data_9IVV
# 
_entry.id   9IVV 
# 
_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   9IVV         pdb_00009ivv 10.2210/pdb9ivv/pdb 
WWPDB D_1300049773 ?            ?                   
# 
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 2025-03-12 ? 
2 'Structure model' 1 1 2025-03-19 ? 
# 
_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.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
5 2 'Structure model' '_citation.title'                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9IVV 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-24 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_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              liguobo@scu.edu.cn 
_pdbx_contact_author.name_first         GuoBo 
_pdbx_contact_author.name_last          Li 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4915-6677 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Li, G.-B.'   1 0000-0002-4915-6677 
'Yu, J.-L.'   2 ?                   
'Zhou, C.'    3 ?                   
'Ning, X.-L.' 4 ?                   
'Mou, J.'     5 ?                   
'Wu, J.-W.'   6 ?                   
'Meng, F.-B.' 7 ?                   
# 
_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                2269 
_citation.page_last                 2269 
_citation.title                     'Knowledge-guided diffusion model for 3D ligand-pharmacophore mapping.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-57485-3 
_citation.pdbx_database_id_PubMed   40050649 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Yu, J.L.'   1  ? 
primary 'Zhou, C.'   2  ? 
primary 'Ning, X.L.' 3  ? 
primary 'Mou, J.'    4  ? 
primary 'Meng, F.B.' 5  ? 
primary 'Wu, J.W.'   6  ? 
primary 'Chen, Y.T.' 7  ? 
primary 'Tang, B.D.' 8  ? 
primary 'Liu, X.G.'  9  ? 
primary 'Li, G.B.'   10 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Glutaminyl-peptide cyclotransferase'                                                           37557.398 1  
2.3.2.5 ? ? ? 
2 non-polymer syn 'ZINC ION'                                                                                      65.409    1  ? ? 
? ? 
3 non-polymer syn '4-azanyl-~{N}-[2-(1~{H}-imidazol-4-yl)ethyl]-2-oxidanidyl-1,2,5-oxadiazol-2-ium-3-carboxamide' 238.203   1  ? ? 
? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                            78.133    2  ? ? 
? ? 
5 non-polymer nat GLYCEROL                                                                                        92.094    4  ? ? 
? ? 
6 non-polymer syn DIMETHYLFORMAMIDE                                                                               73.094    1  ? ? 
? ? 
7 water       nat water                                                                                           18.015    36 ? ? 
? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Glutaminyl cyclase,QC,sQC,Glutaminyl-tRNA cyclotransferase,Glutamyl cyclase,EC' 
# 
_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       
;ASAWPEEKNYHQPAILNSSALRQIAEGTSISEMWQNDLQPLLIERYPGSPGSYAARQHIMQRIQRLQADWVLEIDTFLSQ
TPYGYRSFSNIISTLNPTAKRHLVLACHYDSKYFSHWNNRVFVGATDSAVPCAMMLELARALDKKLLSLKTVSDSKPDLS
LQLIFFDGEEAFLHWSPQDSLYGSRHLAAKMASTPHPPGARGTSQLHGMDLLVLLDLIGAPNPTFPNFFPNSARWFERLQ
AIEHELHELGLLKDHSLEGRYFQNYSYGGVIQDDHIPFLRRGVPVLHLIPSPFPEVWHTMDDNEENLDESTIDNLNKILQ
VFVLEYLHL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ASAWPEEKNYHQPAILNSSALRQIAEGTSISEMWQNDLQPLLIERYPGSPGSYAARQHIMQRIQRLQADWVLEIDTFLSQ
TPYGYRSFSNIISTLNPTAKRHLVLACHYDSKYFSHWNNRVFVGATDSAVPCAMMLELARALDKKLLSLKTVSDSKPDLS
LQLIFFDGEEAFLHWSPQDSLYGSRHLAAKMASTPHPPGARGTSQLHGMDLLVLLDLIGAPNPTFPNFFPNSARWFERLQ
AIEHELHELGLLKDHSLEGRYFQNYSYGGVIQDDHIPFLRRGVPVLHLIPSPFPEVWHTMDDNEENLDESTIDNLNKILQ
VFVLEYLHL
;
_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 'ZINC ION'                                                                                      ZN    
3 '4-azanyl-~{N}-[2-(1~{H}-imidazol-4-yl)ethyl]-2-oxidanidyl-1,2,5-oxadiazol-2-ium-3-carboxamide' A1D94 
4 'DIMETHYL SULFOXIDE'                                                                            DMS   
5 GLYCEROL                                                                                        GOL   
6 DIMETHYLFORMAMIDE                                                                               DMF   
7 water                                                                                           HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   SER n 
1 3   ALA n 
1 4   TRP n 
1 5   PRO n 
1 6   GLU n 
1 7   GLU n 
1 8   LYS n 
1 9   ASN n 
1 10  TYR n 
1 11  HIS n 
1 12  GLN n 
1 13  PRO n 
1 14  ALA n 
1 15  ILE n 
1 16  LEU n 
1 17  ASN n 
1 18  SER n 
1 19  SER n 
1 20  ALA n 
1 21  LEU n 
1 22  ARG n 
1 23  GLN n 
1 24  ILE n 
1 25  ALA n 
1 26  GLU n 
1 27  GLY n 
1 28  THR n 
1 29  SER n 
1 30  ILE n 
1 31  SER n 
1 32  GLU n 
1 33  MET n 
1 34  TRP n 
1 35  GLN n 
1 36  ASN n 
1 37  ASP n 
1 38  LEU n 
1 39  GLN n 
1 40  PRO n 
1 41  LEU n 
1 42  LEU n 
1 43  ILE n 
1 44  GLU n 
1 45  ARG n 
1 46  TYR n 
1 47  PRO n 
1 48  GLY n 
1 49  SER n 
1 50  PRO n 
1 51  GLY n 
1 52  SER n 
1 53  TYR n 
1 54  ALA n 
1 55  ALA n 
1 56  ARG n 
1 57  GLN n 
1 58  HIS n 
1 59  ILE n 
1 60  MET n 
1 61  GLN n 
1 62  ARG n 
1 63  ILE n 
1 64  GLN n 
1 65  ARG n 
1 66  LEU n 
1 67  GLN n 
1 68  ALA n 
1 69  ASP n 
1 70  TRP n 
1 71  VAL n 
1 72  LEU n 
1 73  GLU n 
1 74  ILE n 
1 75  ASP n 
1 76  THR n 
1 77  PHE n 
1 78  LEU n 
1 79  SER n 
1 80  GLN n 
1 81  THR n 
1 82  PRO n 
1 83  TYR n 
1 84  GLY n 
1 85  TYR n 
1 86  ARG n 
1 87  SER n 
1 88  PHE n 
1 89  SER n 
1 90  ASN n 
1 91  ILE n 
1 92  ILE n 
1 93  SER n 
1 94  THR n 
1 95  LEU n 
1 96  ASN n 
1 97  PRO n 
1 98  THR n 
1 99  ALA n 
1 100 LYS n 
1 101 ARG n 
1 102 HIS n 
1 103 LEU n 
1 104 VAL n 
1 105 LEU n 
1 106 ALA n 
1 107 CYS n 
1 108 HIS n 
1 109 TYR n 
1 110 ASP n 
1 111 SER n 
1 112 LYS n 
1 113 TYR n 
1 114 PHE n 
1 115 SER n 
1 116 HIS n 
1 117 TRP n 
1 118 ASN n 
1 119 ASN n 
1 120 ARG n 
1 121 VAL n 
1 122 PHE n 
1 123 VAL n 
1 124 GLY n 
1 125 ALA n 
1 126 THR n 
1 127 ASP n 
1 128 SER n 
1 129 ALA n 
1 130 VAL n 
1 131 PRO n 
1 132 CYS n 
1 133 ALA n 
1 134 MET n 
1 135 MET n 
1 136 LEU n 
1 137 GLU n 
1 138 LEU n 
1 139 ALA n 
1 140 ARG n 
1 141 ALA n 
1 142 LEU n 
1 143 ASP n 
1 144 LYS n 
1 145 LYS n 
1 146 LEU n 
1 147 LEU n 
1 148 SER n 
1 149 LEU n 
1 150 LYS n 
1 151 THR n 
1 152 VAL n 
1 153 SER n 
1 154 ASP n 
1 155 SER n 
1 156 LYS n 
1 157 PRO n 
1 158 ASP n 
1 159 LEU n 
1 160 SER n 
1 161 LEU n 
1 162 GLN n 
1 163 LEU n 
1 164 ILE n 
1 165 PHE n 
1 166 PHE n 
1 167 ASP n 
1 168 GLY n 
1 169 GLU n 
1 170 GLU n 
1 171 ALA n 
1 172 PHE n 
1 173 LEU n 
1 174 HIS n 
1 175 TRP n 
1 176 SER n 
1 177 PRO n 
1 178 GLN n 
1 179 ASP n 
1 180 SER n 
1 181 LEU n 
1 182 TYR n 
1 183 GLY n 
1 184 SER n 
1 185 ARG n 
1 186 HIS n 
1 187 LEU n 
1 188 ALA n 
1 189 ALA n 
1 190 LYS n 
1 191 MET n 
1 192 ALA n 
1 193 SER n 
1 194 THR n 
1 195 PRO n 
1 196 HIS n 
1 197 PRO n 
1 198 PRO n 
1 199 GLY n 
1 200 ALA n 
1 201 ARG n 
1 202 GLY n 
1 203 THR n 
1 204 SER n 
1 205 GLN n 
1 206 LEU n 
1 207 HIS n 
1 208 GLY n 
1 209 MET n 
1 210 ASP n 
1 211 LEU n 
1 212 LEU n 
1 213 VAL n 
1 214 LEU n 
1 215 LEU n 
1 216 ASP n 
1 217 LEU n 
1 218 ILE n 
1 219 GLY n 
1 220 ALA n 
1 221 PRO n 
1 222 ASN n 
1 223 PRO n 
1 224 THR n 
1 225 PHE n 
1 226 PRO n 
1 227 ASN n 
1 228 PHE n 
1 229 PHE n 
1 230 PRO n 
1 231 ASN n 
1 232 SER n 
1 233 ALA n 
1 234 ARG n 
1 235 TRP n 
1 236 PHE n 
1 237 GLU n 
1 238 ARG n 
1 239 LEU n 
1 240 GLN n 
1 241 ALA n 
1 242 ILE n 
1 243 GLU n 
1 244 HIS n 
1 245 GLU n 
1 246 LEU n 
1 247 HIS n 
1 248 GLU n 
1 249 LEU n 
1 250 GLY n 
1 251 LEU n 
1 252 LEU n 
1 253 LYS n 
1 254 ASP n 
1 255 HIS n 
1 256 SER n 
1 257 LEU n 
1 258 GLU n 
1 259 GLY n 
1 260 ARG n 
1 261 TYR n 
1 262 PHE n 
1 263 GLN n 
1 264 ASN n 
1 265 TYR n 
1 266 SER n 
1 267 TYR n 
1 268 GLY n 
1 269 GLY n 
1 270 VAL n 
1 271 ILE n 
1 272 GLN n 
1 273 ASP n 
1 274 ASP n 
1 275 HIS n 
1 276 ILE n 
1 277 PRO n 
1 278 PHE n 
1 279 LEU n 
1 280 ARG n 
1 281 ARG n 
1 282 GLY n 
1 283 VAL n 
1 284 PRO n 
1 285 VAL n 
1 286 LEU n 
1 287 HIS n 
1 288 LEU n 
1 289 ILE n 
1 290 PRO n 
1 291 SER n 
1 292 PRO n 
1 293 PHE n 
1 294 PRO n 
1 295 GLU n 
1 296 VAL n 
1 297 TRP n 
1 298 HIS n 
1 299 THR n 
1 300 MET n 
1 301 ASP n 
1 302 ASP n 
1 303 ASN n 
1 304 GLU n 
1 305 GLU n 
1 306 ASN n 
1 307 LEU n 
1 308 ASP n 
1 309 GLU n 
1 310 SER n 
1 311 THR n 
1 312 ILE n 
1 313 ASP n 
1 314 ASN n 
1 315 LEU n 
1 316 ASN n 
1 317 LYS n 
1 318 ILE n 
1 319 LEU n 
1 320 GLN n 
1 321 VAL n 
1 322 PHE n 
1 323 VAL n 
1 324 LEU n 
1 325 GLU n 
1 326 TYR n 
1 327 LEU n 
1 328 HIS n 
1 329 LEU 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                   329 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 QPCT 
_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                   Human 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1D94 non-polymer         . '4-azanyl-~{N}-[2-(1~{H}-imidazol-4-yl)ethyl]-2-oxidanidyl-1,2,5-oxadiazol-2-ium-3-carboxamide' 
STK779818                       'C8 H10 N6 O3'   238.203 
ALA   'L-peptide linking' y ALANINE                                                                                         ? 
'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                                                        ? 
'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                                      ? 
'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                                 ? 
'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                                        ? 
'C3 H7 N O2 S'   121.158 
DMF   non-polymer         . DIMETHYLFORMAMIDE                                                                               ? 
'C3 H7 N O'      73.094  
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                                            ? 
'C2 H6 O S'      78.133  
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  
GOL   non-polymer         . GLYCEROL                                                                                        
'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS   'L-peptide linking' y HISTIDINE                                                                                       ? 
'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                                           ? 
'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                                      ? 
'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                         ? 
'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                                          ? 
'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                                                      ? 
'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                                   ? 
'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                                                         ? 
'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                                                          ? 
'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                                                       ? 
'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                                      ? 
'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                                                        ? 
'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                                                          ? 
'C5 H11 N O2'    117.146 
ZN    non-polymer         . 'ZINC ION'                                                                                      ? 
'Zn 2'           65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ALA 1   33  33  ALA ALA A . n 
A 1 2   SER 2   34  34  SER SER A . n 
A 1 3   ALA 3   35  35  ALA ALA A . n 
A 1 4   TRP 4   36  36  TRP TRP A . n 
A 1 5   PRO 5   37  37  PRO PRO A . n 
A 1 6   GLU 6   38  38  GLU GLU A . n 
A 1 7   GLU 7   39  39  GLU GLU A . n 
A 1 8   LYS 8   40  40  LYS LYS A . n 
A 1 9   ASN 9   41  41  ASN ASN A . n 
A 1 10  TYR 10  42  42  TYR TYR A . n 
A 1 11  HIS 11  43  43  HIS HIS A . n 
A 1 12  GLN 12  44  44  GLN GLN A . n 
A 1 13  PRO 13  45  45  PRO PRO A . n 
A 1 14  ALA 14  46  46  ALA ALA A . n 
A 1 15  ILE 15  47  47  ILE ILE A . n 
A 1 16  LEU 16  48  48  LEU LEU A . n 
A 1 17  ASN 17  49  49  ASN ASN A . n 
A 1 18  SER 18  50  50  SER SER A . n 
A 1 19  SER 19  51  51  SER SER A . n 
A 1 20  ALA 20  52  52  ALA ALA A . n 
A 1 21  LEU 21  53  53  LEU LEU A . n 
A 1 22  ARG 22  54  54  ARG ARG A . n 
A 1 23  GLN 23  55  55  GLN GLN A . n 
A 1 24  ILE 24  56  56  ILE ILE A . n 
A 1 25  ALA 25  57  57  ALA ALA A . n 
A 1 26  GLU 26  58  58  GLU GLU A . n 
A 1 27  GLY 27  59  59  GLY GLY A . n 
A 1 28  THR 28  60  60  THR THR A . n 
A 1 29  SER 29  61  61  SER SER A . n 
A 1 30  ILE 30  62  62  ILE ILE A . n 
A 1 31  SER 31  63  63  SER SER A . n 
A 1 32  GLU 32  64  64  GLU GLU A . n 
A 1 33  MET 33  65  65  MET MET A . n 
A 1 34  TRP 34  66  66  TRP TRP A . n 
A 1 35  GLN 35  67  67  GLN GLN A . n 
A 1 36  ASN 36  68  68  ASN ASN A . n 
A 1 37  ASP 37  69  69  ASP ASP A . n 
A 1 38  LEU 38  70  70  LEU LEU A . n 
A 1 39  GLN 39  71  71  GLN GLN A . n 
A 1 40  PRO 40  72  72  PRO PRO A . n 
A 1 41  LEU 41  73  73  LEU LEU A . n 
A 1 42  LEU 42  74  74  LEU LEU A . n 
A 1 43  ILE 43  75  75  ILE ILE A . n 
A 1 44  GLU 44  76  76  GLU GLU A . n 
A 1 45  ARG 45  77  77  ARG ARG A . n 
A 1 46  TYR 46  78  78  TYR TYR A . n 
A 1 47  PRO 47  79  79  PRO PRO A . n 
A 1 48  GLY 48  80  80  GLY GLY A . n 
A 1 49  SER 49  81  81  SER SER A . n 
A 1 50  PRO 50  82  82  PRO PRO A . n 
A 1 51  GLY 51  83  83  GLY GLY A . n 
A 1 52  SER 52  84  84  SER SER A . n 
A 1 53  TYR 53  85  85  TYR TYR A . n 
A 1 54  ALA 54  86  86  ALA ALA A . n 
A 1 55  ALA 55  87  87  ALA ALA A . n 
A 1 56  ARG 56  88  88  ARG ARG A . n 
A 1 57  GLN 57  89  89  GLN GLN A . n 
A 1 58  HIS 58  90  90  HIS HIS A . n 
A 1 59  ILE 59  91  91  ILE ILE A . n 
A 1 60  MET 60  92  92  MET MET A . n 
A 1 61  GLN 61  93  93  GLN GLN A . n 
A 1 62  ARG 62  94  94  ARG ARG A . n 
A 1 63  ILE 63  95  95  ILE ILE A . n 
A 1 64  GLN 64  96  96  GLN GLN A . n 
A 1 65  ARG 65  97  97  ARG ARG A . n 
A 1 66  LEU 66  98  98  LEU LEU A . n 
A 1 67  GLN 67  99  99  GLN GLN A . n 
A 1 68  ALA 68  100 100 ALA ALA A . n 
A 1 69  ASP 69  101 101 ASP ASP A . n 
A 1 70  TRP 70  102 102 TRP TRP A . n 
A 1 71  VAL 71  103 103 VAL VAL A . n 
A 1 72  LEU 72  104 104 LEU LEU A . n 
A 1 73  GLU 73  105 105 GLU GLU A . n 
A 1 74  ILE 74  106 106 ILE ILE A . n 
A 1 75  ASP 75  107 107 ASP ASP A . n 
A 1 76  THR 76  108 108 THR THR A . n 
A 1 77  PHE 77  109 109 PHE PHE A . n 
A 1 78  LEU 78  110 110 LEU LEU A . n 
A 1 79  SER 79  111 111 SER SER A . n 
A 1 80  GLN 80  112 112 GLN GLN A . n 
A 1 81  THR 81  113 113 THR THR A . n 
A 1 82  PRO 82  114 114 PRO PRO A . n 
A 1 83  TYR 83  115 115 TYR TYR A . n 
A 1 84  GLY 84  116 116 GLY GLY A . n 
A 1 85  TYR 85  117 117 TYR TYR A . n 
A 1 86  ARG 86  118 118 ARG ARG A . n 
A 1 87  SER 87  119 119 SER SER A . n 
A 1 88  PHE 88  120 120 PHE PHE A . n 
A 1 89  SER 89  121 121 SER SER A . n 
A 1 90  ASN 90  122 122 ASN ASN A . n 
A 1 91  ILE 91  123 123 ILE ILE A . n 
A 1 92  ILE 92  124 124 ILE ILE A . n 
A 1 93  SER 93  125 125 SER SER A . n 
A 1 94  THR 94  126 126 THR THR A . n 
A 1 95  LEU 95  127 127 LEU LEU A . n 
A 1 96  ASN 96  128 128 ASN ASN A . n 
A 1 97  PRO 97  129 129 PRO PRO A . n 
A 1 98  THR 98  130 130 THR THR A . n 
A 1 99  ALA 99  131 131 ALA ALA A . n 
A 1 100 LYS 100 132 132 LYS LYS A . n 
A 1 101 ARG 101 133 133 ARG ARG A . n 
A 1 102 HIS 102 134 134 HIS HIS A . n 
A 1 103 LEU 103 135 135 LEU LEU A . n 
A 1 104 VAL 104 136 136 VAL VAL A . n 
A 1 105 LEU 105 137 137 LEU LEU A . n 
A 1 106 ALA 106 138 138 ALA ALA A . n 
A 1 107 CYS 107 139 139 CYS CYS A . n 
A 1 108 HIS 108 140 140 HIS HIS A . n 
A 1 109 TYR 109 141 141 TYR TYR A . n 
A 1 110 ASP 110 142 142 ASP ASP A . n 
A 1 111 SER 111 143 143 SER SER A . n 
A 1 112 LYS 112 144 144 LYS LYS A . n 
A 1 113 TYR 113 145 145 TYR TYR A . n 
A 1 114 PHE 114 146 146 PHE PHE A . n 
A 1 115 SER 115 147 147 SER SER A . n 
A 1 116 HIS 116 148 148 HIS HIS A . n 
A 1 117 TRP 117 149 149 TRP TRP A . n 
A 1 118 ASN 118 150 150 ASN ASN A . n 
A 1 119 ASN 119 151 151 ASN ASN A . n 
A 1 120 ARG 120 152 152 ARG ARG A . n 
A 1 121 VAL 121 153 153 VAL VAL A . n 
A 1 122 PHE 122 154 154 PHE PHE A . n 
A 1 123 VAL 123 155 155 VAL VAL A . n 
A 1 124 GLY 124 156 156 GLY GLY A . n 
A 1 125 ALA 125 157 157 ALA ALA A . n 
A 1 126 THR 126 158 158 THR THR A . n 
A 1 127 ASP 127 159 159 ASP ASP A . n 
A 1 128 SER 128 160 160 SER SER A . n 
A 1 129 ALA 129 161 161 ALA ALA A . n 
A 1 130 VAL 130 162 162 VAL VAL A . n 
A 1 131 PRO 131 163 163 PRO PRO A . n 
A 1 132 CYS 132 164 164 CYS CYS A . n 
A 1 133 ALA 133 165 165 ALA ALA A . n 
A 1 134 MET 134 166 166 MET MET A . n 
A 1 135 MET 135 167 167 MET MET A . n 
A 1 136 LEU 136 168 168 LEU LEU A . n 
A 1 137 GLU 137 169 169 GLU GLU A . n 
A 1 138 LEU 138 170 170 LEU LEU A . n 
A 1 139 ALA 139 171 171 ALA ALA A . n 
A 1 140 ARG 140 172 172 ARG ARG A . n 
A 1 141 ALA 141 173 173 ALA ALA A . n 
A 1 142 LEU 142 174 174 LEU LEU A . n 
A 1 143 ASP 143 175 175 ASP ASP A . n 
A 1 144 LYS 144 176 176 LYS LYS A . n 
A 1 145 LYS 145 177 177 LYS LYS A . n 
A 1 146 LEU 146 178 178 LEU LEU A . n 
A 1 147 LEU 147 179 179 LEU LEU A . n 
A 1 148 SER 148 180 180 SER SER A . n 
A 1 149 LEU 149 181 181 LEU LEU A . n 
A 1 150 LYS 150 182 182 LYS LYS A . n 
A 1 151 THR 151 183 ?   ?   ?   A . n 
A 1 152 VAL 152 184 ?   ?   ?   A . n 
A 1 153 SER 153 185 ?   ?   ?   A . n 
A 1 154 ASP 154 186 ?   ?   ?   A . n 
A 1 155 SER 155 187 ?   ?   ?   A . n 
A 1 156 LYS 156 188 ?   ?   ?   A . n 
A 1 157 PRO 157 189 189 PRO PRO A . n 
A 1 158 ASP 158 190 190 ASP ASP A . n 
A 1 159 LEU 159 191 191 LEU LEU A . n 
A 1 160 SER 160 192 192 SER SER A . n 
A 1 161 LEU 161 193 193 LEU LEU A . n 
A 1 162 GLN 162 194 194 GLN GLN A . n 
A 1 163 LEU 163 195 195 LEU LEU A . n 
A 1 164 ILE 164 196 196 ILE ILE A . n 
A 1 165 PHE 165 197 197 PHE PHE A . n 
A 1 166 PHE 166 198 198 PHE PHE A . n 
A 1 167 ASP 167 199 199 ASP ASP A . n 
A 1 168 GLY 168 200 200 GLY GLY A . n 
A 1 169 GLU 169 201 201 GLU GLU A . n 
A 1 170 GLU 170 202 202 GLU GLU A . n 
A 1 171 ALA 171 203 203 ALA ALA A . n 
A 1 172 PHE 172 204 204 PHE PHE A . n 
A 1 173 LEU 173 205 205 LEU LEU A . n 
A 1 174 HIS 174 206 206 HIS HIS A . n 
A 1 175 TRP 175 207 207 TRP TRP A . n 
A 1 176 SER 176 208 208 SER SER A . n 
A 1 177 PRO 177 209 209 PRO PRO A . n 
A 1 178 GLN 178 210 210 GLN GLN A . n 
A 1 179 ASP 179 211 211 ASP ASP A . n 
A 1 180 SER 180 212 212 SER SER A . n 
A 1 181 LEU 181 213 213 LEU LEU A . n 
A 1 182 TYR 182 214 214 TYR TYR A . n 
A 1 183 GLY 183 215 215 GLY GLY A . n 
A 1 184 SER 184 216 216 SER SER A . n 
A 1 185 ARG 185 217 217 ARG ARG A . n 
A 1 186 HIS 186 218 218 HIS HIS A . n 
A 1 187 LEU 187 219 219 LEU LEU A . n 
A 1 188 ALA 188 220 220 ALA ALA A . n 
A 1 189 ALA 189 221 221 ALA ALA A . n 
A 1 190 LYS 190 222 222 LYS LYS A . n 
A 1 191 MET 191 223 223 MET MET A . n 
A 1 192 ALA 192 224 224 ALA ALA A . n 
A 1 193 SER 193 225 225 SER SER A . n 
A 1 194 THR 194 226 226 THR THR A . n 
A 1 195 PRO 195 227 227 PRO PRO A . n 
A 1 196 HIS 196 228 228 HIS HIS A . n 
A 1 197 PRO 197 229 229 PRO PRO A . n 
A 1 198 PRO 198 230 230 PRO PRO A . n 
A 1 199 GLY 199 231 231 GLY GLY A . n 
A 1 200 ALA 200 232 232 ALA ALA A . n 
A 1 201 ARG 201 233 233 ARG ARG A . n 
A 1 202 GLY 202 234 234 GLY GLY A . n 
A 1 203 THR 203 235 235 THR THR A . n 
A 1 204 SER 204 236 236 SER SER A . n 
A 1 205 GLN 205 237 237 GLN GLN A . n 
A 1 206 LEU 206 238 238 LEU LEU A . n 
A 1 207 HIS 207 239 239 HIS HIS A . n 
A 1 208 GLY 208 240 240 GLY GLY A . n 
A 1 209 MET 209 241 241 MET MET A . n 
A 1 210 ASP 210 242 242 ASP ASP A . n 
A 1 211 LEU 211 243 243 LEU LEU A . n 
A 1 212 LEU 212 244 244 LEU LEU A . n 
A 1 213 VAL 213 245 245 VAL VAL A . n 
A 1 214 LEU 214 246 246 LEU LEU A . n 
A 1 215 LEU 215 247 247 LEU LEU A . n 
A 1 216 ASP 216 248 248 ASP ASP A . n 
A 1 217 LEU 217 249 249 LEU LEU A . n 
A 1 218 ILE 218 250 250 ILE ILE A . n 
A 1 219 GLY 219 251 251 GLY GLY A . n 
A 1 220 ALA 220 252 252 ALA ALA A . n 
A 1 221 PRO 221 253 253 PRO PRO A . n 
A 1 222 ASN 222 254 254 ASN ASN A . n 
A 1 223 PRO 223 255 255 PRO PRO A . n 
A 1 224 THR 224 256 256 THR THR A . n 
A 1 225 PHE 225 257 257 PHE PHE A . n 
A 1 226 PRO 226 258 258 PRO PRO A . n 
A 1 227 ASN 227 259 259 ASN ASN A . n 
A 1 228 PHE 228 260 260 PHE PHE A . n 
A 1 229 PHE 229 261 261 PHE PHE A . n 
A 1 230 PRO 230 262 262 PRO PRO A . n 
A 1 231 ASN 231 263 263 ASN ASN A . n 
A 1 232 SER 232 264 264 SER SER A . n 
A 1 233 ALA 233 265 265 ALA ALA A . n 
A 1 234 ARG 234 266 266 ARG ARG A . n 
A 1 235 TRP 235 267 267 TRP TRP A . n 
A 1 236 PHE 236 268 268 PHE PHE A . n 
A 1 237 GLU 237 269 269 GLU GLU A . n 
A 1 238 ARG 238 270 270 ARG ARG A . n 
A 1 239 LEU 239 271 271 LEU LEU A . n 
A 1 240 GLN 240 272 272 GLN GLN A . n 
A 1 241 ALA 241 273 273 ALA ALA A . n 
A 1 242 ILE 242 274 274 ILE ILE A . n 
A 1 243 GLU 243 275 275 GLU GLU A . n 
A 1 244 HIS 244 276 276 HIS HIS A . n 
A 1 245 GLU 245 277 277 GLU GLU A . n 
A 1 246 LEU 246 278 278 LEU LEU A . n 
A 1 247 HIS 247 279 279 HIS HIS A . n 
A 1 248 GLU 248 280 280 GLU GLU A . n 
A 1 249 LEU 249 281 281 LEU LEU A . n 
A 1 250 GLY 250 282 282 GLY GLY A . n 
A 1 251 LEU 251 283 283 LEU LEU A . n 
A 1 252 LEU 252 284 284 LEU LEU A . n 
A 1 253 LYS 253 285 285 LYS LYS A . n 
A 1 254 ASP 254 286 286 ASP ASP A . n 
A 1 255 HIS 255 287 287 HIS HIS A . n 
A 1 256 SER 256 288 288 SER SER A . n 
A 1 257 LEU 257 289 289 LEU LEU A . n 
A 1 258 GLU 258 290 290 GLU GLU A . n 
A 1 259 GLY 259 291 291 GLY GLY A . n 
A 1 260 ARG 260 292 292 ARG ARG A . n 
A 1 261 TYR 261 293 293 TYR TYR A . n 
A 1 262 PHE 262 294 294 PHE PHE A . n 
A 1 263 GLN 263 295 295 GLN GLN A . n 
A 1 264 ASN 264 296 296 ASN ASN A . n 
A 1 265 TYR 265 297 297 TYR TYR A . n 
A 1 266 SER 266 298 298 SER SER A . n 
A 1 267 TYR 267 299 299 TYR TYR A . n 
A 1 268 GLY 268 300 300 GLY GLY A . n 
A 1 269 GLY 269 301 301 GLY GLY A . n 
A 1 270 VAL 270 302 302 VAL VAL A . n 
A 1 271 ILE 271 303 303 ILE ILE A . n 
A 1 272 GLN 272 304 304 GLN GLN A . n 
A 1 273 ASP 273 305 305 ASP ASP A . n 
A 1 274 ASP 274 306 306 ASP ASP A . n 
A 1 275 HIS 275 307 307 HIS HIS A . n 
A 1 276 ILE 276 308 308 ILE ILE A . n 
A 1 277 PRO 277 309 309 PRO PRO A . n 
A 1 278 PHE 278 310 310 PHE PHE A . n 
A 1 279 LEU 279 311 311 LEU LEU A . n 
A 1 280 ARG 280 312 312 ARG ARG A . n 
A 1 281 ARG 281 313 313 ARG ARG A . n 
A 1 282 GLY 282 314 314 GLY GLY A . n 
A 1 283 VAL 283 315 315 VAL VAL A . n 
A 1 284 PRO 284 316 316 PRO PRO A . n 
A 1 285 VAL 285 317 317 VAL VAL A . n 
A 1 286 LEU 286 318 318 LEU LEU A . n 
A 1 287 HIS 287 319 319 HIS HIS A . n 
A 1 288 LEU 288 320 320 LEU LEU A . n 
A 1 289 ILE 289 321 321 ILE ILE A . n 
A 1 290 PRO 290 322 322 PRO PRO A . n 
A 1 291 SER 291 323 323 SER SER A . n 
A 1 292 PRO 292 324 324 PRO PRO A . n 
A 1 293 PHE 293 325 325 PHE PHE A . n 
A 1 294 PRO 294 326 326 PRO PRO A . n 
A 1 295 GLU 295 327 327 GLU GLU A . n 
A 1 296 VAL 296 328 328 VAL VAL A . n 
A 1 297 TRP 297 329 329 TRP TRP A . n 
A 1 298 HIS 298 330 330 HIS HIS A . n 
A 1 299 THR 299 331 331 THR THR A . n 
A 1 300 MET 300 332 332 MET MET A . n 
A 1 301 ASP 301 333 333 ASP ASP A . n 
A 1 302 ASP 302 334 334 ASP ASP A . n 
A 1 303 ASN 303 335 335 ASN ASN A . n 
A 1 304 GLU 304 336 336 GLU GLU A . n 
A 1 305 GLU 305 337 337 GLU GLU A . n 
A 1 306 ASN 306 338 338 ASN ASN A . n 
A 1 307 LEU 307 339 339 LEU LEU A . n 
A 1 308 ASP 308 340 340 ASP ASP A . n 
A 1 309 GLU 309 341 341 GLU GLU A . n 
A 1 310 SER 310 342 342 SER SER A . n 
A 1 311 THR 311 343 343 THR THR A . n 
A 1 312 ILE 312 344 344 ILE ILE A . n 
A 1 313 ASP 313 345 345 ASP ASP A . n 
A 1 314 ASN 314 346 346 ASN ASN A . n 
A 1 315 LEU 315 347 347 LEU LEU A . n 
A 1 316 ASN 316 348 348 ASN ASN A . n 
A 1 317 LYS 317 349 349 LYS LYS A . n 
A 1 318 ILE 318 350 350 ILE ILE A . n 
A 1 319 LEU 319 351 351 LEU LEU A . n 
A 1 320 GLN 320 352 352 GLN GLN A . n 
A 1 321 VAL 321 353 353 VAL VAL A . n 
A 1 322 PHE 322 354 354 PHE PHE A . n 
A 1 323 VAL 323 355 355 VAL VAL A . n 
A 1 324 LEU 324 356 356 LEU LEU A . n 
A 1 325 GLU 325 357 357 GLU GLU A . n 
A 1 326 TYR 326 358 358 TYR TYR A . n 
A 1 327 LEU 327 359 359 LEU LEU A . n 
A 1 328 HIS 328 360 360 HIS HIS A . n 
A 1 329 LEU 329 361 361 LEU LEU A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1D94 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1D94 
_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 ZN    1  401 1  ZN    ZN  A . 
C 3 A1D94 1  402 1  A1D94 A08 A . 
D 4 DMS   1  403 2  DMS   DMS A . 
E 4 DMS   1  404 3  DMS   DMS A . 
F 5 GOL   1  405 1  GOL   GOL A . 
G 5 GOL   1  406 2  GOL   GOL A . 
H 5 GOL   1  407 3  GOL   GOL A . 
I 5 GOL   1  408 4  GOL   GOL A . 
J 6 DMF   1  409 2  DMF   DMF A . 
K 7 HOH   1  501 69 HOH   HOH A . 
K 7 HOH   2  502 65 HOH   HOH A . 
K 7 HOH   3  503 64 HOH   HOH A . 
K 7 HOH   4  504 51 HOH   HOH A . 
K 7 HOH   5  505 66 HOH   HOH A . 
K 7 HOH   6  506 71 HOH   HOH A . 
K 7 HOH   7  507 47 HOH   HOH A . 
K 7 HOH   8  508 68 HOH   HOH A . 
K 7 HOH   9  509 57 HOH   HOH A . 
K 7 HOH   10 510 43 HOH   HOH A . 
K 7 HOH   11 511 72 HOH   HOH A . 
K 7 HOH   12 512 46 HOH   HOH A . 
K 7 HOH   13 513 63 HOH   HOH A . 
K 7 HOH   14 514 54 HOH   HOH A . 
K 7 HOH   15 515 4  HOH   HOH A . 
K 7 HOH   16 516 62 HOH   HOH A . 
K 7 HOH   17 517 1  HOH   HOH A . 
K 7 HOH   18 518 33 HOH   HOH A . 
K 7 HOH   19 519 53 HOH   HOH A . 
K 7 HOH   20 520 70 HOH   HOH A . 
K 7 HOH   21 521 44 HOH   HOH A . 
K 7 HOH   22 522 60 HOH   HOH A . 
K 7 HOH   23 523 27 HOH   HOH A . 
K 7 HOH   24 524 32 HOH   HOH A . 
K 7 HOH   25 525 61 HOH   HOH A . 
K 7 HOH   26 526 35 HOH   HOH A . 
K 7 HOH   27 527 48 HOH   HOH A . 
K 7 HOH   28 528 39 HOH   HOH A . 
K 7 HOH   29 529 56 HOH   HOH A . 
K 7 HOH   30 530 59 HOH   HOH A . 
K 7 HOH   31 531 29 HOH   HOH A . 
K 7 HOH   32 532 17 HOH   HOH A . 
K 7 HOH   33 533 58 HOH   HOH A . 
K 7 HOH   34 534 34 HOH   HOH A . 
K 7 HOH   35 535 55 HOH   HOH A . 
K 7 HOH   36 536 67 HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.10.1_2155: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                    2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? .                    3 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9IVV 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     274.600 
_cell.length_a_esd                 ? 
_cell.length_b                     274.600 
_cell.length_b_esd                 ? 
_cell.length_c                     274.600 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        96 
_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                         9IVV 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                210 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'F 41 3 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9IVV 
_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             5.84 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          78.94 
_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, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '12-16% (v/v) polyethylene glycol 4000, 0.2 M MgCl2 and 0.1 M Tris-HCl at pH 8.5.' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     195 
_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 PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-07-21 
_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   0.97946 
_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                        'SSRF BEAMLINE BL18U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97946 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL18U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9IVV 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.96 
_reflns.d_resolution_low                               34.33 
_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                                     19047 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                76.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.99 
_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                                0.564 
_reflns.pdbx_Rpim_I_all                                0.064 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       1460010 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.560 
_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                                    2.96 
_reflns_shell.d_res_low                                     3.04 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           111460 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1392 
_reflns_shell.percent_possible_obs                          100.0 
_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                               80.1 
_reflns_shell.pdbx_chi_squared                              0.96 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.5 
_reflns_shell.pdbx_Rrim_I_all                               4.937 
_reflns_shell.pdbx_Rpim_I_all                               0.549 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.628 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  4.906 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9IVV 
_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                            2.961 
_refine.ls_d_res_low                             34.325 
_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                     19022 
_refine.ls_number_reflns_R_free                  1903 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.97 
_refine.ls_percent_reflns_R_free                 10.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2109 
_refine.ls_R_factor_R_free                       0.2552 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2060 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      3PBB 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 24.75 
_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                            0.37 
_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                       2.961 
_refine_hist.d_res_low                        34.325 
_refine_hist.number_atoms_solvent             36 
_refine_hist.number_atoms_total               2701 
_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        2610 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         55 
_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' ? 0.023  ? 2740 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.325  ? 3712 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 16.121 ? 1608 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.077  ? 391  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009  ? 481  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.9611 3.0351 . . 134 1204 100.00 . . . . 0.3052 . . . . . . . . . . . 0.3644 
'X-RAY DIFFRACTION' 3.0351 3.1171 . . 132 1189 100.00 . . . . 0.2880 . . . . . . . . . . . 0.3574 
'X-RAY DIFFRACTION' 3.1171 3.2088 . . 131 1185 100.00 . . . . 0.2775 . . . . . . . . . . . 0.3507 
'X-RAY DIFFRACTION' 3.2088 3.3123 . . 134 1197 100.00 . . . . 0.2727 . . . . . . . . . . . 0.3071 
'X-RAY DIFFRACTION' 3.3123 3.4305 . . 134 1209 100.00 . . . . 0.2515 . . . . . . . . . . . 0.3187 
'X-RAY DIFFRACTION' 3.4305 3.5677 . . 133 1198 100.00 . . . . 0.2398 . . . . . . . . . . . 0.2840 
'X-RAY DIFFRACTION' 3.5677 3.7299 . . 133 1197 100.00 . . . . 0.2192 . . . . . . . . . . . 0.2792 
'X-RAY DIFFRACTION' 3.7299 3.9263 . . 133 1203 100.00 . . . . 0.2122 . . . . . . . . . . . 0.2714 
'X-RAY DIFFRACTION' 3.9263 4.1719 . . 135 1209 100.00 . . . . 0.1748 . . . . . . . . . . . 0.2485 
'X-RAY DIFFRACTION' 4.1719 4.4934 . . 136 1226 100.00 . . . . 0.1658 . . . . . . . . . . . 0.1991 
'X-RAY DIFFRACTION' 4.4934 4.9444 . . 137 1230 100.00 . . . . 0.1513 . . . . . . . . . . . 0.1991 
'X-RAY DIFFRACTION' 4.9444 5.6571 . . 138 1239 100.00 . . . . 0.1704 . . . . . . . . . . . 0.1873 
'X-RAY DIFFRACTION' 5.6571 7.1169 . . 141 1273 100.00 . . . . 0.2024 . . . . . . . . . . . 0.2370 
'X-RAY DIFFRACTION' 7.1169 34.325 . . 152 1360 100.00 . . . . 0.2084 . . . . . . . . . . . 0.2656 
# 
_struct.entry_id                     9IVV 
_struct.title                        
;Crystal structure of human secretory glutaminyl cyclase in complex with the inhibitor 3-((2-(1H-imidazol-5-yl)ethyl)carbamoyl)-4-amino-1,2,5-oxadiazole 2-oxide (compound 13)
;
_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        9IVV 
_struct_keywords.text            'glutaminyl cyclase, inhibitor, complex, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 5 ? 
G N N 5 ? 
H N N 5 ? 
I N N 5 ? 
J N N 6 ? 
K N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    QPCT_HUMAN 
_struct_ref.pdbx_db_accession          Q16769 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;ASAWPEEKNYHQPAILNSSALRQIAEGTSISEMWQNDLQPLLIERYPGSPGSYAARQHIMQRIQRLQADWVLEIDTFLSQ
TPYGYRSFSNIISTLNPTAKRHLVLACHYDSKYFSHWNNRVFVGATDSAVPCAMMLELARALDKKLLSLKTVSDSKPDLS
LQLIFFDGEEAFLHWSPQDSLYGSRHLAAKMASTPHPPGARGTSQLHGMDLLVLLDLIGAPNPTFPNFFPNSARWFERLQ
AIEHELHELGLLKDHSLEGRYFQNYSYGGVIQDDHIPFLRRGVPVLHLIPSPFPEVWHTMDDNEENLDESTIDNLNKILQ
VFVLEYLHL
;
_struct_ref.pdbx_align_begin           33 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9IVV 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 329 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q16769 
_struct_ref_seq.db_align_beg                  33 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  361 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       33 
_struct_ref_seq.pdbx_auth_seq_align_end       361 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   hexameric 
_pdbx_struct_assembly.oligomeric_count     6 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 15490 ? 
1 MORE         -3    ? 
1 'SSA (A^2)'  71440 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2,3,4,5,6 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K 
# 
_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                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'       1_555 x,y,z 1.0  0.0  0.0  0.0            0.0  1.0  0.0  0.0            0.0  0.0  1.0  0.0           
2 'point symmetry operation' ?     ?     -1.0 0.0  0.0  -68.6500000000 0.0  0.0  1.0  -68.6500000000 0.0  1.0  0.0  68.6500000000 
3 'point symmetry operation' ?     ?     0.0  1.0  0.0  0.0            0.0  0.0  -1.0 0.0            -1.0 0.0  0.0  0.0           
4 'point symmetry operation' ?     ?     0.0  0.0  1.0  -68.6500000000 0.0  -1.0 0.0  -68.6500000000 1.0  0.0  0.0  68.6500000000 
5 'point symmetry operation' ?     ?     0.0  0.0  -1.0 0.0            1.0  0.0  0.0  0.0            0.0  -1.0 0.0  0.0           
6 'point symmetry operation' ?     ?     0.0  -1.0 0.0  -68.6500000000 -1.0 0.0  0.0  -68.6500000000 0.0  0.0  -1.0 68.6500000000 
# 
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 ALA A 3   ? GLU A 7   ? ALA A 35  GLU A 39  5 ? 5  
HELX_P HELX_P2  AA2 SER A 18  ? GLY A 27  ? SER A 50  GLY A 59  1 ? 10 
HELX_P HELX_P3  AA3 SER A 29  ? ASP A 37  ? SER A 61  ASP A 69  1 ? 9  
HELX_P HELX_P4  AA4 LEU A 38  ? LEU A 42  ? LEU A 70  LEU A 74  5 ? 5  
HELX_P HELX_P5  AA5 SER A 49  ? ARG A 65  ? SER A 81  ARG A 97  1 ? 17 
HELX_P HELX_P6  AA6 SER A 128 ? LEU A 142 ? SER A 160 LEU A 174 1 ? 15 
HELX_P HELX_P7  AA7 LEU A 146 ? LYS A 150 ? LEU A 178 LYS A 182 5 ? 5  
HELX_P HELX_P8  AA8 LEU A 181 ? SER A 193 ? LEU A 213 SER A 225 1 ? 13 
HELX_P HELX_P9  AA9 PHE A 229 ? ASN A 231 ? PHE A 261 ASN A 263 5 ? 3  
HELX_P HELX_P10 AB1 SER A 232 ? LEU A 249 ? SER A 264 LEU A 281 1 ? 18 
HELX_P HELX_P11 AB2 SER A 256 ? ARG A 260 ? SER A 288 ARG A 292 5 ? 5  
HELX_P HELX_P12 AB3 HIS A 275 ? ARG A 280 ? HIS A 307 ARG A 312 1 ? 6  
HELX_P HELX_P13 AB4 ASP A 308 ? HIS A 328 ? ASP A 340 HIS A 360 1 ? 21 
# 
_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 127 OD1 ? ? ? 1_555 B ZN    . ZN  ? ? A ASP 159 A ZN    401 1_555 ? ? ? ? ? ? ? 2.406 ? ? 
metalc2 metalc ? ? A ASP 127 OD2 ? ? ? 1_555 B ZN    . ZN  ? ? A ASP 159 A ZN    401 1_555 ? ? ? ? ? ? ? 2.016 ? ? 
metalc3 metalc ? ? A GLU 170 OE2 ? ? ? 1_555 B ZN    . ZN  ? ? A GLU 202 A ZN    401 1_555 ? ? ? ? ? ? ? 2.019 ? ? 
metalc4 metalc ? ? A HIS 298 NE2 ? ? ? 1_555 B ZN    . ZN  ? ? A HIS 330 A ZN    401 1_555 ? ? ? ? ? ? ? 2.063 ? ? 
metalc5 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C A1D94 . N08 ? ? A ZN  401 A A1D94 402 1_555 ? ? ? ? ? ? ? 2.042 ? ? 
# 
_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 127 ? A ASP 159 ? 1_555 ZN ? B ZN . ? A ZN 401 ? 1_555 OD2 ? A ASP   127 ? A ASP   159 ? 1_555 56.1  ? 
2  OD1 ? A ASP 127 ? A ASP 159 ? 1_555 ZN ? B ZN . ? A ZN 401 ? 1_555 OE2 ? A GLU   170 ? A GLU   202 ? 1_555 81.7  ? 
3  OD2 ? A ASP 127 ? A ASP 159 ? 1_555 ZN ? B ZN . ? A ZN 401 ? 1_555 OE2 ? A GLU   170 ? A GLU   202 ? 1_555 112.9 ? 
4  OD1 ? A ASP 127 ? A ASP 159 ? 1_555 ZN ? B ZN . ? A ZN 401 ? 1_555 NE2 ? A HIS   298 ? A HIS   330 ? 1_555 149.1 ? 
5  OD2 ? A ASP 127 ? A ASP 159 ? 1_555 ZN ? B ZN . ? A ZN 401 ? 1_555 NE2 ? A HIS   298 ? A HIS   330 ? 1_555 93.1  ? 
6  OE2 ? A GLU 170 ? A GLU 202 ? 1_555 ZN ? B ZN . ? A ZN 401 ? 1_555 NE2 ? A HIS   298 ? A HIS   330 ? 1_555 112.3 ? 
7  OD1 ? A ASP 127 ? A ASP 159 ? 1_555 ZN ? B ZN . ? A ZN 401 ? 1_555 N08 ? C A1D94 .   ? A A1D94 402 ? 1_555 84.1  ? 
8  OD2 ? A ASP 127 ? A ASP 159 ? 1_555 ZN ? B ZN . ? A ZN 401 ? 1_555 N08 ? C A1D94 .   ? A A1D94 402 ? 1_555 118.1 ? 
9  OE2 ? A GLU 170 ? A GLU 202 ? 1_555 ZN ? B ZN . ? A ZN 401 ? 1_555 N08 ? C A1D94 .   ? A A1D94 402 ? 1_555 104.2 ? 
10 NE2 ? A HIS 298 ? A HIS 330 ? 1_555 ZN ? B ZN . ? A ZN 401 ? 1_555 N08 ? C A1D94 .   ? A A1D94 402 ? 1_555 116.5 ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ASP 127 A . ? ASP 159 A SER 128 A ? SER 160 A 1 7.33  
2 HIS 196 A . ? HIS 228 A PRO 197 A ? PRO 229 A 1 -4.94 
3 SER 291 A . ? SER 323 A PRO 292 A ? PRO 324 A 1 9.69  
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   6 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? 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 VAL A 71  ? THR A 81  ? VAL A 103 THR A 113 
AA1 2 GLY A 84  ? THR A 94  ? GLY A 116 THR A 126 
AA1 3 LEU A 159 ? PHE A 166 ? LEU A 191 PHE A 198 
AA1 4 ARG A 101 ? HIS A 108 ? ARG A 133 HIS A 140 
AA1 5 MET A 209 ? LEU A 215 ? MET A 241 LEU A 247 
AA1 6 VAL A 285 ? LEU A 288 ? VAL A 317 LEU A 320 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 71  ? N VAL A 103 O THR A 94  ? O THR A 126 
AA1 2 3 N SER A 93  ? N SER A 125 O LEU A 163 ? O LEU A 195 
AA1 3 4 O SER A 160 ? O SER A 192 N LEU A 103 ? N LEU A 135 
AA1 4 5 N ALA A 106 ? N ALA A 138 O LEU A 215 ? O LEU A 247 
AA1 5 6 N LEU A 212 ? N LEU A 244 O LEU A 286 ? O LEU A 318 
# 
_pdbx_entry_details.entry_id                   9IVV 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A HIS 228 ? ? OG1 A THR 235 ? ? 1.69 
2 1 O   A THR 130 ? ? O   A HOH 501 ? ? 1.92 
3 1 O   A PRO 209 ? ? O   A HOH 502 ? ? 2.03 
4 1 OD1 A ASN 348 ? ? O   A HOH 503 ? ? 2.09 
5 1 O   A TYR 78  ? ? OG  A SER 81  ? ? 2.19 
# 
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 PRO A 37  ? ? -64.49  9.64    
2  1 SER A 50  ? ? -23.27  -41.26  
3  1 ARG A 77  ? ? -145.35 56.95   
4  1 ASP A 107 ? ? -115.64 64.61   
5  1 PRO A 114 ? ? -32.88  -70.87  
6  1 TYR A 115 ? ? -67.06  13.79   
7  1 SER A 121 ? ? -151.97 88.57   
8  1 SER A 160 ? ? -147.90 48.60   
9  1 ALA A 173 ? ? -39.34  -32.25  
10 1 SER A 180 ? ? -49.02  6.10    
11 1 LEU A 205 ? ? -120.82 -76.27  
12 1 ASP A 211 ? ? -118.22 79.92   
13 1 SER A 212 ? ? 168.52  149.47  
14 1 ARG A 233 ? ? -144.43 20.34   
15 1 SER A 236 ? ? -76.04  -165.63 
16 1 ASP A 305 ? ? 179.43  171.28  
17 1 ASP A 306 ? ? -58.37  0.24    
# 
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 THR 183 ? A THR 151 
2 1 Y 1 A VAL 184 ? A VAL 152 
3 1 Y 1 A SER 185 ? A SER 153 
4 1 Y 1 A ASP 186 ? A ASP 154 
5 1 Y 1 A SER 187 ? A SER 155 
6 1 Y 1 A LYS 188 ? A LYS 156 
# 
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 
A1D94 C11  C  Y N 1   
A1D94 C16  C  Y N 2   
A1D94 N17  N  N N 3   
A1D94 O01  O  N N 4   
A1D94 C02  C  N N 5   
A1D94 N03  N  N N 6   
A1D94 C04  C  N N 7   
A1D94 C05  C  N N 8   
A1D94 C06  C  Y N 9   
A1D94 C07  C  Y N 10  
A1D94 N08  N  Y N 11  
A1D94 C09  C  Y N 12  
A1D94 N10  N  Y N 13  
A1D94 N12  N  Y N 14  
A1D94 O13  O  N N 15  
A1D94 O14  O  Y N 16  
A1D94 N15  N  Y N 17  
A1D94 H1   H  N N 18  
A1D94 H2   H  N N 19  
A1D94 H3   H  N N 20  
A1D94 H4   H  N N 21  
A1D94 H5   H  N N 22  
A1D94 H6   H  N N 23  
A1D94 H7   H  N N 24  
A1D94 H8   H  N N 25  
A1D94 H9   H  N N 26  
A1D94 H10  H  N N 27  
ALA   N    N  N N 28  
ALA   CA   C  N S 29  
ALA   C    C  N N 30  
ALA   O    O  N N 31  
ALA   CB   C  N N 32  
ALA   OXT  O  N N 33  
ALA   H    H  N N 34  
ALA   H2   H  N N 35  
ALA   HA   H  N N 36  
ALA   HB1  H  N N 37  
ALA   HB2  H  N N 38  
ALA   HB3  H  N N 39  
ALA   HXT  H  N N 40  
ARG   N    N  N N 41  
ARG   CA   C  N S 42  
ARG   C    C  N N 43  
ARG   O    O  N N 44  
ARG   CB   C  N N 45  
ARG   CG   C  N N 46  
ARG   CD   C  N N 47  
ARG   NE   N  N N 48  
ARG   CZ   C  N N 49  
ARG   NH1  N  N N 50  
ARG   NH2  N  N N 51  
ARG   OXT  O  N N 52  
ARG   H    H  N N 53  
ARG   H2   H  N N 54  
ARG   HA   H  N N 55  
ARG   HB2  H  N N 56  
ARG   HB3  H  N N 57  
ARG   HG2  H  N N 58  
ARG   HG3  H  N N 59  
ARG   HD2  H  N N 60  
ARG   HD3  H  N N 61  
ARG   HE   H  N N 62  
ARG   HH11 H  N N 63  
ARG   HH12 H  N N 64  
ARG   HH21 H  N N 65  
ARG   HH22 H  N N 66  
ARG   HXT  H  N N 67  
ASN   N    N  N N 68  
ASN   CA   C  N S 69  
ASN   C    C  N N 70  
ASN   O    O  N N 71  
ASN   CB   C  N N 72  
ASN   CG   C  N N 73  
ASN   OD1  O  N N 74  
ASN   ND2  N  N N 75  
ASN   OXT  O  N N 76  
ASN   H    H  N N 77  
ASN   H2   H  N N 78  
ASN   HA   H  N N 79  
ASN   HB2  H  N N 80  
ASN   HB3  H  N N 81  
ASN   HD21 H  N N 82  
ASN   HD22 H  N N 83  
ASN   HXT  H  N N 84  
ASP   N    N  N N 85  
ASP   CA   C  N S 86  
ASP   C    C  N N 87  
ASP   O    O  N N 88  
ASP   CB   C  N N 89  
ASP   CG   C  N N 90  
ASP   OD1  O  N N 91  
ASP   OD2  O  N N 92  
ASP   OXT  O  N N 93  
ASP   H    H  N N 94  
ASP   H2   H  N N 95  
ASP   HA   H  N N 96  
ASP   HB2  H  N N 97  
ASP   HB3  H  N N 98  
ASP   HD2  H  N N 99  
ASP   HXT  H  N N 100 
CYS   N    N  N N 101 
CYS   CA   C  N R 102 
CYS   C    C  N N 103 
CYS   O    O  N N 104 
CYS   CB   C  N N 105 
CYS   SG   S  N N 106 
CYS   OXT  O  N N 107 
CYS   H    H  N N 108 
CYS   H2   H  N N 109 
CYS   HA   H  N N 110 
CYS   HB2  H  N N 111 
CYS   HB3  H  N N 112 
CYS   HG   H  N N 113 
CYS   HXT  H  N N 114 
DMF   C1   C  N N 115 
DMF   C2   C  N N 116 
DMF   C    C  N N 117 
DMF   O    O  N N 118 
DMF   N    N  N N 119 
DMF   H11  H  N N 120 
DMF   H12  H  N N 121 
DMF   H13  H  N N 122 
DMF   H21  H  N N 123 
DMF   H22  H  N N 124 
DMF   H23  H  N N 125 
DMF   HC   H  N N 126 
DMS   S    S  N N 127 
DMS   O    O  N N 128 
DMS   C1   C  N N 129 
DMS   C2   C  N N 130 
DMS   H11  H  N N 131 
DMS   H12  H  N N 132 
DMS   H13  H  N N 133 
DMS   H21  H  N N 134 
DMS   H22  H  N N 135 
DMS   H23  H  N N 136 
GLN   N    N  N N 137 
GLN   CA   C  N S 138 
GLN   C    C  N N 139 
GLN   O    O  N N 140 
GLN   CB   C  N N 141 
GLN   CG   C  N N 142 
GLN   CD   C  N N 143 
GLN   OE1  O  N N 144 
GLN   NE2  N  N N 145 
GLN   OXT  O  N N 146 
GLN   H    H  N N 147 
GLN   H2   H  N N 148 
GLN   HA   H  N N 149 
GLN   HB2  H  N N 150 
GLN   HB3  H  N N 151 
GLN   HG2  H  N N 152 
GLN   HG3  H  N N 153 
GLN   HE21 H  N N 154 
GLN   HE22 H  N N 155 
GLN   HXT  H  N N 156 
GLU   N    N  N N 157 
GLU   CA   C  N S 158 
GLU   C    C  N N 159 
GLU   O    O  N N 160 
GLU   CB   C  N N 161 
GLU   CG   C  N N 162 
GLU   CD   C  N N 163 
GLU   OE1  O  N N 164 
GLU   OE2  O  N N 165 
GLU   OXT  O  N N 166 
GLU   H    H  N N 167 
GLU   H2   H  N N 168 
GLU   HA   H  N N 169 
GLU   HB2  H  N N 170 
GLU   HB3  H  N N 171 
GLU   HG2  H  N N 172 
GLU   HG3  H  N N 173 
GLU   HE2  H  N N 174 
GLU   HXT  H  N N 175 
GLY   N    N  N N 176 
GLY   CA   C  N N 177 
GLY   C    C  N N 178 
GLY   O    O  N N 179 
GLY   OXT  O  N N 180 
GLY   H    H  N N 181 
GLY   H2   H  N N 182 
GLY   HA2  H  N N 183 
GLY   HA3  H  N N 184 
GLY   HXT  H  N N 185 
GOL   C1   C  N N 186 
GOL   O1   O  N N 187 
GOL   C2   C  N N 188 
GOL   O2   O  N N 189 
GOL   C3   C  N N 190 
GOL   O3   O  N N 191 
GOL   H11  H  N N 192 
GOL   H12  H  N N 193 
GOL   HO1  H  N N 194 
GOL   H2   H  N N 195 
GOL   HO2  H  N N 196 
GOL   H31  H  N N 197 
GOL   H32  H  N N 198 
GOL   HO3  H  N N 199 
HIS   N    N  N N 200 
HIS   CA   C  N S 201 
HIS   C    C  N N 202 
HIS   O    O  N N 203 
HIS   CB   C  N N 204 
HIS   CG   C  Y N 205 
HIS   ND1  N  Y N 206 
HIS   CD2  C  Y N 207 
HIS   CE1  C  Y N 208 
HIS   NE2  N  Y N 209 
HIS   OXT  O  N N 210 
HIS   H    H  N N 211 
HIS   H2   H  N N 212 
HIS   HA   H  N N 213 
HIS   HB2  H  N N 214 
HIS   HB3  H  N N 215 
HIS   HD1  H  N N 216 
HIS   HD2  H  N N 217 
HIS   HE1  H  N N 218 
HIS   HE2  H  N N 219 
HIS   HXT  H  N N 220 
HOH   O    O  N N 221 
HOH   H1   H  N N 222 
HOH   H2   H  N N 223 
ILE   N    N  N N 224 
ILE   CA   C  N S 225 
ILE   C    C  N N 226 
ILE   O    O  N N 227 
ILE   CB   C  N S 228 
ILE   CG1  C  N N 229 
ILE   CG2  C  N N 230 
ILE   CD1  C  N N 231 
ILE   OXT  O  N N 232 
ILE   H    H  N N 233 
ILE   H2   H  N N 234 
ILE   HA   H  N N 235 
ILE   HB   H  N N 236 
ILE   HG12 H  N N 237 
ILE   HG13 H  N N 238 
ILE   HG21 H  N N 239 
ILE   HG22 H  N N 240 
ILE   HG23 H  N N 241 
ILE   HD11 H  N N 242 
ILE   HD12 H  N N 243 
ILE   HD13 H  N N 244 
ILE   HXT  H  N N 245 
LEU   N    N  N N 246 
LEU   CA   C  N S 247 
LEU   C    C  N N 248 
LEU   O    O  N N 249 
LEU   CB   C  N N 250 
LEU   CG   C  N N 251 
LEU   CD1  C  N N 252 
LEU   CD2  C  N N 253 
LEU   OXT  O  N N 254 
LEU   H    H  N N 255 
LEU   H2   H  N N 256 
LEU   HA   H  N N 257 
LEU   HB2  H  N N 258 
LEU   HB3  H  N N 259 
LEU   HG   H  N N 260 
LEU   HD11 H  N N 261 
LEU   HD12 H  N N 262 
LEU   HD13 H  N N 263 
LEU   HD21 H  N N 264 
LEU   HD22 H  N N 265 
LEU   HD23 H  N N 266 
LEU   HXT  H  N N 267 
LYS   N    N  N N 268 
LYS   CA   C  N S 269 
LYS   C    C  N N 270 
LYS   O    O  N N 271 
LYS   CB   C  N N 272 
LYS   CG   C  N N 273 
LYS   CD   C  N N 274 
LYS   CE   C  N N 275 
LYS   NZ   N  N N 276 
LYS   OXT  O  N N 277 
LYS   H    H  N N 278 
LYS   H2   H  N N 279 
LYS   HA   H  N N 280 
LYS   HB2  H  N N 281 
LYS   HB3  H  N N 282 
LYS   HG2  H  N N 283 
LYS   HG3  H  N N 284 
LYS   HD2  H  N N 285 
LYS   HD3  H  N N 286 
LYS   HE2  H  N N 287 
LYS   HE3  H  N N 288 
LYS   HZ1  H  N N 289 
LYS   HZ2  H  N N 290 
LYS   HZ3  H  N N 291 
LYS   HXT  H  N N 292 
MET   N    N  N N 293 
MET   CA   C  N S 294 
MET   C    C  N N 295 
MET   O    O  N N 296 
MET   CB   C  N N 297 
MET   CG   C  N N 298 
MET   SD   S  N N 299 
MET   CE   C  N N 300 
MET   OXT  O  N N 301 
MET   H    H  N N 302 
MET   H2   H  N N 303 
MET   HA   H  N N 304 
MET   HB2  H  N N 305 
MET   HB3  H  N N 306 
MET   HG2  H  N N 307 
MET   HG3  H  N N 308 
MET   HE1  H  N N 309 
MET   HE2  H  N N 310 
MET   HE3  H  N N 311 
MET   HXT  H  N N 312 
PHE   N    N  N N 313 
PHE   CA   C  N S 314 
PHE   C    C  N N 315 
PHE   O    O  N N 316 
PHE   CB   C  N N 317 
PHE   CG   C  Y N 318 
PHE   CD1  C  Y N 319 
PHE   CD2  C  Y N 320 
PHE   CE1  C  Y N 321 
PHE   CE2  C  Y N 322 
PHE   CZ   C  Y N 323 
PHE   OXT  O  N N 324 
PHE   H    H  N N 325 
PHE   H2   H  N N 326 
PHE   HA   H  N N 327 
PHE   HB2  H  N N 328 
PHE   HB3  H  N N 329 
PHE   HD1  H  N N 330 
PHE   HD2  H  N N 331 
PHE   HE1  H  N N 332 
PHE   HE2  H  N N 333 
PHE   HZ   H  N N 334 
PHE   HXT  H  N N 335 
PRO   N    N  N N 336 
PRO   CA   C  N S 337 
PRO   C    C  N N 338 
PRO   O    O  N N 339 
PRO   CB   C  N N 340 
PRO   CG   C  N N 341 
PRO   CD   C  N N 342 
PRO   OXT  O  N N 343 
PRO   H    H  N N 344 
PRO   HA   H  N N 345 
PRO   HB2  H  N N 346 
PRO   HB3  H  N N 347 
PRO   HG2  H  N N 348 
PRO   HG3  H  N N 349 
PRO   HD2  H  N N 350 
PRO   HD3  H  N N 351 
PRO   HXT  H  N N 352 
SER   N    N  N N 353 
SER   CA   C  N S 354 
SER   C    C  N N 355 
SER   O    O  N N 356 
SER   CB   C  N N 357 
SER   OG   O  N N 358 
SER   OXT  O  N N 359 
SER   H    H  N N 360 
SER   H2   H  N N 361 
SER   HA   H  N N 362 
SER   HB2  H  N N 363 
SER   HB3  H  N N 364 
SER   HG   H  N N 365 
SER   HXT  H  N N 366 
THR   N    N  N N 367 
THR   CA   C  N S 368 
THR   C    C  N N 369 
THR   O    O  N N 370 
THR   CB   C  N R 371 
THR   OG1  O  N N 372 
THR   CG2  C  N N 373 
THR   OXT  O  N N 374 
THR   H    H  N N 375 
THR   H2   H  N N 376 
THR   HA   H  N N 377 
THR   HB   H  N N 378 
THR   HG1  H  N N 379 
THR   HG21 H  N N 380 
THR   HG22 H  N N 381 
THR   HG23 H  N N 382 
THR   HXT  H  N N 383 
TRP   N    N  N N 384 
TRP   CA   C  N S 385 
TRP   C    C  N N 386 
TRP   O    O  N N 387 
TRP   CB   C  N N 388 
TRP   CG   C  Y N 389 
TRP   CD1  C  Y N 390 
TRP   CD2  C  Y N 391 
TRP   NE1  N  Y N 392 
TRP   CE2  C  Y N 393 
TRP   CE3  C  Y N 394 
TRP   CZ2  C  Y N 395 
TRP   CZ3  C  Y N 396 
TRP   CH2  C  Y N 397 
TRP   OXT  O  N N 398 
TRP   H    H  N N 399 
TRP   H2   H  N N 400 
TRP   HA   H  N N 401 
TRP   HB2  H  N N 402 
TRP   HB3  H  N N 403 
TRP   HD1  H  N N 404 
TRP   HE1  H  N N 405 
TRP   HE3  H  N N 406 
TRP   HZ2  H  N N 407 
TRP   HZ3  H  N N 408 
TRP   HH2  H  N N 409 
TRP   HXT  H  N N 410 
TYR   N    N  N N 411 
TYR   CA   C  N S 412 
TYR   C    C  N N 413 
TYR   O    O  N N 414 
TYR   CB   C  N N 415 
TYR   CG   C  Y N 416 
TYR   CD1  C  Y N 417 
TYR   CD2  C  Y N 418 
TYR   CE1  C  Y N 419 
TYR   CE2  C  Y N 420 
TYR   CZ   C  Y N 421 
TYR   OH   O  N N 422 
TYR   OXT  O  N N 423 
TYR   H    H  N N 424 
TYR   H2   H  N N 425 
TYR   HA   H  N N 426 
TYR   HB2  H  N N 427 
TYR   HB3  H  N N 428 
TYR   HD1  H  N N 429 
TYR   HD2  H  N N 430 
TYR   HE1  H  N N 431 
TYR   HE2  H  N N 432 
TYR   HH   H  N N 433 
TYR   HXT  H  N N 434 
VAL   N    N  N N 435 
VAL   CA   C  N S 436 
VAL   C    C  N N 437 
VAL   O    O  N N 438 
VAL   CB   C  N N 439 
VAL   CG1  C  N N 440 
VAL   CG2  C  N N 441 
VAL   OXT  O  N N 442 
VAL   H    H  N N 443 
VAL   H2   H  N N 444 
VAL   HA   H  N N 445 
VAL   HB   H  N N 446 
VAL   HG11 H  N N 447 
VAL   HG12 H  N N 448 
VAL   HG13 H  N N 449 
VAL   HG21 H  N N 450 
VAL   HG22 H  N N 451 
VAL   HG23 H  N N 452 
VAL   HXT  H  N N 453 
ZN    ZN   ZN N N 454 
# 
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 
A1D94 C09 N08  sing Y N 1   
A1D94 C09 N10  doub Y N 2   
A1D94 N08 C07  sing Y N 3   
A1D94 N10 C06  sing Y N 4   
A1D94 C07 C06  doub Y N 5   
A1D94 C06 C05  sing N N 6   
A1D94 C05 C04  sing N N 7   
A1D94 C04 N03  sing N N 8   
A1D94 N03 C02  sing N N 9   
A1D94 O13 N12  sing N N 10  
A1D94 N12 C11  doub Y N 11  
A1D94 N12 O14  sing Y N 12  
A1D94 C02 C11  sing N N 13  
A1D94 C02 O01  doub N N 14  
A1D94 C11 C16  sing Y N 15  
A1D94 O14 N15  sing Y N 16  
A1D94 C16 N15  doub Y N 17  
A1D94 C16 N17  sing N N 18  
A1D94 N17 H1   sing N N 19  
A1D94 N17 H2   sing N N 20  
A1D94 N03 H3   sing N N 21  
A1D94 C04 H4   sing N N 22  
A1D94 C04 H5   sing N N 23  
A1D94 C05 H6   sing N N 24  
A1D94 C05 H7   sing N N 25  
A1D94 C07 H8   sing N N 26  
A1D94 N08 H9   sing N N 27  
A1D94 C09 H10  sing N N 28  
ALA   N   CA   sing N N 29  
ALA   N   H    sing N N 30  
ALA   N   H2   sing N N 31  
ALA   CA  C    sing N N 32  
ALA   CA  CB   sing N N 33  
ALA   CA  HA   sing N N 34  
ALA   C   O    doub N N 35  
ALA   C   OXT  sing N N 36  
ALA   CB  HB1  sing N N 37  
ALA   CB  HB2  sing N N 38  
ALA   CB  HB3  sing N N 39  
ALA   OXT HXT  sing N N 40  
ARG   N   CA   sing N N 41  
ARG   N   H    sing N N 42  
ARG   N   H2   sing N N 43  
ARG   CA  C    sing N N 44  
ARG   CA  CB   sing N N 45  
ARG   CA  HA   sing N N 46  
ARG   C   O    doub N N 47  
ARG   C   OXT  sing N N 48  
ARG   CB  CG   sing N N 49  
ARG   CB  HB2  sing N N 50  
ARG   CB  HB3  sing N N 51  
ARG   CG  CD   sing N N 52  
ARG   CG  HG2  sing N N 53  
ARG   CG  HG3  sing N N 54  
ARG   CD  NE   sing N N 55  
ARG   CD  HD2  sing N N 56  
ARG   CD  HD3  sing N N 57  
ARG   NE  CZ   sing N N 58  
ARG   NE  HE   sing N N 59  
ARG   CZ  NH1  sing N N 60  
ARG   CZ  NH2  doub N N 61  
ARG   NH1 HH11 sing N N 62  
ARG   NH1 HH12 sing N N 63  
ARG   NH2 HH21 sing N N 64  
ARG   NH2 HH22 sing N N 65  
ARG   OXT HXT  sing N N 66  
ASN   N   CA   sing N N 67  
ASN   N   H    sing N N 68  
ASN   N   H2   sing N N 69  
ASN   CA  C    sing N N 70  
ASN   CA  CB   sing N N 71  
ASN   CA  HA   sing N N 72  
ASN   C   O    doub N N 73  
ASN   C   OXT  sing N N 74  
ASN   CB  CG   sing N N 75  
ASN   CB  HB2  sing N N 76  
ASN   CB  HB3  sing N N 77  
ASN   CG  OD1  doub N N 78  
ASN   CG  ND2  sing N N 79  
ASN   ND2 HD21 sing N N 80  
ASN   ND2 HD22 sing N N 81  
ASN   OXT HXT  sing N N 82  
ASP   N   CA   sing N N 83  
ASP   N   H    sing N N 84  
ASP   N   H2   sing N N 85  
ASP   CA  C    sing N N 86  
ASP   CA  CB   sing N N 87  
ASP   CA  HA   sing N N 88  
ASP   C   O    doub N N 89  
ASP   C   OXT  sing N N 90  
ASP   CB  CG   sing N N 91  
ASP   CB  HB2  sing N N 92  
ASP   CB  HB3  sing N N 93  
ASP   CG  OD1  doub N N 94  
ASP   CG  OD2  sing N N 95  
ASP   OD2 HD2  sing N N 96  
ASP   OXT HXT  sing N N 97  
CYS   N   CA   sing N N 98  
CYS   N   H    sing N N 99  
CYS   N   H2   sing N N 100 
CYS   CA  C    sing N N 101 
CYS   CA  CB   sing N N 102 
CYS   CA  HA   sing N N 103 
CYS   C   O    doub N N 104 
CYS   C   OXT  sing N N 105 
CYS   CB  SG   sing N N 106 
CYS   CB  HB2  sing N N 107 
CYS   CB  HB3  sing N N 108 
CYS   SG  HG   sing N N 109 
CYS   OXT HXT  sing N N 110 
DMF   C1  N    sing N N 111 
DMF   C1  H11  sing N N 112 
DMF   C1  H12  sing N N 113 
DMF   C1  H13  sing N N 114 
DMF   C2  N    sing N N 115 
DMF   C2  H21  sing N N 116 
DMF   C2  H22  sing N N 117 
DMF   C2  H23  sing N N 118 
DMF   C   O    doub N N 119 
DMF   C   N    sing N N 120 
DMF   C   HC   sing N N 121 
DMS   S   O    doub N N 122 
DMS   S   C1   sing N N 123 
DMS   S   C2   sing N N 124 
DMS   C1  H11  sing N N 125 
DMS   C1  H12  sing N N 126 
DMS   C1  H13  sing N N 127 
DMS   C2  H21  sing N N 128 
DMS   C2  H22  sing N N 129 
DMS   C2  H23  sing N N 130 
GLN   N   CA   sing N N 131 
GLN   N   H    sing N N 132 
GLN   N   H2   sing N N 133 
GLN   CA  C    sing N N 134 
GLN   CA  CB   sing N N 135 
GLN   CA  HA   sing N N 136 
GLN   C   O    doub N N 137 
GLN   C   OXT  sing N N 138 
GLN   CB  CG   sing N N 139 
GLN   CB  HB2  sing N N 140 
GLN   CB  HB3  sing N N 141 
GLN   CG  CD   sing N N 142 
GLN   CG  HG2  sing N N 143 
GLN   CG  HG3  sing N N 144 
GLN   CD  OE1  doub N N 145 
GLN   CD  NE2  sing N N 146 
GLN   NE2 HE21 sing N N 147 
GLN   NE2 HE22 sing N N 148 
GLN   OXT HXT  sing N N 149 
GLU   N   CA   sing N N 150 
GLU   N   H    sing N N 151 
GLU   N   H2   sing N N 152 
GLU   CA  C    sing N N 153 
GLU   CA  CB   sing N N 154 
GLU   CA  HA   sing N N 155 
GLU   C   O    doub N N 156 
GLU   C   OXT  sing N N 157 
GLU   CB  CG   sing N N 158 
GLU   CB  HB2  sing N N 159 
GLU   CB  HB3  sing N N 160 
GLU   CG  CD   sing N N 161 
GLU   CG  HG2  sing N N 162 
GLU   CG  HG3  sing N N 163 
GLU   CD  OE1  doub N N 164 
GLU   CD  OE2  sing N N 165 
GLU   OE2 HE2  sing N N 166 
GLU   OXT HXT  sing N N 167 
GLY   N   CA   sing N N 168 
GLY   N   H    sing N N 169 
GLY   N   H2   sing N N 170 
GLY   CA  C    sing N N 171 
GLY   CA  HA2  sing N N 172 
GLY   CA  HA3  sing N N 173 
GLY   C   O    doub N N 174 
GLY   C   OXT  sing N N 175 
GLY   OXT HXT  sing N N 176 
GOL   C1  O1   sing N N 177 
GOL   C1  C2   sing N N 178 
GOL   C1  H11  sing N N 179 
GOL   C1  H12  sing N N 180 
GOL   O1  HO1  sing N N 181 
GOL   C2  O2   sing N N 182 
GOL   C2  C3   sing N N 183 
GOL   C2  H2   sing N N 184 
GOL   O2  HO2  sing N N 185 
GOL   C3  O3   sing N N 186 
GOL   C3  H31  sing N N 187 
GOL   C3  H32  sing N N 188 
GOL   O3  HO3  sing N N 189 
HIS   N   CA   sing N N 190 
HIS   N   H    sing N N 191 
HIS   N   H2   sing N N 192 
HIS   CA  C    sing N N 193 
HIS   CA  CB   sing N N 194 
HIS   CA  HA   sing N N 195 
HIS   C   O    doub N N 196 
HIS   C   OXT  sing N N 197 
HIS   CB  CG   sing N N 198 
HIS   CB  HB2  sing N N 199 
HIS   CB  HB3  sing N N 200 
HIS   CG  ND1  sing Y N 201 
HIS   CG  CD2  doub Y N 202 
HIS   ND1 CE1  doub Y N 203 
HIS   ND1 HD1  sing N N 204 
HIS   CD2 NE2  sing Y N 205 
HIS   CD2 HD2  sing N N 206 
HIS   CE1 NE2  sing Y N 207 
HIS   CE1 HE1  sing N N 208 
HIS   NE2 HE2  sing N N 209 
HIS   OXT HXT  sing N N 210 
HOH   O   H1   sing N N 211 
HOH   O   H2   sing N N 212 
ILE   N   CA   sing N N 213 
ILE   N   H    sing N N 214 
ILE   N   H2   sing N N 215 
ILE   CA  C    sing N N 216 
ILE   CA  CB   sing N N 217 
ILE   CA  HA   sing N N 218 
ILE   C   O    doub N N 219 
ILE   C   OXT  sing N N 220 
ILE   CB  CG1  sing N N 221 
ILE   CB  CG2  sing N N 222 
ILE   CB  HB   sing N N 223 
ILE   CG1 CD1  sing N N 224 
ILE   CG1 HG12 sing N N 225 
ILE   CG1 HG13 sing N N 226 
ILE   CG2 HG21 sing N N 227 
ILE   CG2 HG22 sing N N 228 
ILE   CG2 HG23 sing N N 229 
ILE   CD1 HD11 sing N N 230 
ILE   CD1 HD12 sing N N 231 
ILE   CD1 HD13 sing N N 232 
ILE   OXT HXT  sing N N 233 
LEU   N   CA   sing N N 234 
LEU   N   H    sing N N 235 
LEU   N   H2   sing N N 236 
LEU   CA  C    sing N N 237 
LEU   CA  CB   sing N N 238 
LEU   CA  HA   sing N N 239 
LEU   C   O    doub N N 240 
LEU   C   OXT  sing N N 241 
LEU   CB  CG   sing N N 242 
LEU   CB  HB2  sing N N 243 
LEU   CB  HB3  sing N N 244 
LEU   CG  CD1  sing N N 245 
LEU   CG  CD2  sing N N 246 
LEU   CG  HG   sing N N 247 
LEU   CD1 HD11 sing N N 248 
LEU   CD1 HD12 sing N N 249 
LEU   CD1 HD13 sing N N 250 
LEU   CD2 HD21 sing N N 251 
LEU   CD2 HD22 sing N N 252 
LEU   CD2 HD23 sing N N 253 
LEU   OXT HXT  sing N N 254 
LYS   N   CA   sing N N 255 
LYS   N   H    sing N N 256 
LYS   N   H2   sing N N 257 
LYS   CA  C    sing N N 258 
LYS   CA  CB   sing N N 259 
LYS   CA  HA   sing N N 260 
LYS   C   O    doub N N 261 
LYS   C   OXT  sing N N 262 
LYS   CB  CG   sing N N 263 
LYS   CB  HB2  sing N N 264 
LYS   CB  HB3  sing N N 265 
LYS   CG  CD   sing N N 266 
LYS   CG  HG2  sing N N 267 
LYS   CG  HG3  sing N N 268 
LYS   CD  CE   sing N N 269 
LYS   CD  HD2  sing N N 270 
LYS   CD  HD3  sing N N 271 
LYS   CE  NZ   sing N N 272 
LYS   CE  HE2  sing N N 273 
LYS   CE  HE3  sing N N 274 
LYS   NZ  HZ1  sing N N 275 
LYS   NZ  HZ2  sing N N 276 
LYS   NZ  HZ3  sing N N 277 
LYS   OXT HXT  sing N N 278 
MET   N   CA   sing N N 279 
MET   N   H    sing N N 280 
MET   N   H2   sing N N 281 
MET   CA  C    sing N N 282 
MET   CA  CB   sing N N 283 
MET   CA  HA   sing N N 284 
MET   C   O    doub N N 285 
MET   C   OXT  sing N N 286 
MET   CB  CG   sing N N 287 
MET   CB  HB2  sing N N 288 
MET   CB  HB3  sing N N 289 
MET   CG  SD   sing N N 290 
MET   CG  HG2  sing N N 291 
MET   CG  HG3  sing N N 292 
MET   SD  CE   sing N N 293 
MET   CE  HE1  sing N N 294 
MET   CE  HE2  sing N N 295 
MET   CE  HE3  sing N N 296 
MET   OXT HXT  sing N N 297 
PHE   N   CA   sing N N 298 
PHE   N   H    sing N N 299 
PHE   N   H2   sing N N 300 
PHE   CA  C    sing N N 301 
PHE   CA  CB   sing N N 302 
PHE   CA  HA   sing N N 303 
PHE   C   O    doub N N 304 
PHE   C   OXT  sing N N 305 
PHE   CB  CG   sing N N 306 
PHE   CB  HB2  sing N N 307 
PHE   CB  HB3  sing N N 308 
PHE   CG  CD1  doub Y N 309 
PHE   CG  CD2  sing Y N 310 
PHE   CD1 CE1  sing Y N 311 
PHE   CD1 HD1  sing N N 312 
PHE   CD2 CE2  doub Y N 313 
PHE   CD2 HD2  sing N N 314 
PHE   CE1 CZ   doub Y N 315 
PHE   CE1 HE1  sing N N 316 
PHE   CE2 CZ   sing Y N 317 
PHE   CE2 HE2  sing N N 318 
PHE   CZ  HZ   sing N N 319 
PHE   OXT HXT  sing N N 320 
PRO   N   CA   sing N N 321 
PRO   N   CD   sing N N 322 
PRO   N   H    sing N N 323 
PRO   CA  C    sing N N 324 
PRO   CA  CB   sing N N 325 
PRO   CA  HA   sing N N 326 
PRO   C   O    doub N N 327 
PRO   C   OXT  sing N N 328 
PRO   CB  CG   sing N N 329 
PRO   CB  HB2  sing N N 330 
PRO   CB  HB3  sing N N 331 
PRO   CG  CD   sing N N 332 
PRO   CG  HG2  sing N N 333 
PRO   CG  HG3  sing N N 334 
PRO   CD  HD2  sing N N 335 
PRO   CD  HD3  sing N N 336 
PRO   OXT HXT  sing N N 337 
SER   N   CA   sing N N 338 
SER   N   H    sing N N 339 
SER   N   H2   sing N N 340 
SER   CA  C    sing N N 341 
SER   CA  CB   sing N N 342 
SER   CA  HA   sing N N 343 
SER   C   O    doub N N 344 
SER   C   OXT  sing N N 345 
SER   CB  OG   sing N N 346 
SER   CB  HB2  sing N N 347 
SER   CB  HB3  sing N N 348 
SER   OG  HG   sing N N 349 
SER   OXT HXT  sing N N 350 
THR   N   CA   sing N N 351 
THR   N   H    sing N N 352 
THR   N   H2   sing N N 353 
THR   CA  C    sing N N 354 
THR   CA  CB   sing N N 355 
THR   CA  HA   sing N N 356 
THR   C   O    doub N N 357 
THR   C   OXT  sing N N 358 
THR   CB  OG1  sing N N 359 
THR   CB  CG2  sing N N 360 
THR   CB  HB   sing N N 361 
THR   OG1 HG1  sing N N 362 
THR   CG2 HG21 sing N N 363 
THR   CG2 HG22 sing N N 364 
THR   CG2 HG23 sing N N 365 
THR   OXT HXT  sing N N 366 
TRP   N   CA   sing N N 367 
TRP   N   H    sing N N 368 
TRP   N   H2   sing N N 369 
TRP   CA  C    sing N N 370 
TRP   CA  CB   sing N N 371 
TRP   CA  HA   sing N N 372 
TRP   C   O    doub N N 373 
TRP   C   OXT  sing N N 374 
TRP   CB  CG   sing N N 375 
TRP   CB  HB2  sing N N 376 
TRP   CB  HB3  sing N N 377 
TRP   CG  CD1  doub Y N 378 
TRP   CG  CD2  sing Y N 379 
TRP   CD1 NE1  sing Y N 380 
TRP   CD1 HD1  sing N N 381 
TRP   CD2 CE2  doub Y N 382 
TRP   CD2 CE3  sing Y N 383 
TRP   NE1 CE2  sing Y N 384 
TRP   NE1 HE1  sing N N 385 
TRP   CE2 CZ2  sing Y N 386 
TRP   CE3 CZ3  doub Y N 387 
TRP   CE3 HE3  sing N N 388 
TRP   CZ2 CH2  doub Y N 389 
TRP   CZ2 HZ2  sing N N 390 
TRP   CZ3 CH2  sing Y N 391 
TRP   CZ3 HZ3  sing N N 392 
TRP   CH2 HH2  sing N N 393 
TRP   OXT HXT  sing N N 394 
TYR   N   CA   sing N N 395 
TYR   N   H    sing N N 396 
TYR   N   H2   sing N N 397 
TYR   CA  C    sing N N 398 
TYR   CA  CB   sing N N 399 
TYR   CA  HA   sing N N 400 
TYR   C   O    doub N N 401 
TYR   C   OXT  sing N N 402 
TYR   CB  CG   sing N N 403 
TYR   CB  HB2  sing N N 404 
TYR   CB  HB3  sing N N 405 
TYR   CG  CD1  doub Y N 406 
TYR   CG  CD2  sing Y N 407 
TYR   CD1 CE1  sing Y N 408 
TYR   CD1 HD1  sing N N 409 
TYR   CD2 CE2  doub Y N 410 
TYR   CD2 HD2  sing N N 411 
TYR   CE1 CZ   doub Y N 412 
TYR   CE1 HE1  sing N N 413 
TYR   CE2 CZ   sing Y N 414 
TYR   CE2 HE2  sing N N 415 
TYR   CZ  OH   sing N N 416 
TYR   OH  HH   sing N N 417 
TYR   OXT HXT  sing N N 418 
VAL   N   CA   sing N N 419 
VAL   N   H    sing N N 420 
VAL   N   H2   sing N N 421 
VAL   CA  C    sing N N 422 
VAL   CA  CB   sing N N 423 
VAL   CA  HA   sing N N 424 
VAL   C   O    doub N N 425 
VAL   C   OXT  sing N N 426 
VAL   CB  CG1  sing N N 427 
VAL   CB  CG2  sing N N 428 
VAL   CB  HB   sing N N 429 
VAL   CG1 HG11 sing N N 430 
VAL   CG1 HG12 sing N N 431 
VAL   CG1 HG13 sing N N 432 
VAL   CG2 HG21 sing N N 433 
VAL   CG2 HG22 sing N N 434 
VAL   CG2 HG23 sing N N 435 
VAL   OXT HXT  sing N N 436 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Natural Science Foundation of China (NSFC)' China 82073698 1 
'National Natural Science Foundation of China (NSFC)' China 82073698 2 
# 
_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   3PBB 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9IVV 
_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]   0.003642 
_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]   0.003642 
_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]   0.003642 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
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   . ALA   A 1 1   ? -10.454 -54.461 26.542  1.00 94.94  ?  33  ALA   A N   1 
ATOM   2    C  CA  . ALA   A 1 1   ? -11.356 -54.106 25.451  1.00 111.40 ?  33  ALA   A CA  1 
ATOM   3    C  C   . ALA   A 1 1   ? -10.887 -54.744 24.146  1.00 125.96 ?  33  ALA   A C   1 
ATOM   4    O  O   . ALA   A 1 1   ? -9.852  -55.419 24.109  1.00 124.34 ?  33  ALA   A O   1 
ATOM   5    C  CB  . ALA   A 1 1   ? -11.450 -52.579 25.295  1.00 90.90  ?  33  ALA   A CB  1 
ATOM   6    N  N   . SER   A 1 2   ? -11.654 -54.527 23.078  1.00 120.33 ?  34  SER   A N   1 
ATOM   7    C  CA  . SER   A 1 2   ? -11.294 -55.027 21.760  1.00 115.05 ?  34  SER   A CA  1 
ATOM   8    C  C   . SER   A 1 2   ? -10.221 -54.138 21.127  1.00 112.23 ?  34  SER   A C   1 
ATOM   9    O  O   . SER   A 1 2   ? -10.182 -52.921 21.347  1.00 115.86 ?  34  SER   A O   1 
ATOM   10   C  CB  . SER   A 1 2   ? -12.539 -55.085 20.864  1.00 110.53 ?  34  SER   A CB  1 
ATOM   11   O  OG  . SER   A 1 2   ? -13.544 -55.959 21.359  1.00 84.92  ?  34  SER   A OG  1 
ATOM   12   N  N   . ALA   A 1 3   ? -9.349  -54.752 20.319  1.00 93.72  ?  35  ALA   A N   1 
ATOM   13   C  CA  . ALA   A 1 3   ? -8.234  -54.008 19.734  1.00 97.09  ?  35  ALA   A CA  1 
ATOM   14   C  C   . ALA   A 1 3   ? -8.705  -52.951 18.732  1.00 98.10  ?  35  ALA   A C   1 
ATOM   15   O  O   . ALA   A 1 3   ? -8.298  -51.789 18.817  1.00 88.78  ?  35  ALA   A O   1 
ATOM   16   C  CB  . ALA   A 1 3   ? -7.247  -54.972 19.073  1.00 82.83  ?  35  ALA   A CB  1 
ATOM   17   N  N   . TRP   A 1 4   ? -9.574  -53.328 17.776  1.00 97.34  ?  36  TRP   A N   1 
ATOM   18   C  CA  . TRP   A 1 4   ? -9.756  -52.530 16.560  1.00 86.49  ?  36  TRP   A CA  1 
ATOM   19   C  C   . TRP   A 1 4   ? -10.517 -51.212 16.719  1.00 86.93  ?  36  TRP   A C   1 
ATOM   20   O  O   . TRP   A 1 4   ? -10.233 -50.272 15.968  1.00 95.06  ?  36  TRP   A O   1 
ATOM   21   C  CB  . TRP   A 1 4   ? -10.444 -53.356 15.455  1.00 91.83  ?  36  TRP   A CB  1 
ATOM   22   C  CG  . TRP   A 1 4   ? -11.855 -53.804 15.743  1.00 88.64  ?  36  TRP   A CG  1 
ATOM   23   C  CD1 . TRP   A 1 4   ? -12.228 -54.981 16.293  1.00 89.70  ?  36  TRP   A CD1 1 
ATOM   24   C  CD2 . TRP   A 1 4   ? -13.069 -53.080 15.500  1.00 87.20  ?  36  TRP   A CD2 1 
ATOM   25   N  NE1 . TRP   A 1 4   ? -13.583 -55.034 16.422  1.00 83.97  ?  36  TRP   A NE1 1 
ATOM   26   C  CE2 . TRP   A 1 4   ? -14.122 -53.878 15.938  1.00 82.06  ?  36  TRP   A CE2 1 
ATOM   27   C  CE3 . TRP   A 1 4   ? -13.363 -51.829 14.968  1.00 97.74  ?  36  TRP   A CE3 1 
ATOM   28   C  CZ2 . TRP   A 1 4   ? -15.444 -53.473 15.861  1.00 88.01  ?  36  TRP   A CZ2 1 
ATOM   29   C  CZ3 . TRP   A 1 4   ? -14.694 -51.435 14.884  1.00 86.99  ?  36  TRP   A CZ3 1 
ATOM   30   C  CH2 . TRP   A 1 4   ? -15.705 -52.249 15.327  1.00 79.45  ?  36  TRP   A CH2 1 
ATOM   31   N  N   . PRO   A 1 5   ? -11.481 -51.064 17.620  1.00 77.28  ?  37  PRO   A N   1 
ATOM   32   C  CA  . PRO   A 1 5   ? -12.217 -49.793 17.639  1.00 77.15  ?  37  PRO   A CA  1 
ATOM   33   C  C   . PRO   A 1 5   ? -11.419 -48.550 17.997  1.00 75.56  ?  37  PRO   A C   1 
ATOM   34   O  O   . PRO   A 1 5   ? -12.002 -47.485 18.201  1.00 74.30  ?  37  PRO   A O   1 
ATOM   35   C  CB  . PRO   A 1 5   ? -13.308 -50.071 18.665  1.00 80.49  ?  37  PRO   A CB  1 
ATOM   36   C  CG  . PRO   A 1 5   ? -13.600 -51.522 18.424  1.00 78.11  ?  37  PRO   A CG  1 
ATOM   37   C  CD  . PRO   A 1 5   ? -12.209 -52.063 18.413  1.00 81.47  ?  37  PRO   A CD  1 
ATOM   38   N  N   . GLU   A 1 6   ? -10.099 -48.656 18.074  1.00 89.01  ?  38  GLU   A N   1 
ATOM   39   C  CA  . GLU   A 1 6   ? -9.214  -47.496 18.069  1.00 86.75  ?  38  GLU   A CA  1 
ATOM   40   C  C   . GLU   A 1 6   ? -8.671  -47.189 16.687  1.00 81.34  ?  38  GLU   A C   1 
ATOM   41   O  O   . GLU   A 1 6   ? -8.137  -46.100 16.484  1.00 72.95  ?  38  GLU   A O   1 
ATOM   42   C  CB  . GLU   A 1 6   ? -8.019  -47.712 19.009  1.00 89.11  ?  38  GLU   A CB  1 
ATOM   43   C  CG  . GLU   A 1 6   ? -8.346  -47.861 20.470  1.00 86.55  ?  38  GLU   A CG  1 
ATOM   44   C  CD  . GLU   A 1 6   ? -7.979  -46.635 21.232  1.00 81.19  ?  38  GLU   A CD  1 
ATOM   45   O  OE1 . GLU   A 1 6   ? -7.298  -46.755 22.274  1.00 73.02  ?  38  GLU   A OE1 1 
ATOM   46   O  OE2 . GLU   A 1 6   ? -8.369  -45.551 20.764  1.00 79.62  ?  38  GLU   A OE2 1 
ATOM   47   N  N   . GLU   A 1 7   ? -8.810  -48.116 15.736  1.00 89.09  ?  39  GLU   A N   1 
ATOM   48   C  CA  . GLU   A 1 7   ? -8.116  -48.022 14.458  1.00 82.35  ?  39  GLU   A CA  1 
ATOM   49   C  C   . GLU   A 1 7   ? -8.277  -46.661 13.804  1.00 71.98  ?  39  GLU   A C   1 
ATOM   50   O  O   . GLU   A 1 7   ? -7.456  -46.293 12.962  1.00 70.95  ?  39  GLU   A O   1 
ATOM   51   C  CB  . GLU   A 1 7   ? -8.608  -49.134 13.511  1.00 78.63  ?  39  GLU   A CB  1 
ATOM   52   C  CG  . GLU   A 1 7   ? -8.046  -50.512 13.843  1.00 70.46  ?  39  GLU   A CG  1 
ATOM   53   C  CD  . GLU   A 1 7   ? -8.264  -51.577 12.780  1.00 70.38  ?  39  GLU   A CD  1 
ATOM   54   O  OE1 . GLU   A 1 7   ? -8.761  -51.276 11.682  1.00 69.17  ?  39  GLU   A OE1 1 
ATOM   55   O  OE2 . GLU   A 1 7   ? -7.918  -52.745 13.053  1.00 72.21  ?  39  GLU   A OE2 1 
ATOM   56   N  N   . LYS   A 1 8   ? -9.287  -45.894 14.189  1.00 70.27  ?  40  LYS   A N   1 
ATOM   57   C  CA  . LYS   A 1 8   ? -9.599  -44.648 13.510  1.00 67.15  ?  40  LYS   A CA  1 
ATOM   58   C  C   . LYS   A 1 8   ? -8.817  -43.456 14.039  1.00 63.97  ?  40  LYS   A C   1 
ATOM   59   O  O   . LYS   A 1 8   ? -8.507  -42.548 13.268  1.00 69.41  ?  40  LYS   A O   1 
ATOM   60   C  CB  . LYS   A 1 8   ? -11.106 -44.378 13.603  1.00 66.76  ?  40  LYS   A CB  1 
ATOM   61   C  CG  . LYS   A 1 8   ? -11.609 -43.784 14.908  1.00 61.64  ?  40  LYS   A CG  1 
ATOM   62   C  CD  . LYS   A 1 8   ? -13.027 -44.250 15.160  1.00 64.73  ?  40  LYS   A CD  1 
ATOM   63   C  CE  . LYS   A 1 8   ? -13.489 -44.008 16.583  1.00 66.84  ?  40  LYS   A CE  1 
ATOM   64   N  NZ  . LYS   A 1 8   ? -14.525 -45.005 16.947  1.00 67.29  ?  40  LYS   A NZ  1 
ATOM   65   N  N   . ASN   A 1 9   ? -8.466  -43.423 15.316  1.00 59.83  ?  41  ASN   A N   1 
ATOM   66   C  CA  . ASN   A 1 9   ? -7.706  -42.292 15.818  1.00 63.56  ?  41  ASN   A CA  1 
ATOM   67   C  C   . ASN   A 1 9   ? -6.375  -42.135 15.114  1.00 63.73  ?  41  ASN   A C   1 
ATOM   68   O  O   . ASN   A 1 9   ? -5.742  -41.084 15.228  1.00 56.02  ?  41  ASN   A O   1 
ATOM   69   C  CB  . ASN   A 1 9   ? -7.420  -42.458 17.290  1.00 75.84  ?  41  ASN   A CB  1 
ATOM   70   C  CG  . ASN   A 1 9   ? -8.627  -42.368 18.126  1.00 78.65  ?  41  ASN   A CG  1 
ATOM   71   O  OD1 . ASN   A 1 9   ? -8.810  -41.385 18.839  1.00 84.81  ?  41  ASN   A OD1 1 
ATOM   72   N  ND2 . ASN   A 1 9   ? -9.451  -43.402 18.097  1.00 77.28  ?  41  ASN   A ND2 1 
ATOM   73   N  N   . TYR   A 1 10  ? -5.921  -43.174 14.434  1.00 65.87  ?  42  TYR   A N   1 
ATOM   74   C  CA  . TYR   A 1 10  ? -4.597  -43.219 13.845  1.00 61.32  ?  42  TYR   A CA  1 
ATOM   75   C  C   . TYR   A 1 10  ? -4.685  -43.454 12.352  1.00 56.29  ?  42  TYR   A C   1 
ATOM   76   O  O   . TYR   A 1 10  ? -3.661  -43.630 11.693  1.00 56.32  ?  42  TYR   A O   1 
ATOM   77   C  CB  . TYR   A 1 10  ? -3.758  -44.318 14.511  1.00 67.87  ?  42  TYR   A CB  1 
ATOM   78   C  CG  . TYR   A 1 10  ? -3.635  -44.197 16.024  1.00 72.35  ?  42  TYR   A CG  1 
ATOM   79   C  CD1 . TYR   A 1 10  ? -2.941  -43.155 16.612  1.00 81.30  ?  42  TYR   A CD1 1 
ATOM   80   C  CD2 . TYR   A 1 10  ? -4.208  -45.135 16.861  1.00 83.11  ?  42  TYR   A CD2 1 
ATOM   81   C  CE1 . TYR   A 1 10  ? -2.839  -43.049 17.987  1.00 81.55  ?  42  TYR   A CE1 1 
ATOM   82   C  CE2 . TYR   A 1 10  ? -4.102  -45.033 18.229  1.00 84.99  ?  42  TYR   A CE2 1 
ATOM   83   C  CZ  . TYR   A 1 10  ? -3.422  -43.995 18.776  1.00 83.59  ?  42  TYR   A CZ  1 
ATOM   84   O  OH  . TYR   A 1 10  ? -3.343  -43.931 20.131  1.00 78.91  ?  42  TYR   A OH  1 
ATOM   85   N  N   . HIS   A 1 11  ? -5.885  -43.455 11.807  1.00 63.59  ?  43  HIS   A N   1 
ATOM   86   C  CA  . HIS   A 1 11  ? -6.064  -43.742 10.402  1.00 58.95  ?  43  HIS   A CA  1 
ATOM   87   C  C   . HIS   A 1 11  ? -5.623  -42.545 9.597   1.00 58.97  ?  43  HIS   A C   1 
ATOM   88   O  O   . HIS   A 1 11  ? -5.937  -41.408 9.944   1.00 59.25  ?  43  HIS   A O   1 
ATOM   89   C  CB  . HIS   A 1 11  ? -7.517  -44.044 10.130  1.00 50.31  ?  43  HIS   A CB  1 
ATOM   90   C  CG  . HIS   A 1 11  ? -7.793  -44.440 8.730   1.00 49.22  ?  43  HIS   A CG  1 
ATOM   91   N  ND1 . HIS   A 1 11  ? -7.494  -45.687 8.243   1.00 54.75  ?  43  HIS   A ND1 1 
ATOM   92   C  CD2 . HIS   A 1 11  ? -8.366  -43.763 7.713   1.00 55.08  ?  43  HIS   A CD2 1 
ATOM   93   C  CE1 . HIS   A 1 11  ? -7.857  -45.758 6.979   1.00 58.08  ?  43  HIS   A CE1 1 
ATOM   94   N  NE2 . HIS   A 1 11  ? -8.391  -44.603 6.633   1.00 55.32  ?  43  HIS   A NE2 1 
ATOM   95   N  N   . GLN   A 1 12  ? -4.892  -42.788 8.527   1.00 53.87  ?  44  GLN   A N   1 
ATOM   96   C  CA  . GLN   A 1 12  ? -4.400  -41.697 7.714   1.00 57.11  ?  44  GLN   A CA  1 
ATOM   97   C  C   . GLN   A 1 12  ? -4.720  -41.959 6.253   1.00 58.62  ?  44  GLN   A C   1 
ATOM   98   O  O   . GLN   A 1 12  ? -4.928  -43.106 5.841   1.00 50.66  ?  44  GLN   A O   1 
ATOM   99   C  CB  . GLN   A 1 12  ? -2.891  -41.502 7.906   1.00 60.15  ?  44  GLN   A CB  1 
ATOM   100  C  CG  . GLN   A 1 12  ? -2.468  -41.271 9.327   1.00 52.58  ?  44  GLN   A CG  1 
ATOM   101  C  CD  . GLN   A 1 12  ? -2.612  -39.852 9.786   1.00 53.32  ?  44  GLN   A CD  1 
ATOM   102  O  OE1 . GLN   A 1 12  ? -2.899  -38.953 9.010   1.00 62.00  ?  44  GLN   A OE1 1 
ATOM   103  N  NE2 . GLN   A 1 12  ? -2.406  -39.638 11.064  1.00 61.49  ?  44  GLN   A NE2 1 
ATOM   104  N  N   . PRO   A 1 13  ? -4.776  -40.909 5.450   1.00 52.65  ?  45  PRO   A N   1 
ATOM   105  C  CA  . PRO   A 1 13  ? -5.210  -41.045 4.067   1.00 49.42  ?  45  PRO   A CA  1 
ATOM   106  C  C   . PRO   A 1 13  ? -4.106  -41.436 3.112   1.00 52.60  ?  45  PRO   A C   1 
ATOM   107  O  O   . PRO   A 1 13  ? -2.928  -41.154 3.324   1.00 52.39  ?  45  PRO   A O   1 
ATOM   108  C  CB  . PRO   A 1 13  ? -5.678  -39.639 3.742   1.00 48.41  ?  45  PRO   A CB  1 
ATOM   109  C  CG  . PRO   A 1 13  ? -4.783  -38.833 4.534   1.00 55.49  ?  45  PRO   A CG  1 
ATOM   110  C  CD  . PRO   A 1 13  ? -4.680  -39.501 5.824   1.00 49.03  ?  45  PRO   A CD  1 
ATOM   111  N  N   . ALA   A 1 14  ? -4.531  -42.048 2.010   1.00 51.56  ?  46  ALA   A N   1 
ATOM   112  C  CA  . ALA   A 1 14  ? -3.694  -42.286 0.840   1.00 52.24  ?  46  ALA   A CA  1 
ATOM   113  C  C   . ALA   A 1 14  ? -3.851  -41.128 -0.130  1.00 54.32  ?  46  ALA   A C   1 
ATOM   114  O  O   . ALA   A 1 14  ? -4.606  -41.196 -1.096  1.00 52.99  ?  46  ALA   A O   1 
ATOM   115  C  CB  . ALA   A 1 14  ? -4.094  -43.571 0.144   1.00 58.92  ?  46  ALA   A CB  1 
ATOM   116  N  N   . ILE   A 1 15  ? -3.094  -40.065 0.115   1.00 48.20  ?  47  ILE   A N   1 
ATOM   117  C  CA  . ILE   A 1 15  ? -3.175  -38.885 -0.725  1.00 49.45  ?  47  ILE   A CA  1 
ATOM   118  C  C   . ILE   A 1 15  ? -3.064  -39.269 -2.187  1.00 51.68  ?  47  ILE   A C   1 
ATOM   119  O  O   . ILE   A 1 15  ? -2.176  -40.026 -2.582  1.00 56.96  ?  47  ILE   A O   1 
ATOM   120  C  CB  . ILE   A 1 15  ? -2.078  -37.890 -0.328  1.00 53.41  ?  47  ILE   A CB  1 
ATOM   121  C  CG1 . ILE   A 1 15  ? -2.477  -37.126 0.915   1.00 45.77  ?  47  ILE   A CG1 1 
ATOM   122  C  CG2 . ILE   A 1 15  ? -1.807  -36.924 -1.431  1.00 57.01  ?  47  ILE   A CG2 1 
ATOM   123  C  CD1 . ILE   A 1 15  ? -1.669  -37.438 2.072   1.00 58.41  ?  47  ILE   A CD1 1 
ATOM   124  N  N   . LEU   A 1 16  ? -3.953  -38.722 -3.001  1.00 53.97  ?  48  LEU   A N   1 
ATOM   125  C  CA  . LEU   A 1 16  ? -3.936  -38.967 -4.423  1.00 58.20  ?  48  LEU   A CA  1 
ATOM   126  C  C   . LEU   A 1 16  ? -2.979  -38.006 -5.113  1.00 63.20  ?  48  LEU   A C   1 
ATOM   127  O  O   . LEU   A 1 16  ? -2.584  -36.978 -4.569  1.00 55.38  ?  48  LEU   A O   1 
ATOM   128  C  CB  . LEU   A 1 16  ? -5.339  -38.828 -4.998  1.00 57.04  ?  48  LEU   A CB  1 
ATOM   129  C  CG  . LEU   A 1 16  ? -6.392  -39.842 -4.610  1.00 48.75  ?  48  LEU   A CG  1 
ATOM   130  C  CD1 . LEU   A 1 16  ? -7.572  -39.688 -5.489  1.00 55.94  ?  48  LEU   A CD1 1 
ATOM   131  C  CD2 . LEU   A 1 16  ? -5.883  -41.207 -4.753  1.00 64.57  ?  48  LEU   A CD2 1 
ATOM   132  N  N   . ASN   A 1 17  ? -2.593  -38.354 -6.324  1.00 66.06  ?  49  ASN   A N   1 
ATOM   133  C  CA  . ASN   A 1 17  ? -1.591  -37.575 -7.011  1.00 70.51  ?  49  ASN   A CA  1 
ATOM   134  C  C   . ASN   A 1 17  ? -2.045  -37.250 -8.412  1.00 73.93  ?  49  ASN   A C   1 
ATOM   135  O  O   . ASN   A 1 17  ? -2.613  -38.090 -9.116  1.00 76.76  ?  49  ASN   A O   1 
ATOM   136  C  CB  . ASN   A 1 17  ? -0.256  -38.278 -7.043  1.00 82.29  ?  49  ASN   A CB  1 
ATOM   137  C  CG  . ASN   A 1 17  ? 0.811   -37.500 -6.268  1.00 90.94  ?  49  ASN   A CG  1 
ATOM   138  O  OD1 . ASN   A 1 17  ? 1.262   -37.928 -5.205  1.00 78.53  ?  49  ASN   A OD1 1 
ATOM   139  N  ND2 . ASN   A 1 17  ? 1.186   -36.324 -6.786  1.00 80.03  ?  49  ASN   A ND2 1 
ATOM   140  N  N   . SER   A 1 18  ? -1.717  -36.026 -8.797  1.00 70.78  ?  50  SER   A N   1 
ATOM   141  C  CA  . SER   A 1 18  ? -2.263  -35.298 -9.925  1.00 60.38  ?  50  SER   A CA  1 
ATOM   142  C  C   . SER   A 1 18  ? -2.865  -36.147 -11.028 1.00 65.17  ?  50  SER   A C   1 
ATOM   143  O  O   . SER   A 1 18  ? -3.918  -35.796 -11.545 1.00 75.13  ?  50  SER   A O   1 
ATOM   144  C  CB  . SER   A 1 18  ? -1.158  -34.416 -10.441 1.00 66.40  ?  50  SER   A CB  1 
ATOM   145  O  OG  . SER   A 1 18  ? -0.444  -33.944 -9.302  1.00 68.29  ?  50  SER   A OG  1 
ATOM   146  N  N   . SER   A 1 19  ? -2.253  -37.260 -11.406 1.00 74.48  ?  51  SER   A N   1 
ATOM   147  C  CA  . SER   A 1 19  ? -2.906  -38.103 -12.400 1.00 72.17  ?  51  SER   A CA  1 
ATOM   148  C  C   . SER   A 1 19  ? -4.222  -38.620 -11.859 1.00 72.07  ?  51  SER   A C   1 
ATOM   149  O  O   . SER   A 1 19  ? -5.208  -38.709 -12.595 1.00 67.39  ?  51  SER   A O   1 
ATOM   150  C  CB  . SER   A 1 19  ? -2.001  -39.262 -12.808 1.00 84.66  ?  51  SER   A CB  1 
ATOM   151  O  OG  . SER   A 1 19  ? -2.555  -39.976 -13.899 1.00 80.95  ?  51  SER   A OG  1 
ATOM   152  N  N   . ALA   A 1 20  ? -4.254  -38.955 -10.564 1.00 75.76  ?  52  ALA   A N   1 
ATOM   153  C  CA  . ALA   A 1 20  ? -5.476  -39.449 -9.938  1.00 70.11  ?  52  ALA   A CA  1 
ATOM   154  C  C   . ALA   A 1 20  ? -6.523  -38.362 -9.848  1.00 66.78  ?  52  ALA   A C   1 
ATOM   155  O  O   . ALA   A 1 20  ? -7.691  -38.580 -10.180 1.00 66.26  ?  52  ALA   A O   1 
ATOM   156  C  CB  . ALA   A 1 20  ? -5.183  -39.980 -8.544  1.00 69.62  ?  52  ALA   A CB  1 
ATOM   157  N  N   . LEU   A 1 21  ? -6.130  -37.185 -9.370  1.00 62.44  ?  53  LEU   A N   1 
ATOM   158  C  CA  . LEU   A 1 21  ? -7.081  -36.093 -9.294  1.00 62.64  ?  53  LEU   A CA  1 
ATOM   159  C  C   . LEU   A 1 21  ? -7.719  -35.838 -10.653 1.00 63.09  ?  53  LEU   A C   1 
ATOM   160  O  O   . LEU   A 1 21  ? -8.944  -35.871 -10.787 1.00 64.52  ?  53  LEU   A O   1 
ATOM   161  C  CB  . LEU   A 1 21  ? -6.396  -34.856 -8.723  1.00 50.52  ?  53  LEU   A CB  1 
ATOM   162  C  CG  . LEU   A 1 21  ? -5.851  -35.079 -7.305  1.00 51.44  ?  53  LEU   A CG  1 
ATOM   163  C  CD1 . LEU   A 1 21  ? -5.241  -33.877 -6.723  1.00 46.41  ?  53  LEU   A CD1 1 
ATOM   164  C  CD2 . LEU   A 1 21  ? -6.908  -35.478 -6.362  1.00 51.32  ?  53  LEU   A CD2 1 
ATOM   165  N  N   . ARG   A 1 22  ? -6.916  -35.660 -11.691 1.00 61.78  ?  54  ARG   A N   1 
ATOM   166  C  CA  . ARG   A 1 22  ? -7.497  -35.402 -12.995 1.00 56.41  ?  54  ARG   A CA  1 
ATOM   167  C  C   . ARG   A 1 22  ? -8.553  -36.432 -13.367 1.00 63.65  ?  54  ARG   A C   1 
ATOM   168  O  O   . ARG   A 1 22  ? -9.518  -36.101 -14.057 1.00 66.83  ?  54  ARG   A O   1 
ATOM   169  C  CB  . ARG   A 1 22  ? -6.416  -35.361 -14.063 1.00 64.25  ?  54  ARG   A CB  1 
ATOM   170  C  CG  . ARG   A 1 22  ? -5.410  -34.260 -13.889 1.00 66.12  ?  54  ARG   A CG  1 
ATOM   171  C  CD  . ARG   A 1 22  ? -4.646  -33.936 -15.150 1.00 54.18  ?  54  ARG   A CD  1 
ATOM   172  N  NE  . ARG   A 1 22  ? -3.896  -32.707 -14.964 1.00 44.52  ?  54  ARG   A NE  1 
ATOM   173  C  CZ  . ARG   A 1 22  ? -2.627  -32.652 -14.594 1.00 56.32  ?  54  ARG   A CZ  1 
ATOM   174  N  NH1 . ARG   A 1 22  ? -1.924  -33.757 -14.384 1.00 55.68  ?  54  ARG   A NH1 1 
ATOM   175  N  NH2 . ARG   A 1 22  ? -2.050  -31.475 -14.436 1.00 70.10  ?  54  ARG   A NH2 1 
ATOM   176  N  N   . GLN   A 1 23  ? -8.418  -37.677 -12.932 1.00 66.65  ?  55  GLN   A N   1 
ATOM   177  C  CA  . GLN   A 1 23  ? -9.439  -38.620 -13.375 1.00 73.40  ?  55  GLN   A CA  1 
ATOM   178  C  C   . GLN   A 1 23  ? -10.694 -38.496 -12.525 1.00 69.63  ?  55  GLN   A C   1 
ATOM   179  O  O   . GLN   A 1 23  ? -11.804 -38.516 -13.067 1.00 66.96  ?  55  GLN   A O   1 
ATOM   180  C  CB  . GLN   A 1 23  ? -8.921  -40.071 -13.410 1.00 75.80  ?  55  GLN   A CB  1 
ATOM   181  C  CG  . GLN   A 1 23  ? -8.312  -40.634 -12.143 1.00 82.67  ?  55  GLN   A CG  1 
ATOM   182  C  CD  . GLN   A 1 23  ? -8.431  -42.165 -12.063 1.00 92.47  ?  55  GLN   A CD  1 
ATOM   183  O  OE1 . GLN   A 1 23  ? -9.264  -42.763 -12.742 1.00 89.74  ?  55  GLN   A OE1 1 
ATOM   184  N  NE2 . GLN   A 1 23  ? -7.609  -42.796 -11.217 1.00 87.59  ?  55  GLN   A NE2 1 
ATOM   185  N  N   . ILE   A 1 24  ? -10.557 -38.315 -11.207 1.00 70.51  ?  56  ILE   A N   1 
ATOM   186  C  CA  . ILE   A 1 24  ? -11.753 -38.153 -10.386 1.00 62.58  ?  56  ILE   A CA  1 
ATOM   187  C  C   . ILE   A 1 24  ? -12.575 -36.998 -10.905 1.00 55.90  ?  56  ILE   A C   1 
ATOM   188  O  O   . ILE   A 1 24  ? -13.792 -37.102 -11.037 1.00 52.96  ?  56  ILE   A O   1 
ATOM   189  C  CB  . ILE   A 1 24  ? -11.404 -37.947 -8.909  1.00 57.11  ?  56  ILE   A CB  1 
ATOM   190  C  CG1 . ILE   A 1 24  ? -10.434 -38.995 -8.417  1.00 53.06  ?  56  ILE   A CG1 1 
ATOM   191  C  CG2 . ILE   A 1 24  ? -12.645 -38.045 -8.119  1.00 61.21  ?  56  ILE   A CG2 1 
ATOM   192  C  CD1 . ILE   A 1 24  ? -10.824 -40.367 -8.722  1.00 60.34  ?  56  ILE   A CD1 1 
ATOM   193  N  N   . ALA   A 1 25  ? -11.911 -35.890 -11.225 1.00 55.72  ?  57  ALA   A N   1 
ATOM   194  C  CA  . ALA   A 1 25  ? -12.566 -34.729 -11.810 1.00 51.69  ?  57  ALA   A CA  1 
ATOM   195  C  C   . ALA   A 1 25  ? -13.199 -35.040 -13.153 1.00 56.56  ?  57  ALA   A C   1 
ATOM   196  O  O   . ALA   A 1 25  ? -14.262 -34.509 -13.488 1.00 52.65  ?  57  ALA   A O   1 
ATOM   197  C  CB  . ALA   A 1 25  ? -11.542 -33.631 -11.979 1.00 48.82  ?  57  ALA   A CB  1 
ATOM   198  N  N   . GLU   A 1 26  ? -12.517 -35.830 -13.971 1.00 61.61  ?  58  GLU   A N   1 
ATOM   199  C  CA  . GLU   A 1 26  ? -13.083 -36.251 -15.240 1.00 68.02  ?  58  GLU   A CA  1 
ATOM   200  C  C   . GLU   A 1 26  ? -14.338 -37.069 -15.025 1.00 68.38  ?  58  GLU   A C   1 
ATOM   201  O  O   . GLU   A 1 26  ? -15.267 -37.001 -15.831 1.00 75.72  ?  58  GLU   A O   1 
ATOM   202  C  CB  . GLU   A 1 26  ? -12.050 -37.069 -16.012 1.00 87.34  ?  58  GLU   A CB  1 
ATOM   203  C  CG  . GLU   A 1 26  ? -11.611 -36.502 -17.339 1.00 96.64  ?  58  GLU   A CG  1 
ATOM   204  C  CD  . GLU   A 1 26  ? -10.293 -37.106 -17.826 1.00 97.19  ?  58  GLU   A CD  1 
ATOM   205  O  OE1 . GLU   A 1 26  ? -9.941  -38.230 -17.396 1.00 94.98  ?  58  GLU   A OE1 1 
ATOM   206  O  OE2 . GLU   A 1 26  ? -9.606  -36.453 -18.637 1.00 91.91  ?  58  GLU   A OE2 1 
ATOM   207  N  N   . GLY   A 1 27  ? -14.393 -37.821 -13.937 1.00 65.41  ?  59  GLY   A N   1 
ATOM   208  C  CA  . GLY   A 1 27  ? -15.406 -38.831 -13.730 1.00 61.18  ?  59  GLY   A CA  1 
ATOM   209  C  C   . GLY   A 1 27  ? -16.683 -38.415 -13.041 1.00 56.85  ?  59  GLY   A C   1 
ATOM   210  O  O   . GLY   A 1 27  ? -17.430 -39.306 -12.646 1.00 61.69  ?  59  GLY   A O   1 
ATOM   211  N  N   . THR   A 1 28  ? -16.961 -37.123 -12.885 1.00 54.45  ?  60  THR   A N   1 
ATOM   212  C  CA  . THR   A 1 28  ? -18.207 -36.631 -12.318 1.00 54.73  ?  60  THR   A CA  1 
ATOM   213  C  C   . THR   A 1 28  ? -18.878 -35.726 -13.331 1.00 55.63  ?  60  THR   A C   1 
ATOM   214  O  O   . THR   A 1 28  ? -18.249 -34.809 -13.854 1.00 63.98  ?  60  THR   A O   1 
ATOM   215  C  CB  . THR   A 1 28  ? -17.975 -35.851 -11.020 1.00 54.57  ?  60  THR   A CB  1 
ATOM   216  O  OG1 . THR   A 1 28  ? -17.254 -36.664 -10.104 1.00 66.03  ?  60  THR   A OG1 1 
ATOM   217  C  CG2 . THR   A 1 28  ? -19.291 -35.468 -10.357 1.00 49.62  ?  60  THR   A CG2 1 
ATOM   218  N  N   . SER   A 1 29  ? -20.154 -35.953 -13.568 1.00 53.03  ?  61  SER   A N   1 
ATOM   219  C  CA  . SER   A 1 29  ? -20.931 -35.142 -14.484 1.00 58.01  ?  61  SER   A CA  1 
ATOM   220  C  C   . SER   A 1 29  ? -21.951 -34.345 -13.706 1.00 54.22  ?  61  SER   A C   1 
ATOM   221  O  O   . SER   A 1 29  ? -23.034 -34.845 -13.410 1.00 54.47  ?  61  SER   A O   1 
ATOM   222  C  CB  . SER   A 1 29  ? -21.639 -36.006 -15.504 1.00 71.18  ?  61  SER   A CB  1 
ATOM   223  O  OG  . SER   A 1 29  ? -22.693 -35.256 -16.088 1.00 75.38  ?  61  SER   A OG  1 
ATOM   224  N  N   . ILE   A 1 30  ? -21.639 -33.089 -13.417 1.00 54.35  ?  62  ILE   A N   1 
ATOM   225  C  CA  . ILE   A 1 30  ? -22.646 -32.283 -12.755 1.00 50.34  ?  62  ILE   A CA  1 
ATOM   226  C  C   . ILE   A 1 30  ? -23.956 -32.369 -13.502 1.00 55.63  ?  62  ILE   A C   1 
ATOM   227  O  O   . ILE   A 1 30  ? -25.020 -32.394 -12.887 1.00 60.51  ?  62  ILE   A O   1 
ATOM   228  C  CB  . ILE   A 1 30  ? -22.181 -30.831 -12.602 1.00 51.53  ?  62  ILE   A CB  1 
ATOM   229  C  CG1 . ILE   A 1 30  ? -23.191 -30.031 -11.807 1.00 56.91  ?  62  ILE   A CG1 1 
ATOM   230  C  CG2 . ILE   A 1 30  ? -22.072 -30.166 -13.887 1.00 56.23  ?  62  ILE   A CG2 1 
ATOM   231  C  CD1 . ILE   A 1 30  ? -23.395 -30.521 -10.401 1.00 52.01  ?  62  ILE   A CD1 1 
ATOM   232  N  N   . SER   A 1 31  ? -23.909 -32.471 -14.828 1.00 67.92  ?  63  SER   A N   1 
ATOM   233  C  CA  . SER   A 1 31  ? -25.135 -32.473 -15.625 1.00 61.30  ?  63  SER   A CA  1 
ATOM   234  C  C   . SER   A 1 31  ? -25.906 -33.768 -15.456 1.00 62.83  ?  63  SER   A C   1 
ATOM   235  O  O   . SER   A 1 31  ? -27.137 -33.766 -15.418 1.00 58.86  ?  63  SER   A O   1 
ATOM   236  C  CB  . SER   A 1 31  ? -24.786 -32.266 -17.084 1.00 58.64  ?  63  SER   A CB  1 
ATOM   237  O  OG  . SER   A 1 31  ? -23.396 -32.470 -17.262 1.00 70.60  ?  63  SER   A OG  1 
ATOM   238  N  N   . GLU   A 1 32  ? -25.201 -34.887 -15.374 1.00 65.87  ?  64  GLU   A N   1 
ATOM   239  C  CA  . GLU   A 1 32  ? -25.866 -36.150 -15.121 1.00 63.33  ?  64  GLU   A CA  1 
ATOM   240  C  C   . GLU   A 1 32  ? -26.567 -36.132 -13.783 1.00 63.07  ?  64  GLU   A C   1 
ATOM   241  O  O   . GLU   A 1 32  ? -27.757 -36.431 -13.695 1.00 67.33  ?  64  GLU   A O   1 
ATOM   242  C  CB  . GLU   A 1 32  ? -24.863 -37.279 -15.167 1.00 73.98  ?  64  GLU   A CB  1 
ATOM   243  C  CG  . GLU   A 1 32  ? -24.432 -37.611 -16.556 1.00 75.15  ?  64  GLU   A CG  1 
ATOM   244  C  CD  . GLU   A 1 32  ? -25.214 -38.753 -17.098 1.00 81.51  ?  64  GLU   A CD  1 
ATOM   245  O  OE1 . GLU   A 1 32  ? -24.795 -39.908 -16.867 1.00 88.93  ?  64  GLU   A OE1 1 
ATOM   246  O  OE2 . GLU   A 1 32  ? -26.260 -38.497 -17.723 1.00 78.09  ?  64  GLU   A OE2 1 
ATOM   247  N  N   . MET   A 1 33  ? -25.841 -35.794 -12.720 1.00 65.00  ?  65  MET   A N   1 
ATOM   248  C  CA  . MET   A 1 33  ? -26.462 -35.690 -11.405 1.00 63.07  ?  65  MET   A CA  1 
ATOM   249  C  C   . MET   A 1 33  ? -27.688 -34.799 -11.461 1.00 54.41  ?  65  MET   A C   1 
ATOM   250  O  O   . MET   A 1 33  ? -28.762 -35.151 -10.970 1.00 52.93  ?  65  MET   A O   1 
ATOM   251  C  CB  . MET   A 1 33  ? -25.458 -35.137 -10.399 1.00 58.95  ?  65  MET   A CB  1 
ATOM   252  C  CG  . MET   A 1 33  ? -25.930 -35.120 -8.962  1.00 51.35  ?  65  MET   A CG  1 
ATOM   253  S  SD  . MET   A 1 33  ? -25.166 -33.850 -7.961  1.00 34.96  ?  65  MET   A SD  1 
ATOM   254  C  CE  . MET   A 1 33  ? -25.993 -32.460 -8.561  1.00 39.01  ?  65  MET   A CE  1 
ATOM   255  N  N   . TRP   A 1 34  ? -27.552 -33.649 -12.079 1.00 47.11  ?  66  TRP   A N   1 
ATOM   256  C  CA  . TRP   A 1 34  ? -28.608 -32.673 -11.984 1.00 50.98  ?  66  TRP   A CA  1 
ATOM   257  C  C   . TRP   A 1 34  ? -29.898 -33.127 -12.639 1.00 53.03  ?  66  TRP   A C   1 
ATOM   258  O  O   . TRP   A 1 34  ? -30.961 -32.627 -12.289 1.00 56.54  ?  66  TRP   A O   1 
ATOM   259  C  CB  . TRP   A 1 34  ? -28.118 -31.385 -12.595 1.00 51.60  ?  66  TRP   A CB  1 
ATOM   260  C  CG  . TRP   A 1 34  ? -28.853 -30.157 -12.239 1.00 40.09  ?  66  TRP   A CG  1 
ATOM   261  C  CD1 . TRP   A 1 34  ? -30.094 -29.794 -12.624 1.00 44.28  ?  66  TRP   A CD1 1 
ATOM   262  C  CD2 . TRP   A 1 34  ? -28.349 -29.099 -11.470 1.00 33.72  ?  66  TRP   A CD2 1 
ATOM   263  N  NE1 . TRP   A 1 34  ? -30.399 -28.561 -12.129 1.00 36.27  ?  66  TRP   A NE1 1 
ATOM   264  C  CE2 . TRP   A 1 34  ? -29.330 -28.122 -11.413 1.00 33.42  ?  66  TRP   A CE2 1 
ATOM   265  C  CE3 . TRP   A 1 34  ? -27.150 -28.883 -10.821 1.00 37.03  ?  66  TRP   A CE3 1 
ATOM   266  C  CZ2 . TRP   A 1 34  ? -29.156 -26.970 -10.741 1.00 45.33  ?  66  TRP   A CZ2 1 
ATOM   267  C  CZ3 . TRP   A 1 34  ? -26.982 -27.751 -10.161 1.00 37.50  ?  66  TRP   A CZ3 1 
ATOM   268  C  CH2 . TRP   A 1 34  ? -27.972 -26.798 -10.113 1.00 47.34  ?  66  TRP   A CH2 1 
ATOM   269  N  N   . GLN   A 1 35  ? -29.853 -34.048 -13.574 1.00 53.52  ?  67  GLN   A N   1 
ATOM   270  C  CA  . GLN   A 1 35  ? -31.070 -34.475 -14.230 1.00 58.42  ?  67  GLN   A CA  1 
ATOM   271  C  C   . GLN   A 1 35  ? -31.480 -35.856 -13.807 1.00 55.64  ?  67  GLN   A C   1 
ATOM   272  O  O   . GLN   A 1 35  ? -32.664 -36.150 -13.762 1.00 61.51  ?  67  GLN   A O   1 
ATOM   273  C  CB  . GLN   A 1 35  ? -30.892 -34.425 -15.755 1.00 75.36  ?  67  GLN   A CB  1 
ATOM   274  C  CG  . GLN   A 1 35  ? -31.447 -35.626 -16.550 1.00 85.76  ?  67  GLN   A CG  1 
ATOM   275  C  CD  . GLN   A 1 35  ? -31.521 -35.363 -18.053 1.00 84.84  ?  67  GLN   A CD  1 
ATOM   276  O  OE1 . GLN   A 1 35  ? -32.188 -34.422 -18.489 1.00 82.19  ?  67  GLN   A OE1 1 
ATOM   277  N  NE2 . GLN   A 1 35  ? -30.842 -36.198 -18.847 1.00 67.50  ?  67  GLN   A NE2 1 
ATOM   278  N  N   . ASN   A 1 36  ? -30.523 -36.683 -13.459 1.00 54.86  ?  68  ASN   A N   1 
ATOM   279  C  CA  . ASN   A 1 36  ? -30.780 -38.056 -13.090 1.00 56.86  ?  68  ASN   A CA  1 
ATOM   280  C  C   . ASN   A 1 36  ? -30.939 -38.259 -11.596 1.00 54.47  ?  68  ASN   A C   1 
ATOM   281  O  O   . ASN   A 1 36  ? -31.712 -39.119 -11.178 1.00 50.91  ?  68  ASN   A O   1 
ATOM   282  C  CB  . ASN   A 1 36  ? -29.630 -38.926 -13.570 1.00 62.62  ?  68  ASN   A CB  1 
ATOM   283  C  CG  . ASN   A 1 36  ? -29.606 -39.090 -15.040 1.00 64.04  ?  68  ASN   A CG  1 
ATOM   284  O  OD1 . ASN   A 1 36  ? -30.448 -38.554 -15.752 1.00 58.68  ?  68  ASN   A OD1 1 
ATOM   285  N  ND2 . ASN   A 1 36  ? -28.630 -39.836 -15.520 1.00 66.65  ?  68  ASN   A ND2 1 
ATOM   286  N  N   . ASP   A 1 37  ? -30.220 -37.500 -10.781 1.00 60.52  ?  69  ASP   A N   1 
ATOM   287  C  CA  . ASP   A 1 37  ? -30.193 -37.688 -9.340  1.00 51.79  ?  69  ASP   A CA  1 
ATOM   288  C  C   . ASP   A 1 37  ? -30.965 -36.627 -8.573  1.00 53.90  ?  69  ASP   A C   1 
ATOM   289  O  O   . ASP   A 1 37  ? -31.674 -36.957 -7.628  1.00 52.04  ?  69  ASP   A O   1 
ATOM   290  C  CB  . ASP   A 1 37  ? -28.752 -37.701 -8.851  1.00 49.36  ?  69  ASP   A CB  1 
ATOM   291  C  CG  . ASP   A 1 37  ? -28.064 -39.017 -9.092  1.00 59.64  ?  69  ASP   A CG  1 
ATOM   292  O  OD1 . ASP   A 1 37  ? -28.544 -40.016 -8.544  1.00 60.93  ?  69  ASP   A OD1 1 
ATOM   293  O  OD2 . ASP   A 1 37  ? -27.033 -39.069 -9.797  1.00 58.95  ?  69  ASP   A OD2 1 
ATOM   294  N  N   . LEU   A 1 38  ? -30.874 -35.360 -8.959  1.00 49.36  ?  70  LEU   A N   1 
ATOM   295  C  CA  . LEU   A 1 38  ? -31.450 -34.290 -8.158  1.00 42.09  ?  70  LEU   A CA  1 
ATOM   296  C  C   . LEU   A 1 38  ? -32.826 -33.834 -8.604  1.00 42.15  ?  70  LEU   A C   1 
ATOM   297  O  O   . LEU   A 1 38  ? -33.659 -33.527 -7.767  1.00 40.87  ?  70  LEU   A O   1 
ATOM   298  C  CB  . LEU   A 1 38  ? -30.529 -33.085 -8.153  1.00 37.20  ?  70  LEU   A CB  1 
ATOM   299  C  CG  . LEU   A 1 38  ? -31.139 -31.723 -7.828  1.00 41.71  ?  70  LEU   A CG  1 
ATOM   300  C  CD1 . LEU   A 1 38  ? -31.437 -31.670 -6.388  1.00 48.29  ?  70  LEU   A CD1 1 
ATOM   301  C  CD2 . LEU   A 1 38  ? -30.216 -30.606 -8.148  1.00 38.87  ?  70  LEU   A CD2 1 
ATOM   302  N  N   . GLN   A 1 39  ? -33.088 -33.696 -9.887  1.00 48.84  ?  71  GLN   A N   1 
ATOM   303  C  CA  . GLN   A 1 39  ? -34.374 -33.135 -10.278 1.00 51.37  ?  71  GLN   A CA  1 
ATOM   304  C  C   . GLN   A 1 39  ? -35.545 -33.965 -9.773  1.00 44.24  ?  71  GLN   A C   1 
ATOM   305  O  O   . GLN   A 1 39  ? -36.583 -33.382 -9.431  1.00 41.72  ?  71  GLN   A O   1 
ATOM   306  C  CB  . GLN   A 1 39  ? -34.408 -32.962 -11.799 1.00 54.98  ?  71  GLN   A CB  1 
ATOM   307  C  CG  . GLN   A 1 39  ? -34.121 -31.549 -12.253 1.00 44.48  ?  71  GLN   A CG  1 
ATOM   308  C  CD  . GLN   A 1 39  ? -34.064 -31.442 -13.717 1.00 55.73  ?  71  GLN   A CD  1 
ATOM   309  O  OE1 . GLN   A 1 39  ? -34.209 -32.436 -14.429 1.00 64.28  ?  71  GLN   A OE1 1 
ATOM   310  N  NE2 . GLN   A 1 39  ? -33.854 -30.241 -14.199 1.00 50.66  ?  71  GLN   A NE2 1 
ATOM   311  N  N   . PRO   A 1 40  ? -35.461 -35.280 -9.699  1.00 40.04  ?  72  PRO   A N   1 
ATOM   312  C  CA  . PRO   A 1 40  ? -36.544 -36.050 -9.100  1.00 44.37  ?  72  PRO   A CA  1 
ATOM   313  C  C   . PRO   A 1 40  ? -36.753 -35.795 -7.624  1.00 49.84  ?  72  PRO   A C   1 
ATOM   314  O  O   . PRO   A 1 40  ? -37.758 -36.242 -7.082  1.00 45.56  ?  72  PRO   A O   1 
ATOM   315  C  CB  . PRO   A 1 40  ? -36.105 -37.490 -9.342  1.00 48.95  ?  72  PRO   A CB  1 
ATOM   316  C  CG  . PRO   A 1 40  ? -35.299 -37.426 -10.490 1.00 56.59  ?  72  PRO   A CG  1 
ATOM   317  C  CD  . PRO   A 1 40  ? -34.561 -36.136 -10.451 1.00 53.87  ?  72  PRO   A CD  1 
ATOM   318  N  N   . LEU   A 1 41  ? -35.831 -35.142 -6.931  1.00 55.72  ?  73  LEU   A N   1 
ATOM   319  C  CA  . LEU   A 1 41  ? -35.987 -34.951 -5.500  1.00 40.94  ?  73  LEU   A CA  1 
ATOM   320  C  C   . LEU   A 1 41  ? -36.524 -33.586 -5.163  1.00 43.10  ?  73  LEU   A C   1 
ATOM   321  O  O   . LEU   A 1 41  ? -36.812 -33.332 -3.999  1.00 48.05  ?  73  LEU   A O   1 
ATOM   322  C  CB  . LEU   A 1 41  ? -34.668 -35.146 -4.758  1.00 39.51  ?  73  LEU   A CB  1 
ATOM   323  C  CG  . LEU   A 1 41  ? -34.236 -36.573 -4.496  1.00 40.96  ?  73  LEU   A CG  1 
ATOM   324  C  CD1 . LEU   A 1 41  ? -32.842 -36.614 -4.081  1.00 46.12  ?  73  LEU   A CD1 1 
ATOM   325  C  CD2 . LEU   A 1 41  ? -35.011 -37.145 -3.442  1.00 37.68  ?  73  LEU   A CD2 1 
ATOM   326  N  N   . LEU   A 1 42  ? -36.677 -32.710 -6.148  1.00 39.76  ?  74  LEU   A N   1 
ATOM   327  C  CA  . LEU   A 1 42  ? -37.173 -31.366 -5.906  1.00 40.18  ?  74  LEU   A CA  1 
ATOM   328  C  C   . LEU   A 1 42  ? -38.698 -31.343 -5.866  1.00 42.63  ?  74  LEU   A C   1 
ATOM   329  O  O   . LEU   A 1 42  ? -39.375 -30.637 -6.608  1.00 40.40  ?  74  LEU   A O   1 
ATOM   330  C  CB  . LEU   A 1 42  ? -36.640 -30.418 -6.954  1.00 38.55  ?  74  LEU   A CB  1 
ATOM   331  C  CG  . LEU   A 1 42  ? -35.146 -30.333 -6.911  1.00 39.38  ?  74  LEU   A CG  1 
ATOM   332  C  CD1 . LEU   A 1 42  ? -34.682 -29.728 -8.154  1.00 39.85  ?  74  LEU   A CD1 1 
ATOM   333  C  CD2 . LEU   A 1 42  ? -34.718 -29.523 -5.757  1.00 38.83  ?  74  LEU   A CD2 1 
ATOM   334  N  N   . ILE   A 1 43  ? -39.219 -32.077 -4.895  1.00 46.05  ?  75  ILE   A N   1 
ATOM   335  C  CA  . ILE   A 1 43  ? -40.642 -32.219 -4.656  1.00 47.76  ?  75  ILE   A CA  1 
ATOM   336  C  C   . ILE   A 1 43  ? -40.868 -32.023 -3.176  1.00 41.54  ?  75  ILE   A C   1 
ATOM   337  O  O   . ILE   A 1 43  ? -39.950 -32.146 -2.380  1.00 42.23  ?  75  ILE   A O   1 
ATOM   338  C  CB  . ILE   A 1 43  ? -41.130 -33.595 -5.103  1.00 41.93  ?  75  ILE   A CB  1 
ATOM   339  C  CG1 . ILE   A 1 43  ? -40.339 -34.670 -4.406  1.00 39.56  ?  75  ILE   A CG1 1 
ATOM   340  C  CG2 . ILE   A 1 43  ? -40.831 -33.745 -6.509  1.00 40.95  ?  75  ILE   A CG2 1 
ATOM   341  C  CD1 . ILE   A 1 43  ? -40.823 -36.026 -4.619  1.00 47.85  ?  75  ILE   A CD1 1 
ATOM   342  N  N   . GLU   A 1 44  ? -42.096 -31.701 -2.817  1.00 39.51  ?  76  GLU   A N   1 
ATOM   343  C  CA  . GLU   A 1 44  ? -42.494 -31.652 -1.418  1.00 39.18  ?  76  GLU   A CA  1 
ATOM   344  C  C   . GLU   A 1 44  ? -42.382 -33.045 -0.838  1.00 42.34  ?  76  GLU   A C   1 
ATOM   345  O  O   . GLU   A 1 44  ? -42.976 -33.982 -1.364  1.00 44.84  ?  76  GLU   A O   1 
ATOM   346  C  CB  . GLU   A 1 44  ? -43.926 -31.130 -1.326  1.00 56.78  ?  76  GLU   A CB  1 
ATOM   347  C  CG  . GLU   A 1 44  ? -44.437 -30.661 0.029   1.00 60.47  ?  76  GLU   A CG  1 
ATOM   348  C  CD  . GLU   A 1 44  ? -45.853 -30.099 -0.037  1.00 62.97  ?  76  GLU   A CD  1 
ATOM   349  O  OE1 . GLU   A 1 44  ? -46.584 -30.374 -1.011  1.00 56.98  ?  76  GLU   A OE1 1 
ATOM   350  O  OE2 . GLU   A 1 44  ? -46.229 -29.364 0.892   1.00 65.77  ?  76  GLU   A OE2 1 
ATOM   351  N  N   . ARG   A 1 45  ? -41.606 -33.204 0.228   1.00 40.38  ?  77  ARG   A N   1 
ATOM   352  C  CA  . ARG   A 1 45  ? -41.343 -34.524 0.785   1.00 40.56  ?  77  ARG   A CA  1 
ATOM   353  C  C   . ARG   A 1 45  ? -41.215 -34.480 2.303   1.00 41.70  ?  77  ARG   A C   1 
ATOM   354  O  O   . ARG   A 1 45  ? -40.236 -34.916 2.881   1.00 44.98  ?  77  ARG   A O   1 
ATOM   355  C  CB  . ARG   A 1 45  ? -40.080 -35.119 0.178   1.00 36.47  ?  77  ARG   A CB  1 
ATOM   356  C  CG  . ARG   A 1 45  ? -39.011 -34.115 -0.008  1.00 39.65  ?  77  ARG   A CG  1 
ATOM   357  C  CD  . ARG   A 1 45  ? -37.728 -34.672 -0.534  1.00 40.09  ?  77  ARG   A CD  1 
ATOM   358  N  NE  . ARG   A 1 45  ? -36.591 -33.866 -0.109  1.00 36.09  ?  77  ARG   A NE  1 
ATOM   359  C  CZ  . ARG   A 1 45  ? -36.300 -32.664 -0.576  1.00 29.92  ?  77  ARG   A CZ  1 
ATOM   360  N  NH1 . ARG   A 1 45  ? -37.032 -32.094 -1.477  1.00 34.49  ?  77  ARG   A NH1 1 
ATOM   361  N  NH2 . ARG   A 1 45  ? -35.269 -32.014 -0.135  1.00 36.77  ?  77  ARG   A NH2 1 
ATOM   362  N  N   . TYR   A 1 46  ? -42.231 -33.989 2.980   1.00 43.91  ?  78  TYR   A N   1 
ATOM   363  C  CA  . TYR   A 1 46  ? -42.241 -34.047 4.420   1.00 43.84  ?  78  TYR   A CA  1 
ATOM   364  C  C   . TYR   A 1 46  ? -42.618 -35.448 4.835   1.00 49.08  ?  78  TYR   A C   1 
ATOM   365  O  O   . TYR   A 1 46  ? -43.046 -36.245 4.019   1.00 55.17  ?  78  TYR   A O   1 
ATOM   366  C  CB  . TYR   A 1 46  ? -43.186 -33.013 5.002   1.00 41.87  ?  78  TYR   A CB  1 
ATOM   367  C  CG  . TYR   A 1 46  ? -44.565 -32.980 4.461   1.00 47.98  ?  78  TYR   A CG  1 
ATOM   368  C  CD1 . TYR   A 1 46  ? -45.529 -33.797 4.966   1.00 55.03  ?  78  TYR   A CD1 1 
ATOM   369  C  CD2 . TYR   A 1 46  ? -44.927 -32.077 3.488   1.00 57.72  ?  78  TYR   A CD2 1 
ATOM   370  C  CE1 . TYR   A 1 46  ? -46.806 -33.750 4.498   1.00 64.76  ?  78  TYR   A CE1 1 
ATOM   371  C  CE2 . TYR   A 1 46  ? -46.202 -32.033 3.009   1.00 62.91  ?  78  TYR   A CE2 1 
ATOM   372  C  CZ  . TYR   A 1 46  ? -47.136 -32.873 3.525   1.00 60.27  ?  78  TYR   A CZ  1 
ATOM   373  O  OH  . TYR   A 1 46  ? -48.427 -32.849 3.072   1.00 60.92  ?  78  TYR   A OH  1 
ATOM   374  N  N   . PRO   A 1 47  ? -42.427 -35.795 6.099   1.00 48.05  ?  79  PRO   A N   1 
ATOM   375  C  CA  . PRO   A 1 47  ? -42.596 -37.186 6.514   1.00 47.69  ?  79  PRO   A CA  1 
ATOM   376  C  C   . PRO   A 1 47  ? -44.041 -37.648 6.448   1.00 46.81  ?  79  PRO   A C   1 
ATOM   377  O  O   . PRO   A 1 47  ? -44.941 -37.006 6.980   1.00 51.42  ?  79  PRO   A O   1 
ATOM   378  C  CB  . PRO   A 1 47  ? -42.079 -37.166 7.948   1.00 51.39  ?  79  PRO   A CB  1 
ATOM   379  C  CG  . PRO   A 1 47  ? -41.164 -36.092 7.971   1.00 47.38  ?  79  PRO   A CG  1 
ATOM   380  C  CD  . PRO   A 1 47  ? -41.745 -35.030 7.144   1.00 47.55  ?  79  PRO   A CD  1 
ATOM   381  N  N   . GLY   A 1 48  ? -44.252 -38.789 5.833   1.00 45.13  ?  80  GLY   A N   1 
ATOM   382  C  CA  . GLY   A 1 48  ? -45.579 -39.284 5.591   1.00 58.61  ?  80  GLY   A CA  1 
ATOM   383  C  C   . GLY   A 1 48  ? -46.216 -38.829 4.298   1.00 53.51  ?  80  GLY   A C   1 
ATOM   384  O  O   . GLY   A 1 48  ? -47.167 -39.457 3.840   1.00 54.37  ?  80  GLY   A O   1 
ATOM   385  N  N   . SER   A 1 49  ? -45.733 -37.762 3.697   1.00 57.25  ?  81  SER   A N   1 
ATOM   386  C  CA  . SER   A 1 49  ? -46.284 -37.337 2.432   1.00 57.97  ?  81  SER   A CA  1 
ATOM   387  C  C   . SER   A 1 49  ? -46.016 -38.371 1.364   1.00 57.97  ?  81  SER   A C   1 
ATOM   388  O  O   . SER   A 1 49  ? -45.129 -39.207 1.498   1.00 62.08  ?  81  SER   A O   1 
ATOM   389  C  CB  . SER   A 1 49  ? -45.662 -36.041 1.964   1.00 58.00  ?  81  SER   A CB  1 
ATOM   390  O  OG  . SER   A 1 49  ? -44.283 -36.091 2.224   1.00 62.51  ?  81  SER   A OG  1 
ATOM   391  N  N   . PRO   A 1 50  ? -46.742 -38.302 0.267   1.00 57.84  ?  82  PRO   A N   1 
ATOM   392  C  CA  . PRO   A 1 50  ? -46.418 -39.171 -0.852  1.00 45.30  ?  82  PRO   A CA  1 
ATOM   393  C  C   . PRO   A 1 50  ? -45.051 -38.904 -1.393  1.00 51.46  ?  82  PRO   A C   1 
ATOM   394  O  O   . PRO   A 1 50  ? -44.420 -39.819 -1.923  1.00 58.63  ?  82  PRO   A O   1 
ATOM   395  C  CB  . PRO   A 1 50  ? -47.507 -38.835 -1.864  1.00 42.62  ?  82  PRO   A CB  1 
ATOM   396  C  CG  . PRO   A 1 50  ? -48.551 -38.225 -1.093  1.00 51.22  ?  82  PRO   A CG  1 
ATOM   397  C  CD  . PRO   A 1 50  ? -47.908 -37.475 -0.020  1.00 59.90  ?  82  PRO   A CD  1 
ATOM   398  N  N   . GLY   A 1 51  ? -44.566 -37.669 -1.275  1.00 55.44  ?  83  GLY   A N   1 
ATOM   399  C  CA  . GLY   A 1 51  ? -43.228 -37.358 -1.751  1.00 53.23  ?  83  GLY   A CA  1 
ATOM   400  C  C   . GLY   A 1 51  ? -42.120 -38.008 -0.944  1.00 52.59  ?  83  GLY   A C   1 
ATOM   401  O  O   . GLY   A 1 51  ? -41.032 -38.256 -1.465  1.00 44.92  ?  83  GLY   A O   1 
ATOM   402  N  N   . SER   A 1 52  ? -42.363 -38.283 0.333   1.00 52.19  ?  84  SER   A N   1 
ATOM   403  C  CA  . SER   A 1 52  ? -41.414 -39.092 1.068   1.00 45.06  ?  84  SER   A CA  1 
ATOM   404  C  C   . SER   A 1 52  ? -41.287 -40.460 0.438   1.00 51.53  ?  84  SER   A C   1 
ATOM   405  O  O   . SER   A 1 52  ? -40.185 -40.994 0.321   1.00 54.19  ?  84  SER   A O   1 
ATOM   406  C  CB  . SER   A 1 52  ? -41.836 -39.223 2.515   1.00 52.79  ?  84  SER   A CB  1 
ATOM   407  O  OG  . SER   A 1 52  ? -40.722 -39.116 3.359   1.00 53.16  ?  84  SER   A OG  1 
ATOM   408  N  N   . TYR   A 1 53  ? -42.402 -41.054 0.029   1.00 53.35  ?  85  TYR   A N   1 
ATOM   409  C  CA  . TYR   A 1 53  ? -42.328 -42.347 -0.631  1.00 57.04  ?  85  TYR   A CA  1 
ATOM   410  C  C   . TYR   A 1 53  ? -41.623 -42.234 -1.974  1.00 53.77  ?  85  TYR   A C   1 
ATOM   411  O  O   . TYR   A 1 53  ? -40.760 -43.045 -2.312  1.00 54.02  ?  85  TYR   A O   1 
ATOM   412  C  CB  . TYR   A 1 53  ? -43.722 -42.917 -0.814  1.00 56.68  ?  85  TYR   A CB  1 
ATOM   413  C  CG  . TYR   A 1 53  ? -43.717 -44.273 -1.439  1.00 65.31  ?  85  TYR   A CG  1 
ATOM   414  C  CD1 . TYR   A 1 53  ? -43.333 -45.373 -0.712  1.00 70.30  ?  85  TYR   A CD1 1 
ATOM   415  C  CD2 . TYR   A 1 53  ? -44.085 -44.453 -2.756  1.00 66.55  ?  85  TYR   A CD2 1 
ATOM   416  C  CE1 . TYR   A 1 53  ? -43.319 -46.615 -1.265  1.00 78.56  ?  85  TYR   A CE1 1 
ATOM   417  C  CE2 . TYR   A 1 53  ? -44.076 -45.701 -3.323  1.00 70.05  ?  85  TYR   A CE2 1 
ATOM   418  C  CZ  . TYR   A 1 53  ? -43.692 -46.780 -2.562  1.00 79.91  ?  85  TYR   A CZ  1 
ATOM   419  O  OH  . TYR   A 1 53  ? -43.678 -48.041 -3.095  1.00 91.24  ?  85  TYR   A OH  1 
ATOM   420  N  N   . ALA   A 1 54  ? -41.992 -41.243 -2.766  1.00 51.10  ?  86  ALA   A N   1 
ATOM   421  C  CA  . ALA   A 1 54  ? -41.317 -41.038 -4.034  1.00 52.93  ?  86  ALA   A CA  1 
ATOM   422  C  C   . ALA   A 1 54  ? -39.824 -40.894 -3.832  1.00 54.64  ?  86  ALA   A C   1 
ATOM   423  O  O   . ALA   A 1 54  ? -39.029 -41.512 -4.541  1.00 60.37  ?  86  ALA   A O   1 
ATOM   424  C  CB  . ALA   A 1 54  ? -41.879 -39.807 -4.730  1.00 50.90  ?  86  ALA   A CB  1 
ATOM   425  N  N   . ALA   A 1 55  ? -39.416 -40.086 -2.866  1.00 50.23  ?  87  ALA   A N   1 
ATOM   426  C  CA  . ALA   A 1 55  ? -38.000 -39.819 -2.719  1.00 42.87  ?  87  ALA   A CA  1 
ATOM   427  C  C   . ALA   A 1 55  ? -37.272 -41.054 -2.251  1.00 51.36  ?  87  ALA   A C   1 
ATOM   428  O  O   . ALA   A 1 55  ? -36.214 -41.392 -2.779  1.00 53.52  ?  87  ALA   A O   1 
ATOM   429  C  CB  . ALA   A 1 55  ? -37.788 -38.670 -1.757  1.00 41.34  ?  87  ALA   A CB  1 
ATOM   430  N  N   . ARG   A 1 56  ? -37.832 -41.735 -1.256  1.00 55.59  ?  88  ARG   A N   1 
ATOM   431  C  CA  . ARG   A 1 56  ? -37.306 -43.010 -0.791  1.00 43.46  ?  88  ARG   A CA  1 
ATOM   432  C  C   . ARG   A 1 56  ? -37.097 -43.958 -1.952  1.00 49.07  ?  88  ARG   A C   1 
ATOM   433  O  O   . ARG   A 1 56  ? -36.018 -44.521 -2.128  1.00 56.11  ?  88  ARG   A O   1 
ATOM   434  C  CB  . ARG   A 1 56  ? -38.293 -43.593 0.212   1.00 54.29  ?  88  ARG   A CB  1 
ATOM   435  C  CG  . ARG   A 1 56  ? -37.710 -44.409 1.312   1.00 59.29  ?  88  ARG   A CG  1 
ATOM   436  C  CD  . ARG   A 1 56  ? -38.756 -44.791 2.360   1.00 61.82  ?  88  ARG   A CD  1 
ATOM   437  N  NE  . ARG   A 1 56  ? -39.637 -43.684 2.708   1.00 61.57  ?  88  ARG   A NE  1 
ATOM   438  C  CZ  . ARG   A 1 56  ? -40.964 -43.719 2.657   1.00 58.35  ?  88  ARG   A CZ  1 
ATOM   439  N  NH1 . ARG   A 1 56  ? -41.601 -44.817 2.288   1.00 70.16  ?  88  ARG   A NH1 1 
ATOM   440  N  NH2 . ARG   A 1 56  ? -41.663 -42.649 2.990   1.00 59.08  ?  88  ARG   A NH2 1 
ATOM   441  N  N   . GLN   A 1 57  ? -38.118 -44.128 -2.777  1.00 59.29  ?  89  GLN   A N   1 
ATOM   442  C  CA  . GLN   A 1 57  ? -38.006 -45.030 -3.910  1.00 67.86  ?  89  GLN   A CA  1 
ATOM   443  C  C   . GLN   A 1 57  ? -36.897 -44.591 -4.838  1.00 64.48  ?  89  GLN   A C   1 
ATOM   444  O  O   . GLN   A 1 57  ? -35.976 -45.355 -5.125  1.00 74.24  ?  89  GLN   A O   1 
ATOM   445  C  CB  . GLN   A 1 57  ? -39.329 -45.091 -4.653  1.00 72.41  ?  89  GLN   A CB  1 
ATOM   446  C  CG  . GLN   A 1 57  ? -40.392 -45.862 -3.908  1.00 73.46  ?  89  GLN   A CG  1 
ATOM   447  C  CD  . GLN   A 1 57  ? -40.010 -47.293 -3.731  1.00 82.19  ?  89  GLN   A CD  1 
ATOM   448  O  OE1 . GLN   A 1 57  ? -39.719 -47.993 -4.701  1.00 86.32  ?  89  GLN   A OE1 1 
ATOM   449  N  NE2 . GLN   A 1 57  ? -39.977 -47.740 -2.488  1.00 76.28  ?  89  GLN   A NE2 1 
ATOM   450  N  N   . HIS   A 1 58  ? -36.964 -43.350 -5.306  1.00 60.19  ?  90  HIS   A N   1 
ATOM   451  C  CA  . HIS   A 1 58  ? -35.929 -42.803 -6.178  1.00 61.30  ?  90  HIS   A CA  1 
ATOM   452  C  C   . HIS   A 1 58  ? -34.519 -43.039 -5.658  1.00 61.50  ?  90  HIS   A C   1 
ATOM   453  O  O   . HIS   A 1 58  ? -33.598 -43.275 -6.440  1.00 60.71  ?  90  HIS   A O   1 
ATOM   454  C  CB  . HIS   A 1 58  ? -36.141 -41.322 -6.339  1.00 53.25  ?  90  HIS   A CB  1 
ATOM   455  C  CG  . HIS   A 1 58  ? -35.025 -40.632 -7.045  1.00 52.71  ?  90  HIS   A CG  1 
ATOM   456  N  ND1 . HIS   A 1 58  ? -34.876 -40.666 -8.410  1.00 56.60  ?  90  HIS   A ND1 1 
ATOM   457  C  CD2 . HIS   A 1 58  ? -34.015 -39.870 -6.575  1.00 50.82  ?  90  HIS   A CD2 1 
ATOM   458  C  CE1 . HIS   A 1 58  ? -33.813 -39.966 -8.749  1.00 56.98  ?  90  HIS   A CE1 1 
ATOM   459  N  NE2 . HIS   A 1 58  ? -33.276 -39.469 -7.654  1.00 55.02  ?  90  HIS   A NE2 1 
ATOM   460  N  N   . ILE   A 1 59  ? -34.308 -42.930 -4.354  1.00 57.47  ?  91  ILE   A N   1 
ATOM   461  C  CA  . ILE   A 1 59  ? -32.953 -43.070 -3.851  1.00 53.08  ?  91  ILE   A CA  1 
ATOM   462  C  C   . ILE   A 1 59  ? -32.486 -44.496 -4.018  1.00 59.23  ?  91  ILE   A C   1 
ATOM   463  O  O   . ILE   A 1 59  ? -31.389 -44.751 -4.516  1.00 66.24  ?  91  ILE   A O   1 
ATOM   464  C  CB  . ILE   A 1 59  ? -32.865 -42.596 -2.396  1.00 46.90  ?  91  ILE   A CB  1 
ATOM   465  C  CG1 . ILE   A 1 59  ? -32.688 -41.090 -2.372  1.00 44.50  ?  91  ILE   A CG1 1 
ATOM   466  C  CG2 . ILE   A 1 59  ? -31.707 -43.169 -1.711  1.00 41.71  ?  91  ILE   A CG2 1 
ATOM   467  C  CD1 . ILE   A 1 59  ? -33.214 -40.443 -1.176  1.00 44.86  ?  91  ILE   A CD1 1 
ATOM   468  N  N   . MET   A 1 60  ? -33.323 -45.448 -3.646  1.00 63.69  ?  92  MET   A N   1 
ATOM   469  C  CA  . MET   A 1 60  ? -32.932 -46.847 -3.763  1.00 70.82  ?  92  MET   A CA  1 
ATOM   470  C  C   . MET   A 1 60  ? -32.780 -47.252 -5.215  1.00 62.11  ?  92  MET   A C   1 
ATOM   471  O  O   . MET   A 1 60  ? -31.813 -47.914 -5.591  1.00 61.74  ?  92  MET   A O   1 
ATOM   472  C  CB  . MET   A 1 60  ? -33.969 -47.719 -3.086  1.00 73.20  ?  92  MET   A CB  1 
ATOM   473  C  CG  . MET   A 1 60  ? -33.756 -47.920 -1.612  1.00 71.95  ?  92  MET   A CG  1 
ATOM   474  S  SD  . MET   A 1 60  ? -35.304 -48.360 -0.852  1.00 74.29  ?  92  MET   A SD  1 
ATOM   475  C  CE  . MET   A 1 60  ? -36.187 -49.234 -2.182  1.00 81.58  ?  92  MET   A CE  1 
ATOM   476  N  N   . GLN   A 1 61  ? -33.742 -46.891 -6.042  1.00 59.73  ?  93  GLN   A N   1 
ATOM   477  C  CA  . GLN   A 1 61  ? -33.644 -47.217 -7.450  1.00 69.37  ?  93  GLN   A CA  1 
ATOM   478  C  C   . GLN   A 1 61  ? -32.318 -46.755 -8.035  1.00 69.66  ?  93  GLN   A C   1 
ATOM   479  O  O   . GLN   A 1 61  ? -31.657 -47.501 -8.762  1.00 76.12  ?  93  GLN   A O   1 
ATOM   480  C  CB  . GLN   A 1 61  ? -34.815 -46.599 -8.204  1.00 75.34  ?  93  GLN   A CB  1 
ATOM   481  C  CG  . GLN   A 1 61  ? -36.163 -47.114 -7.709  1.00 81.42  ?  93  GLN   A CG  1 
ATOM   482  C  CD  . GLN   A 1 61  ? -37.327 -46.605 -8.529  1.00 94.97  ?  93  GLN   A CD  1 
ATOM   483  O  OE1 . GLN   A 1 61  ? -37.252 -45.534 -9.133  1.00 92.72  ?  93  GLN   A OE1 1 
ATOM   484  N  NE2 . GLN   A 1 61  ? -38.416 -47.373 -8.555  1.00 87.87  ?  93  GLN   A NE2 1 
ATOM   485  N  N   . ARG   A 1 62  ? -31.909 -45.524 -7.740  1.00 65.69  ?  94  ARG   A N   1 
ATOM   486  C  CA  . ARG   A 1 62  ? -30.672 -45.037 -8.324  1.00 60.99  ?  94  ARG   A CA  1 
ATOM   487  C  C   . ARG   A 1 62  ? -29.445 -45.682 -7.717  1.00 62.19  ?  94  ARG   A C   1 
ATOM   488  O  O   . ARG   A 1 62  ? -28.390 -45.675 -8.349  1.00 65.85  ?  94  ARG   A O   1 
ATOM   489  C  CB  . ARG   A 1 62  ? -30.587 -43.541 -8.185  1.00 57.11  ?  94  ARG   A CB  1 
ATOM   490  C  CG  . ARG   A 1 62  ? -31.408 -42.829 -9.212  1.00 63.88  ?  94  ARG   A CG  1 
ATOM   491  C  CD  . ARG   A 1 62  ? -30.699 -41.664 -9.830  1.00 67.74  ?  94  ARG   A CD  1 
ATOM   492  N  NE  . ARG   A 1 62  ? -29.348 -41.993 -10.260 1.00 63.15  ?  94  ARG   A NE  1 
ATOM   493  C  CZ  . ARG   A 1 62  ? -28.942 -42.063 -11.519 1.00 68.56  ?  94  ARG   A CZ  1 
ATOM   494  N  NH1 . ARG   A 1 62  ? -29.769 -41.840 -12.523 1.00 60.43  ?  94  ARG   A NH1 1 
ATOM   495  N  NH2 . ARG   A 1 62  ? -27.682 -42.373 -11.770 1.00 78.16  ?  94  ARG   A NH2 1 
ATOM   496  N  N   . ILE   A 1 63  ? -29.543 -46.240 -6.520  1.00 62.93  ?  95  ILE   A N   1 
ATOM   497  C  CA  . ILE   A 1 63  ? -28.438 -47.031 -5.994  1.00 58.43  ?  95  ILE   A CA  1 
ATOM   498  C  C   . ILE   A 1 63  ? -28.410 -48.410 -6.630  1.00 66.83  ?  95  ILE   A C   1 
ATOM   499  O  O   . ILE   A 1 63  ? -27.371 -48.862 -7.118  1.00 72.11  ?  95  ILE   A O   1 
ATOM   500  C  CB  . ILE   A 1 63  ? -28.537 -47.129 -4.468  1.00 64.85  ?  95  ILE   A CB  1 
ATOM   501  C  CG1 . ILE   A 1 63  ? -28.304 -45.752 -3.846  1.00 59.40  ?  95  ILE   A CG1 1 
ATOM   502  C  CG2 . ILE   A 1 63  ? -27.568 -48.165 -3.945  1.00 60.71  ?  95  ILE   A CG2 1 
ATOM   503  C  CD1 . ILE   A 1 63  ? -28.077 -45.776 -2.351  1.00 57.15  ?  95  ILE   A CD1 1 
ATOM   504  N  N   . GLN   A 1 64  ? -29.546 -49.109 -6.612  1.00 74.43  ?  96  GLN   A N   1 
ATOM   505  C  CA  . GLN   A 1 64  ? -29.607 -50.471 -7.127  1.00 69.65  ?  96  GLN   A CA  1 
ATOM   506  C  C   . GLN   A 1 64  ? -29.034 -50.574 -8.522  1.00 70.23  ?  96  GLN   A C   1 
ATOM   507  O  O   . GLN   A 1 64  ? -28.447 -51.595 -8.874  1.00 83.74  ?  96  GLN   A O   1 
ATOM   508  C  CB  . GLN   A 1 64  ? -31.046 -50.958 -7.123  1.00 72.45  ?  96  GLN   A CB  1 
ATOM   509  C  CG  . GLN   A 1 64  ? -31.541 -51.368 -5.754  1.00 77.73  ?  96  GLN   A CG  1 
ATOM   510  C  CD  . GLN   A 1 64  ? -33.049 -51.379 -5.665  1.00 83.45  ?  96  GLN   A CD  1 
ATOM   511  O  OE1 . GLN   A 1 64  ? -33.752 -51.129 -6.651  1.00 74.28  ?  96  GLN   A OE1 1 
ATOM   512  N  NE2 . GLN   A 1 64  ? -33.559 -51.663 -4.478  1.00 81.45  ?  96  GLN   A NE2 1 
ATOM   513  N  N   . ARG   A 1 65  ? -29.170 -49.559 -9.314  1.00 63.45  ?  97  ARG   A N   1 
ATOM   514  C  CA  . ARG   A 1 65  ? -28.632 -49.681 -10.649 1.00 70.31  ?  97  ARG   A CA  1 
ATOM   515  C  C   . ARG   A 1 65  ? -27.197 -49.657 -10.680 1.00 71.73  ?  97  ARG   A C   1 
ATOM   516  O  O   . ARG   A 1 65  ? -26.717 -49.586 -11.801 1.00 74.63  ?  97  ARG   A O   1 
ATOM   517  C  CB  . ARG   A 1 65  ? -29.148 -48.574 -11.566 1.00 74.50  ?  97  ARG   A CB  1 
ATOM   518  C  CG  . ARG   A 1 65  ? -28.460 -47.227 -11.430 1.00 73.58  ?  97  ARG   A CG  1 
ATOM   519  C  CD  . ARG   A 1 65  ? -28.639 -46.371 -12.645 1.00 67.35  ?  97  ARG   A CD  1 
ATOM   520  N  NE  . ARG   A 1 65  ? -29.781 -46.733 -13.457 1.00 72.95  ?  97  ARG   A NE  1 
ATOM   521  C  CZ  . ARG   A 1 65  ? -29.908 -46.369 -14.726 1.00 85.29  ?  97  ARG   A CZ  1 
ATOM   522  N  NH1 . ARG   A 1 65  ? -28.963 -45.647 -15.309 1.00 90.06  ?  97  ARG   A NH1 1 
ATOM   523  N  NH2 . ARG   A 1 65  ? -30.974 -46.731 -15.418 1.00 80.32  ?  97  ARG   A NH2 1 
ATOM   524  N  N   . LEU   A 1 66  ? -26.478 -49.668 -9.570  1.00 75.66  ?  98  LEU   A N   1 
ATOM   525  C  CA  . LEU   A 1 66  ? -25.031 -49.611 -9.596  1.00 76.86  ?  98  LEU   A CA  1 
ATOM   526  C  C   . LEU   A 1 66  ? -24.487 -51.013 -9.435  1.00 77.15  ?  98  LEU   A C   1 
ATOM   527  O  O   . LEU   A 1 66  ? -25.222 -51.958 -9.147  1.00 78.51  ?  98  LEU   A O   1 
ATOM   528  C  CB  . LEU   A 1 66  ? -24.495 -48.710 -8.486  1.00 83.44  ?  98  LEU   A CB  1 
ATOM   529  C  CG  . LEU   A 1 66  ? -24.953 -47.257 -8.393  1.00 73.94  ?  98  LEU   A CG  1 
ATOM   530  C  CD1 . LEU   A 1 66  ? -24.233 -46.618 -7.238  1.00 67.32  ?  98  LEU   A CD1 1 
ATOM   531  C  CD2 . LEU   A 1 66  ? -24.696 -46.499 -9.673  1.00 61.64  ?  98  LEU   A CD2 1 
ATOM   532  N  N   . GLN   A 1 67  ? -23.177 -51.143 -9.595  1.00 73.36  ?  99  GLN   A N   1 
ATOM   533  C  CA  . GLN   A 1 67  ? -22.598 -52.469 -9.535  1.00 71.76  ?  99  GLN   A CA  1 
ATOM   534  C  C   . GLN   A 1 67  ? -22.159 -52.867 -8.138  1.00 75.21  ?  99  GLN   A C   1 
ATOM   535  O  O   . GLN   A 1 67  ? -22.236 -54.050 -7.799  1.00 85.87  ?  99  GLN   A O   1 
ATOM   536  C  CB  . GLN   A 1 67  ? -21.424 -52.567 -10.493 1.00 67.20  ?  99  GLN   A CB  1 
ATOM   537  C  CG  . GLN   A 1 67  ? -21.856 -52.537 -11.934 1.00 77.13  ?  99  GLN   A CG  1 
ATOM   538  C  CD  . GLN   A 1 67  ? -20.688 -52.579 -12.888 1.00 87.93  ?  99  GLN   A CD  1 
ATOM   539  O  OE1 . GLN   A 1 67  ? -20.559 -51.723 -13.756 1.00 98.82  ?  99  GLN   A OE1 1 
ATOM   540  N  NE2 . GLN   A 1 67  ? -19.827 -53.574 -12.734 1.00 82.65  ?  99  GLN   A NE2 1 
ATOM   541  N  N   . ALA   A 1 68  ? -21.710 -51.942 -7.306  1.00 62.66  ?  100 ALA   A N   1 
ATOM   542  C  CA  . ALA   A 1 68  ? -21.148 -52.398 -6.048  1.00 69.87  ?  100 ALA   A CA  1 
ATOM   543  C  C   . ALA   A 1 68  ? -22.234 -53.048 -5.213  1.00 74.93  ?  100 ALA   A C   1 
ATOM   544  O  O   . ALA   A 1 68  ? -23.421 -52.868 -5.465  1.00 78.74  ?  100 ALA   A O   1 
ATOM   545  C  CB  . ALA   A 1 68  ? -20.483 -51.250 -5.310  1.00 65.50  ?  100 ALA   A CB  1 
ATOM   546  N  N   . ASP   A 1 69  ? -21.822 -53.848 -4.231  1.00 72.81  ?  101 ASP   A N   1 
ATOM   547  C  CA  . ASP   A 1 69  ? -22.786 -54.634 -3.458  1.00 83.97  ?  101 ASP   A CA  1 
ATOM   548  C  C   . ASP   A 1 69  ? -23.380 -53.758 -2.369  1.00 77.09  ?  101 ASP   A C   1 
ATOM   549  O  O   . ASP   A 1 69  ? -23.207 -53.992 -1.172  1.00 72.16  ?  101 ASP   A O   1 
ATOM   550  C  CB  . ASP   A 1 69  ? -22.160 -55.891 -2.868  1.00 83.53  ?  101 ASP   A CB  1 
ATOM   551  C  CG  . ASP   A 1 69  ? -22.652 -57.135 -3.540  1.00 89.76  ?  101 ASP   A CG  1 
ATOM   552  O  OD1 . ASP   A 1 69  ? -23.797 -57.129 -4.029  1.00 86.36  ?  101 ASP   A OD1 1 
ATOM   553  O  OD2 . ASP   A 1 69  ? -21.879 -58.106 -3.601  1.00 90.03  ?  101 ASP   A OD2 1 
ATOM   554  N  N   . TRP   A 1 70  ? -24.120 -52.750 -2.816  1.00 74.39  ?  102 TRP   A N   1 
ATOM   555  C  CA  . TRP   A 1 70  ? -24.827 -51.883 -1.894  1.00 72.07  ?  102 TRP   A CA  1 
ATOM   556  C  C   . TRP   A 1 70  ? -25.982 -52.653 -1.272  1.00 63.76  ?  102 TRP   A C   1 
ATOM   557  O  O   . TRP   A 1 70  ? -26.846 -53.184 -1.972  1.00 62.02  ?  102 TRP   A O   1 
ATOM   558  C  CB  . TRP   A 1 70  ? -25.339 -50.636 -2.608  1.00 67.49  ?  102 TRP   A CB  1 
ATOM   559  C  CG  . TRP   A 1 70  ? -24.300 -49.608 -3.001  1.00 60.75  ?  102 TRP   A CG  1 
ATOM   560  C  CD1 . TRP   A 1 70  ? -23.911 -49.300 -4.260  1.00 70.46  ?  102 TRP   A CD1 1 
ATOM   561  C  CD2 . TRP   A 1 70  ? -23.564 -48.739 -2.138  1.00 50.53  ?  102 TRP   A CD2 1 
ATOM   562  N  NE1 . TRP   A 1 70  ? -22.966 -48.311 -4.241  1.00 60.06  ?  102 TRP   A NE1 1 
ATOM   563  C  CE2 . TRP   A 1 70  ? -22.742 -47.951 -2.943  1.00 56.86  ?  102 TRP   A CE2 1 
ATOM   564  C  CE3 . TRP   A 1 70  ? -23.520 -48.555 -0.765  1.00 51.52  ?  102 TRP   A CE3 1 
ATOM   565  C  CZ2 . TRP   A 1 70  ? -21.892 -46.996 -2.420  1.00 57.61  ?  102 TRP   A CZ2 1 
ATOM   566  C  CZ3 . TRP   A 1 70  ? -22.668 -47.622 -0.253  1.00 49.88  ?  102 TRP   A CZ3 1 
ATOM   567  C  CH2 . TRP   A 1 70  ? -21.868 -46.852 -1.073  1.00 51.53  ?  102 TRP   A CH2 1 
ATOM   568  N  N   . VAL   A 1 71  ? -25.987 -52.709 0.043   1.00 52.63  ?  103 VAL   A N   1 
ATOM   569  C  CA  . VAL   A 1 71  ? -27.014 -53.390 0.809   1.00 58.49  ?  103 VAL   A CA  1 
ATOM   570  C  C   . VAL   A 1 71  ? -27.929 -52.342 1.436   1.00 58.27  ?  103 VAL   A C   1 
ATOM   571  O  O   . VAL   A 1 71  ? -27.568 -51.674 2.413   1.00 52.88  ?  103 VAL   A O   1 
ATOM   572  C  CB  . VAL   A 1 71  ? -26.376 -54.301 1.861   1.00 61.22  ?  103 VAL   A CB  1 
ATOM   573  C  CG1 . VAL   A 1 71  ? -27.293 -54.587 3.016   1.00 55.38  ?  103 VAL   A CG1 1 
ATOM   574  C  CG2 . VAL   A 1 71  ? -25.988 -55.567 1.216   1.00 66.08  ?  103 VAL   A CG2 1 
ATOM   575  N  N   . LEU   A 1 72  ? -29.133 -52.227 0.905   1.00 54.31  ?  104 LEU   A N   1 
ATOM   576  C  CA  . LEU   A 1 72  ? -30.076 -51.217 1.344   1.00 53.52  ?  104 LEU   A CA  1 
ATOM   577  C  C   . LEU   A 1 72  ? -30.950 -51.726 2.471   1.00 53.60  ?  104 LEU   A C   1 
ATOM   578  O  O   . LEU   A 1 72  ? -31.300 -52.894 2.516   1.00 64.88  ?  104 LEU   A O   1 
ATOM   579  C  CB  . LEU   A 1 72  ? -30.946 -50.794 0.182   1.00 50.73  ?  104 LEU   A CB  1 
ATOM   580  C  CG  . LEU   A 1 72  ? -30.256 -49.781 -0.696  1.00 58.64  ?  104 LEU   A CG  1 
ATOM   581  C  CD1 . LEU   A 1 72  ? -30.697 -49.828 -2.147  1.00 55.91  ?  104 LEU   A CD1 1 
ATOM   582  C  CD2 . LEU   A 1 72  ? -30.517 -48.451 -0.082  1.00 63.68  ?  104 LEU   A CD2 1 
ATOM   583  N  N   . GLU   A 1 73  ? -31.315 -50.825 3.376   1.00 52.15  ?  105 GLU   A N   1 
ATOM   584  C  CA  . GLU   A 1 73  ? -32.124 -51.160 4.542   1.00 53.41  ?  105 GLU   A CA  1 
ATOM   585  C  C   . GLU   A 1 73  ? -32.995 -49.955 4.864   1.00 64.19  ?  105 GLU   A C   1 
ATOM   586  O  O   . GLU   A 1 73  ? -32.481 -48.937 5.323   1.00 67.16  ?  105 GLU   A O   1 
ATOM   587  C  CB  . GLU   A 1 73  ? -31.252 -51.533 5.744   1.00 58.16  ?  105 GLU   A CB  1 
ATOM   588  C  CG  . GLU   A 1 73  ? -31.951 -51.431 7.134   1.00 65.19  ?  105 GLU   A CG  1 
ATOM   589  C  CD  . GLU   A 1 73  ? -30.974 -51.429 8.311   1.00 88.39  ?  105 GLU   A CD  1 
ATOM   590  O  OE1 . GLU   A 1 73  ? -31.442 -51.276 9.473   1.00 79.35  ?  105 GLU   A OE1 1 
ATOM   591  O  OE2 . GLU   A 1 73  ? -29.745 -51.569 8.075   1.00 76.37  ?  105 GLU   A OE2 1 
ATOM   592  N  N   . ILE   A 1 74  ? -34.301 -50.067 4.649   1.00 65.21  ?  106 ILE   A N   1 
ATOM   593  C  CA  . ILE   A 1 74  ? -35.248 -49.032 5.040   1.00 55.48  ?  106 ILE   A CA  1 
ATOM   594  C  C   . ILE   A 1 74  ? -35.681 -49.289 6.467   1.00 50.36  ?  106 ILE   A C   1 
ATOM   595  O  O   . ILE   A 1 74  ? -36.186 -50.364 6.783   1.00 64.91  ?  106 ILE   A O   1 
ATOM   596  C  CB  . ILE   A 1 74  ? -36.463 -49.007 4.115   1.00 48.03  ?  106 ILE   A CB  1 
ATOM   597  C  CG1 . ILE   A 1 74  ? -35.992 -48.846 2.676   1.00 51.19  ?  106 ILE   A CG1 1 
ATOM   598  C  CG2 . ILE   A 1 74  ? -37.415 -47.938 4.574   1.00 57.38  ?  106 ILE   A CG2 1 
ATOM   599  C  CD1 . ILE   A 1 74  ? -36.436 -47.619 2.047   1.00 57.82  ?  106 ILE   A CD1 1 
ATOM   600  N  N   . ASP   A 1 75  ? -35.538 -48.285 7.312   1.00 48.31  ?  107 ASP   A N   1 
ATOM   601  C  CA  . ASP   A 1 75  ? -35.686 -48.430 8.743   1.00 55.38  ?  107 ASP   A CA  1 
ATOM   602  C  C   . ASP   A 1 75  ? -36.884 -47.602 9.198   1.00 67.41  ?  107 ASP   A C   1 
ATOM   603  O  O   . ASP   A 1 75  ? -36.757 -46.618 9.936   1.00 64.42  ?  107 ASP   A O   1 
ATOM   604  C  CB  . ASP   A 1 75  ? -34.405 -48.005 9.405   1.00 61.52  ?  107 ASP   A CB  1 
ATOM   605  C  CG  . ASP   A 1 75  ? -34.544 -47.803 10.870  1.00 69.88  ?  107 ASP   A CG  1 
ATOM   606  O  OD1 . ASP   A 1 75  ? -35.185 -48.674 11.507  1.00 69.87  ?  107 ASP   A OD1 1 
ATOM   607  O  OD2 . ASP   A 1 75  ? -34.016 -46.775 11.372  1.00 58.62  ?  107 ASP   A OD2 1 
ATOM   608  N  N   . THR   A 1 76  ? -38.069 -48.003 8.724   1.00 70.08  ?  108 THR   A N   1 
ATOM   609  C  CA  . THR   A 1 76  ? -39.322 -47.360 9.103   1.00 55.80  ?  108 THR   A CA  1 
ATOM   610  C  C   . THR   A 1 76  ? -39.610 -47.527 10.583  1.00 59.99  ?  108 THR   A C   1 
ATOM   611  O  O   . THR   A 1 76  ? -39.715 -48.649 11.082  1.00 67.87  ?  108 THR   A O   1 
ATOM   612  C  CB  . THR   A 1 76  ? -40.458 -47.951 8.315   1.00 50.68  ?  108 THR   A CB  1 
ATOM   613  O  OG1 . THR   A 1 76  ? -40.323 -47.572 6.955   1.00 58.78  ?  108 THR   A OG1 1 
ATOM   614  C  CG2 . THR   A 1 76  ? -41.758 -47.435 8.818   1.00 58.97  ?  108 THR   A CG2 1 
ATOM   615  N  N   . PHE   A 1 77  ? -39.797 -46.417 11.275  1.00 50.55  ?  109 PHE   A N   1 
ATOM   616  C  CA  . PHE   A 1 77  ? -39.983 -46.439 12.700  1.00 49.84  ?  109 PHE   A CA  1 
ATOM   617  C  C   . PHE   A 1 77  ? -41.050 -45.423 13.043  1.00 51.27  ?  109 PHE   A C   1 
ATOM   618  O  O   . PHE   A 1 77  ? -41.612 -44.789 12.160  1.00 53.61  ?  109 PHE   A O   1 
ATOM   619  C  CB  . PHE   A 1 77  ? -38.675 -46.144 13.399  1.00 56.38  ?  109 PHE   A CB  1 
ATOM   620  C  CG  . PHE   A 1 77  ? -38.217 -44.737 13.246  1.00 54.73  ?  109 PHE   A CG  1 
ATOM   621  C  CD1 . PHE   A 1 77  ? -38.566 -43.791 14.157  1.00 48.36  ?  109 PHE   A CD1 1 
ATOM   622  C  CD2 . PHE   A 1 77  ? -37.418 -44.367 12.210  1.00 52.62  ?  109 PHE   A CD2 1 
ATOM   623  C  CE1 . PHE   A 1 77  ? -38.141 -42.520 14.020  1.00 46.32  ?  109 PHE   A CE1 1 
ATOM   624  C  CE2 . PHE   A 1 77  ? -37.004 -43.098 12.102  1.00 48.19  ?  109 PHE   A CE2 1 
ATOM   625  C  CZ  . PHE   A 1 77  ? -37.369 -42.188 13.004  1.00 42.26  ?  109 PHE   A CZ  1 
ATOM   626  N  N   . LEU   A 1 78  ? -41.331 -45.256 14.331  1.00 50.65  ?  110 LEU   A N   1 
ATOM   627  C  CA  . LEU   A 1 78  ? -42.344 -44.333 14.798  1.00 47.71  ?  110 LEU   A CA  1 
ATOM   628  C  C   . LEU   A 1 78  ? -41.785 -43.558 15.962  1.00 54.42  ?  110 LEU   A C   1 
ATOM   629  O  O   . LEU   A 1 78  ? -40.936 -44.063 16.694  1.00 56.33  ?  110 LEU   A O   1 
ATOM   630  C  CB  . LEU   A 1 78  ? -43.590 -45.019 15.264  1.00 57.65  ?  110 LEU   A CB  1 
ATOM   631  C  CG  . LEU   A 1 78  ? -44.582 -45.536 14.243  1.00 61.70  ?  110 LEU   A CG  1 
ATOM   632  C  CD1 . LEU   A 1 78  ? -44.279 -46.916 13.781  1.00 59.18  ?  110 LEU   A CD1 1 
ATOM   633  C  CD2 . LEU   A 1 78  ? -45.912 -45.484 14.896  1.00 73.77  ?  110 LEU   A CD2 1 
ATOM   634  N  N   . SER   A 1 79  ? -42.286 -42.338 16.138  1.00 55.54  ?  111 SER   A N   1 
ATOM   635  C  CA  . SER   A 1 79  ? -41.791 -41.418 17.149  1.00 56.58  ?  111 SER   A CA  1 
ATOM   636  C  C   . SER   A 1 79  ? -42.786 -40.286 17.283  1.00 53.02  ?  111 SER   A C   1 
ATOM   637  O  O   . SER   A 1 79  ? -43.623 -40.067 16.416  1.00 44.93  ?  111 SER   A O   1 
ATOM   638  C  CB  . SER   A 1 79  ? -40.406 -40.861 16.808  1.00 55.41  ?  111 SER   A CB  1 
ATOM   639  O  OG  . SER   A 1 79  ? -39.887 -40.103 17.893  1.00 69.04  ?  111 SER   A OG  1 
ATOM   640  N  N   . GLN   A 1 80  ? -42.663 -39.554 18.369  1.00 60.05  ?  112 GLN   A N   1 
ATOM   641  C  CA  . GLN   A 1 80  ? -43.715 -38.666 18.810  1.00 58.35  ?  112 GLN   A CA  1 
ATOM   642  C  C   . GLN   A 1 80  ? -43.390 -37.278 18.336  1.00 56.37  ?  112 GLN   A C   1 
ATOM   643  O  O   . GLN   A 1 80  ? -42.236 -36.857 18.392  1.00 70.46  ?  112 GLN   A O   1 
ATOM   644  C  CB  . GLN   A 1 80  ? -43.849 -38.655 20.337  1.00 74.67  ?  112 GLN   A CB  1 
ATOM   645  C  CG  . GLN   A 1 80  ? -43.184 -39.834 21.077  1.00 92.36  ?  112 GLN   A CG  1 
ATOM   646  C  CD  . GLN   A 1 80  ? -43.259 -39.729 22.609  1.00 99.70  ?  112 GLN   A CD  1 
ATOM   647  O  OE1 . GLN   A 1 80  ? -44.109 -39.028 23.159  1.00 98.36  ?  112 GLN   A OE1 1 
ATOM   648  N  NE2 . GLN   A 1 80  ? -42.354 -40.426 23.295  1.00 91.24  ?  112 GLN   A NE2 1 
ATOM   649  N  N   . THR   A 1 81  ? -44.407 -36.563 17.895  1.00 48.70  ?  113 THR   A N   1 
ATOM   650  C  CA  . THR   A 1 81  ? -44.271 -35.219 17.378  1.00 52.47  ?  113 THR   A CA  1 
ATOM   651  C  C   . THR   A 1 81  ? -45.429 -34.389 17.855  1.00 55.66  ?  113 THR   A C   1 
ATOM   652  O  O   . THR   A 1 81  ? -46.463 -34.932 18.262  1.00 68.27  ?  113 THR   A O   1 
ATOM   653  C  CB  . THR   A 1 81  ? -44.315 -35.175 15.857  1.00 60.25  ?  113 THR   A CB  1 
ATOM   654  O  OG1 . THR   A 1 81  ? -45.683 -35.260 15.477  1.00 63.27  ?  113 THR   A OG1 1 
ATOM   655  C  CG2 . THR   A 1 81  ? -43.573 -36.314 15.270  1.00 55.91  ?  113 THR   A CG2 1 
ATOM   656  N  N   . PRO   A 1 82  ? -45.332 -33.102 17.784  1.00 56.41  ?  114 PRO   A N   1 
ATOM   657  C  CA  . PRO   A 1 82  ? -46.482 -32.268 18.081  1.00 62.98  ?  114 PRO   A CA  1 
ATOM   658  C  C   . PRO   A 1 82  ? -47.782 -32.926 17.681  1.00 68.29  ?  114 PRO   A C   1 
ATOM   659  O  O   . PRO   A 1 82  ? -48.522 -33.395 18.547  1.00 79.56  ?  114 PRO   A O   1 
ATOM   660  C  CB  . PRO   A 1 82  ? -46.195 -30.998 17.273  1.00 73.03  ?  114 PRO   A CB  1 
ATOM   661  C  CG  . PRO   A 1 82  ? -44.711 -30.908 17.241  1.00 60.88  ?  114 PRO   A CG  1 
ATOM   662  C  CD  . PRO   A 1 82  ? -44.135 -32.274 17.588  1.00 58.40  ?  114 PRO   A CD  1 
ATOM   663  N  N   . TYR   A 1 83  ? -48.041 -33.039 16.414  1.00 67.35  ?  115 TYR   A N   1 
ATOM   664  C  CA  . TYR   A 1 83  ? -49.322 -33.564 15.979  1.00 71.71  ?  115 TYR   A CA  1 
ATOM   665  C  C   . TYR   A 1 83  ? -49.561 -35.090 16.323  1.00 67.36  ?  115 TYR   A C   1 
ATOM   666  O  O   . TYR   A 1 83  ? -50.493 -35.683 15.787  1.00 71.57  ?  115 TYR   A O   1 
ATOM   667  C  CB  . TYR   A 1 83  ? -49.434 -33.321 14.486  1.00 70.91  ?  115 TYR   A CB  1 
ATOM   668  C  CG  . TYR   A 1 83  ? -49.239 -31.886 14.107  1.00 62.74  ?  115 TYR   A CG  1 
ATOM   669  C  CD1 . TYR   A 1 83  ? -49.935 -30.885 14.736  1.00 71.70  ?  115 TYR   A CD1 1 
ATOM   670  C  CD2 . TYR   A 1 83  ? -48.353 -31.534 13.124  1.00 66.09  ?  115 TYR   A CD2 1 
ATOM   671  C  CE1 . TYR   A 1 83  ? -49.758 -29.570 14.379  1.00 71.70  ?  115 TYR   A CE1 1 
ATOM   672  C  CE2 . TYR   A 1 83  ? -48.168 -30.230 12.774  1.00 68.94  ?  115 TYR   A CE2 1 
ATOM   673  C  CZ  . TYR   A 1 83  ? -48.873 -29.259 13.403  1.00 59.53  ?  115 TYR   A CZ  1 
ATOM   674  O  OH  . TYR   A 1 83  ? -48.694 -27.962 13.039  1.00 64.08  ?  115 TYR   A OH  1 
ATOM   675  N  N   . GLY   A 1 84  ? -48.800 -35.754 17.175  1.00 55.63  ?  116 GLY   A N   1 
ATOM   676  C  CA  . GLY   A 1 84  ? -49.029 -37.137 17.513  1.00 56.98  ?  116 GLY   A CA  1 
ATOM   677  C  C   . GLY   A 1 84  ? -47.851 -38.000 17.131  1.00 64.08  ?  116 GLY   A C   1 
ATOM   678  O  O   . GLY   A 1 84  ? -46.777 -37.517 16.781  1.00 73.84  ?  116 GLY   A O   1 
ATOM   679  N  N   . TYR   A 1 85  ? -48.058 -39.300 17.225  1.00 64.40  ?  117 TYR   A N   1 
ATOM   680  C  CA  . TYR   A 1 85  ? -47.107 -40.283 16.748  1.00 61.29  ?  117 TYR   A CA  1 
ATOM   681  C  C   . TYR   A 1 85  ? -47.140 -40.357 15.227  1.00 60.34  ?  117 TYR   A C   1 
ATOM   682  O  O   . TYR   A 1 85  ? -48.212 -40.289 14.627  1.00 53.18  ?  117 TYR   A O   1 
ATOM   683  C  CB  . TYR   A 1 85  ? -47.469 -41.642 17.328  1.00 74.53  ?  117 TYR   A CB  1 
ATOM   684  C  CG  . TYR   A 1 85  ? -46.533 -42.126 18.388  1.00 83.48  ?  117 TYR   A CG  1 
ATOM   685  C  CD1 . TYR   A 1 85  ? -45.412 -42.876 18.052  1.00 80.46  ?  117 TYR   A CD1 1 
ATOM   686  C  CD2 . TYR   A 1 85  ? -46.765 -41.840 19.728  1.00 76.27  ?  117 TYR   A CD2 1 
ATOM   687  C  CE1 . TYR   A 1 85  ? -44.536 -43.319 19.016  1.00 79.91  ?  117 TYR   A CE1 1 
ATOM   688  C  CE2 . TYR   A 1 85  ? -45.890 -42.282 20.707  1.00 82.21  ?  117 TYR   A CE2 1 
ATOM   689  C  CZ  . TYR   A 1 85  ? -44.770 -43.028 20.343  1.00 81.94  ?  117 TYR   A CZ  1 
ATOM   690  O  OH  . TYR   A 1 85  ? -43.871 -43.492 21.289  1.00 73.71  ?  117 TYR   A OH  1 
ATOM   691  N  N   . ARG   A 1 86  ? -45.971 -40.500 14.594  1.00 55.01  ?  118 ARG   A N   1 
ATOM   692  C  CA  . ARG   A 1 86  ? -45.910 -40.529 13.142  1.00 44.25  ?  118 ARG   A CA  1 
ATOM   693  C  C   . ARG   A 1 86  ? -44.846 -41.489 12.663  1.00 39.97  ?  118 ARG   A C   1 
ATOM   694  O  O   . ARG   A 1 86  ? -43.968 -41.886 13.409  1.00 44.27  ?  118 ARG   A O   1 
ATOM   695  C  CB  . ARG   A 1 86  ? -45.647 -39.160 12.589  1.00 39.72  ?  118 ARG   A CB  1 
ATOM   696  C  CG  . ARG   A 1 86  ? -46.758 -38.275 12.850  1.00 49.15  ?  118 ARG   A CG  1 
ATOM   697  C  CD  . ARG   A 1 86  ? -47.140 -37.464 11.660  1.00 54.04  ?  118 ARG   A CD  1 
ATOM   698  N  NE  . ARG   A 1 86  ? -48.423 -36.839 11.917  1.00 59.19  ?  118 ARG   A NE  1 
ATOM   699  C  CZ  . ARG   A 1 86  ? -49.032 -36.019 11.086  1.00 76.58  ?  118 ARG   A CZ  1 
ATOM   700  N  NH1 . ARG   A 1 86  ? -48.468 -35.714 9.919   1.00 74.69  ?  118 ARG   A NH1 1 
ATOM   701  N  NH2 . ARG   A 1 86  ? -50.207 -35.511 11.434  1.00 74.51  ?  118 ARG   A NH2 1 
ATOM   702  N  N   . SER   A 1 87  ? -44.916 -41.822 11.385  1.00 38.00  ?  119 SER   A N   1 
ATOM   703  C  CA  . SER   A 1 87  ? -44.087 -42.843 10.775  1.00 40.41  ?  119 SER   A CA  1 
ATOM   704  C  C   . SER   A 1 87  ? -42.959 -42.186 9.996   1.00 48.07  ?  119 SER   A C   1 
ATOM   705  O  O   . SER   A 1 87  ? -43.214 -41.329 9.153   1.00 58.53  ?  119 SER   A O   1 
ATOM   706  C  CB  . SER   A 1 87  ? -44.953 -43.699 9.860   1.00 58.10  ?  119 SER   A CB  1 
ATOM   707  O  OG  . SER   A 1 87  ? -44.265 -44.791 9.303   1.00 63.47  ?  119 SER   A OG  1 
ATOM   708  N  N   . PHE   A 1 88  ? -41.716 -42.568 10.289  1.00 50.15  ?  120 PHE   A N   1 
ATOM   709  C  CA  . PHE   A 1 88  ? -40.542 -42.079 9.582   1.00 46.35  ?  120 PHE   A CA  1 
ATOM   710  C  C   . PHE   A 1 88  ? -39.833 -43.255 8.936   1.00 45.60  ?  120 PHE   A C   1 
ATOM   711  O  O   . PHE   A 1 88  ? -40.086 -44.397 9.274   1.00 50.86  ?  120 PHE   A O   1 
ATOM   712  C  CB  . PHE   A 1 88  ? -39.572 -41.357 10.513  1.00 41.03  ?  120 PHE   A CB  1 
ATOM   713  C  CG  . PHE   A 1 88  ? -40.144 -40.171 11.184  1.00 39.16  ?  120 PHE   A CG  1 
ATOM   714  C  CD1 . PHE   A 1 88  ? -40.900 -40.301 12.290  1.00 39.55  ?  120 PHE   A CD1 1 
ATOM   715  C  CD2 . PHE   A 1 88  ? -39.904 -38.920 10.721  1.00 45.19  ?  120 PHE   A CD2 1 
ATOM   716  C  CE1 . PHE   A 1 88  ? -41.411 -39.213 12.900  1.00 37.40  ?  120 PHE   A CE1 1 
ATOM   717  C  CE2 . PHE   A 1 88  ? -40.427 -37.840 11.356  1.00 41.47  ?  120 PHE   A CE2 1 
ATOM   718  C  CZ  . PHE   A 1 88  ? -41.173 -38.001 12.432  1.00 34.42  ?  120 PHE   A CZ  1 
ATOM   719  N  N   . SER   A 1 89  ? -38.921 -42.978 8.016   1.00 51.39  ?  121 SER   A N   1 
ATOM   720  C  CA  . SER   A 1 89  ? -38.239 -44.057 7.302   1.00 50.77  ?  121 SER   A CA  1 
ATOM   721  C  C   . SER   A 1 89  ? -36.855 -43.579 6.872   1.00 46.81  ?  121 SER   A C   1 
ATOM   722  O  O   . SER   A 1 89  ? -36.696 -43.059 5.773   1.00 48.91  ?  121 SER   A O   1 
ATOM   723  C  CB  . SER   A 1 89  ? -39.052 -44.505 6.107   1.00 52.85  ?  121 SER   A CB  1 
ATOM   724  O  OG  . SER   A 1 89  ? -40.403 -44.579 6.477   1.00 61.00  ?  121 SER   A OG  1 
ATOM   725  N  N   . ASN   A 1 90  ? -35.872 -43.761 7.747   1.00 47.44  ?  122 ASN   A N   1 
ATOM   726  C  CA  . ASN   A 1 90  ? -34.479 -43.597 7.366   1.00 40.91  ?  122 ASN   A CA  1 
ATOM   727  C  C   . ASN   A 1 90  ? -34.116 -44.581 6.269   1.00 43.20  ?  122 ASN   A C   1 
ATOM   728  O  O   . ASN   A 1 90  ? -34.602 -45.699 6.242   1.00 51.50  ?  122 ASN   A O   1 
ATOM   729  C  CB  . ASN   A 1 90  ? -33.569 -43.828 8.560   1.00 41.28  ?  122 ASN   A CB  1 
ATOM   730  C  CG  . ASN   A 1 90  ? -33.709 -42.771 9.607   1.00 41.18  ?  122 ASN   A CG  1 
ATOM   731  O  OD1 . ASN   A 1 90  ? -34.161 -41.697 9.333   1.00 49.55  ?  122 ASN   A OD1 1 
ATOM   732  N  ND2 . ASN   A 1 90  ? -33.325 -43.068 10.804  1.00 40.06  ?  122 ASN   A ND2 1 
ATOM   733  N  N   . ILE   A 1 91  ? -33.238 -44.158 5.365   1.00 53.26  ?  123 ILE   A N   1 
ATOM   734  C  CA  . ILE   A 1 91  ? -32.696 -44.993 4.295   1.00 48.24  ?  123 ILE   A CA  1 
ATOM   735  C  C   . ILE   A 1 91  ? -31.225 -45.214 4.574   1.00 48.55  ?  123 ILE   A C   1 
ATOM   736  O  O   . ILE   A 1 91  ? -30.487 -44.253 4.767   1.00 54.17  ?  123 ILE   A O   1 
ATOM   737  C  CB  . ILE   A 1 91  ? -32.830 -44.330 2.924   1.00 39.82  ?  123 ILE   A CB  1 
ATOM   738  C  CG1 . ILE   A 1 91  ? -34.196 -43.734 2.746   1.00 51.47  ?  123 ILE   A CG1 1 
ATOM   739  C  CG2 . ILE   A 1 91  ? -32.573 -45.325 1.873   1.00 48.54  ?  123 ILE   A CG2 1 
ATOM   740  C  CD1 . ILE   A 1 91  ? -34.339 -42.931 1.489   1.00 49.37  ?  123 ILE   A CD1 1 
ATOM   741  N  N   . ILE   A 1 92  ? -30.784 -46.457 4.547   1.00 49.68  ?  124 ILE   A N   1 
ATOM   742  C  CA  . ILE   A 1 92  ? -29.406 -46.786 4.852   1.00 47.42  ?  124 ILE   A CA  1 
ATOM   743  C  C   . ILE   A 1 92  ? -28.868 -47.687 3.762   1.00 56.60  ?  124 ILE   A C   1 
ATOM   744  O  O   . ILE   A 1 92  ? -29.453 -48.731 3.473   1.00 72.41  ?  124 ILE   A O   1 
ATOM   745  C  CB  . ILE   A 1 92  ? -29.294 -47.446 6.215   1.00 48.00  ?  124 ILE   A CB  1 
ATOM   746  C  CG1 . ILE   A 1 92  ? -29.760 -46.449 7.249   1.00 47.55  ?  124 ILE   A CG1 1 
ATOM   747  C  CG2 . ILE   A 1 92  ? -27.902 -47.836 6.454   1.00 53.08  ?  124 ILE   A CG2 1 
ATOM   748  C  CD1 . ILE   A 1 92  ? -29.907 -46.989 8.584   1.00 60.62  ?  124 ILE   A CD1 1 
ATOM   749  N  N   . SER   A 1 93  ? -27.765 -47.283 3.152   1.00 49.90  ?  125 SER   A N   1 
ATOM   750  C  CA  . SER   A 1 93  ? -27.148 -48.003 2.054   1.00 46.90  ?  125 SER   A CA  1 
ATOM   751  C  C   . SER   A 1 93  ? -25.726 -48.291 2.480   1.00 51.67  ?  125 SER   A C   1 
ATOM   752  O  O   . SER   A 1 93  ? -24.977 -47.366 2.768   1.00 50.00  ?  125 SER   A O   1 
ATOM   753  C  CB  . SER   A 1 93  ? -27.174 -47.175 0.783   1.00 50.11  ?  125 SER   A CB  1 
ATOM   754  O  OG  . SER   A 1 93  ? -26.749 -47.917 -0.331  1.00 61.44  ?  125 SER   A OG  1 
ATOM   755  N  N   . THR   A 1 94  ? -25.364 -49.558 2.564   1.00 63.30  ?  126 THR   A N   1 
ATOM   756  C  CA  . THR   A 1 94  ? -24.081 -49.947 3.122   1.00 54.71  ?  126 THR   A CA  1 
ATOM   757  C  C   . THR   A 1 94  ? -23.340 -50.885 2.191   1.00 59.76  ?  126 THR   A C   1 
ATOM   758  O  O   . THR   A 1 94  ? -23.944 -51.694 1.487   1.00 67.54  ?  126 THR   A O   1 
ATOM   759  C  CB  . THR   A 1 94  ? -24.278 -50.606 4.420   1.00 50.91  ?  126 THR   A CB  1 
ATOM   760  O  OG1 . THR   A 1 94  ? -24.912 -49.680 5.298   1.00 52.06  ?  126 THR   A OG1 1 
ATOM   761  C  CG2 . THR   A 1 94  ? -22.995 -50.990 4.996   1.00 51.95  ?  126 THR   A CG2 1 
ATOM   762  N  N   . LEU   A 1 95  ? -22.023 -50.746 2.184   1.00 61.24  ?  127 LEU   A N   1 
ATOM   763  C  CA  . LEU   A 1 95  ? -21.125 -51.650 1.490   1.00 63.62  ?  127 LEU   A CA  1 
ATOM   764  C  C   . LEU   A 1 95  ? -20.321 -52.414 2.529   1.00 72.53  ?  127 LEU   A C   1 
ATOM   765  O  O   . LEU   A 1 95  ? -19.824 -51.828 3.502   1.00 58.94  ?  127 LEU   A O   1 
ATOM   766  C  CB  . LEU   A 1 95  ? -20.174 -50.909 0.563   1.00 62.78  ?  127 LEU   A CB  1 
ATOM   767  C  CG  . LEU   A 1 95  ? -20.586 -50.552 -0.860  1.00 61.31  ?  127 LEU   A CG  1 
ATOM   768  C  CD1 . LEU   A 1 95  ? -19.538 -49.722 -1.467  1.00 58.35  ?  127 LEU   A CD1 1 
ATOM   769  C  CD2 . LEU   A 1 95  ? -20.791 -51.737 -1.743  1.00 71.38  ?  127 LEU   A CD2 1 
ATOM   770  N  N   . ASN   A 1 96  ? -20.204 -53.726 2.325   1.00 78.51  ?  128 ASN   A N   1 
ATOM   771  C  CA  . ASN   A 1 96  ? -19.477 -54.554 3.272   1.00 75.09  ?  128 ASN   A CA  1 
ATOM   772  C  C   . ASN   A 1 96  ? -19.985 -54.271 4.675   1.00 72.83  ?  128 ASN   A C   1 
ATOM   773  O  O   . ASN   A 1 96  ? -19.276 -53.650 5.476   1.00 71.87  ?  128 ASN   A O   1 
ATOM   774  C  CB  . ASN   A 1 96  ? -17.981 -54.280 3.175   1.00 64.57  ?  128 ASN   A CB  1 
ATOM   775  C  CG  . ASN   A 1 96  ? -17.436 -54.598 1.810   1.00 84.16  ?  128 ASN   A CG  1 
ATOM   776  O  OD1 . ASN   A 1 96  ? -17.965 -54.153 0.792   1.00 76.49  ?  128 ASN   A OD1 1 
ATOM   777  N  ND2 . ASN   A 1 96  ? -16.390 -55.405 1.773   1.00 106.10 ?  128 ASN   A ND2 1 
ATOM   778  N  N   . PRO   A 1 97  ? -21.218 -54.680 4.993   1.00 62.92  ?  129 PRO   A N   1 
ATOM   779  C  CA  . PRO   A 1 97  ? -21.740 -54.457 6.339   1.00 55.51  ?  129 PRO   A CA  1 
ATOM   780  C  C   . PRO   A 1 97  ? -21.154 -55.384 7.341   1.00 63.17  ?  129 PRO   A C   1 
ATOM   781  O  O   . PRO   A 1 97  ? -21.171 -55.062 8.540   1.00 62.11  ?  129 PRO   A O   1 
ATOM   782  C  CB  . PRO   A 1 97  ? -23.227 -54.724 6.190   1.00 53.40  ?  129 PRO   A CB  1 
ATOM   783  C  CG  . PRO   A 1 97  ? -23.351 -55.581 5.033   1.00 58.61  ?  129 PRO   A CG  1 
ATOM   784  C  CD  . PRO   A 1 97  ? -22.170 -55.407 4.149   1.00 62.63  ?  129 PRO   A CD  1 
ATOM   785  N  N   . THR   A 1 98  ? -20.703 -56.551 6.878   1.00 70.63  ?  130 THR   A N   1 
ATOM   786  C  CA  . THR   A 1 98  ? -19.996 -57.495 7.728   1.00 72.40  ?  130 THR   A CA  1 
ATOM   787  C  C   . THR   A 1 98  ? -18.839 -56.827 8.435   1.00 77.31  ?  130 THR   A C   1 
ATOM   788  O  O   . THR   A 1 98  ? -18.531 -57.171 9.583   1.00 66.62  ?  130 THR   A O   1 
ATOM   789  C  CB  . THR   A 1 98  ? -19.494 -58.683 6.899   1.00 74.00  ?  130 THR   A CB  1 
ATOM   790  O  OG1 . THR   A 1 98  ? -18.449 -59.347 7.618   1.00 86.29  ?  130 THR   A OG1 1 
ATOM   791  C  CG2 . THR   A 1 98  ? -18.960 -58.271 5.511   1.00 65.30  ?  130 THR   A CG2 1 
ATOM   792  N  N   . ALA   A 1 99  ? -18.231 -55.838 7.778   1.00 77.67  ?  131 ALA   A N   1 
ATOM   793  C  CA  . ALA   A 1 99  ? -16.992 -55.207 8.196   1.00 75.17  ?  131 ALA   A CA  1 
ATOM   794  C  C   . ALA   A 1 99  ? -17.182 -54.375 9.454   1.00 69.30  ?  131 ALA   A C   1 
ATOM   795  O  O   . ALA   A 1 99  ? -18.290 -54.013 9.830   1.00 78.48  ?  131 ALA   A O   1 
ATOM   796  C  CB  . ALA   A 1 99  ? -16.471 -54.327 7.077   1.00 70.74  ?  131 ALA   A CB  1 
ATOM   797  N  N   . LYS   A 1 100 ? -16.077 -54.044 10.097  1.00 56.42  ?  132 LYS   A N   1 
ATOM   798  C  CA  . LYS   A 1 100 ? -16.170 -53.482 11.428  1.00 63.90  ?  132 LYS   A CA  1 
ATOM   799  C  C   . LYS   A 1 100 ? -16.183 -51.977 11.407  1.00 65.31  ?  132 LYS   A C   1 
ATOM   800  O  O   . LYS   A 1 100 ? -16.796 -51.356 12.276  1.00 65.32  ?  132 LYS   A O   1 
ATOM   801  C  CB  . LYS   A 1 100 ? -15.002 -53.968 12.290  1.00 74.91  ?  132 LYS   A CB  1 
ATOM   802  C  CG  . LYS   A 1 100 ? -14.487 -55.344 11.913  1.00 74.79  ?  132 LYS   A CG  1 
ATOM   803  C  CD  . LYS   A 1 100 ? -13.284 -55.776 12.738  1.00 76.81  ?  132 LYS   A CD  1 
ATOM   804  C  CE  . LYS   A 1 100 ? -12.140 -56.323 11.850  1.00 79.87  ?  132 LYS   A CE  1 
ATOM   805  N  NZ  . LYS   A 1 100 ? -11.706 -57.719 12.192  1.00 72.25  ?  132 LYS   A NZ  1 
ATOM   806  N  N   . ARG   A 1 101 ? -15.532 -51.381 10.419  1.00 75.12  ?  133 ARG   A N   1 
ATOM   807  C  CA  . ARG   A 1 101 ? -15.272 -49.953 10.391  1.00 73.23  ?  133 ARG   A CA  1 
ATOM   808  C  C   . ARG   A 1 101 ? -15.895 -49.347 9.151   1.00 61.83  ?  133 ARG   A C   1 
ATOM   809  O  O   . ARG   A 1 101 ? -15.728 -49.868 8.051   1.00 55.91  ?  133 ARG   A O   1 
ATOM   810  C  CB  . ARG   A 1 101 ? -13.774 -49.682 10.423  1.00 64.49  ?  133 ARG   A CB  1 
ATOM   811  C  CG  . ARG   A 1 101 ? -13.238 -49.646 11.811  1.00 72.96  ?  133 ARG   A CG  1 
ATOM   812  C  CD  . ARG   A 1 101 ? -12.021 -48.820 11.868  1.00 78.62  ?  133 ARG   A CD  1 
ATOM   813  N  NE  . ARG   A 1 101 ? -11.037 -49.299 10.911  1.00 72.84  ?  133 ARG   A NE  1 
ATOM   814  C  CZ  . ARG   A 1 101 ? -10.160 -48.516 10.294  1.00 67.09  ?  133 ARG   A CZ  1 
ATOM   815  N  NH1 . ARG   A 1 101 ? -10.152 -47.221 10.521  1.00 69.51  ?  133 ARG   A NH1 1 
ATOM   816  N  NH2 . ARG   A 1 101 ? -9.290  -49.025 9.437   1.00 75.94  ?  133 ARG   A NH2 1 
ATOM   817  N  N   . HIS   A 1 102 ? -16.621 -48.264 9.327   1.00 62.82  ?  134 HIS   A N   1 
ATOM   818  C  CA  . HIS   A 1 102 ? -17.232 -47.606 8.194   1.00 63.08  ?  134 HIS   A CA  1 
ATOM   819  C  C   . HIS   A 1 102 ? -17.000 -46.100 8.258   1.00 59.42  ?  134 HIS   A C   1 
ATOM   820  O  O   . HIS   A 1 102 ? -17.129 -45.477 9.311   1.00 53.01  ?  134 HIS   A O   1 
ATOM   821  C  CB  . HIS   A 1 102 ? -18.715 -47.944 8.138   1.00 61.83  ?  134 HIS   A CB  1 
ATOM   822  C  CG  . HIS   A 1 102 ? -19.005 -49.273 7.517   1.00 59.74  ?  134 HIS   A CG  1 
ATOM   823  N  ND1 . HIS   A 1 102 ? -19.025 -50.442 8.240   1.00 63.18  ?  134 HIS   A ND1 1 
ATOM   824  C  CD2 . HIS   A 1 102 ? -19.286 -49.617 6.240   1.00 60.92  ?  134 HIS   A CD2 1 
ATOM   825  C  CE1 . HIS   A 1 102 ? -19.301 -51.450 7.432   1.00 60.68  ?  134 HIS   A CE1 1 
ATOM   826  N  NE2 . HIS   A 1 102 ? -19.464 -50.976 6.211   1.00 55.36  ?  134 HIS   A NE2 1 
ATOM   827  N  N   . LEU   A 1 103 ? -16.617 -45.533 7.124   1.00 55.94  ?  135 LEU   A N   1 
ATOM   828  C  CA  . LEU   A 1 103 ? -16.745 -44.107 6.910   1.00 54.18  ?  135 LEU   A CA  1 
ATOM   829  C  C   . LEU   A 1 103 ? -18.163 -43.870 6.449   1.00 54.06  ?  135 LEU   A C   1 
ATOM   830  O  O   . LEU   A 1 103 ? -18.624 -44.545 5.526   1.00 44.54  ?  135 LEU   A O   1 
ATOM   831  C  CB  . LEU   A 1 103 ? -15.769 -43.610 5.842   1.00 55.92  ?  135 LEU   A CB  1 
ATOM   832  C  CG  . LEU   A 1 103 ? -15.976 -42.173 5.340   1.00 49.42  ?  135 LEU   A CG  1 
ATOM   833  C  CD1 . LEU   A 1 103 ? -15.383 -41.142 6.269   1.00 46.63  ?  135 LEU   A CD1 1 
ATOM   834  C  CD2 . LEU   A 1 103 ? -15.415 -42.027 4.019   1.00 36.86  ?  135 LEU   A CD2 1 
ATOM   835  N  N   . VAL   A 1 104 ? -18.846 -42.917 7.081   1.00 54.11  ?  136 VAL   A N   1 
ATOM   836  C  CA  . VAL   A 1 104 ? -20.258 -42.661 6.837   1.00 55.02  ?  136 VAL   A CA  1 
ATOM   837  C  C   . VAL   A 1 104 ? -20.425 -41.268 6.255   1.00 44.73  ?  136 VAL   A C   1 
ATOM   838  O  O   . VAL   A 1 104 ? -19.942 -40.290 6.830   1.00 41.98  ?  136 VAL   A O   1 
ATOM   839  C  CB  . VAL   A 1 104 ? -21.081 -42.790 8.129   1.00 57.75  ?  136 VAL   A CB  1 
ATOM   840  C  CG1 . VAL   A 1 104 ? -22.499 -42.771 7.815   1.00 57.44  ?  136 VAL   A CG1 1 
ATOM   841  C  CG2 . VAL   A 1 104 ? -20.783 -44.058 8.819   1.00 59.42  ?  136 VAL   A CG2 1 
ATOM   842  N  N   . LEU   A 1 105 ? -21.147 -41.180 5.154   1.00 35.55  ?  137 LEU   A N   1 
ATOM   843  C  CA  . LEU   A 1 105 ? -21.648 -39.930 4.620   1.00 40.87  ?  137 LEU   A CA  1 
ATOM   844  C  C   . LEU   A 1 105 ? -23.143 -39.845 4.891   1.00 45.75  ?  137 LEU   A C   1 
ATOM   845  O  O   . LEU   A 1 105 ? -23.828 -40.862 4.931   1.00 45.67  ?  137 LEU   A O   1 
ATOM   846  C  CB  . LEU   A 1 105 ? -21.402 -39.861 3.125   1.00 48.82  ?  137 LEU   A CB  1 
ATOM   847  C  CG  . LEU   A 1 105 ? -19.980 -39.880 2.588   1.00 51.20  ?  137 LEU   A CG  1 
ATOM   848  C  CD1 . LEU   A 1 105 ? -20.013 -40.042 1.109   1.00 61.60  ?  137 LEU   A CD1 1 
ATOM   849  C  CD2 . LEU   A 1 105 ? -19.307 -38.638 2.862   1.00 50.57  ?  137 LEU   A CD2 1 
ATOM   850  N  N   . ALA   A 1 106 ? -23.662 -38.633 5.076   1.00 42.69  ?  138 ALA   A N   1 
ATOM   851  C  CA  . ALA   A 1 106 ? -25.064 -38.528 5.452   1.00 46.39  ?  138 ALA   A CA  1 
ATOM   852  C  C   . ALA   A 1 106 ? -25.637 -37.169 5.124   1.00 45.40  ?  138 ALA   A C   1 
ATOM   853  O  O   . ALA   A 1 106 ? -24.933 -36.171 5.166   1.00 55.22  ?  138 ALA   A O   1 
ATOM   854  C  CB  . ALA   A 1 106 ? -25.250 -38.765 6.942   1.00 47.95  ?  138 ALA   A CB  1 
ATOM   855  N  N   . CYS   A 1 107 ? -26.941 -37.143 4.868   1.00 42.41  ?  139 CYS   A N   1 
ATOM   856  C  CA  . CYS   A 1 107 ? -27.752 -35.936 4.838   1.00 36.28  ?  139 CYS   A CA  1 
ATOM   857  C  C   . CYS   A 1 107 ? -29.158 -36.306 5.263   1.00 37.49  ?  139 CYS   A C   1 
ATOM   858  O  O   . CYS   A 1 107 ? -29.415 -37.442 5.657   1.00 34.82  ?  139 CYS   A O   1 
ATOM   859  C  CB  . CYS   A 1 107 ? -27.752 -35.332 3.445   1.00 47.86  ?  139 CYS   A CB  1 
ATOM   860  S  SG  . CYS   A 1 107 ? -28.570 -36.360 2.292   1.00 35.94  ?  139 CYS   A SG  1 
ATOM   861  N  N   . HIS   A 1 108 ? -30.091 -35.367 5.157   1.00 40.17  ?  140 HIS   A N   1 
ATOM   862  C  CA  . HIS   A 1 108 ? -31.494 -35.675 5.392   1.00 38.77  ?  140 HIS   A CA  1 
ATOM   863  C  C   . HIS   A 1 108 ? -32.310 -35.521 4.124   1.00 32.76  ?  140 HIS   A C   1 
ATOM   864  O  O   . HIS   A 1 108 ? -32.115 -34.589 3.356   1.00 35.19  ?  140 HIS   A O   1 
ATOM   865  C  CB  . HIS   A 1 108 ? -32.067 -34.813 6.500   1.00 38.27  ?  140 HIS   A CB  1 
ATOM   866  C  CG  . HIS   A 1 108 ? -32.445 -33.425 6.090   1.00 35.46  ?  140 HIS   A CG  1 
ATOM   867  N  ND1 . HIS   A 1 108 ? -33.718 -33.077 5.716   1.00 35.95  ?  140 HIS   A ND1 1 
ATOM   868  C  CD2 . HIS   A 1 108 ? -31.733 -32.286 6.069   1.00 36.36  ?  140 HIS   A CD2 1 
ATOM   869  C  CE1 . HIS   A 1 108 ? -33.765 -31.791 5.459   1.00 31.70  ?  140 HIS   A CE1 1 
ATOM   870  N  NE2 . HIS   A 1 108 ? -32.571 -31.288 5.662   1.00 27.79  ?  140 HIS   A NE2 1 
ATOM   871  N  N   . TYR   A 1 109 ? -33.222 -36.445 3.898   1.00 35.26  ?  141 TYR   A N   1 
ATOM   872  C  CA  . TYR   A 1 109 ? -34.020 -36.391 2.695   1.00 31.77  ?  141 TYR   A CA  1 
ATOM   873  C  C   . TYR   A 1 109 ? -35.399 -35.859 2.947   1.00 31.28  ?  141 TYR   A C   1 
ATOM   874  O  O   . TYR   A 1 109 ? -36.120 -35.643 1.992   1.00 34.37  ?  141 TYR   A O   1 
ATOM   875  C  CB  . TYR   A 1 109 ? -34.117 -37.750 2.006   1.00 28.04  ?  141 TYR   A CB  1 
ATOM   876  C  CG  . TYR   A 1 109 ? -35.102 -38.765 2.556   1.00 35.46  ?  141 TYR   A CG  1 
ATOM   877  C  CD1 . TYR   A 1 109 ? -34.747 -39.654 3.538   1.00 37.67  ?  141 TYR   A CD1 1 
ATOM   878  C  CD2 . TYR   A 1 109 ? -36.360 -38.873 2.045   1.00 31.92  ?  141 TYR   A CD2 1 
ATOM   879  C  CE1 . TYR   A 1 109 ? -35.630 -40.568 4.005   1.00 35.89  ?  141 TYR   A CE1 1 
ATOM   880  C  CE2 . TYR   A 1 109 ? -37.232 -39.799 2.511   1.00 37.26  ?  141 TYR   A CE2 1 
ATOM   881  C  CZ  . TYR   A 1 109 ? -36.859 -40.642 3.485   1.00 36.41  ?  141 TYR   A CZ  1 
ATOM   882  O  OH  . TYR   A 1 109 ? -37.726 -41.578 3.949   1.00 38.79  ?  141 TYR   A OH  1 
ATOM   883  N  N   . ASP   A 1 110 ? -35.771 -35.587 4.182   1.00 34.54  ?  142 ASP   A N   1 
ATOM   884  C  CA  . ASP   A 1 110 ? -37.066 -34.965 4.356   1.00 41.03  ?  142 ASP   A CA  1 
ATOM   885  C  C   . ASP   A 1 110 ? -36.944 -33.502 4.011   1.00 38.50  ?  142 ASP   A C   1 
ATOM   886  O  O   . ASP   A 1 110 ? -35.855 -32.940 4.012   1.00 42.87  ?  142 ASP   A O   1 
ATOM   887  C  CB  . ASP   A 1 110 ? -37.592 -35.137 5.779   1.00 37.01  ?  142 ASP   A CB  1 
ATOM   888  C  CG  . ASP   A 1 110 ? -36.877 -34.308 6.742   1.00 33.32  ?  142 ASP   A CG  1 
ATOM   889  O  OD1 . ASP   A 1 110 ? -35.710 -34.560 6.925   1.00 32.35  ?  142 ASP   A OD1 1 
ATOM   890  O  OD2 . ASP   A 1 110 ? -37.478 -33.418 7.339   1.00 37.74  ?  142 ASP   A OD2 1 
ATOM   891  N  N   . SER   A 1 111 ? -38.068 -32.891 3.694   1.00 34.28  ?  143 SER   A N   1 
ATOM   892  C  CA  . SER   A 1 111 ? -38.132 -31.458 3.494   1.00 37.25  ?  143 SER   A CA  1 
ATOM   893  C  C   . SER   A 1 111 ? -39.022 -30.850 4.558   1.00 37.27  ?  143 SER   A C   1 
ATOM   894  O  O   . SER   A 1 111 ? -40.021 -31.443 4.930   1.00 35.39  ?  143 SER   A O   1 
ATOM   895  C  CB  . SER   A 1 111 ? -38.665 -31.117 2.116   1.00 39.95  ?  143 SER   A CB  1 
ATOM   896  O  OG  . SER   A 1 111 ? -40.045 -31.372 1.992   1.00 40.42  ?  143 SER   A OG  1 
ATOM   897  N  N   . LYS   A 1 112 ? -38.651 -29.676 5.059   1.00 36.40  ?  144 LYS   A N   1 
ATOM   898  C  CA  . LYS   A 1 112 ? -39.461 -29.012 6.061   1.00 30.69  ?  144 LYS   A CA  1 
ATOM   899  C  C   . LYS   A 1 112 ? -40.878 -28.863 5.571   1.00 36.47  ?  144 LYS   A C   1 
ATOM   900  O  O   . LYS   A 1 112 ? -41.120 -28.690 4.384   1.00 41.48  ?  144 LYS   A O   1 
ATOM   901  C  CB  . LYS   A 1 112 ? -38.914 -27.650 6.385   1.00 32.77  ?  144 LYS   A CB  1 
ATOM   902  C  CG  . LYS   A 1 112 ? -39.306 -27.204 7.722   1.00 46.62  ?  144 LYS   A CG  1 
ATOM   903  C  CD  . LYS   A 1 112 ? -39.136 -25.764 8.015   1.00 39.90  ?  144 LYS   A CD  1 
ATOM   904  C  CE  . LYS   A 1 112 ? -39.403 -25.542 9.484   1.00 44.85  ?  144 LYS   A CE  1 
ATOM   905  N  NZ  . LYS   A 1 112 ? -40.709 -26.123 9.907   1.00 56.50  ?  144 LYS   A NZ  1 
ATOM   906  N  N   . TYR   A 1 113 ? -41.829 -28.940 6.493   1.00 48.02  ?  145 TYR   A N   1 
ATOM   907  C  CA  . TYR   A 1 113 ? -43.223 -28.756 6.136   1.00 50.62  ?  145 TYR   A CA  1 
ATOM   908  C  C   . TYR   A 1 113 ? -43.614 -27.290 6.185   1.00 43.69  ?  145 TYR   A C   1 
ATOM   909  O  O   . TYR   A 1 113 ? -43.317 -26.594 7.153   1.00 38.66  ?  145 TYR   A O   1 
ATOM   910  C  CB  . TYR   A 1 113 ? -44.138 -29.545 7.046   1.00 51.35  ?  145 TYR   A CB  1 
ATOM   911  C  CG  . TYR   A 1 113 ? -45.564 -29.207 6.779   1.00 53.09  ?  145 TYR   A CG  1 
ATOM   912  C  CD1 . TYR   A 1 113 ? -46.114 -29.422 5.546   1.00 58.07  ?  145 TYR   A CD1 1 
ATOM   913  C  CD2 . TYR   A 1 113 ? -46.360 -28.658 7.751   1.00 60.58  ?  145 TYR   A CD2 1 
ATOM   914  C  CE1 . TYR   A 1 113 ? -47.414 -29.093 5.295   1.00 65.74  ?  145 TYR   A CE1 1 
ATOM   915  C  CE2 . TYR   A 1 113 ? -47.661 -28.334 7.502   1.00 59.35  ?  145 TYR   A CE2 1 
ATOM   916  C  CZ  . TYR   A 1 113 ? -48.177 -28.546 6.282   1.00 54.50  ?  145 TYR   A CZ  1 
ATOM   917  O  OH  . TYR   A 1 113 ? -49.476 -28.219 6.048   1.00 70.90  ?  145 TYR   A OH  1 
ATOM   918  N  N   . PHE   A 1 114 ? -44.304 -26.845 5.143   1.00 49.22  ?  146 PHE   A N   1 
ATOM   919  C  CA  . PHE   A 1 114 ? -44.788 -25.487 5.015   1.00 52.95  ?  146 PHE   A CA  1 
ATOM   920  C  C   . PHE   A 1 114 ? -46.149 -25.522 4.366   1.00 56.39  ?  146 PHE   A C   1 
ATOM   921  O  O   . PHE   A 1 114 ? -46.389 -26.293 3.442   1.00 58.58  ?  146 PHE   A O   1 
ATOM   922  C  CB  . PHE   A 1 114 ? -43.885 -24.628 4.160   1.00 52.33  ?  146 PHE   A CB  1 
ATOM   923  C  CG  . PHE   A 1 114 ? -42.710 -24.099 4.866   1.00 43.99  ?  146 PHE   A CG  1 
ATOM   924  C  CD1 . PHE   A 1 114 ? -42.860 -23.244 5.899   1.00 55.01  ?  146 PHE   A CD1 1 
ATOM   925  C  CD2 . PHE   A 1 114 ? -41.454 -24.422 4.466   1.00 44.07  ?  146 PHE   A CD2 1 
ATOM   926  C  CE1 . PHE   A 1 114 ? -41.789 -22.753 6.527   1.00 61.64  ?  146 PHE   A CE1 1 
ATOM   927  C  CE2 . PHE   A 1 114 ? -40.382 -23.917 5.102   1.00 42.21  ?  146 PHE   A CE2 1 
ATOM   928  C  CZ  . PHE   A 1 114 ? -40.547 -23.094 6.118   1.00 48.32  ?  146 PHE   A CZ  1 
ATOM   929  N  N   . SER   A 1 115 ? -47.022 -24.667 4.838   1.00 61.60  ?  147 SER   A N   1 
ATOM   930  C  CA  . SER   A 1 115 ? -48.307 -24.482 4.200   1.00 67.80  ?  147 SER   A CA  1 
ATOM   931  C  C   . SER   A 1 115 ? -48.116 -23.703 2.911   1.00 67.49  ?  147 SER   A C   1 
ATOM   932  O  O   . SER   A 1 115 ? -47.459 -22.664 2.904   1.00 81.06  ?  147 SER   A O   1 
ATOM   933  C  CB  . SER   A 1 115 ? -49.235 -23.739 5.147   1.00 76.25  ?  147 SER   A CB  1 
ATOM   934  O  OG  . SER   A 1 115 ? -48.485 -23.229 6.245   1.00 85.01  ?  147 SER   A OG  1 
ATOM   935  N  N   . HIS   A 1 116 ? -48.662 -24.216 1.819   1.00 64.04  ?  148 HIS   A N   1 
ATOM   936  C  CA  . HIS   A 1 116 ? -48.521 -23.545 0.542   1.00 64.08  ?  148 HIS   A CA  1 
ATOM   937  C  C   . HIS   A 1 116 ? -48.816 -22.063 0.687   1.00 74.58  ?  148 HIS   A C   1 
ATOM   938  O  O   . HIS   A 1 116 ? -49.714 -21.656 1.423   1.00 78.38  ?  148 HIS   A O   1 
ATOM   939  C  CB  . HIS   A 1 116 ? -49.449 -24.161 -0.495  1.00 55.08  ?  148 HIS   A CB  1 
ATOM   940  C  CG  . HIS   A 1 116 ? -49.147 -25.588 -0.796  1.00 59.94  ?  148 HIS   A CG  1 
ATOM   941  N  ND1 . HIS   A 1 116 ? -49.722 -26.262 -1.848  1.00 62.16  ?  148 HIS   A ND1 1 
ATOM   942  C  CD2 . HIS   A 1 116 ? -48.337 -26.477 -0.179  1.00 66.10  ?  148 HIS   A CD2 1 
ATOM   943  C  CE1 . HIS   A 1 116 ? -49.271 -27.502 -1.872  1.00 63.56  ?  148 HIS   A CE1 1 
ATOM   944  N  NE2 . HIS   A 1 116 ? -48.435 -27.661 -0.866  1.00 63.24  ?  148 HIS   A NE2 1 
ATOM   945  N  N   . TRP   A 1 117 ? -48.034 -21.263 -0.008  1.00 66.95  ?  149 TRP   A N   1 
ATOM   946  C  CA  . TRP   A 1 117 ? -48.131 -19.821 0.018   1.00 69.76  ?  149 TRP   A CA  1 
ATOM   947  C  C   . TRP   A 1 117 ? -48.087 -19.375 -1.422  1.00 68.42  ?  149 TRP   A C   1 
ATOM   948  O  O   . TRP   A 1 117 ? -47.335 -19.935 -2.211  1.00 75.34  ?  149 TRP   A O   1 
ATOM   949  C  CB  . TRP   A 1 117 ? -46.975 -19.226 0.813   1.00 77.29  ?  149 TRP   A CB  1 
ATOM   950  C  CG  . TRP   A 1 117 ? -47.146 -17.825 1.263   1.00 86.96  ?  149 TRP   A CG  1 
ATOM   951  C  CD1 . TRP   A 1 117 ? -46.569 -16.718 0.718   1.00 90.94  ?  149 TRP   A CD1 1 
ATOM   952  C  CD2 . TRP   A 1 117 ? -47.926 -17.368 2.374   1.00 97.27  ?  149 TRP   A CD2 1 
ATOM   953  N  NE1 . TRP   A 1 117 ? -46.948 -15.596 1.412   1.00 96.08  ?  149 TRP   A NE1 1 
ATOM   954  C  CE2 . TRP   A 1 117 ? -47.783 -15.968 2.434   1.00 100.32 ?  149 TRP   A CE2 1 
ATOM   955  C  CE3 . TRP   A 1 117 ? -48.740 -18.004 3.319   1.00 103.79 ?  149 TRP   A CE3 1 
ATOM   956  C  CZ2 . TRP   A 1 117 ? -48.425 -15.192 3.404   1.00 95.79  ?  149 TRP   A CZ2 1 
ATOM   957  C  CZ3 . TRP   A 1 117 ? -49.379 -17.230 4.280   1.00 98.00  ?  149 TRP   A CZ3 1 
ATOM   958  C  CH2 . TRP   A 1 117 ? -49.219 -15.841 4.311   1.00 88.45  ?  149 TRP   A CH2 1 
ATOM   959  N  N   . ASN   A 1 118 ? -48.923 -18.414 -1.785  1.00 76.52  ?  150 ASN   A N   1 
ATOM   960  C  CA  . ASN   A 1 118 ? -48.937 -17.908 -3.155  1.00 83.08  ?  150 ASN   A CA  1 
ATOM   961  C  C   . ASN   A 1 118 ? -48.892 -19.038 -4.169  1.00 76.41  ?  150 ASN   A C   1 
ATOM   962  O  O   . ASN   A 1 118 ? -48.340 -18.886 -5.251  1.00 74.43  ?  150 ASN   A O   1 
ATOM   963  C  CB  . ASN   A 1 118 ? -47.770 -16.962 -3.404  1.00 80.62  ?  150 ASN   A CB  1 
ATOM   964  C  CG  . ASN   A 1 118 ? -47.938 -15.662 -2.716  1.00 86.21  ?  150 ASN   A CG  1 
ATOM   965  O  OD1 . ASN   A 1 118 ? -49.055 -15.217 -2.472  1.00 85.29  ?  150 ASN   A OD1 1 
ATOM   966  N  ND2 . ASN   A 1 118 ? -46.827 -15.033 -2.382  1.00 91.75  ?  150 ASN   A ND2 1 
ATOM   967  N  N   . ASN   A 1 119 ? -49.446 -20.190 -3.826  1.00 75.42  ?  151 ASN   A N   1 
ATOM   968  C  CA  . ASN   A 1 119 ? -49.396 -21.348 -4.698  1.00 69.47  ?  151 ASN   A CA  1 
ATOM   969  C  C   . ASN   A 1 119 ? -47.963 -21.794 -4.932  1.00 61.32  ?  151 ASN   A C   1 
ATOM   970  O  O   . ASN   A 1 119 ? -47.635 -22.331 -5.986  1.00 57.09  ?  151 ASN   A O   1 
ATOM   971  C  CB  . ASN   A 1 119 ? -50.108 -21.062 -6.017  1.00 75.44  ?  151 ASN   A CB  1 
ATOM   972  C  CG  . ASN   A 1 119 ? -51.507 -20.518 -5.801  1.00 90.51  ?  151 ASN   A CG  1 
ATOM   973  O  OD1 . ASN   A 1 119 ? -52.178 -20.887 -4.838  1.00 90.99  ?  151 ASN   A OD1 1 
ATOM   974  N  ND2 . ASN   A 1 119 ? -51.951 -19.627 -6.685  1.00 93.43  ?  151 ASN   A ND2 1 
ATOM   975  N  N   . ARG   A 1 120 ? -47.110 -21.585 -3.937  1.00 64.72  ?  152 ARG   A N   1 
ATOM   976  C  CA  . ARG   A 1 120 ? -45.725 -22.017 -3.962  1.00 55.17  ?  152 ARG   A CA  1 
ATOM   977  C  C   . ARG   A 1 120 ? -45.469 -23.068 -2.891  1.00 52.34  ?  152 ARG   A C   1 
ATOM   978  O  O   . ARG   A 1 120 ? -46.007 -22.990 -1.796  1.00 68.93  ?  152 ARG   A O   1 
ATOM   979  C  CB  . ARG   A 1 120 ? -44.808 -20.824 -3.753  1.00 58.93  ?  152 ARG   A CB  1 
ATOM   980  C  CG  . ARG   A 1 120 ? -44.139 -20.344 -5.026  1.00 65.70  ?  152 ARG   A CG  1 
ATOM   981  C  CD  . ARG   A 1 120 ? -43.503 -19.004 -4.817  1.00 57.12  ?  152 ARG   A CD  1 
ATOM   982  N  NE  . ARG   A 1 120 ? -42.072 -19.106 -4.972  1.00 44.13  ?  152 ARG   A NE  1 
ATOM   983  C  CZ  . ARG   A 1 120 ? -41.229 -18.261 -4.433  1.00 43.89  ?  152 ARG   A CZ  1 
ATOM   984  N  NH1 . ARG   A 1 120 ? -41.681 -17.252 -3.718  1.00 48.88  ?  152 ARG   A NH1 1 
ATOM   985  N  NH2 . ARG   A 1 120 ? -39.941 -18.446 -4.601  1.00 55.21  ?  152 ARG   A NH2 1 
ATOM   986  N  N   . VAL   A 1 121 ? -44.636 -24.040 -3.207  1.00 57.80  ?  153 VAL   A N   1 
ATOM   987  C  CA  . VAL   A 1 121 ? -44.324 -25.158 -2.331  1.00 57.34  ?  153 VAL   A CA  1 
ATOM   988  C  C   . VAL   A 1 121 ? -42.853 -25.131 -1.938  1.00 56.71  ?  153 VAL   A C   1 
ATOM   989  O  O   . VAL   A 1 121 ? -41.996 -24.751 -2.733  1.00 62.41  ?  153 VAL   A O   1 
ATOM   990  C  CB  . VAL   A 1 121 ? -44.652 -26.467 -3.054  1.00 53.95  ?  153 VAL   A CB  1 
ATOM   991  C  CG1 . VAL   A 1 121 ? -44.729 -27.582 -2.082  1.00 66.63  ?  153 VAL   A CG1 1 
ATOM   992  C  CG2 . VAL   A 1 121 ? -45.931 -26.328 -3.772  1.00 66.65  ?  153 VAL   A CG2 1 
ATOM   993  N  N   . PHE   A 1 122 ? -42.545 -25.587 -0.731  1.00 51.65  ?  154 PHE   A N   1 
ATOM   994  C  CA  . PHE   A 1 122 ? -41.160 -25.688 -0.296  1.00 43.63  ?  154 PHE   A CA  1 
ATOM   995  C  C   . PHE   A 1 122 ? -40.602 -27.039 -0.699  1.00 45.46  ?  154 PHE   A C   1 
ATOM   996  O  O   . PHE   A 1 122 ? -41.072 -28.073 -0.233  1.00 41.42  ?  154 PHE   A O   1 
ATOM   997  C  CB  . PHE   A 1 122 ? -41.031 -25.490 1.206   1.00 41.82  ?  154 PHE   A CB  1 
ATOM   998  C  CG  . PHE   A 1 122 ? -39.617 -25.509 1.703   1.00 44.92  ?  154 PHE   A CG  1 
ATOM   999  C  CD1 . PHE   A 1 122 ? -38.831 -24.402 1.624   1.00 46.05  ?  154 PHE   A CD1 1 
ATOM   1000 C  CD2 . PHE   A 1 122 ? -39.080 -26.631 2.272   1.00 48.40  ?  154 PHE   A CD2 1 
ATOM   1001 C  CE1 . PHE   A 1 122 ? -37.571 -24.424 2.083   1.00 42.06  ?  154 PHE   A CE1 1 
ATOM   1002 C  CE2 . PHE   A 1 122 ? -37.804 -26.632 2.720   1.00 36.61  ?  154 PHE   A CE2 1 
ATOM   1003 C  CZ  . PHE   A 1 122 ? -37.067 -25.533 2.620   1.00 39.65  ?  154 PHE   A CZ  1 
ATOM   1004 N  N   . VAL   A 1 123 ? -39.577 -27.018 -1.541  1.00 51.75  ?  155 VAL   A N   1 
ATOM   1005 C  CA  . VAL   A 1 123 ? -38.932 -28.228 -2.025  1.00 43.19  ?  155 VAL   A CA  1 
ATOM   1006 C  C   . VAL   A 1 123 ? -37.527 -28.397 -1.498  1.00 41.60  ?  155 VAL   A C   1 
ATOM   1007 O  O   . VAL   A 1 123 ? -36.915 -29.439 -1.746  1.00 41.18  ?  155 VAL   A O   1 
ATOM   1008 C  CB  . VAL   A 1 123 ? -38.889 -28.250 -3.557  1.00 43.32  ?  155 VAL   A CB  1 
ATOM   1009 C  CG1 . VAL   A 1 123 ? -40.170 -27.766 -4.117  1.00 52.38  ?  155 VAL   A CG1 1 
ATOM   1010 C  CG2 . VAL   A 1 123 ? -37.808 -27.394 -4.011  1.00 44.68  ?  155 VAL   A CG2 1 
ATOM   1011 N  N   . GLY   A 1 124 ? -36.969 -27.396 -0.859  1.00 44.57  ?  156 GLY   A N   1 
ATOM   1012 C  CA  . GLY   A 1 124 ? -35.762 -27.562 -0.104  1.00 36.67  ?  156 GLY   A CA  1 
ATOM   1013 C  C   . GLY   A 1 124 ? -34.630 -28.052 -0.943  1.00 37.21  ?  156 GLY   A C   1 
ATOM   1014 O  O   . GLY   A 1 124 ? -34.136 -29.155 -0.730  1.00 42.36  ?  156 GLY   A O   1 
ATOM   1015 N  N   . ALA   A 1 125 ? -34.185 -27.216 -1.872  1.00 42.86  ?  157 ALA   A N   1 
ATOM   1016 C  CA  . ALA   A 1 125 ? -33.125 -27.597 -2.793  1.00 38.13  ?  157 ALA   A CA  1 
ATOM   1017 C  C   . ALA   A 1 125 ? -31.759 -27.672 -2.120  1.00 33.77  ?  157 ALA   A C   1 
ATOM   1018 O  O   . ALA   A 1 125 ? -31.006 -28.605 -2.374  1.00 29.86  ?  157 ALA   A O   1 
ATOM   1019 C  CB  . ALA   A 1 125 ? -33.105 -26.629 -3.950  1.00 41.81  ?  157 ALA   A CB  1 
ATOM   1020 N  N   . THR   A 1 126 ? -31.387 -26.685 -1.308  1.00 33.08  ?  158 THR   A N   1 
ATOM   1021 C  CA  . THR   A 1 126 ? -30.165 -26.820 -0.536  1.00 34.66  ?  158 THR   A CA  1 
ATOM   1022 C  C   . THR   A 1 126 ? -30.352 -27.618 0.736   1.00 38.17  ?  158 THR   A C   1 
ATOM   1023 O  O   . THR   A 1 126 ? -29.354 -28.080 1.285   1.00 38.74  ?  158 THR   A O   1 
ATOM   1024 C  CB  . THR   A 1 126 ? -29.620 -25.468 -0.109  1.00 31.65  ?  158 THR   A CB  1 
ATOM   1025 O  OG1 . THR   A 1 126 ? -30.527 -24.896 0.813   1.00 43.23  ?  158 THR   A OG1 1 
ATOM   1026 C  CG2 . THR   A 1 126 ? -29.517 -24.550 -1.217  1.00 36.80  ?  158 THR   A CG2 1 
ATOM   1027 N  N   . ASP   A 1 127 ? -31.563 -27.643 1.239   1.00 32.59  ?  159 ASP   A N   1 
ATOM   1028 C  CA  . ASP   A 1 127 ? -31.924 -28.171 2.534   1.00 37.58  ?  159 ASP   A CA  1 
ATOM   1029 C  C   . ASP   A 1 127 ? -32.970 -29.219 2.408   1.00 40.37  ?  159 ASP   A C   1 
ATOM   1030 O  O   . ASP   A 1 127 ? -34.096 -28.960 2.743   1.00 37.49  ?  159 ASP   A O   1 
ATOM   1031 C  CB  . ASP   A 1 127 ? -32.417 -26.905 3.269   1.00 42.79  ?  159 ASP   A CB  1 
ATOM   1032 C  CG  . ASP   A 1 127 ? -33.077 -27.117 4.617   1.00 42.19  ?  159 ASP   A CG  1 
ATOM   1033 O  OD1 . ASP   A 1 127 ? -32.885 -28.082 5.305   1.00 38.81  ?  159 ASP   A OD1 1 
ATOM   1034 O  OD2 . ASP   A 1 127 ? -33.773 -26.191 5.012   1.00 41.59  ?  159 ASP   A OD2 1 
ATOM   1035 N  N   . SER   A 1 128 ? -32.632 -30.400 1.891   1.00 40.64  ?  160 SER   A N   1 
ATOM   1036 C  CA  . SER   A 1 128 ? -31.280 -30.832 1.563   1.00 33.66  ?  160 SER   A CA  1 
ATOM   1037 C  C   . SER   A 1 128 ? -31.257 -31.769 0.369   1.00 38.82  ?  160 SER   A C   1 
ATOM   1038 O  O   . SER   A 1 128 ? -30.619 -32.799 0.398   1.00 42.66  ?  160 SER   A O   1 
ATOM   1039 C  CB  . SER   A 1 128 ? -30.659 -31.556 2.729   1.00 36.21  ?  160 SER   A CB  1 
ATOM   1040 O  OG  . SER   A 1 128 ? -29.999 -30.695 3.576   1.00 39.45  ?  160 SER   A OG  1 
ATOM   1041 N  N   . ALA   A 1 129 ? -31.928 -31.403 -0.706  1.00 34.83  ?  161 ALA   A N   1 
ATOM   1042 C  CA  . ALA   A 1 129 ? -31.970 -32.266 -1.869  1.00 28.67  ?  161 ALA   A CA  1 
ATOM   1043 C  C   . ALA   A 1 129 ? -30.624 -32.378 -2.559  1.00 37.65  ?  161 ALA   A C   1 
ATOM   1044 O  O   . ALA   A 1 129 ? -30.280 -33.444 -3.066  1.00 42.50  ?  161 ALA   A O   1 
ATOM   1045 C  CB  . ALA   A 1 129 ? -33.007 -31.744 -2.833  1.00 35.70  ?  161 ALA   A CB  1 
ATOM   1046 N  N   . VAL   A 1 130 ? -29.878 -31.287 -2.654  1.00 38.32  ?  162 VAL   A N   1 
ATOM   1047 C  CA  . VAL   A 1 130 ? -28.563 -31.301 -3.292  1.00 37.44  ?  162 VAL   A CA  1 
ATOM   1048 C  C   . VAL   A 1 130 ? -27.683 -32.302 -2.560  1.00 37.86  ?  162 VAL   A C   1 
ATOM   1049 O  O   . VAL   A 1 130 ? -27.162 -33.228 -3.190  1.00 35.28  ?  162 VAL   A O   1 
ATOM   1050 C  CB  . VAL   A 1 130 ? -27.943 -29.890 -3.323  1.00 34.94  ?  162 VAL   A CB  1 
ATOM   1051 C  CG1 . VAL   A 1 130 ? -26.500 -29.896 -3.588  1.00 33.97  ?  162 VAL   A CG1 1 
ATOM   1052 C  CG2 . VAL   A 1 130 ? -28.544 -29.090 -4.375  1.00 31.32  ?  162 VAL   A CG2 1 
ATOM   1053 N  N   . PRO   A 1 131 ? -27.486 -32.170 -1.255  1.00 35.50  ?  163 PRO   A N   1 
ATOM   1054 C  CA  . PRO   A 1 131 ? -26.711 -33.181 -0.547  1.00 37.16  ?  163 PRO   A CA  1 
ATOM   1055 C  C   . PRO   A 1 131 ? -27.161 -34.591 -0.830  1.00 42.39  ?  163 PRO   A C   1 
ATOM   1056 O  O   . PRO   A 1 131 ? -26.324 -35.491 -0.888  1.00 43.54  ?  163 PRO   A O   1 
ATOM   1057 C  CB  . PRO   A 1 131 ? -26.931 -32.808 0.907   1.00 36.14  ?  163 PRO   A CB  1 
ATOM   1058 C  CG  . PRO   A 1 131 ? -27.145 -31.434 0.888   1.00 38.65  ?  163 PRO   A CG  1 
ATOM   1059 C  CD  . PRO   A 1 131 ? -27.840 -31.078 -0.353  1.00 37.89  ?  163 PRO   A CD  1 
ATOM   1060 N  N   . CYS   A 1 132 ? -28.457 -34.837 -0.989  1.00 43.52  ?  164 CYS   A N   1 
ATOM   1061 C  CA  . CYS   A 1 132 ? -28.861 -36.176 -1.385  1.00 40.35  ?  164 CYS   A CA  1 
ATOM   1062 C  C   . CYS   A 1 132 ? -28.218 -36.533 -2.700  1.00 41.89  ?  164 CYS   A C   1 
ATOM   1063 O  O   . CYS   A 1 132 ? -27.554 -37.561 -2.820  1.00 46.27  ?  164 CYS   A O   1 
ATOM   1064 C  CB  . CYS   A 1 132 ? -30.364 -36.291 -1.503  1.00 40.61  ?  164 CYS   A CB  1 
ATOM   1065 S  SG  . CYS   A 1 132 ? -31.262 -36.206 0.013   1.00 30.72  ?  164 CYS   A SG  1 
ATOM   1066 N  N   . ALA   A 1 133 ? -28.365 -35.666 -3.689  1.00 44.08  ?  165 ALA   A N   1 
ATOM   1067 C  CA  . ALA   A 1 133 ? -27.819 -35.959 -4.996  1.00 39.35  ?  165 ALA   A CA  1 
ATOM   1068 C  C   . ALA   A 1 133 ? -26.314 -36.066 -4.941  1.00 38.81  ?  165 ALA   A C   1 
ATOM   1069 O  O   . ALA   A 1 133 ? -25.727 -36.939 -5.580  1.00 45.56  ?  165 ALA   A O   1 
ATOM   1070 C  CB  . ALA   A 1 133 ? -28.246 -34.891 -5.975  1.00 38.33  ?  165 ALA   A CB  1 
ATOM   1071 N  N   . MET   A 1 134 ? -25.661 -35.201 -4.180  1.00 41.66  ?  166 MET   A N   1 
ATOM   1072 C  CA  . MET   A 1 134 ? -24.210 -35.278 -4.125  1.00 41.80  ?  166 MET   A CA  1 
ATOM   1073 C  C   . MET   A 1 134 ? -23.753 -36.632 -3.656  1.00 36.58  ?  166 MET   A C   1 
ATOM   1074 O  O   . MET   A 1 134 ? -22.699 -37.098 -4.072  1.00 48.35  ?  166 MET   A O   1 
ATOM   1075 C  CB  . MET   A 1 134 ? -23.640 -34.207 -3.218  1.00 39.94  ?  166 MET   A CB  1 
ATOM   1076 C  CG  . MET   A 1 134 ? -23.827 -32.867 -3.744  1.00 36.22  ?  166 MET   A CG  1 
ATOM   1077 S  SD  . MET   A 1 134 ? -23.249 -31.651 -2.615  1.00 29.94  ?  166 MET   A SD  1 
ATOM   1078 C  CE  . MET   A 1 134 ? -21.551 -31.989 -2.467  1.00 28.26  ?  166 MET   A CE  1 
ATOM   1079 N  N   . MET   A 1 135 ? -24.518 -37.272 -2.800  1.00 38.33  ?  167 MET   A N   1 
ATOM   1080 C  CA  . MET   A 1 135 ? -24.135 -38.578 -2.304  1.00 41.13  ?  167 MET   A CA  1 
ATOM   1081 C  C   . MET   A 1 135 ? -24.469 -39.657 -3.302  1.00 43.10  ?  167 MET   A C   1 
ATOM   1082 O  O   . MET   A 1 135 ? -23.774 -40.666 -3.355  1.00 45.01  ?  167 MET   A O   1 
ATOM   1083 C  CB  . MET   A 1 135 ? -24.823 -38.874 -0.976  1.00 43.07  ?  167 MET   A CB  1 
ATOM   1084 C  CG  . MET   A 1 135 ? -24.385 -37.991 0.130   1.00 50.72  ?  167 MET   A CG  1 
ATOM   1085 S  SD  . MET   A 1 135 ? -25.479 -37.920 1.527   1.00 49.71  ?  167 MET   A SD  1 
ATOM   1086 C  CE  . MET   A 1 135 ? -25.538 -39.616 1.964   1.00 52.00  ?  167 MET   A CE  1 
ATOM   1087 N  N   . LEU   A 1 136 ? -25.516 -39.476 -4.097  1.00 45.45  ?  168 LEU   A N   1 
ATOM   1088 C  CA  . LEU   A 1 136 ? -25.770 -40.424 -5.168  1.00 44.72  ?  168 LEU   A CA  1 
ATOM   1089 C  C   . LEU   A 1 136 ? -24.702 -40.329 -6.238  1.00 48.20  ?  168 LEU   A C   1 
ATOM   1090 O  O   . LEU   A 1 136 ? -24.121 -41.341 -6.629  1.00 58.11  ?  168 LEU   A O   1 
ATOM   1091 C  CB  . LEU   A 1 136 ? -27.138 -40.200 -5.772  1.00 43.84  ?  168 LEU   A CB  1 
ATOM   1092 C  CG  . LEU   A 1 136 ? -28.318 -40.338 -4.843  1.00 41.17  ?  168 LEU   A CG  1 
ATOM   1093 C  CD1 . LEU   A 1 136 ? -29.544 -40.176 -5.660  1.00 50.12  ?  168 LEU   A CD1 1 
ATOM   1094 C  CD2 . LEU   A 1 136 ? -28.327 -41.622 -4.191  1.00 36.17  ?  168 LEU   A CD2 1 
ATOM   1095 N  N   . GLU   A 1 137 ? -24.409 -39.127 -6.716  1.00 44.39  ?  169 GLU   A N   1 
ATOM   1096 C  CA  . GLU   A 1 137 ? -23.361 -39.002 -7.718  1.00 48.19  ?  169 GLU   A CA  1 
ATOM   1097 C  C   . GLU   A 1 137 ? -22.068 -39.604 -7.221  1.00 49.31  ?  169 GLU   A C   1 
ATOM   1098 O  O   . GLU   A 1 137 ? -21.332 -40.221 -7.988  1.00 53.19  ?  169 GLU   A O   1 
ATOM   1099 C  CB  . GLU   A 1 137 ? -23.145 -37.552 -8.094  1.00 47.39  ?  169 GLU   A CB  1 
ATOM   1100 C  CG  . GLU   A 1 137 ? -21.964 -37.312 -8.990  1.00 52.74  ?  169 GLU   A CG  1 
ATOM   1101 C  CD  . GLU   A 1 137 ? -22.165 -37.810 -10.365 1.00 55.08  ?  169 GLU   A CD  1 
ATOM   1102 O  OE1 . GLU   A 1 137 ? -23.192 -38.438 -10.620 1.00 63.68  ?  169 GLU   A OE1 1 
ATOM   1103 O  OE2 . GLU   A 1 137 ? -21.300 -37.566 -11.205 1.00 55.45  ?  169 GLU   A OE2 1 
ATOM   1104 N  N   . LEU   A 1 138 ? -21.776 -39.448 -5.939  1.00 50.45  ?  170 LEU   A N   1 
ATOM   1105 C  CA  . LEU   A 1 138 ? -20.538 -39.994 -5.411  1.00 48.73  ?  170 LEU   A CA  1 
ATOM   1106 C  C   . LEU   A 1 138 ? -20.538 -41.498 -5.487  1.00 50.86  ?  170 LEU   A C   1 
ATOM   1107 O  O   . LEU   A 1 138 ? -19.493 -42.115 -5.695  1.00 56.37  ?  170 LEU   A O   1 
ATOM   1108 C  CB  . LEU   A 1 138 ? -20.339 -39.567 -3.980  1.00 40.98  ?  170 LEU   A CB  1 
ATOM   1109 C  CG  . LEU   A 1 138 ? -19.106 -40.157 -3.351  1.00 40.51  ?  170 LEU   A CG  1 
ATOM   1110 C  CD1 . LEU   A 1 138 ? -18.598 -39.202 -2.368  1.00 42.87  ?  170 LEU   A CD1 1 
ATOM   1111 C  CD2 . LEU   A 1 138 ? -19.385 -41.418 -2.625  1.00 39.35  ?  170 LEU   A CD2 1 
ATOM   1112 N  N   . ALA   A 1 139 ? -21.696 -42.106 -5.281  1.00 55.14  ?  171 ALA   A N   1 
ATOM   1113 C  CA  . ALA   A 1 139 ? -21.793 -43.548 -5.382  1.00 56.56  ?  171 ALA   A CA  1 
ATOM   1114 C  C   . ALA   A 1 139 ? -21.609 -44.006 -6.802  1.00 53.23  ?  171 ALA   A C   1 
ATOM   1115 O  O   . ALA   A 1 139 ? -21.178 -45.133 -7.029  1.00 61.59  ?  171 ALA   A O   1 
ATOM   1116 C  CB  . ALA   A 1 139 ? -23.141 -44.014 -4.876  1.00 55.00  ?  171 ALA   A CB  1 
ATOM   1117 N  N   . ARG   A 1 140 ? -21.936 -43.158 -7.762  1.00 49.69  ?  172 ARG   A N   1 
ATOM   1118 C  CA  . ARG   A 1 140 ? -21.849 -43.540 -9.167  1.00 61.79  ?  172 ARG   A CA  1 
ATOM   1119 C  C   . ARG   A 1 140 ? -20.433 -43.333 -9.687  1.00 63.11  ?  172 ARG   A C   1 
ATOM   1120 O  O   . ARG   A 1 140 ? -19.734 -44.285 -10.031 1.00 70.29  ?  172 ARG   A O   1 
ATOM   1121 C  CB  . ARG   A 1 140 ? -22.853 -42.726 -9.979  1.00 59.43  ?  172 ARG   A CB  1 
ATOM   1122 C  CG  . ARG   A 1 140 ? -22.824 -43.009 -11.419 1.00 53.25  ?  172 ARG   A CG  1 
ATOM   1123 C  CD  . ARG   A 1 140 ? -23.507 -41.927 -12.185 1.00 60.81  ?  172 ARG   A CD  1 
ATOM   1124 N  NE  . ARG   A 1 140 ? -22.658 -40.768 -12.314 1.00 67.87  ?  172 ARG   A NE  1 
ATOM   1125 C  CZ  . ARG   A 1 140 ? -21.566 -40.749 -13.055 1.00 66.30  ?  172 ARG   A CZ  1 
ATOM   1126 N  NH1 . ARG   A 1 140 ? -21.205 -41.829 -13.722 1.00 82.32  ?  172 ARG   A NH1 1 
ATOM   1127 N  NH2 . ARG   A 1 140 ? -20.827 -39.660 -13.123 1.00 67.95  ?  172 ARG   A NH2 1 
ATOM   1128 N  N   . ALA   A 1 141 ? -20.005 -42.086 -9.741  1.00 62.21  ?  173 ALA   A N   1 
ATOM   1129 C  CA  . ALA   A 1 141 ? -18.664 -41.723 -10.152 1.00 61.04  ?  173 ALA   A CA  1 
ATOM   1130 C  C   . ALA   A 1 141 ? -17.612 -42.683 -9.622  1.00 63.63  ?  173 ALA   A C   1 
ATOM   1131 O  O   . ALA   A 1 141 ? -16.590 -42.906 -10.274 1.00 73.28  ?  173 ALA   A O   1 
ATOM   1132 C  CB  . ALA   A 1 141 ? -18.354 -40.307 -9.676  1.00 61.47  ?  173 ALA   A CB  1 
ATOM   1133 N  N   . LEU   A 1 142 ? -17.835 -43.248 -8.445  1.00 50.05  ?  174 LEU   A N   1 
ATOM   1134 C  CA  . LEU   A 1 142 ? -16.854 -44.115 -7.828  1.00 53.02  ?  174 LEU   A CA  1 
ATOM   1135 C  C   . LEU   A 1 142 ? -17.310 -45.557 -7.780  1.00 56.88  ?  174 LEU   A C   1 
ATOM   1136 O  O   . LEU   A 1 142 ? -16.733 -46.349 -7.039  1.00 60.65  ?  174 LEU   A O   1 
ATOM   1137 C  CB  . LEU   A 1 142 ? -16.532 -43.628 -6.423  1.00 53.20  ?  174 LEU   A CB  1 
ATOM   1138 C  CG  . LEU   A 1 142 ? -16.117 -42.170 -6.281  1.00 47.44  ?  174 LEU   A CG  1 
ATOM   1139 C  CD1 . LEU   A 1 142 ? -15.541 -41.913 -4.922  1.00 42.57  ?  174 LEU   A CD1 1 
ATOM   1140 C  CD2 . LEU   A 1 142 ? -15.091 -41.810 -7.275  1.00 64.60  ?  174 LEU   A CD2 1 
ATOM   1141 N  N   . ASP   A 1 143 ? -18.327 -45.919 -8.557  1.00 56.79  ?  175 ASP   A N   1 
ATOM   1142 C  CA  . ASP   A 1 143 ? -18.844 -47.280 -8.510  1.00 62.75  ?  175 ASP   A CA  1 
ATOM   1143 C  C   . ASP   A 1 143 ? -17.723 -48.277 -8.723  1.00 68.35  ?  175 ASP   A C   1 
ATOM   1144 O  O   . ASP   A 1 143 ? -17.466 -49.135 -7.878  1.00 67.93  ?  175 ASP   A O   1 
ATOM   1145 C  CB  . ASP   A 1 143 ? -19.928 -47.457 -9.566  1.00 64.88  ?  175 ASP   A CB  1 
ATOM   1146 C  CG  . ASP   A 1 143 ? -20.834 -48.616 -9.278  1.00 62.17  ?  175 ASP   A CG  1 
ATOM   1147 O  OD1 . ASP   A 1 143 ? -20.766 -49.162 -8.168  1.00 56.82  ?  175 ASP   A OD1 1 
ATOM   1148 O  OD2 . ASP   A 1 143 ? -21.635 -48.969 -10.164 1.00 64.59  ?  175 ASP   A OD2 1 
ATOM   1149 N  N   . LYS   A 1 144 ? -17.037 -48.159 -9.857  1.00 75.08  ?  176 LYS   A N   1 
ATOM   1150 C  CA  . LYS   A 1 144 ? -15.890 -49.003 -10.164 1.00 67.63  ?  176 LYS   A CA  1 
ATOM   1151 C  C   . LYS   A 1 144 ? -14.905 -49.057 -9.004  1.00 67.70  ?  176 LYS   A C   1 
ATOM   1152 O  O   . LYS   A 1 144 ? -14.667 -50.117 -8.420  1.00 64.25  ?  176 LYS   A O   1 
ATOM   1153 C  CB  . LYS   A 1 144 ? -15.216 -48.484 -11.430 1.00 78.03  ?  176 LYS   A CB  1 
ATOM   1154 C  CG  . LYS   A 1 144 ? -15.212 -46.944 -11.543 1.00 88.60  ?  176 LYS   A CG  1 
ATOM   1155 C  CD  . LYS   A 1 144 ? -14.321 -46.440 -12.679 1.00 105.83 ?  176 LYS   A CD  1 
ATOM   1156 C  CE  . LYS   A 1 144 ? -13.245 -45.445 -12.207 1.00 98.23  ?  176 LYS   A CE  1 
ATOM   1157 N  NZ  . LYS   A 1 144 ? -13.190 -44.240 -13.085 1.00 102.29 ?  176 LYS   A NZ  1 
ATOM   1158 N  N   . LYS   A 1 145 ? -14.325 -47.914 -8.641  1.00 73.68  ?  177 LYS   A N   1 
ATOM   1159 C  CA  . LYS   A 1 145 ? -13.346 -47.913 -7.566  1.00 66.62  ?  177 LYS   A CA  1 
ATOM   1160 C  C   . LYS   A 1 145 ? -13.918 -48.553 -6.312  1.00 61.90  ?  177 LYS   A C   1 
ATOM   1161 O  O   . LYS   A 1 145 ? -13.176 -49.099 -5.494  1.00 62.74  ?  177 LYS   A O   1 
ATOM   1162 C  CB  . LYS   A 1 145 ? -12.884 -46.485 -7.276  1.00 65.05  ?  177 LYS   A CB  1 
ATOM   1163 C  CG  . LYS   A 1 145 ? -12.151 -45.765 -8.398  1.00 75.19  ?  177 LYS   A CG  1 
ATOM   1164 C  CD  . LYS   A 1 145 ? -10.704 -45.508 -8.010  1.00 78.88  ?  177 LYS   A CD  1 
ATOM   1165 C  CE  . LYS   A 1 145 ? -10.065 -44.414 -8.847  1.00 78.37  ?  177 LYS   A CE  1 
ATOM   1166 N  NZ  . LYS   A 1 145 ? -8.678  -44.089 -8.336  1.00 82.77  ?  177 LYS   A NZ  1 
ATOM   1167 N  N   . LEU   A 1 146 ? -15.226 -48.503 -6.140  1.00 66.75  ?  178 LEU   A N   1 
ATOM   1168 C  CA  . LEU   A 1 146 ? -15.846 -49.057 -4.953  1.00 68.69  ?  178 LEU   A CA  1 
ATOM   1169 C  C   . LEU   A 1 146 ? -16.256 -50.498 -5.148  1.00 73.49  ?  178 LEU   A C   1 
ATOM   1170 O  O   . LEU   A 1 146 ? -16.805 -51.101 -4.226  1.00 74.66  ?  178 LEU   A O   1 
ATOM   1171 C  CB  . LEU   A 1 146 ? -17.072 -48.243 -4.550  1.00 69.39  ?  178 LEU   A CB  1 
ATOM   1172 C  CG  . LEU   A 1 146 ? -16.899 -46.837 -3.990  1.00 66.31  ?  178 LEU   A CG  1 
ATOM   1173 C  CD1 . LEU   A 1 146 ? -18.255 -46.229 -3.853  1.00 71.56  ?  178 LEU   A CD1 1 
ATOM   1174 C  CD2 . LEU   A 1 146 ? -16.192 -46.826 -2.652  1.00 63.03  ?  178 LEU   A CD2 1 
ATOM   1175 N  N   . LEU   A 1 147 ? -15.991 -51.081 -6.311  1.00 75.82  ?  179 LEU   A N   1 
ATOM   1176 C  CA  . LEU   A 1 147 ? -16.192 -52.516 -6.436  1.00 73.71  ?  179 LEU   A CA  1 
ATOM   1177 C  C   . LEU   A 1 147 ? -15.132 -53.265 -5.657  1.00 75.82  ?  179 LEU   A C   1 
ATOM   1178 O  O   . LEU   A 1 147 ? -15.414 -54.274 -5.004  1.00 78.66  ?  179 LEU   A O   1 
ATOM   1179 C  CB  . LEU   A 1 147 ? -16.146 -52.931 -7.889  1.00 61.60  ?  179 LEU   A CB  1 
ATOM   1180 C  CG  . LEU   A 1 147 ? -17.287 -53.799 -8.376  1.00 70.31  ?  179 LEU   A CG  1 
ATOM   1181 C  CD1 . LEU   A 1 147 ? -17.971 -54.637 -7.276  1.00 74.59  ?  179 LEU   A CD1 1 
ATOM   1182 C  CD2 . LEU   A 1 147 ? -18.250 -52.922 -9.082  1.00 68.13  ?  179 LEU   A CD2 1 
ATOM   1183 N  N   . SER   A 1 148 ? -13.918 -52.741 -5.675  1.00 79.63  ?  180 SER   A N   1 
ATOM   1184 C  CA  . SER   A 1 148 ? -12.751 -53.302 -5.017  1.00 85.30  ?  180 SER   A CA  1 
ATOM   1185 C  C   . SER   A 1 148 ? -12.932 -53.702 -3.558  1.00 87.70  ?  180 SER   A C   1 
ATOM   1186 O  O   . SER   A 1 148 ? -11.950 -54.071 -2.907  1.00 92.96  ?  180 SER   A O   1 
ATOM   1187 C  CB  . SER   A 1 148 ? -11.617 -52.280 -5.103  1.00 76.77  ?  180 SER   A CB  1 
ATOM   1188 O  OG  . SER   A 1 148 ? -11.535 -51.722 -6.403  1.00 73.62  ?  180 SER   A OG  1 
ATOM   1189 N  N   . LEU   A 1 149 ? -14.141 -53.637 -3.016  1.00 82.45  ?  181 LEU   A N   1 
ATOM   1190 C  CA  . LEU   A 1 149 ? -14.325 -53.935 -1.608  1.00 91.19  ?  181 LEU   A CA  1 
ATOM   1191 C  C   . LEU   A 1 149 ? -15.012 -55.265 -1.361  1.00 91.65  ?  181 LEU   A C   1 
ATOM   1192 O  O   . LEU   A 1 149 ? -15.279 -55.588 -0.208  1.00 95.16  ?  181 LEU   A O   1 
ATOM   1193 C  CB  . LEU   A 1 149 ? -15.092 -52.798 -0.937  1.00 100.58 ?  181 LEU   A CB  1 
ATOM   1194 C  CG  . LEU   A 1 149 ? -14.366 -51.463 -1.135  1.00 87.51  ?  181 LEU   A CG  1 
ATOM   1195 C  CD1 . LEU   A 1 149 ? -15.089 -50.702 -2.181  1.00 84.08  ?  181 LEU   A CD1 1 
ATOM   1196 C  CD2 . LEU   A 1 149 ? -14.233 -50.622 0.106   1.00 60.13  ?  181 LEU   A CD2 1 
ATOM   1197 N  N   . LYS   A 1 150 ? -15.295 -56.034 -2.408  1.00 93.09  ?  182 LYS   A N   1 
ATOM   1198 C  CA  . LYS   A 1 150 ? -15.608 -57.469 -2.334  1.00 95.36  ?  182 LYS   A CA  1 
ATOM   1199 C  C   . LYS   A 1 150 ? -17.063 -57.697 -2.707  1.00 91.38  ?  182 LYS   A C   1 
ATOM   1200 O  O   . LYS   A 1 150 ? -17.354 -58.158 -3.811  1.00 81.51  ?  182 LYS   A O   1 
ATOM   1201 C  CB  . LYS   A 1 150 ? -15.317 -58.082 -0.947  1.00 97.16  ?  182 LYS   A CB  1 
ATOM   1202 C  CG  . LYS   A 1 150 ? -13.847 -58.013 -0.457  1.00 85.23  ?  182 LYS   A CG  1 
ATOM   1203 C  CD  . LYS   A 1 150 ? -12.944 -58.911 -1.267  1.00 75.28  ?  182 LYS   A CD  1 
ATOM   1204 C  CE  . LYS   A 1 150 ? -11.518 -58.382 -1.241  1.00 81.45  ?  182 LYS   A CE  1 
ATOM   1205 N  NZ  . LYS   A 1 150 ? -10.946 -58.290 0.149   1.00 80.45  ?  182 LYS   A NZ  1 
ATOM   1206 N  N   . PRO   A 1 157 ? -6.847  -53.690 6.016   1.00 74.07  ?  189 PRO   A N   1 
ATOM   1207 C  CA  . PRO   A 1 157 ? -7.699  -52.601 6.517   1.00 85.18  ?  189 PRO   A CA  1 
ATOM   1208 C  C   . PRO   A 1 157 ? -9.176  -52.901 6.335   1.00 87.65  ?  189 PRO   A C   1 
ATOM   1209 O  O   . PRO   A 1 157 ? -9.674  -52.782 5.218   1.00 80.55  ?  189 PRO   A O   1 
ATOM   1210 C  CB  . PRO   A 1 157 ? -7.296  -51.427 5.648   1.00 70.24  ?  189 PRO   A CB  1 
ATOM   1211 C  CG  . PRO   A 1 157 ? -7.024  -52.107 4.305   1.00 79.05  ?  189 PRO   A CG  1 
ATOM   1212 C  CD  . PRO   A 1 157 ? -6.497  -53.500 4.598   1.00 65.36  ?  189 PRO   A CD  1 
ATOM   1213 N  N   . ASP   A 1 158 ? -9.870  -53.281 7.406   1.00 87.83  ?  190 ASP   A N   1 
ATOM   1214 C  CA  . ASP   A 1 158 ? -11.274 -53.678 7.305   1.00 79.60  ?  190 ASP   A CA  1 
ATOM   1215 C  C   . ASP   A 1 158 ? -12.146 -52.459 7.521   1.00 77.29  ?  190 ASP   A C   1 
ATOM   1216 O  O   . ASP   A 1 158 ? -12.596 -52.178 8.638   1.00 71.21  ?  190 ASP   A O   1 
ATOM   1217 C  CB  . ASP   A 1 158 ? -11.626 -54.749 8.315   1.00 80.36  ?  190 ASP   A CB  1 
ATOM   1218 C  CG  . ASP   A 1 158 ? -12.900 -55.421 7.976   1.00 76.04  ?  190 ASP   A CG  1 
ATOM   1219 O  OD1 . ASP   A 1 158 ? -13.146 -55.636 6.761   1.00 68.52  ?  190 ASP   A OD1 1 
ATOM   1220 O  OD2 . ASP   A 1 158 ? -13.655 -55.707 8.918   1.00 69.73  ?  190 ASP   A OD2 1 
ATOM   1221 N  N   . LEU   A 1 159 ? -12.401 -51.739 6.432   1.00 67.57  ?  191 LEU   A N   1 
ATOM   1222 C  CA  . LEU   A 1 159 ? -13.088 -50.464 6.505   1.00 66.03  ?  191 LEU   A CA  1 
ATOM   1223 C  C   . LEU   A 1 159 ? -13.870 -50.274 5.227   1.00 57.45  ?  191 LEU   A C   1 
ATOM   1224 O  O   . LEU   A 1 159 ? -13.422 -50.705 4.169   1.00 52.65  ?  191 LEU   A O   1 
ATOM   1225 C  CB  . LEU   A 1 159 ? -12.092 -49.337 6.694   1.00 69.61  ?  191 LEU   A CB  1 
ATOM   1226 C  CG  . LEU   A 1 159 ? -12.565 -47.912 6.528   1.00 57.10  ?  191 LEU   A CG  1 
ATOM   1227 C  CD1 . LEU   A 1 159 ? -12.506 -47.170 7.828   1.00 70.31  ?  191 LEU   A CD1 1 
ATOM   1228 C  CD2 . LEU   A 1 159 ? -11.639 -47.286 5.596   1.00 57.19  ?  191 LEU   A CD2 1 
ATOM   1229 N  N   . SER   A 1 160 ? -15.035 -49.645 5.322   1.00 60.91  ?  192 SER   A N   1 
ATOM   1230 C  CA  . SER   A 1 160 ? -15.831 -49.458 4.124   1.00 58.10  ?  192 SER   A CA  1 
ATOM   1231 C  C   . SER   A 1 160 ? -16.710 -48.215 4.272   1.00 55.48  ?  192 SER   A C   1 
ATOM   1232 O  O   . SER   A 1 160 ? -16.493 -47.375 5.149   1.00 47.44  ?  192 SER   A O   1 
ATOM   1233 C  CB  . SER   A 1 160 ? -16.613 -50.734 3.841   1.00 52.72  ?  192 SER   A CB  1 
ATOM   1234 O  OG  . SER   A 1 160 ? -16.971 -50.772 2.489   1.00 55.26  ?  192 SER   A OG  1 
ATOM   1235 N  N   . LEU   A 1 161 ? -17.701 -48.093 3.401   1.00 54.19  ?  193 LEU   A N   1 
ATOM   1236 C  CA  . LEU   A 1 161 ? -18.466 -46.871 3.230   1.00 57.03  ?  193 LEU   A CA  1 
ATOM   1237 C  C   . LEU   A 1 161 ? -19.945 -47.116 3.467   1.00 55.83  ?  193 LEU   A C   1 
ATOM   1238 O  O   . LEU   A 1 161 ? -20.494 -48.105 2.999   1.00 55.58  ?  193 LEU   A O   1 
ATOM   1239 C  CB  . LEU   A 1 161 ? -18.279 -46.346 1.821   1.00 58.46  ?  193 LEU   A CB  1 
ATOM   1240 C  CG  . LEU   A 1 161 ? -18.984 -45.067 1.436   1.00 47.81  ?  193 LEU   A CG  1 
ATOM   1241 C  CD1 . LEU   A 1 161 ? -18.302 -43.950 2.088   1.00 48.19  ?  193 LEU   A CD1 1 
ATOM   1242 C  CD2 . LEU   A 1 161 ? -18.950 -44.903 -0.034  1.00 47.69  ?  193 LEU   A CD2 1 
ATOM   1243 N  N   . GLN   A 1 162 ? -20.593 -46.184 4.148   1.00 59.78  ?  194 GLN   A N   1 
ATOM   1244 C  CA  . GLN   A 1 162 ? -22.011 -46.255 4.449   1.00 56.16  ?  194 GLN   A CA  1 
ATOM   1245 C  C   . GLN   A 1 162 ? -22.632 -44.922 4.071   1.00 54.77  ?  194 GLN   A C   1 
ATOM   1246 O  O   . GLN   A 1 162 ? -22.013 -43.877 4.249   1.00 50.95  ?  194 GLN   A O   1 
ATOM   1247 C  CB  . GLN   A 1 162 ? -22.231 -46.561 5.927   1.00 55.31  ?  194 GLN   A CB  1 
ATOM   1248 C  CG  . GLN   A 1 162 ? -23.634 -46.836 6.339   1.00 48.25  ?  194 GLN   A CG  1 
ATOM   1249 C  CD  . GLN   A 1 162 ? -23.748 -47.269 7.793   1.00 50.47  ?  194 GLN   A CD  1 
ATOM   1250 O  OE1 . GLN   A 1 162 ? -23.440 -46.535 8.713   1.00 47.98  ?  194 GLN   A OE1 1 
ATOM   1251 N  NE2 . GLN   A 1 162 ? -24.182 -48.472 7.991   1.00 55.13  ?  194 GLN   A NE2 1 
ATOM   1252 N  N   . LEU   A 1 163 ? -23.838 -44.962 3.525   1.00 60.00  ?  195 LEU   A N   1 
ATOM   1253 C  CA  . LEU   A 1 163 ? -24.640 -43.780 3.265   1.00 42.86  ?  195 LEU   A CA  1 
ATOM   1254 C  C   . LEU   A 1 163 ? -25.862 -43.807 4.156   1.00 47.98  ?  195 LEU   A C   1 
ATOM   1255 O  O   . LEU   A 1 163 ? -26.530 -44.830 4.248   1.00 55.87  ?  195 LEU   A O   1 
ATOM   1256 C  CB  . LEU   A 1 163 ? -25.096 -43.743 1.832   1.00 36.13  ?  195 LEU   A CB  1 
ATOM   1257 C  CG  . LEU   A 1 163 ? -24.008 -43.813 0.796   1.00 46.80  ?  195 LEU   A CG  1 
ATOM   1258 C  CD1 . LEU   A 1 163 ? -24.586 -43.498 -0.512  1.00 48.14  ?  195 LEU   A CD1 1 
ATOM   1259 C  CD2 . LEU   A 1 163 ? -22.929 -42.854 1.078   1.00 48.70  ?  195 LEU   A CD2 1 
ATOM   1260 N  N   . ILE   A 1 164 ? -26.160 -42.697 4.806   1.00 50.00  ?  196 ILE   A N   1 
ATOM   1261 C  CA  . ILE   A 1 164 ? -27.362 -42.569 5.606   1.00 44.58  ?  196 ILE   A CA  1 
ATOM   1262 C  C   . ILE   A 1 164 ? -28.112 -41.366 5.088   1.00 46.35  ?  196 ILE   A C   1 
ATOM   1263 O  O   . ILE   A 1 164 ? -27.525 -40.292 4.956   1.00 43.30  ?  196 ILE   A O   1 
ATOM   1264 C  CB  . ILE   A 1 164 ? -27.049 -42.382 7.088   1.00 42.05  ?  196 ILE   A CB  1 
ATOM   1265 C  CG1 . ILE   A 1 164 ? -26.202 -43.528 7.578   1.00 40.76  ?  196 ILE   A CG1 1 
ATOM   1266 C  CG2 . ILE   A 1 164 ? -28.308 -42.245 7.862   1.00 41.08  ?  196 ILE   A CG2 1 
ATOM   1267 C  CD1 . ILE   A 1 164 ? -25.749 -43.336 8.980   1.00 44.03  ?  196 ILE   A CD1 1 
ATOM   1268 N  N   . PHE   A 1 165 ? -29.395 -41.540 4.795   1.00 48.21  ?  197 PHE   A N   1 
ATOM   1269 C  CA  . PHE   A 1 165 ? -30.290 -40.447 4.434   1.00 41.48  ?  197 PHE   A CA  1 
ATOM   1270 C  C   . PHE   A 1 165 ? -31.381 -40.353 5.493   1.00 39.51  ?  197 PHE   A C   1 
ATOM   1271 O  O   . PHE   A 1 165 ? -32.382 -41.052 5.408   1.00 41.63  ?  197 PHE   A O   1 
ATOM   1272 C  CB  . PHE   A 1 165 ? -30.925 -40.676 3.083   1.00 40.57  ?  197 PHE   A CB  1 
ATOM   1273 C  CG  . PHE   A 1 165 ? -29.973 -40.937 1.960   1.00 41.52  ?  197 PHE   A CG  1 
ATOM   1274 C  CD1 . PHE   A 1 165 ? -29.402 -42.160 1.804   1.00 45.45  ?  197 PHE   A CD1 1 
ATOM   1275 C  CD2 . PHE   A 1 165 ? -29.745 -39.993 0.992   1.00 43.19  ?  197 PHE   A CD2 1 
ATOM   1276 C  CE1 . PHE   A 1 165 ? -28.590 -42.421 0.740   1.00 44.56  ?  197 PHE   A CE1 1 
ATOM   1277 C  CE2 . PHE   A 1 165 ? -28.921 -40.273 -0.060  1.00 45.15  ?  197 PHE   A CE2 1 
ATOM   1278 C  CZ  . PHE   A 1 165 ? -28.350 -41.485 -0.173  1.00 38.93  ?  197 PHE   A CZ  1 
ATOM   1279 N  N   . PHE   A 1 166 ? -31.219 -39.486 6.472   1.00 39.87  ?  198 PHE   A N   1 
ATOM   1280 C  CA  . PHE   A 1 166 ? -32.150 -39.442 7.579   1.00 32.69  ?  198 PHE   A CA  1 
ATOM   1281 C  C   . PHE   A 1 166 ? -33.486 -38.892 7.148   1.00 33.23  ?  198 PHE   A C   1 
ATOM   1282 O  O   . PHE   A 1 166 ? -33.567 -38.028 6.293   1.00 35.93  ?  198 PHE   A O   1 
ATOM   1283 C  CB  . PHE   A 1 166 ? -31.614 -38.548 8.674   1.00 43.62  ?  198 PHE   A CB  1 
ATOM   1284 C  CG  . PHE   A 1 166 ? -30.362 -39.041 9.307   1.00 48.41  ?  198 PHE   A CG  1 
ATOM   1285 C  CD1 . PHE   A 1 166 ? -30.380 -40.086 10.193  1.00 47.73  ?  198 PHE   A CD1 1 
ATOM   1286 C  CD2 . PHE   A 1 166 ? -29.169 -38.438 9.042   1.00 51.41  ?  198 PHE   A CD2 1 
ATOM   1287 C  CE1 . PHE   A 1 166 ? -29.256 -40.523 10.769  1.00 49.69  ?  198 PHE   A CE1 1 
ATOM   1288 C  CE2 . PHE   A 1 166 ? -28.032 -38.889 9.623   1.00 51.49  ?  198 PHE   A CE2 1 
ATOM   1289 C  CZ  . PHE   A 1 166 ? -28.085 -39.935 10.487  1.00 56.00  ?  198 PHE   A CZ  1 
ATOM   1290 N  N   . ASP   A 1 167 ? -34.535 -39.354 7.795   1.00 38.77  ?  199 ASP   A N   1 
ATOM   1291 C  CA  . ASP   A 1 167 ? -35.859 -38.776 7.665   1.00 34.50  ?  199 ASP   A CA  1 
ATOM   1292 C  C   . ASP   A 1 167 ? -36.120 -37.955 8.900   1.00 28.88  ?  199 ASP   A C   1 
ATOM   1293 O  O   . ASP   A 1 167 ? -35.469 -38.112 9.920   1.00 34.40  ?  199 ASP   A O   1 
ATOM   1294 C  CB  . ASP   A 1 167 ? -36.938 -39.846 7.498   1.00 38.51  ?  199 ASP   A CB  1 
ATOM   1295 C  CG  . ASP   A 1 167 ? -38.253 -39.309 6.963   1.00 39.07  ?  199 ASP   A CG  1 
ATOM   1296 O  OD1 . ASP   A 1 167 ? -38.424 -38.114 6.711   1.00 37.08  ?  199 ASP   A OD1 1 
ATOM   1297 O  OD2 . ASP   A 1 167 ? -39.164 -40.113 6.795   1.00 45.57  ?  199 ASP   A OD2 1 
ATOM   1298 N  N   . GLY   A 1 168 ? -37.034 -37.014 8.769   1.00 32.33  ?  200 GLY   A N   1 
ATOM   1299 C  CA  . GLY   A 1 168 ? -37.428 -36.202 9.895   1.00 32.63  ?  200 GLY   A CA  1 
ATOM   1300 C  C   . GLY   A 1 168 ? -36.328 -35.367 10.497  1.00 37.89  ?  200 GLY   A C   1 
ATOM   1301 O  O   . GLY   A 1 168 ? -36.275 -35.210 11.719  1.00 44.21  ?  200 GLY   A O   1 
ATOM   1302 N  N   . GLU   A 1 169 ? -35.473 -34.779 9.679   1.00 37.39  ?  201 GLU   A N   1 
ATOM   1303 C  CA  . GLU   A 1 169 ? -34.529 -33.858 10.276  1.00 36.46  ?  201 GLU   A CA  1 
ATOM   1304 C  C   . GLU   A 1 169 ? -35.256 -32.644 10.761  1.00 34.80  ?  201 GLU   A C   1 
ATOM   1305 O  O   . GLU   A 1 169 ? -34.992 -32.151 11.850  1.00 33.55  ?  201 GLU   A O   1 
ATOM   1306 C  CB  . GLU   A 1 169 ? -33.443 -33.448 9.301   1.00 38.28  ?  201 GLU   A CB  1 
ATOM   1307 C  CG  . GLU   A 1 169 ? -32.353 -32.640 9.926   1.00 44.46  ?  201 GLU   A CG  1 
ATOM   1308 C  CD  . GLU   A 1 169 ? -32.645 -31.181 9.956   1.00 43.83  ?  201 GLU   A CD  1 
ATOM   1309 O  OE1 . GLU   A 1 169 ? -33.432 -30.748 9.120   1.00 38.04  ?  201 GLU   A OE1 1 
ATOM   1310 O  OE2 . GLU   A 1 169 ? -32.094 -30.459 10.806  1.00 41.09  ?  201 GLU   A OE2 1 
ATOM   1311 N  N   . GLU   A 1 170 ? -36.149 -32.174 9.955   1.00 42.95  ?  202 GLU   A N   1 
ATOM   1312 C  CA  . GLU   A 1 170 ? -36.826 -30.948 10.239  1.00 43.81  ?  202 GLU   A CA  1 
ATOM   1313 C  C   . GLU   A 1 170 ? -37.899 -30.952 11.225  1.00 40.15  ?  202 GLU   A C   1 
ATOM   1314 O  O   . GLU   A 1 170 ? -38.504 -31.936 11.475  1.00 45.86  ?  202 GLU   A O   1 
ATOM   1315 C  CB  . GLU   A 1 170 ? -37.357 -30.404 8.955   1.00 42.31  ?  202 GLU   A CB  1 
ATOM   1316 C  CG  . GLU   A 1 170 ? -36.244 -30.194 7.987   1.00 45.41  ?  202 GLU   A CG  1 
ATOM   1317 C  CD  . GLU   A 1 170 ? -35.654 -28.855 8.115   1.00 38.96  ?  202 GLU   A CD  1 
ATOM   1318 O  OE1 . GLU   A 1 170 ? -35.772 -28.240 9.161   1.00 50.47  ?  202 GLU   A OE1 1 
ATOM   1319 O  OE2 . GLU   A 1 170 ? -35.105 -28.414 7.155   1.00 33.04  ?  202 GLU   A OE2 1 
ATOM   1320 N  N   . ALA   A 1 171 ? -38.140 -29.797 11.786  1.00 35.96  ?  203 ALA   A N   1 
ATOM   1321 C  CA  . ALA   A 1 171 ? -39.199 -29.690 12.747  1.00 34.53  ?  203 ALA   A CA  1 
ATOM   1322 C  C   . ALA   A 1 171 ? -40.547 -29.577 12.073  1.00 48.09  ?  203 ALA   A C   1 
ATOM   1323 O  O   . ALA   A 1 171 ? -40.676 -29.006 10.995  1.00 51.56  ?  203 ALA   A O   1 
ATOM   1324 C  CB  . ALA   A 1 171 ? -38.986 -28.467 13.586  1.00 42.77  ?  203 ALA   A CB  1 
ATOM   1325 N  N   . PHE   A 1 172 ? -41.571 -30.099 12.729  1.00 46.77  ?  204 PHE   A N   1 
ATOM   1326 C  CA  . PHE   A 1 172 ? -42.899 -29.902 12.183  1.00 49.06  ?  204 PHE   A CA  1 
ATOM   1327 C  C   . PHE   A 1 172 ? -43.411 -28.515 12.498  1.00 50.18  ?  204 PHE   A C   1 
ATOM   1328 O  O   . PHE   A 1 172 ? -44.112 -27.923 11.684  1.00 46.90  ?  204 PHE   A O   1 
ATOM   1329 C  CB  . PHE   A 1 172 ? -43.854 -30.947 12.723  1.00 58.54  ?  204 PHE   A CB  1 
ATOM   1330 C  CG  . PHE   A 1 172 ? -43.743 -32.277 12.055  1.00 59.23  ?  204 PHE   A CG  1 
ATOM   1331 C  CD1 . PHE   A 1 172 ? -44.466 -32.556 10.932  1.00 66.05  ?  204 PHE   A CD1 1 
ATOM   1332 C  CD2 . PHE   A 1 172 ? -42.933 -33.247 12.557  1.00 45.71  ?  204 PHE   A CD2 1 
ATOM   1333 C  CE1 . PHE   A 1 172 ? -44.356 -33.756 10.349  1.00 65.30  ?  204 PHE   A CE1 1 
ATOM   1334 C  CE2 . PHE   A 1 172 ? -42.835 -34.429 11.963  1.00 40.86  ?  204 PHE   A CE2 1 
ATOM   1335 C  CZ  . PHE   A 1 172 ? -43.540 -34.693 10.885  1.00 50.55  ?  204 PHE   A CZ  1 
ATOM   1336 N  N   . LEU   A 1 173 ? -43.033 -27.973 13.647  1.00 51.33  ?  205 LEU   A N   1 
ATOM   1337 C  CA  . LEU   A 1 173 ? -43.570 -26.711 14.114  1.00 62.95  ?  205 LEU   A CA  1 
ATOM   1338 C  C   . LEU   A 1 173 ? -42.470 -25.689 14.312  1.00 75.02  ?  205 LEU   A C   1 
ATOM   1339 O  O   . LEU   A 1 173 ? -42.314 -24.774 13.502  1.00 93.22  ?  205 LEU   A O   1 
ATOM   1340 C  CB  . LEU   A 1 173 ? -44.308 -26.896 15.433  1.00 76.32  ?  205 LEU   A CB  1 
ATOM   1341 C  CG  . LEU   A 1 173 ? -45.743 -26.429 15.520  1.00 73.71  ?  205 LEU   A CG  1 
ATOM   1342 C  CD1 . LEU   A 1 173 ? -45.974 -25.062 14.829  1.00 75.14  ?  205 LEU   A CD1 1 
ATOM   1343 C  CD2 . LEU   A 1 173 ? -46.550 -27.537 14.949  1.00 70.62  ?  205 LEU   A CD2 1 
ATOM   1344 N  N   . HIS   A 1 174 ? -41.716 -25.820 15.394  1.00 65.80  ?  206 HIS   A N   1 
ATOM   1345 C  CA  . HIS   A 1 174 ? -40.696 -24.848 15.719  1.00 61.69  ?  206 HIS   A CA  1 
ATOM   1346 C  C   . HIS   A 1 174 ? -39.507 -25.567 16.319  1.00 59.11  ?  206 HIS   A C   1 
ATOM   1347 O  O   . HIS   A 1 174 ? -39.658 -26.485 17.124  1.00 60.02  ?  206 HIS   A O   1 
ATOM   1348 C  CB  . HIS   A 1 174 ? -41.227 -23.760 16.661  1.00 66.63  ?  206 HIS   A CB  1 
ATOM   1349 C  CG  . HIS   A 1 174 ? -41.720 -24.264 17.981  1.00 76.27  ?  206 HIS   A CG  1 
ATOM   1350 N  ND1 . HIS   A 1 174 ? -40.878 -24.574 19.026  1.00 75.54  ?  206 HIS   A ND1 1 
ATOM   1351 C  CD2 . HIS   A 1 174 ? -42.977 -24.481 18.438  1.00 87.06  ?  206 HIS   A CD2 1 
ATOM   1352 C  CE1 . HIS   A 1 174 ? -41.590 -24.982 20.062  1.00 78.17  ?  206 HIS   A CE1 1 
ATOM   1353 N  NE2 . HIS   A 1 174 ? -42.868 -24.933 19.732  1.00 87.70  ?  206 HIS   A NE2 1 
ATOM   1354 N  N   . TRP   A 1 175 ? -38.328 -25.133 15.913  1.00 59.30  ?  207 TRP   A N   1 
ATOM   1355 C  CA  . TRP   A 1 175 ? -37.117 -25.865 16.213  1.00 58.31  ?  207 TRP   A CA  1 
ATOM   1356 C  C   . TRP   A 1 175 ? -36.995 -26.043 17.710  1.00 50.20  ?  207 TRP   A C   1 
ATOM   1357 O  O   . TRP   A 1 175 ? -37.080 -25.084 18.470  1.00 51.11  ?  207 TRP   A O   1 
ATOM   1358 C  CB  . TRP   A 1 175 ? -35.915 -25.119 15.633  1.00 63.80  ?  207 TRP   A CB  1 
ATOM   1359 C  CG  . TRP   A 1 175 ? -34.642 -25.883 15.610  1.00 64.53  ?  207 TRP   A CG  1 
ATOM   1360 C  CD1 . TRP   A 1 175 ? -33.531 -25.629 16.340  1.00 72.35  ?  207 TRP   A CD1 1 
ATOM   1361 C  CD2 . TRP   A 1 175 ? -34.347 -27.035 14.821  1.00 62.76  ?  207 TRP   A CD2 1 
ATOM   1362 N  NE1 . TRP   A 1 175 ? -32.558 -26.553 16.059  1.00 71.68  ?  207 TRP   A NE1 1 
ATOM   1363 C  CE2 . TRP   A 1 175 ? -33.040 -27.424 15.124  1.00 64.27  ?  207 TRP   A CE2 1 
ATOM   1364 C  CE3 . TRP   A 1 175 ? -35.060 -27.769 13.877  1.00 62.58  ?  207 TRP   A CE3 1 
ATOM   1365 C  CZ2 . TRP   A 1 175 ? -32.439 -28.505 14.526  1.00 67.63  ?  207 TRP   A CZ2 1 
ATOM   1366 C  CZ3 . TRP   A 1 175 ? -34.462 -28.842 13.289  1.00 54.87  ?  207 TRP   A CZ3 1 
ATOM   1367 C  CH2 . TRP   A 1 175 ? -33.167 -29.202 13.609  1.00 61.83  ?  207 TRP   A CH2 1 
ATOM   1368 N  N   . SER   A 1 176 ? -36.829 -27.281 18.137  1.00 47.11  ?  208 SER   A N   1 
ATOM   1369 C  CA  . SER   A 1 176 ? -36.636 -27.565 19.545  1.00 60.70  ?  208 SER   A CA  1 
ATOM   1370 C  C   . SER   A 1 176 ? -36.055 -28.954 19.677  1.00 61.81  ?  208 SER   A C   1 
ATOM   1371 O  O   . SER   A 1 176 ? -36.118 -29.743 18.731  1.00 66.89  ?  208 SER   A O   1 
ATOM   1372 C  CB  . SER   A 1 176 ? -37.950 -27.476 20.311  1.00 67.73  ?  208 SER   A CB  1 
ATOM   1373 O  OG  . SER   A 1 176 ? -38.670 -28.669 20.130  1.00 68.14  ?  208 SER   A OG  1 
ATOM   1374 N  N   . PRO   A 1 177 ? -35.487 -29.291 20.829  1.00 55.55  ?  209 PRO   A N   1 
ATOM   1375 C  CA  . PRO   A 1 177 ? -34.853 -30.600 20.972  1.00 67.50  ?  209 PRO   A CA  1 
ATOM   1376 C  C   . PRO   A 1 177 ? -35.846 -31.713 20.918  1.00 66.06  ?  209 PRO   A C   1 
ATOM   1377 O  O   . PRO   A 1 177 ? -35.468 -32.864 20.669  1.00 61.70  ?  209 PRO   A O   1 
ATOM   1378 C  CB  . PRO   A 1 177 ? -34.190 -30.520 22.350  1.00 68.38  ?  209 PRO   A CB  1 
ATOM   1379 C  CG  . PRO   A 1 177 ? -34.143 -29.085 22.658  1.00 56.77  ?  209 PRO   A CG  1 
ATOM   1380 C  CD  . PRO   A 1 177 ? -35.355 -28.513 22.054  1.00 58.17  ?  209 PRO   A CD  1 
ATOM   1381 N  N   . GLN   A 1 178 ? -37.106 -31.389 21.150  1.00 66.49  ?  210 GLN   A N   1 
ATOM   1382 C  CA  . GLN   A 1 178 ? -38.176 -32.358 21.178  1.00 66.45  ?  210 GLN   A CA  1 
ATOM   1383 C  C   . GLN   A 1 178 ? -38.868 -32.484 19.835  1.00 66.23  ?  210 GLN   A C   1 
ATOM   1384 O  O   . GLN   A 1 178 ? -39.490 -33.519 19.568  1.00 61.10  ?  210 GLN   A O   1 
ATOM   1385 C  CB  . GLN   A 1 178 ? -39.205 -31.981 22.247  1.00 73.78  ?  210 GLN   A CB  1 
ATOM   1386 C  CG  . GLN   A 1 178 ? -39.216 -30.529 22.743  1.00 90.30  ?  210 GLN   A CG  1 
ATOM   1387 C  CD  . GLN   A 1 178 ? -38.331 -30.299 23.943  1.00 93.34  ?  210 GLN   A CD  1 
ATOM   1388 O  OE1 . GLN   A 1 178 ? -37.782 -31.243 24.506  1.00 98.70  ?  210 GLN   A OE1 1 
ATOM   1389 N  NE2 . GLN   A 1 178 ? -38.206 -29.040 24.360  1.00 83.75  ?  210 GLN   A NE2 1 
ATOM   1390 N  N   . ASP   A 1 179 ? -38.766 -31.453 18.997  1.00 61.27  ?  211 ASP   A N   1 
ATOM   1391 C  CA  . ASP   A 1 179 ? -39.295 -31.411 17.634  1.00 49.52  ?  211 ASP   A CA  1 
ATOM   1392 C  C   . ASP   A 1 179 ? -38.134 -31.228 16.649  1.00 53.87  ?  211 ASP   A C   1 
ATOM   1393 O  O   . ASP   A 1 179 ? -37.896 -30.129 16.161  1.00 53.09  ?  211 ASP   A O   1 
ATOM   1394 C  CB  . ASP   A 1 179 ? -40.235 -30.326 17.538  1.00 43.55  ?  211 ASP   A CB  1 
ATOM   1395 C  CG  . ASP   A 1 179 ? -41.032 -30.369 16.300  1.00 42.81  ?  211 ASP   A CG  1 
ATOM   1396 O  OD1 . ASP   A 1 179 ? -41.094 -31.446 15.713  1.00 50.42  ?  211 ASP   A OD1 1 
ATOM   1397 O  OD2 . ASP   A 1 179 ? -41.620 -29.350 15.921  1.00 43.28  ?  211 ASP   A OD2 1 
ATOM   1398 N  N   . SER   A 1 180 ? -37.429 -32.312 16.340  1.00 47.00  ?  212 SER   A N   1 
ATOM   1399 C  CA  . SER   A 1 180 ? -36.258 -32.248 15.488  1.00 40.15  ?  212 SER   A CA  1 
ATOM   1400 C  C   . SER   A 1 180 ? -35.481 -33.551 15.517  1.00 42.51  ?  212 SER   A C   1 
ATOM   1401 O  O   . SER   A 1 180 ? -35.462 -34.260 16.514  1.00 51.61  ?  212 SER   A O   1 
ATOM   1402 C  CB  . SER   A 1 180 ? -35.331 -31.136 15.912  1.00 44.32  ?  212 SER   A CB  1 
ATOM   1403 O  OG  . SER   A 1 180 ? -34.741 -31.448 17.138  1.00 56.71  ?  212 SER   A OG  1 
ATOM   1404 N  N   . LEU   A 1 181 ? -34.822 -33.890 14.437  1.00 40.95  ?  213 LEU   A N   1 
ATOM   1405 C  CA  . LEU   A 1 181 ? -33.864 -34.969 14.463  1.00 44.74  ?  213 LEU   A CA  1 
ATOM   1406 C  C   . LEU   A 1 181 ? -34.543 -36.293 14.752  1.00 48.13  ?  213 LEU   A C   1 
ATOM   1407 O  O   . LEU   A 1 181 ? -33.958 -37.205 15.316  1.00 54.36  ?  213 LEU   A O   1 
ATOM   1408 C  CB  . LEU   A 1 181 ? -32.760 -34.670 15.474  1.00 49.05  ?  213 LEU   A CB  1 
ATOM   1409 C  CG  . LEU   A 1 181 ? -32.175 -33.266 15.330  1.00 43.56  ?  213 LEU   A CG  1 
ATOM   1410 C  CD1 . LEU   A 1 181 ? -31.221 -32.950 16.394  1.00 49.08  ?  213 LEU   A CD1 1 
ATOM   1411 C  CD2 . LEU   A 1 181 ? -31.471 -33.194 14.058  1.00 50.49  ?  213 LEU   A CD2 1 
ATOM   1412 N  N   . TYR   A 1 182 ? -35.778 -36.434 14.315  1.00 50.16  ?  214 TYR   A N   1 
ATOM   1413 C  CA  . TYR   A 1 182 ? -36.490 -37.674 14.545  1.00 41.43  ?  214 TYR   A CA  1 
ATOM   1414 C  C   . TYR   A 1 182 ? -35.745 -38.877 14.019  1.00 41.56  ?  214 TYR   A C   1 
ATOM   1415 O  O   . TYR   A 1 182 ? -35.711 -39.916 14.669  1.00 52.02  ?  214 TYR   A O   1 
ATOM   1416 C  CB  . TYR   A 1 182 ? -37.849 -37.597 13.902  1.00 38.53  ?  214 TYR   A CB  1 
ATOM   1417 C  CG  . TYR   A 1 182 ? -38.704 -36.555 14.517  1.00 37.97  ?  214 TYR   A CG  1 
ATOM   1418 C  CD1 . TYR   A 1 182 ? -39.287 -36.744 15.731  1.00 40.99  ?  214 TYR   A CD1 1 
ATOM   1419 C  CD2 . TYR   A 1 182 ? -38.910 -35.385 13.889  1.00 44.65  ?  214 TYR   A CD2 1 
ATOM   1420 C  CE1 . TYR   A 1 182 ? -40.052 -35.806 16.279  1.00 39.65  ?  214 TYR   A CE1 1 
ATOM   1421 C  CE2 . TYR   A 1 182 ? -39.677 -34.437 14.443  1.00 47.00  ?  214 TYR   A CE2 1 
ATOM   1422 C  CZ  . TYR   A 1 182 ? -40.246 -34.657 15.633  1.00 39.47  ?  214 TYR   A CZ  1 
ATOM   1423 O  OH  . TYR   A 1 182 ? -41.023 -33.687 16.167  1.00 42.85  ?  214 TYR   A OH  1 
ATOM   1424 N  N   . GLY   A 1 183 ? -35.171 -38.783 12.835  1.00 49.10  ?  215 GLY   A N   1 
ATOM   1425 C  CA  . GLY   A 1 183 ? -34.582 -39.972 12.256  1.00 44.70  ?  215 GLY   A CA  1 
ATOM   1426 C  C   . GLY   A 1 183 ? -33.177 -40.211 12.709  1.00 47.56  ?  215 GLY   A C   1 
ATOM   1427 O  O   . GLY   A 1 183 ? -32.660 -41.313 12.532  1.00 45.56  ?  215 GLY   A O   1 
ATOM   1428 N  N   . SER   A 1 184 ? -32.543 -39.196 13.275  1.00 45.63  ?  216 SER   A N   1 
ATOM   1429 C  CA  . SER   A 1 184 ? -31.187 -39.341 13.746  1.00 45.98  ?  216 SER   A CA  1 
ATOM   1430 C  C   . SER   A 1 184 ? -31.173 -39.791 15.185  1.00 46.03  ?  216 SER   A C   1 
ATOM   1431 O  O   . SER   A 1 184 ? -30.494 -40.755 15.525  1.00 48.83  ?  216 SER   A O   1 
ATOM   1432 C  CB  . SER   A 1 184 ? -30.442 -38.026 13.612  1.00 48.04  ?  216 SER   A CB  1 
ATOM   1433 O  OG  . SER   A 1 184 ? -31.343 -36.978 13.366  1.00 58.22  ?  216 SER   A OG  1 
ATOM   1434 N  N   . ARG   A 1 185 ? -31.922 -39.098 16.035  1.00 45.16  ?  217 ARG   A N   1 
ATOM   1435 C  CA  . ARG   A 1 185 ? -32.062 -39.520 17.418  1.00 41.20  ?  217 ARG   A CA  1 
ATOM   1436 C  C   . ARG   A 1 185 ? -32.435 -40.986 17.533  1.00 41.16  ?  217 ARG   A C   1 
ATOM   1437 O  O   . ARG   A 1 185 ? -32.090 -41.635 18.511  1.00 45.07  ?  217 ARG   A O   1 
ATOM   1438 C  CB  . ARG   A 1 185 ? -33.098 -38.664 18.110  1.00 32.02  ?  217 ARG   A CB  1 
ATOM   1439 C  CG  . ARG   A 1 185 ? -32.699 -37.262 18.227  1.00 43.03  ?  217 ARG   A CG  1 
ATOM   1440 C  CD  . ARG   A 1 185 ? -33.507 -36.488 19.237  1.00 52.66  ?  217 ARG   A CD  1 
ATOM   1441 N  NE  . ARG   A 1 185 ? -34.801 -36.069 18.742  1.00 56.34  ?  217 ARG   A NE  1 
ATOM   1442 C  CZ  . ARG   A 1 185 ? -35.892 -36.829 18.735  1.00 51.14  ?  217 ARG   A CZ  1 
ATOM   1443 N  NH1 . ARG   A 1 185 ? -35.881 -38.061 19.184  1.00 53.06  ?  217 ARG   A NH1 1 
ATOM   1444 N  NH2 . ARG   A 1 185 ? -37.012 -36.356 18.273  1.00 52.19  ?  217 ARG   A NH2 1 
ATOM   1445 N  N   . HIS   A 1 186 ? -33.098 -41.532 16.541  1.00 43.01  ?  218 HIS   A N   1 
ATOM   1446 C  CA  . HIS   A 1 186 ? -33.537 -42.907 16.589  1.00 41.80  ?  218 HIS   A CA  1 
ATOM   1447 C  C   . HIS   A 1 186 ? -32.485 -43.862 16.094  1.00 51.22  ?  218 HIS   A C   1 
ATOM   1448 O  O   . HIS   A 1 186 ? -32.337 -44.943 16.649  1.00 62.51  ?  218 HIS   A O   1 
ATOM   1449 C  CB  . HIS   A 1 186 ? -34.792 -43.078 15.754  1.00 49.91  ?  218 HIS   A CB  1 
ATOM   1450 C  CG  . HIS   A 1 186 ? -35.216 -44.498 15.581  1.00 48.58  ?  218 HIS   A CG  1 
ATOM   1451 N  ND1 . HIS   A 1 186 ? -34.859 -45.256 14.488  1.00 47.55  ?  218 HIS   A ND1 1 
ATOM   1452 C  CD2 . HIS   A 1 186 ? -35.999 -45.287 16.347  1.00 44.81  ?  218 HIS   A CD2 1 
ATOM   1453 C  CE1 . HIS   A 1 186 ? -35.387 -46.460 14.598  1.00 48.34  ?  218 HIS   A CE1 1 
ATOM   1454 N  NE2 . HIS   A 1 186 ? -36.084 -46.503 15.719  1.00 52.86  ?  218 HIS   A NE2 1 
ATOM   1455 N  N   . LEU   A 1 187 ? -31.754 -43.506 15.052  1.00 56.82  ?  219 LEU   A N   1 
ATOM   1456 C  CA  . LEU   A 1 187 ? -30.720 -44.403 14.577  1.00 48.00  ?  219 LEU   A CA  1 
ATOM   1457 C  C   . LEU   A 1 187 ? -29.491 -44.329 15.448  1.00 45.59  ?  219 LEU   A C   1 
ATOM   1458 O  O   . LEU   A 1 187 ? -28.768 -45.304 15.558  1.00 53.78  ?  219 LEU   A O   1 
ATOM   1459 C  CB  . LEU   A 1 187 ? -30.361 -44.083 13.139  1.00 49.37  ?  219 LEU   A CB  1 
ATOM   1460 C  CG  . LEU   A 1 187 ? -29.546 -45.154 12.433  1.00 51.44  ?  219 LEU   A CG  1 
ATOM   1461 C  CD1 . LEU   A 1 187 ? -30.331 -46.381 12.268  1.00 60.19  ?  219 LEU   A CD1 1 
ATOM   1462 C  CD2 . LEU   A 1 187 ? -29.084 -44.699 11.090  1.00 39.58  ?  219 LEU   A CD2 1 
ATOM   1463 N  N   . ALA   A 1 188 ? -29.217 -43.202 16.077  1.00 42.05  ?  220 ALA   A N   1 
ATOM   1464 C  CA  . ALA   A 1 188 ? -28.106 -43.182 17.007  1.00 51.89  ?  220 ALA   A CA  1 
ATOM   1465 C  C   . ALA   A 1 188 ? -28.302 -44.251 18.061  1.00 62.30  ?  220 ALA   A C   1 
ATOM   1466 O  O   . ALA   A 1 188 ? -27.422 -45.092 18.302  1.00 53.11  ?  220 ALA   A O   1 
ATOM   1467 C  CB  . ALA   A 1 188 ? -27.983 -41.807 17.655  1.00 53.00  ?  220 ALA   A CB  1 
ATOM   1468 N  N   . ALA   A 1 189 ? -29.495 -44.270 18.651  1.00 63.70  ?  221 ALA   A N   1 
ATOM   1469 C  CA  . ALA   A 1 189 ? -29.765 -45.146 19.771  1.00 51.00  ?  221 ALA   A CA  1 
ATOM   1470 C  C   . ALA   A 1 189 ? -29.733 -46.594 19.344  1.00 46.43  ?  221 ALA   A C   1 
ATOM   1471 O  O   . ALA   A 1 189 ? -29.080 -47.420 19.973  1.00 60.54  ?  221 ALA   A O   1 
ATOM   1472 C  CB  . ALA   A 1 189 ? -31.100 -44.783 20.355  1.00 47.71  ?  221 ALA   A CB  1 
ATOM   1473 N  N   . LYS   A 1 190 ? -30.420 -46.917 18.266  1.00 46.57  ?  222 LYS   A N   1 
ATOM   1474 C  CA  . LYS   A 1 190 ? -30.444 -48.284 17.770  1.00 49.41  ?  222 LYS   A CA  1 
ATOM   1475 C  C   . LYS   A 1 190 ? -29.041 -48.792 17.489  1.00 55.62  ?  222 LYS   A C   1 
ATOM   1476 O  O   . LYS   A 1 190 ? -28.675 -49.904 17.889  1.00 55.09  ?  222 LYS   A O   1 
ATOM   1477 C  CB  . LYS   A 1 190 ? -31.319 -48.332 16.528  1.00 48.15  ?  222 LYS   A CB  1 
ATOM   1478 C  CG  . LYS   A 1 190 ? -31.303 -49.587 15.750  1.00 47.19  ?  222 LYS   A CG  1 
ATOM   1479 C  CD  . LYS   A 1 190 ? -32.497 -49.576 14.878  1.00 47.31  ?  222 LYS   A CD  1 
ATOM   1480 C  CE  . LYS   A 1 190 ? -32.465 -50.632 13.837  1.00 61.06  ?  222 LYS   A CE  1 
ATOM   1481 N  NZ  . LYS   A 1 190 ? -33.830 -50.814 13.293  1.00 73.05  ?  222 LYS   A NZ  1 
ATOM   1482 N  N   . MET   A 1 191 ? -28.237 -47.978 16.806  1.00 66.68  ?  223 MET   A N   1 
ATOM   1483 C  CA  . MET   A 1 191 ? -26.836 -48.305 16.575  1.00 64.02  ?  223 MET   A CA  1 
ATOM   1484 C  C   . MET   A 1 191 ? -26.104 -48.479 17.888  1.00 71.17  ?  223 MET   A C   1 
ATOM   1485 O  O   . MET   A 1 191 ? -25.439 -49.493 18.111  1.00 75.77  ?  223 MET   A O   1 
ATOM   1486 C  CB  . MET   A 1 191 ? -26.173 -47.204 15.762  1.00 63.18  ?  223 MET   A CB  1 
ATOM   1487 C  CG  . MET   A 1 191 ? -26.669 -47.072 14.365  1.00 63.75  ?  223 MET   A CG  1 
ATOM   1488 S  SD  . MET   A 1 191 ? -25.529 -46.128 13.383  1.00 51.39  ?  223 MET   A SD  1 
ATOM   1489 C  CE  . MET   A 1 191 ? -25.286 -47.326 12.103  1.00 55.22  ?  223 MET   A CE  1 
ATOM   1490 N  N   . ALA   A 1 192 ? -26.220 -47.499 18.783  1.00 60.38  ?  224 ALA   A N   1 
ATOM   1491 C  CA  . ALA   A 1 192 ? -25.494 -47.593 20.031  1.00 58.48  ?  224 ALA   A CA  1 
ATOM   1492 C  C   . ALA   A 1 192 ? -25.736 -48.909 20.741  1.00 64.61  ?  224 ALA   A C   1 
ATOM   1493 O  O   . ALA   A 1 192 ? -24.911 -49.324 21.558  1.00 73.64  ?  224 ALA   A O   1 
ATOM   1494 C  CB  . ALA   A 1 192 ? -25.876 -46.450 20.935  1.00 55.04  ?  224 ALA   A CB  1 
ATOM   1495 N  N   . SER   A 1 193 ? -26.820 -49.598 20.424  1.00 58.81  ?  225 SER   A N   1 
ATOM   1496 C  CA  . SER   A 1 193 ? -27.218 -50.779 21.159  1.00 56.45  ?  225 SER   A CA  1 
ATOM   1497 C  C   . SER   A 1 193 ? -27.147 -52.021 20.319  1.00 57.02  ?  225 SER   A C   1 
ATOM   1498 O  O   . SER   A 1 193 ? -27.803 -53.001 20.645  1.00 73.02  ?  225 SER   A O   1 
ATOM   1499 C  CB  . SER   A 1 193 ? -28.639 -50.640 21.661  1.00 58.77  ?  225 SER   A CB  1 
ATOM   1500 O  OG  . SER   A 1 193 ? -29.481 -51.077 20.615  1.00 54.95  ?  225 SER   A OG  1 
ATOM   1501 N  N   . THR   A 1 194 ? -26.427 -51.998 19.238  1.00 58.61  ?  226 THR   A N   1 
ATOM   1502 C  CA  . THR   A 1 194 ? -26.345 -53.179 18.405  1.00 64.38  ?  226 THR   A CA  1 
ATOM   1503 C  C   . THR   A 1 194 ? -24.953 -53.786 18.459  1.00 69.83  ?  226 THR   A C   1 
ATOM   1504 O  O   . THR   A 1 194 ? -23.971 -53.079 18.216  1.00 68.90  ?  226 THR   A O   1 
ATOM   1505 C  CB  . THR   A 1 194 ? -26.701 -52.817 16.986  1.00 62.39  ?  226 THR   A CB  1 
ATOM   1506 O  OG1 . THR   A 1 194 ? -27.954 -52.131 17.007  1.00 65.34  ?  226 THR   A OG1 1 
ATOM   1507 C  CG2 . THR   A 1 194 ? -26.833 -54.052 16.139  1.00 57.76  ?  226 THR   A CG2 1 
ATOM   1508 N  N   . PRO   A 1 195 ? -24.803 -55.065 18.788  1.00 76.12  ?  227 PRO   A N   1 
ATOM   1509 C  CA  . PRO   A 1 195 ? -23.457 -55.627 18.815  1.00 79.68  ?  227 PRO   A CA  1 
ATOM   1510 C  C   . PRO   A 1 195 ? -22.813 -55.444 17.454  1.00 75.19  ?  227 PRO   A C   1 
ATOM   1511 O  O   . PRO   A 1 195 ? -23.445 -55.678 16.422  1.00 64.96  ?  227 PRO   A O   1 
ATOM   1512 C  CB  . PRO   A 1 195 ? -23.690 -57.109 19.150  1.00 79.08  ?  227 PRO   A CB  1 
ATOM   1513 C  CG  . PRO   A 1 195 ? -25.016 -57.209 19.615  1.00 71.04  ?  227 PRO   A CG  1 
ATOM   1514 C  CD  . PRO   A 1 195 ? -25.804 -56.118 18.989  1.00 72.74  ?  227 PRO   A CD  1 
ATOM   1515 N  N   . HIS   A 1 196 ? -21.568 -54.972 17.457  1.00 78.55  ?  228 HIS   A N   1 
ATOM   1516 C  CA  . HIS   A 1 196 ? -20.784 -54.913 16.232  1.00 75.70  ?  228 HIS   A CA  1 
ATOM   1517 C  C   . HIS   A 1 196 ? -19.341 -55.199 16.566  1.00 64.73  ?  228 HIS   A C   1 
ATOM   1518 O  O   . HIS   A 1 196 ? -18.790 -54.557 17.441  1.00 65.85  ?  228 HIS   A O   1 
ATOM   1519 C  CB  . HIS   A 1 196 ? -20.886 -53.552 15.533  1.00 70.79  ?  228 HIS   A CB  1 
ATOM   1520 C  CG  . HIS   A 1 196 ? -20.548 -53.614 14.082  1.00 58.56  ?  228 HIS   A CG  1 
ATOM   1521 N  ND1 . HIS   A 1 196 ? -21.256 -54.381 13.188  1.00 65.00  ?  228 HIS   A ND1 1 
ATOM   1522 C  CD2 . HIS   A 1 196 ? -19.560 -53.034 13.372  1.00 63.68  ?  228 HIS   A CD2 1 
ATOM   1523 C  CE1 . HIS   A 1 196 ? -20.726 -54.262 11.984  1.00 63.13  ?  228 HIS   A CE1 1 
ATOM   1524 N  NE2 . HIS   A 1 196 ? -19.692 -53.452 12.071  1.00 66.06  ?  228 HIS   A NE2 1 
ATOM   1525 N  N   . PRO   A 1 197 ? -18.730 -56.173 15.904  1.00 57.14  ?  229 PRO   A N   1 
ATOM   1526 C  CA  . PRO   A 1 197 ? -19.378 -57.056 14.949  1.00 69.89  ?  229 PRO   A CA  1 
ATOM   1527 C  C   . PRO   A 1 197 ? -20.348 -57.996 15.637  1.00 63.24  ?  229 PRO   A C   1 
ATOM   1528 O  O   . PRO   A 1 197 ? -20.355 -58.107 16.852  1.00 55.72  ?  229 PRO   A O   1 
ATOM   1529 C  CB  . PRO   A 1 197 ? -18.212 -57.818 14.316  1.00 70.66  ?  229 PRO   A CB  1 
ATOM   1530 C  CG  . PRO   A 1 197 ? -17.160 -57.801 15.323  1.00 72.11  ?  229 PRO   A CG  1 
ATOM   1531 C  CD  . PRO   A 1 197 ? -17.312 -56.497 16.063  1.00 64.90  ?  229 PRO   A CD  1 
ATOM   1532 N  N   . PRO   A 1 198 ? -21.171 -58.662 14.847  1.00 58.48  ?  230 PRO   A N   1 
ATOM   1533 C  CA  . PRO   A 1 198 ? -22.194 -59.532 15.413  1.00 60.93  ?  230 PRO   A CA  1 
ATOM   1534 C  C   . PRO   A 1 198 ? -21.574 -60.573 16.321  1.00 67.30  ?  230 PRO   A C   1 
ATOM   1535 O  O   . PRO   A 1 198 ? -20.820 -61.432 15.879  1.00 70.03  ?  230 PRO   A O   1 
ATOM   1536 C  CB  . PRO   A 1 198 ? -22.827 -60.164 14.177  1.00 60.75  ?  230 PRO   A CB  1 
ATOM   1537 C  CG  . PRO   A 1 198 ? -22.570 -59.234 13.117  1.00 67.18  ?  230 PRO   A CG  1 
ATOM   1538 C  CD  . PRO   A 1 198 ? -21.238 -58.631 13.388  1.00 69.00  ?  230 PRO   A CD  1 
ATOM   1539 N  N   . GLY   A 1 199 ? -21.916 -60.506 17.593  1.00 62.54  ?  231 GLY   A N   1 
ATOM   1540 C  CA  . GLY   A 1 199 ? -21.362 -61.396 18.580  1.00 62.61  ?  231 GLY   A CA  1 
ATOM   1541 C  C   . GLY   A 1 199 ? -20.444 -60.697 19.526  1.00 56.99  ?  231 GLY   A C   1 
ATOM   1542 O  O   . GLY   A 1 199 ? -19.995 -61.296 20.503  1.00 55.66  ?  231 GLY   A O   1 
ATOM   1543 N  N   . ALA   A 1 200 ? -20.141 -59.447 19.266  1.00 53.33  ?  232 ALA   A N   1 
ATOM   1544 C  CA  . ALA   A 1 200 ? -19.283 -58.739 20.178  1.00 52.96  ?  232 ALA   A CA  1 
ATOM   1545 C  C   . ALA   A 1 200 ? -19.988 -58.662 21.500  1.00 51.57  ?  232 ALA   A C   1 
ATOM   1546 O  O   . ALA   A 1 200 ? -21.132 -59.085 21.622  1.00 67.91  ?  232 ALA   A O   1 
ATOM   1547 C  CB  . ALA   A 1 200 ? -18.977 -57.346 19.661  1.00 74.94  ?  232 ALA   A CB  1 
ATOM   1548 N  N   . ARG   A 1 201 ? -19.340 -58.091 22.472  1.00 51.77  ?  233 ARG   A N   1 
ATOM   1549 C  CA  . ARG   A 1 201 ? -19.994 -57.901 23.749  1.00 54.31  ?  233 ARG   A CA  1 
ATOM   1550 C  C   . ARG   A 1 201 ? -19.573 -56.612 24.401  1.00 57.58  ?  233 ARG   A C   1 
ATOM   1551 O  O   . ARG   A 1 201 ? -19.706 -56.478 25.611  1.00 51.66  ?  233 ARG   A O   1 
ATOM   1552 C  CB  . ARG   A 1 201 ? -19.684 -59.047 24.666  1.00 69.37  ?  233 ARG   A CB  1 
ATOM   1553 C  CG  . ARG   A 1 201 ? -18.223 -59.421 24.752  1.00 85.36  ?  233 ARG   A CG  1 
ATOM   1554 C  CD  . ARG   A 1 201 ? -17.994 -60.563 25.761  1.00 102.15 ?  233 ARG   A CD  1 
ATOM   1555 N  NE  . ARG   A 1 201 ? -19.102 -61.521 25.778  1.00 109.43 ?  233 ARG   A NE  1 
ATOM   1556 C  CZ  . ARG   A 1 201 ? -19.175 -62.582 26.574  1.00 88.05  ?  233 ARG   A CZ  1 
ATOM   1557 N  NH1 . ARG   A 1 201 ? -18.200 -62.852 27.431  1.00 84.73  ?  233 ARG   A NH1 1 
ATOM   1558 N  NH2 . ARG   A 1 201 ? -20.232 -63.376 26.497  1.00 72.77  ?  233 ARG   A NH2 1 
ATOM   1559 N  N   . GLY   A 1 202 ? -19.053 -55.674 23.636  1.00 69.87  ?  234 GLY   A N   1 
ATOM   1560 C  CA  . GLY   A 1 202 ? -18.717 -54.376 24.173  1.00 68.65  ?  234 GLY   A CA  1 
ATOM   1561 C  C   . GLY   A 1 202 ? -18.675 -53.311 23.107  1.00 62.19  ?  234 GLY   A C   1 
ATOM   1562 O  O   . GLY   A 1 202 ? -18.764 -52.131 23.430  1.00 47.26  ?  234 GLY   A O   1 
ATOM   1563 N  N   . THR   A 1 203 ? -18.534 -53.716 21.844  1.00 68.83  ?  235 THR   A N   1 
ATOM   1564 C  CA  . THR   A 1 203 ? -18.415 -52.793 20.723  1.00 70.64  ?  235 THR   A CA  1 
ATOM   1565 C  C   . THR   A 1 203 ? -19.783 -52.618 20.092  1.00 72.57  ?  235 THR   A C   1 
ATOM   1566 O  O   . THR   A 1 203 ? -20.303 -53.549 19.463  1.00 61.49  ?  235 THR   A O   1 
ATOM   1567 C  CB  . THR   A 1 203 ? -17.454 -53.313 19.661  1.00 68.84  ?  235 THR   A CB  1 
ATOM   1568 O  OG1 . THR   A 1 203 ? -18.081 -54.390 18.969  1.00 66.25  ?  235 THR   A OG1 1 
ATOM   1569 C  CG2 . THR   A 1 203 ? -16.179 -53.797 20.250  1.00 72.97  ?  235 THR   A CG2 1 
ATOM   1570 N  N   . SER   A 1 204 ? -20.339 -51.416 20.216  1.00 75.91  ?  236 SER   A N   1 
ATOM   1571 C  CA  . SER   A 1 204 ? -21.607 -51.100 19.575  1.00 73.69  ?  236 SER   A CA  1 
ATOM   1572 C  C   . SER   A 1 204 ? -21.367 -50.880 18.085  1.00 67.41  ?  236 SER   A C   1 
ATOM   1573 O  O   . SER   A 1 204 ? -20.338 -51.264 17.531  1.00 65.65  ?  236 SER   A O   1 
ATOM   1574 C  CB  . SER   A 1 204 ? -22.255 -49.898 20.245  1.00 66.49  ?  236 SER   A CB  1 
ATOM   1575 O  OG  . SER   A 1 204 ? -21.527 -48.733 19.983  1.00 62.33  ?  236 SER   A OG  1 
ATOM   1576 N  N   . GLN   A 1 205 ? -22.338 -50.304 17.399  1.00 68.53  ?  237 GLN   A N   1 
ATOM   1577 C  CA  . GLN   A 1 205 ? -22.191 -50.029 15.977  1.00 70.87  ?  237 GLN   A CA  1 
ATOM   1578 C  C   . GLN   A 1 205 ? -21.661 -48.637 15.721  1.00 63.80  ?  237 GLN   A C   1 
ATOM   1579 O  O   . GLN   A 1 205 ? -21.299 -48.333 14.583  1.00 57.60  ?  237 GLN   A O   1 
ATOM   1580 C  CB  . GLN   A 1 205 ? -23.521 -50.187 15.236  1.00 70.04  ?  237 GLN   A CB  1 
ATOM   1581 C  CG  . GLN   A 1 205 ? -23.733 -51.536 14.627  1.00 65.28  ?  237 GLN   A CG  1 
ATOM   1582 C  CD  . GLN   A 1 205 ? -25.011 -51.619 13.839  1.00 60.12  ?  237 GLN   A CD  1 
ATOM   1583 O  OE1 . GLN   A 1 205 ? -25.867 -50.745 13.922  1.00 60.69  ?  237 GLN   A OE1 1 
ATOM   1584 N  NE2 . GLN   A 1 205 ? -25.147 -52.672 13.066  1.00 49.91  ?  237 GLN   A NE2 1 
ATOM   1585 N  N   . LEU   A 1 206 ? -21.630 -47.794 16.749  1.00 55.60  ?  238 LEU   A N   1 
ATOM   1586 C  CA  . LEU   A 1 206 ? -20.924 -46.528 16.655  1.00 67.65  ?  238 LEU   A CA  1 
ATOM   1587 C  C   . LEU   A 1 206 ? -19.426 -46.764 16.602  1.00 67.65  ?  238 LEU   A C   1 
ATOM   1588 O  O   . LEU   A 1 206 ? -18.706 -46.154 15.806  1.00 68.71  ?  238 LEU   A O   1 
ATOM   1589 C  CB  . LEU   A 1 206 ? -21.300 -45.639 17.837  1.00 52.60  ?  238 LEU   A CB  1 
ATOM   1590 C  CG  . LEU   A 1 206 ? -22.813 -45.582 18.055  1.00 44.19  ?  238 LEU   A CG  1 
ATOM   1591 C  CD1 . LEU   A 1 206 ? -23.199 -44.472 18.964  1.00 44.63  ?  238 LEU   A CD1 1 
ATOM   1592 C  CD2 . LEU   A 1 206 ? -23.580 -45.422 16.783  1.00 54.54  ?  238 LEU   A CD2 1 
ATOM   1593 N  N   . HIS   A 1 207 ? -18.951 -47.703 17.384  1.00 62.22  ?  239 HIS   A N   1 
ATOM   1594 C  CA  . HIS   A 1 207 ? -17.536 -47.975 17.378  1.00 71.00  ?  239 HIS   A CA  1 
ATOM   1595 C  C   . HIS   A 1 207 ? -17.008 -48.290 15.988  1.00 67.21  ?  239 HIS   A C   1 
ATOM   1596 O  O   . HIS   A 1 207 ? -15.815 -48.128 15.748  1.00 75.77  ?  239 HIS   A O   1 
ATOM   1597 C  CB  . HIS   A 1 207 ? -17.288 -49.092 18.374  1.00 74.63  ?  239 HIS   A CB  1 
ATOM   1598 C  CG  . HIS   A 1 207 ? -17.639 -48.702 19.777  1.00 66.71  ?  239 HIS   A CG  1 
ATOM   1599 N  ND1 . HIS   A 1 207 ? -17.598 -49.580 20.831  1.00 50.49  ?  239 HIS   A ND1 1 
ATOM   1600 C  CD2 . HIS   A 1 207 ? -18.038 -47.513 20.294  1.00 71.81  ?  239 HIS   A CD2 1 
ATOM   1601 C  CE1 . HIS   A 1 207 ? -17.950 -48.953 21.937  1.00 62.61  ?  239 HIS   A CE1 1 
ATOM   1602 N  NE2 . HIS   A 1 207 ? -18.220 -47.697 21.641  1.00 65.73  ?  239 HIS   A NE2 1 
ATOM   1603 N  N   . GLY   A 1 208 ? -17.865 -48.689 15.063  1.00 62.41  ?  240 GLY   A N   1 
ATOM   1604 C  CA  . GLY   A 1 208 ? -17.504 -48.845 13.673  1.00 59.16  ?  240 GLY   A CA  1 
ATOM   1605 C  C   . GLY   A 1 208 ? -17.716 -47.604 12.850  1.00 64.11  ?  240 GLY   A C   1 
ATOM   1606 O  O   . GLY   A 1 208 ? -17.349 -47.582 11.671  1.00 61.40  ?  240 GLY   A O   1 
ATOM   1607 N  N   . MET   A 1 209 ? -18.293 -46.560 13.449  1.00 60.39  ?  241 MET   A N   1 
ATOM   1608 C  CA  . MET   A 1 209 ? -18.508 -45.285 12.770  1.00 57.01  ?  241 MET   A CA  1 
ATOM   1609 C  C   . MET   A 1 209 ? -17.251 -44.462 12.899  1.00 56.78  ?  241 MET   A C   1 
ATOM   1610 O  O   . MET   A 1 209 ? -17.048 -43.724 13.866  1.00 50.71  ?  241 MET   A O   1 
ATOM   1611 C  CB  . MET   A 1 209 ? -19.691 -44.538 13.347  1.00 63.48  ?  241 MET   A CB  1 
ATOM   1612 C  CG  . MET   A 1 209 ? -20.996 -44.894 12.725  1.00 68.59  ?  241 MET   A CG  1 
ATOM   1613 S  SD  . MET   A 1 209 ? -22.188 -43.795 13.428  1.00 62.81  ?  241 MET   A SD  1 
ATOM   1614 C  CE  . MET   A 1 209 ? -22.313 -42.713 12.054  1.00 57.57  ?  241 MET   A CE  1 
ATOM   1615 N  N   . ASP   A 1 210 ? -16.416 -44.571 11.876  1.00 59.39  ?  242 ASP   A N   1 
ATOM   1616 C  CA  . ASP   A 1 210 ? -15.092 -43.983 11.936  1.00 56.38  ?  242 ASP   A CA  1 
ATOM   1617 C  C   . ASP   A 1 210 ? -15.185 -42.479 11.977  1.00 46.73  ?  242 ASP   A C   1 
ATOM   1618 O  O   . ASP   A 1 210 ? -14.514 -41.830 12.774  1.00 47.52  ?  242 ASP   A O   1 
ATOM   1619 C  CB  . ASP   A 1 210 ? -14.270 -44.439 10.736  1.00 60.41  ?  242 ASP   A CB  1 
ATOM   1620 C  CG  . ASP   A 1 210 ? -13.157 -45.398 11.107  1.00 63.87  ?  242 ASP   A CG  1 
ATOM   1621 O  OD1 . ASP   A 1 210 ? -13.187 -45.994 12.207  1.00 68.59  ?  242 ASP   A OD1 1 
ATOM   1622 O  OD2 . ASP   A 1 210 ? -12.250 -45.554 10.271  1.00 60.44  ?  242 ASP   A OD2 1 
ATOM   1623 N  N   . LEU   A 1 211 ? -16.002 -41.911 11.108  1.00 50.85  ?  243 LEU   A N   1 
ATOM   1624 C  CA  . LEU   A 1 211 ? -16.203 -40.477 11.036  1.00 43.59  ?  243 LEU   A CA  1 
ATOM   1625 C  C   . LEU   A 1 211 ? -17.545 -40.275 10.372  1.00 44.50  ?  243 LEU   A C   1 
ATOM   1626 O  O   . LEU   A 1 211 ? -17.907 -41.037 9.475   1.00 47.69  ?  243 LEU   A O   1 
ATOM   1627 C  CB  . LEU   A 1 211 ? -15.077 -39.828 10.250  1.00 44.62  ?  243 LEU   A CB  1 
ATOM   1628 C  CG  . LEU   A 1 211 ? -15.190 -38.437 9.672   1.00 42.16  ?  243 LEU   A CG  1 
ATOM   1629 C  CD1 . LEU   A 1 211 ? -14.858 -37.397 10.668  1.00 42.24  ?  243 LEU   A CD1 1 
ATOM   1630 C  CD2 . LEU   A 1 211 ? -14.287 -38.340 8.515   1.00 43.67  ?  243 LEU   A CD2 1 
ATOM   1631 N  N   . LEU   A 1 212 ? -18.298 -39.302 10.846  1.00 36.34  ?  244 LEU   A N   1 
ATOM   1632 C  CA  . LEU   A 1 212 ? -19.576 -38.964 10.249  1.00 41.20  ?  244 LEU   A CA  1 
ATOM   1633 C  C   . LEU   A 1 212 ? -19.419 -37.676 9.469   1.00 44.48  ?  244 LEU   A C   1 
ATOM   1634 O  O   . LEU   A 1 212 ? -19.338 -36.603 10.062  1.00 43.20  ?  244 LEU   A O   1 
ATOM   1635 C  CB  . LEU   A 1 212 ? -20.647 -38.797 11.310  1.00 53.51  ?  244 LEU   A CB  1 
ATOM   1636 C  CG  . LEU   A 1 212 ? -22.031 -38.492 10.742  1.00 48.17  ?  244 LEU   A CG  1 
ATOM   1637 C  CD1 . LEU   A 1 212 ? -22.570 -39.653 9.900   1.00 44.87  ?  244 LEU   A CD1 1 
ATOM   1638 C  CD2 . LEU   A 1 212 ? -22.982 -38.137 11.824  1.00 33.43  ?  244 LEU   A CD2 1 
ATOM   1639 N  N   . VAL   A 1 213 ? -19.414 -37.771 8.145   1.00 42.92  ?  245 VAL   A N   1 
ATOM   1640 C  CA  . VAL   A 1 213 ? -19.384 -36.591 7.290   1.00 42.56  ?  245 VAL   A CA  1 
ATOM   1641 C  C   . VAL   A 1 213 ? -20.824 -36.243 6.962   1.00 36.53  ?  245 VAL   A C   1 
ATOM   1642 O  O   . VAL   A 1 213 ? -21.430 -36.858 6.098   1.00 36.27  ?  245 VAL   A O   1 
ATOM   1643 C  CB  . VAL   A 1 213 ? -18.599 -36.831 6.006   1.00 40.69  ?  245 VAL   A CB  1 
ATOM   1644 C  CG1 . VAL   A 1 213 ? -18.301 -35.558 5.381   1.00 40.01  ?  245 VAL   A CG1 1 
ATOM   1645 C  CG2 . VAL   A 1 213 ? -17.343 -37.575 6.247   1.00 39.42  ?  245 VAL   A CG2 1 
ATOM   1646 N  N   . LEU   A 1 214 ? -21.356 -35.236 7.610   1.00 26.12  ?  246 LEU   A N   1 
ATOM   1647 C  CA  . LEU   A 1 214 ? -22.743 -34.856 7.421   1.00 32.57  ?  246 LEU   A CA  1 
ATOM   1648 C  C   . LEU   A 1 214 ? -22.843 -33.636 6.516   1.00 38.39  ?  246 LEU   A C   1 
ATOM   1649 O  O   . LEU   A 1 214 ? -22.299 -32.588 6.857   1.00 42.03  ?  246 LEU   A O   1 
ATOM   1650 C  CB  . LEU   A 1 214 ? -23.374 -34.553 8.769   1.00 33.51  ?  246 LEU   A CB  1 
ATOM   1651 C  CG  . LEU   A 1 214 ? -24.772 -33.982 8.747   1.00 34.01  ?  246 LEU   A CG  1 
ATOM   1652 C  CD1 . LEU   A 1 214 ? -25.748 -35.010 8.371   1.00 35.32  ?  246 LEU   A CD1 1 
ATOM   1653 C  CD2 . LEU   A 1 214 ? -25.111 -33.439 10.027  1.00 36.66  ?  246 LEU   A CD2 1 
ATOM   1654 N  N   . LEU   A 1 215 ? -23.592 -33.748 5.409   1.00 30.52  ?  247 LEU   A N   1 
ATOM   1655 C  CA  . LEU   A 1 215 ? -23.780 -32.668 4.447   1.00 33.65  ?  247 LEU   A CA  1 
ATOM   1656 C  C   . LEU   A 1 215 ? -25.128 -31.989 4.641   1.00 36.01  ?  247 LEU   A C   1 
ATOM   1657 O  O   . LEU   A 1 215 ? -26.136 -32.661 4.796   1.00 40.44  ?  247 LEU   A O   1 
ATOM   1658 C  CB  . LEU   A 1 215 ? -23.727 -33.208 3.023   1.00 42.21  ?  247 LEU   A CB  1 
ATOM   1659 C  CG  . LEU   A 1 215 ? -22.701 -34.249 2.545   1.00 40.87  ?  247 LEU   A CG  1 
ATOM   1660 C  CD1 . LEU   A 1 215 ? -22.819 -34.496 1.114   1.00 41.01  ?  247 LEU   A CD1 1 
ATOM   1661 C  CD2 . LEU   A 1 215 ? -21.337 -33.815 2.750   1.00 44.78  ?  247 LEU   A CD2 1 
ATOM   1662 N  N   . ASP   A 1 216 ? -25.172 -30.661 4.577   1.00 31.47  ?  248 ASP   A N   1 
ATOM   1663 C  CA  . ASP   A 1 216 ? -26.445 -29.988 4.799   1.00 33.91  ?  248 ASP   A CA  1 
ATOM   1664 C  C   . ASP   A 1 216 ? -26.377 -28.534 4.331   1.00 36.53  ?  248 ASP   A C   1 
ATOM   1665 O  O   . ASP   A 1 216 ? -25.406 -27.840 4.602   1.00 33.55  ?  248 ASP   A O   1 
ATOM   1666 C  CB  . ASP   A 1 216 ? -26.792 -30.074 6.284   1.00 37.92  ?  248 ASP   A CB  1 
ATOM   1667 C  CG  . ASP   A 1 216 ? -28.218 -29.751 6.604   1.00 36.91  ?  248 ASP   A CG  1 
ATOM   1668 O  OD1 . ASP   A 1 216 ? -29.071 -29.758 5.718   1.00 37.97  ?  248 ASP   A OD1 1 
ATOM   1669 O  OD2 . ASP   A 1 216 ? -28.487 -29.514 7.791   1.00 36.90  ?  248 ASP   A OD2 1 
ATOM   1670 N  N   . LEU   A 1 217 ? -27.414 -28.087 3.623   1.00 36.71  ?  249 LEU   A N   1 
ATOM   1671 C  CA  . LEU   A 1 217 ? -27.556 -26.709 3.162   1.00 30.59  ?  249 LEU   A CA  1 
ATOM   1672 C  C   . LEU   A 1 217 ? -26.491 -26.355 2.154   1.00 39.51  ?  249 LEU   A C   1 
ATOM   1673 O  O   . LEU   A 1 217 ? -25.837 -25.328 2.267   1.00 38.32  ?  249 LEU   A O   1 
ATOM   1674 C  CB  . LEU   A 1 217 ? -27.519 -25.716 4.308   1.00 34.50  ?  249 LEU   A CB  1 
ATOM   1675 C  CG  . LEU   A 1 217 ? -28.406 -25.911 5.525   1.00 33.41  ?  249 LEU   A CG  1 
ATOM   1676 C  CD1 . LEU   A 1 217 ? -28.575 -24.643 6.149   1.00 34.10  ?  249 LEU   A CD1 1 
ATOM   1677 C  CD2 . LEU   A 1 217 ? -29.708 -26.403 5.209   1.00 35.13  ?  249 LEU   A CD2 1 
ATOM   1678 N  N   . ILE   A 1 218 ? -26.351 -27.195 1.139   1.00 46.30  ?  250 ILE   A N   1 
ATOM   1679 C  CA  . ILE   A 1 218 ? -25.324 -27.056 0.120   1.00 32.23  ?  250 ILE   A CA  1 
ATOM   1680 C  C   . ILE   A 1 218 ? -25.976 -26.849 -1.227  1.00 33.18  ?  250 ILE   A C   1 
ATOM   1681 O  O   . ILE   A 1 218 ? -26.862 -27.601 -1.618  1.00 36.02  ?  250 ILE   A O   1 
ATOM   1682 C  CB  . ILE   A 1 218 ? -24.424 -28.282 0.054   1.00 25.11  ?  250 ILE   A CB  1 
ATOM   1683 C  CG1 . ILE   A 1 218 ? -23.722 -28.451 1.361   1.00 31.57  ?  250 ILE   A CG1 1 
ATOM   1684 C  CG2 . ILE   A 1 218 ? -23.434 -28.080 -1.023  1.00 39.62  ?  250 ILE   A CG2 1 
ATOM   1685 C  CD1 . ILE   A 1 218 ? -22.688 -29.491 1.371   1.00 32.53  ?  250 ILE   A CD1 1 
ATOM   1686 N  N   . GLY   A 1 219 ? -25.490 -25.882 -1.963  1.00 39.52  ?  251 GLY   A N   1 
ATOM   1687 C  CA  . GLY   A 1 219 ? -26.012 -25.653 -3.279  1.00 34.06  ?  251 GLY   A CA  1 
ATOM   1688 C  C   . GLY   A 1 219 ? -26.048 -24.197 -3.612  1.00 31.53  ?  251 GLY   A C   1 
ATOM   1689 O  O   . GLY   A 1 219 ? -26.318 -23.826 -4.736  1.00 45.81  ?  251 GLY   A O   1 
ATOM   1690 N  N   . ALA   A 1 220 ? -25.767 -23.355 -2.652  1.00 37.02  ?  252 ALA   A N   1 
ATOM   1691 C  CA  . ALA   A 1 220 ? -25.741 -21.926 -2.889  1.00 37.54  ?  252 ALA   A CA  1 
ATOM   1692 C  C   . ALA   A 1 220 ? -24.350 -21.522 -3.277  1.00 37.70  ?  252 ALA   A C   1 
ATOM   1693 O  O   . ALA   A 1 220 ? -23.406 -22.280 -3.125  1.00 36.52  ?  252 ALA   A O   1 
ATOM   1694 C  CB  . ALA   A 1 220 ? -26.184 -21.169 -1.653  1.00 41.53  ?  252 ALA   A CB  1 
ATOM   1695 N  N   . PRO   A 1 221 ? -24.189 -20.330 -3.806  1.00 42.93  ?  253 PRO   A N   1 
ATOM   1696 C  CA  . PRO   A 1 221 ? -22.862 -19.868 -4.164  1.00 46.07  ?  253 PRO   A CA  1 
ATOM   1697 C  C   . PRO   A 1 221 ? -22.097 -19.278 -2.998  1.00 40.83  ?  253 PRO   A C   1 
ATOM   1698 O  O   . PRO   A 1 221 ? -22.652 -18.767 -2.032  1.00 48.34  ?  253 PRO   A O   1 
ATOM   1699 C  CB  . PRO   A 1 221 ? -23.168 -18.811 -5.213  1.00 46.15  ?  253 PRO   A CB  1 
ATOM   1700 C  CG  . PRO   A 1 221 ? -24.513 -18.440 -4.944  1.00 37.55  ?  253 PRO   A CG  1 
ATOM   1701 C  CD  . PRO   A 1 221 ? -25.201 -19.589 -4.549  1.00 41.79  ?  253 PRO   A CD  1 
ATOM   1702 N  N   . ASN   A 1 222 ? -20.827 -19.383 -3.091  1.00 41.30  ?  254 ASN   A N   1 
ATOM   1703 C  CA  . ASN   A 1 222 ? -19.925 -18.749 -2.158  1.00 51.45  ?  254 ASN   A CA  1 
ATOM   1704 C  C   . ASN   A 1 222 ? -20.160 -19.232 -0.745  1.00 41.72  ?  254 ASN   A C   1 
ATOM   1705 O  O   . ASN   A 1 222 ? -20.271 -18.423 0.172   1.00 48.33  ?  254 ASN   A O   1 
ATOM   1706 C  CB  . ASN   A 1 222 ? -20.069 -17.234 -2.231  1.00 58.06  ?  254 ASN   A CB  1 
ATOM   1707 C  CG  . ASN   A 1 222 ? -19.621 -16.675 -3.559  1.00 56.94  ?  254 ASN   A CG  1 
ATOM   1708 O  OD1 . ASN   A 1 222 ? -18.716 -17.208 -4.208  1.00 52.50  ?  254 ASN   A OD1 1 
ATOM   1709 N  ND2 . ASN   A 1 222 ? -20.268 -15.610 -3.984  1.00 55.61  ?  254 ASN   A ND2 1 
ATOM   1710 N  N   . PRO   A 1 223 ? -20.219 -20.529 -0.524  1.00 39.10  ?  255 PRO   A N   1 
ATOM   1711 C  CA  . PRO   A 1 223 ? -20.278 -21.036 0.834   1.00 41.53  ?  255 PRO   A CA  1 
ATOM   1712 C  C   . PRO   A 1 223 ? -18.963 -20.860 1.544   1.00 40.99  ?  255 PRO   A C   1 
ATOM   1713 O  O   . PRO   A 1 223 ? -17.915 -20.711 0.932   1.00 49.63  ?  255 PRO   A O   1 
ATOM   1714 C  CB  . PRO   A 1 223 ? -20.590 -22.513 0.640   1.00 45.13  ?  255 PRO   A CB  1 
ATOM   1715 C  CG  . PRO   A 1 223 ? -20.144 -22.803 -0.651  1.00 50.97  ?  255 PRO   A CG  1 
ATOM   1716 C  CD  . PRO   A 1 223 ? -20.415 -21.611 -1.476  1.00 49.97  ?  255 PRO   A CD  1 
ATOM   1717 N  N   . THR   A 1 224 ? -19.046 -20.865 2.864   1.00 40.28  ?  256 THR   A N   1 
ATOM   1718 C  CA  . THR   A 1 224 ? -17.901 -20.887 3.752   1.00 37.35  ?  256 THR   A CA  1 
ATOM   1719 C  C   . THR   A 1 224 ? -18.200 -21.936 4.795   1.00 38.53  ?  256 THR   A C   1 
ATOM   1720 O  O   . THR   A 1 224 ? -19.215 -21.844 5.477   1.00 43.61  ?  256 THR   A O   1 
ATOM   1721 C  CB  . THR   A 1 224 ? -17.687 -19.541 4.431   1.00 43.39  ?  256 THR   A CB  1 
ATOM   1722 O  OG1 . THR   A 1 224 ? -18.877 -19.154 5.105   1.00 57.54  ?  256 THR   A OG1 1 
ATOM   1723 C  CG2 . THR   A 1 224 ? -17.434 -18.513 3.478   1.00 34.38  ?  256 THR   A CG2 1 
ATOM   1724 N  N   . PHE   A 1 225 ? -17.338 -22.920 4.924   1.00 37.81  ?  257 PHE   A N   1 
ATOM   1725 C  CA  . PHE   A 1 225 ? -17.553 -24.016 5.842   1.00 34.26  ?  257 PHE   A CA  1 
ATOM   1726 C  C   . PHE   A 1 225 ? -16.613 -23.885 7.024   1.00 37.68  ?  257 PHE   A C   1 
ATOM   1727 O  O   . PHE   A 1 225 ? -15.401 -23.995 6.836   1.00 44.59  ?  257 PHE   A O   1 
ATOM   1728 C  CB  . PHE   A 1 225 ? -17.307 -25.341 5.139   1.00 37.16  ?  257 PHE   A CB  1 
ATOM   1729 C  CG  . PHE   A 1 225 ? -18.296 -25.677 4.111   1.00 29.50  ?  257 PHE   A CG  1 
ATOM   1730 C  CD1 . PHE   A 1 225 ? -19.421 -26.334 4.436   1.00 33.51  ?  257 PHE   A CD1 1 
ATOM   1731 C  CD2 . PHE   A 1 225 ? -18.082 -25.383 2.807   1.00 42.35  ?  257 PHE   A CD2 1 
ATOM   1732 C  CE1 . PHE   A 1 225 ? -20.325 -26.662 3.493   1.00 31.86  ?  257 PHE   A CE1 1 
ATOM   1733 C  CE2 . PHE   A 1 225 ? -19.012 -25.715 1.867   1.00 39.13  ?  257 PHE   A CE2 1 
ATOM   1734 C  CZ  . PHE   A 1 225 ? -20.120 -26.348 2.231   1.00 33.67  ?  257 PHE   A CZ  1 
ATOM   1735 N  N   . PRO   A 1 226 ? -17.074 -23.695 8.242   1.00 39.90  ?  258 PRO   A N   1 
ATOM   1736 C  CA  . PRO   A 1 226 ? -16.153 -23.581 9.362   1.00 43.85  ?  258 PRO   A CA  1 
ATOM   1737 C  C   . PRO   A 1 226 ? -15.644 -24.932 9.802   1.00 47.69  ?  258 PRO   A C   1 
ATOM   1738 O  O   . PRO   A 1 226 ? -16.169 -25.977 9.432   1.00 50.26  ?  258 PRO   A O   1 
ATOM   1739 C  CB  . PRO   A 1 226 ? -17.015 -22.962 10.436  1.00 56.55  ?  258 PRO   A CB  1 
ATOM   1740 C  CG  . PRO   A 1 226 ? -18.055 -22.307 9.722   1.00 56.47  ?  258 PRO   A CG  1 
ATOM   1741 C  CD  . PRO   A 1 226 ? -18.386 -23.205 8.640   1.00 45.94  ?  258 PRO   A CD  1 
ATOM   1742 N  N   . ASN   A 1 227 ? -14.621 -24.890 10.633  1.00 49.19  ?  259 ASN   A N   1 
ATOM   1743 C  CA  . ASN   A 1 227 ? -14.040 -26.091 11.211  1.00 53.97  ?  259 ASN   A CA  1 
ATOM   1744 C  C   . ASN   A 1 227 ? -14.550 -26.242 12.626  1.00 56.95  ?  259 ASN   A C   1 
ATOM   1745 O  O   . ASN   A 1 227 ? -14.097 -25.545 13.530  1.00 67.72  ?  259 ASN   A O   1 
ATOM   1746 C  CB  . ASN   A 1 227 ? -12.527 -26.042 11.218  1.00 58.42  ?  259 ASN   A CB  1 
ATOM   1747 C  CG  . ASN   A 1 227 ? -11.951 -27.296 11.717  1.00 55.80  ?  259 ASN   A CG  1 
ATOM   1748 O  OD1 . ASN   A 1 227 ? -12.615 -28.053 12.407  1.00 54.49  ?  259 ASN   A OD1 1 
ATOM   1749 N  ND2 . ASN   A 1 227 ? -10.721 -27.553 11.360  1.00 64.09  ?  259 ASN   A ND2 1 
ATOM   1750 N  N   . PHE   A 1 228 ? -15.419 -27.212 12.829  1.00 59.83  ?  260 PHE   A N   1 
ATOM   1751 C  CA  . PHE   A 1 228 ? -16.302 -27.179 13.975  1.00 57.19  ?  260 PHE   A CA  1 
ATOM   1752 C  C   . PHE   A 1 228 ? -15.728 -27.905 15.173  1.00 48.53  ?  260 PHE   A C   1 
ATOM   1753 O  O   . PHE   A 1 228 ? -15.795 -27.390 16.280  1.00 58.36  ?  260 PHE   A O   1 
ATOM   1754 C  CB  . PHE   A 1 228 ? -17.646 -27.773 13.598  1.00 50.10  ?  260 PHE   A CB  1 
ATOM   1755 C  CG  . PHE   A 1 228 ? -18.526 -26.852 12.791  1.00 44.73  ?  260 PHE   A CG  1 
ATOM   1756 C  CD1 . PHE   A 1 228 ? -18.961 -25.662 13.297  1.00 55.60  ?  260 PHE   A CD1 1 
ATOM   1757 C  CD2 . PHE   A 1 228 ? -18.959 -27.206 11.542  1.00 47.97  ?  260 PHE   A CD2 1 
ATOM   1758 C  CE1 . PHE   A 1 228 ? -19.790 -24.851 12.564  1.00 50.29  ?  260 PHE   A CE1 1 
ATOM   1759 C  CE2 . PHE   A 1 228 ? -19.777 -26.380 10.827  1.00 43.82  ?  260 PHE   A CE2 1 
ATOM   1760 C  CZ  . PHE   A 1 228 ? -20.186 -25.215 11.350  1.00 41.24  ?  260 PHE   A CZ  1 
ATOM   1761 N  N   . PHE   A 1 229 ? -15.131 -29.063 14.984  1.00 54.05  ?  261 PHE   A N   1 
ATOM   1762 C  CA  . PHE   A 1 229 ? -14.682 -29.855 16.110  1.00 60.42  ?  261 PHE   A CA  1 
ATOM   1763 C  C   . PHE   A 1 229 ? -13.226 -30.265 15.954  1.00 54.66  ?  261 PHE   A C   1 
ATOM   1764 O  O   . PHE   A 1 229 ? -12.817 -30.740 14.894  1.00 55.54  ?  261 PHE   A O   1 
ATOM   1765 C  CB  . PHE   A 1 229 ? -15.530 -31.129 16.268  1.00 68.39  ?  261 PHE   A CB  1 
ATOM   1766 C  CG  . PHE   A 1 229 ? -16.945 -30.959 15.862  1.00 61.58  ?  261 PHE   A CG  1 
ATOM   1767 C  CD1 . PHE   A 1 229 ? -17.770 -30.109 16.550  1.00 54.03  ?  261 PHE   A CD1 1 
ATOM   1768 C  CD2 . PHE   A 1 229 ? -17.451 -31.646 14.795  1.00 61.87  ?  261 PHE   A CD2 1 
ATOM   1769 C  CE1 . PHE   A 1 229 ? -19.039 -29.945 16.196  1.00 43.14  ?  261 PHE   A CE1 1 
ATOM   1770 C  CE2 . PHE   A 1 229 ? -18.735 -31.468 14.431  1.00 56.90  ?  261 PHE   A CE2 1 
ATOM   1771 C  CZ  . PHE   A 1 229 ? -19.528 -30.609 15.142  1.00 54.46  ?  261 PHE   A CZ  1 
ATOM   1772 N  N   . PRO   A 1 230 ? -12.440 -30.162 17.014  1.00 47.82  ?  262 PRO   A N   1 
ATOM   1773 C  CA  . PRO   A 1 230 ? -11.068 -30.656 16.938  1.00 52.26  ?  262 PRO   A CA  1 
ATOM   1774 C  C   . PRO   A 1 230 ? -10.939 -32.158 16.789  1.00 52.11  ?  262 PRO   A C   1 
ATOM   1775 O  O   . PRO   A 1 230 ? -9.933  -32.617 16.251  1.00 53.03  ?  262 PRO   A O   1 
ATOM   1776 C  CB  . PRO   A 1 230 ? -10.473 -30.183 18.257  1.00 52.45  ?  262 PRO   A CB  1 
ATOM   1777 C  CG  . PRO   A 1 230 ? -11.634 -30.068 19.130  1.00 57.31  ?  262 PRO   A CG  1 
ATOM   1778 C  CD  . PRO   A 1 230 ? -12.703 -29.528 18.306  1.00 48.64  ?  262 PRO   A CD  1 
ATOM   1779 N  N   . ASN   A 1 231 ? -11.881 -32.959 17.270  1.00 59.38  ?  263 ASN   A N   1 
ATOM   1780 C  CA  . ASN   A 1 231 ? -11.721 -34.399 17.094  1.00 67.87  ?  263 ASN   A CA  1 
ATOM   1781 C  C   . ASN   A 1 231 ? -11.681 -34.786 15.615  1.00 65.64  ?  263 ASN   A C   1 
ATOM   1782 O  O   . ASN   A 1 231 ? -11.386 -35.942 15.295  1.00 65.10  ?  263 ASN   A O   1 
ATOM   1783 C  CB  . ASN   A 1 231 ? -12.832 -35.172 17.866  1.00 65.64  ?  263 ASN   A CB  1 
ATOM   1784 C  CG  . ASN   A 1 231 ? -14.197 -34.433 17.880  1.00 83.63  ?  263 ASN   A CG  1 
ATOM   1785 O  OD1 . ASN   A 1 231 ? -14.364 -33.420 18.580  1.00 74.23  ?  263 ASN   A OD1 1 
ATOM   1786 N  ND2 . ASN   A 1 231 ? -15.176 -34.952 17.118  1.00 67.23  ?  263 ASN   A ND2 1 
ATOM   1787 N  N   . SER   A 1 232 ? -11.934 -33.843 14.709  1.00 57.41  ?  264 SER   A N   1 
ATOM   1788 C  CA  . SER   A 1 232 ? -11.943 -34.119 13.281  1.00 60.21  ?  264 SER   A CA  1 
ATOM   1789 C  C   . SER   A 1 232 ? -11.250 -33.042 12.460  1.00 61.43  ?  264 SER   A C   1 
ATOM   1790 O  O   . SER   A 1 232 ? -11.390 -33.037 11.239  1.00 53.16  ?  264 SER   A O   1 
ATOM   1791 C  CB  . SER   A 1 232 ? -13.356 -34.223 12.792  1.00 65.11  ?  264 SER   A CB  1 
ATOM   1792 O  OG  . SER   A 1 232 ? -13.932 -32.934 12.808  1.00 59.00  ?  264 SER   A OG  1 
ATOM   1793 N  N   . ALA   A 1 233 ? -10.519 -32.127 13.078  1.00 65.46  ?  265 ALA   A N   1 
ATOM   1794 C  CA  . ALA   A 1 233 ? -9.972  -31.004 12.339  1.00 55.24  ?  265 ALA   A CA  1 
ATOM   1795 C  C   . ALA   A 1 233 ? -8.874  -31.417 11.375  1.00 47.61  ?  265 ALA   A C   1 
ATOM   1796 O  O   . ALA   A 1 233 ? -8.631  -30.724 10.399  1.00 53.85  ?  265 ALA   A O   1 
ATOM   1797 C  CB  . ALA   A 1 233 ? -9.440  -29.975 13.311  1.00 54.00  ?  265 ALA   A CB  1 
ATOM   1798 N  N   . ARG   A 1 234 ? -8.167  -32.496 11.649  1.00 50.08  ?  266 ARG   A N   1 
ATOM   1799 C  CA  . ARG   A 1 234 ? -7.199  -32.985 10.684  1.00 48.98  ?  266 ARG   A CA  1 
ATOM   1800 C  C   . ARG   A 1 234 ? -7.878  -33.376 9.402   1.00 45.55  ?  266 ARG   A C   1 
ATOM   1801 O  O   . ARG   A 1 234 ? -7.313  -33.235 8.318   1.00 48.63  ?  266 ARG   A O   1 
ATOM   1802 C  CB  . ARG   A 1 234 ? -6.434  -34.181 11.249  1.00 46.59  ?  266 ARG   A CB  1 
ATOM   1803 C  CG  . ARG   A 1 234 ? -7.280  -35.200 11.942  1.00 54.36  ?  266 ARG   A CG  1 
ATOM   1804 C  CD  . ARG   A 1 234 ? -6.469  -36.200 12.660  1.00 53.14  ?  266 ARG   A CD  1 
ATOM   1805 N  NE  . ARG   A 1 234 ? -6.182  -37.364 11.838  1.00 49.20  ?  266 ARG   A NE  1 
ATOM   1806 C  CZ  . ARG   A 1 234 ? -6.792  -38.529 11.937  1.00 48.28  ?  266 ARG   A CZ  1 
ATOM   1807 N  NH1 . ARG   A 1 234 ? -7.749  -38.725 12.823  1.00 49.39  ?  266 ARG   A NH1 1 
ATOM   1808 N  NH2 . ARG   A 1 234 ? -6.420  -39.509 11.142  1.00 54.70  ?  266 ARG   A NH2 1 
ATOM   1809 N  N   . TRP   A 1 235 ? -9.088  -33.862 9.498   1.00 50.14  ?  267 TRP   A N   1 
ATOM   1810 C  CA  . TRP   A 1 235 ? -9.795  -34.233 8.297   1.00 53.86  ?  267 TRP   A CA  1 
ATOM   1811 C  C   . TRP   A 1 235 ? -10.346 -33.013 7.593   1.00 52.11  ?  267 TRP   A C   1 
ATOM   1812 O  O   . TRP   A 1 235 ? -10.568 -33.045 6.389   1.00 45.86  ?  267 TRP   A O   1 
ATOM   1813 C  CB  . TRP   A 1 235 ? -10.893 -35.210 8.663   1.00 51.57  ?  267 TRP   A CB  1 
ATOM   1814 C  CG  . TRP   A 1 235 ? -10.343 -36.457 9.071   1.00 49.68  ?  267 TRP   A CG  1 
ATOM   1815 C  CD1 . TRP   A 1 235 ? -10.425 -37.014 10.280  1.00 47.35  ?  267 TRP   A CD1 1 
ATOM   1816 C  CD2 . TRP   A 1 235 ? -9.562  -37.329 8.269   1.00 50.86  ?  267 TRP   A CD2 1 
ATOM   1817 N  NE1 . TRP   A 1 235 ? -9.758  -38.201 10.291  1.00 50.51  ?  267 TRP   A NE1 1 
ATOM   1818 C  CE2 . TRP   A 1 235 ? -9.225  -38.415 9.054   1.00 49.84  ?  267 TRP   A CE2 1 
ATOM   1819 C  CE3 . TRP   A 1 235 ? -9.141  -37.303 6.947   1.00 51.70  ?  267 TRP   A CE3 1 
ATOM   1820 C  CZ2 . TRP   A 1 235 ? -8.491  -39.459 8.574   1.00 53.58  ?  267 TRP   A CZ2 1 
ATOM   1821 C  CZ3 . TRP   A 1 235 ? -8.427  -38.329 6.478   1.00 48.68  ?  267 TRP   A CZ3 1 
ATOM   1822 C  CH2 . TRP   A 1 235 ? -8.101  -39.399 7.281   1.00 49.07  ?  267 TRP   A CH2 1 
ATOM   1823 N  N   . PHE   A 1 236 ? -10.596 -31.945 8.327   1.00 53.67  ?  268 PHE   A N   1 
ATOM   1824 C  CA  . PHE   A 1 236 ? -11.012 -30.724 7.683   1.00 48.63  ?  268 PHE   A CA  1 
ATOM   1825 C  C   . PHE   A 1 236 ? -9.872  -30.155 6.886   1.00 45.46  ?  268 PHE   A C   1 
ATOM   1826 O  O   . PHE   A 1 236 ? -10.094 -29.590 5.820   1.00 42.58  ?  268 PHE   A O   1 
ATOM   1827 C  CB  . PHE   A 1 236 ? -11.505 -29.735 8.730   1.00 51.09  ?  268 PHE   A CB  1 
ATOM   1828 C  CG  . PHE   A 1 236 ? -11.916 -28.418 8.185   1.00 47.70  ?  268 PHE   A CG  1 
ATOM   1829 C  CD1 . PHE   A 1 236 ? -13.189 -28.203 7.763   1.00 45.97  ?  268 PHE   A CD1 1 
ATOM   1830 C  CD2 . PHE   A 1 236 ? -11.039 -27.383 8.144   1.00 55.83  ?  268 PHE   A CD2 1 
ATOM   1831 C  CE1 . PHE   A 1 236 ? -13.562 -26.989 7.281   1.00 41.65  ?  268 PHE   A CE1 1 
ATOM   1832 C  CE2 . PHE   A 1 236 ? -11.418 -26.186 7.667   1.00 56.40  ?  268 PHE   A CE2 1 
ATOM   1833 C  CZ  . PHE   A 1 236 ? -12.682 -25.995 7.242   1.00 48.67  ?  268 PHE   A CZ  1 
ATOM   1834 N  N   . GLU   A 1 237 ? -8.644  -30.347 7.354   1.00 51.51  ?  269 GLU   A N   1 
ATOM   1835 C  CA  . GLU   A 1 237 ? -7.508  -29.772 6.655   1.00 49.34  ?  269 GLU   A CA  1 
ATOM   1836 C  C   . GLU   A 1 237 ? -7.275  -30.496 5.354   1.00 49.65  ?  269 GLU   A C   1 
ATOM   1837 O  O   . GLU   A 1 237 ? -6.971  -29.870 4.339   1.00 49.45  ?  269 GLU   A O   1 
ATOM   1838 C  CB  . GLU   A 1 237 ? -6.266  -29.792 7.535   1.00 52.06  ?  269 GLU   A CB  1 
ATOM   1839 C  CG  . GLU   A 1 237 ? -6.072  -28.456 8.246   1.00 68.38  ?  269 GLU   A CG  1 
ATOM   1840 C  CD  . GLU   A 1 237 ? -5.578  -28.589 9.650   1.00 73.63  ?  269 GLU   A CD  1 
ATOM   1841 O  OE1 . GLU   A 1 237 ? -6.219  -27.982 10.548  1.00 65.37  ?  269 GLU   A OE1 1 
ATOM   1842 O  OE2 . GLU   A 1 237 ? -4.564  -29.294 9.845   1.00 75.87  ?  269 GLU   A OE2 1 
ATOM   1843 N  N   . ARG   A 1 238 ? -7.472  -31.804 5.338   1.00 46.25  ?  270 ARG   A N   1 
ATOM   1844 C  CA  . ARG   A 1 238 ? -7.483  -32.483 4.060   1.00 42.15  ?  270 ARG   A CA  1 
ATOM   1845 C  C   . ARG   A 1 238 ? -8.435  -31.817 3.082   1.00 41.35  ?  270 ARG   A C   1 
ATOM   1846 O  O   . ARG   A 1 238 ? -8.112  -31.654 1.914   1.00 51.48  ?  270 ARG   A O   1 
ATOM   1847 C  CB  . ARG   A 1 238 ? -7.855  -33.932 4.248   1.00 47.07  ?  270 ARG   A CB  1 
ATOM   1848 C  CG  . ARG   A 1 238 ? -6.902  -34.683 5.077   1.00 44.42  ?  270 ARG   A CG  1 
ATOM   1849 C  CD  . ARG   A 1 238 ? -5.587  -34.696 4.500   1.00 42.10  ?  270 ARG   A CD  1 
ATOM   1850 N  NE  . ARG   A 1 238 ? -5.650  -35.070 3.111   1.00 46.94  ?  270 ARG   A NE  1 
ATOM   1851 C  CZ  . ARG   A 1 238 ? -4.913  -34.514 2.169   1.00 45.65  ?  270 ARG   A CZ  1 
ATOM   1852 N  NH1 . ARG   A 1 238 ? -4.070  -33.551 2.473   1.00 39.82  ?  270 ARG   A NH1 1 
ATOM   1853 N  NH2 . ARG   A 1 238 ? -5.037  -34.909 0.922   1.00 52.25  ?  270 ARG   A NH2 1 
ATOM   1854 N  N   . LEU   A 1 239 ? -9.608  -31.411 3.527   1.00 44.19  ?  271 LEU   A N   1 
ATOM   1855 C  CA  . LEU   A 1 239 ? -10.527 -30.779 2.601   1.00 40.80  ?  271 LEU   A CA  1 
ATOM   1856 C  C   . LEU   A 1 239 ? -9.923  -29.501 2.046   1.00 37.37  ?  271 LEU   A C   1 
ATOM   1857 O  O   . LEU   A 1 239 ? -9.950  -29.270 0.846   1.00 33.91  ?  271 LEU   A O   1 
ATOM   1858 C  CB  . LEU   A 1 239 ? -11.855 -30.510 3.297   1.00 40.87  ?  271 LEU   A CB  1 
ATOM   1859 C  CG  . LEU   A 1 239 ? -12.751 -31.695 3.609   1.00 34.23  ?  271 LEU   A CG  1 
ATOM   1860 C  CD1 . LEU   A 1 239 ? -13.976 -31.226 4.251   1.00 34.38  ?  271 LEU   A CD1 1 
ATOM   1861 C  CD2 . LEU   A 1 239 ? -13.138 -32.436 2.409   1.00 34.60  ?  271 LEU   A CD2 1 
ATOM   1862 N  N   . GLN   A 1 240 ? -9.350  -28.668 2.902   1.00 40.32  ?  272 GLN   A N   1 
ATOM   1863 C  CA  . GLN   A 1 240 ? -8.666  -27.479 2.426   1.00 37.96  ?  272 GLN   A CA  1 
ATOM   1864 C  C   . GLN   A 1 240 ? -7.611  -27.843 1.407   1.00 35.13  ?  272 GLN   A C   1 
ATOM   1865 O  O   . GLN   A 1 240 ? -7.582  -27.311 0.310   1.00 42.60  ?  272 GLN   A O   1 
ATOM   1866 C  CB  . GLN   A 1 240 ? -7.993  -26.746 3.571   1.00 48.49  ?  272 GLN   A CB  1 
ATOM   1867 C  CG  . GLN   A 1 240 ? -8.833  -26.275 4.643   1.00 48.16  ?  272 GLN   A CG  1 
ATOM   1868 C  CD  . GLN   A 1 240 ? -8.089  -25.311 5.495   1.00 56.58  ?  272 GLN   A CD  1 
ATOM   1869 O  OE1 . GLN   A 1 240 ? -7.288  -25.686 6.336   1.00 60.48  ?  272 GLN   A OE1 1 
ATOM   1870 N  NE2 . GLN   A 1 240 ? -8.322  -24.053 5.264   1.00 71.02  ?  272 GLN   A NE2 1 
ATOM   1871 N  N   . ALA   A 1 241 ? -6.697  -28.723 1.778   1.00 37.72  ?  273 ALA   A N   1 
ATOM   1872 C  CA  . ALA   A 1 241 ? -5.666  -29.153 0.854   1.00 39.82  ?  273 ALA   A CA  1 
ATOM   1873 C  C   . ALA   A 1 241 ? -6.260  -29.666 -0.441  1.00 39.62  ?  273 ALA   A C   1 
ATOM   1874 O  O   . ALA   A 1 241 ? -5.854  -29.255 -1.522  1.00 46.62  ?  273 ALA   A O   1 
ATOM   1875 C  CB  . ALA   A 1 241 ? -4.825  -30.232 1.499   1.00 41.06  ?  273 ALA   A CB  1 
ATOM   1876 N  N   . ILE   A 1 242 ? -7.220  -30.574 -0.354  1.00 39.56  ?  274 ILE   A N   1 
ATOM   1877 C  CA  . ILE   A 1 242 ? -7.801  -31.116 -1.559  1.00 34.72  ?  274 ILE   A CA  1 
ATOM   1878 C  C   . ILE   A 1 242 ? -8.415  -30.012 -2.381  1.00 43.53  ?  274 ILE   A C   1 
ATOM   1879 O  O   . ILE   A 1 242 ? -8.496  -30.108 -3.605  1.00 51.28  ?  274 ILE   A O   1 
ATOM   1880 C  CB  . ILE   A 1 242 ? -8.844  -32.190 -1.241  1.00 39.96  ?  274 ILE   A CB  1 
ATOM   1881 C  CG1 . ILE   A 1 242 ? -8.299  -33.219 -0.265  1.00 46.52  ?  274 ILE   A CG1 1 
ATOM   1882 C  CG2 . ILE   A 1 242 ? -9.279  -32.813 -2.498  1.00 38.98  ?  274 ILE   A CG2 1 
ATOM   1883 C  CD1 . ILE   A 1 242 ? -8.635  -34.622 -0.555  1.00 53.15  ?  274 ILE   A CD1 1 
ATOM   1884 N  N   . GLU   A 1 243 ? -8.899  -28.969 -1.744  1.00 44.69  ?  275 GLU   A N   1 
ATOM   1885 C  CA  . GLU   A 1 243 ? -9.515  -27.907 -2.517  1.00 42.62  ?  275 GLU   A CA  1 
ATOM   1886 C  C   . GLU   A 1 243 ? -8.449  -27.064 -3.166  1.00 45.87  ?  275 GLU   A C   1 
ATOM   1887 O  O   . GLU   A 1 243 ? -8.612  -26.610 -4.297  1.00 53.08  ?  275 GLU   A O   1 
ATOM   1888 C  CB  . GLU   A 1 243 ? -10.408 -27.060 -1.630  1.00 46.95  ?  275 GLU   A CB  1 
ATOM   1889 C  CG  . GLU   A 1 243 ? -11.109 -25.963 -2.306  1.00 37.89  ?  275 GLU   A CG  1 
ATOM   1890 C  CD  . GLU   A 1 243 ? -11.555 -24.931 -1.356  1.00 39.04  ?  275 GLU   A CD  1 
ATOM   1891 O  OE1 . GLU   A 1 243 ? -10.934 -24.766 -0.278  1.00 33.06  ?  275 GLU   A OE1 1 
ATOM   1892 O  OE2 . GLU   A 1 243 ? -12.538 -24.277 -1.708  1.00 39.91  ?  275 GLU   A OE2 1 
ATOM   1893 N  N   . HIS   A 1 244 ? -7.333  -26.882 -2.476  1.00 48.89  ?  276 HIS   A N   1 
ATOM   1894 C  CA  . HIS   A 1 244 ? -6.230  -26.115 -3.020  1.00 48.20  ?  276 HIS   A CA  1 
ATOM   1895 C  C   . HIS   A 1 244 ? -5.642  -26.798 -4.235  1.00 52.38  ?  276 HIS   A C   1 
ATOM   1896 O  O   . HIS   A 1 244 ? -5.613  -26.227 -5.325  1.00 59.19  ?  276 HIS   A O   1 
ATOM   1897 C  CB  . HIS   A 1 244 ? -5.186  -25.934 -1.960  1.00 46.31  ?  276 HIS   A CB  1 
ATOM   1898 C  CG  . HIS   A 1 244 ? -4.126  -24.966 -2.328  1.00 57.96  ?  276 HIS   A CG  1 
ATOM   1899 N  ND1 . HIS   A 1 244 ? -4.258  -23.616 -2.118  1.00 63.30  ?  276 HIS   A ND1 1 
ATOM   1900 C  CD2 . HIS   A 1 244 ? -2.905  -25.148 -2.876  1.00 58.02  ?  276 HIS   A CD2 1 
ATOM   1901 C  CE1 . HIS   A 1 244 ? -3.165  -23.004 -2.524  1.00 61.05  ?  276 HIS   A CE1 1 
ATOM   1902 N  NE2 . HIS   A 1 244 ? -2.329  -23.911 -2.987  1.00 64.89  ?  276 HIS   A NE2 1 
ATOM   1903 N  N   . GLU   A 1 245 ? -5.193  -28.037 -4.078  1.00 52.91  ?  277 GLU   A N   1 
ATOM   1904 C  CA  . GLU   A 1 245 ? -4.566  -28.721 -5.200  1.00 54.34  ?  277 GLU   A CA  1 
ATOM   1905 C  C   . GLU   A 1 245 ? -5.515  -28.822 -6.370  1.00 52.22  ?  277 GLU   A C   1 
ATOM   1906 O  O   . GLU   A 1 245 ? -5.114  -28.634 -7.519  1.00 58.38  ?  277 GLU   A O   1 
ATOM   1907 C  CB  . GLU   A 1 245 ? -4.090  -30.105 -4.810  1.00 51.73  ?  277 GLU   A CB  1 
ATOM   1908 C  CG  . GLU   A 1 245 ? -3.375  -30.810 -5.909  1.00 61.25  ?  277 GLU   A CG  1 
ATOM   1909 C  CD  . GLU   A 1 245 ? -2.012  -30.234 -6.167  1.00 64.96  ?  277 GLU   A CD  1 
ATOM   1910 O  OE1 . GLU   A 1 245 ? -1.593  -29.361 -5.382  1.00 56.51  ?  277 GLU   A OE1 1 
ATOM   1911 O  OE2 . GLU   A 1 245 ? -1.361  -30.660 -7.143  1.00 62.52  ?  277 GLU   A OE2 1 
ATOM   1912 N  N   . LEU   A 1 246 ? -6.780  -29.118 -6.112  1.00 53.69  ?  278 LEU   A N   1 
ATOM   1913 C  CA  . LEU   A 1 246 ? -7.718  -29.146 -7.219  1.00 54.93  ?  278 LEU   A CA  1 
ATOM   1914 C  C   . LEU   A 1 246 ? -7.844  -27.783 -7.869  1.00 56.64  ?  278 LEU   A C   1 
ATOM   1915 O  O   . LEU   A 1 246 ? -8.260  -27.694 -9.024  1.00 54.88  ?  278 LEU   A O   1 
ATOM   1916 C  CB  . LEU   A 1 246 ? -9.073  -29.622 -6.746  1.00 53.84  ?  278 LEU   A CB  1 
ATOM   1917 C  CG  . LEU   A 1 246 ? -9.238  -31.107 -6.518  1.00 47.39  ?  278 LEU   A CG  1 
ATOM   1918 C  CD1 . LEU   A 1 246 ? -10.489 -31.332 -5.796  1.00 53.73  ?  278 LEU   A CD1 1 
ATOM   1919 C  CD2 . LEU   A 1 246 ? -9.333  -31.848 -7.790  1.00 53.40  ?  278 LEU   A CD2 1 
ATOM   1920 N  N   . HIS   A 1 247 ? -7.491  -26.720 -7.159  1.00 51.45  ?  279 HIS   A N   1 
ATOM   1921 C  CA  . HIS   A 1 247 ? -7.586  -25.406 -7.755  1.00 54.30  ?  279 HIS   A CA  1 
ATOM   1922 C  C   . HIS   A 1 247 ? -6.403  -25.124 -8.654  1.00 61.05  ?  279 HIS   A C   1 
ATOM   1923 O  O   . HIS   A 1 247 ? -6.575  -24.684 -9.789  1.00 65.61  ?  279 HIS   A O   1 
ATOM   1924 C  CB  . HIS   A 1 247 ? -7.664  -24.344 -6.689  1.00 52.85  ?  279 HIS   A CB  1 
ATOM   1925 C  CG  . HIS   A 1 247 ? -7.660  -22.978 -7.257  1.00 58.13  ?  279 HIS   A CG  1 
ATOM   1926 N  ND1 . HIS   A 1 247 ? -8.722  -22.476 -7.967  1.00 63.42  ?  279 HIS   A ND1 1 
ATOM   1927 C  CD2 . HIS   A 1 247 ? -6.702  -22.034 -7.291  1.00 54.22  ?  279 HIS   A CD2 1 
ATOM   1928 C  CE1 . HIS   A 1 247 ? -8.436  -21.258 -8.377  1.00 56.67  ?  279 HIS   A CE1 1 
ATOM   1929 N  NE2 . HIS   A 1 247 ? -7.214  -20.968 -7.982  1.00 57.71  ?  279 HIS   A NE2 1 
ATOM   1930 N  N   . GLU   A 1 248 ? -5.198  -25.365 -8.153  1.00 54.97  ?  280 GLU   A N   1 
ATOM   1931 C  CA  . GLU   A 1 248 ? -3.972  -25.125 -8.879  1.00 50.07  ?  280 GLU   A CA  1 
ATOM   1932 C  C   . GLU   A 1 248 ? -3.768  -26.096 -10.020 1.00 55.18  ?  280 GLU   A C   1 
ATOM   1933 O  O   . GLU   A 1 248 ? -2.794  -25.960 -10.748 1.00 66.09  ?  280 GLU   A O   1 
ATOM   1934 C  CB  . GLU   A 1 248 ? -2.787  -25.192 -7.920  1.00 45.11  ?  280 GLU   A CB  1 
ATOM   1935 C  CG  . GLU   A 1 248 ? -2.852  -24.178 -6.826  1.00 49.00  ?  280 GLU   A CG  1 
ATOM   1936 C  CD  . GLU   A 1 248 ? -1.918  -22.998 -6.989  1.00 60.71  ?  280 GLU   A CD  1 
ATOM   1937 O  OE1 . GLU   A 1 248 ? -0.985  -22.883 -6.185  1.00 69.30  ?  280 GLU   A OE1 1 
ATOM   1938 O  OE2 . GLU   A 1 248 ? -2.107  -22.164 -7.893  1.00 63.92  ?  280 GLU   A OE2 1 
ATOM   1939 N  N   . LEU   A 1 249 ? -4.633  -27.069 -10.202 1.00 47.72  ?  281 LEU   A N   1 
ATOM   1940 C  CA  . LEU   A 1 249 ? -4.602  -27.906 -11.383 1.00 51.22  ?  281 LEU   A CA  1 
ATOM   1941 C  C   . LEU   A 1 249 ? -5.624  -27.502 -12.426 1.00 55.26  ?  281 LEU   A C   1 
ATOM   1942 O  O   . LEU   A 1 249 ? -5.758  -28.192 -13.431 1.00 57.68  ?  281 LEU   A O   1 
ATOM   1943 C  CB  . LEU   A 1 249 ? -4.858  -29.358 -11.022 1.00 55.04  ?  281 LEU   A CB  1 
ATOM   1944 C  CG  . LEU   A 1 249 ? -3.949  -30.012 -10.019 1.00 58.62  ?  281 LEU   A CG  1 
ATOM   1945 C  CD1 . LEU   A 1 249 ? -4.556  -31.304 -9.635  1.00 59.81  ?  281 LEU   A CD1 1 
ATOM   1946 C  CD2 . LEU   A 1 249 ? -2.629  -30.255 -10.611 1.00 71.72  ?  281 LEU   A CD2 1 
ATOM   1947 N  N   . GLY   A 1 250 ? -6.377  -26.440 -12.208 1.00 60.03  ?  282 GLY   A N   1 
ATOM   1948 C  CA  . GLY   A 1 250 ? -7.358  -26.067 -13.197 1.00 66.10  ?  282 GLY   A CA  1 
ATOM   1949 C  C   . GLY   A 1 250 ? -8.508  -27.022 -13.278 1.00 54.12  ?  282 GLY   A C   1 
ATOM   1950 O  O   . GLY   A 1 250 ? -9.146  -27.132 -14.330 1.00 51.32  ?  282 GLY   A O   1 
ATOM   1951 N  N   . LEU   A 1 251 ? -8.798  -27.714 -12.188 1.00 52.68  ?  283 LEU   A N   1 
ATOM   1952 C  CA  . LEU   A 1 251 ? -9.843  -28.721 -12.166 1.00 64.26  ?  283 LEU   A CA  1 
ATOM   1953 C  C   . LEU   A 1 251 ? -11.136 -28.220 -11.543 1.00 60.92  ?  283 LEU   A C   1 
ATOM   1954 O  O   . LEU   A 1 251 ? -12.083 -28.992 -11.384 1.00 54.88  ?  283 LEU   A O   1 
ATOM   1955 C  CB  . LEU   A 1 251 ? -9.343  -29.944 -11.429 1.00 54.03  ?  283 LEU   A CB  1 
ATOM   1956 C  CG  . LEU   A 1 251 ? -8.190  -30.659 -12.095 1.00 45.76  ?  283 LEU   A CG  1 
ATOM   1957 C  CD1 . LEU   A 1 251 ? -7.571  -31.569 -11.138 1.00 54.68  ?  283 LEU   A CD1 1 
ATOM   1958 C  CD2 . LEU   A 1 251 ? -8.656  -31.449 -13.220 1.00 51.21  ?  283 LEU   A CD2 1 
ATOM   1959 N  N   . LEU   A 1 252 ? -11.206 -26.944 -11.221 1.00 61.08  ?  284 LEU   A N   1 
ATOM   1960 C  CA  . LEU   A 1 252 ? -12.357 -26.346 -10.591 1.00 53.73  ?  284 LEU   A CA  1 
ATOM   1961 C  C   . LEU   A 1 252 ? -12.889 -25.263 -11.505 1.00 56.56  ?  284 LEU   A C   1 
ATOM   1962 O  O   . LEU   A 1 252 ? -12.176 -24.781 -12.381 1.00 70.75  ?  284 LEU   A O   1 
ATOM   1963 C  CB  . LEU   A 1 252 ? -11.962 -25.781 -9.233  1.00 54.70  ?  284 LEU   A CB  1 
ATOM   1964 C  CG  . LEU   A 1 252 ? -12.172 -26.639 -7.991  1.00 46.38  ?  284 LEU   A CG  1 
ATOM   1965 C  CD1 . LEU   A 1 252 ? -12.114 -28.068 -8.247  1.00 52.59  ?  284 LEU   A CD1 1 
ATOM   1966 C  CD2 . LEU   A 1 252 ? -11.162 -26.332 -7.037  1.00 42.21  ?  284 LEU   A CD2 1 
ATOM   1967 N  N   . LYS   A 1 253 ? -14.149 -24.876 -11.307 1.00 55.60  ?  285 LYS   A N   1 
ATOM   1968 C  CA  . LYS   A 1 253 ? -14.802 -23.907 -12.177 1.00 52.34  ?  285 LYS   A CA  1 
ATOM   1969 C  C   . LYS   A 1 253 ? -15.252 -22.701 -11.389 1.00 47.14  ?  285 LYS   A C   1 
ATOM   1970 O  O   . LYS   A 1 253 ? -15.880 -22.833 -10.349 1.00 57.02  ?  285 LYS   A O   1 
ATOM   1971 C  CB  . LYS   A 1 253 ? -15.999 -24.502 -12.887 1.00 49.31  ?  285 LYS   A CB  1 
ATOM   1972 C  CG  . LYS   A 1 253 ? -15.719 -25.886 -13.422 1.00 70.70  ?  285 LYS   A CG  1 
ATOM   1973 C  CD  . LYS   A 1 253 ? -16.328 -26.152 -14.782 1.00 69.35  ?  285 LYS   A CD  1 
ATOM   1974 C  CE  . LYS   A 1 253 ? -15.539 -27.210 -15.519 1.00 65.84  ?  285 LYS   A CE  1 
ATOM   1975 N  NZ  . LYS   A 1 253 ? -16.349 -27.817 -16.569 1.00 63.67  ?  285 LYS   A NZ  1 
ATOM   1976 N  N   . ASP   A 1 254 ? -14.944 -21.528 -11.891 1.00 57.26  ?  286 ASP   A N   1 
ATOM   1977 C  CA  . ASP   A 1 254 ? -15.440 -20.314 -11.290 1.00 55.51  ?  286 ASP   A CA  1 
ATOM   1978 C  C   . ASP   A 1 254 ? -15.035 -20.256 -9.842  1.00 52.97  ?  286 ASP   A C   1 
ATOM   1979 O  O   . ASP   A 1 254 ? -15.777 -19.760 -9.011  1.00 59.68  ?  286 ASP   A O   1 
ATOM   1980 C  CB  . ASP   A 1 254 ? -16.952 -20.219 -11.427 1.00 65.13  ?  286 ASP   A CB  1 
ATOM   1981 C  CG  . ASP   A 1 254 ? -17.396 -19.993 -12.855 1.00 62.99  ?  286 ASP   A CG  1 
ATOM   1982 O  OD1 . ASP   A 1 254 ? -16.916 -19.016 -13.452 1.00 76.33  ?  286 ASP   A OD1 1 
ATOM   1983 O  OD2 . ASP   A 1 254 ? -18.210 -20.768 -13.391 1.00 55.50  ?  286 ASP   A OD2 1 
ATOM   1984 N  N   . HIS   A 1 255 ? -13.852 -20.785 -9.548  1.00 54.80  ?  287 HIS   A N   1 
ATOM   1985 C  CA  . HIS   A 1 255 ? -13.326 -20.911 -8.199  1.00 50.88  ?  287 HIS   A CA  1 
ATOM   1986 C  C   . HIS   A 1 255 ? -12.161 -19.972 -7.984  1.00 50.91  ?  287 HIS   A C   1 
ATOM   1987 O  O   . HIS   A 1 255 ? -11.308 -19.822 -8.855  1.00 55.95  ?  287 HIS   A O   1 
ATOM   1988 C  CB  . HIS   A 1 255 ? -12.858 -22.330 -7.952  1.00 55.55  ?  287 HIS   A CB  1 
ATOM   1989 C  CG  . HIS   A 1 255 ? -12.487 -22.621 -6.536  1.00 49.99  ?  287 HIS   A CG  1 
ATOM   1990 N  ND1 . HIS   A 1 255 ? -11.207 -22.923 -6.152  1.00 44.24  ?  287 HIS   A ND1 1 
ATOM   1991 C  CD2 . HIS   A 1 255 ? -13.233 -22.698 -5.421  1.00 51.28  ?  287 HIS   A CD2 1 
ATOM   1992 C  CE1 . HIS   A 1 255 ? -11.176 -23.154 -4.860  1.00 44.83  ?  287 HIS   A CE1 1 
ATOM   1993 N  NE2 . HIS   A 1 255 ? -12.394 -23.036 -4.393  1.00 44.73  ?  287 HIS   A NE2 1 
ATOM   1994 N  N   . SER   A 1 256 ? -12.100 -19.397 -6.794  1.00 51.50  ?  288 SER   A N   1 
ATOM   1995 C  CA  . SER   A 1 256 ? -11.055 -18.466 -6.416  1.00 47.92  ?  288 SER   A CA  1 
ATOM   1996 C  C   . SER   A 1 256 ? -10.485 -18.801 -5.051  1.00 49.32  ?  288 SER   A C   1 
ATOM   1997 O  O   . SER   A 1 256 ? -11.235 -18.986 -4.102  1.00 59.47  ?  288 SER   A O   1 
ATOM   1998 C  CB  . SER   A 1 256 ? -11.599 -17.076 -6.341  1.00 49.16  ?  288 SER   A CB  1 
ATOM   1999 O  OG  . SER   A 1 256 ? -11.075 -16.522 -5.158  1.00 59.55  ?  288 SER   A OG  1 
ATOM   2000 N  N   . LEU   A 1 257 ? -9.171  -18.794 -4.923  1.00 53.13  ?  289 LEU   A N   1 
ATOM   2001 C  CA  . LEU   A 1 257 ? -8.588  -19.008 -3.616  1.00 57.75  ?  289 LEU   A CA  1 
ATOM   2002 C  C   . LEU   A 1 257 ? -8.940  -17.891 -2.659  1.00 59.24  ?  289 LEU   A C   1 
ATOM   2003 O  O   . LEU   A 1 257 ? -8.897  -18.087 -1.443  1.00 58.20  ?  289 LEU   A O   1 
ATOM   2004 C  CB  . LEU   A 1 257 ? -7.073  -19.146 -3.730  1.00 61.77  ?  289 LEU   A CB  1 
ATOM   2005 C  CG  . LEU   A 1 257 ? -6.562  -20.335 -4.532  1.00 60.34  ?  289 LEU   A CG  1 
ATOM   2006 C  CD1 . LEU   A 1 257 ? -5.058  -20.233 -4.658  1.00 63.37  ?  289 LEU   A CD1 1 
ATOM   2007 C  CD2 . LEU   A 1 257 ? -6.944  -21.659 -3.920  1.00 55.67  ?  289 LEU   A CD2 1 
ATOM   2008 N  N   . GLU   A 1 258 ? -9.288  -16.725 -3.161  1.00 61.60  ?  290 GLU   A N   1 
ATOM   2009 C  CA  . GLU   A 1 258 ? -9.729  -15.690 -2.253  1.00 67.37  ?  290 GLU   A CA  1 
ATOM   2010 C  C   . GLU   A 1 258 ? -11.154 -15.923 -1.823  1.00 67.76  ?  290 GLU   A C   1 
ATOM   2011 O  O   . GLU   A 1 258 ? -11.670 -15.176 -0.991  1.00 61.56  ?  290 GLU   A O   1 
ATOM   2012 C  CB  . GLU   A 1 258 ? -9.575  -14.321 -2.902  1.00 73.06  ?  290 GLU   A CB  1 
ATOM   2013 C  CG  . GLU   A 1 258 ? -8.133  -13.857 -2.955  1.00 92.09  ?  290 GLU   A CG  1 
ATOM   2014 C  CD  . GLU   A 1 258 ? -7.945  -12.516 -3.627  1.00 106.82 ?  290 GLU   A CD  1 
ATOM   2015 O  OE1 . GLU   A 1 258 ? -7.278  -11.650 -3.025  1.00 111.27 ?  290 GLU   A OE1 1 
ATOM   2016 O  OE2 . GLU   A 1 258 ? -8.447  -12.330 -4.756  1.00 109.71 ?  290 GLU   A OE2 1 
ATOM   2017 N  N   . GLY   A 1 259 ? -11.780 -16.950 -2.385  1.00 63.71  ?  291 GLY   A N   1 
ATOM   2018 C  CA  . GLY   A 1 259 ? -13.107 -17.373 -2.026  1.00 55.52  ?  291 GLY   A CA  1 
ATOM   2019 C  C   . GLY   A 1 259 ? -13.172 -18.854 -1.754  1.00 45.88  ?  291 GLY   A C   1 
ATOM   2020 O  O   . GLY   A 1 259 ? -14.145 -19.501 -2.117  1.00 40.14  ?  291 GLY   A O   1 
ATOM   2021 N  N   . ARG   A 1 260 ? -12.147 -19.403 -1.119  1.00 50.24  ?  292 ARG   A N   1 
ATOM   2022 C  CA  . ARG   A 1 260 ? -12.111 -20.836 -0.891  1.00 52.67  ?  292 ARG   A CA  1 
ATOM   2023 C  C   . ARG   A 1 260 ? -13.365 -21.199 -0.130  1.00 50.99  ?  292 ARG   A C   1 
ATOM   2024 O  O   . ARG   A 1 260 ? -14.008 -20.332 0.456   1.00 53.79  ?  292 ARG   A O   1 
ATOM   2025 C  CB  . ARG   A 1 260 ? -10.879 -21.287 -0.104  1.00 58.88  ?  292 ARG   A CB  1 
ATOM   2026 C  CG  . ARG   A 1 260 ? -9.629  -20.615 -0.465  1.00 67.93  ?  292 ARG   A CG  1 
ATOM   2027 C  CD  . ARG   A 1 260 ? -8.390  -21.451 -0.128  1.00 81.07  ?  292 ARG   A CD  1 
ATOM   2028 N  NE  . ARG   A 1 260 ? -8.190  -21.645 1.297   1.00 88.00  ?  292 ARG   A NE  1 
ATOM   2029 C  CZ  . ARG   A 1 260 ? -7.952  -20.667 2.169   1.00 97.21  ?  292 ARG   A CZ  1 
ATOM   2030 N  NH1 . ARG   A 1 260 ? -7.900  -19.398 1.786   1.00 98.01  ?  292 ARG   A NH1 1 
ATOM   2031 N  NH2 . ARG   A 1 260 ? -7.769  -20.952 3.448   1.00 93.00  ?  292 ARG   A NH2 1 
ATOM   2032 N  N   . TYR   A 1 261 ? -13.726 -22.463 -0.142  1.00 42.64  ?  293 TYR   A N   1 
ATOM   2033 C  CA  . TYR   A 1 261 ? -14.843 -22.908 0.647   1.00 35.67  ?  293 TYR   A CA  1 
ATOM   2034 C  C   . TYR   A 1 261 ? -14.456 -23.334 2.044   1.00 41.33  ?  293 TYR   A C   1 
ATOM   2035 O  O   . TYR   A 1 261 ? -15.303 -23.344 2.925   1.00 46.49  ?  293 TYR   A O   1 
ATOM   2036 C  CB  . TYR   A 1 261 ? -15.506 -24.090 -0.031  1.00 43.24  ?  293 TYR   A CB  1 
ATOM   2037 C  CG  . TYR   A 1 261 ? -15.895 -23.904 -1.452  1.00 37.75  ?  293 TYR   A CG  1 
ATOM   2038 C  CD1 . TYR   A 1 261 ? -16.437 -22.737 -1.875  1.00 41.57  ?  293 TYR   A CD1 1 
ATOM   2039 C  CD2 . TYR   A 1 261 ? -15.742 -24.920 -2.359  1.00 36.34  ?  293 TYR   A CD2 1 
ATOM   2040 C  CE1 . TYR   A 1 261 ? -16.811 -22.569 -3.145  1.00 41.21  ?  293 TYR   A CE1 1 
ATOM   2041 C  CE2 . TYR   A 1 261 ? -16.108 -24.759 -3.646  1.00 41.97  ?  293 TYR   A CE2 1 
ATOM   2042 C  CZ  . TYR   A 1 261 ? -16.645 -23.572 -4.032  1.00 44.58  ?  293 TYR   A CZ  1 
ATOM   2043 O  OH  . TYR   A 1 261 ? -17.025 -23.343 -5.318  1.00 46.77  ?  293 TYR   A OH  1 
ATOM   2044 N  N   . PHE   A 1 262 ? -13.222 -23.737 2.273   1.00 47.98  ?  294 PHE   A N   1 
ATOM   2045 C  CA  . PHE   A 1 262 ? -12.810 -24.298 3.546   1.00 40.16  ?  294 PHE   A CA  1 
ATOM   2046 C  C   . PHE   A 1 262 ? -11.756 -23.396 4.152   1.00 46.60  ?  294 PHE   A C   1 
ATOM   2047 O  O   . PHE   A 1 262 ? -10.571 -23.646 3.990   1.00 56.28  ?  294 PHE   A O   1 
ATOM   2048 C  CB  . PHE   A 1 262 ? -12.304 -25.693 3.347   1.00 45.47  ?  294 PHE   A CB  1 
ATOM   2049 C  CG  . PHE   A 1 262 ? -13.353 -26.648 2.837   1.00 45.13  ?  294 PHE   A CG  1 
ATOM   2050 C  CD1 . PHE   A 1 262 ? -14.315 -27.153 3.665   1.00 42.31  ?  294 PHE   A CD1 1 
ATOM   2051 C  CD2 . PHE   A 1 262 ? -13.385 -27.023 1.529   1.00 48.29  ?  294 PHE   A CD2 1 
ATOM   2052 C  CE1 . PHE   A 1 262 ? -15.279 -27.997 3.180   1.00 35.50  ?  294 PHE   A CE1 1 
ATOM   2053 C  CE2 . PHE   A 1 262 ? -14.355 -27.874 1.065   1.00 39.02  ?  294 PHE   A CE2 1 
ATOM   2054 C  CZ  . PHE   A 1 262 ? -15.290 -28.345 1.897   1.00 30.95  ?  294 PHE   A CZ  1 
ATOM   2055 N  N   . GLN   A 1 263 ? -12.189 -22.377 4.877   1.00 55.63  ?  295 GLN   A N   1 
ATOM   2056 C  CA  . GLN   A 1 263 ? -11.303 -21.424 5.527   1.00 65.13  ?  295 GLN   A CA  1 
ATOM   2057 C  C   . GLN   A 1 263 ? -11.006 -21.865 6.938   1.00 76.68  ?  295 GLN   A C   1 
ATOM   2058 O  O   . GLN   A 1 263 ? -11.911 -22.300 7.646   1.00 77.31  ?  295 GLN   A O   1 
ATOM   2059 C  CB  . GLN   A 1 263 ? -11.942 -20.057 5.617   1.00 75.93  ?  295 GLN   A CB  1 
ATOM   2060 C  CG  . GLN   A 1 263 ? -11.929 -19.306 4.377   1.00 81.26  ?  295 GLN   A CG  1 
ATOM   2061 C  CD  . GLN   A 1 263 ? -13.206 -18.573 4.187   1.00 73.92  ?  295 GLN   A CD  1 
ATOM   2062 O  OE1 . GLN   A 1 263 ? -13.715 -17.939 5.104   1.00 70.54  ?  295 GLN   A OE1 1 
ATOM   2063 N  NE2 . GLN   A 1 263 ? -13.762 -18.681 3.002   1.00 73.71  ?  295 GLN   A NE2 1 
ATOM   2064 N  N   . ASN   A 1 264 ? -9.763  -21.679 7.379   1.00 83.35  ?  296 ASN   A N   1 
ATOM   2065 C  CA  . ASN   A 1 264 ? -9.435  -22.092 8.737   1.00 90.84  ?  296 ASN   A CA  1 
ATOM   2066 C  C   . ASN   A 1 264 ? -10.006 -21.048 9.686   1.00 90.33  ?  296 ASN   A C   1 
ATOM   2067 O  O   . ASN   A 1 264 ? -9.275  -20.310 10.346  1.00 88.85  ?  296 ASN   A O   1 
ATOM   2068 C  CB  . ASN   A 1 264 ? -7.922  -22.305 8.918   1.00 99.18  ?  296 ASN   A CB  1 
ATOM   2069 C  CG  . ASN   A 1 264 ? -7.572  -23.738 9.438   1.00 108.44 ?  296 ASN   A CG  1 
ATOM   2070 O  OD1 . ASN   A 1 264 ? -8.384  -24.397 10.115  1.00 91.07  ?  296 ASN   A OD1 1 
ATOM   2071 N  ND2 . ASN   A 1 264 ? -6.355  -24.206 9.126   1.00 95.11  ?  296 ASN   A ND2 1 
ATOM   2072 N  N   . TYR   A 1 265 ? -11.328 -20.970 9.721   1.00 99.24  ?  297 TYR   A N   1 
ATOM   2073 C  CA  . TYR   A 1 265 ? -12.074 -20.125 10.637  1.00 95.91  ?  297 TYR   A CA  1 
ATOM   2074 C  C   . TYR   A 1 265 ? -12.785 -21.090 11.578  1.00 97.83  ?  297 TYR   A C   1 
ATOM   2075 O  O   . TYR   A 1 265 ? -13.540 -21.952 11.122  1.00 91.31  ?  297 TYR   A O   1 
ATOM   2076 C  CB  . TYR   A 1 265 ? -13.026 -19.206 9.850   1.00 93.57  ?  297 TYR   A CB  1 
ATOM   2077 C  CG  . TYR   A 1 265 ? -14.443 -19.002 10.384  1.00 109.13 ?  297 TYR   A CG  1 
ATOM   2078 C  CD1 . TYR   A 1 265 ? -14.685 -18.731 11.737  1.00 116.36 ?  297 TYR   A CD1 1 
ATOM   2079 C  CD2 . TYR   A 1 265 ? -15.545 -19.044 9.517   1.00 101.68 ?  297 TYR   A CD2 1 
ATOM   2080 C  CE1 . TYR   A 1 265 ? -15.984 -18.543 12.223  1.00 108.05 ?  297 TYR   A CE1 1 
ATOM   2081 C  CE2 . TYR   A 1 265 ? -16.855 -18.854 9.994   1.00 97.10  ?  297 TYR   A CE2 1 
ATOM   2082 C  CZ  . TYR   A 1 265 ? -17.060 -18.603 11.350  1.00 107.47 ?  297 TYR   A CZ  1 
ATOM   2083 O  OH  . TYR   A 1 265 ? -18.334 -18.411 11.845  1.00 96.51  ?  297 TYR   A OH  1 
ATOM   2084 N  N   . SER   A 1 266 ? -12.474 -21.004 12.871  1.00 103.88 ?  298 SER   A N   1 
ATOM   2085 C  CA  . SER   A 1 266 ? -13.043 -21.895 13.874  1.00 99.65  ?  298 SER   A CA  1 
ATOM   2086 C  C   . SER   A 1 266 ? -14.396 -21.374 14.360  1.00 110.00 ?  298 SER   A C   1 
ATOM   2087 O  O   . SER   A 1 266 ? -14.693 -20.178 14.297  1.00 112.61 ?  298 SER   A O   1 
ATOM   2088 C  CB  . SER   A 1 266 ? -12.083 -22.044 15.054  1.00 108.09 ?  298 SER   A CB  1 
ATOM   2089 O  OG  . SER   A 1 266 ? -11.752 -20.784 15.606  1.00 106.22 ?  298 SER   A OG  1 
ATOM   2090 N  N   . TYR   A 1 267 ? -15.222 -22.290 14.861  1.00 100.26 ?  299 TYR   A N   1 
ATOM   2091 C  CA  . TYR   A 1 267 ? -16.594 -21.963 15.249  1.00 102.91 ?  299 TYR   A CA  1 
ATOM   2092 C  C   . TYR   A 1 267 ? -16.810 -22.441 16.674  1.00 103.74 ?  299 TYR   A C   1 
ATOM   2093 O  O   . TYR   A 1 267 ? -16.990 -23.639 16.916  1.00 90.72  ?  299 TYR   A O   1 
ATOM   2094 C  CB  . TYR   A 1 267 ? -17.604 -22.598 14.312  1.00 90.16  ?  299 TYR   A CB  1 
ATOM   2095 C  CG  . TYR   A 1 267 ? -18.999 -21.999 14.352  1.00 90.33  ?  299 TYR   A CG  1 
ATOM   2096 C  CD1 . TYR   A 1 267 ? -19.337 -20.915 13.557  1.00 89.29  ?  299 TYR   A CD1 1 
ATOM   2097 C  CD2 . TYR   A 1 267 ? -19.986 -22.542 15.157  1.00 93.27  ?  299 TYR   A CD2 1 
ATOM   2098 C  CE1 . TYR   A 1 267 ? -20.611 -20.389 13.576  1.00 86.65  ?  299 TYR   A CE1 1 
ATOM   2099 C  CE2 . TYR   A 1 267 ? -21.260 -22.015 15.181  1.00 88.15  ?  299 TYR   A CE2 1 
ATOM   2100 C  CZ  . TYR   A 1 267 ? -21.564 -20.945 14.389  1.00 84.43  ?  299 TYR   A CZ  1 
ATOM   2101 O  OH  . TYR   A 1 267 ? -22.835 -20.437 14.418  1.00 85.04  ?  299 TYR   A OH  1 
ATOM   2102 N  N   . GLY   A 1 268 ? -16.818 -21.487 17.603  1.00 108.07 ?  300 GLY   A N   1 
ATOM   2103 C  CA  . GLY   A 1 268 ? -16.974 -21.834 19.001  1.00 107.55 ?  300 GLY   A CA  1 
ATOM   2104 C  C   . GLY   A 1 268 ? -18.349 -22.387 19.313  1.00 109.59 ?  300 GLY   A C   1 
ATOM   2105 O  O   . GLY   A 1 268 ? -18.478 -23.399 20.007  1.00 115.89 ?  300 GLY   A O   1 
ATOM   2106 N  N   . GLY   A 1 269 ? -19.392 -21.717 18.835  1.00 113.83 ?  301 GLY   A N   1 
ATOM   2107 C  CA  . GLY   A 1 269 ? -20.754 -22.090 19.157  1.00 115.17 ?  301 GLY   A CA  1 
ATOM   2108 C  C   . GLY   A 1 269 ? -21.201 -23.389 18.501  1.00 107.72 ?  301 GLY   A C   1 
ATOM   2109 O  O   . GLY   A 1 269 ? -20.422 -24.153 17.925  1.00 98.47  ?  301 GLY   A O   1 
ATOM   2110 N  N   . VAL   A 1 270 ? -22.511 -23.629 18.591  1.00 90.27  ?  302 VAL   A N   1 
ATOM   2111 C  CA  . VAL   A 1 270 ? -23.057 -24.917 18.207  1.00 87.31  ?  302 VAL   A CA  1 
ATOM   2112 C  C   . VAL   A 1 270 ? -24.185 -24.728 17.205  1.00 81.37  ?  302 VAL   A C   1 
ATOM   2113 O  O   . VAL   A 1 270 ? -24.803 -23.668 17.105  1.00 80.98  ?  302 VAL   A O   1 
ATOM   2114 C  CB  . VAL   A 1 270 ? -23.539 -25.722 19.425  1.00 78.99  ?  302 VAL   A CB  1 
ATOM   2115 C  CG1 . VAL   A 1 270 ? -24.980 -25.390 19.780  1.00 77.34  ?  302 VAL   A CG1 1 
ATOM   2116 C  CG2 . VAL   A 1 270 ? -23.356 -27.201 19.159  1.00 87.60  ?  302 VAL   A CG2 1 
ATOM   2117 N  N   . ILE   A 1 271 ? -24.426 -25.791 16.447  1.00 72.91  ?  303 ILE   A N   1 
ATOM   2118 C  CA  . ILE   A 1 271 ? -25.503 -25.882 15.478  1.00 62.06  ?  303 ILE   A CA  1 
ATOM   2119 C  C   . ILE   A 1 271 ? -26.154 -27.225 15.688  1.00 58.53  ?  303 ILE   A C   1 
ATOM   2120 O  O   . ILE   A 1 271 ? -25.456 -28.239 15.755  1.00 61.37  ?  303 ILE   A O   1 
ATOM   2121 C  CB  . ILE   A 1 271 ? -24.999 -25.772 14.033  1.00 60.36  ?  303 ILE   A CB  1 
ATOM   2122 C  CG1 . ILE   A 1 271 ? -24.684 -24.330 13.699  1.00 61.61  ?  303 ILE   A CG1 1 
ATOM   2123 C  CG2 . ILE   A 1 271 ? -26.031 -26.288 13.085  1.00 61.55  ?  303 ILE   A CG2 1 
ATOM   2124 C  CD1 . ILE   A 1 271 ? -24.204 -24.120 12.293  1.00 54.75  ?  303 ILE   A CD1 1 
ATOM   2125 N  N   . GLN   A 1 272 ? -27.476 -27.238 15.778  1.00 55.46  ?  304 GLN   A N   1 
ATOM   2126 C  CA  . GLN   A 1 272 ? -28.210 -28.478 15.985  1.00 52.41  ?  304 GLN   A CA  1 
ATOM   2127 C  C   . GLN   A 1 272 ? -28.480 -29.141 14.639  1.00 40.24  ?  304 GLN   A C   1 
ATOM   2128 O  O   . GLN   A 1 272 ? -28.765 -28.469 13.653  1.00 43.89  ?  304 GLN   A O   1 
ATOM   2129 C  CB  . GLN   A 1 272 ? -29.507 -28.179 16.733  1.00 61.53  ?  304 GLN   A CB  1 
ATOM   2130 C  CG  . GLN   A 1 272 ? -29.594 -28.689 18.195  1.00 63.56  ?  304 GLN   A CG  1 
ATOM   2131 C  CD  . GLN   A 1 272 ? -28.449 -28.251 19.061  1.00 62.60  ?  304 GLN   A CD  1 
ATOM   2132 O  OE1 . GLN   A 1 272 ? -28.222 -27.056 19.276  1.00 57.43  ?  304 GLN   A OE1 1 
ATOM   2133 N  NE2 . GLN   A 1 272 ? -27.726 -29.226 19.587  1.00 59.59  ?  304 GLN   A NE2 1 
ATOM   2134 N  N   . ASP   A 1 273 ? -28.326 -30.452 14.574  1.00 31.31  ?  305 ASP   A N   1 
ATOM   2135 C  CA  . ASP   A 1 273 ? -28.402 -31.149 13.294  1.00 39.79  ?  305 ASP   A CA  1 
ATOM   2136 C  C   . ASP   A 1 273 ? -28.170 -32.634 13.559  1.00 38.01  ?  305 ASP   A C   1 
ATOM   2137 O  O   . ASP   A 1 273 ? -27.779 -33.033 14.655  1.00 43.62  ?  305 ASP   A O   1 
ATOM   2138 C  CB  . ASP   A 1 273 ? -27.389 -30.580 12.278  1.00 47.14  ?  305 ASP   A CB  1 
ATOM   2139 C  CG  . ASP   A 1 273 ? -27.766 -30.855 10.817  1.00 46.73  ?  305 ASP   A CG  1 
ATOM   2140 O  OD1 . ASP   A 1 273 ? -28.663 -31.657 10.545  1.00 42.72  ?  305 ASP   A OD1 1 
ATOM   2141 O  OD2 . ASP   A 1 273 ? -27.151 -30.264 9.920   1.00 38.49  ?  305 ASP   A OD2 1 
ATOM   2142 N  N   . ASP   A 1 274 ? -28.380 -33.449 12.536  1.00 36.47  ?  306 ASP   A N   1 
ATOM   2143 C  CA  . ASP   A 1 274 ? -28.382 -34.899 12.701  1.00 46.43  ?  306 ASP   A CA  1 
ATOM   2144 C  C   . ASP   A 1 274 ? -27.093 -35.479 13.264  1.00 48.59  ?  306 ASP   A C   1 
ATOM   2145 O  O   . ASP   A 1 274 ? -26.978 -36.697 13.415  1.00 51.71  ?  306 ASP   A O   1 
ATOM   2146 C  CB  . ASP   A 1 274 ? -28.649 -35.600 11.377  1.00 43.45  ?  306 ASP   A CB  1 
ATOM   2147 C  CG  . ASP   A 1 274 ? -30.012 -35.333 10.842  1.00 45.36  ?  306 ASP   A CG  1 
ATOM   2148 O  OD1 . ASP   A 1 274 ? -30.950 -35.159 11.635  1.00 49.64  ?  306 ASP   A OD1 1 
ATOM   2149 O  OD2 . ASP   A 1 274 ? -30.145 -35.297 9.613   1.00 43.84  ?  306 ASP   A OD2 1 
ATOM   2150 N  N   . HIS   A 1 275 ? -26.110 -34.657 13.554  1.00 47.01  ?  307 HIS   A N   1 
ATOM   2151 C  CA  . HIS   A 1 275 ? -24.878 -35.176 14.098  1.00 43.44  ?  307 HIS   A CA  1 
ATOM   2152 C  C   . HIS   A 1 275 ? -24.909 -35.250 15.606  1.00 49.32  ?  307 HIS   A C   1 
ATOM   2153 O  O   . HIS   A 1 275 ? -24.176 -36.062 16.176  1.00 50.27  ?  307 HIS   A O   1 
ATOM   2154 C  CB  . HIS   A 1 275 ? -23.713 -34.320 13.636  1.00 36.47  ?  307 HIS   A CB  1 
ATOM   2155 C  CG  . HIS   A 1 275 ? -23.734 -32.943 14.180  1.00 34.39  ?  307 HIS   A CG  1 
ATOM   2156 N  ND1 . HIS   A 1 275 ? -24.530 -31.965 13.659  1.00 32.99  ?  307 HIS   A ND1 1 
ATOM   2157 C  CD2 . HIS   A 1 275 ? -23.053 -32.371 15.193  1.00 47.88  ?  307 HIS   A CD2 1 
ATOM   2158 C  CE1 . HIS   A 1 275 ? -24.371 -30.852 14.345  1.00 45.58  ?  307 HIS   A CE1 1 
ATOM   2159 N  NE2 . HIS   A 1 275 ? -23.472 -31.068 15.278  1.00 48.51  ?  307 HIS   A NE2 1 
ATOM   2160 N  N   . ILE   A 1 276 ? -25.766 -34.472 16.260  1.00 46.22  ?  308 ILE   A N   1 
ATOM   2161 C  CA  . ILE   A 1 276 ? -25.762 -34.400 17.723  1.00 51.43  ?  308 ILE   A CA  1 
ATOM   2162 C  C   . ILE   A 1 276 ? -25.993 -35.774 18.346  1.00 51.36  ?  308 ILE   A C   1 
ATOM   2163 O  O   . ILE   A 1 276 ? -25.189 -36.224 19.167  1.00 53.95  ?  308 ILE   A O   1 
ATOM   2164 C  CB  . ILE   A 1 276 ? -26.797 -33.400 18.241  1.00 43.48  ?  308 ILE   A CB  1 
ATOM   2165 C  CG1 . ILE   A 1 276 ? -26.557 -32.020 17.641  1.00 47.92  ?  308 ILE   A CG1 1 
ATOM   2166 C  CG2 . ILE   A 1 276 ? -26.719 -33.368 19.721  1.00 48.88  ?  308 ILE   A CG2 1 
ATOM   2167 C  CD1 . ILE   A 1 276 ? -25.417 -31.269 18.183  1.00 50.62  ?  308 ILE   A CD1 1 
ATOM   2168 N  N   . PRO   A 1 277 ? -27.046 -36.450 18.022  1.00 43.82  ?  309 PRO   A N   1 
ATOM   2169 C  CA  . PRO   A 1 277 ? -27.210 -37.811 18.503  1.00 50.83  ?  309 PRO   A CA  1 
ATOM   2170 C  C   . PRO   A 1 277 ? -25.984 -38.678 18.393  1.00 48.51  ?  309 PRO   A C   1 
ATOM   2171 O  O   . PRO   A 1 277 ? -25.834 -39.608 19.172  1.00 50.43  ?  309 PRO   A O   1 
ATOM   2172 C  CB  . PRO   A 1 277 ? -28.320 -38.351 17.605  1.00 44.93  ?  309 PRO   A CB  1 
ATOM   2173 C  CG  . PRO   A 1 277 ? -28.887 -37.232 16.945  1.00 50.12  ?  309 PRO   A CG  1 
ATOM   2174 C  CD  . PRO   A 1 277 ? -28.306 -35.978 17.474  1.00 49.67  ?  309 PRO   A CD  1 
ATOM   2175 N  N   . PHE   A 1 278 ? -25.137 -38.433 17.411  1.00 51.38  ?  310 PHE   A N   1 
ATOM   2176 C  CA  . PHE   A 1 278 ? -23.939 -39.228 17.250  1.00 47.27  ?  310 PHE   A CA  1 
ATOM   2177 C  C   . PHE   A 1 278 ? -22.729 -38.569 17.863  1.00 49.01  ?  310 PHE   A C   1 
ATOM   2178 O  O   . PHE   A 1 278 ? -21.737 -39.246 18.129  1.00 42.64  ?  310 PHE   A O   1 
ATOM   2179 C  CB  . PHE   A 1 278 ? -23.663 -39.465 15.780  1.00 49.08  ?  310 PHE   A CB  1 
ATOM   2180 C  CG  . PHE   A 1 278 ? -24.698 -40.272 15.086  1.00 44.56  ?  310 PHE   A CG  1 
ATOM   2181 C  CD1 . PHE   A 1 278 ? -25.804 -39.677 14.550  1.00 40.18  ?  310 PHE   A CD1 1 
ATOM   2182 C  CD2 . PHE   A 1 278 ? -24.537 -41.621 14.928  1.00 46.07  ?  310 PHE   A CD2 1 
ATOM   2183 C  CE1 . PHE   A 1 278 ? -26.715 -40.406 13.903  1.00 36.03  ?  310 PHE   A CE1 1 
ATOM   2184 C  CE2 . PHE   A 1 278 ? -25.467 -42.342 14.279  1.00 50.64  ?  310 PHE   A CE2 1 
ATOM   2185 C  CZ  . PHE   A 1 278 ? -26.545 -41.737 13.768  1.00 40.86  ?  310 PHE   A CZ  1 
ATOM   2186 N  N   . LEU   A 1 279 ? -22.782 -37.259 18.048  1.00 49.54  ?  311 LEU   A N   1 
ATOM   2187 C  CA  . LEU   A 1 279 ? -21.710 -36.522 18.680  1.00 50.07  ?  311 LEU   A CA  1 
ATOM   2188 C  C   . LEU   A 1 279 ? -21.707 -36.864 20.156  1.00 58.52  ?  311 LEU   A C   1 
ATOM   2189 O  O   . LEU   A 1 279 ? -20.828 -37.579 20.631  1.00 64.17  ?  311 LEU   A O   1 
ATOM   2190 C  CB  . LEU   A 1 279 ? -21.897 -35.022 18.452  1.00 45.68  ?  311 LEU   A CB  1 
ATOM   2191 C  CG  . LEU   A 1 279 ? -20.709 -34.133 18.744  1.00 41.30  ?  311 LEU   A CG  1 
ATOM   2192 C  CD1 . LEU   A 1 279 ? -19.733 -34.368 17.678  1.00 56.41  ?  311 LEU   A CD1 1 
ATOM   2193 C  CD2 . LEU   A 1 279 ? -21.049 -32.705 18.752  1.00 37.06  ?  311 LEU   A CD2 1 
ATOM   2194 N  N   . ARG   A 1 280 ? -22.737 -36.415 20.869  1.00 60.89  ?  312 ARG   A N   1 
ATOM   2195 C  CA  . ARG   A 1 280 ? -22.831 -36.599 22.308  1.00 57.42  ?  312 ARG   A CA  1 
ATOM   2196 C  C   . ARG   A 1 280 ? -22.437 -37.998 22.750  1.00 57.95  ?  312 ARG   A C   1 
ATOM   2197 O  O   . ARG   A 1 280 ? -22.024 -38.172 23.896  1.00 66.78  ?  312 ARG   A O   1 
ATOM   2198 C  CB  . ARG   A 1 280 ? -24.251 -36.294 22.767  1.00 66.36  ?  312 ARG   A CB  1 
ATOM   2199 C  CG  . ARG   A 1 280 ? -24.674 -34.815 22.666  1.00 65.94  ?  312 ARG   A CG  1 
ATOM   2200 C  CD  . ARG   A 1 280 ? -25.955 -34.544 23.475  1.00 76.99  ?  312 ARG   A CD  1 
ATOM   2201 N  NE  . ARG   A 1 280 ? -27.198 -34.953 22.808  1.00 80.96  ?  312 ARG   A NE  1 
ATOM   2202 C  CZ  . ARG   A 1 280 ? -27.734 -36.181 22.828  1.00 85.13  ?  312 ARG   A CZ  1 
ATOM   2203 N  NH1 . ARG   A 1 280 ? -27.161 -37.183 23.478  1.00 73.45  ?  312 ARG   A NH1 1 
ATOM   2204 N  NH2 . ARG   A 1 280 ? -28.869 -36.420 22.173  1.00 85.66  ?  312 ARG   A NH2 1 
ATOM   2205 N  N   . ARG   A 1 281 ? -22.554 -38.995 21.879  1.00 49.46  ?  313 ARG   A N   1 
ATOM   2206 C  CA  . ARG   A 1 281 ? -22.037 -40.337 22.111  1.00 55.22  ?  313 ARG   A CA  1 
ATOM   2207 C  C   . ARG   A 1 281 ? -20.621 -40.513 21.583  1.00 65.92  ?  313 ARG   A C   1 
ATOM   2208 O  O   . ARG   A 1 281 ? -20.214 -41.643 21.281  1.00 51.04  ?  313 ARG   A O   1 
ATOM   2209 C  CB  . ARG   A 1 281 ? -22.933 -41.386 21.441  1.00 62.32  ?  313 ARG   A CB  1 
ATOM   2210 C  CG  . ARG   A 1 281 ? -24.315 -41.604 22.043  1.00 67.69  ?  313 ARG   A CG  1 
ATOM   2211 C  CD  . ARG   A 1 281 ? -25.206 -42.166 20.973  1.00 72.41  ?  313 ARG   A CD  1 
ATOM   2212 N  NE  . ARG   A 1 281 ? -26.500 -42.671 21.401  1.00 70.18  ?  313 ARG   A NE  1 
ATOM   2213 C  CZ  . ARG   A 1 281 ? -27.477 -41.921 21.887  1.00 66.17  ?  313 ARG   A CZ  1 
ATOM   2214 N  NH1 . ARG   A 1 281 ? -27.298 -40.617 22.082  1.00 58.15  ?  313 ARG   A NH1 1 
ATOM   2215 N  NH2 . ARG   A 1 281 ? -28.626 -42.498 22.213  1.00 68.66  ?  313 ARG   A NH2 1 
ATOM   2216 N  N   . GLY   A 1 282 ? -19.887 -39.419 21.410  1.00 72.89  ?  314 GLY   A N   1 
ATOM   2217 C  CA  . GLY   A 1 282 ? -18.514 -39.461 20.946  1.00 62.56  ?  314 GLY   A CA  1 
ATOM   2218 C  C   . GLY   A 1 282 ? -18.296 -40.174 19.629  1.00 61.65  ?  314 GLY   A C   1 
ATOM   2219 O  O   . GLY   A 1 282 ? -17.517 -41.127 19.569  1.00 57.12  ?  314 GLY   A O   1 
ATOM   2220 N  N   . VAL   A 1 283 ? -18.965 -39.743 18.580  1.00 62.64  ?  315 VAL   A N   1 
ATOM   2221 C  CA  . VAL   A 1 283 ? -18.633 -40.139 17.213  1.00 57.86  ?  315 VAL   A CA  1 
ATOM   2222 C  C   . VAL   A 1 283 ? -17.942 -38.943 16.569  1.00 55.94  ?  315 VAL   A C   1 
ATOM   2223 O  O   . VAL   A 1 283 ? -18.371 -37.814 16.788  1.00 55.05  ?  315 VAL   A O   1 
ATOM   2224 C  CB  . VAL   A 1 283 ? -19.873 -40.560 16.413  1.00 59.46  ?  315 VAL   A CB  1 
ATOM   2225 C  CG1 . VAL   A 1 283 ? -19.508 -41.039 15.028  1.00 57.32  ?  315 VAL   A CG1 1 
ATOM   2226 C  CG2 . VAL   A 1 283 ? -20.557 -41.661 17.107  1.00 56.02  ?  315 VAL   A CG2 1 
ATOM   2227 N  N   . PRO   A 1 284 ? -16.825 -39.136 15.885  1.00 54.55  ?  316 PRO   A N   1 
ATOM   2228 C  CA  . PRO   A 1 284 ? -16.150 -37.998 15.263  1.00 51.83  ?  316 PRO   A CA  1 
ATOM   2229 C  C   . PRO   A 1 284 ? -16.899 -37.486 14.050  1.00 46.40  ?  316 PRO   A C   1 
ATOM   2230 O  O   . PRO   A 1 284 ? -17.355 -38.248 13.202  1.00 41.24  ?  316 PRO   A O   1 
ATOM   2231 C  CB  . PRO   A 1 284 ? -14.787 -38.575 14.883  1.00 60.85  ?  316 PRO   A CB  1 
ATOM   2232 C  CG  . PRO   A 1 284 ? -14.930 -40.017 15.000  1.00 56.08  ?  316 PRO   A CG  1 
ATOM   2233 C  CD  . PRO   A 1 284 ? -15.916 -40.273 16.025  1.00 61.85  ?  316 PRO   A CD  1 
ATOM   2234 N  N   . VAL   A 1 285 ? -17.000 -36.173 13.956  1.00 46.79  ?  317 VAL   A N   1 
ATOM   2235 C  CA  . VAL   A 1 285 ? -17.912 -35.536 13.021  1.00 51.48  ?  317 VAL   A CA  1 
ATOM   2236 C  C   . VAL   A 1 285 ? -17.197 -34.482 12.197  1.00 48.38  ?  317 VAL   A C   1 
ATOM   2237 O  O   . VAL   A 1 285 ? -16.458 -33.649 12.726  1.00 52.99  ?  317 VAL   A O   1 
ATOM   2238 C  CB  . VAL   A 1 285 ? -19.100 -34.899 13.759  1.00 55.48  ?  317 VAL   A CB  1 
ATOM   2239 C  CG1 . VAL   A 1 285 ? -20.075 -34.295 12.784  1.00 53.46  ?  317 VAL   A CG1 1 
ATOM   2240 C  CG2 . VAL   A 1 285 ? -19.784 -35.924 14.573  1.00 54.52  ?  317 VAL   A CG2 1 
ATOM   2241 N  N   . LEU   A 1 286 ? -17.455 -34.508 10.907  1.00 39.29  ?  318 LEU   A N   1 
ATOM   2242 C  CA  . LEU   A 1 286 ? -17.129 -33.445 9.976   1.00 36.15  ?  318 LEU   A CA  1 
ATOM   2243 C  C   . LEU   A 1 286 ? -18.451 -32.858 9.549   1.00 32.10  ?  318 LEU   A C   1 
ATOM   2244 O  O   . LEU   A 1 286 ? -19.254 -33.540 8.921   1.00 42.75  ?  318 LEU   A O   1 
ATOM   2245 C  CB  . LEU   A 1 286 ? -16.385 -34.033 8.791   1.00 48.32  ?  318 LEU   A CB  1 
ATOM   2246 C  CG  . LEU   A 1 286 ? -15.450 -33.238 7.912   1.00 39.66  ?  318 LEU   A CG  1 
ATOM   2247 C  CD1 . LEU   A 1 286 ? -14.786 -32.143 8.639   1.00 44.18  ?  318 LEU   A CD1 1 
ATOM   2248 C  CD2 . LEU   A 1 286 ? -14.469 -34.190 7.444   1.00 38.97  ?  318 LEU   A CD2 1 
ATOM   2249 N  N   . HIS   A 1 287 ? -18.712 -31.648 9.900   1.00 35.11  ?  319 HIS   A N   1 
ATOM   2250 C  CA  . HIS   A 1 287 ? -20.049 -31.114 9.722   1.00 36.29  ?  319 HIS   A CA  1 
ATOM   2251 C  C   . HIS   A 1 287 ? -20.000 -30.137 8.564   1.00 32.46  ?  319 HIS   A C   1 
ATOM   2252 O  O   . HIS   A 1 287 ? -19.672 -28.972 8.731   1.00 40.49  ?  319 HIS   A O   1 
ATOM   2253 C  CB  . HIS   A 1 287 ? -20.539 -30.471 11.015  1.00 46.98  ?  319 HIS   A CB  1 
ATOM   2254 C  CG  . HIS   A 1 287 ? -21.979 -30.073 11.004  1.00 38.04  ?  319 HIS   A CG  1 
ATOM   2255 N  ND1 . HIS   A 1 287 ? -22.908 -30.636 10.161  1.00 41.25  ?  319 HIS   A ND1 1 
ATOM   2256 C  CD2 . HIS   A 1 287 ? -22.642 -29.153 11.726  1.00 35.06  ?  319 HIS   A CD2 1 
ATOM   2257 C  CE1 . HIS   A 1 287 ? -24.080 -30.078 10.358  1.00 32.48  ?  319 HIS   A CE1 1 
ATOM   2258 N  NE2 . HIS   A 1 287 ? -23.944 -29.172 11.301  1.00 40.94  ?  319 HIS   A NE2 1 
ATOM   2259 N  N   . LEU   A 1 288 ? -20.333 -30.611 7.386   1.00 30.39  ?  320 LEU   A N   1 
ATOM   2260 C  CA  . LEU   A 1 288 ? -20.272 -29.790 6.191   1.00 29.90  ?  320 LEU   A CA  1 
ATOM   2261 C  C   . LEU   A 1 288 ? -21.608 -29.102 5.999   1.00 31.47  ?  320 LEU   A C   1 
ATOM   2262 O  O   . LEU   A 1 288 ? -22.423 -29.472 5.159   1.00 35.10  ?  320 LEU   A O   1 
ATOM   2263 C  CB  . LEU   A 1 288 ? -19.923 -30.624 4.974   1.00 26.13  ?  320 LEU   A CB  1 
ATOM   2264 C  CG  . LEU   A 1 288 ? -18.721 -31.532 5.078   1.00 32.39  ?  320 LEU   A CG  1 
ATOM   2265 C  CD1 . LEU   A 1 288 ? -18.415 -32.097 3.765   1.00 28.66  ?  320 LEU   A CD1 1 
ATOM   2266 C  CD2 . LEU   A 1 288 ? -17.572 -30.789 5.550   1.00 35.10  ?  320 LEU   A CD2 1 
ATOM   2267 N  N   . ILE   A 1 289 ? -21.819 -28.101 6.833   1.00 28.74  ?  321 ILE   A N   1 
ATOM   2268 C  CA  . ILE   A 1 289 ? -22.923 -27.162 6.727   1.00 29.29  ?  321 ILE   A CA  1 
ATOM   2269 C  C   . ILE   A 1 289 ? -22.264 -25.798 6.723   1.00 34.84  ?  321 ILE   A C   1 
ATOM   2270 O  O   . ILE   A 1 289 ? -21.307 -25.596 7.469   1.00 37.25  ?  321 ILE   A O   1 
ATOM   2271 C  CB  . ILE   A 1 289 ? -23.914 -27.297 7.894   1.00 34.31  ?  321 ILE   A CB  1 
ATOM   2272 C  CG1 . ILE   A 1 289 ? -25.097 -26.383 7.675   1.00 34.14  ?  321 ILE   A CG1 1 
ATOM   2273 C  CG2 . ILE   A 1 289 ? -23.289 -26.951 9.174   1.00 38.72  ?  321 ILE   A CG2 1 
ATOM   2274 C  CD1 . ILE   A 1 289 ? -26.125 -26.477 8.689   1.00 38.82  ?  321 ILE   A CD1 1 
ATOM   2275 N  N   . PRO   A 1 290 ? -22.713 -24.846 5.929   1.00 30.16  ?  322 PRO   A N   1 
ATOM   2276 C  CA  . PRO   A 1 290 ? -22.039 -23.562 5.873   1.00 32.09  ?  322 PRO   A CA  1 
ATOM   2277 C  C   . PRO   A 1 290 ? -22.485 -22.582 6.942   1.00 36.04  ?  322 PRO   A C   1 
ATOM   2278 O  O   . PRO   A 1 290 ? -23.578 -22.638 7.468   1.00 41.99  ?  322 PRO   A O   1 
ATOM   2279 C  CB  . PRO   A 1 290 ? -22.420 -23.072 4.481   1.00 36.89  ?  322 PRO   A CB  1 
ATOM   2280 C  CG  . PRO   A 1 290 ? -23.574 -23.711 4.195   1.00 34.79  ?  322 PRO   A CG  1 
ATOM   2281 C  CD  . PRO   A 1 290 ? -23.476 -25.044 4.714   1.00 32.74  ?  322 PRO   A CD  1 
ATOM   2282 N  N   . SER   A 1 291 ? -21.606 -21.657 7.245   1.00 45.98  ?  323 SER   A N   1 
ATOM   2283 C  CA  . SER   A 1 291 ? -21.940 -20.597 8.152   1.00 45.01  ?  323 SER   A CA  1 
ATOM   2284 C  C   . SER   A 1 291 ? -21.416 -19.325 7.575   1.00 45.44  ?  323 SER   A C   1 
ATOM   2285 O  O   . SER   A 1 291 ? -20.229 -19.111 7.558   1.00 56.45  ?  323 SER   A O   1 
ATOM   2286 C  CB  . SER   A 1 291 ? -21.336 -20.848 9.501   1.00 52.05  ?  323 SER   A CB  1 
ATOM   2287 O  OG  . SER   A 1 291 ? -21.660 -19.803 10.385  1.00 68.07  ?  323 SER   A OG  1 
ATOM   2288 N  N   . PRO   A 1 292 ? -22.288 -18.454 7.115   1.00 40.07  ?  324 PRO   A N   1 
ATOM   2289 C  CA  . PRO   A 1 292 ? -23.732 -18.392 7.211   1.00 43.66  ?  324 PRO   A CA  1 
ATOM   2290 C  C   . PRO   A 1 292 ? -24.470 -19.307 6.281   1.00 40.62  ?  324 PRO   A C   1 
ATOM   2291 O  O   . PRO   A 1 292 ? -23.926 -19.737 5.278   1.00 39.73  ?  324 PRO   A O   1 
ATOM   2292 C  CB  . PRO   A 1 292 ? -24.025 -16.958 6.839   1.00 43.96  ?  324 PRO   A CB  1 
ATOM   2293 C  CG  . PRO   A 1 292 ? -22.981 -16.618 5.963   1.00 45.84  ?  324 PRO   A CG  1 
ATOM   2294 C  CD  . PRO   A 1 292 ? -21.765 -17.253 6.484   1.00 44.33  ?  324 PRO   A CD  1 
ATOM   2295 N  N   . PHE   A 1 293 ? -25.722 -19.562 6.638   1.00 40.11  ?  325 PHE   A N   1 
ATOM   2296 C  CA  . PHE   A 1 293 ? -26.604 -20.380 5.863   1.00 34.37  ?  325 PHE   A CA  1 
ATOM   2297 C  C   . PHE   A 1 293 ? -26.961 -19.680 4.570   1.00 34.47  ?  325 PHE   A C   1 
ATOM   2298 O  O   . PHE   A 1 293 ? -26.812 -18.472 4.445   1.00 40.20  ?  325 PHE   A O   1 
ATOM   2299 C  CB  . PHE   A 1 293 ? -27.887 -20.659 6.626   1.00 35.43  ?  325 PHE   A CB  1 
ATOM   2300 C  CG  . PHE   A 1 293 ? -27.733 -21.489 7.860   1.00 33.05  ?  325 PHE   A CG  1 
ATOM   2301 C  CD1 . PHE   A 1 293 ? -26.634 -22.244 8.092   1.00 35.21  ?  325 PHE   A CD1 1 
ATOM   2302 C  CD2 . PHE   A 1 293 ? -28.744 -21.534 8.779   1.00 34.27  ?  325 PHE   A CD2 1 
ATOM   2303 C  CE1 . PHE   A 1 293 ? -26.547 -23.002 9.204   1.00 37.98  ?  325 PHE   A CE1 1 
ATOM   2304 C  CE2 . PHE   A 1 293 ? -28.630 -22.291 9.890   1.00 40.30  ?  325 PHE   A CE2 1 
ATOM   2305 C  CZ  . PHE   A 1 293 ? -27.542 -23.016 10.099  1.00 38.26  ?  325 PHE   A CZ  1 
ATOM   2306 N  N   . PRO   A 1 294 ? -27.442 -20.412 3.593   1.00 29.07  ?  326 PRO   A N   1 
ATOM   2307 C  CA  . PRO   A 1 294 ? -27.788 -19.787 2.339   1.00 37.62  ?  326 PRO   A CA  1 
ATOM   2308 C  C   . PRO   A 1 294 ? -28.754 -18.661 2.565   1.00 42.60  ?  326 PRO   A C   1 
ATOM   2309 O  O   . PRO   A 1 294 ? -29.481 -18.651 3.538   1.00 42.25  ?  326 PRO   A O   1 
ATOM   2310 C  CB  . PRO   A 1 294 ? -28.427 -20.920 1.565   1.00 34.60  ?  326 PRO   A CB  1 
ATOM   2311 C  CG  . PRO   A 1 294 ? -27.737 -22.032 2.029   1.00 36.14  ?  326 PRO   A CG  1 
ATOM   2312 C  CD  . PRO   A 1 294 ? -27.580 -21.850 3.473   1.00 37.57  ?  326 PRO   A CD  1 
ATOM   2313 N  N   . GLU   A 1 295 ? -28.739 -17.698 1.662   1.00 49.44  ?  327 GLU   A N   1 
ATOM   2314 C  CA  . GLU   A 1 295 ? -29.643 -16.583 1.831   1.00 53.24  ?  327 GLU   A CA  1 
ATOM   2315 C  C   . GLU   A 1 295 ? -31.081 -17.052 1.763   1.00 53.28  ?  327 GLU   A C   1 
ATOM   2316 O  O   . GLU   A 1 295 ? -31.954 -16.455 2.391   1.00 65.20  ?  327 GLU   A O   1 
ATOM   2317 C  CB  . GLU   A 1 295 ? -29.342 -15.502 0.783   1.00 61.59  ?  327 GLU   A CB  1 
ATOM   2318 C  CG  . GLU   A 1 295 ? -28.980 -14.156 1.365   1.00 67.92  ?  327 GLU   A CG  1 
ATOM   2319 C  CD  . GLU   A 1 295 ? -27.999 -13.399 0.544   1.00 74.25  ?  327 GLU   A CD  1 
ATOM   2320 O  OE1 . GLU   A 1 295 ? -27.717 -13.817 -0.593  1.00 78.42  ?  327 GLU   A OE1 1 
ATOM   2321 O  OE2 . GLU   A 1 295 ? -27.495 -12.378 1.043   1.00 85.29  ?  327 GLU   A OE2 1 
ATOM   2322 N  N   . VAL   A 1 296 ? -31.346 -18.130 1.043   1.00 49.75  ?  328 VAL   A N   1 
ATOM   2323 C  CA  . VAL   A 1 296 ? -32.715 -18.539 0.766   1.00 49.04  ?  328 VAL   A CA  1 
ATOM   2324 C  C   . VAL   A 1 296 ? -33.229 -19.482 1.844   1.00 46.87  ?  328 VAL   A C   1 
ATOM   2325 O  O   . VAL   A 1 296 ? -34.328 -20.017 1.736   1.00 43.05  ?  328 VAL   A O   1 
ATOM   2326 C  CB  . VAL   A 1 296 ? -32.808 -19.196 -0.617  1.00 50.48  ?  328 VAL   A CB  1 
ATOM   2327 C  CG1 . VAL   A 1 296 ? -32.516 -18.226 -1.643  1.00 53.90  ?  328 VAL   A CG1 1 
ATOM   2328 C  CG2 . VAL   A 1 296 ? -31.833 -20.307 -0.759  1.00 50.00  ?  328 VAL   A CG2 1 
ATOM   2329 N  N   . TRP   A 1 297 ? -32.447 -19.676 2.889   1.00 45.51  ?  329 TRP   A N   1 
ATOM   2330 C  CA  . TRP   A 1 297 ? -32.753 -20.663 3.899   1.00 39.20  ?  329 TRP   A CA  1 
ATOM   2331 C  C   . TRP   A 1 297 ? -34.183 -20.545 4.364   1.00 45.00  ?  329 TRP   A C   1 
ATOM   2332 O  O   . TRP   A 1 297 ? -34.607 -19.493 4.831   1.00 46.28  ?  329 TRP   A O   1 
ATOM   2333 C  CB  . TRP   A 1 297 ? -31.836 -20.454 5.072   1.00 38.19  ?  329 TRP   A CB  1 
ATOM   2334 C  CG  . TRP   A 1 297 ? -31.917 -21.390 6.169   1.00 36.64  ?  329 TRP   A CG  1 
ATOM   2335 C  CD1 . TRP   A 1 297 ? -31.394 -22.621 6.213   1.00 46.98  ?  329 TRP   A CD1 1 
ATOM   2336 C  CD2 . TRP   A 1 297 ? -32.478 -21.145 7.445   1.00 37.70  ?  329 TRP   A CD2 1 
ATOM   2337 N  NE1 . TRP   A 1 297 ? -31.612 -23.183 7.435   1.00 44.00  ?  329 TRP   A NE1 1 
ATOM   2338 C  CE2 . TRP   A 1 297 ? -32.283 -22.284 8.210   1.00 42.90  ?  329 TRP   A CE2 1 
ATOM   2339 C  CE3 . TRP   A 1 297 ? -33.143 -20.081 8.007   1.00 38.30  ?  329 TRP   A CE3 1 
ATOM   2340 C  CZ2 . TRP   A 1 297 ? -32.732 -22.388 9.498   1.00 40.97  ?  329 TRP   A CZ2 1 
ATOM   2341 C  CZ3 . TRP   A 1 297 ? -33.575 -20.193 9.274   1.00 46.89  ?  329 TRP   A CZ3 1 
ATOM   2342 C  CH2 . TRP   A 1 297 ? -33.376 -21.335 10.005  1.00 42.26  ?  329 TRP   A CH2 1 
ATOM   2343 N  N   . HIS   A 1 298 ? -34.891 -21.644 4.308   1.00 47.18  ?  330 HIS   A N   1 
ATOM   2344 C  CA  . HIS   A 1 298 ? -36.232 -21.731 4.794   1.00 42.02  ?  330 HIS   A CA  1 
ATOM   2345 C  C   . HIS   A 1 298 ? -37.209 -20.734 4.263   1.00 42.61  ?  330 HIS   A C   1 
ATOM   2346 O  O   . HIS   A 1 298 ? -38.073 -20.268 4.950   1.00 45.45  ?  330 HIS   A O   1 
ATOM   2347 C  CB  . HIS   A 1 298 ? -36.239 -21.733 6.290   1.00 37.38  ?  330 HIS   A CB  1 
ATOM   2348 C  CG  . HIS   A 1 298 ? -35.831 -23.029 6.898   1.00 33.85  ?  330 HIS   A CG  1 
ATOM   2349 N  ND1 . HIS   A 1 298 ? -35.944 -23.265 8.237   1.00 29.20  ?  330 HIS   A ND1 1 
ATOM   2350 C  CD2 . HIS   A 1 298 ? -35.291 -24.145 6.368   1.00 37.73  ?  330 HIS   A CD2 1 
ATOM   2351 C  CE1 . HIS   A 1 298 ? -35.490 -24.467 8.510   1.00 40.76  ?  330 HIS   A CE1 1 
ATOM   2352 N  NE2 . HIS   A 1 298 ? -35.105 -25.033 7.389   1.00 31.90  ?  330 HIS   A NE2 1 
ATOM   2353 N  N   . THR   A 1 299 ? -37.068 -20.440 2.999   1.00 42.27  ?  331 THR   A N   1 
ATOM   2354 C  CA  . THR   A 1 299 ? -38.008 -19.642 2.240   1.00 44.29  ?  331 THR   A CA  1 
ATOM   2355 C  C   . THR   A 1 299 ? -38.342 -20.390 0.972   1.00 40.61  ?  331 THR   A C   1 
ATOM   2356 O  O   . THR   A 1 299 ? -37.654 -21.321 0.596   1.00 41.56  ?  331 THR   A O   1 
ATOM   2357 C  CB  . THR   A 1 299 ? -37.443 -18.296 1.844   1.00 46.97  ?  331 THR   A CB  1 
ATOM   2358 O  OG1 . THR   A 1 299 ? -36.486 -18.492 0.806   1.00 44.99  ?  331 THR   A OG1 1 
ATOM   2359 C  CG2 . THR   A 1 299 ? -36.816 -17.645 3.007   1.00 50.73  ?  331 THR   A CG2 1 
ATOM   2360 N  N   . MET   A 1 300 ? -39.383 -19.958 0.280   1.00 46.57  ?  332 MET   A N   1 
ATOM   2361 C  CA  . MET   A 1 300 ? -39.761 -20.660 -0.928  1.00 45.82  ?  332 MET   A CA  1 
ATOM   2362 C  C   . MET   A 1 300 ? -38.772 -20.424 -2.043  1.00 52.29  ?  332 MET   A C   1 
ATOM   2363 O  O   . MET   A 1 300 ? -38.899 -21.021 -3.112  1.00 50.81  ?  332 MET   A O   1 
ATOM   2364 C  CB  . MET   A 1 300 ? -41.138 -20.211 -1.360  1.00 55.59  ?  332 MET   A CB  1 
ATOM   2365 C  CG  . MET   A 1 300 ? -42.209 -20.496 -0.380  1.00 62.48  ?  332 MET   A CG  1 
ATOM   2366 S  SD  . MET   A 1 300 ? -42.692 -22.197 -0.399  1.00 41.33  ?  332 MET   A SD  1 
ATOM   2367 C  CE  . MET   A 1 300 ? -44.042 -22.099 0.737   1.00 65.77  ?  332 MET   A CE  1 
ATOM   2368 N  N   . ASP   A 1 301 ? -37.805 -19.557 -1.814  1.00 56.14  ?  333 ASP   A N   1 
ATOM   2369 C  CA  . ASP   A 1 301 ? -36.800 -19.212 -2.795  1.00 53.63  ?  333 ASP   A CA  1 
ATOM   2370 C  C   . ASP   A 1 301 ? -35.649 -20.196 -2.808  1.00 52.38  ?  333 ASP   A C   1 
ATOM   2371 O  O   . ASP   A 1 301 ? -34.697 -20.001 -3.558  1.00 58.21  ?  333 ASP   A O   1 
ATOM   2372 C  CB  . ASP   A 1 301 ? -36.271 -17.807 -2.503  1.00 56.30  ?  333 ASP   A CB  1 
ATOM   2373 C  CG  . ASP   A 1 301 ? -37.155 -16.716 -3.040  1.00 56.64  ?  333 ASP   A CG  1 
ATOM   2374 O  OD1 . ASP   A 1 301 ? -37.776 -16.898 -4.103  1.00 59.82  ?  333 ASP   A OD1 1 
ATOM   2375 O  OD2 . ASP   A 1 301 ? -37.207 -15.661 -2.393  1.00 55.21  ?  333 ASP   A OD2 1 
ATOM   2376 N  N   . ASP   A 1 302 ? -35.695 -21.224 -1.973  1.00 54.08  ?  334 ASP   A N   1 
ATOM   2377 C  CA  . ASP   A 1 302 ? -34.692 -22.279 -1.979  1.00 47.13  ?  334 ASP   A CA  1 
ATOM   2378 C  C   . ASP   A 1 302 ? -35.088 -23.325 -2.998  1.00 44.98  ?  334 ASP   A C   1 
ATOM   2379 O  O   . ASP   A 1 302 ? -35.542 -24.398 -2.657  1.00 35.40  ?  334 ASP   A O   1 
ATOM   2380 C  CB  . ASP   A 1 302 ? -34.583 -22.906 -0.610  1.00 41.88  ?  334 ASP   A CB  1 
ATOM   2381 C  CG  . ASP   A 1 302 ? -33.547 -23.977 -0.549  1.00 42.80  ?  334 ASP   A CG  1 
ATOM   2382 O  OD1 . ASP   A 1 302 ? -33.020 -24.357 -1.592  1.00 42.96  ?  334 ASP   A OD1 1 
ATOM   2383 O  OD2 . ASP   A 1 302 ? -33.243 -24.447 0.556   1.00 44.84  ?  334 ASP   A OD2 1 
ATOM   2384 N  N   . ASN   A 1 303 ? -34.906 -22.983 -4.259  1.00 50.86  ?  335 ASN   A N   1 
ATOM   2385 C  CA  . ASN   A 1 303 ? -35.319 -23.835 -5.356  1.00 46.26  ?  335 ASN   A CA  1 
ATOM   2386 C  C   . ASN   A 1 303 ? -34.121 -24.159 -6.224  1.00 44.87  ?  335 ASN   A C   1 
ATOM   2387 O  O   . ASN   A 1 303 ? -32.980 -23.903 -5.855  1.00 42.20  ?  335 ASN   A O   1 
ATOM   2388 C  CB  . ASN   A 1 303 ? -36.423 -23.163 -6.158  1.00 49.19  ?  335 ASN   A CB  1 
ATOM   2389 C  CG  . ASN   A 1 303 ? -36.135 -21.749 -6.426  1.00 49.52  ?  335 ASN   A CG  1 
ATOM   2390 O  OD1 . ASN   A 1 303 ? -34.995 -21.339 -6.382  1.00 52.00  ?  335 ASN   A OD1 1 
ATOM   2391 N  ND2 . ASN   A 1 303 ? -37.160 -20.976 -6.691  1.00 63.21  ?  335 ASN   A ND2 1 
ATOM   2392 N  N   . GLU   A 1 304 ? -34.407 -24.761 -7.371  1.00 44.91  ?  336 GLU   A N   1 
ATOM   2393 C  CA  . GLU   A 1 304 ? -33.387 -25.099 -8.352  1.00 43.45  ?  336 GLU   A CA  1 
ATOM   2394 C  C   . GLU   A 1 304 ? -32.848 -23.868 -9.070  1.00 47.86  ?  336 GLU   A C   1 
ATOM   2395 O  O   . GLU   A 1 304 ? -31.665 -23.820 -9.403  1.00 46.08  ?  336 GLU   A O   1 
ATOM   2396 C  CB  . GLU   A 1 304 ? -33.989 -26.108 -9.331  1.00 38.77  ?  336 GLU   A CB  1 
ATOM   2397 C  CG  . GLU   A 1 304 ? -33.239 -26.385 -10.580 1.00 38.32  ?  336 GLU   A CG  1 
ATOM   2398 C  CD  . GLU   A 1 304 ? -33.873 -27.467 -11.411 1.00 46.57  ?  336 GLU   A CD  1 
ATOM   2399 O  OE1 . GLU   A 1 304 ? -35.096 -27.703 -11.248 1.00 40.43  ?  336 GLU   A OE1 1 
ATOM   2400 O  OE2 . GLU   A 1 304 ? -33.144 -28.087 -12.222 1.00 43.57  ?  336 GLU   A OE2 1 
ATOM   2401 N  N   . GLU   A 1 305 ? -33.664 -22.850 -9.301  1.00 46.74  ?  337 GLU   A N   1 
ATOM   2402 C  CA  . GLU   A 1 305 ? -33.142 -21.726 -10.048 1.00 53.06  ?  337 GLU   A CA  1 
ATOM   2403 C  C   . GLU   A 1 305 ? -32.003 -21.067 -9.304  1.00 53.74  ?  337 GLU   A C   1 
ATOM   2404 O  O   . GLU   A 1 305 ? -31.038 -20.617 -9.926  1.00 67.70  ?  337 GLU   A O   1 
ATOM   2405 C  CB  . GLU   A 1 305 ? -34.245 -20.726 -10.365 1.00 61.46  ?  337 GLU   A CB  1 
ATOM   2406 C  CG  . GLU   A 1 305 ? -34.510 -20.555 -11.878 1.00 85.98  ?  337 GLU   A CG  1 
ATOM   2407 C  CD  . GLU   A 1 305 ? -33.344 -19.910 -12.680 1.00 91.93  ?  337 GLU   A CD  1 
ATOM   2408 O  OE1 . GLU   A 1 305 ? -33.095 -18.687 -12.539 1.00 68.22  ?  337 GLU   A OE1 1 
ATOM   2409 O  OE2 . GLU   A 1 305 ? -32.687 -20.629 -13.476 1.00 91.84  ?  337 GLU   A OE2 1 
ATOM   2410 N  N   . ASN   A 1 306 ? -32.057 -21.045 -7.985  1.00 47.76  ?  338 ASN   A N   1 
ATOM   2411 C  CA  . ASN   A 1 306 ? -31.022 -20.403 -7.193  1.00 48.20  ?  338 ASN   A CA  1 
ATOM   2412 C  C   . ASN   A 1 306 ? -29.890 -21.327 -6.789  1.00 39.69  ?  338 ASN   A C   1 
ATOM   2413 O  O   . ASN   A 1 306 ? -29.106 -20.958 -5.923  1.00 35.85  ?  338 ASN   A O   1 
ATOM   2414 C  CB  . ASN   A 1 306 ? -31.620 -19.782 -5.945  1.00 47.24  ?  338 ASN   A CB  1 
ATOM   2415 C  CG  . ASN   A 1 306 ? -32.490 -18.633 -6.252  1.00 52.21  ?  338 ASN   A CG  1 
ATOM   2416 O  OD1 . ASN   A 1 306 ? -32.077 -17.483 -6.179  1.00 61.06  ?  338 ASN   A OD1 1 
ATOM   2417 N  ND2 . ASN   A 1 306 ? -33.716 -18.925 -6.611  1.00 62.30  ?  338 ASN   A ND2 1 
ATOM   2418 N  N   . LEU   A 1 307 ? -29.758 -22.494 -7.394  1.00 44.25  ?  339 LEU   A N   1 
ATOM   2419 C  CA  . LEU   A 1 307 ? -28.563 -23.285 -7.166  1.00 45.17  ?  339 LEU   A CA  1 
ATOM   2420 C  C   . LEU   A 1 307 ? -27.462 -22.814 -8.093  1.00 52.30  ?  339 LEU   A C   1 
ATOM   2421 O  O   . LEU   A 1 307 ? -27.734 -22.281 -9.170  1.00 59.23  ?  339 LEU   A O   1 
ATOM   2422 C  CB  . LEU   A 1 307 ? -28.834 -24.764 -7.396  1.00 44.81  ?  339 LEU   A CB  1 
ATOM   2423 C  CG  . LEU   A 1 307 ? -29.800 -25.455 -6.450  1.00 42.44  ?  339 LEU   A CG  1 
ATOM   2424 C  CD1 . LEU   A 1 307 ? -30.027 -26.891 -6.779  1.00 33.45  ?  339 LEU   A CD1 1 
ATOM   2425 C  CD2 . LEU   A 1 307 ? -29.236 -25.394 -5.113  1.00 45.00  ?  339 LEU   A CD2 1 
ATOM   2426 N  N   . ASP   A 1 308 ? -26.210 -22.989 -7.663  1.00 43.61  ?  340 ASP   A N   1 
ATOM   2427 C  CA  . ASP   A 1 308 ? -25.058 -22.664 -8.497  1.00 59.43  ?  340 ASP   A CA  1 
ATOM   2428 C  C   . ASP   A 1 308 ? -24.394 -23.960 -8.926  1.00 47.51  ?  340 ASP   A C   1 
ATOM   2429 O  O   . ASP   A 1 308 ? -23.708 -24.601 -8.140  1.00 50.50  ?  340 ASP   A O   1 
ATOM   2430 C  CB  . ASP   A 1 308 ? -24.062 -21.742 -7.793  1.00 54.29  ?  340 ASP   A CB  1 
ATOM   2431 C  CG  . ASP   A 1 308 ? -23.002 -21.196 -8.746  1.00 55.14  ?  340 ASP   A CG  1 
ATOM   2432 O  OD1 . ASP   A 1 308 ? -23.316 -20.914 -9.918  1.00 62.26  ?  340 ASP   A OD1 1 
ATOM   2433 O  OD2 . ASP   A 1 308 ? -21.847 -21.045 -8.348  1.00 53.61  ?  340 ASP   A OD2 1 
ATOM   2434 N  N   . GLU   A 1 309 ? -24.580 -24.322 -10.188 1.00 53.40  ?  341 GLU   A N   1 
ATOM   2435 C  CA  . GLU   A 1 309 ? -23.956 -25.509 -10.752 1.00 51.11  ?  341 GLU   A CA  1 
ATOM   2436 C  C   . GLU   A 1 309 ? -22.476 -25.595 -10.412 1.00 52.77  ?  341 GLU   A C   1 
ATOM   2437 O  O   . GLU   A 1 309 ? -21.969 -26.646 -10.008 1.00 44.19  ?  341 GLU   A O   1 
ATOM   2438 C  CB  . GLU   A 1 309 ? -24.135 -25.471 -12.257 1.00 47.28  ?  341 GLU   A CB  1 
ATOM   2439 C  CG  . GLU   A 1 309 ? -23.663 -26.644 -12.980 1.00 47.73  ?  341 GLU   A CG  1 
ATOM   2440 C  CD  . GLU   A 1 309 ? -23.723 -26.402 -14.452 1.00 65.91  ?  341 GLU   A CD  1 
ATOM   2441 O  OE1 . GLU   A 1 309 ? -23.111 -25.398 -14.896 1.00 58.30  ?  341 GLU   A OE1 1 
ATOM   2442 O  OE2 . GLU   A 1 309 ? -24.412 -27.183 -15.153 1.00 68.56  ?  341 GLU   A OE2 1 
ATOM   2443 N  N   . SER   A 1 310 ? -21.756 -24.501 -10.592 1.00 55.11  ?  342 SER   A N   1 
ATOM   2444 C  CA  . SER   A 1 310 ? -20.312 -24.595 -10.527 1.00 51.29  ?  342 SER   A CA  1 
ATOM   2445 C  C   . SER   A 1 310 ? -19.871 -25.065 -9.161  1.00 46.27  ?  342 SER   A C   1 
ATOM   2446 O  O   . SER   A 1 310 ? -18.973 -25.896 -9.050  1.00 48.07  ?  342 SER   A O   1 
ATOM   2447 C  CB  . SER   A 1 310 ? -19.679 -23.255 -10.869 1.00 61.86  ?  342 SER   A CB  1 
ATOM   2448 O  OG  . SER   A 1 310 ? -19.788 -23.033 -12.254 1.00 63.48  ?  342 SER   A OG  1 
ATOM   2449 N  N   . THR   A 1 311 ? -20.489 -24.563 -8.102  1.00 46.56  ?  343 THR   A N   1 
ATOM   2450 C  CA  . THR   A 1 311 ? -19.927 -24.901 -6.807  1.00 45.21  ?  343 THR   A CA  1 
ATOM   2451 C  C   . THR   A 1 311 ? -20.439 -26.236 -6.307  1.00 41.59  ?  343 THR   A C   1 
ATOM   2452 O  O   . THR   A 1 311 ? -19.749 -26.919 -5.567  1.00 41.68  ?  343 THR   A O   1 
ATOM   2453 C  CB  . THR   A 1 311 ? -20.164 -23.807 -5.762  1.00 42.26  ?  343 THR   A CB  1 
ATOM   2454 O  OG1 . THR   A 1 311 ? -20.769 -24.374 -4.624  1.00 37.92  ?  343 THR   A OG1 1 
ATOM   2455 C  CG2 . THR   A 1 311 ? -21.012 -22.726 -6.249  1.00 44.92  ?  343 THR   A CG2 1 
ATOM   2456 N  N   . ILE   A 1 312 ? -21.585 -26.688 -6.753  1.00 41.31  ?  344 ILE   A N   1 
ATOM   2457 C  CA  . ILE   A 1 312 ? -21.930 -28.056 -6.458  1.00 30.64  ?  344 ILE   A CA  1 
ATOM   2458 C  C   . ILE   A 1 312 ? -20.955 -28.988 -7.142  1.00 41.52  ?  344 ILE   A C   1 
ATOM   2459 O  O   . ILE   A 1 312 ? -20.543 -30.001 -6.576  1.00 40.99  ?  344 ILE   A O   1 
ATOM   2460 C  CB  . ILE   A 1 312 ? -23.378 -28.301 -6.878  1.00 39.07  ?  344 ILE   A CB  1 
ATOM   2461 C  CG1 . ILE   A 1 312 ? -24.291 -27.381 -6.072  1.00 35.68  ?  344 ILE   A CG1 1 
ATOM   2462 C  CG2 . ILE   A 1 312 ? -23.737 -29.718 -6.680  1.00 34.24  ?  344 ILE   A CG2 1 
ATOM   2463 C  CD1 . ILE   A 1 312 ? -25.607 -27.306 -6.570  1.00 38.12  ?  344 ILE   A CD1 1 
ATOM   2464 N  N   . ASP   A 1 313 ? -20.559 -28.653 -8.368  1.00 47.98  ?  345 ASP   A N   1 
ATOM   2465 C  CA  . ASP   A 1 313 ? -19.562 -29.437 -9.077  1.00 39.32  ?  345 ASP   A CA  1 
ATOM   2466 C  C   . ASP   A 1 313 ? -18.232 -29.410 -8.355  1.00 40.41  ?  345 ASP   A C   1 
ATOM   2467 O  O   . ASP   A 1 313 ? -17.573 -30.440 -8.235  1.00 46.38  ?  345 ASP   A O   1 
ATOM   2468 C  CB  . ASP   A 1 313 ? -19.404 -28.903 -10.479 1.00 42.21  ?  345 ASP   A CB  1 
ATOM   2469 C  CG  . ASP   A 1 313 ? -18.674 -29.838 -11.374 1.00 50.13  ?  345 ASP   A CG  1 
ATOM   2470 O  OD1 . ASP   A 1 313 ? -19.052 -31.019 -11.483 1.00 52.51  ?  345 ASP   A OD1 1 
ATOM   2471 O  OD2 . ASP   A 1 313 ? -17.709 -29.370 -11.989 1.00 54.68  ?  345 ASP   A OD2 1 
ATOM   2472 N  N   . ASN   A 1 314 ? -17.809 -28.256 -7.858  1.00 35.83  ?  346 ASN   A N   1 
ATOM   2473 C  CA  . ASN   A 1 314 ? -16.504 -28.226 -7.227  1.00 35.68  ?  346 ASN   A CA  1 
ATOM   2474 C  C   . ASN   A 1 314 ? -16.518 -29.055 -5.972  1.00 41.49  ?  346 ASN   A C   1 
ATOM   2475 O  O   . ASN   A 1 314 ? -15.535 -29.728 -5.660  1.00 44.94  ?  346 ASN   A O   1 
ATOM   2476 C  CB  . ASN   A 1 314 ? -16.069 -26.814 -6.890  1.00 38.16  ?  346 ASN   A CB  1 
ATOM   2477 C  CG  . ASN   A 1 314 ? -15.928 -25.942 -8.087  1.00 40.95  ?  346 ASN   A CG  1 
ATOM   2478 O  OD1 . ASN   A 1 314 ? -15.715 -26.411 -9.189  1.00 47.73  ?  346 ASN   A OD1 1 
ATOM   2479 N  ND2 . ASN   A 1 314 ? -16.027 -24.651 -7.873  1.00 40.69  ?  346 ASN   A ND2 1 
ATOM   2480 N  N   . LEU   A 1 315 ? -17.625 -29.028 -5.238  1.00 40.47  ?  347 LEU   A N   1 
ATOM   2481 C  CA  . LEU   A 1 315 ? -17.672 -29.757 -3.980  1.00 35.33  ?  347 LEU   A CA  1 
ATOM   2482 C  C   . LEU   A 1 315 ? -17.803 -31.234 -4.227  1.00 36.21  ?  347 LEU   A C   1 
ATOM   2483 O  O   . LEU   A 1 315 ? -17.160 -32.040 -3.562  1.00 36.84  ?  347 LEU   A O   1 
ATOM   2484 C  CB  . LEU   A 1 315 ? -18.821 -29.274 -3.127  1.00 35.01  ?  347 LEU   A CB  1 
ATOM   2485 C  CG  . LEU   A 1 315 ? -18.602 -27.957 -2.433  1.00 28.62  ?  347 LEU   A CG  1 
ATOM   2486 C  CD1 . LEU   A 1 315 ? -19.837 -27.498 -1.816  1.00 29.10  ?  347 LEU   A CD1 1 
ATOM   2487 C  CD2 . LEU   A 1 315 ? -17.623 -28.148 -1.395  1.00 34.59  ?  347 LEU   A CD2 1 
ATOM   2488 N  N   . ASN   A 1 316 ? -18.617 -31.608 -5.194  1.00 40.94  ?  348 ASN   A N   1 
ATOM   2489 C  CA  . ASN   A 1 316 ? -18.647 -32.992 -5.612  1.00 37.54  ?  348 ASN   A CA  1 
ATOM   2490 C  C   . ASN   A 1 316 ? -17.257 -33.514 -5.832  1.00 33.63  ?  348 ASN   A C   1 
ATOM   2491 O  O   . ASN   A 1 316 ? -16.866 -34.508 -5.227  1.00 35.88  ?  348 ASN   A O   1 
ATOM   2492 C  CB  . ASN   A 1 316 ? -19.468 -33.124 -6.862  1.00 34.59  ?  348 ASN   A CB  1 
ATOM   2493 C  CG  . ASN   A 1 316 ? -20.821 -33.574 -6.572  1.00 40.19  ?  348 ASN   A CG  1 
ATOM   2494 O  OD1 . ASN   A 1 316 ? -21.042 -34.411 -5.692  1.00 42.73  ?  348 ASN   A OD1 1 
ATOM   2495 N  ND2 . ASN   A 1 316 ? -21.758 -33.037 -7.293  1.00 42.73  ?  348 ASN   A ND2 1 
ATOM   2496 N  N   . LYS   A 1 317 ? -16.474 -32.830 -6.662  1.00 40.39  ?  349 LYS   A N   1 
ATOM   2497 C  CA  . LYS   A 1 317 ? -15.126 -33.302 -6.957  1.00 41.04  ?  349 LYS   A CA  1 
ATOM   2498 C  C   . LYS   A 1 317 ? -14.296 -33.442 -5.693  1.00 37.96  ?  349 LYS   A C   1 
ATOM   2499 O  O   . LYS   A 1 317 ? -13.638 -34.463 -5.505  1.00 37.74  ?  349 LYS   A O   1 
ATOM   2500 C  CB  . LYS   A 1 317 ? -14.443 -32.376 -7.948  1.00 41.39  ?  349 LYS   A CB  1 
ATOM   2501 C  CG  . LYS   A 1 317 ? -15.009 -32.423 -9.338  1.00 43.69  ?  349 LYS   A CG  1 
ATOM   2502 C  CD  . LYS   A 1 317 ? -14.274 -31.460 -10.253 1.00 49.44  ?  349 LYS   A CD  1 
ATOM   2503 C  CE  . LYS   A 1 317 ? -14.939 -31.274 -11.621 1.00 54.79  ?  349 LYS   A CE  1 
ATOM   2504 N  NZ  . LYS   A 1 317 ? -14.577 -29.978 -12.252 1.00 55.52  ?  349 LYS   A NZ  1 
ATOM   2505 N  N   . ILE   A 1 318 ? -14.350 -32.451 -4.797  1.00 44.18  ?  350 ILE   A N   1 
ATOM   2506 C  CA  . ILE   A 1 318 ? -13.567 -32.479 -3.558  1.00 43.94  ?  350 ILE   A CA  1 
ATOM   2507 C  C   . ILE   A 1 318 ? -13.966 -33.650 -2.679  1.00 41.61  ?  350 ILE   A C   1 
ATOM   2508 O  O   . ILE   A 1 318 ? -13.123 -34.306 -2.067  1.00 42.35  ?  350 ILE   A O   1 
ATOM   2509 C  CB  . ILE   A 1 318 ? -13.740 -31.167 -2.778  1.00 40.12  ?  350 ILE   A CB  1 
ATOM   2510 C  CG1 . ILE   A 1 318 ? -13.229 -29.986 -3.580  1.00 39.38  ?  350 ILE   A CG1 1 
ATOM   2511 C  CG2 . ILE   A 1 318 ? -13.030 -31.252 -1.470  1.00 41.36  ?  350 ILE   A CG2 1 
ATOM   2512 C  CD1 . ILE   A 1 318 ? -13.402 -28.703 -2.949  1.00 38.94  ?  350 ILE   A CD1 1 
ATOM   2513 N  N   . LEU   A 1 319 ? -15.250 -33.877 -2.528  1.00 40.86  ?  351 LEU   A N   1 
ATOM   2514 C  CA  . LEU   A 1 319 ? -15.701 -34.879 -1.583  1.00 40.49  ?  351 LEU   A CA  1 
ATOM   2515 C  C   . LEU   A 1 319 ? -15.318 -36.262 -2.060  1.00 42.35  ?  351 LEU   A C   1 
ATOM   2516 O  O   . LEU   A 1 319 ? -14.810 -37.080 -1.290  1.00 41.59  ?  351 LEU   A O   1 
ATOM   2517 C  CB  . LEU   A 1 319 ? -17.202 -34.746 -1.424  1.00 41.59  ?  351 LEU   A CB  1 
ATOM   2518 C  CG  . LEU   A 1 319 ? -17.943 -35.722 -0.578  1.00 38.36  ?  351 LEU   A CG  1 
ATOM   2519 C  CD1 . LEU   A 1 319 ? -17.629 -35.414 0.824   1.00 33.02  ?  351 LEU   A CD1 1 
ATOM   2520 C  CD2 . LEU   A 1 319 ? -19.370 -35.558 -0.882  1.00 38.17  ?  351 LEU   A CD2 1 
ATOM   2521 N  N   . GLN   A 1 320 ? -15.534 -36.526 -3.346  1.00 48.25  ?  352 GLN   A N   1 
ATOM   2522 C  CA  . GLN   A 1 320 ? -15.141 -37.800 -3.934  1.00 46.97  ?  352 GLN   A CA  1 
ATOM   2523 C  C   . GLN   A 1 320 ? -13.662 -38.100 -3.704  1.00 44.32  ?  352 GLN   A C   1 
ATOM   2524 O  O   . GLN   A 1 320 ? -13.305 -39.215 -3.333  1.00 54.06  ?  352 GLN   A O   1 
ATOM   2525 C  CB  . GLN   A 1 320 ? -15.479 -37.799 -5.413  1.00 37.98  ?  352 GLN   A CB  1 
ATOM   2526 C  CG  . GLN   A 1 320 ? -16.935 -37.689 -5.662  1.00 37.48  ?  352 GLN   A CG  1 
ATOM   2527 C  CD  . GLN   A 1 320 ? -17.307 -37.606 -7.106  1.00 45.16  ?  352 GLN   A CD  1 
ATOM   2528 O  OE1 . GLN   A 1 320 ? -18.309 -36.995 -7.448  1.00 34.62  ?  352 GLN   A OE1 1 
ATOM   2529 N  NE2 . GLN   A 1 320 ? -16.532 -38.249 -7.969  1.00 54.87  ?  352 GLN   A NE2 1 
ATOM   2530 N  N   . VAL   A 1 321 ? -12.789 -37.118 -3.887  1.00 39.89  ?  353 VAL   A N   1 
ATOM   2531 C  CA  . VAL   A 1 321 ? -11.390 -37.317 -3.549  1.00 39.64  ?  353 VAL   A CA  1 
ATOM   2532 C  C   . VAL   A 1 321 ? -11.252 -37.666 -2.090  1.00 41.13  ?  353 VAL   A C   1 
ATOM   2533 O  O   . VAL   A 1 321 ? -10.563 -38.613 -1.726  1.00 47.75  ?  353 VAL   A O   1 
ATOM   2534 C  CB  . VAL   A 1 321 ? -10.574 -36.065 -3.879  1.00 43.64  ?  353 VAL   A CB  1 
ATOM   2535 C  CG1 . VAL   A 1 321 ? -9.212  -36.223 -3.372  1.00 47.49  ?  353 VAL   A CG1 1 
ATOM   2536 C  CG2 . VAL   A 1 321 ? -10.511 -35.854 -5.328  1.00 46.61  ?  353 VAL   A CG2 1 
ATOM   2537 N  N   . PHE   A 1 322 ? -11.861 -36.875 -1.226  1.00 46.16  ?  354 PHE   A N   1 
ATOM   2538 C  CA  . PHE   A 1 322 ? -11.757 -37.126 0.202   1.00 47.03  ?  354 PHE   A CA  1 
ATOM   2539 C  C   . PHE   A 1 322 ? -12.121 -38.556 0.555   1.00 47.54  ?  354 PHE   A C   1 
ATOM   2540 O  O   . PHE   A 1 322 ? -11.552 -39.142 1.477   1.00 42.01  ?  354 PHE   A O   1 
ATOM   2541 C  CB  . PHE   A 1 322 ? -12.667 -36.170 0.946   1.00 45.15  ?  354 PHE   A CB  1 
ATOM   2542 C  CG  . PHE   A 1 322 ? -12.642 -36.339 2.419   1.00 44.28  ?  354 PHE   A CG  1 
ATOM   2543 C  CD1 . PHE   A 1 322 ? -13.454 -37.255 3.036   1.00 42.29  ?  354 PHE   A CD1 1 
ATOM   2544 C  CD2 . PHE   A 1 322 ? -11.829 -35.557 3.186   1.00 42.12  ?  354 PHE   A CD2 1 
ATOM   2545 C  CE1 . PHE   A 1 322 ? -13.434 -37.394 4.374   1.00 39.63  ?  354 PHE   A CE1 1 
ATOM   2546 C  CE2 . PHE   A 1 322 ? -11.809 -35.703 4.530   1.00 45.19  ?  354 PHE   A CE2 1 
ATOM   2547 C  CZ  . PHE   A 1 322 ? -12.610 -36.627 5.120   1.00 48.12  ?  354 PHE   A CZ  1 
ATOM   2548 N  N   . VAL   A 1 323 ? -13.072 -39.131 -0.158  1.00 44.30  ?  355 VAL   A N   1 
ATOM   2549 C  CA  . VAL   A 1 323 ? -13.544 -40.459 0.181   1.00 44.04  ?  355 VAL   A CA  1 
ATOM   2550 C  C   . VAL   A 1 323 ? -12.562 -41.510 -0.290  1.00 51.20  ?  355 VAL   A C   1 
ATOM   2551 O  O   . VAL   A 1 323 ? -12.116 -42.350 0.496   1.00 54.22  ?  355 VAL   A O   1 
ATOM   2552 C  CB  . VAL   A 1 323 ? -14.946 -40.680 -0.404  1.00 52.35  ?  355 VAL   A CB  1 
ATOM   2553 C  CG1 . VAL   A 1 323 ? -15.324 -42.109 -0.406  1.00 49.05  ?  355 VAL   A CG1 1 
ATOM   2554 C  CG2 . VAL   A 1 323 ? -15.949 -39.885 0.402   1.00 51.21  ?  355 VAL   A CG2 1 
ATOM   2555 N  N   . LEU   A 1 324 ? -12.213 -41.488 -1.576  1.00 49.54  ?  356 LEU   A N   1 
ATOM   2556 C  CA  . LEU   A 1 324 ? -11.134 -42.344 -2.057  1.00 45.84  ?  356 LEU   A CA  1 
ATOM   2557 C  C   . LEU   A 1 324 ? -9.893  -42.195 -1.203  1.00 49.64  ?  356 LEU   A C   1 
ATOM   2558 O  O   . LEU   A 1 324 ? -9.209  -43.173 -0.916  1.00 49.92  ?  356 LEU   A O   1 
ATOM   2559 C  CB  . LEU   A 1 324 ? -10.792 -42.027 -3.495  1.00 41.53  ?  356 LEU   A CB  1 
ATOM   2560 C  CG  . LEU   A 1 324 ? -11.895 -42.151 -4.506  1.00 46.32  ?  356 LEU   A CG  1 
ATOM   2561 C  CD1 . LEU   A 1 324 ? -11.400 -41.638 -5.810  1.00 50.76  ?  356 LEU   A CD1 1 
ATOM   2562 C  CD2 . LEU   A 1 324 ? -12.255 -43.566 -4.638  1.00 57.35  ?  356 LEU   A CD2 1 
ATOM   2563 N  N   . GLU   A 1 325 ? -9.578  -40.981 -0.789  1.00 46.18  ?  357 GLU   A N   1 
ATOM   2564 C  CA  . GLU   A 1 325 ? -8.432  -40.808 0.074   1.00 47.93  ?  357 GLU   A CA  1 
ATOM   2565 C  C   . GLU   A 1 325 ? -8.642  -41.440 1.442   1.00 49.78  ?  357 GLU   A C   1 
ATOM   2566 O  O   . GLU   A 1 325 ? -7.693  -41.969 2.018   1.00 50.29  ?  357 GLU   A O   1 
ATOM   2567 C  CB  . GLU   A 1 325 ? -8.107  -39.338 0.209   1.00 57.40  ?  357 GLU   A CB  1 
ATOM   2568 C  CG  . GLU   A 1 325 ? -7.304  -38.792 -0.938  1.00 54.71  ?  357 GLU   A CG  1 
ATOM   2569 C  CD  . GLU   A 1 325 ? -6.715  -37.433 -0.648  1.00 60.66  ?  357 GLU   A CD  1 
ATOM   2570 O  OE1 . GLU   A 1 325 ? -6.816  -36.936 0.508   1.00 47.31  ?  357 GLU   A OE1 1 
ATOM   2571 O  OE2 . GLU   A 1 325 ? -6.150  -36.864 -1.603  1.00 59.29  ?  357 GLU   A OE2 1 
ATOM   2572 N  N   . TYR   A 1 326 ? -9.857  -41.390 1.996   1.00 53.81  ?  358 TYR   A N   1 
ATOM   2573 C  CA  . TYR   A 1 326 ? -10.076 -42.005 3.307   1.00 51.69  ?  358 TYR   A CA  1 
ATOM   2574 C  C   . TYR   A 1 326 ? -10.085 -43.521 3.218   1.00 53.23  ?  358 TYR   A C   1 
ATOM   2575 O  O   . TYR   A 1 326 ? -9.590  -44.197 4.122   1.00 50.43  ?  358 TYR   A O   1 
ATOM   2576 C  CB  . TYR   A 1 326 ? -11.382 -41.536 3.935   1.00 53.21  ?  358 TYR   A CB  1 
ATOM   2577 C  CG  . TYR   A 1 326 ? -11.482 -41.823 5.432   1.00 52.15  ?  358 TYR   A CG  1 
ATOM   2578 C  CD1 . TYR   A 1 326 ? -11.722 -43.101 5.915   1.00 57.85  ?  358 TYR   A CD1 1 
ATOM   2579 C  CD2 . TYR   A 1 326 ? -11.329 -40.818 6.354   1.00 50.54  ?  358 TYR   A CD2 1 
ATOM   2580 C  CE1 . TYR   A 1 326 ? -11.790 -43.355 7.276   1.00 50.94  ?  358 TYR   A CE1 1 
ATOM   2581 C  CE2 . TYR   A 1 326 ? -11.402 -41.062 7.694   1.00 49.74  ?  358 TYR   A CE2 1 
ATOM   2582 C  CZ  . TYR   A 1 326 ? -11.629 -42.329 8.150   1.00 53.36  ?  358 TYR   A CZ  1 
ATOM   2583 O  OH  . TYR   A 1 326 ? -11.683 -42.565 9.505   1.00 55.88  ?  358 TYR   A OH  1 
ATOM   2584 N  N   . LEU   A 1 327 ? -10.656 -44.073 2.153   1.00 56.06  ?  359 LEU   A N   1 
ATOM   2585 C  CA  . LEU   A 1 327 ? -10.724 -45.514 1.945   1.00 54.99  ?  359 LEU   A CA  1 
ATOM   2586 C  C   . LEU   A 1 327 ? -9.483  -46.114 1.290   1.00 54.26  ?  359 LEU   A C   1 
ATOM   2587 O  O   . LEU   A 1 327 ? -9.443  -47.318 1.075   1.00 57.16  ?  359 LEU   A O   1 
ATOM   2588 C  CB  . LEU   A 1 327 ? -11.920 -45.865 1.064   1.00 55.10  ?  359 LEU   A CB  1 
ATOM   2589 C  CG  . LEU   A 1 327 ? -13.281 -45.310 1.392   1.00 53.29  ?  359 LEU   A CG  1 
ATOM   2590 C  CD1 . LEU   A 1 327 ? -14.309 -45.858 0.418   1.00 49.70  ?  359 LEU   A CD1 1 
ATOM   2591 C  CD2 . LEU   A 1 327 ? -13.604 -45.691 2.791   1.00 50.54  ?  359 LEU   A CD2 1 
ATOM   2592 N  N   . HIS   A 1 328 ? -8.490  -45.327 0.925   1.00 60.45  ?  360 HIS   A N   1 
ATOM   2593 C  CA  . HIS   A 1 328 ? -7.352  -45.850 0.180   1.00 64.34  ?  360 HIS   A CA  1 
ATOM   2594 C  C   . HIS   A 1 328 ? -7.798  -46.526 -1.121  1.00 67.55  ?  360 HIS   A C   1 
ATOM   2595 O  O   . HIS   A 1 328 ? -7.676  -47.729 -1.288  1.00 67.18  ?  360 HIS   A O   1 
ATOM   2596 C  CB  . HIS   A 1 328 ? -6.570  -46.827 1.049   1.00 47.34  ?  360 HIS   A CB  1 
ATOM   2597 C  CG  . HIS   A 1 328 ? -6.114  -46.249 2.343   1.00 49.70  ?  360 HIS   A CG  1 
ATOM   2598 N  ND1 . HIS   A 1 328 ? -5.211  -46.884 3.158   1.00 54.66  ?  360 HIS   A ND1 1 
ATOM   2599 C  CD2 . HIS   A 1 328 ? -6.419  -45.087 2.961   1.00 60.56  ?  360 HIS   A CD2 1 
ATOM   2600 C  CE1 . HIS   A 1 328 ? -4.980  -46.142 4.225   1.00 58.48  ?  360 HIS   A CE1 1 
ATOM   2601 N  NE2 . HIS   A 1 328 ? -5.694  -45.041 4.126   1.00 55.30  ?  360 HIS   A NE2 1 
ATOM   2602 N  N   . LEU   A 1 329 ? -8.289  -45.713 -2.058  1.00 66.91  ?  361 LEU   A N   1 
ATOM   2603 C  CA  . LEU   A 1 329 ? -8.703  -46.214 -3.373  1.00 60.82  ?  361 LEU   A CA  1 
ATOM   2604 C  C   . LEU   A 1 329 ? -8.245  -45.332 -4.530  1.00 70.77  ?  361 LEU   A C   1 
ATOM   2605 O  O   . LEU   A 1 329 ? -8.636  -45.557 -5.686  1.00 69.32  ?  361 LEU   A O   1 
ATOM   2606 C  CB  . LEU   A 1 329 ? -10.209 -46.348 -3.435  1.00 56.19  ?  361 LEU   A CB  1 
ATOM   2607 C  CG  . LEU   A 1 329 ? -10.809 -47.230 -2.345  1.00 57.50  ?  361 LEU   A CG  1 
ATOM   2608 C  CD1 . LEU   A 1 329 ? -12.296 -47.180 -2.395  1.00 62.67  ?  361 LEU   A CD1 1 
ATOM   2609 C  CD2 . LEU   A 1 329 ? -10.396 -48.634 -2.557  1.00 72.42  ?  361 LEU   A CD2 1 
ATOM   2610 O  OXT . LEU   A 1 329 ? -7.475  -44.393 -4.334  1.00 62.73  ?  361 LEU   A OXT 1 
HETATM 2611 ZN ZN  . ZN    B 2 .   ? -34.017 -26.727 6.940   1.00 32.05  ?  401 ZN    A ZN  1 
HETATM 2612 C  C11 . A1D94 C 3 .   ? -32.627 -23.515 13.196  1.00 62.83  ?  402 A1D94 A C11 1 
HETATM 2613 C  C16 . A1D94 C 3 .   ? -32.601 -22.330 13.838  1.00 71.81  ?  402 A1D94 A C16 1 
HETATM 2614 N  N17 . A1D94 C 3 .   ? -31.401 -21.717 14.341  1.00 71.83  ?  402 A1D94 A N17 1 
HETATM 2615 O  O01 . A1D94 C 3 .   ? -30.431 -24.045 13.399  1.00 62.27  ?  402 A1D94 A O01 1 
HETATM 2616 C  C02 . A1D94 C 3 .   ? -31.446 -24.369 12.943  1.00 60.20  ?  402 A1D94 A C02 1 
HETATM 2617 N  N03 . A1D94 C 3 .   ? -31.590 -25.564 12.186  1.00 57.85  ?  402 A1D94 A N03 1 
HETATM 2618 C  C04 . A1D94 C 3 .   ? -30.426 -26.387 11.996  1.00 59.99  ?  402 A1D94 A C04 1 
HETATM 2619 C  C05 . A1D94 C 3 .   ? -29.831 -26.323 10.609  1.00 45.06  ?  402 A1D94 A C05 1 
HETATM 2620 C  C06 . A1D94 C 3 .   ? -30.697 -26.831 9.495   1.00 35.51  ?  402 A1D94 A C06 1 
HETATM 2621 C  C07 . A1D94 C 3 .   ? -31.908 -26.389 9.110   1.00 42.94  ?  402 A1D94 A C07 1 
HETATM 2622 N  N08 . A1D94 C 3 .   ? -32.345 -27.062 8.064   1.00 37.58  ?  402 A1D94 A N08 1 
HETATM 2623 C  C09 . A1D94 C 3 .   ? -31.382 -27.942 7.863   1.00 41.47  ?  402 A1D94 A C09 1 
HETATM 2624 N  N10 . A1D94 C 3 .   ? -30.415 -27.781 8.698   1.00 35.50  ?  402 A1D94 A N10 1 
HETATM 2625 N  N12 . A1D94 C 3 .   ? -33.836 -23.783 12.883  1.00 64.01  1  402 A1D94 A N12 1 
HETATM 2626 O  O13 . A1D94 C 3 .   ? -34.228 -24.914 12.210  1.00 55.59  -1 402 A1D94 A O13 1 
HETATM 2627 O  O14 . A1D94 C 3 .   ? -34.611 -22.781 13.294  1.00 70.25  ?  402 A1D94 A O14 1 
HETATM 2628 N  N15 . A1D94 C 3 .   ? -33.823 -21.876 13.893  1.00 70.79  ?  402 A1D94 A N15 1 
HETATM 2629 S  S   . DMS   D 4 .   ? -48.884 -32.261 8.836   1.00 92.51  ?  403 DMS   A S   1 
HETATM 2630 O  O   . DMS   D 4 .   ? -47.437 -31.893 8.856   1.00 71.81  ?  403 DMS   A O   1 
HETATM 2631 C  C1  . DMS   D 4 .   ? -49.854 -30.730 8.783   1.00 57.36  ?  403 DMS   A C1  1 
HETATM 2632 C  C2  . DMS   D 4 .   ? -49.299 -33.033 7.239   1.00 63.07  ?  403 DMS   A C2  1 
HETATM 2633 S  S   . DMS   E 4 .   ? -10.122 -22.335 -12.077 1.00 84.96  ?  404 DMS   A S   1 
HETATM 2634 O  O   . DMS   E 4 .   ? -8.958  -21.399 -12.166 1.00 69.62  ?  404 DMS   A O   1 
HETATM 2635 C  C1  . DMS   E 4 .   ? -10.762 -22.668 -13.751 1.00 63.30  ?  404 DMS   A C1  1 
HETATM 2636 C  C2  . DMS   E 4 .   ? -9.525  -23.981 -11.594 1.00 54.69  ?  404 DMS   A C2  1 
HETATM 2637 C  C1  . GOL   F 5 .   ? -8.228  -37.839 15.714  1.00 55.11  ?  405 GOL   A C1  1 
HETATM 2638 O  O1  . GOL   F 5 .   ? -8.452  -36.467 15.515  1.00 67.04  ?  405 GOL   A O1  1 
HETATM 2639 C  C2  . GOL   F 5 .   ? -7.358  -37.904 16.951  1.00 61.11  ?  405 GOL   A C2  1 
HETATM 2640 O  O2  . GOL   F 5 .   ? -7.160  -36.548 17.297  1.00 45.10  ?  405 GOL   A O2  1 
HETATM 2641 C  C3  . GOL   F 5 .   ? -8.112  -38.728 18.020  1.00 69.25  ?  405 GOL   A C3  1 
HETATM 2642 O  O3  . GOL   F 5 .   ? -7.308  -39.607 18.827  1.00 66.10  ?  405 GOL   A O3  1 
HETATM 2643 C  C1  . GOL   G 5 .   ? -27.470 -28.674 -16.681 1.00 57.74  ?  406 GOL   A C1  1 
HETATM 2644 O  O1  . GOL   G 5 .   ? -26.535 -29.212 -15.775 1.00 61.41  ?  406 GOL   A O1  1 
HETATM 2645 C  C2  . GOL   G 5 .   ? -27.958 -27.280 -16.261 1.00 60.18  ?  406 GOL   A C2  1 
HETATM 2646 O  O2  . GOL   G 5 .   ? -29.312 -27.321 -15.897 1.00 58.23  ?  406 GOL   A O2  1 
HETATM 2647 C  C3  . GOL   G 5 .   ? -27.219 -26.635 -15.096 1.00 57.78  ?  406 GOL   A C3  1 
HETATM 2648 O  O3  . GOL   G 5 .   ? -28.092 -25.720 -14.455 1.00 52.70  ?  406 GOL   A O3  1 
HETATM 2649 C  C1  . GOL   H 5 .   ? -28.355 -18.314 -10.466 1.00 53.95  ?  407 GOL   A C1  1 
HETATM 2650 O  O1  . GOL   H 5 .   ? -27.935 -18.132 -11.810 1.00 60.63  ?  407 GOL   A O1  1 
HETATM 2651 C  C2  . GOL   H 5 .   ? -27.218 -18.864 -9.598  1.00 60.37  ?  407 GOL   A C2  1 
HETATM 2652 O  O2  . GOL   H 5 .   ? -26.056 -19.095 -10.378 1.00 56.96  ?  407 GOL   A O2  1 
HETATM 2653 C  C3  . GOL   H 5 .   ? -26.965 -17.908 -8.412  1.00 60.56  ?  407 GOL   A C3  1 
HETATM 2654 O  O3  . GOL   H 5 .   ? -25.624 -17.451 -8.339  1.00 55.23  ?  407 GOL   A O3  1 
HETATM 2655 C  C1  . GOL   I 5 .   ? -37.772 -49.656 15.422  1.00 65.71  ?  408 GOL   A C1  1 
HETATM 2656 O  O1  . GOL   I 5 .   ? -37.072 -49.635 16.645  1.00 69.48  ?  408 GOL   A O1  1 
HETATM 2657 C  C2  . GOL   I 5 .   ? -36.802 -50.165 14.376  1.00 66.42  ?  408 GOL   A C2  1 
HETATM 2658 O  O2  . GOL   I 5 .   ? -36.255 -51.358 14.883  1.00 71.17  ?  408 GOL   A O2  1 
HETATM 2659 C  C3  . GOL   I 5 .   ? -37.463 -50.363 13.016  1.00 66.36  ?  408 GOL   A C3  1 
HETATM 2660 O  O3  . GOL   I 5 .   ? -36.440 -50.635 12.071  1.00 71.51  ?  408 GOL   A O3  1 
HETATM 2661 C  C1  . DMF   J 6 .   ? -19.356 -20.094 -5.779  1.00 46.48  ?  409 DMF   A C1  1 
HETATM 2662 C  C2  . DMF   J 6 .   ? -19.252 -19.559 -8.336  1.00 47.92  ?  409 DMF   A C2  1 
HETATM 2663 C  C   . DMF   J 6 .   ? -17.537 -20.811 -7.065  1.00 59.28  ?  409 DMF   A C   1 
HETATM 2664 O  O   . DMF   J 6 .   ? -16.871 -20.760 -6.026  1.00 57.69  ?  409 DMF   A O   1 
HETATM 2665 N  N   . DMF   J 6 .   ? -18.688 -20.154 -7.088  1.00 68.32  ?  409 DMF   A N   1 
HETATM 2666 O  O   . HOH   K 7 .   ? -20.087 -57.819 10.508  1.00 30.00  ?  501 HOH   A O   1 
HETATM 2667 O  O   . HOH   K 7 .   ? -34.324 -33.372 19.069  1.00 30.00  ?  502 HOH   A O   1 
HETATM 2668 O  O   . HOH   K 7 .   ? -20.023 -36.233 -5.721  1.00 30.00  ?  503 HOH   A O   1 
HETATM 2669 O  O   . HOH   K 7 .   ? -46.372 -36.298 9.152   1.00 58.63  ?  504 HOH   A O   1 
HETATM 2670 O  O   . HOH   K 7 .   ? -19.708 -32.887 -10.221 1.00 30.00  ?  505 HOH   A O   1 
HETATM 2671 O  O   . HOH   K 7 .   ? -10.521 -41.301 11.135  1.00 30.00  ?  506 HOH   A O   1 
HETATM 2672 O  O   . HOH   K 7 .   ? -37.066 -27.234 10.933  1.00 52.45  ?  507 HOH   A O   1 
HETATM 2673 O  O   . HOH   K 7 .   ? -39.758 -37.423 4.816   1.00 30.00  ?  508 HOH   A O   1 
HETATM 2674 O  O   . HOH   K 7 .   ? -27.768 -44.601 -10.485 1.00 66.76  ?  509 HOH   A O   1 
HETATM 2675 O  O   . HOH   K 7 .   ? -28.908 -32.882 8.405   1.00 42.18  ?  510 HOH   A O   1 
HETATM 2676 O  O   . HOH   K 7 .   ? -27.336 -50.591 4.700   1.00 30.00  ?  511 HOH   A O   1 
HETATM 2677 O  O   . HOH   K 7 .   ? -16.308 -30.501 -14.043 1.00 62.59  ?  512 HOH   A O   1 
HETATM 2678 O  O   . HOH   K 7 .   ? -15.256 -27.651 -11.441 1.00 30.00  ?  513 HOH   A O   1 
HETATM 2679 O  O   . HOH   K 7 .   ? -23.433 -24.491 -1.239  1.00 40.46  ?  514 HOH   A O   1 
HETATM 2680 O  O   . HOH   K 7 .   ? -33.932 -24.212 3.340   1.00 35.54  ?  515 HOH   A O   1 
HETATM 2681 O  O   . HOH   K 7 .   ? -34.287 -33.317 1.970   1.00 30.00  ?  516 HOH   A O   1 
HETATM 2682 O  O   . HOH   K 7 .   ? -36.024 -29.113 4.511   1.00 36.27  ?  517 HOH   A O   1 
HETATM 2683 O  O   . HOH   K 7 .   ? -42.125 -29.134 1.983   1.00 42.79  ?  518 HOH   A O   1 
HETATM 2684 O  O   . HOH   K 7 .   ? -24.806 -23.311 0.907   1.00 36.04  ?  519 HOH   A O   1 
HETATM 2685 O  O   . HOH   K 7 .   ? -40.560 -17.656 0.868   1.00 30.00  ?  520 HOH   A O   1 
HETATM 2686 O  O   . HOH   K 7 .   ? -33.067 -27.984 11.155  1.00 56.35  ?  521 HOH   A O   1 
HETATM 2687 O  O   . HOH   K 7 .   ? -8.822  -58.585 1.831   1.00 43.60  ?  522 HOH   A O   1 
HETATM 2688 O  O   . HOH   K 7 .   ? -19.288 -49.875 10.910  1.00 47.37  ?  523 HOH   A O   1 
HETATM 2689 O  O   . HOH   K 7 .   ? -44.667 -27.161 1.391   1.00 47.57  ?  524 HOH   A O   1 
HETATM 2690 O  O   . HOH   K 7 .   ? -33.372 -37.185 11.442  1.00 30.00  ?  525 HOH   A O   1 
HETATM 2691 O  O   . HOH   K 7 .   ? -28.764 -32.941 5.668   1.00 35.77  ?  526 HOH   A O   1 
HETATM 2692 O  O   . HOH   K 7 .   ? -28.972 -24.826 15.676  1.00 53.98  ?  527 HOH   A O   1 
HETATM 2693 O  O   . HOH   K 7 .   ? -29.116 -20.949 -3.082  1.00 32.97  ?  528 HOH   A O   1 
HETATM 2694 O  O   . HOH   K 7 .   ? -26.392 -44.601 -12.981 1.00 52.41  ?  529 HOH   A O   1 
HETATM 2695 O  O   . HOH   K 7 .   ? -6.015  -43.961 -7.288  1.00 37.77  ?  530 HOH   A O   1 
HETATM 2696 O  O   . HOH   K 7 .   ? -31.454 -22.621 -3.544  1.00 46.41  ?  531 HOH   A O   1 
HETATM 2697 O  O   . HOH   K 7 .   ? -33.000 -27.376 19.090  1.00 36.43  ?  532 HOH   A O   1 
HETATM 2698 O  O   . HOH   K 7 .   ? -21.237 -19.618 -12.076 1.00 45.11  ?  533 HOH   A O   1 
HETATM 2699 O  O   . HOH   K 7 .   ? -29.465 -23.322 -11.983 1.00 37.07  ?  534 HOH   A O   1 
HETATM 2700 O  O   . HOH   K 7 .   ? -26.568 -31.389 22.327  1.00 38.25  ?  535 HOH   A O   1 
HETATM 2701 O  O   . HOH   K 7 .   ? -1.942  -32.476 -0.987  1.00 30.00  ?  536 HOH   A O   1 
# 
