 275 ? 38.68600 28.45800 5.24200  1.000 78.99671  ? 272 HIS   A CE1 1 
ATOM   2131 N  NE2 . HIS   A 1 275 ? 38.70200 27.20600 5.66100  1.000 72.44094  ? 272 HIS   A NE2 1 
ATOM   2132 N  N   . TYR   A 1 276 ? 42.99000 27.68200 4.87700  1.000 64.54746  ? 273 TYR   A N   1 
ATOM   2133 C  CA  . TYR   A 1 276 ? 43.81600 27.23500 5.98600  1.000 56.43434  ? 273 TYR   A CA  1 
ATOM   2134 C  C   . TYR   A 1 276 ? 42.99600 26.40200 6.96300  1.000 55.08255  ? 273 TYR   A C   1 
ATOM   2135 O  O   . TYR   A 1 276 ? 41.80700 26.65000 7.17800  1.000 59.03817  ? 273 TYR   A O   1 
ATOM   2136 C  CB  . TYR   A 1 276 ? 44.42400 28.42800 6.72500  1.000 50.65303  ? 273 TYR   A CB  1 
ATOM   2137 C  CG  . TYR   A 1 276 ? 45.75300 28.91500 6.18900  1.000 53.93501  ? 273 TYR   A CG  1 
ATOM   2138 C  CD1 . TYR   A 1 276 ? 46.91500 28.17800 6.38100  1.000 54.45916  ? 273 TYR   A CD1 1 
ATOM   2139 C  CD2 . TYR   A 1 276 ? 45.84800 30.12100 5.50300  1.000 45.80767  ? 273 TYR   A CD2 1 
ATOM   2140 C  CE1 . TYR   A 1 276 ? 48.13700 28.62600 5.90500  1.000 46.58254  ? 273 TYR   A CE1 1 
ATOM   2141 C  CE2 . TYR   A 1 276 ? 47.06300 30.57700 5.02200  1.000 44.18189  ? 273 TYR   A CE2 1 
ATOM   2142 C  CZ  . TYR   A 1 276 ? 48.20300 29.82700 5.22700  1.000 51.25091  ? 273 TYR   A CZ  1 
ATOM   2143 O  OH  . TYR   A 1 276 ? 49.41300 30.27900 4.75000  1.000 53.04037  ? 273 TYR   A OH  1 
ATOM   2144 N  N   . LYS   A 1 277 ? 43.65000 25.40200 7.54700  1.000 65.25655  ? 274 LYS   A N   1 
ATOM   2145 C  CA  . LYS   A 1 277 ? 43.12400 24.65700 8.68000  1.000 61.57720  ? 274 LYS   A CA  1 
ATOM   2146 C  C   . LYS   A 1 277 ? 44.22700 24.52200 9.71900  1.000 54.12993  ? 274 LYS   A C   1 
ATOM   2147 O  O   . LYS   A 1 277 ? 45.41500 24.65500 9.41200  1.000 53.39127  ? 274 LYS   A O   1 
ATOM   2148 C  CB  . LYS   A 1 277 ? 42.60700 23.27500 8.26600  1.000 68.30113  ? 274 LYS   A CB  1 
ATOM   2149 C  CG  . LYS   A 1 277 ? 41.24800 23.29900 7.59100  1.000 67.87811  ? 274 LYS   A CG  1 
ATOM   2150 C  CD  . LYS   A 1 277 ? 40.75000 21.89200 7.31900  1.000 69.36733  ? 274 LYS   A CD  1 
ATOM   2151 C  CE  . LYS   A 1 277 ? 39.50600 21.90700 6.45100  1.000 69.62930  ? 274 LYS   A CE  1 
ATOM   2152 N  NZ  . LYS   A 1 277 ? 39.24100 20.56100 5.87700  1.000 67.53652  ? 274 LYS   A NZ  1 
ATOM   2153 N  N   . HIS   A 1 278 ? 43.82400 24.25200 10.95800 1.000 56.32799  ? 275 HIS   A N   1 
ATOM   2154 C  CA  . HIS   A 1 278 ? 44.74400 24.20900 12.08900 1.000 48.91144  ? 275 HIS   A CA  1 
ATOM   2155 C  C   . HIS   A 1 278 ? 44.74300 22.81400 12.69900 1.000 60.52951  ? 275 HIS   A C   1 
ATOM   2156 O  O   . HIS   A 1 278 ? 43.68800 22.30500 13.09500 1.000 49.35887  ? 275 HIS   A O   1 
ATOM   2157 C  CB  . HIS   A 1 278 ? 44.36300 25.25500 13.13800 1.000 51.12638  ? 275 HIS   A CB  1 
ATOM   2158 C  CG  . HIS   A 1 278 ? 45.30700 25.31900 14.29700 1.000 53.03865  ? 275 HIS   A CG  1 
ATOM   2159 N  ND1 . HIS   A 1 278 ? 46.55000 25.90900 14.21400 1.000 53.87872  ? 275 HIS   A ND1 1 
ATOM   2160 C  CD2 . HIS   A 1 278 ? 45.19400 24.85900 15.56500 1.000 46.07930  ? 275 HIS   A CD2 1 
ATOM   2161 C  CE1 . HIS   A 1 278 ? 47.15900 25.81600 15.38300 1.000 56.37223  ? 275 HIS   A CE1 1 
ATOM   2162 N  NE2 . HIS   A 1 278 ? 46.35700 25.18200 16.21900 1.000 50.38411  ? 275 HIS   A NE2 1 
ATOM   2163 N  N   . ILE   A 1 279 ? 45.92400 22.20600 12.78000 1.000 52.88418  ? 276 ILE   A N   1 
ATOM   2164 C  CA  . ILE   A 1 279 ? 46.11800 20.91900 13.44000 1.000 60.21059  ? 276 ILE   A CA  1 
ATOM   2165 C  C   . ILE   A 1 279 ? 46.87100 21.16400 14.74000 1.000 53.97500  ? 276 ILE   A C   1 
ATOM   2166 O  O   . ILE   A 1 279 ? 47.91300 21.83000 14.74300 1.000 49.15668  ? 276 ILE   A O   1 
ATOM   2167 C  CB  . ILE   A 1 279 ? 46.89000 19.93000 12.54800 1.000 52.68946  ? 276 ILE   A CB  1 
ATOM   2168 C  CG1 . ILE   A 1 279 ? 46.32200 19.91100 11.12200 1.000 59.83337  ? 276 ILE   A CG1 1 
ATOM   2169 C  CG2 . ILE   A 1 279 ? 46.86700 18.53800 13.16300 1.000 55.53812  ? 276 ILE   A CG2 1 
ATOM   2170 C  CD1 . ILE   A 1 279 ? 44.84200 19.61800 11.04400 1.000 64.66661  ? 276 ILE   A CD1 1 
ATOM   2171 N  N   . THR   A 1 280 ? 46.35000 20.62400 15.84000 1.000 52.67358  ? 277 THR   A N   1 
ATOM   2172 C  CA  . THR   A 1 280 ? 46.99300 20.74200 17.14200 1.000 56.27763  ? 277 THR   A CA  1 
ATOM   2173 C  C   . THR   A 1 280 ? 47.08600 19.36700 17.79200 1.000 51.92537  ? 277 THR   A C   1 
ATOM   2174 O  O   . THR   A 1 280 ? 46.16700 18.55000 17.67400 1.000 53.74652  ? 277 THR   A O   1 
ATOM   2175 C  CB  . THR   A 1 280 ? 46.23300 21.71800 18.05900 1.000 53.18860  ? 277 THR   A CB  1 
ATOM   2176 O  OG1 . THR   A 1 280 ? 46.82300 21.71500 19.36400 1.000 49.66204  ? 277 THR   A OG1 1 
ATOM   2177 C  CG2 . THR   A 1 280 ? 44.76400 21.33800 18.16400 1.000 49.28916  ? 277 THR   A CG2 1 
ATOM   2178 N  N   . SER   A 1 281 ? 48.20600 19.11600 18.47200 1.000 45.68585  ? 278 SER   A N   1 
ATOM   2179 C  CA  . SER   A 1 281 ? 48.46600 17.83800 19.13100 1.000 52.75121  ? 278 SER   A CA  1 
ATOM   2180 C  C   . SER   A 1 281 ? 48.10600 17.94700 20.61000 1.000 57.46129  ? 278 SER   A C   1 
ATOM   2181 O  O   . SER   A 1 281 ? 48.79800 18.62400 21.37700 1.000 51.20820  ? 278 SER   A O   1 
ATOM   2182 C  CB  . SER   A 1 281 ? 49.92600 17.42700 18.96400 1.000 50.86084  ? 278 SER   A CB  1 
ATOM   2183 O  OG  . SER   A 1 281 ? 50.18500 16.19500 19.61900 1.000 56.43041  ? 278 SER   A OG  1 
ATOM   2184 N  N   . LYS   A 1 282 ? 47.03200 17.26600 21.00900 1.000 52.15824  ? 279 LYS   A N   1 
ATOM   2185 C  CA  . LYS   A 1 282 ? 46.63000 17.21100 22.41000 1.000 58.35256  ? 279 LYS   A CA  1 
ATOM   2186 C  C   . LYS   A 1 282 ? 46.74100 15.78400 22.93500 1.000 62.51023  ? 279 LYS   A C   1 
ATOM   2187 O  O   . LYS   A 1 282 ? 47.77000 15.12800 22.73400 1.000 51.34355  ? 279 LYS   A O   1 
ATOM   2188 C  CB  . LYS   A 1 282 ? 45.20800 17.74800 22.57000 1.000 52.90525  ? 279 LYS   A CB  1 
ATOM   2189 C  CG  . LYS   A 1 282 ? 45.15600 19.17300 23.08300 1.000 72.96159  ? 279 LYS   A CG  1 
ATOM   2190 C  CD  . LYS   A 1 282 ? 45.50800 20.17400 22.00100 1.000 63.68238  ? 279 LYS   A CD  1 
ATOM   2191 C  CE  . LYS   A 1 282 ? 45.27800 21.60100 22.47700 1.000 57.87363  ? 279 LYS   A CE  1 
ATOM   2192 N  NZ  . LYS   A 1 282 ? 43.86000 21.83200 22.88400 1.000 64.83594  ? 279 LYS   A NZ  1 
ATOM   2193 N  N   . GLU   A 1 283 ? 45.70500 15.29400 23.62400 1.000 53.51386  ? 280 GLU   A N   1 
ATOM   2194 C  CA  . GLU   A 1 283 ? 45.66200 13.86800 23.93300 1.000 63.96905  ? 280 GLU   A CA  1 
ATOM   2195 C  C   . GLU   A 1 283 ? 45.51900 13.04900 22.65600 1.000 65.87229  ? 280 GLU   A C   1 
ATOM   2196 O  O   . GLU   A 1 283 ? 45.97000 11.89900 22.59800 1.000 69.50130  ? 280 GLU   A O   1 
ATOM   2197 C  CB  . GLU   A 1 283 ? 44.52500 13.56500 24.91500 1.000 52.57532  ? 280 GLU   A CB  1 
ATOM   2198 C  CG  . GLU   A 1 283 ? 43.19300 13.24800 24.26100 1.000 55.31969  ? 280 GLU   A CG  1 
ATOM   2199 C  CD  . GLU   A 1 283 ? 42.32800 14.47800 24.07800 1.000 62.83464  ? 280 GLU   A CD  1 
ATOM   2200 O  OE1 . GLU   A 1 283 ? 42.88200 15.59900 24.09100 1.000 61.70007  ? 280 GLU   A OE1 1 
ATOM   2201 O  OE2 . GLU   A 1 283 ? 41.10100 14.32600 23.89900 1.000 67.26421  ? 280 GLU   A OE2 1 
ATOM   2202 N  N   . THR   A 1 284 ? 44.91100 13.63600 21.62400 1.000 56.14084  ? 281 THR   A N   1 
ATOM   2203 C  CA  . THR   A 1 284 ? 44.89300 13.09500 20.27400 1.000 64.70572  ? 281 THR   A CA  1 
ATOM   2204 C  C   . THR   A 1 284 ? 45.01900 14.26800 19.30800 1.000 69.22840  ? 281 THR   A C   1 
ATOM   2205 O  O   . THR   A 1 284 ? 45.05600 15.43200 19.71900 1.000 66.04667  ? 281 THR   A O   1 
ATOM   2206 C  CB  . THR   A 1 284 ? 43.62300 12.27300 20.01700 1.000 55.93827  ? 281 THR   A CB  1 
ATOM   2207 O  OG1 . THR   A 1 284 ? 43.77100 11.51900 18.80800 1.000 61.41046  ? 281 THR   A OG1 1 
ATOM   2208 C  CG2 . THR   A 1 284 ? 42.40600 13.18200 19.90400 1.000 56.02243  ? 281 THR   A CG2 1 
ATOM   2209 N  N   . LEU   A 1 285 ? 45.09500 13.96800 18.01300 1.000 62.36466  ? 282 LEU   A N   1 
ATOM   2210 C  CA  . LEU   A 1 285 ? 45.23600 15.01600 17.01100 1.000 61.64082  ? 282 LEU   A CA  1 
ATOM   2211 C  C   . LEU   A 1 285 ? 43.88300 15.65900 16.73700 1.000 65.86019  ? 282 LEU   A C   1 
ATOM   2212 O  O   . LEU   A 1 285 ? 42.90800 14.97000 16.42200 1.000 63.08998  ? 282 LEU   A O   1 
ATOM   2213 C  CB  . LEU   A 1 285 ? 45.82900 14.45300 15.72000 1.000 54.36779  ? 282 LEU   A CB  1 
ATOM   2214 C  CG  . LEU   A 1 285 ? 47.25800 13.91600 15.82500 1.000 68.16902  ? 282 LEU   A CG  1 
ATOM   2215 C  CD1 . LEU   A 1 285 ? 47.69300 13.26100 14.51900 1.000 66.58515  ? 282 LEU   A CD1 1 
ATOM   2216 C  CD2 . LEU   A 1 285 ? 48.21900 15.02700 16.21900 1.000 59.21468  ? 282 LEU   A CD2 1 
ATOM   2217 N  N   . TYR   A 1 286 ? 43.82500 16.98000 16.86400 1.000 54.04719  ? 283 TYR   A N   1 
ATOM   2218 C  CA  . TYR   A 1 286 ? 42.60800 17.74400 16.63900 1.000 57.89772  ? 283 TYR   A CA  1 
ATOM   2219 C  C   . TYR   A 1 286 ? 42.78700 18.64700 15.42500 1.000 58.67674  ? 283 TYR   A C   1 
ATOM   2220 O  O   . TYR   A 1 286 ? 43.86200 19.21900 15.22000 1.000 54.14580  ? 283 TYR   A O   1 
ATOM   2221 C  CB  . TYR   A 1 286 ? 42.25700 18.59300 17.86300 1.000 55.72101  ? 283 TYR   A CB  1 
ATOM   2222 C  CG  . TYR   A 1 286 ? 41.60600 17.83700 18.99700 1.000 64.39118  ? 283 TYR   A CG  1 
ATOM   2223 C  CD1 . TYR   A 1 286 ? 40.25500 17.51900 18.95800 1.000 58.82190  ? 283 TYR   A CD1 1 
ATOM   2224 C  CD2 . TYR   A 1 286 ? 42.33800 17.45700 20.11600 1.000 67.72442  ? 283 TYR   A CD2 1 
ATOM   2225 C  CE1 . TYR   A 1 286 ? 39.65200 16.83600 19.99600 1.000 60.52995  ? 283 TYR   A CE1 1 
ATOM   2226 C  CE2 . TYR   A 1 286 ? 41.74300 16.77600 21.16100 1.000 54.14746  ? 283 TYR   A CE2 1 
ATOM   2227 C  CZ  . TYR   A 1 286 ? 40.40100 16.46700 21.09500 1.000 66.09650  ? 283 TYR   A CZ  1 
ATOM   2228 O  OH  . TYR   A 1 286 ? 39.80400 15.78800 22.13100 1.000 65.73980  ? 283 TYR   A OH  1 
ATOM   2229 N  N   . CYS   A 1 287 ? 41.73000 18.77200 14.62500 1.000 60.91276  ? 284 CYS   A N   1 
ATOM   2230 C  CA  . CYS   A 1 287 ? 41.71600 19.66000 13.46800 1.000 51.86034  ? 284 CYS   A CA  1 
ATOM   2231 C  C   . CYS   A 1 287 ? 40.64800 20.72100 13.68200 1.000 60.14016  ? 284 CYS   A C   1 
ATOM   2232 O  O   . CYS   A 1 287 ? 39.46500 20.39300 13.83000 1.000 62.19721  ? 284 CYS   A O   1 
ATOM   2233 C  CB  . CYS   A 1 287 ? 41.45200 18.88900 12.17500 1.000 67.79338  ? 284 CYS   A CB  1 
ATOM   2234 S  SG  . CYS   A 1 287 ? 41.26500 19.94600 10.71600 1.000 70.45763  ? 284 CYS   A SG  1 
ATOM   2235 N  N   . ILE   A 1 288 ? 41.06200 21.98400 13.69500 1.000 60.48316  ? 285 ILE   A N   1 
ATOM   2236 C  CA  . ILE   A 1 288 ? 40.16400 23.11100 13.91300 1.000 60.86547  ? 285 ILE   A CA  1 
ATOM   2237 C  C   . ILE   A 1 288 ? 40.02000 23.85600 12.59300 1.000 59.74875  ? 285 ILE   A C   1 
ATOM   2238 O  O   . ILE   A 1 288 ? 40.99300 24.42000 12.07700 1.000 69.55828  ? 285 ILE   A O   1 
ATOM   2239 C  CB  . ILE   A 1 288 ? 40.67400 24.03800 15.02200 1.000 56.88072  ? 285 ILE   A CB  1 
ATOM   2240 C  CG1 . ILE   A 1 288 ? 40.96000 23.23000 16.29000 1.000 56.23095  ? 285 ILE   A CG1 1 
ATOM   2241 C  CG2 . ILE   A 1 288 ? 39.66300 25.14500 15.29600 1.000 63.67731  ? 285 ILE   A CG2 1 
ATOM   2242 C  CD1 . ILE   A 1 288 ? 41.11400 24.06800 17.53200 1.000 45.10463  ? 285 ILE   A CD1 1 
ATOM   2243 N  N   . ASP   A 1 289 ? 38.80800 23.85500 12.04400 1.000 64.37481  ? 286 ASP   A N   1 
ATOM   2244 C  CA  . ASP   A 1 289 ? 38.47500 24.57700 10.81600 1.000 61.82541  ? 286 ASP   A CA  1 
ATOM   2245 C  C   . ASP   A 1 289 ? 37.43700 25.63200 11.17900 1.000 59.74583  ? 286 ASP   A C   1 
ATOM   2246 O  O   . ASP   A 1 289 ? 36.23500 25.44000 10.98000 1.000 61.29266  ? 286 ASP   A O   1 
ATOM   2247 C  CB  . ASP   A 1 289 ? 37.96400 23.61700 9.72300  1.000 55.53804  ? 286 ASP   A CB  1 
ATOM   2248 C  CG  . ASP   A 1 289 ? 37.75200 24.30900 8.38600  1.000 74.98366  ? 286 ASP   A CG  1 
ATOM   2249 O  OD1 . ASP   A 1 289 ? 38.31500 25.40500 8.18200  1.000 68.90471  ? 286 ASP   A OD1 1 
ATOM   2250 O  OD2 . ASP   A 1 289 ? 37.02200 23.75300 7.53700  1.000 83.75185  ? 286 ASP   A OD2 1 
ATOM   2251 N  N   . GLY   A 1 290 ? 37.90800 26.75100 11.72200 1.000 58.92758  ? 287 GLY   A N   1 
ATOM   2252 C  CA  . GLY   A 1 290 ? 37.01400 27.80700 12.14600 1.000 58.78152  ? 287 GLY   A CA  1 
ATOM   2253 C  C   . GLY   A 1 290 ? 36.16200 27.40500 13.33200 1.000 65.36814  ? 287 GLY   A C   1 
ATOM   2254 O  O   . GLY   A 1 290 ? 36.65400 27.33700 14.46100 1.000 63.46194  ? 287 GLY   A O   1 
ATOM   2255 N  N   . ALA   A 1 291 ? 34.87900 27.13400 13.09100 1.000 62.04828  ? 288 ALA   A N   1 
ATOM   2256 C  CA  . ALA   A 1 291 ? 33.98000 26.67400 14.13900 1.000 68.12943  ? 288 ALA   A CA  1 
ATOM   2257 C  C   . ALA   A 1 291 ? 33.84100 25.15900 14.18400 1.000 64.28553  ? 288 ALA   A C   1 
ATOM   2258 O  O   . ALA   A 1 291 ? 33.26400 24.63600 15.14300 1.000 74.72795  ? 288 ALA   A O   1 
ATOM   2259 C  CB  . ALA   A 1 291 ? 32.59300 27.30700 13.96700 1.000 51.39444  ? 288 ALA   A CB  1 
ATOM   2260 N  N   . LEU   A 1 292 ? 34.35300 24.44700 13.18300 1.000 64.41792  ? 289 LEU   A N   1 
ATOM   2261 C  CA  . LEU   A 1 292 ? 34.22700 22.99900 13.11600 1.000 67.90937  ? 289 LEU   A CA  1 
ATOM   2262 C  C   . LEU   A 1 292 ? 35.43700 22.33000 13.75400 1.000 66.79905  ? 289 LEU   A C   1 
ATOM   2263 O  O   . LEU   A 1 292 ? 36.56900 22.80800 13.62500 1.000 60.46722  ? 289 LEU   A O   1 
ATOM   2264 C  CB  . LEU   A 1 292 ? 34.08200 22.53500 11.66400 1.000 59.87698  ? 289 LEU   A CB  1 
ATOM   2265 C  CG  . LEU   A 1 292 ? 33.28600 23.44600 10.72700 1.000 74.04588  ? 289 LEU   A CG  1 
ATOM   2266 C  CD1 . LEU   A 1 292 ? 33.29900 22.89500 9.31000  1.000 80.28507  ? 289 LEU   A CD1 1 
ATOM   2267 C  CD2 . LEU   A 1 292 ? 31.85900 23.61800 11.22500 1.000 70.43811  ? 289 LEU   A CD2 1 
ATOM   2268 N  N   . LEU   A 1 293 ? 35.19100 21.21300 14.43400 1.000 64.48605  ? 290 LEU   A N   1 
ATOM   2269 C  CA  . LEU   A 1 293 ? 36.23200 20.47200 15.13200 1.000 66.48307  ? 290 LEU   A CA  1 
ATOM   2270 C  C   . LEU   A 1 293 ? 36.13300 18.99600 14.77800 1.000 70.03175  ? 290 LEU   A C   1 
ATOM   2271 O  O   . LEU   A 1 293 ? 35.05800 18.39700 14.88900 1.000 70.13462  ? 290 LEU   A O   1 
ATOM   2272 C  CB  . LEU   A 1 293 ? 36.11700 20.65600 16.64900 1.000 58.82458  ? 290 LEU   A CB  1 
ATOM   2273 C  CG  . LEU   A 1 293 ? 37.11000 19.86400 17.50100 1.000 58.37969  ? 290 LEU   A CG  1 
ATOM   2274 C  CD1 . LEU   A 1 293 ? 38.52800 20.34600 17.25000 1.000 59.82964  ? 290 LEU   A CD1 1 
ATOM   2275 C  CD2 . LEU   A 1 293 ? 36.75300 19.97900 18.97200 1.000 58.81536  ? 290 LEU   A CD2 1 
ATOM   2276 N  N   . THR   A 1 294 ? 37.25200 18.41800 14.35000 1.000 62.76642  ? 291 THR   A N   1 
ATOM   2277 C  CA  . THR   A 1 294 ? 37.35900 16.98900 14.10400 1.000 70.98144  ? 291 THR   A CA  1 
ATOM   2278 C  C   . THR   A 1 294 ? 38.61400 16.46600 14.78800 1.000 68.34264  ? 291 THR   A C   1 
ATOM   2279 O  O   . THR   A 1 294 ? 39.55900 17.21500 15.04900 1.000 71.38084  ? 291 THR   A O   1 
ATOM   2280 C  CB  . THR   A 1 294 ? 37.40600 16.66300 12.60300 1.000 71.10852  ? 291 THR   A CB  1 
ATOM   2281 O  OG1 . THR   A 1 294 ? 38.48800 17.37600 11.99100 1.000 64.83684  ? 291 THR   A OG1 1 
ATOM   2282 C  CG2 . THR   A 1 294 ? 36.09800 17.05200 11.92700 1.000 59.21424  ? 291 THR   A CG2 1 
ATOM   2283 N  N   . LYS   A 1 295 ? 38.61600 15.16800 15.08200 1.000 69.34072  ? 292 LYS   A N   1 
ATOM   2284 C  CA  . LYS   A 1 295 ? 39.74200 14.54400 15.76000 1.000 74.04162  ? 292 LYS   A CA  1 
ATOM   2285 C  C   . LYS   A 1 295 ? 40.04100 13.19000 15.13300 1.000 74.12579  ? 292 LYS   A C   1 
ATOM   2286 O  O   . LYS   A 1 295 ? 39.14900 12.51600 14.61200 1.000 82.11165  ? 292 LYS   A O   1 
ATOM   2287 C  CB  . LYS   A 1 295 ? 39.48100 14.38400 17.26600 1.000 72.14129  ? 292 LYS   A CB  1 
ATOM   2288 C  CG  . LYS   A 1 295 ? 38.35600 13.42600 17.62000 1.000 80.88959  ? 292 LYS   A CG  1 
ATOM   2289 C  CD  . LYS   A 1 295 ? 38.21700 13.29200 19.13000 1.000 88.33895  ? 292 LYS   A CD  1 
ATOM   2290 C  CE  . LYS   A 1 295 ? 37.59600 11.96000 19.51800 1.000 98.72379  ? 292 LYS   A CE  1 
ATOM   2291 N  NZ  . LYS   A 1 295 ? 37.51100 11.80100 20.99700 1.000 84.98319  ? 292 LYS   A NZ  1 
ATOM   2292 N  N   . SER   A 1 296 ? 41.31300 12.80500 15.18900 1.000 70.01165  ? 293 SER   A N   1 
ATOM   2293 C  CA  . SER   A 1 296 ? 41.76100 11.52900 14.65300 1.000 71.22460  ? 293 SER   A CA  1 
ATOM   2294 C  C   . SER   A 1 296 ? 43.06300 11.14300 15.34000 1.000 74.33671  ? 293 SER   A C   1 
ATOM   2295 O  O   . SER   A 1 296 ? 43.79700 12.00200 15.83400 1.000 67.72240  ? 293 SER   A O   1 
ATOM   2296 C  CB  . SER   A 1 296 ? 41.95400 11.59300 13.13400 1.000 69.55315  ? 293 SER   A CB  1 
ATOM   2297 O  OG  . SER   A 1 296 ? 42.97500 12.51300 12.78600 1.000 67.65821  ? 293 SER   A OG  1 
ATOM   2298 N  N   . SER   A 1 297 ? 43.33900 9.83700  15.36900 1.000 72.40255  ? 294 SER   A N   1 
ATOM   2299 C  CA  . SER   A 1 297 ? 44.58200 9.37000  15.97200 1.000 73.65056  ? 294 SER   A CA  1 
ATOM   2300 C  C   . SER   A 1 297 ? 45.78100 9.67000  15.08500 1.000 65.51336  ? 294 SER   A C   1 
ATOM   2301 O  O   . SER   A 1 297 ? 46.88700 9.89100  15.59300 1.000 69.20248  ? 294 SER   A O   1 
ATOM   2302 C  CB  . SER   A 1 297 ? 44.49900 7.87100  16.26200 1.000 64.69908  ? 294 SER   A CB  1 
ATOM   2303 O  OG  . SER   A 1 297 ? 43.39200 7.57300  17.09500 1.000 101.02641 ? 294 SER   A OG  1 
ATOM   2304 N  N   . GLU   A 1 298 ? 45.58600 9.68800  13.77000 1.000 75.33234  ? 295 GLU   A N   1 
ATOM   2305 C  CA  . GLU   A 1 298 ? 46.65900 9.93700  12.82300 1.000 78.75941  ? 295 GLU   A CA  1 
ATOM   2306 C  C   . GLU   A 1 298 ? 46.24600 11.04900 11.87000 1.000 71.01251  ? 295 GLU   A C   1 
ATOM   2307 O  O   . GLU   A 1 298 ? 45.06300 11.37000 11.73300 1.000 69.47033  ? 295 GLU   A O   1 
ATOM   2308 C  CB  . GLU   A 1 298 ? 47.01100 8.67200  12.03400 1.000 78.66259  ? 295 GLU   A CB  1 
ATOM   2309 C  CG  . GLU   A 1 298 ? 48.10700 7.83700  12.67100 1.000 81.19476  ? 295 GLU   A CG  1 
ATOM   2310 C  CD  . GLU   A 1 298 ? 49.49400 8.42400  12.46500 1.000 106.42061 ? 295 GLU   A CD  1 
ATOM   2311 O  OE1 . GLU   A 1 298 ? 49.61500 9.49800  11.83800 1.000 100.14849 ? 295 GLU   A OE1 1 
ATOM   2312 O  OE2 . GLU   A 1 298 ? 50.47100 7.79500  12.92700 1.000 100.03958 ? 295 GLU   A OE2 1 
ATOM   2313 N  N   . TYR   A 1 299 ? 47.24000 11.63700 11.21000 1.000 68.23239  ? 296 TYR   A N   1 
ATOM   2314 C  CA  . TYR   A 1 299 ? 46.97500 12.71400 10.26600 1.000 68.71286  ? 296 TYR   A CA  1 
ATOM   2315 C  C   . TYR   A 1 299 ? 48.01200 12.70500 9.15600  1.000 78.09756  ? 296 TYR   A C   1 
ATOM   2316 O  O   . TYR   A 1 299 ? 49.21600 12.63700 9.42200  1.000 64.58341  ? 296 TYR   A O   1 
ATOM   2317 C  CB  . TYR   A 1 299 ? 46.97600 14.08200 10.95500 1.000 70.45998  ? 296 TYR   A CB  1 
ATOM   2318 C  CG  . TYR   A 1 299 ? 46.78300 15.22200 9.98200  1.000 69.86290  ? 296 TYR   A CG  1 
ATOM   2319 C  CD1 . TYR   A 1 299 ? 45.51000 15.64200 9.62000  1.000 72.03168  ? 296 TYR   A CD1 1 
ATOM   2320 C  CD2 . TYR   A 1 299 ? 47.87300 15.86200 9.40400  1.000 70.36968  ? 296 TYR   A CD2 1 
ATOM   2321 C  CE1 . TYR   A 1 299 ? 45.32900 16.67700 8.72300  1.000 65.94147  ? 296 TYR   A CE1 1 
ATOM   2322 C  CE2 . TYR   A 1 299 ? 47.70200 16.89100 8.50600  1.000 70.33261  ? 296 TYR   A CE2 1 
ATOM   2323 C  CZ  . TYR   A 1 299 ? 46.43000 17.29600 8.16900  1.000 72.89044  ? 296 TYR   A CZ  1 
ATOM   2324 O  OH  . TYR   A 1 299 ? 46.26300 18.32500 7.27500  1.000 89.36432  ? 296 TYR   A OH  1 
ATOM   2325 N  N   . LYS   A 1 300 ? 47.53500 12.80900 7.91800  1.000 78.99831  ? 297 LYS   A N   1 
ATOM   2326 C  CA  . LYS   A 1 300 ? 48.39200 12.98600 6.75400  1.000 83.75152  ? 297 LYS   A CA  1 
ATOM   2327 C  C   . LYS   A 1 300 ? 47.70600 13.97300 5.82500  1.000 74.97078  ? 297 LYS   A C   1 
ATOM   2328 O  O   . LYS   A 1 300 ? 46.57000 13.73900 5.40000  1.000 73.71767  ? 297 LYS   A O   1 
ATOM   2329 C  CB  . LYS   A 1 300 ? 48.65100 11.65500 6.04200  1.000 84.23044  ? 297 LYS   A CB  1 
ATOM   2330 C  CG  . LYS   A 1 300 ? 49.46800 11.78800 4.76500  1.000 103.11458 ? 297 LYS   A CG  1 
ATOM   2331 C  CD  . LYS   A 1 300 ? 50.68100 10.86600 4.76500  1.000 108.86721 ? 297 LYS   A CD  1 
ATOM   2332 C  CE  . LYS   A 1 300 ? 50.31000 9.45800  5.21500  1.000 119.56422 ? 297 LYS   A CE  1 
ATOM   2333 N  NZ  . LYS   A 1 300 ? 51.47900 8.69600  5.73800  1.000 100.62395 ? 297 LYS   A NZ  1 
ATOM   2334 N  N   . GLY   A 1 301 ? 48.38000 15.07900 5.52300  1.000 72.36404  ? 298 GLY   A N   1 
ATOM   2335 C  CA  . GLY   A 1 301 ? 47.79600 16.11500 4.70700  1.000 58.45328  ? 298 GLY   A CA  1 
ATOM   2336 C  C   . GLY   A 1 301 ? 48.80200 17.16000 4.27400  1.000 66.00610  ? 298 GLY   A C   1 
ATOM   2337 O  O   . GLY   A 1 301 ? 49.99200 17.08900 4.60200  1.000 60.61286  ? 298 GLY   A O   1 
ATOM   2338 N  N   . PRO   A 1 302 ? 48.33700 18.16000 3.52000  1.000 63.93294  ? 299 PRO   A N   1 
ATOM   2339 C  CA  . PRO   A 1 302 ? 49.22700 19.22600 3.03800  1.000 65.15262  ? 299 PRO   A CA  1 
ATOM   2340 C  C   . PRO   A 1 302 ? 49.50600 20.23400 4.14000  1.000 70.52445  ? 299 PRO   A C   1 
ATOM   2341 O  O   . PRO   A 1 302 ? 48.63900 21.03400 4.51100  1.000 58.15591  ? 299 PRO   A O   1 
ATOM   2342 C  CB  . PRO   A 1 302 ? 48.42900 19.84300 1.88100  1.000 47.86897  ? 299 PRO   A CB  1 
ATOM   2343 C  CG  . PRO   A 1 302 ? 47.00000 19.59900 2.23600  1.000 63.02883  ? 299 PRO   A CG  1 
ATOM   2344 C  CD  . PRO   A 1 302 ? 46.94100 18.35400 3.08900  1.000 64.00152  ? 299 PRO   A CD  1 
ATOM   2345 N  N   . ILE   A 1 303 ? 50.72400 20.19800 4.67200  1.000 49.29690  ? 300 ILE   A N   1 
ATOM   2346 C  CA  . ILE   A 1 303 ? 51.13700 21.03400 5.79100  1.000 54.60072  ? 300 ILE   A CA  1 
ATOM   2347 C  C   . ILE   A 1 303 ? 52.15800 22.04200 5.28500  1.000 60.34062  ? 300 ILE   A C   1 
ATOM   2348 O  O   . ILE   A 1 303 ? 53.02900 21.70000 4.47700  1.000 58.94637  ? 300 ILE   A O   1 
ATOM   2349 C  CB  . ILE   A 1 303 ? 51.72300 20.18200 6.93700  1.000 59.89903  ? 300 ILE   A CB  1 
ATOM   2350 C  CG1 . ILE   A 1 303 ? 50.64100 19.32500 7.60000  1.000 54.21338  ? 300 ILE   A CG1 1 
ATOM   2351 C  CG2 . ILE   A 1 303 ? 52.37500 21.06400 7.98500  1.000 57.52488  ? 300 ILE   A CG2 1 
ATOM   2352 C  CD1 . ILE   A 1 303 ? 49.26400 19.94800 7.60800  1.000 61.83478  ? 300 ILE   A CD1 1 
ATOM   2353 N  N   . THR   A 1 304 ? 52.05000 23.28700 5.75700  1.000 56.61786  ? 301 THR   A N   1 
ATOM   2354 C  CA  . THR   A 1 304 ? 52.98900 24.32900 5.37100  1.000 59.08838  ? 301 THR   A CA  1 
ATOM   2355 C  C   . THR   A 1 304 ? 53.71200 24.98300 6.54400  1.000 48.15659  ? 301 THR   A C   1 
ATOM   2356 O  O   . THR   A 1 304 ? 54.77900 25.56700 6.33000  1.000 60.71922  ? 301 THR   A O   1 
ATOM   2357 C  CB  . THR   A 1 304 ? 52.27700 25.41100 4.53800  1.000 59.93164  ? 301 THR   A CB  1 
ATOM   2358 O  OG1 . THR   A 1 304 ? 53.24000 26.34400 4.02900  1.000 52.80868  ? 301 THR   A OG1 1 
ATOM   2359 C  CG2 . THR   A 1 304 ? 51.23700 26.15000 5.36900  1.000 48.19229  ? 301 THR   A CG2 1 
ATOM   2360 N  N   . ASP   A 1 305 ? 53.18300 24.89200 7.76700  1.000 57.74070  ? 302 ASP   A N   1 
ATOM   2361 C  CA  . ASP   A 1 305 ? 53.88500 25.34600 8.96300  1.000 52.25084  ? 302 ASP   A CA  1 
ATOM   2362 C  C   . ASP   A 1 305 ? 53.74500 24.30200 10.06200 1.000 60.58616  ? 302 ASP   A C   1 
ATOM   2363 O  O   . ASP   A 1 305 ? 52.68500 23.69000 10.20900 1.000 59.01596  ? 302 ASP   A O   1 
ATOM   2364 C  CB  . ASP   A 1 305 ? 53.34400 26.68600 9.48600  1.000 61.81789  ? 302 ASP   A CB  1 
ATOM   2365 C  CG  . ASP   A 1 305 ? 53.25500 27.74700 8.41100  1.000 63.49960  ? 302 ASP   A CG  1 
ATOM   2366 O  OD1 . ASP   A 1 305 ? 54.30600 28.11700 7.84400  1.000 66.97274  ? 302 ASP   A OD1 1 
ATOM   2367 O  OD2 . ASP   A 1 305 ? 52.13100 28.21900 8.14100  1.000 65.45659  ? 302 ASP   A OD2 1 
ATOM   2368 N  N   . VAL   A 1 306 ? 54.81400 24.10600 10.83500 1.000 57.88525  ? 303 VAL   A N   1 
ATOM   2369 C  CA  . VAL   A 1 306 ? 54.77900 23.26600 12.03000 1.000 56.83235  ? 303 VAL   A CA  1 
ATOM   2370 C  C   . VAL   A 1 306 ? 55.49600 24.00300 13.15400 1.000 54.18701  ? 303 VAL   A C   1 
ATOM   2371 O  O   . VAL   A 1 306 ? 56.58400 24.55200 12.94700 1.000 54.27034  ? 303 VAL   A O   1 
ATOM   2372 C  CB  . VAL   A 1 306 ? 55.42300 21.88100 11.80800 1.000 64.86004  ? 303 VAL   A CB  1 
ATOM   2373 C  CG1 . VAL   A 1 306 ? 55.21500 21.00600 13.03800 1.000 55.38746  ? 303 VAL   A CG1 1 
ATOM   2374 C  CG2 . VAL   A 1 306 ? 54.84900 21.19600 10.57400 1.000 41.47481  ? 303 VAL   A CG2 1 
ATOM   2375 N  N   . PHE   A 1 307 ? 54.89200 24.00900 14.34100 1.000 51.19149  ? 304 PHE   A N   1 
ATOM   2376 C  CA  . PHE   A 1 307 ? 55.44900 24.66300 15.51700 1.000 66.78168  ? 304 PHE   A CA  1 
ATOM   2377 C  C   . PHE   A 1 307 ? 55.86900 23.61900 16.54500 1.000 54.91811  ? 304 PHE   A C   1 
ATOM   2378 O  O   . PHE   A 1 307 ? 55.14300 22.65100 16.79300 1.000 54.62631  ? 304 PHE   A O   1 
ATOM   2379 C  CB  . PHE   A 1 307 ? 54.43700 25.63400 16.13700 1.000 50.64546  ? 304 PHE   A CB  1 
ATOM   2380 C  CG  . PHE   A 1 307 ? 54.11100 26.81200 15.25800 1.000 63.60287  ? 304 PHE   A CG  1 
ATOM   2381 C  CD1 . PHE   A 1 307 ? 53.22100 26.68200 14.20200 1.000 60.38240  ? 304 PHE   A CD1 1 
ATOM   2382 C  CD2 . PHE   A 1 307 ? 54.69800 28.04700 15.48400 1.000 55.94647  ? 304 PHE   A CD2 1 
ATOM   2383 C  CE1 . PHE   A 1 307 ? 52.92200 27.76200 13.38600 1.000 56.43336  ? 304 PHE   A CE1 1 
ATOM   2384 C  CE2 . PHE   A 1 307 ? 54.40200 29.13000 14.67500 1.000 53.55509  ? 304 PHE   A CE2 1 
ATOM   2385 C  CZ  . PHE   A 1 307 ? 53.51400 28.98700 13.62500 1.000 53.48746  ? 304 PHE   A CZ  1 
ATOM   2386 N  N   . TYR   A 1 308 ? 57.04500 23.81900 17.13800 1.000 51.23369  ? 305 TYR   A N   1 
ATOM   2387 C  CA  . TYR   A 1 308 ? 57.59400 22.90600 18.13100 1.000 56.57458  ? 305 TYR   A CA  1 
ATOM   2388 C  C   . TYR   A 1 308 ? 57.94300 23.67100 19.39900 1.000 61.49079  ? 305 TYR   A C   1 
ATOM   2389 O  O   . TYR   A 1 308 ? 58.18100 24.88100 19.37500 1.000 60.06820  ? 305 TYR   A O   1 
ATOM   2390 C  CB  . TYR   A 1 308 ? 58.85100 22.18400 17.61700 1.000 55.39668  ? 305 TYR   A CB  1 
ATOM   2391 C  CG  . TYR   A 1 308 ? 58.66800 21.42000 16.32500 1.000 70.71076  ? 305 TYR   A CG  1 
ATOM   2392 C  CD1 . TYR   A 1 308 ? 58.78400 22.05500 15.09400 1.000 60.68060  ? 305 TYR   A CD1 1 
ATOM   2393 C  CD2 . TYR   A 1 308 ? 58.39500 20.05800 16.33700 1.000 62.86047  ? 305 TYR   A CD2 1 
ATOM   2394 C  CE1 . TYR   A 1 308 ? 58.62500 21.35500 13.91000 1.000 57.82484  ? 305 TYR   A CE1 1 
ATOM   2395 C  CE2 . TYR   A 1 308 ? 58.23300 19.35100 15.15900 1.000 63.56476  ? 305 TYR   A CE2 1 
ATOM   2396 C  CZ  . TYR   A 1 308 ? 58.35100 20.00300 13.95000 1.000 65.86789  ? 305 TYR   A CZ  1 
ATOM   2397 O  OH  . TYR   A 1 308 ? 58.19000 19.29900 12.77800 1.000 60.23562  ? 305 TYR   A OH  1 
ATOM   2398 N  N   . LYS   A 1 309 ? 57.98000 22.94600 20.51300 1.000 67.08379  ? 306 LYS   A N   1 
ATOM   2399 C  CA  . LYS   A 1 309 ? 58.41100 23.50900 21.78200 1.000 60.48342  ? 306 LYS   A CA  1 
ATOM   2400 C  C   . LYS   A 1 309 ? 59.93000 23.43400 21.90500 1.000 60.90921  ? 306 LYS   A C   1 
ATOM   2401 O  O   . LYS   A 1 309 ? 60.58800 22.58900 21.29100 1.000 61.84415  ? 306 LYS   A O   1 
ATOM   2402 C  CB  . LYS   A 1 309 ? 57.75400 22.77800 22.95500 1.000 56.94111  ? 306 LYS   A CB  1 
ATOM   2403 C  CG  . LYS   A 1 309 ? 56.27300 23.08700 23.13100 1.000 68.84553  ? 306 LYS   A CG  1 
ATOM   2404 C  CD  . LYS   A 1 309 ? 56.02600 24.58300 23.24800 1.000 72.08662  ? 306 LYS   A CD  1 
ATOM   2405 C  CE  . LYS   A 1 309 ? 54.71700 24.88400 23.96600 1.000 63.61672  ? 306 LYS   A CE  1 
ATOM   2406 N  NZ  . LYS   A 1 309 ? 53.87700 23.66800 24.15100 1.000 54.76688  ? 306 LYS   A NZ  1 
ATOM   2407 N  N   . GLU   A 1 310 ? 60.48300 24.33200 22.71500 1.000 66.31894  ? 307 GLU   A N   1 
ATOM   2408 C  CA  . GLU   A 1 310 ? 61.92600 24.40700 22.89900 1.000 73.68610  ? 307 GLU   A CA  1 
ATOM   2409 C  C   . GLU   A 1 310 ? 62.21100 25.24300 24.13900 1.000 74.08406  ? 307 GLU   A C   1 
ATOM   2410 O  O   . GLU   A 1 310 ? 61.36800 26.02000 24.59200 1.000 80.94122  ? 307 GLU   A O   1 
ATOM   2411 C  CB  . GLU   A 1 310 ? 62.61200 25.00000 21.65800 1.000 66.94071  ? 307 GLU   A CB  1 
ATOM   2412 C  CG  . GLU   A 1 310 ? 64.13800 25.00200 21.68800 1.000 73.63880  ? 307 GLU   A CG  1 
ATOM   2413 C  CD  . GLU   A 1 310 ? 64.73200 23.61300 21.54600 1.000 84.59958  ? 307 GLU   A CD  1 
ATOM   2414 O  OE1 . GLU   A 1 310 ? 64.97900 23.18400 20.39900 1.000 84.32497  ? 307 GLU   A OE1 1 
ATOM   2415 O  OE2 . GLU   A 1 310 ? 64.95800 22.95200 22.58200 1.000 92.77962  ? 307 GLU   A OE2 1 
ATOM   2416 N  N   . ASN   A 1 311 ? 63.40400 25.04800 24.69800 1.000 68.76241  ? 308 ASN   A N   1 
ATOM   2417 C  CA  . ASN   A 1 311 ? 63.92000 25.91900 25.74700 1.000 77.34623  ? 308 ASN   A CA  1 
ATOM   2418 C  C   . ASN   A 1 311 ? 65.40500 26.15000 25.51100 1.000 76.78959  ? 308 ASN   A C   1 
ATOM   2419 O  O   . ASN   A 1 311 ? 65.84500 27.29000 25.33100 1.000 81.93868  ? 308 ASN   A O   1 
ATOM   2420 C  CB  . ASN   A 1 311 ? 63.67600 25.32100 27.13600 1.000 81.06120  ? 308 ASN   A CB  1 
ATOM   2421 C  CG  . ASN   A 1 311 ? 64.18800 26.21700 28.25700 1.000 94.76990  ? 308 ASN   A CG  1 
ATOM   2422 O  OD1 . ASN   A 1 311 ? 63.72200 27.34500 28.43400 1.000 77.56570  ? 308 ASN   A OD1 1 
ATOM   2423 N  ND2 . ASN   A 1 311 ? 65.15100 25.71300 29.02200 1.000 99.53197  ? 308 ASN   A ND2 1 
ATOM   2424 N  N   . SER   A 1 312 ? 66.17800 25.06700 25.50200 1.000 86.36348  ? 309 SER   A N   1 
ATOM   2425 C  CA  . SER   A 1 312 ? 67.60300 25.13200 25.21500 1.000 89.67107  ? 309 SER   A CA  1 
ATOM   2426 C  C   . SER   A 1 312 ? 68.01200 23.83300 24.53900 1.000 77.82280  ? 309 SER   A C   1 
ATOM   2427 O  O   . SER   A 1 312 ? 67.63400 22.75000 24.99500 1.000 93.45412  ? 309 SER   A O   1 
ATOM   2428 C  CB  . SER   A 1 312 ? 68.42000 25.35700 26.49300 1.000 88.80348  ? 309 SER   A CB  1 
ATOM   2429 O  OG  . SER   A 1 312 ? 69.76500 25.67900 26.18800 1.000 91.35573  ? 309 SER   A OG  1 
ATOM   2430 N  N   . TYR   A 1 313 ? 68.76900 23.94600 23.45200 1.000 80.23306  ? 310 TYR   A N   1 
ATOM   2431 C  CA  . TYR   A 1 313 ? 69.20700 22.78700 22.68700 1.000 78.96463  ? 310 TYR   A CA  1 
ATOM   2432 C  C   . TYR   A 1 313 ? 70.64500 22.99400 22.24300 1.000 84.42090  ? 310 TYR   A C   1 
ATOM   2433 O  O   . TYR   A 1 313 ? 70.99500 24.06900 21.74900 1.000 88.96601  ? 310 TYR   A O   1 
ATOM   2434 C  CB  . TYR   A 1 313 ? 68.30700 22.55100 21.46900 1.000 79.52800  ? 310 TYR   A CB  1 
ATOM   2435 C  CG  . TYR   A 1 313 ? 68.82400 21.49600 20.51600 1.000 83.28099  ? 310 TYR   A CG  1 
ATOM   2436 C  CD1 . TYR   A 1 313 ? 68.56800 20.14900 20.73700 1.000 84.05727  ? 310 TYR   A CD1 1 
ATOM   2437 C  CD2 . TYR   A 1 313 ? 69.56200 21.84700 19.39100 1.000 88.56717  ? 310 TYR   A CD2 1 
ATOM   2438 C  CE1 . TYR   A 1 313 ? 69.03800 19.18100 19.86800 1.000 88.00578  ? 310 TYR   A CE1 1 
ATOM   2439 C  CE2 . TYR   A 1 313 ? 70.03600 20.88600 18.51800 1.000 82.31894  ? 310 TYR   A CE2 1 
ATOM   2440 C  CZ  . TYR   A 1 313 ? 69.77000 19.55600 18.76100 1.000 84.88959  ? 310 TYR   A CZ  1 
ATOM   2441 O  OH  . TYR   A 1 313 ? 70.23800 18.59800 17.89300 1.000 92.81085  ? 310 TYR   A OH  1 
ATOM   2442 N  N   . THR   A 1 314 ? 71.46900 21.96500 22.41900 1.000 87.31971  ? 311 THR   A N   1 
ATOM   2443 C  CA  . THR   A 1 314 ? 72.84700 21.96300 21.94600 1.000 82.34198  ? 311 THR   A CA  1 
ATOM   2444 C  C   . THR   A 1 314 ? 73.10300 20.65000 21.22400 1.000 92.18439  ? 311 THR   A C   1 
ATOM   2445 O  O   . THR   A 1 314 ? 72.81800 19.57700 21.76500 1.000 99.79033  ? 311 THR   A O   1 
ATOM   2446 C  CB  . THR   A 1 314 ? 73.84300 22.13900 23.09600 1.000 74.72075  ? 311 THR   A CB  1 
ATOM   2447 O  OG1 . THR   A 1 314 ? 73.59800 23.38500 23.76200 1.000 79.83065  ? 311 THR   A OG1 1 
ATOM   2448 C  CG2 . THR   A 1 314 ? 75.26800 22.12600 22.56600 1.000 82.22980  ? 311 THR   A CG2 1 
ATOM   2449 N  N   . THR   A 1 315 ? 73.63500 20.73800 20.00900 1.000 95.15698  ? 312 THR   A N   1 
ATOM   2450 C  CA  . THR   A 1 315 ? 73.83600 19.55100 19.19500 1.000 105.10102 ? 312 THR   A CA  1 
ATOM   2451 C  C   . THR   A 1 315 ? 74.96600 18.69000 19.75600 1.000 108.82155 ? 312 THR   A C   1 
ATOM   2452 O  O   . THR   A 1 315 ? 75.77600 19.12800 20.57900 1.000 94.81170  ? 312 THR   A O   1 
ATOM   2453 C  CB  . THR   A 1 315 ? 74.14800 19.93600 17.74800 1.000 96.49707  ? 312 THR   A CB  1 
ATOM   2454 O  OG1 . THR   A 1 315 ? 74.15700 18.75900 16.93100 1.000 95.47422  ? 312 THR   A OG1 1 
ATOM   2455 C  CG2 . THR   A 1 315 ? 75.50600 20.61600 17.66100 1.000 93.00376  ? 312 THR   A CG2 1 
ATOM   2456 N  N   . THR   A 1 316 ? 75.00700 17.44000 19.29600 1.000 117.84547 ? 313 THR   A N   1 
ATOM   2457 C  CA  . THR   A 1 316 ? 76.04100 16.48900 19.68100 1.000 120.20145 ? 313 THR   A CA  1 
ATOM   2458 C  C   . THR   A 1 316 ? 77.01700 16.20100 18.54700 1.000 125.09951 ? 313 THR   A C   1 
ATOM   2459 O  O   . THR   A 1 316 ? 77.87500 15.32200 18.68800 1.000 134.51540 ? 313 THR   A O   1 
ATOM   2460 C  CB  . THR   A 1 316 ? 75.40900 15.18200 20.16800 1.000 109.36305 ? 313 THR   A CB  1 
ATOM   2461 O  OG1 . THR   A 1 316 ? 74.64900 14.59100 19.10500 1.000 111.75580 ? 313 THR   A OG1 1 
ATOM   2462 C  CG2 . THR   A 1 316 ? 74.49400 15.43900 21.35700 1.000 91.94124  ? 313 THR   A CG2 1 
ATOM   2463 N  N   . ILE   A 1 317 ? 76.90700 16.91400 17.43000 1.000 123.31417 ? 314 ILE   A N   1 
ATOM   2464 C  CA  . ILE   A 1 317 ? 77.79400 16.70000 16.29200 1.000 128.69162 ? 314 ILE   A CA  1 
ATOM   2465 C  C   . ILE   A 1 317 ? 79.12800 17.38100 16.56800 1.000 134.20393 ? 314 ILE   A C   1 
ATOM   2466 O  O   . ILE   A 1 317 ? 79.17300 18.55400 16.95800 1.000 125.81165 ? 314 ILE   A O   1 
ATOM   2467 C  CB  . ILE   A 1 317 ? 77.15200 17.22700 14.99700 1.000 128.43415 ? 314 ILE   A CB  1 
ATOM   2468 C  CG1 . ILE   A 1 317 ? 76.20100 16.18100 14.40900 1.000 122.46920 ? 314 ILE   A CG1 1 
ATOM   2469 C  CG2 . ILE   A 1 317 ? 78.21700 17.61000 13.97700 1.000 125.98463 ? 314 ILE   A CG2 1 
ATOM   2470 C  CD1 . ILE   A 1 317 ? 76.86500 14.85600 14.09400 1.000 113.82430 ? 314 ILE   A CD1 1 
ATOM   2471 N  N   . LYS   A 1 318 ? 80.21700 16.64300 16.37500 1.000 142.38958 ? 315 LYS   A N   1 
ATOM   2472 C  CA  . LYS   A 1 318 ? 81.55500 17.17700 16.60000 1.000 141.78802 ? 315 LYS   A CA  1 
ATOM   2473 C  C   . LYS   A 1 318 ? 81.98200 18.08800 15.45400 1.000 139.01782 ? 315 LYS   A C   1 
ATOM   2474 O  O   . LYS   A 1 318 ? 82.69200 19.07300 15.65700 1.000 127.11340 ? 315 LYS   A O   1 
ATOM   2475 C  CB  . LYS   A 1 318 ? 82.56400 16.03900 16.77300 1.000 132.86068 ? 315 LYS   A CB  1 
ATOM   2476 O  OXT . LYS   A 1 318 ? 81.62600 17.86100 14.29700 1.000 135.74515 ? 315 LYS   A OXT 1 
HETATM 2477 C  C13 . A1BF2 B 2 .   ? 48.54300 33.34800 0.76200  1.000 51.35198  ? 401 A1BF2 A C13 1 
HETATM 2478 C  C15 . A1BF2 B 2 .   ? 49.33800 35.51600 0.27100  1.000 43.25404  ? 401 A1BF2 A C15 1 
HETATM 2479 C  C21 . A1BF2 B 2 .   ? 54.99600 38.67100 -0.64100 1.000 61.65870  ? 401 A1BF2 A C21 1 
HETATM 2480 C  C22 . A1BF2 B 2 .   ? 55.05800 37.72700 -1.61100 1.000 66.36503  ? 401 A1BF2 A C22 1 
HETATM 2481 C  C24 . A1BF2 B 2 .   ? 52.79200 39.40900 -0.02000 1.000 63.36087  ? 401 A1BF2 A C24 1 
HETATM 2482 C  C26 . A1BF2 B 2 .   ? 47.53600 32.44400 1.36800  1.000 53.01946  ? 401 A1BF2 A C26 1 
HETATM 2483 C  C28 . A1BF2 B 2 .   ? 51.29800 28.60100 2.28600  1.000 54.34884  ? 401 A1BF2 A C28 1 
HETATM 2484 C  C01 . A1BF2 B 2 .   ? 58.36600 31.63800 0.74800  1.000 73.97865  ? 401 A1BF2 A C01 1 
HETATM 2485 C  C04 . A1BF2 B 2 .   ? 56.90000 29.14700 -1.33100 1.000 63.90750  ? 401 A1BF2 A C04 1 
HETATM 2486 C  C05 . A1BF2 B 2 .   ? 55.78300 29.64100 -0.64800 1.000 69.32299  ? 401 A1BF2 A C05 1 
HETATM 2487 C  C06 . A1BF2 B 2 .   ? 54.32300 29.14500 -0.85400 1.000 52.40858  ? 401 A1BF2 A C06 1 
HETATM 2488 C  C07 . A1BF2 B 2 .   ? 53.34900 29.39200 0.12200  1.000 54.88708  ? 401 A1BF2 A C07 1 
HETATM 2489 C  C08 . A1BF2 B 2 .   ? 52.04900 28.92200 -0.11600 1.000 60.48858  ? 401 A1BF2 A C08 1 
HETATM 2490 C  C09 . A1BF2 B 2 .   ? 50.90700 29.15400 0.91900  1.000 66.29728  ? 401 A1BF2 A C09 1 
HETATM 2491 C  C11 . A1BF2 B 2 .   ? 49.84400 31.25000 0.00300  1.000 63.00250  ? 401 A1BF2 A C11 1 
HETATM 2492 C  C12 . A1BF2 B 2 .   ? 49.65500 32.79700 0.10100  1.000 46.32226  ? 401 A1BF2 A C12 1 
HETATM 2493 C  C14 . A1BF2 B 2 .   ? 48.39900 34.70500 0.83200  1.000 53.23715  ? 401 A1BF2 A C14 1 
HETATM 2494 C  C16 . A1BF2 B 2 .   ? 50.44200 34.94800 -0.37400 1.000 54.56739  ? 401 A1BF2 A C16 1 
HETATM 2495 C  C18 . A1BF2 B 2 .   ? 51.69700 36.98000 -0.37200 1.000 50.81805  ? 401 A1BF2 A C18 1 
HETATM 2496 C  C19 . A1BF2 B 2 .   ? 53.25900 37.06500 -0.50000 1.000 66.82949  ? 401 A1BF2 A C19 1 
HETATM 2497 C  C23 . A1BF2 B 2 .   ? 53.62300 37.16700 -1.74300 1.000 66.46965  ? 401 A1BF2 A C23 1 
HETATM 2498 C  C25 . A1BF2 B 2 .   ? 50.58500 33.59000 -0.45100 1.000 54.64280  ? 401 A1BF2 A C25 1 
HETATM 2499 C  C29 . A1BF2 B 2 .   ? 51.79600 28.22000 -1.36900 1.000 53.63383  ? 401 A1BF2 A C29 1 
HETATM 2500 C  C30 . A1BF2 B 2 .   ? 50.49200 27.73400 -1.64300 1.000 59.72643  ? 401 A1BF2 A C30 1 
HETATM 2501 C  C31 . A1BF2 B 2 .   ? 50.23200 27.04400 -2.84800 1.000 72.92771  ? 401 A1BF2 A C31 1 
HETATM 2502 C  C32 . A1BF2 B 2 .   ? 51.27900 26.83900 -3.79000 1.000 60.44982  ? 401 A1BF2 A C32 1 
HETATM 2503 C  C33 . A1BF2 B 2 .   ? 52.55300 27.30900 -3.52200 1.000 59.88977  ? 401 A1BF2 A C33 1 
HETATM 2504 C  C34 . A1BF2 B 2 .   ? 52.81000 28.01400 -2.27800 1.000 53.69646  ? 401 A1BF2 A C34 1 
HETATM 2505 C  C36 . A1BF2 B 2 .   ? 56.20500 30.62700 0.19900  1.000 70.60098  ? 401 A1BF2 A C36 1 
HETATM 2506 N  N02 . A1BF2 B 2 .   ? 57.52200 30.72500 0.04300  1.000 83.63432  ? 401 A1BF2 A N02 1 
HETATM 2507 N  N03 . A1BF2 B 2 .   ? 57.97000 29.82800 -0.88800 1.000 79.01487  ? 401 A1BF2 A N03 1 
HETATM 2508 N  N10 . A1BF2 B 2 .   ? 50.73000 30.56800 1.02400  1.000 57.74365  ? 401 A1BF2 A N10 1 
HETATM 2509 N  N20 . A1BF2 B 2 .   ? 53.78600 38.36100 0.14000  1.000 56.09816  ? 401 A1BF2 A N20 1 
HETATM 2510 N  N35 . A1BF2 B 2 .   ? 54.04700 28.47800 -2.01200 1.000 57.07485  ? 401 A1BF2 A N35 1 
HETATM 2511 O  O17 . A1BF2 B 2 .   ? 51.41400 35.72800 -0.98300 1.000 68.84556  ? 401 A1BF2 A O17 1 
HETATM 2512 O  O27 . A1BF2 B 2 .   ? 49.30400 30.62500 -0.86500 1.000 59.11343  ? 401 A1BF2 A O27 1 
HETATM 2513 C  C1  . PEG   C 3 .   ? 35.62800 27.10100 3.49500  1.000 92.77849  ? 402 PEG   A C1  1 
HETATM 2514 O  O1  . PEG   C 3 .   ? 35.51100 28.46800 3.13700  1.000 104.24994 ? 402 PEG   A O1  1 
HETATM 2515 C  C2  . PEG   C 3 .   ? 34.35600 26.58300 4.09500  1.000 100.01367 ? 402 PEG   A C2  1 
HETATM 2516 O  O2  . PEG   C 3 .   ? 34.65700 25.72700 5.18900  1.000 111.76242 ? 402 PEG   A O2  1 
HETATM 2517 C  C3  . PEG   C 3 .   ? 34.30500 26.28600 6.44800  1.000 97.73868  ? 402 PEG   A C3  1 
HETATM 2518 C  C4  . PEG   C 3 .   ? 35.53500 26.81300 7.12400  1.000 98.25018  ? 402 PEG   A C4  1 
HETATM 2519 O  O4  . PEG   C 3 .   ? 35.25000 27.30800 8.42300  1.000 78.85777  ? 402 PEG   A O4  1 
HETATM 2520 ZN ZN  . ZN    D 4 .   ? 81.94200 26.32700 -0.85900 1.000 137.51895 ? 403 ZN    A ZN  1 
HETATM 2521 ZN ZN  . ZN    E 4 .   ? 57.88100 48.69000 19.92200 1.000 52.75742  ? 404 ZN    A ZN  1 
HETATM 2522 ZN ZN  . ZN    F 4 .   ? 32.83800 41.99300 7.42800  1.000 78.45612  ? 405 ZN    A ZN  1 
HETATM 2523 ZN ZN  . ZN    G 4 .   ? 54.93100 47.68500 12.60300 1.000 112.08610 ? 406 ZN    A ZN  1 
HETATM 2524 ZN ZN  . ZN    H 4 .   ? 83.79300 29.56500 1.01300  1.000 167.56783 ? 407 ZN    A ZN  1 
HETATM 2525 ZN ZN  . ZN    I 4 .   ? 40.00600 30.75300 3.82400  1.000 77.51595  ? 408 ZN    A ZN  1 
HETATM 2526 CL CL  . CL    J 5 .   ? 58.84400 50.40000 18.59600 1.000 54.04888  ? 409 CL    A CL  1 
HETATM 2527 CL CL  . CL    K 5 .   ? 57.04000 47.04600 18.61200 1.000 50.88708  ? 410 CL    A CL  1 
HETATM 2528 CL CL  . CL    L 5 .   ? 56.18900 48.98100 14.66300 1.000 115.30017 ? 411 CL    A CL  1 
HETATM 2529 CL CL  . CL    M 5 .   ? 55.41500 46.86800 10.44100 1.000 128.18481 ? 412 CL    A CL  1 
HETATM 2530 CL CL  . CL    N 5 .   ? 37.99700 31.47900 4.89800  1.000 72.87389  ? 413 CL    A CL  1 
HETATM 2531 O  O   . HOH   O 6 .   ? 54.46500 33.38800 1.74400  1.000 65.87371  ? 501 HOH   A O   1 
HETATM 2532 O  O   . HOH   O 6 .   ? 37.71000 19.28400 23.28900 1.000 74.03495  ? 502 HOH   A O   1 
HETATM 2533 O  O   . HOH   O 6 .   ? 36.32700 24.08000 4.83500  1.000 79.16610  ? 503 HOH   A O   1 
HETATM 2534 O  O   . HOH   O 6 .   ? 49.54100 61.67000 28.74300 1.000 65.81715  ? 504 HOH   A O   1 
HETATM 2535 O  O   . HOH   O 6 .   ? 57.92000 37.11700 23.77700 1.000 66.23006  ? 505 HOH   A O   1 
HETATM 2536 O  O   . HOH   O 6 .   ? 50.10600 15.79700 22.43300 1.000 48.99393  ? 506 HOH   A O   1 
HETATM 2537 O  O   . HOH   O 6 .   ? 46.97300 45.06200 -0.01600 1.000 83.48339  ? 507 HOH   A O   1 
HETATM 2538 O  O   . HOH   O 6 .   ? 39.76200 44.01500 1.45300  1.000 67.53599  ? 508 HOH   A O   1 
HETATM 2539 O  O   . HOH   O 6 .   ? 30.757   46.554   8.571    1.000 82.32606  ? 509 HOH   A O   1 
HETATM 2540 O  O   . HOH   O 6 .   ? 71.88400 19.52800 15.19700 1.000 102.43909 ? 510 HOH   A O   1 
HETATM 2541 O  O   . HOH   O 6 .   ? 41.552   38.995   30.464   1.000 67.99632  ? 511 HOH   A O   1 
HETATM 2542 O  O   . HOH   O 6 .   ? 55.50000 21.47900 3.30200  1.000 61.81729  ? 512 HOH   A O   1 
HETATM 2543 O  O   . HOH   O 6 .   ? 44.34600 57.17700 10.50000 1.000 64.73930  ? 513 HOH   A O   1 
HETATM 2544 O  O   . HOH   O 6 .   ? 42.62000 18.06600 7.95400  1.000 69.20090  ? 514 HOH   A O   1 
HETATM 2545 O  O   . HOH   O 6 .   ? 44.69600 46.75600 23.32000 1.000 56.42401  ? 515 HOH   A O   1 
HETATM 2546 O  O   . HOH   O 6 .   ? 51.33600 9.12800  20.07200 1.000 68.52681  ? 516 HOH   A O   1 
HETATM 2547 O  O   . HOH   O 6 .   ? 42.51200 45.40700 24.78500 1.000 70.32832  ? 517 HOH   A O   1 
HETATM 2548 O  O   . HOH   O 6 .   ? 50.74600 49.26200 9.83700  1.000 70.82980  ? 518 HOH   A O   1 
HETATM 2549 O  O   . HOH   O 6 .   ? 51.92700 37.08500 26.54800 1.000 79.01605  ? 519 HOH   A O   1 
HETATM 2550 O  O   . HOH   O 6 .   ? 49.46400 8.44800  21.13800 1.000 80.78268  ? 520 HOH   A O   1 
HETATM 2551 O  O   . HOH   O 6 .   ? 55.61100 57.56500 11.15800 1.000 82.99868  ? 521 HOH   A O   1 
HETATM 2552 O  O   . HOH   O 6 .   ? 31.83100 36.82400 4.97300  1.000 69.84975  ? 522 HOH   A O   1 
HETATM 2553 O  O   . HOH   O 6 .   ? 42.93300 23.44800 4.74600  1.000 70.53794  ? 523 HOH   A O   1 
HETATM 2554 O  O   . HOH   O 6 .   ? 53.85400 28.58800 5.18400  1.000 50.84832  ? 524 HOH   A O   1 
HETATM 2555 O  O   . HOH   O 6 .   ? 22.38600 63.08100 25.51600 1.000 104.89471 ? 525 HOH   A O   1 
HETATM 2556 O  O   . HOH   O 6 .   ? 55.41400 13.11800 6.44400  1.000 73.23074  ? 526 HOH   A O   1 
HETATM 2557 O  O   . HOH   O 6 .   ? 38.03900 47.74800 5.93900  1.000 68.32156  ? 527 HOH   A O   1 
HETATM 2558 O  O   . HOH   O 6 .   ? 49.45900 10.31000 15.58300 1.000 66.83427  ? 528 HOH   A O   1 
HETATM 2559 O  O   . HOH   O 6 .   ? 50.10000 20.89300 21.43600 1.000 59.75843  ? 529 HOH   A O   1 
HETATM 2560 O  O   . HOH   O 6 .   ? 50.09000 37.39100 4.06700  1.000 52.34851  ? 530 HOH   A O   1 
HETATM 2561 O  O   . HOH   O 6 .   ? 65.14500 20.74000 23.98900 1.000 85.65395  ? 531 HOH   A O   1 
HETATM 2562 O  O   . HOH   O 6 .   ? 36.35600 24.33300 24.47000 1.000 63.03749  ? 532 HOH   A O   1 
HETATM 2563 O  O   . HOH   O 6 .   ? 73.25200 29.95300 26.41700 1.000 106.84189 ? 533 HOH   A O   1 
HETATM 2564 O  O   . HOH   O 6 .   ? 36.53000 28.74500 0.72700  1.000 88.98977  ? 534 HOH   A O   1 
HETATM 2565 O  O   . HOH   O 6 .   ? 43.06700 36.93500 29.67500 1.000 62.07534  ? 535 HOH   A O   1 
HETATM 2566 O  O   . HOH   O 6 .   ? 50.87100 52.53600 6.44200  1.000 70.94379  ? 536 HOH   A O   1 
HETATM 2567 O  O   . HOH   O 6 .   ? 35.32000 22.29400 21.61300 1.000 70.11502  ? 537 HOH   A O   1 
HETATM 2568 O  O   . HOH   O 6 .   ? 32.65700 34.95600 12.10800 1.000 61.78342  ? 538 HOH   A O   1 
HETATM 2569 O  O   . HOH   O 6 .   ? 51.76300 29.94100 5.94500  1.000 50.08851  ? 539 HOH   A O   1 
HETATM 2570 O  O   . HOH   O 6 .   ? 49.097   43.856   29.669   1.000 78.55792  ? 540 HOH   A O   1 
HETATM 2571 O  O   . HOH   O 6 .   ? 55.009   68.864   18.574   1.000 77.61067  ? 541 HOH   A O   1 
HETATM 2572 O  O   . HOH   O 6 .   ? 51.28100 24.70500 23.83700 1.000 58.04319  ? 542 HOH   A O   1 
HETATM 2573 O  O   . HOH   O 6 .   ? 45.05300 47.57500 7.64200  1.000 59.44826  ? 543 HOH   A O   1 
HETATM 2574 O  O   . HOH   O 6 .   ? 41.08300 41.30000 21.86300 1.000 55.25848  ? 544 HOH   A O   1 
HETATM 2575 O  O   . HOH   O 6 .   ? 56.12500 54.50800 13.71400 1.000 62.96205  ? 545 HOH   A O   1 
HETATM 2576 O  O   . HOH   O 6 .   ? 70.51600 38.01100 10.67900 1.000 96.97573  ? 546 HOH   A O   1 
HETATM 2577 O  O   . HOH   O 6 .   ? 31.79500 35.23400 19.54100 1.000 72.33761  ? 547 HOH   A O   1 
HETATM 2578 O  O   . HOH   O 6 .   ? 34.92600 33.31000 22.98900 1.000 69.36299  ? 548 HOH   A O   1 
HETATM 2579 O  O   . HOH   O 6 .   ? 57.37400 21.92200 -0.15200 1.000 56.94268  ? 549 HOH   A O   1 
HETATM 2580 O  O   . HOH   O 6 .   ? 50.39800 30.25700 24.88500 1.000 72.24042  ? 550 HOH   A O   1 
HETATM 2581 O  O   . HOH   O 6 .   ? 62.72200 27.73100 12.94600 1.000 59.04255  ? 551 HOH   A O   1 
HETATM 2582 O  O   . HOH   O 6 .   ? 47.834   49.154   29.129   1.000 64.06334  ? 552 HOH   A O   1 
HETATM 2583 O  O   . HOH   O 6 .   ? 52.56800 39.89100 3.54700  1.000 63.46694  ? 553 HOH   A O   1 
HETATM 2584 O  O   . HOH   O 6 .   ? 41.06400 18.60400 5.29700  1.000 88.90875  ? 554 HOH   A O   1 
HETATM 2585 O  O   . HOH   O 6 .   ? 63.39900 43.78100 20.73300 1.000 72.72393  ? 555 HOH   A O   1 
HETATM 2586 O  O   . HOH   O 6 .   ? 59.58400 26.85400 26.51500 1.000 65.39863  ? 556 HOH   A O   1 
HETATM 2587 O  O   . HOH   O 6 .   ? 54.34800 59.17600 29.18400 1.000 95.08845  ? 557 HOH   A O   1 
HETATM 2588 O  O   . HOH   O 6 .   ? 55.13600 51.23900 25.86200 1.000 53.00600  ? 558 HOH   A O   1 
HETATM 2589 O  O   . HOH   O 6 .   ? 39.78600 56.34900 8.24400  1.000 70.73000  ? 559 HOH   A O   1 
HETATM 2590 O  O   . HOH   O 6 .   ? 52.24100 33.45800 24.97200 1.000 71.46775  ? 560 HOH   A O   1 
HETATM 2591 O  O   . HOH   O 6 .   ? 29.46900 73.07300 22.97400 1.000 124.94524 ? 561 HOH   A O   1 
HETATM 2592 O  O   . HOH   O 6 .   ? 53.94400 66.55100 25.16000 1.000 66.52469  ? 562 HOH   A O   1 
HETATM 2593 O  O   . HOH   O 6 .   ? 47.30200 56.45300 13.75700 1.000 71.20345  ? 563 HOH   A O   1 
HETATM 2594 O  O   . HOH   O 6 .   ? 59.01900 29.79800 9.18300  1.000 64.10150  ? 564 HOH   A O   1 
HETATM 2595 O  O   . HOH   O 6 .   ? 37.91700 19.98600 11.21700 1.000 68.90963  ? 565 HOH   A O   1 
HETATM 2596 O  O   . HOH   O 6 .   ? 54.61900 43.40600 27.21900 1.000 64.10967  ? 566 HOH   A O   1 
HETATM 2597 O  O   . HOH   O 6 .   ? 68.57400 27.47800 4.30400  1.000 94.77988  ? 567 HOH   A O   1 
HETATM 2598 O  O   . HOH   O 6 .   ? 31.91600 29.04000 22.03300 1.000 71.42760  ? 568 HOH   A O   1 
HETATM 2599 O  O   . HOH   O 6 .   ? 49.31000 65.18600 15.09200 1.000 68.97327  ? 569 HOH   A O   1 
HETATM 2600 O  O   . HOH   O 6 .   ? 49.37100 55.42900 26.08200 1.000 54.03403  ? 570 HOH   A O   1 
HETATM 2601 O  O   . HOH   O 6 .   ? 42.39800 39.85100 5.66300  1.000 54.14919  ? 571 HOH   A O   1 
HETATM 2602 O  O   . HOH   O 6 .   ? 56.69100 16.96000 12.48700 1.000 64.96411  ? 572 HOH   A O   1 
HETATM 2603 O  O   . HOH   O 6 .   ? 39.85200 39.21900 6.63100  1.000 53.63169  ? 573 HOH   A O   1 
HETATM 2604 O  O   . HOH   O 6 .   ? 44.76300 12.41100 7.85100  1.000 72.46344  ? 574 HOH   A O   1 
HETATM 2605 O  O   . HOH   O 6 .   ? 40.68400 15.67100 11.64500 1.000 71.36432  ? 575 HOH   A O   1 
HETATM 2606 O  O   . HOH   O 6 .   ? 49.07000 26.65300 12.87600 1.000 50.44339  ? 576 HOH   A O   1 
HETATM 2607 O  O   . HOH   O 6 .   ? 40.60700 27.37700 12.14600 1.000 62.30787  ? 577 HOH   A O   1 
HETATM 2608 O  O   . HOH   O 6 .   ? 64.76900 30.38000 6.73300  1.000 79.24361  ? 578 HOH   A O   1 
HETATM 2609 O  O   . HOH   O 6 .   ? 46.09600 46.13100 1.84100  1.000 81.17993  ? 579 HOH   A O   1 
HETATM 2610 O  O   . HOH   O 6 .   ? 60.07700 19.94500 20.45800 1.000 65.60589  ? 580 HOH   A O   1 
HETATM 2611 O  O   . HOH   O 6 .   ? 34.15500 24.44800 23.57800 1.000 75.62874  ? 581 HOH   A O   1 
HETATM 2612 O  O   . HOH   O 6 .   ? 37.79100 43.15700 24.83200 1.000 81.16844  ? 582 HOH   A O   1 
HETATM 2613 O  O   . HOH   O 6 .   ? 35.00600 54.24600 20.24000 1.000 83.65293  ? 583 HOH   A O   1 
HETATM 2614 O  O   . HOH   O 6 .   ? 35.50800 34.37700 2.72200  1.000 78.02609  ? 584 HOH   A O   1 
HETATM 2615 O  O   . HOH   O 6 .   ? 38.71000 53.84600 8.74300  1.000 68.82154  ? 585 HOH   A O   1 
HETATM 2616 O  O   . HOH   O 6 .   ? 37.77900 31.03400 10.23900 1.000 57.73529  ? 586 HOH   A O   1 
HETATM 2617 O  O   . HOH   O 6 .   ? 54.36700 30.76700 3.41400  1.000 54.06564  ? 587 HOH   A O   1 
HETATM 2618 O  O   . HOH   O 6 .   ? 44.43900 58.90000 24.84900 1.000 69.30109  ? 588 HOH   A O   1 
HETATM 2619 O  O   . HOH   O 6 .   ? 63.15800 40.65400 19.51500 1.000 60.07577  ? 589 HOH   A O   1 
HETATM 2620 O  O   . HOH   O 6 .   ? 20.26800 60.52600 13.59600 1.000 102.73962 ? 590 HOH   A O   1 
HETATM 2621 O  O   . HOH   O 6 .   ? 42.31500 48.09500 7.62700  1.000 53.82669  ? 591 HOH   A O   1 
HETATM 2622 O  O   . HOH   O 6 .   ? 37.36800 35.45200 -1.68600 1.000 60.56274  ? 592 HOH   A O   1 
HETATM 2623 O  O   . HOH   O 6 .   ? 64.11700 20.29600 20.89600 1.000 61.75303  ? 593 HOH   A O   1 
HETATM 2624 O  O   . HOH   O 6 .   ? 31.90000 26.10300 17.21200 1.000 67.06487  ? 594 HOH   A O   1 
HETATM 2625 O  O   . HOH   O 6 .   ? 37.70700 42.51500 21.57500 1.000 63.06283  ? 595 HOH   A O   1 
HETATM 2626 O  O   . HOH   O 6 .   ? 48.40400 62.17200 14.02400 1.000 82.75596  ? 596 HOH   A O   1 
HETATM 2627 O  O   . HOH   O 6 .   ? 32.35500 20.85400 14.80200 1.000 83.81889  ? 597 HOH   A O   1 
HETATM 2628 O  O   . HOH   O 6 .   ? 55.27200 33.75300 -1.17600 1.000 74.80561  ? 598 HOH   A O   1 
HETATM 2629 O  O   . HOH   O 6 .   ? 61.34800 41.15700 17.63100 1.000 59.66233  ? 599 HOH   A O   1 
HETATM 2630 O  O   . HOH   O 6 .   ? 29.48100 42.35200 7.24900  1.000 117.23993 ? 600 HOH   A O   1 
HETATM 2631 O  O   . HOH   O 6 .   ? 33.56000 28.12500 10.63300 1.000 68.83104  ? 601 HOH   A O   1 
HETATM 2632 O  O   . HOH   O 6 .   ? 55.15000 14.77400 13.15300 1.000 59.99854  ? 602 HOH   A O   1 
HETATM 2633 O  O   . HOH   O 6 .   ? 59.98200 15.25100 12.10800 1.000 82.27810  ? 603 HOH   A O   1 
HETATM 2634 O  O   . HOH   O 6 .   ? 56.26400 27.95000 23.44800 1.000 46.63213  ? 604 HOH   A O   1 
HETATM 2635 O  O   . HOH   O 6 .   ? 48.81200 22.94800 22.55700 1.000 67.66427  ? 605 HOH   A O   1 
HETATM 2636 O  O   . HOH   O 6 .   ? 56.80600 20.25300 20.40200 1.000 52.75231  ? 606 HOH   A O   1 
HETATM 2637 O  O   . HOH   O 6 .   ? 46.26900 48.30500 5.01200  1.000 68.20008  ? 607 HOH   A O   1 
HETATM 2638 O  O   . HOH   O 6 .   ? 42.53100 67.31100 24.84200 1.000 93.58002  ? 608 HOH   A O   1 
HETATM 2639 O  O   . HOH   O 6 .   ? 59.51700 19.11800 4.88100  1.000 65.08621  ? 609 HOH   A O   1 
HETATM 2640 O  O   . HOH   O 6 .   ? 42.66200 15.46400 12.86300 1.000 69.53747  ? 610 HOH   A O   1 
HETATM 2641 O  O   . HOH   O 6 .   ? 42.34600 64.77000 14.63100 1.000 77.63824  ? 611 HOH   A O   1 
HETATM 2642 O  O   . HOH   O 6 .   ? 49.84500 39.01000 6.49000  1.000 58.66119  ? 612 HOH   A O   1 
HETATM 2643 O  O   . HOH   O 6 .   ? 48.03700 27.45100 -7.53800 1.000 74.56763  ? 613 HOH   A O   1 
HETATM 2644 O  O   . HOH   O 6 .   ? 40.64400 27.78900 9.68000  1.000 67.79250  ? 614 HOH   A O   1 
HETATM 2645 O  O   . HOH   O 6 .   ? 63.16600 36.89400 24.17900 1.000 78.00085  ? 615 HOH   A O   1 
HETATM 2646 O  O   . HOH   O 6 .   ? 37.90800 28.66500 8.66500  1.000 67.76420  ? 616 HOH   A O   1 
HETATM 2647 O  O   . HOH   O 6 .   ? 43.98700 32.28600 1.61100  1.000 75.53511  ? 617 HOH   A O   1 
HETATM 2648 O  O   . HOH   O 6 .   ? 51.45300 8.93400  22.26900 1.000 90.00781  ? 618 HOH   A O   1 
HETATM 2649 O  O   . HOH   O 6 .   ? 59.91400 16.76300 18.26000 1.000 92.20994  ? 619 HOH   A O   1 
HETATM 2650 O  O   . HOH   O 6 .   ? 48.37400 8.84600  19.24700 1.000 79.73630  ? 620 HOH   A O   1 
HETATM 2651 O  O   . HOH   O 6 .   ? 41.20400 10.15500 18.02400 1.000 75.30992  ? 621 HOH   A O   1 
HETATM 2652 O  O   . HOH   O 6 .   ? 47.62100 9.82200  24.03300 1.000 79.34634  ? 622 HOH   A O   1 
HETATM 2653 O  O   . HOH   O 6 .   ? 60.63300 16.94900 13.60000 1.000 64.63408  ? 623 HOH   A O   1 
HETATM 2654 O  O   . HOH   O 6 .   ? 40.04800 46.45500 7.09100  1.000 55.41111  ? 624 HOH   A O   1 
HETATM 2655 O  O   . HOH   O 6 .   ? 51.33900 62.44500 26.62400 1.000 67.46367  ? 625 HOH   A O   1 
HETATM 2656 O  O   . HOH   O 6 .   ? 52.66600 50.97300 11.45500 1.000 67.60883  ? 626 HOH   A O   1 
HETATM 2657 O  O   . HOH   O 6 .   ? 42.81100 50.15700 21.67900 1.000 77.33145  ? 627 HOH   A O   1 
HETATM 2658 O  O   . HOH   O 6 .   ? 41.22900 8.31200  13.78300 1.000 86.72750  ? 628 HOH   A O   1 
HETATM 2659 O  O   . HOH   O 6 .   ? 33.74600 27.56200 0.81700  1.000 85.43279  ? 629 HOH   A O   1 
HETATM 2660 O  O   . HOH   O 6 .   ? 44.53100 66.11700 24.57800 1.000 77.44347  ? 630 HOH   A O   1 
HETATM 2661 O  O   . HOH   O 6 .   ? 38.12900 49.39100 20.95600 1.000 74.95009  ? 631 HOH   A O   1 
HETATM 2662 O  O   . HOH   O 6 .   ? 22.27100 59.23000 12.34600 1.000 98.98541  ? 632 HOH   A O   1 
HETATM 2663 O  O   . HOH   O 6 .   ? 53.13900 52.72600 27.53600 1.000 75.99449  ? 633 HOH   A O   1 
HETATM 2664 O  O   . HOH   O 6 .   ? 51.63100 41.39000 5.43800  1.000 100.02749 ? 634 HOH   A O   1 
HETATM 2665 O  O   . HOH   O 6 .   ? 33.63900 38.58500 2.30400  1.000 69.84084  ? 635 HOH   A O   1 
HETATM 2666 O  O   . HOH   O 6 .   ? 53.73700 23.79200 -3.09200 1.000 77.36728  ? 636 HOH   A O   1 
HETATM 2667 O  O   . HOH   O 6 .   ? 49.37100 55.71700 30.16000 1.000 69.85458  ? 637 HOH   A O   1 
HETATM 2668 O  O   . HOH   O 6 .   ? 32.81700 35.41600 3.48600  1.000 86.91430  ? 638 HOH   A O   1 
HETATM 2669 O  O   . HOH   O 6 .   ? 58.94100 34.36100 24.37500 1.000 67.89195  ? 639 HOH   A O   1 
HETATM 2670 O  O   . HOH   O 6 .   ? 56.14900 29.50700 28.44300 1.000 68.18283  ? 640 HOH   A O   1 
HETATM 2671 O  O   . HOH   O 6 .   ? 61.76700 43.50700 22.61200 1.000 77.60615  ? 641 HOH   A O   1 
HETATM 2672 O  O   . HOH   O 6 .   ? 30.36500 39.75100 5.46900  1.000 87.21146  ? 642 HOH   A O   1 
HETATM 2673 O  O   . HOH   O 6 .   ? 70.00900 38.20700 13.32300 1.000 86.11075  ? 643 HOH   A O   1 
HETATM 2674 O  O   . HOH   O 6 .   ? 61.64400 43.19700 18.55200 1.000 74.56952  ? 644 HOH   A O   1 
HETATM 2675 O  O   . HOH   O 6 .   ? 35.37400 40.17200 20.98200 1.000 56.84322  ? 645 HOH   A O   1 
HETATM 2676 O  O   . HOH   O 6 .   ? 35.75600 13.81000 14.64200 1.000 71.93830  ? 646 HOH   A O   1 
HETATM 2677 O  O   . HOH   O 6 .   ? 45.90000 60.26300 8.44100  1.000 71.73333  ? 647 HOH   A O   1 
HETATM 2678 O  O   . HOH   O 6 .   ? 52.35600 5.40800  9.51100  1.000 104.55760 ? 648 HOH   A O   1 
HETATM 2679 O  O   . HOH   O 6 .   ? 40.86900 65.56100 20.76100 1.000 80.73634  ? 649 HOH   A O   1 
HETATM 2680 O  O   . HOH   O 6 .   ? 54.645   66.733   15.356   1.000 75.21419  ? 650 HOH   A O   1 
HETATM 2681 O  O   . HOH   O 6 .   ? 42.99700 33.78800 3.48300  1.000 60.56489  ? 651 HOH   A O   1 
HETATM 2682 O  O   . HOH   O 6 .   ? 52.37000 48.63700 11.35900 1.000 75.81005  ? 652 HOH   A O   1 
HETATM 2683 O  O   . HOH   O 6 .   ? 50.37200 69.91900 17.29400 1.000 71.60141  ? 653 HOH   A O   1 
HETATM 2684 O  O   . HOH   O 6 .   ? 64.56400 22.26200 26.25000 1.000 83.62478  ? 654 HOH   A O   1 
HETATM 2685 O  O   . HOH   O 6 .   ? 59.90000 31.78800 7.47200  1.000 70.62446  ? 655 HOH   A O   1 
HETATM 2686 O  O   . HOH   O 6 .   ? 44.07100 15.84100 4.77100  1.000 80.62138  ? 656 HOH   A O   1 
HETATM 2687 O  O   . HOH   O 6 .   ? 41.42600 27.39800 -4.46300 1.000 83.62648  ? 657 HOH   A O   1 
HETATM 2688 O  O   . HOH   O 6 .   ? 45.83000 9.14000  19.92100 1.000 88.39184  ? 658 HOH   A O   1 
HETATM 2689 O  O   . HOH   O 6 .   ? 42.29900 18.80500 3.34600  1.000 80.21079  ? 659 HOH   A O   1 
HETATM 2690 O  O   . HOH   O 6 .   ? 51.22300 23.59500 -3.07700 1.000 66.33463  ? 660 HOH   A O   1 
HETATM 2691 O  O   . HOH   O 6 .   ? 67.61400 34.38600 8.25200  1.000 87.97918  ? 661 HOH   A O   1 
HETATM 2692 O  O   . HOH   O 6 .   ? 51.96900 5.33000  7.16000  1.000 96.08948  ? 662 HOH   A O   1 
HETATM 2693 O  O   . HOH   O 6 .   ? 40.58200 44.02900 23.52900 1.000 68.75631  ? 663 HOH   A O   1 
HETATM 2694 O  O   . HOH   O 6 .   ? 40.01800 18.07800 8.13900  1.000 77.83594  ? 664 HOH   A O   1 
HETATM 2695 O  O   . HOH   O 6 .   ? 34.72800 49.27000 20.21400 1.000 83.05999  ? 665 HOH   A O   1 
HETATM 2696 O  O   . HOH   O 6 .   ? 50.65700 53.02300 27.15700 1.000 72.53270  ? 666 HOH   A O   1 
HETATM 2697 O  O   . HOH   O 6 .   ? 36.57200 26.79600 26.42500 1.000 83.48141  ? 667 HOH   A O   1 
HETATM 2698 O  O   . HOH   O 6 .   ? 31.62700 41.00400 9.12300  1.000 61.10972  ? 668 HOH   A O   1 
HETATM 2699 O  O   . HOH   O 6 .   ? 62.723   37.414   27.379   1.000 77.51646  ? 669 HOH   A O   1 
HETATM 2700 O  O   . HOH   O 6 .   ? 43.53400 56.00800 7.65400  1.000 68.55366  ? 670 HOH   A O   1 
HETATM 2701 O  O   . HOH   O 6 .   ? 50.01500 57.91400 31.94500 1.000 89.69951  ? 671 HOH   A O   1 
HETATM 2702 O  O   . HOH   O 6 .   ? 44.91800 67.30400 26.44700 1.000 82.60529  ? 672 HOH   A O   1 
HETATM 2703 O  O   . HOH   O 6 .   ? 32.46500 47.75500 18.67100 1.000 95.88259  ? 673 HOH   A O   1 
HETATM 2704 O  O   . HOH   O 6 .   ? 61.723   44.928   25.018   1.000 71.29291  ? 674 HOH   A O   1 
HETATM 2705 O  O   . HOH   O 6 .   ? 50.17000 59.47500 30.14000 1.000 74.89281  ? 675 HOH   A O   1 
HETATM 2706 O  O   . HOH   O 6 .   ? 50.89400 57.27100 27.80500 1.000 69.88670  ? 676 HOH   A O   1 
HETATM 2707 O  O   . HOH   O 6 .   ? 52.84900 44.85100 27.34400 1.000 65.11094  ? 677 HOH   A O   1 
HETATM 2708 O  O   . HOH   O 6 .   ? 39.40400 47.80700 23.84900 1.000 80.89502  ? 678 HOH   A O   1 
HETATM 2709 O  O   . HOH   O 6 .   ? 58.36300 47.02000 13.46000 1.000 82.22843  ? 679 HOH   A O   1 
HETATM 2710 O  O   . HOH   O 6 .   ? 46.98500 64.51600 29.20500 1.000 89.75608  ? 680 HOH   A O   1 
HETATM 2711 O  O   . HOH   O 6 .   ? 52.22900 59.75600 27.99900 1.000 79.38081  ? 681 HOH   A O   1 
HETATM 2712 O  O   . HOH   O 6 .   ? 61.41200 21.72500 25.18600 1.000 81.74130  ? 682 HOH   A O   1 
HETATM 2713 O  O   . HOH   O 6 .   ? 49.10200 57.83200 15.59500 1.000 77.53568  ? 683 HOH   A O   1 
HETATM 2714 O  O   . HOH   O 6 .   ? 48.01100 47.35800 1.23500  1.000 83.47213  ? 684 HOH   A O   1 
HETATM 2715 O  O   . HOH   O 6 .   ? 41.75600 50.31700 6.03800  1.000 63.15544  ? 685 HOH   A O   1 
HETATM 2716 O  O   . HOH   O 6 .   ? 50.49500 27.18300 26.01200 1.000 75.22472  ? 686 HOH   A O   1 
HETATM 2717 O  O   . HOH   O 6 .   ? 58.88800 52.54200 16.04300 1.000 57.38804  ? 687 HOH   A O   1 
HETATM 2718 O  O   . HOH   O 6 .   ? 50.054   47.600   29.935   1.000 87.25911  ? 688 HOH   A O   1 
HETATM 2719 O  O   . HOH   O 6 .   ? 63.02600 32.44200 7.58400  1.000 67.13858  ? 689 HOH   A O   1 
HETATM 2720 O  O   . HOH   O 6 .   ? 51.09800 8.37900  17.02800 1.000 83.47922  ? 690 HOH   A O   1 
HETATM 2721 O  O   . HOH   O 6 .   ? 36.60200 51.47400 20.09700 1.000 84.83329  ? 691 HOH   A O   1 
HETATM 2722 O  O   . HOH   O 6 .   ? 50.63000 27.57200 -7.10600 1.000 83.94586  ? 692 HOH   A O   1 
HETATM 2723 O  O   . HOH   O 6 .   ? 48.37700 7.84000  23.04300 1.000 81.59997  ? 693 HOH   A O   1 
HETATM 2724 O  O   . HOH   O 6 .   ? 45.299   54.103   4.839    1.000 70.59663  ? 694 HOH   A O   1 
HETATM 2725 O  O   . HOH   O 6 .   ? 57.93600 19.72000 1.03100  1.000 82.90725  ? 695 HOH   A O   1 
HETATM 2726 O  O   . HOH   O 6 .   ? 62.26500 32.84400 3.87000  1.000 86.13289  ? 696 HOH   A O   1 
HETATM 2727 O  O   . HOH   O 6 .   ? 60.77000 24.10500 28.39500 1.000 87.17657  ? 697 HOH   A O   1 
HETATM 2728 O  O   . HOH   O 6 .   ? 42.38000 15.77000 9.96800  1.000 91.24375  ? 698 HOH   A O   1 
HETATM 2729 O  O   . HOH   O 6 .   ? 54.98100 30.36300 -5.94700 1.000 85.77966  ? 699 HOH   A O   1 
HETATM 2730 O  O   . HOH   O 6 .   ? 52.65100 43.83400 0.14200  1.000 83.79848  ? 700 HOH   A O   1 
HETATM 2731 O  O   . HOH   O 6 .   ? 57.27500 19.10800 3.39400  1.000 67.24481  ? 701 HOH   A O   1 
HETATM 2732 O  O   . HOH   O 6 .   ? 56.44300 50.04500 11.95800 1.000 89.36509  ? 702 HOH   A O   1 
HETATM 2733 O  O   . HOH   O 6 .   ? 37.950   57.289   4.348    1.000 81.40361  ? 703 HOH   A O   1 
HETATM 2734 O  O   . HOH   O 6 .   ? 34.96100 13.33200 12.15400 1.000 92.65454  ? 704 HOH   A O   1 
HETATM 2735 O  O   . HOH   O 6 .   ? 53.49600 28.84100 -6.93200 1.000 77.61133  ? 705 HOH   A O   1 
HETATM 2736 O  O   . HOH   O 6 .   ? 52.30000 60.55000 31.17000 1.000 83.18202  ? 706 HOH   A O   1 
# 
