data_6DTK
# 
_entry.id   6DTK 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.311 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   6DTK         
WWPDB D_1000235215 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        'Zn-deficient mutant' 
_pdbx_database_related.db_id          2R27 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        6DTK 
_pdbx_database_status.recvd_initial_deposition_date   2018-06-17 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Streltsov, V.A.' 1 ? 
'Nuttall, S.D.'   2 ? 
'Ganio, K.E.'     3 ? 
'Roberts, B.'     4 ? 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Structural characterization of heterodimers of FALS mutant SOD enzyme' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Streltsov, V.A.' 1 ? 
primary 'Nuttall, S.D.'   2 ? 
primary 'Ganio, K.E.'     3 ? 
primary 'Roberts, B.'     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                     6DTK 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     162.699 
_cell.length_a_esd                 ? 
_cell.length_b                     201.671 
_cell.length_b_esd                 ? 
_cell.length_c                     143.834 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        40 
_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             ? 
# 
_symmetry.entry_id                         6DTK 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
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 'Superoxide dismutase C111S/D83S-C111S HETERODIMER' 32725.129 5    1.15.1.1 ? ? ? 
2 non-polymer syn 'ZINC ION'                                          65.409    10   ?        ? ? ? 
3 non-polymer syn 'COPPER (II) ION'                                   63.546    10   ?        ? ? ? 
4 non-polymer syn 'MALONATE ION'                                      102.046   1    ?        ? ? ? 
5 water       nat water                                               18.015    1356 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Superoxide dismutase 1,hSod1,Superoxide dismutase 1,hSod1' 
# 
_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       
;MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEER
HVGSLGNVTADKDGVADVSIEDSVISLSGDHSIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQGAAASG
GGGGSGGGGSATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRK
HGGPKDEERHVGSLGNVTADKDGVADVSIEDSVISLSGDHSIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIG
IAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEER
HVGSLGNVTADKDGVADVSIEDSVISLSGDHSIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQGAAASG
GGGGSGGGGSATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRK
HGGPKDEERHVGSLGNVTADKDGVADVSIEDSVISLSGDHSIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIG
IAQ
;
_entity_poly.pdbx_strand_id                 A,C,E,G,I 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   THR n 
1 4   LYS n 
1 5   ALA n 
1 6   VAL n 
1 7   CYS n 
1 8   VAL n 
1 9   LEU n 
1 10  LYS n 
1 11  GLY n 
1 12  ASP n 
1 13  GLY n 
1 14  PRO n 
1 15  VAL n 
1 16  GLN n 
1 17  GLY n 
1 18  ILE n 
1 19  ILE n 
1 20  ASN n 
1 21  PHE n 
1 22  GLU n 
1 23  GLN n 
1 24  LYS n 
1 25  GLU n 
1 26  SER n 
1 27  ASN n 
1 28  GLY n 
1 29  PRO n 
1 30  VAL n 
1 31  LYS n 
1 32  VAL n 
1 33  TRP n 
1 34  GLY n 
1 35  SER n 
1 36  ILE n 
1 37  LYS n 
1 38  GLY n 
1 39  LEU n 
1 40  THR n 
1 41  GLU n 
1 42  GLY n 
1 43  LEU n 
1 44  HIS n 
1 45  GLY n 
1 46  PHE n 
1 47  HIS n 
1 48  VAL n 
1 49  HIS n 
1 50  GLU n 
1 51  PHE n 
1 52  GLY n 
1 53  ASP n 
1 54  ASN n 
1 55  THR n 
1 56  ALA n 
1 57  GLY n 
1 58  CYS n 
1 59  THR n 
1 60  SER n 
1 61  ALA n 
1 62  GLY n 
1 63  PRO n 
1 64  HIS n 
1 65  PHE n 
1 66  ASN n 
1 67  PRO n 
1 68  LEU n 
1 69  SER n 
1 70  ARG n 
1 71  LYS n 
1 72  HIS n 
1 73  GLY n 
1 74  GLY n 
1 75  PRO n 
1 76  LYS n 
1 77  ASP n 
1 78  GLU n 
1 79  GLU n 
1 80  ARG n 
1 81  HIS n 
1 82  VAL n 
1 83  GLY n 
1 84  SER y 
1 84  ASP y 
1 85  LEU n 
1 86  GLY n 
1 87  ASN n 
1 88  VAL n 
1 89  THR n 
1 90  ALA n 
1 91  ASP n 
1 92  LYS n 
1 93  ASP n 
1 94  GLY n 
1 95  VAL n 
1 96  ALA n 
1 97  ASP n 
1 98  VAL n 
1 99  SER n 
1 100 ILE n 
1 101 GLU n 
1 102 ASP n 
1 103 SER n 
1 104 VAL n 
1 105 ILE n 
1 106 SER n 
1 107 LEU n 
1 108 SER n 
1 109 GLY n 
1 110 ASP n 
1 111 HIS n 
1 112 SER n 
1 113 ILE n 
1 114 ILE n 
1 115 GLY n 
1 116 ARG n 
1 117 THR n 
1 118 LEU n 
1 119 VAL n 
1 120 VAL n 
1 121 HIS n 
1 122 GLU n 
1 123 LYS n 
1 124 ALA n 
1 125 ASP n 
1 126 ASP n 
1 127 LEU n 
1 128 GLY n 
1 129 LYS n 
1 130 GLY n 
1 131 GLY n 
1 132 ASN n 
1 133 GLU n 
1 134 GLU n 
1 135 SER n 
1 136 THR n 
1 137 LYS n 
1 138 THR n 
1 139 GLY n 
1 140 ASN n 
1 141 ALA n 
1 142 GLY n 
1 143 SER n 
1 144 ARG n 
1 145 LEU n 
1 146 ALA n 
1 147 CYS n 
1 148 GLY n 
1 149 VAL n 
1 150 ILE n 
1 151 GLY n 
1 152 ILE n 
1 153 ALA n 
1 154 GLN n 
1 155 GLY n 
1 156 ALA n 
1 157 ALA n 
1 158 ALA n 
1 159 SER n 
1 160 GLY n 
1 161 GLY n 
1 162 GLY n 
1 163 GLY n 
1 164 GLY n 
1 165 SER n 
1 166 GLY n 
1 167 GLY n 
1 168 GLY n 
1 169 GLY n 
1 170 SER n 
1 171 ALA n 
1 172 THR n 
1 173 LYS n 
1 174 ALA n 
1 175 VAL n 
1 176 CYS n 
1 177 VAL n 
1 178 LEU n 
1 179 LYS n 
1 180 GLY n 
1 181 ASP n 
1 182 GLY n 
1 183 PRO n 
1 184 VAL n 
1 185 GLN n 
1 186 GLY n 
1 187 ILE n 
1 188 ILE n 
1 189 ASN n 
1 190 PHE n 
1 191 GLU n 
1 192 GLN n 
1 193 LYS n 
1 194 GLU n 
1 195 SER n 
1 196 ASN n 
1 197 GLY n 
1 198 PRO n 
1 199 VAL n 
1 200 LYS n 
1 201 VAL n 
1 202 TRP n 
1 203 GLY n 
1 204 SER n 
1 205 ILE n 
1 206 LYS n 
1 207 GLY n 
1 208 LEU n 
1 209 THR n 
1 210 GLU n 
1 211 GLY n 
1 212 LEU n 
1 213 HIS n 
1 214 GLY n 
1 215 PHE n 
1 216 HIS n 
1 217 VAL n 
1 218 HIS n 
1 219 GLU n 
1 220 PHE n 
1 221 GLY n 
1 222 ASP n 
1 223 ASN n 
1 224 THR n 
1 225 ALA n 
1 226 GLY n 
1 227 CYS n 
1 228 THR n 
1 229 SER n 
1 230 ALA n 
1 231 GLY n 
1 232 PRO n 
1 233 HIS n 
1 234 PHE n 
1 235 ASN n 
1 236 PRO n 
1 237 LEU n 
1 238 SER n 
1 239 ARG n 
1 240 LYS n 
1 241 HIS n 
1 242 GLY n 
1 243 GLY n 
1 244 PRO n 
1 245 LYS n 
1 246 ASP n 
1 247 GLU n 
1 248 GLU n 
1 249 ARG n 
1 250 HIS n 
1 251 VAL n 
1 252 GLY n 
1 253 SER y 
1 253 ASP y 
1 254 LEU n 
1 255 GLY n 
1 256 ASN n 
1 257 VAL n 
1 258 THR n 
1 259 ALA n 
1 260 ASP n 
1 261 LYS n 
1 262 ASP n 
1 263 GLY n 
1 264 VAL n 
1 265 ALA n 
1 266 ASP n 
1 267 VAL n 
1 268 SER n 
1 269 ILE n 
1 270 GLU n 
1 271 ASP n 
1 272 SER n 
1 273 VAL n 
1 274 ILE n 
1 275 SER n 
1 276 LEU n 
1 277 SER n 
1 278 GLY n 
1 279 ASP n 
1 280 HIS n 
1 281 SER n 
1 282 ILE n 
1 283 ILE n 
1 284 GLY n 
1 285 ARG n 
1 286 THR n 
1 287 LEU n 
1 288 VAL n 
1 289 VAL n 
1 290 HIS n 
1 291 GLU n 
1 292 LYS n 
1 293 ALA n 
1 294 ASP n 
1 295 ASP n 
1 296 LEU n 
1 297 GLY n 
1 298 LYS n 
1 299 GLY n 
1 300 GLY n 
1 301 ASN n 
1 302 GLU n 
1 303 GLU n 
1 304 SER n 
1 305 THR n 
1 306 LYS n 
1 307 THR n 
1 308 GLY n 
1 309 ASN n 
1 310 ALA n 
1 311 GLY n 
1 312 SER n 
1 313 ARG n 
1 314 LEU n 
1 315 ALA n 
1 316 CYS n 
1 317 GLY n 
1 318 VAL n 
1 319 ILE n 
1 320 GLY n 
1 321 ILE n 
1 322 ALA n 
1 323 GLN n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
1 1 sample 'Biological sequence' 1   158 Human ? SOD1 ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Escherichia coli' 469008 ? 
? ? ? ? ? 'BL21(DE3)pLysS' ? ? ? ? ? ? ? pET3d ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 159 323 Human ? SOD1 ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Escherichia coli' 469008 ? 
? ? ? ? ? 'BL21(DE3)pLysS' ? ? ? ? ? ? ? pET3d ? ? ? ? ? ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP SODC_HUMAN P00441 ? 1 
;MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEER
HVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
1 
2 UNP SODC_HUMAN P00441 ? 1 
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
2 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1  1 6DTK A 1   ? 154 ? P00441 1 ? 154 ? 0   153 
2  2 6DTK A 171 ? 323 ? P00441 2 ? 154 ? 170 322 
3  1 6DTK C 1   ? 154 ? P00441 1 ? 154 ? 0   153 
4  2 6DTK C 171 ? 323 ? P00441 2 ? 154 ? 170 322 
5  1 6DTK E 1   ? 154 ? P00441 1 ? 154 ? 0   153 
6  2 6DTK E 171 ? 323 ? P00441 2 ? 154 ? 170 322 
7  1 6DTK G 1   ? 154 ? P00441 1 ? 154 ? 0   153 
8  2 6DTK G 171 ? 323 ? P00441 2 ? 154 ? 170 322 
9  1 6DTK I 1   ? 154 ? P00441 1 ? 154 ? 0   153 
10 2 6DTK I 171 ? 323 ? P00441 2 ? 154 ? 170 322 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1  6DTK SER A 84  ? UNP P00441 ASP 84  microheterogeneity    83  1   
1  6DTK SER A 112 ? UNP P00441 CYS 112 'engineered mutation' 111 2   
1  6DTK GLY A 155 ? UNP P00441 ?   ?   linker                154 3   
1  6DTK ALA A 156 ? UNP P00441 ?   ?   linker                155 4   
1  6DTK ALA A 157 ? UNP P00441 ?   ?   linker                156 5   
1  6DTK ALA A 158 ? UNP P00441 ?   ?   linker                157 6   
1  6DTK SER A 159 ? UNP P00441 ?   ?   linker                158 7   
1  6DTK GLY A 160 ? UNP P00441 ?   ?   linker                159 8   
1  6DTK GLY A 161 ? UNP P00441 ?   ?   linker                160 9   
1  6DTK GLY A 162 ? UNP P00441 ?   ?   linker                161 10  
1  6DTK GLY A 163 ? UNP P00441 ?   ?   linker                162 11  
1  6DTK GLY A 164 ? UNP P00441 ?   ?   linker                163 12  
1  6DTK SER A 165 ? UNP P00441 ?   ?   linker                164 13  
1  6DTK GLY A 166 ? UNP P00441 ?   ?   linker                165 14  
1  6DTK GLY A 167 ? UNP P00441 ?   ?   linker                166 15  
1  6DTK GLY A 168 ? UNP P00441 ?   ?   linker                167 16  
1  6DTK GLY A 169 ? UNP P00441 ?   ?   linker                168 17  
1  6DTK SER A 170 ? UNP P00441 ?   ?   linker                169 18  
2  6DTK SER A 253 ? UNP P00441 ASP 84  microheterogeneity    252 19  
2  6DTK SER A 281 ? UNP P00441 CYS 112 'engineered mutation' 280 20  
3  6DTK SER C 84  ? UNP P00441 ASP 84  microheterogeneity    83  21  
3  6DTK SER C 112 ? UNP P00441 CYS 112 'engineered mutation' 111 22  
3  6DTK GLY C 155 ? UNP P00441 ?   ?   linker                154 23  
3  6DTK ALA C 156 ? UNP P00441 ?   ?   linker                155 24  
3  6DTK ALA C 157 ? UNP P00441 ?   ?   linker                156 25  
3  6DTK ALA C 158 ? UNP P00441 ?   ?   linker                157 26  
3  6DTK SER C 159 ? UNP P00441 ?   ?   linker                158 27  
3  6DTK GLY C 160 ? UNP P00441 ?   ?   linker                159 28  
3  6DTK GLY C 161 ? UNP P00441 ?   ?   linker                160 29  
3  6DTK GLY C 162 ? UNP P00441 ?   ?   linker                161 30  
3  6DTK GLY C 163 ? UNP P00441 ?   ?   linker                162 31  
3  6DTK GLY C 164 ? UNP P00441 ?   ?   linker                163 32  
3  6DTK SER C 165 ? UNP P00441 ?   ?   linker                164 33  
3  6DTK GLY C 166 ? UNP P00441 ?   ?   linker                165 34  
3  6DTK GLY C 167 ? UNP P00441 ?   ?   linker                166 35  
3  6DTK GLY C 168 ? UNP P00441 ?   ?   linker                167 36  
3  6DTK GLY C 169 ? UNP P00441 ?   ?   linker                168 37  
3  6DTK SER C 170 ? UNP P00441 ?   ?   linker                169 38  
4  6DTK SER C 253 ? UNP P00441 ASP 84  microheterogeneity    252 39  
4  6DTK SER C 281 ? UNP P00441 CYS 112 'engineered mutation' 280 40  
5  6DTK SER E 84  ? UNP P00441 ASP 84  microheterogeneity    83  41  
5  6DTK SER E 112 ? UNP P00441 CYS 112 'engineered mutation' 111 42  
5  6DTK GLY E 155 ? UNP P00441 ?   ?   linker                154 43  
5  6DTK ALA E 156 ? UNP P00441 ?   ?   linker                155 44  
5  6DTK ALA E 157 ? UNP P00441 ?   ?   linker                156 45  
5  6DTK ALA E 158 ? UNP P00441 ?   ?   linker                157 46  
5  6DTK SER E 159 ? UNP P00441 ?   ?   linker                158 47  
5  6DTK GLY E 160 ? UNP P00441 ?   ?   linker                159 48  
5  6DTK GLY E 161 ? UNP P00441 ?   ?   linker                160 49  
5  6DTK GLY E 162 ? UNP P00441 ?   ?   linker                161 50  
5  6DTK GLY E 163 ? UNP P00441 ?   ?   linker                162 51  
5  6DTK GLY E 164 ? UNP P00441 ?   ?   linker                163 52  
5  6DTK SER E 165 ? UNP P00441 ?   ?   linker                164 53  
5  6DTK GLY E 166 ? UNP P00441 ?   ?   linker                165 54  
5  6DTK GLY E 167 ? UNP P00441 ?   ?   linker                166 55  
5  6DTK GLY E 168 ? UNP P00441 ?   ?   linker                167 56  
5  6DTK GLY E 169 ? UNP P00441 ?   ?   linker                168 57  
5  6DTK SER E 170 ? UNP P00441 ?   ?   linker                169 58  
6  6DTK SER E 253 ? UNP P00441 ASP 84  microheterogeneity    252 59  
6  6DTK SER E 281 ? UNP P00441 CYS 112 'engineered mutation' 280 60  
7  6DTK SER G 84  ? UNP P00441 ASP 84  microheterogeneity    83  61  
7  6DTK SER G 112 ? UNP P00441 CYS 112 'engineered mutation' 111 62  
7  6DTK GLY G 155 ? UNP P00441 ?   ?   linker                154 63  
7  6DTK ALA G 156 ? UNP P00441 ?   ?   linker                155 64  
7  6DTK ALA G 157 ? UNP P00441 ?   ?   linker                156 65  
7  6DTK ALA G 158 ? UNP P00441 ?   ?   linker                157 66  
7  6DTK SER G 159 ? UNP P00441 ?   ?   linker                158 67  
7  6DTK GLY G 160 ? UNP P00441 ?   ?   linker                159 68  
7  6DTK GLY G 161 ? UNP P00441 ?   ?   linker                160 69  
7  6DTK GLY G 162 ? UNP P00441 ?   ?   linker                161 70  
7  6DTK GLY G 163 ? UNP P00441 ?   ?   linker                162 71  
7  6DTK GLY G 164 ? UNP P00441 ?   ?   linker                163 72  
7  6DTK SER G 165 ? UNP P00441 ?   ?   linker                164 73  
7  6DTK GLY G 166 ? UNP P00441 ?   ?   linker                165 74  
7  6DTK GLY G 167 ? UNP P00441 ?   ?   linker                166 75  
7  6DTK GLY G 168 ? UNP P00441 ?   ?   linker                167 76  
7  6DTK GLY G 169 ? UNP P00441 ?   ?   linker                168 77  
7  6DTK SER G 170 ? UNP P00441 ?   ?   linker                169 78  
8  6DTK SER G 253 ? UNP P00441 ASP 84  microheterogeneity    252 79  
8  6DTK SER G 281 ? UNP P00441 CYS 112 'engineered mutation' 280 80  
9  6DTK SER I 84  ? UNP P00441 ASP 84  microheterogeneity    83  81  
9  6DTK SER I 112 ? UNP P00441 CYS 112 'engineered mutation' 111 82  
9  6DTK GLY I 155 ? UNP P00441 ?   ?   linker                154 83  
9  6DTK ALA I 156 ? UNP P00441 ?   ?   linker                155 84  
9  6DTK ALA I 157 ? UNP P00441 ?   ?   linker                156 85  
9  6DTK ALA I 158 ? UNP P00441 ?   ?   linker                157 86  
9  6DTK SER I 159 ? UNP P00441 ?   ?   linker                158 87  
9  6DTK GLY I 160 ? UNP P00441 ?   ?   linker                159 88  
9  6DTK GLY I 161 ? UNP P00441 ?   ?   linker                160 89  
9  6DTK GLY I 162 ? UNP P00441 ?   ?   linker                161 90  
9  6DTK GLY I 163 ? UNP P00441 ?   ?   linker                162 91  
9  6DTK GLY I 164 ? UNP P00441 ?   ?   linker                163 92  
9  6DTK SER I 165 ? UNP P00441 ?   ?   linker                164 93  
9  6DTK GLY I 166 ? UNP P00441 ?   ?   linker                165 94  
9  6DTK GLY I 167 ? UNP P00441 ?   ?   linker                166 95  
9  6DTK GLY I 168 ? UNP P00441 ?   ?   linker                167 96  
9  6DTK GLY I 169 ? UNP P00441 ?   ?   linker                168 97  
9  6DTK SER I 170 ? UNP P00441 ?   ?   linker                169 98  
10 6DTK SER I 253 ? UNP P00441 ASP 84  microheterogeneity    252 99  
10 6DTK SER I 281 ? UNP P00441 CYS 112 'engineered mutation' 280 100 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE           ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE          ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE        ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'   ? 'C4 H7 N O4'     133.103 
CU  non-polymer         . 'COPPER (II) ION' ? 'Cu 2'           63.546  
CYS 'L-peptide linking' y CYSTEINE          ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE         ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'   ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE           ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE         ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER             ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE        ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE           ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE            ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE        ? 'C5 H11 N O2 S'  149.211 
MLI non-polymer         . 'MALONATE ION'    ? 'C3 H2 O4 -2'    102.046 
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 
VAL 'L-peptide linking' y VALINE            ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'        ? 'Zn 2'           65.409  
# 
_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                   6DTK 
_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            3.65 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         66.27 
_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_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '2-3 M Ammonium sulfate or Sodium malonate' 
_exptl_crystal_grow.pdbx_pH_range   4.5-7 
# 
_diffrn.ambient_environment    ? 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.ambient_temp_esd       ? 
_diffrn.crystal_id             1 
_diffrn.crystal_support        ? 
_diffrn.crystal_treatment      ? 
_diffrn.details                ? 
_diffrn.id                     1 
_diffrn.ambient_pressure       ? 
_diffrn.ambient_pressure_esd   ? 
_diffrn.ambient_pressure_gt    ? 
_diffrn.ambient_pressure_lt    ? 
_diffrn.ambient_temp_gt        ? 
_diffrn.ambient_temp_lt        ? 
# 
_diffrn_detector.details                      mirrors 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'ADSC QUANTUM 315' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2013-02-17 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    Si 
_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   0.953700 
_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                        'AUSTRALIAN SYNCHROTRON BEAMLINE MX1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.953700 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MX1 
_diffrn_source.pdbx_synchrotron_site       'Australian Synchrotron' 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         6DTK 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                2.000 
_reflns.d_resolution_low                 47.570 
_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                       158995 
_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       1.000 
_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                  14.20 
_reflns.pdbx_Rmerge_I_obs                0.08600 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  ? 
_reflns.pdbx_netI_over_av_sigmaI         ? 
_reflns.pdbx_netI_over_sigmaI            25.2500 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  ? 
_reflns.pdbx_Rpim_I_all                  ? 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         ? 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_R_split                     ? 
# 
_reflns_shell.d_res_high                  2.00 
_reflns_shell.d_res_low                   2.05 
_reflns_shell.meanI_over_sigI_all         ? 
_reflns_shell.meanI_over_sigI_obs         2.470 
_reflns_shell.number_measured_all         ? 
_reflns_shell.number_measured_obs         ? 
_reflns_shell.number_possible             ? 
_reflns_shell.number_unique_all           ? 
_reflns_shell.number_unique_obs           ? 
_reflns_shell.percent_possible_all        98.9 
_reflns_shell.percent_possible_obs        ? 
_reflns_shell.Rmerge_F_all                ? 
_reflns_shell.Rmerge_F_obs                ? 
_reflns_shell.Rmerge_I_all                ? 
_reflns_shell.Rmerge_I_obs                0.87100 
_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             13.40 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.pdbx_chi_squared            ? 
_reflns_shell.pdbx_netI_over_sigmaI_all   ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs   ? 
_reflns_shell.pdbx_Rrim_I_all             ? 
_reflns_shell.pdbx_Rpim_I_all             ? 
_reflns_shell.pdbx_rejects                ? 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_CC_half                ? 
_reflns_shell.pdbx_R_split                ? 
# 
_refine.aniso_B[1][1]                            1.38000 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.00000 
_refine.aniso_B[2][2]                            0.40000 
_refine.aniso_B[2][3]                            0.00000 
_refine.aniso_B[3][3]                            -1.78000 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               38.62 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.970 
_refine.correlation_coeff_Fo_to_Fc_free          0.956 
_refine.details                                  
;HYDROGENS HAVE BEEN ADDED IN THE RIDING
  POSITIONS
;
_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                                 6DTK 
_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                            2.00 
_refine.ls_d_res_low                             47.57 
_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                     150990 
_refine.ls_number_reflns_R_free                  7971 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.9 
_refine.ls_percent_reflns_R_free                 5.000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.158 
_refine.ls_R_factor_R_free                       0.190 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.156 
_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                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_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                          ? 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      1FUN 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.113 
_refine.pdbx_overall_ESU_R_Free                  0.112 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_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                 ? 
_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                             3.021 
_refine.overall_SU_ML                            0.082 
_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.pdbx_number_atoms_protein        11297 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         27 
_refine_hist.number_atoms_solvent             1356 
_refine_hist.number_atoms_total               12680 
_refine_hist.d_res_high                       2.00 
_refine_hist.d_res_low                        47.57 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.013  0.015  11661 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.017  10387 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.361  1.645  15651 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.193  1.660  24408 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 19.181 5.417  1629  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 40.530 24.494 514   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 15.406 15.000 1844  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 14.586 15.000 39    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.166  0.200  1477  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020  14484 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  2051  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 2.830  3.598  6289  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.829  3.598  6288  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 4.187  5.374  7859  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.188  5.374  7860  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.946  4.074  5372  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.946  4.074  5370  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 6.243  5.882  7791  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 8.997  46.041 12809 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 8.817  45.010 12362 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.00 
_refine_ls_shell.d_res_low                        2.05 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             576 
_refine_ls_shell.number_reflns_R_work             10937 
_refine_ls_shell.percent_reflns_obs               98.88 
_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                  0.2430 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2250 
_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_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
# 
_struct.entry_id                     6DTK 
_struct.title                        'Heterodimers of FALS mutant SOD enzyme' 
_struct.pdbx_descriptor              'Tetrabrachion,Neuraminidase (E.C.3.2.1.18)' 
_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        6DTK 
_struct_keywords.text            
'Copper/Zinc superoxide dismutase Cu, Zn-SOD1, metal binding protein, FALS Zn-deficient SOD1, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 1 ? 
C  N N 1 ? 
D  N N 1 ? 
E  N N 1 ? 
F  N N 2 ? 
G  N N 3 ? 
H  N N 2 ? 
I  N N 3 ? 
J  N N 2 ? 
K  N N 3 ? 
L  N N 2 ? 
M  N N 3 ? 
N  N N 2 ? 
O  N N 3 ? 
P  N N 2 ? 
Q  N N 3 ? 
R  N N 4 ? 
S  N N 2 ? 
T  N N 3 ? 
U  N N 2 ? 
V  N N 3 ? 
W  N N 2 ? 
X  N N 3 ? 
Y  N N 2 ? 
Z  N N 3 ? 
AA N N 5 ? 
BA N N 5 ? 
CA N N 5 ? 
DA N N 5 ? 
EA N N 5 ? 
# 
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 CYS A 58  ? GLY A 62  ? CYS A 57  GLY A 61  5 ? 5 
HELX_P HELX_P2  AA2 GLU A 133 ? LYS A 137 ? GLU A 132 LYS A 136 5 ? 5 
HELX_P HELX_P3  AA3 ALA A 225 ? GLY A 231 ? ALA A 224 GLY A 230 5 ? 7 
HELX_P HELX_P4  AA4 GLU A 303 ? GLY A 308 ? GLU A 302 GLY A 307 1 ? 6 
HELX_P HELX_P5  AA5 ALA B 56  ? GLY B 62  ? ALA C 55  GLY C 61  5 ? 7 
HELX_P HELX_P6  AA6 GLU B 133 ? LYS B 137 ? GLU C 132 LYS C 136 5 ? 5 
HELX_P HELX_P7  AA7 ALA B 225 ? GLY B 231 ? ALA C 224 GLY C 230 5 ? 7 
HELX_P HELX_P8  AA8 GLU B 303 ? GLY B 308 ? GLU C 302 GLY C 307 1 ? 6 
HELX_P HELX_P9  AA9 ALA C 56  ? GLY C 62  ? ALA E 55  GLY E 61  5 ? 7 
HELX_P HELX_P10 AB1 GLU C 134 ? GLY C 139 ? GLU E 133 GLY E 138 1 ? 6 
HELX_P HELX_P11 AB2 ALA C 225 ? GLY C 231 ? ALA E 224 GLY E 230 5 ? 7 
HELX_P HELX_P12 AB3 SER C 277 ? SER C 281 ? SER E 276 SER E 280 5 ? 5 
HELX_P HELX_P13 AB4 GLU C 303 ? GLY C 308 ? GLU E 302 GLY E 307 1 ? 6 
HELX_P HELX_P14 AB5 ALA D 56  ? GLY D 62  ? ALA G 55  GLY G 61  5 ? 7 
HELX_P HELX_P15 AB6 GLU D 134 ? GLY D 139 ? GLU G 133 GLY G 138 1 ? 6 
HELX_P HELX_P16 AB7 ALA D 225 ? GLY D 231 ? ALA G 224 GLY G 230 5 ? 7 
HELX_P HELX_P17 AB8 SER D 277 ? SER D 281 ? SER G 276 SER G 280 5 ? 5 
HELX_P HELX_P18 AB9 GLU D 303 ? GLY D 308 ? GLU G 302 GLY G 307 1 ? 6 
HELX_P HELX_P19 AC1 ALA E 56  ? GLY E 62  ? ALA I 55  GLY I 61  5 ? 7 
HELX_P HELX_P20 AC2 SER E 108 ? SER E 112 ? SER I 107 SER I 111 5 ? 5 
HELX_P HELX_P21 AC3 GLU E 134 ? GLY E 139 ? GLU I 133 GLY I 138 1 ? 6 
HELX_P HELX_P22 AC4 ALA E 225 ? GLY E 231 ? ALA I 224 GLY I 230 5 ? 7 
HELX_P HELX_P23 AC5 SER E 277 ? SER E 281 ? SER I 276 SER I 280 5 ? 5 
HELX_P HELX_P24 AC6 GLU E 302 ? LYS E 306 ? GLU I 301 LYS I 305 5 ? 5 
# 
_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 
disulf1   disulf ? ? A CYS 58  SG  ? ? ? 1_555 A  CYS 147 SG ? ? A CYS 57  A CYS 146 1_555 ? ? ? ? ? ? ? 2.154 ? 
disulf2   disulf ? ? A CYS 227 SG  ? ? ? 1_555 A  CYS 316 SG ? ? A CYS 226 A CYS 315 1_555 ? ? ? ? ? ? ? 2.171 ? 
disulf3   disulf ? ? B CYS 58  SG  ? ? ? 1_555 B  CYS 147 SG ? ? C CYS 57  C CYS 146 1_555 ? ? ? ? ? ? ? 2.090 ? 
disulf4   disulf ? ? B CYS 227 SG  ? ? ? 1_555 B  CYS 316 SG ? ? C CYS 226 C CYS 315 1_555 ? ? ? ? ? ? ? 2.111 ? 
disulf5   disulf ? ? C CYS 58  SG  ? ? ? 1_555 C  CYS 147 SG ? ? E CYS 57  E CYS 146 1_555 ? ? ? ? ? ? ? 2.208 ? 
disulf6   disulf ? ? C CYS 227 SG  ? ? ? 1_555 C  CYS 316 SG ? ? E CYS 226 E CYS 315 1_555 ? ? ? ? ? ? ? 2.191 ? 
disulf7   disulf ? ? D CYS 58  SG  ? ? ? 1_555 D  CYS 147 SG ? ? G CYS 57  G CYS 146 1_555 ? ? ? ? ? ? ? 2.181 ? 
disulf8   disulf ? ? D CYS 227 SG  ? ? ? 1_555 D  CYS 316 SG ? ? G CYS 226 G CYS 315 1_555 ? ? ? ? ? ? ? 2.166 ? 
disulf9   disulf ? ? E CYS 58  SG  ? ? ? 1_555 E  CYS 147 SG ? ? I CYS 57  I CYS 146 1_555 ? ? ? ? ? ? ? 2.179 ? 
disulf10  disulf ? ? E CYS 227 SG  ? ? ? 1_555 E  CYS 316 SG ? ? I CYS 226 I CYS 315 1_555 ? ? ? ? ? ? ? 2.166 ? 
metalc1   metalc ? ? A HIS 47  ND1 ? ? ? 1_555 G  CU  .   CU A ? A HIS 46  A CU  402 1_555 ? ? ? ? ? ? ? 2.037 ? 
metalc2   metalc ? ? A HIS 47  ND1 ? ? ? 1_555 G  CU  .   CU B ? A HIS 46  A CU  402 1_555 ? ? ? ? ? ? ? 2.140 ? 
metalc3   metalc ? ? A HIS 49  NE2 ? ? ? 1_555 G  CU  .   CU A ? A HIS 48  A CU  402 1_555 ? ? ? ? ? ? ? 2.016 ? 
metalc4   metalc ? ? A HIS 49  NE2 ? ? ? 1_555 G  CU  .   CU B ? A HIS 48  A CU  402 1_555 ? ? ? ? ? ? ? 2.161 ? 
metalc5   metalc ? ? A HIS 64  ND1 ? ? ? 1_555 F  ZN  .   ZN ? ? A HIS 63  A ZN  401 1_555 ? ? ? ? ? ? ? 2.120 ? 
metalc6   metalc ? ? A HIS 64  NE2 ? ? ? 1_555 G  CU  .   CU B ? A HIS 63  A CU  402 1_555 ? ? ? ? ? ? ? 2.146 ? 
metalc7   metalc ? ? A HIS 72  ND1 ? ? ? 1_555 F  ZN  .   ZN ? ? A HIS 71  A ZN  401 1_555 ? ? ? ? ? ? ? 2.134 ? 
metalc8   metalc ? ? A HIS 81  ND1 ? ? ? 1_555 F  ZN  .   ZN ? ? A HIS 80  A ZN  401 1_555 ? ? ? ? ? ? ? 2.071 ? 
metalc9   metalc ? ? A ASP 84  OD1 B ? ? 1_555 F  ZN  .   ZN ? ? A ASP 83  A ZN  401 1_555 ? ? ? ? ? ? ? 1.971 ? 
metalc10  metalc ? ? A HIS 121 NE2 ? ? ? 1_555 G  CU  .   CU A ? A HIS 120 A CU  402 1_555 ? ? ? ? ? ? ? 2.056 ? 
metalc11  metalc ? ? A HIS 121 NE2 ? ? ? 1_555 G  CU  .   CU B ? A HIS 120 A CU  402 1_555 ? ? ? ? ? ? ? 2.133 ? 
metalc12  metalc ? ? A HIS 216 ND1 ? ? ? 1_555 I  CU  .   CU A ? A HIS 215 A CU  404 1_555 ? ? ? ? ? ? ? 2.097 ? 
metalc13  metalc ? ? A HIS 216 ND1 ? ? ? 1_555 I  CU  .   CU B ? A HIS 215 A CU  404 1_555 ? ? ? ? ? ? ? 2.049 ? 
metalc14  metalc ? ? A HIS 218 NE2 ? ? ? 1_555 I  CU  .   CU A ? A HIS 217 A CU  404 1_555 ? ? ? ? ? ? ? 2.029 ? 
metalc15  metalc ? ? A HIS 233 ND1 ? ? ? 1_555 H  ZN  .   ZN ? ? A HIS 232 A ZN  403 1_555 ? ? ? ? ? ? ? 2.014 ? 
metalc16  metalc ? ? A HIS 233 NE2 ? ? ? 1_555 I  CU  .   CU B ? A HIS 232 A CU  404 1_555 ? ? ? ? ? ? ? 2.131 ? 
metalc17  metalc ? ? A HIS 241 ND1 ? ? ? 1_555 H  ZN  .   ZN ? ? A HIS 240 A ZN  403 1_555 ? ? ? ? ? ? ? 1.957 ? 
metalc18  metalc ? ? A HIS 250 ND1 ? ? ? 1_555 H  ZN  .   ZN ? ? A HIS 249 A ZN  403 1_555 ? ? ? ? ? ? ? 2.114 ? 
metalc19  metalc ? ? A SER 253 OG  A ? ? 1_555 H  ZN  .   ZN ? ? A SER 252 A ZN  403 1_555 ? ? ? ? ? ? ? 2.222 ? 
metalc20  metalc ? ? A ASP 253 OD1 B ? ? 1_555 H  ZN  .   ZN ? ? A ASP 252 A ZN  403 1_555 ? ? ? ? ? ? ? 1.974 ? 
metalc21  metalc ? ? A HIS 290 NE2 ? ? ? 1_555 I  CU  .   CU A ? A HIS 289 A CU  404 1_555 ? ? ? ? ? ? ? 2.073 ? 
metalc22  metalc ? ? A HIS 290 NE2 ? ? ? 1_555 I  CU  .   CU B ? A HIS 289 A CU  404 1_555 ? ? ? ? ? ? ? 2.148 ? 
metalc23  metalc ? ? B HIS 47  ND1 ? ? ? 1_555 K  CU  .   CU ? ? C HIS 46  C CU  402 1_555 ? ? ? ? ? ? ? 2.103 ? 
metalc24  metalc ? ? B HIS 49  NE2 ? ? ? 1_555 K  CU  .   CU ? ? C HIS 48  C CU  402 1_555 ? ? ? ? ? ? ? 2.104 ? 
metalc25  metalc ? ? B HIS 64  ND1 ? ? ? 1_555 J  ZN  .   ZN ? ? C HIS 63  C ZN  401 1_555 ? ? ? ? ? ? ? 1.961 ? 
metalc26  metalc ? ? B HIS 72  ND1 ? ? ? 1_555 J  ZN  .   ZN ? ? C HIS 71  C ZN  401 1_555 ? ? ? ? ? ? ? 2.083 ? 
metalc27  metalc ? ? B HIS 81  ND1 ? ? ? 1_555 J  ZN  .   ZN ? ? C HIS 80  C ZN  401 1_555 ? ? ? ? ? ? ? 2.107 ? 
metalc28  metalc ? ? B SER 84  OG  A ? ? 1_555 J  ZN  .   ZN ? ? C SER 83  C ZN  401 1_555 ? ? ? ? ? ? ? 2.233 ? 
metalc29  metalc ? ? B ASP 84  OD1 B ? ? 1_555 J  ZN  .   ZN ? ? C ASP 83  C ZN  401 1_555 ? ? ? ? ? ? ? 1.971 ? 
metalc30  metalc ? ? B HIS 121 NE2 ? ? ? 1_555 K  CU  .   CU ? ? C HIS 120 C CU  402 1_555 ? ? ? ? ? ? ? 2.046 ? 
metalc31  metalc ? ? B HIS 216 ND1 ? ? ? 1_555 M  CU  .   CU A ? C HIS 215 C CU  404 1_555 ? ? ? ? ? ? ? 2.097 ? 
metalc32  metalc ? ? B HIS 216 ND1 ? ? ? 1_555 M  CU  .   CU B ? C HIS 215 C CU  404 1_555 ? ? ? ? ? ? ? 2.107 ? 
metalc33  metalc ? ? B HIS 218 NE2 ? ? ? 1_555 M  CU  .   CU A ? C HIS 217 C CU  404 1_555 ? ? ? ? ? ? ? 2.012 ? 
metalc34  metalc ? ? B HIS 218 NE2 ? ? ? 1_555 M  CU  .   CU B ? C HIS 217 C CU  404 1_555 ? ? ? ? ? ? ? 2.175 ? 
metalc35  metalc ? ? B HIS 233 ND1 ? ? ? 1_555 L  ZN  .   ZN ? ? C HIS 232 C ZN  403 1_555 ? ? ? ? ? ? ? 2.046 ? 
metalc36  metalc ? ? B HIS 233 NE2 ? ? ? 1_555 M  CU  .   CU B ? C HIS 232 C CU  404 1_555 ? ? ? ? ? ? ? 2.121 ? 
metalc37  metalc ? ? B HIS 241 ND1 ? ? ? 1_555 L  ZN  .   ZN ? ? C HIS 240 C ZN  403 1_555 ? ? ? ? ? ? ? 2.141 ? 
metalc38  metalc ? ? B HIS 250 ND1 ? ? ? 1_555 L  ZN  .   ZN ? ? C HIS 249 C ZN  403 1_555 ? ? ? ? ? ? ? 2.129 ? 
metalc39  metalc ? ? B SER 253 OG  A ? ? 1_555 L  ZN  .   ZN ? ? C SER 252 C ZN  403 1_555 ? ? ? ? ? ? ? 2.214 ? 
metalc40  metalc ? ? B ASP 253 OD1 B ? ? 1_555 L  ZN  .   ZN ? ? C ASP 252 C ZN  403 1_555 ? ? ? ? ? ? ? 1.977 ? 
metalc41  metalc ? ? B HIS 290 NE2 ? ? ? 1_555 M  CU  .   CU A ? C HIS 289 C CU  404 1_555 ? ? ? ? ? ? ? 1.996 ? 
metalc42  metalc ? ? B HIS 290 NE2 ? ? ? 1_555 M  CU  .   CU B ? C HIS 289 C CU  404 1_555 ? ? ? ? ? ? ? 2.134 ? 
metalc43  metalc ? ? C HIS 47  ND1 ? ? ? 1_555 O  CU  .   CU A ? E HIS 46  E CU  402 1_555 ? ? ? ? ? ? ? 2.055 ? 
metalc44  metalc ? ? C HIS 47  ND1 ? ? ? 1_555 O  CU  .   CU B ? E HIS 46  E CU  402 1_555 ? ? ? ? ? ? ? 2.107 ? 
metalc45  metalc ? ? C HIS 49  NE2 ? ? ? 1_555 O  CU  .   CU A ? E HIS 48  E CU  402 1_555 ? ? ? ? ? ? ? 2.039 ? 
metalc46  metalc ? ? C HIS 49  NE2 ? ? ? 1_555 O  CU  .   CU B ? E HIS 48  E CU  402 1_555 ? ? ? ? ? ? ? 2.154 ? 
metalc47  metalc ? ? C HIS 64  ND1 ? ? ? 1_555 N  ZN  .   ZN ? ? E HIS 63  E ZN  401 1_555 ? ? ? ? ? ? ? 2.041 ? 
metalc48  metalc ? ? C HIS 64  NE2 ? ? ? 1_555 O  CU  .   CU B ? E HIS 63  E CU  402 1_555 ? ? ? ? ? ? ? 2.147 ? 
metalc49  metalc ? ? C HIS 72  ND1 ? ? ? 1_555 N  ZN  .   ZN ? ? E HIS 71  E ZN  401 1_555 ? ? ? ? ? ? ? 2.151 ? 
metalc50  metalc ? ? C HIS 81  ND1 ? ? ? 1_555 N  ZN  .   ZN ? ? E HIS 80  E ZN  401 1_555 ? ? ? ? ? ? ? 2.049 ? 
metalc51  metalc ? ? C SER 84  OG  A ? ? 1_555 N  ZN  .   ZN ? ? E SER 83  E ZN  401 1_555 ? ? ? ? ? ? ? 2.226 ? 
metalc52  metalc ? ? C ASP 84  OD1 B ? ? 1_555 N  ZN  .   ZN ? ? E ASP 83  E ZN  401 1_555 ? ? ? ? ? ? ? 1.971 ? 
metalc53  metalc ? ? C HIS 121 NE2 ? ? ? 1_555 O  CU  .   CU A ? E HIS 120 E CU  402 1_555 ? ? ? ? ? ? ? 2.030 ? 
metalc54  metalc ? ? C HIS 121 NE2 ? ? ? 1_555 O  CU  .   CU B ? E HIS 120 E CU  402 1_555 ? ? ? ? ? ? ? 2.173 ? 
metalc55  metalc ? ? C HIS 216 ND1 ? ? ? 1_555 Q  CU  .   CU A ? E HIS 215 E CU  404 1_555 ? ? ? ? ? ? ? 2.122 ? 
metalc56  metalc ? ? C HIS 216 ND1 ? ? ? 1_555 Q  CU  .   CU B ? E HIS 215 E CU  404 1_555 ? ? ? ? ? ? ? 2.081 ? 
metalc57  metalc ? ? C HIS 218 NE2 ? ? ? 1_555 Q  CU  .   CU A ? E HIS 217 E CU  404 1_555 ? ? ? ? ? ? ? 1.978 ? 
metalc58  metalc ? ? C HIS 218 NE2 ? ? ? 1_555 Q  CU  .   CU B ? E HIS 217 E CU  404 1_555 ? ? ? ? ? ? ? 2.226 ? 
metalc59  metalc ? ? C HIS 233 ND1 ? ? ? 1_555 P  ZN  .   ZN ? ? E HIS 232 E ZN  403 1_555 ? ? ? ? ? ? ? 1.976 ? 
metalc60  metalc ? ? C HIS 233 NE2 ? ? ? 1_555 Q  CU  .   CU B ? E HIS 232 E CU  404 1_555 ? ? ? ? ? ? ? 2.181 ? 
metalc61  metalc ? ? C HIS 241 ND1 ? ? ? 1_555 P  ZN  .   ZN ? ? E HIS 240 E ZN  403 1_555 ? ? ? ? ? ? ? 2.099 ? 
metalc62  metalc ? ? C HIS 250 ND1 ? ? ? 1_555 P  ZN  .   ZN ? ? E HIS 249 E ZN  403 1_555 ? ? ? ? ? ? ? 2.087 ? 
metalc63  metalc ? ? C SER 253 OG  A ? ? 1_555 P  ZN  .   ZN ? ? E SER 252 E ZN  403 1_555 ? ? ? ? ? ? ? 2.232 ? 
metalc64  metalc ? ? C ASP 253 OD1 B ? ? 1_555 P  ZN  .   ZN ? ? E ASP 252 E ZN  403 1_555 ? ? ? ? ? ? ? 1.959 ? 
metalc65  metalc ? ? C HIS 290 NE2 ? ? ? 1_555 Q  CU  .   CU A ? E HIS 289 E CU  404 1_555 ? ? ? ? ? ? ? 1.998 ? 
metalc66  metalc ? ? C HIS 290 NE2 ? ? ? 1_555 Q  CU  .   CU B ? E HIS 289 E CU  404 1_555 ? ? ? ? ? ? ? 2.168 ? 
metalc67  metalc ? ? D HIS 47  ND1 ? ? ? 1_555 T  CU  .   CU A ? G HIS 46  G CU  402 1_555 ? ? ? ? ? ? ? 2.113 ? 
metalc68  metalc ? ? D HIS 47  ND1 ? ? ? 1_555 T  CU  .   CU B ? G HIS 46  G CU  402 1_555 ? ? ? ? ? ? ? 2.077 ? 
metalc69  metalc ? ? D HIS 49  NE2 ? ? ? 1_555 T  CU  .   CU A ? G HIS 48  G CU  402 1_555 ? ? ? ? ? ? ? 1.983 ? 
metalc70  metalc ? ? D HIS 49  NE2 ? ? ? 1_555 T  CU  .   CU B ? G HIS 48  G CU  402 1_555 ? ? ? ? ? ? ? 2.187 ? 
metalc71  metalc ? ? D HIS 64  ND1 ? ? ? 1_555 S  ZN  .   ZN ? ? G HIS 63  G ZN  401 1_555 ? ? ? ? ? ? ? 1.965 ? 
metalc72  metalc ? ? D HIS 64  NE2 ? ? ? 1_555 T  CU  .   CU B ? G HIS 63  G CU  402 1_555 ? ? ? ? ? ? ? 2.161 ? 
metalc73  metalc ? ? D HIS 72  ND1 ? ? ? 1_555 S  ZN  .   ZN ? ? G HIS 71  G ZN  401 1_555 ? ? ? ? ? ? ? 2.137 ? 
metalc74  metalc ? ? D HIS 81  ND1 ? ? ? 1_555 S  ZN  .   ZN ? ? G HIS 80  G ZN  401 1_555 ? ? ? ? ? ? ? 2.030 ? 
metalc75  metalc ? ? D ASP 84  OD1 B ? ? 1_555 S  ZN  .   ZN ? ? G ASP 83  G ZN  401 1_555 ? ? ? ? ? ? ? 1.970 ? 
metalc76  metalc ? ? D HIS 121 NE2 ? ? ? 1_555 T  CU  .   CU A ? G HIS 120 G CU  402 1_555 ? ? ? ? ? ? ? 1.991 ? 
metalc77  metalc ? ? D HIS 121 NE2 ? ? ? 1_555 T  CU  .   CU B ? G HIS 120 G CU  402 1_555 ? ? ? ? ? ? ? 2.183 ? 
metalc78  metalc ? ? D HIS 216 ND1 ? ? ? 1_555 V  CU  .   CU A ? G HIS 215 G CU  404 1_555 ? ? ? ? ? ? ? 2.091 ? 
metalc79  metalc ? ? D HIS 216 ND1 ? ? ? 1_555 V  CU  .   CU B ? G HIS 215 G CU  404 1_555 ? ? ? ? ? ? ? 2.063 ? 
metalc80  metalc ? ? D HIS 218 NE2 ? ? ? 1_555 V  CU  .   CU A ? G HIS 217 G CU  404 1_555 ? ? ? ? ? ? ? 2.046 ? 
metalc81  metalc ? ? D HIS 218 NE2 ? ? ? 1_555 V  CU  .   CU B ? G HIS 217 G CU  404 1_555 ? ? ? ? ? ? ? 2.178 ? 
metalc82  metalc ? ? D HIS 233 ND1 ? ? ? 1_555 U  ZN  .   ZN ? ? G HIS 232 G ZN  403 1_555 ? ? ? ? ? ? ? 1.938 ? 
metalc83  metalc ? ? D HIS 233 NE2 ? ? ? 1_555 V  CU  .   CU B ? G HIS 232 G CU  404 1_555 ? ? ? ? ? ? ? 2.155 ? 
metalc84  metalc ? ? D HIS 241 ND1 ? ? ? 1_555 U  ZN  .   ZN ? ? G HIS 240 G ZN  403 1_555 ? ? ? ? ? ? ? 2.154 ? 
metalc85  metalc ? ? D HIS 250 ND1 ? ? ? 1_555 U  ZN  .   ZN ? ? G HIS 249 G ZN  403 1_555 ? ? ? ? ? ? ? 2.045 ? 
metalc86  metalc ? ? D ASP 253 OD1 B ? ? 1_555 U  ZN  .   ZN ? ? G ASP 252 G ZN  403 1_555 ? ? ? ? ? ? ? 1.985 ? 
metalc87  metalc ? ? D HIS 290 NE2 ? ? ? 1_555 V  CU  .   CU A ? G HIS 289 G CU  404 1_555 ? ? ? ? ? ? ? 2.008 ? 
metalc88  metalc ? ? D HIS 290 NE2 ? ? ? 1_555 V  CU  .   CU B ? G HIS 289 G CU  404 1_555 ? ? ? ? ? ? ? 2.175 ? 
metalc89  metalc ? ? E HIS 47  ND1 ? ? ? 1_555 X  CU  .   CU A ? I HIS 46  I CU  402 1_555 ? ? ? ? ? ? ? 2.110 ? 
metalc90  metalc ? ? E HIS 47  ND1 ? ? ? 1_555 X  CU  .   CU B ? I HIS 46  I CU  402 1_555 ? ? ? ? ? ? ? 2.064 ? 
metalc91  metalc ? ? E HIS 49  NE2 ? ? ? 1_555 X  CU  .   CU A ? I HIS 48  I CU  402 1_555 ? ? ? ? ? ? ? 1.979 ? 
metalc92  metalc ? ? E HIS 49  NE2 ? ? ? 1_555 X  CU  .   CU B ? I HIS 48  I CU  402 1_555 ? ? ? ? ? ? ? 2.209 ? 
metalc93  metalc ? ? E HIS 64  ND1 ? ? ? 1_555 W  ZN  .   ZN ? ? I HIS 63  I ZN  401 1_555 ? ? ? ? ? ? ? 1.931 ? 
metalc94  metalc ? ? E HIS 64  NE2 ? ? ? 1_555 X  CU  .   CU B ? I HIS 63  I CU  402 1_555 ? ? ? ? ? ? ? 2.204 ? 
metalc95  metalc ? ? E HIS 72  ND1 ? ? ? 1_555 W  ZN  .   ZN ? ? I HIS 71  I ZN  401 1_555 ? ? ? ? ? ? ? 2.060 ? 
metalc96  metalc ? ? E HIS 81  ND1 ? ? ? 1_555 W  ZN  .   ZN ? ? I HIS 80  I ZN  401 1_555 ? ? ? ? ? ? ? 2.114 ? 
metalc97  metalc ? ? E SER 84  OG  A ? ? 1_555 W  ZN  .   ZN ? ? I SER 83  I ZN  401 1_555 ? ? ? ? ? ? ? 2.242 ? 
metalc98  metalc ? ? E ASP 84  OD1 B ? ? 1_555 W  ZN  .   ZN ? ? I ASP 83  I ZN  401 1_555 ? ? ? ? ? ? ? 1.990 ? 
metalc99  metalc ? ? E HIS 121 NE2 ? ? ? 1_555 X  CU  .   CU A ? I HIS 120 I CU  402 1_555 ? ? ? ? ? ? ? 1.999 ? 
metalc100 metalc ? ? E HIS 121 NE2 ? ? ? 1_555 X  CU  .   CU B ? I HIS 120 I CU  402 1_555 ? ? ? ? ? ? ? 2.207 ? 
metalc101 metalc ? ? E HIS 216 ND1 ? ? ? 1_555 Z  CU  .   CU A ? I HIS 215 I CU  404 1_555 ? ? ? ? ? ? ? 2.039 ? 
metalc102 metalc ? ? E HIS 216 ND1 ? ? ? 1_555 Z  CU  .   CU B ? I HIS 215 I CU  404 1_555 ? ? ? ? ? ? ? 2.136 ? 
metalc103 metalc ? ? E HIS 218 NE2 ? ? ? 1_555 Z  CU  .   CU A ? I HIS 217 I CU  404 1_555 ? ? ? ? ? ? ? 2.050 ? 
metalc104 metalc ? ? E HIS 218 NE2 ? ? ? 1_555 Z  CU  .   CU B ? I HIS 217 I CU  404 1_555 ? ? ? ? ? ? ? 2.172 ? 
metalc105 metalc ? ? E HIS 233 ND1 ? ? ? 1_555 Y  ZN  .   ZN ? ? I HIS 232 I ZN  403 1_555 ? ? ? ? ? ? ? 2.180 ? 
metalc106 metalc ? ? E HIS 233 NE2 ? ? ? 1_555 Z  CU  .   CU B ? I HIS 232 I CU  404 1_555 ? ? ? ? ? ? ? 2.154 ? 
metalc107 metalc ? ? E HIS 241 ND1 ? ? ? 1_555 Y  ZN  .   ZN ? ? I HIS 240 I ZN  403 1_555 ? ? ? ? ? ? ? 2.169 ? 
metalc108 metalc ? ? E HIS 250 ND1 ? ? ? 1_555 Y  ZN  .   ZN ? ? I HIS 249 I ZN  403 1_555 ? ? ? ? ? ? ? 2.131 ? 
metalc109 metalc ? ? E SER 253 OG  A ? ? 1_555 Y  ZN  .   ZN ? ? I SER 252 I ZN  403 1_555 ? ? ? ? ? ? ? 2.211 ? 
metalc110 metalc ? ? E ASP 253 OD1 B ? ? 1_555 Y  ZN  .   ZN ? ? I ASP 252 I ZN  403 1_555 ? ? ? ? ? ? ? 1.969 ? 
metalc111 metalc ? ? E HIS 290 NE2 ? ? ? 1_555 Z  CU  .   CU A ? I HIS 289 I CU  404 1_555 ? ? ? ? ? ? ? 2.043 ? 
metalc112 metalc ? ? E HIS 290 NE2 ? ? ? 1_555 Z  CU  .   CU B ? I HIS 289 I CU  404 1_555 ? ? ? ? ? ? ? 2.152 ? 
metalc113 metalc ? ? F ZN  .   ZN  ? ? ? 1_555 AA HOH .   O  ? ? A ZN  401 A HOH 501 1_555 ? ? ? ? ? ? ? 2.227 ? 
metalc114 metalc ? ? I CU  .   CU  B ? ? 1_555 AA HOH .   O  ? ? A CU  404 A HOH 567 1_555 ? ? ? ? ? ? ? 2.297 ? 
metalc115 metalc ? ? I CU  .   CU  B ? ? 1_555 AA HOH .   O  ? ? A CU  404 A HOH 619 1_555 ? ? ? ? ? ? ? 2.452 ? 
metalc116 metalc ? ? M CU  .   CU  B ? ? 1_555 BA HOH .   O  ? ? C CU  404 C HOH 565 1_555 ? ? ? ? ? ? ? 2.661 ? 
metalc117 metalc ? ? O CU  .   CU  B ? ? 1_555 CA HOH .   O  ? ? E CU  402 E HOH 623 1_555 ? ? ? ? ? ? ? 2.528 ? 
metalc118 metalc ? ? Q CU  .   CU  B ? ? 1_555 CA HOH .   O  ? ? E CU  404 E HOH 575 1_555 ? ? ? ? ? ? ? 2.389 ? 
metalc119 metalc ? ? Q CU  .   CU  B ? ? 1_555 CA HOH .   O  ? ? E CU  404 E HOH 662 1_555 ? ? ? ? ? ? ? 2.676 ? 
metalc120 metalc ? ? T CU  .   CU  B ? ? 1_555 DA HOH .   O  ? ? G CU  402 G HOH 595 1_555 ? ? ? ? ? ? ? 2.599 ? 
metalc121 metalc ? ? V CU  .   CU  B ? ? 1_555 DA HOH .   O  ? ? G CU  404 G HOH 565 1_555 ? ? ? ? ? ? ? 2.298 ? 
metalc122 metalc ? ? X CU  .   CU  B ? ? 1_555 EA HOH .   O  ? ? I CU  402 I HOH 605 1_555 ? ? ? ? ? ? ? 2.457 ? 
metalc123 metalc ? ? Z CU  .   CU  B ? ? 1_555 EA HOH .   O  ? ? I CU  404 I HOH 543 1_555 ? ? ? ? ? ? ? 2.423 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 4 ? 
AA3 ? 5 ? 
AA4 ? 4 ? 
AA5 ? 5 ? 
AA6 ? 4 ? 
AA7 ? 5 ? 
AA8 ? 4 ? 
AA9 ? 5 ? 
AB1 ? 4 ? 
AB2 ? 5 ? 
AB3 ? 4 ? 
AB4 ? 5 ? 
AB5 ? 4 ? 
AB6 ? 5 ? 
AB7 ? 4 ? 
AB8 ? 5 ? 
AB9 ? 4 ? 
AC1 ? 5 ? 
AC2 ? 4 ? 
# 
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 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AA9 4 5 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB2 4 5 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB4 4 5 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB6 2 3 ? anti-parallel 
AB6 3 4 ? anti-parallel 
AB6 4 5 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB8 2 3 ? anti-parallel 
AB8 3 4 ? anti-parallel 
AB8 4 5 ? anti-parallel 
AB9 1 2 ? anti-parallel 
AB9 2 3 ? anti-parallel 
AB9 3 4 ? anti-parallel 
AC1 1 2 ? anti-parallel 
AC1 2 3 ? anti-parallel 
AC1 3 4 ? anti-parallel 
AC1 4 5 ? anti-parallel 
AC2 1 2 ? anti-parallel 
AC2 2 3 ? anti-parallel 
AC2 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ALA A 96  ? ASP A 102 ? ALA A 95  ASP A 101 
AA1 2 VAL A 30  ? LYS A 37  ? VAL A 29  LYS A 36  
AA1 3 GLN A 16  ? GLU A 22  ? GLN A 15  GLU A 21  
AA1 4 LYS A 4   ? LEU A 9   ? LYS A 3   LEU A 8   
AA1 5 GLY A 151 ? ILE A 152 ? GLY A 150 ILE A 151 
AA2 1 SER A 84  ? ALA A 90  ? SER A 83  ALA A 89  
AA2 2 GLY A 42  ? HIS A 49  ? GLY A 41  HIS A 48  
AA2 3 THR A 117 ? HIS A 121 ? THR A 116 HIS A 120 
AA2 4 ARG A 144 ? VAL A 149 ? ARG A 143 VAL A 148 
AA3 1 ALA A 265 ? ASP A 271 ? ALA A 264 ASP A 270 
AA3 2 VAL A 199 ? LYS A 206 ? VAL A 198 LYS A 205 
AA3 3 GLN A 185 ? GLU A 191 ? GLN A 184 GLU A 190 
AA3 4 LYS A 173 ? LYS A 179 ? LYS A 172 LYS A 178 
AA3 5 GLY A 320 ? ILE A 321 ? GLY A 319 ILE A 320 
AA4 1 SER A 253 ? ALA A 259 ? SER A 252 ALA A 258 
AA4 2 GLY A 211 ? HIS A 218 ? GLY A 210 HIS A 217 
AA4 3 THR A 286 ? HIS A 290 ? THR A 285 HIS A 289 
AA4 4 ARG A 313 ? VAL A 318 ? ARG A 312 VAL A 317 
AA5 1 ALA B 96  ? ASP B 102 ? ALA C 95  ASP C 101 
AA5 2 VAL B 30  ? LYS B 37  ? VAL C 29  LYS C 36  
AA5 3 GLN B 16  ? GLU B 22  ? GLN C 15  GLU C 21  
AA5 4 LYS B 4   ? LEU B 9   ? LYS C 3   LEU C 8   
AA5 5 GLY B 151 ? ILE B 152 ? GLY C 150 ILE C 151 
AA6 1 SER B 84  ? ALA B 90  ? SER C 83  ALA C 89  
AA6 2 GLY B 42  ? HIS B 49  ? GLY C 41  HIS C 48  
AA6 3 THR B 117 ? HIS B 121 ? THR C 116 HIS C 120 
AA6 4 ARG B 144 ? VAL B 149 ? ARG C 143 VAL C 148 
AA7 1 ALA B 265 ? ASP B 271 ? ALA C 264 ASP C 270 
AA7 2 VAL B 199 ? LYS B 206 ? VAL C 198 LYS C 205 
AA7 3 GLN B 185 ? GLN B 192 ? GLN C 184 GLN C 191 
AA7 4 LYS B 173 ? LYS B 179 ? LYS C 172 LYS C 178 
AA7 5 GLY B 320 ? ALA B 322 ? GLY C 319 ALA C 321 
AA8 1 SER B 253 ? ALA B 259 ? SER C 252 ALA C 258 
AA8 2 GLY B 211 ? HIS B 218 ? GLY C 210 HIS C 217 
AA8 3 THR B 286 ? HIS B 290 ? THR C 285 HIS C 289 
AA8 4 ARG B 313 ? VAL B 318 ? ARG C 312 VAL C 317 
AA9 1 ALA C 96  ? ASP C 102 ? ALA E 95  ASP E 101 
AA9 2 VAL C 30  ? LYS C 37  ? VAL E 29  LYS E 36  
AA9 3 GLN C 16  ? GLN C 23  ? GLN E 15  GLN E 22  
AA9 4 LYS C 4   ? LEU C 9   ? LYS E 3   LEU E 8   
AA9 5 GLY C 151 ? ILE C 152 ? GLY E 150 ILE E 151 
AB1 1 SER C 84  ? ALA C 90  ? SER E 83  ALA E 89  
AB1 2 GLY C 42  ? HIS C 49  ? GLY E 41  HIS E 48  
AB1 3 THR C 117 ? HIS C 121 ? THR E 116 HIS E 120 
AB1 4 ARG C 144 ? VAL C 149 ? ARG E 143 VAL E 148 
AB2 1 ALA C 265 ? ASP C 271 ? ALA E 264 ASP E 270 
AB2 2 VAL C 199 ? LYS C 206 ? VAL E 198 LYS E 205 
AB2 3 GLN C 185 ? GLU C 191 ? GLN E 184 GLU E 190 
AB2 4 LYS C 173 ? LEU C 178 ? LYS E 172 LEU E 177 
AB2 5 GLY C 320 ? ILE C 321 ? GLY E 319 ILE E 320 
AB3 1 SER C 253 ? ALA C 259 ? SER E 252 ALA E 258 
AB3 2 GLY C 211 ? HIS C 218 ? GLY E 210 HIS E 217 
AB3 3 THR C 286 ? HIS C 290 ? THR E 285 HIS E 289 
AB3 4 ARG C 313 ? VAL C 318 ? ARG E 312 VAL E 317 
AB4 1 ALA D 96  ? ASP D 102 ? ALA G 95  ASP G 101 
AB4 2 VAL D 30  ? LYS D 37  ? VAL G 29  LYS G 36  
AB4 3 GLN D 16  ? GLU D 22  ? GLN G 15  GLU G 21  
AB4 4 LYS D 4   ? LEU D 9   ? LYS G 3   LEU G 8   
AB4 5 GLY D 151 ? ILE D 152 ? GLY G 150 ILE G 151 
AB5 1 SER D 84  ? ALA D 90  ? SER G 83  ALA G 89  
AB5 2 GLY D 42  ? HIS D 49  ? GLY G 41  HIS G 48  
AB5 3 THR D 117 ? HIS D 121 ? THR G 116 HIS G 120 
AB5 4 ARG D 144 ? VAL D 149 ? ARG G 143 VAL G 148 
AB6 1 ALA D 265 ? ASP D 271 ? ALA G 264 ASP G 270 
AB6 2 VAL D 199 ? LYS D 206 ? VAL G 198 LYS G 205 
AB6 3 GLN D 185 ? GLU D 191 ? GLN G 184 GLU G 190 
AB6 4 LYS D 173 ? LEU D 178 ? LYS G 172 LEU G 177 
AB6 5 GLY D 320 ? ILE D 321 ? GLY G 319 ILE G 320 
AB7 1 SER D 253 ? ALA D 259 ? SER G 252 ALA G 258 
AB7 2 GLY D 211 ? HIS D 218 ? GLY G 210 HIS G 217 
AB7 3 THR D 286 ? HIS D 290 ? THR G 285 HIS G 289 
AB7 4 ARG D 313 ? VAL D 318 ? ARG G 312 VAL G 317 
AB8 1 ALA E 96  ? ASP E 102 ? ALA I 95  ASP I 101 
AB8 2 VAL E 30  ? LYS E 37  ? VAL I 29  LYS I 36  
AB8 3 GLN E 16  ? GLU E 22  ? GLN I 15  GLU I 21  
AB8 4 LYS E 4   ? LEU E 9   ? LYS I 3   LEU I 8   
AB8 5 GLY E 151 ? ILE E 152 ? GLY I 150 ILE I 151 
AB9 1 SER E 84  ? ALA E 90  ? SER I 83  ALA I 89  
AB9 2 GLY E 42  ? HIS E 49  ? GLY I 41  HIS I 48  
AB9 3 THR E 117 ? HIS E 121 ? THR I 116 HIS I 120 
AB9 4 ARG E 144 ? VAL E 149 ? ARG I 143 VAL I 148 
AC1 1 ALA E 265 ? ASP E 271 ? ALA I 264 ASP I 270 
AC1 2 VAL E 199 ? LYS E 206 ? VAL I 198 LYS I 205 
AC1 3 GLN E 185 ? GLU E 191 ? GLN I 184 GLU I 190 
AC1 4 LYS E 173 ? LEU E 178 ? LYS I 172 LEU I 177 
AC1 5 GLY E 320 ? ILE E 321 ? GLY I 319 ILE I 320 
AC2 1 SER E 253 ? ALA E 259 ? SER I 252 ALA I 258 
AC2 2 GLY E 211 ? HIS E 218 ? GLY I 210 HIS I 217 
AC2 3 THR E 286 ? HIS E 290 ? THR I 285 HIS I 289 
AC2 4 ARG E 313 ? VAL E 318 ? ARG I 312 VAL I 317 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ASP A 102 ? O ASP A 101 N VAL A 30  ? N VAL A 29  
AA1 2 3 O TRP A 33  ? O TRP A 32  N ASN A 20  ? N ASN A 19  
AA1 3 4 O GLY A 17  ? O GLY A 16  N LEU A 9   ? N LEU A 8   
AA1 4 5 N VAL A 6   ? N VAL A 5   O GLY A 151 ? O GLY A 150 
AA2 1 2 O ALA A 90  ? O ALA A 89  N GLY A 42  ? N GLY A 41  
AA2 2 3 N HIS A 49  ? N HIS A 48  O THR A 117 ? O THR A 116 
AA2 3 4 N VAL A 120 ? N VAL A 119 O ALA A 146 ? O ALA A 145 
AA3 1 2 O ILE A 269 ? O ILE A 268 N VAL A 201 ? N VAL A 200 
AA3 2 3 O TRP A 202 ? O TRP A 201 N ASN A 189 ? N ASN A 188 
AA3 3 4 O PHE A 190 ? O PHE A 189 N ALA A 174 ? N ALA A 173 
AA3 4 5 N VAL A 175 ? N VAL A 174 O GLY A 320 ? O GLY A 319 
AA4 1 2 O ALA A 259 ? O ALA A 258 N GLY A 211 ? N GLY A 210 
AA4 2 3 N HIS A 218 ? N HIS A 217 O THR A 286 ? O THR A 285 
AA4 3 4 N LEU A 287 ? N LEU A 286 O GLY A 317 ? O GLY A 316 
AA5 1 2 O ASP B 102 ? O ASP C 101 N VAL B 30  ? N VAL C 29  
AA5 2 3 O TRP B 33  ? O TRP C 32  N ASN B 20  ? N ASN C 19  
AA5 3 4 O PHE B 21  ? O PHE C 20  N ALA B 5   ? N ALA C 4   
AA5 4 5 N VAL B 6   ? N VAL C 5   O GLY B 151 ? O GLY C 150 
AA6 1 2 O ALA B 90  ? O ALA C 89  N GLY B 42  ? N GLY C 41  
AA6 2 3 N GLY B 45  ? N GLY C 44  O HIS B 121 ? O HIS C 120 
AA6 3 4 N LEU B 118 ? N LEU C 117 O GLY B 148 ? O GLY C 147 
AA7 1 2 O ASP B 271 ? O ASP C 270 N VAL B 199 ? N VAL C 198 
AA7 2 3 O TRP B 202 ? O TRP C 201 N ASN B 189 ? N ASN C 188 
AA7 3 4 O PHE B 190 ? O PHE C 189 N ALA B 174 ? N ALA C 173 
AA7 4 5 N VAL B 175 ? N VAL C 174 O GLY B 320 ? O GLY C 319 
AA8 1 2 O ALA B 259 ? O ALA C 258 N GLY B 211 ? N GLY C 210 
AA8 2 3 N HIS B 218 ? N HIS C 217 O THR B 286 ? O THR C 285 
AA8 3 4 N LEU B 287 ? N LEU C 286 O GLY B 317 ? O GLY C 316 
AA9 1 2 O ALA C 96  ? O ALA E 95  N ILE C 36  ? N ILE E 35  
AA9 2 3 O TRP C 33  ? O TRP E 32  N ASN C 20  ? N ASN E 19  
AA9 3 4 O GLY C 17  ? O GLY E 16  N LEU C 9   ? N LEU E 8   
AA9 4 5 N VAL C 6   ? N VAL E 5   O GLY C 151 ? O GLY E 150 
AB1 1 2 O ALA C 90  ? O ALA E 89  N GLY C 42  ? N GLY E 41  
AB1 2 3 N HIS C 49  ? N HIS E 48  O THR C 117 ? O THR E 116 
AB1 3 4 N VAL C 120 ? N VAL E 119 O ALA C 146 ? O ALA E 145 
AB2 1 2 O ASP C 271 ? O ASP E 270 N VAL C 199 ? N VAL E 198 
AB2 2 3 O TRP C 202 ? O TRP E 201 N ASN C 189 ? N ASN E 188 
AB2 3 4 O ILE C 188 ? O ILE E 187 N CYS C 176 ? N CYS E 175 
AB2 4 5 N VAL C 175 ? N VAL E 174 O GLY C 320 ? O GLY E 319 
AB3 1 2 O VAL C 257 ? O VAL E 256 N HIS C 213 ? N HIS E 212 
AB3 2 3 N HIS C 218 ? N HIS E 217 O THR C 286 ? O THR E 285 
AB3 3 4 N LEU C 287 ? N LEU E 286 O GLY C 317 ? O GLY E 316 
AB4 1 2 O ILE D 100 ? O ILE G 99  N VAL D 32  ? N VAL G 31  
AB4 2 3 O TRP D 33  ? O TRP G 32  N ASN D 20  ? N ASN G 19  
AB4 3 4 O GLY D 17  ? O GLY G 16  N LEU D 9   ? N LEU G 8   
AB4 4 5 N VAL D 6   ? N VAL G 5   O GLY D 151 ? O GLY G 150 
AB5 1 2 O ALA D 90  ? O ALA G 89  N GLY D 42  ? N GLY G 41  
AB5 2 3 N HIS D 49  ? N HIS G 48  O THR D 117 ? O THR G 116 
AB5 3 4 N VAL D 120 ? N VAL G 119 O ALA D 146 ? O ALA G 145 
AB6 1 2 O ASP D 271 ? O ASP G 270 N VAL D 199 ? N VAL G 198 
AB6 2 3 O TRP D 202 ? O TRP G 201 N ASN D 189 ? N ASN G 188 
AB6 3 4 O ILE D 188 ? O ILE G 187 N CYS D 176 ? N CYS G 175 
AB6 4 5 N VAL D 175 ? N VAL G 174 O GLY D 320 ? O GLY G 319 
AB7 1 2 O ALA D 259 ? O ALA G 258 N GLY D 211 ? N GLY G 210 
AB7 2 3 N HIS D 218 ? N HIS G 217 O THR D 286 ? O THR G 285 
AB7 3 4 N LEU D 287 ? N LEU G 286 O GLY D 317 ? O GLY G 316 
AB8 1 2 O ALA E 96  ? O ALA I 95  N ILE E 36  ? N ILE I 35  
AB8 2 3 O TRP E 33  ? O TRP I 32  N ASN E 20  ? N ASN I 19  
AB8 3 4 O GLY E 17  ? O GLY I 16  N LEU E 9   ? N LEU I 8   
AB8 4 5 N VAL E 6   ? N VAL I 5   O GLY E 151 ? O GLY I 150 
AB9 1 2 O ALA E 90  ? O ALA I 89  N GLY E 42  ? N GLY I 41  
AB9 2 3 N HIS E 49  ? N HIS I 48  O THR E 117 ? O THR I 116 
AB9 3 4 N VAL E 120 ? N VAL I 119 O ALA E 146 ? O ALA I 145 
AC1 1 2 O ASP E 271 ? O ASP I 270 N VAL E 199 ? N VAL I 198 
AC1 2 3 O TRP E 202 ? O TRP I 201 N ASN E 189 ? N ASN I 188 
AC1 3 4 O ILE E 188 ? O ILE I 187 N CYS E 176 ? N CYS I 175 
AC1 4 5 N VAL E 175 ? N VAL I 174 O GLY E 320 ? O GLY I 319 
AC2 1 2 O ALA E 259 ? O ALA I 258 N GLY E 211 ? N GLY I 210 
AC2 2 3 N HIS E 218 ? N HIS I 217 O THR E 286 ? O THR I 285 
AC2 3 4 N LEU E 287 ? N LEU I 286 O GLY E 317 ? O GLY I 316 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  401 ? 6 'binding site for residue ZN A 401'  
AC2 Software A CU  402 ? 5 'binding site for residue CU A 402'  
AC3 Software A ZN  403 ? 5 'binding site for residue ZN A 403'  
AC4 Software A CU  404 ? 6 'binding site for residue CU A 404'  
AC5 Software C ZN  401 ? 5 'binding site for residue ZN C 401'  
AC6 Software C CU  402 ? 5 'binding site for residue CU C 402'  
AC7 Software C ZN  403 ? 5 'binding site for residue ZN C 403'  
AC8 Software C CU  404 ? 5 'binding site for residue CU C 404'  
AC9 Software E ZN  401 ? 5 'binding site for residue ZN E 401'  
AD1 Software E CU  402 ? 5 'binding site for residue CU E 402'  
AD2 Software E ZN  403 ? 5 'binding site for residue ZN E 403'  
AD3 Software E CU  404 ? 6 'binding site for residue CU E 404'  
AD4 Software E MLI 405 ? 6 'binding site for residue MLI E 405' 
AD5 Software G ZN  401 ? 5 'binding site for residue ZN G 401'  
AD6 Software G CU  402 ? 5 'binding site for residue CU G 402'  
AD7 Software G ZN  403 ? 6 'binding site for residue ZN G 403'  
AD8 Software G CU  404 ? 5 'binding site for residue CU G 404'  
AD9 Software I ZN  401 ? 5 'binding site for residue ZN I 401'  
AE1 Software I CU  402 ? 6 'binding site for residue CU I 402'  
AE2 Software I ZN  403 ? 6 'binding site for residue ZN I 403'  
AE3 Software I CU  404 ? 5 'binding site for residue CU I 404'  
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1   AC1 6 HIS A  64  ? HIS A 63  . ? 1_555 ? 
2   AC1 6 HIS A  72  ? HIS A 71  . ? 1_555 ? 
3   AC1 6 HIS A  81  ? HIS A 80  . ? 1_555 ? 
4   AC1 6 SER A  84  ? SER A 83  . ? 1_555 ? 
5   AC1 6 ASP A  84  ? ASP A 83  . ? 1_555 ? 
6   AC1 6 HOH AA .   ? HOH A 501 . ? 1_555 ? 
7   AC2 5 HIS A  47  ? HIS A 46  . ? 1_555 ? 
8   AC2 5 HIS A  49  ? HIS A 48  . ? 1_555 ? 
9   AC2 5 HIS A  64  ? HIS A 63  . ? 1_555 ? 
10  AC2 5 HIS A  121 ? HIS A 120 . ? 1_555 ? 
11  AC2 5 HOH AA .   ? HOH A 608 . ? 1_555 ? 
12  AC3 5 HIS A  233 ? HIS A 232 . ? 1_555 ? 
13  AC3 5 HIS A  241 ? HIS A 240 . ? 1_555 ? 
14  AC3 5 HIS A  250 ? HIS A 249 . ? 1_555 ? 
15  AC3 5 SER A  253 ? SER A 252 . ? 1_555 ? 
16  AC3 5 ASP A  253 ? ASP A 252 . ? 1_555 ? 
17  AC4 6 HIS A  216 ? HIS A 215 . ? 1_555 ? 
18  AC4 6 HIS A  218 ? HIS A 217 . ? 1_555 ? 
19  AC4 6 HIS A  233 ? HIS A 232 . ? 1_555 ? 
20  AC4 6 HIS A  290 ? HIS A 289 . ? 1_555 ? 
21  AC4 6 HOH AA .   ? HOH A 567 . ? 1_555 ? 
22  AC4 6 HOH AA .   ? HOH A 619 . ? 1_555 ? 
23  AC5 5 HIS B  64  ? HIS C 63  . ? 1_555 ? 
24  AC5 5 HIS B  72  ? HIS C 71  . ? 1_555 ? 
25  AC5 5 HIS B  81  ? HIS C 80  . ? 1_555 ? 
26  AC5 5 ASP B  84  ? ASP C 83  . ? 1_555 ? 
27  AC5 5 SER B  84  ? SER C 83  . ? 1_555 ? 
28  AC6 5 HIS B  47  ? HIS C 46  . ? 1_555 ? 
29  AC6 5 HIS B  49  ? HIS C 48  . ? 1_555 ? 
30  AC6 5 HIS B  64  ? HIS C 63  . ? 1_555 ? 
31  AC6 5 HIS B  121 ? HIS C 120 . ? 1_555 ? 
32  AC6 5 HOH BA .   ? HOH C 522 . ? 1_555 ? 
33  AC7 5 HIS B  233 ? HIS C 232 . ? 1_555 ? 
34  AC7 5 HIS B  241 ? HIS C 240 . ? 1_555 ? 
35  AC7 5 HIS B  250 ? HIS C 249 . ? 1_555 ? 
36  AC7 5 ASP B  253 ? ASP C 252 . ? 1_555 ? 
37  AC7 5 SER B  253 ? SER C 252 . ? 1_555 ? 
38  AC8 5 HIS B  216 ? HIS C 215 . ? 1_555 ? 
39  AC8 5 HIS B  218 ? HIS C 217 . ? 1_555 ? 
40  AC8 5 HIS B  233 ? HIS C 232 . ? 1_555 ? 
41  AC8 5 HIS B  290 ? HIS C 289 . ? 1_555 ? 
42  AC8 5 HOH BA .   ? HOH C 565 . ? 1_555 ? 
43  AC9 5 HIS C  64  ? HIS E 63  . ? 1_555 ? 
44  AC9 5 HIS C  72  ? HIS E 71  . ? 1_555 ? 
45  AC9 5 HIS C  81  ? HIS E 80  . ? 1_555 ? 
46  AC9 5 ASP C  84  ? ASP E 83  . ? 1_555 ? 
47  AC9 5 SER C  84  ? SER E 83  . ? 1_555 ? 
48  AD1 5 HIS C  47  ? HIS E 46  . ? 1_555 ? 
49  AD1 5 HIS C  49  ? HIS E 48  . ? 1_555 ? 
50  AD1 5 HIS C  64  ? HIS E 63  . ? 1_555 ? 
51  AD1 5 HIS C  121 ? HIS E 120 . ? 1_555 ? 
52  AD1 5 HOH CA .   ? HOH E 623 . ? 1_555 ? 
53  AD2 5 HIS C  233 ? HIS E 232 . ? 1_555 ? 
54  AD2 5 HIS C  241 ? HIS E 240 . ? 1_555 ? 
55  AD2 5 HIS C  250 ? HIS E 249 . ? 1_555 ? 
56  AD2 5 ASP C  253 ? ASP E 252 . ? 1_555 ? 
57  AD2 5 SER C  253 ? SER E 252 . ? 1_555 ? 
58  AD3 6 HIS C  216 ? HIS E 215 . ? 1_555 ? 
59  AD3 6 HIS C  218 ? HIS E 217 . ? 1_555 ? 
60  AD3 6 HIS C  233 ? HIS E 232 . ? 1_555 ? 
61  AD3 6 HIS C  290 ? HIS E 289 . ? 1_555 ? 
62  AD3 6 HOH CA .   ? HOH E 575 . ? 1_555 ? 
63  AD3 6 HOH CA .   ? HOH E 662 . ? 1_555 ? 
64  AD4 6 SER C  26  ? SER E 25  . ? 1_555 ? 
65  AD4 6 SER C  108 ? SER E 107 . ? 3_455 ? 
66  AD4 6 SER C  108 ? SER E 107 . ? 1_555 ? 
67  AD4 6 ALA C  157 ? ALA E 156 . ? 3_455 ? 
68  AD4 6 HOH CA .   ? HOH E 506 . ? 3_455 ? 
69  AD4 6 HOH CA .   ? HOH E 507 . ? 1_555 ? 
70  AD5 5 HIS D  64  ? HIS G 63  . ? 1_555 ? 
71  AD5 5 HIS D  72  ? HIS G 71  . ? 1_555 ? 
72  AD5 5 HIS D  81  ? HIS G 80  . ? 1_555 ? 
73  AD5 5 ASP D  84  ? ASP G 83  . ? 1_555 ? 
74  AD5 5 SER D  84  ? SER G 83  . ? 1_555 ? 
75  AD6 5 HIS D  47  ? HIS G 46  . ? 1_555 ? 
76  AD6 5 HIS D  49  ? HIS G 48  . ? 1_555 ? 
77  AD6 5 HIS D  64  ? HIS G 63  . ? 1_555 ? 
78  AD6 5 HIS D  121 ? HIS G 120 . ? 1_555 ? 
79  AD6 5 HOH DA .   ? HOH G 595 . ? 1_555 ? 
80  AD7 6 HIS D  233 ? HIS G 232 . ? 1_555 ? 
81  AD7 6 HIS D  241 ? HIS G 240 . ? 1_555 ? 
82  AD7 6 HIS D  250 ? HIS G 249 . ? 1_555 ? 
83  AD7 6 SER D  253 ? SER G 252 . ? 1_555 ? 
84  AD7 6 ASP D  253 ? ASP G 252 . ? 1_555 ? 
85  AD7 6 LYS D  306 ? LYS G 305 . ? 1_555 ? 
86  AD8 5 HIS D  216 ? HIS G 215 . ? 1_555 ? 
87  AD8 5 HIS D  218 ? HIS G 217 . ? 1_555 ? 
88  AD8 5 HIS D  233 ? HIS G 232 . ? 1_555 ? 
89  AD8 5 HIS D  290 ? HIS G 289 . ? 1_555 ? 
90  AD8 5 HOH DA .   ? HOH G 565 . ? 1_555 ? 
91  AD9 5 HIS E  64  ? HIS I 63  . ? 1_555 ? 
92  AD9 5 HIS E  72  ? HIS I 71  . ? 1_555 ? 
93  AD9 5 HIS E  81  ? HIS I 80  . ? 1_555 ? 
94  AD9 5 ASP E  84  ? ASP I 83  . ? 1_555 ? 
95  AD9 5 SER E  84  ? SER I 83  . ? 1_555 ? 
96  AE1 6 HIS E  47  ? HIS I 46  . ? 1_555 ? 
97  AE1 6 HIS E  49  ? HIS I 48  . ? 1_555 ? 
98  AE1 6 HIS E  64  ? HIS I 63  . ? 1_555 ? 
99  AE1 6 HIS E  121 ? HIS I 120 . ? 1_555 ? 
100 AE1 6 HOH EA .   ? HOH I 605 . ? 1_555 ? 
101 AE1 6 HOH EA .   ? HOH I 642 . ? 1_555 ? 
102 AE2 6 HIS E  233 ? HIS I 232 . ? 1_555 ? 
103 AE2 6 HIS E  241 ? HIS I 240 . ? 1_555 ? 
104 AE2 6 HIS E  250 ? HIS I 249 . ? 1_555 ? 
105 AE2 6 SER E  253 ? SER I 252 . ? 1_555 ? 
106 AE2 6 ASP E  253 ? ASP I 252 . ? 1_555 ? 
107 AE2 6 HOH EA .   ? HOH I 517 . ? 1_555 ? 
108 AE3 5 HIS E  216 ? HIS I 215 . ? 1_555 ? 
109 AE3 5 HIS E  218 ? HIS I 217 . ? 1_555 ? 
110 AE3 5 HIS E  233 ? HIS I 232 . ? 1_555 ? 
111 AE3 5 HIS E  290 ? HIS I 289 . ? 1_555 ? 
112 AE3 5 HOH EA .   ? HOH I 543 . ? 1_555 ? 
# 
_atom_sites.entry_id                    6DTK 
_atom_sites.fract_transf_matrix[1][1]   0.006146 
_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]   0.004959 
_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]   0.006952 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CU 
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 2   ? -84.797  -52.525 99.801  1.00 63.38  ? 1   ALA A N   1 
ATOM   2     C  CA  . ALA A  1 2   ? -85.434  -53.538 98.899  1.00 61.28  ? 1   ALA A CA  1 
ATOM   3     C  C   . ALA A  1 2   ? -84.440  -54.671 98.588  1.00 57.76  ? 1   ALA A C   1 
ATOM   4     O  O   . ALA A  1 2   ? -83.256  -54.592 98.906  1.00 57.40  ? 1   ALA A O   1 
ATOM   5     C  CB  . ALA A  1 2   ? -85.916  -52.858 97.637  1.00 62.49  ? 1   ALA A CB  1 
ATOM   6     N  N   . THR A  1 3   ? -84.936  -55.732 97.948  1.00 53.54  ? 2   THR A N   1 
ATOM   7     C  CA  . THR A  1 3   ? -84.114  -56.872 97.615  1.00 51.56  ? 2   THR A CA  1 
ATOM   8     C  C   . THR A  1 3   ? -83.634  -56.764 96.160  1.00 49.16  ? 2   THR A C   1 
ATOM   9     O  O   . THR A  1 3   ? -82.738  -57.510 95.779  1.00 47.71  ? 2   THR A O   1 
ATOM   10    C  CB  . THR A  1 3   ? -84.844  -58.197 97.886  1.00 52.35  ? 2   THR A CB  1 
ATOM   11    O  OG1 . THR A  1 3   ? -85.907  -58.355 96.945  1.00 57.70  ? 2   THR A OG1 1 
ATOM   12    C  CG2 . THR A  1 3   ? -85.396  -58.285 99.291  1.00 54.58  ? 2   THR A CG2 1 
ATOM   13    N  N   . LYS A  1 4   ? -84.232  -55.861 95.364  1.00 44.66  ? 3   LYS A N   1 
ATOM   14    C  CA  . LYS A  1 4   ? -83.832  -55.643 93.966  1.00 43.82  ? 3   LYS A CA  1 
ATOM   15    C  C   . LYS A  1 4   ? -83.809  -54.146 93.648  1.00 39.43  ? 3   LYS A C   1 
ATOM   16    O  O   . LYS A  1 4   ? -84.688  -53.387 94.070  1.00 33.27  ? 3   LYS A O   1 
ATOM   17    C  CB  . LYS A  1 4   ? -84.781  -56.336 92.986  1.00 50.21  ? 3   LYS A CB  1 
ATOM   18    C  CG  . LYS A  1 4   ? -84.685  -57.857 92.957  1.00 58.95  ? 3   LYS A CG  1 
ATOM   19    C  CD  . LYS A  1 4   ? -85.014  -58.475 91.617  1.00 65.48  ? 3   LYS A CD  1 
ATOM   20    C  CE  . LYS A  1 4   ? -84.162  -57.933 90.483  1.00 71.25  ? 3   LYS A CE  1 
ATOM   21    N  NZ  . LYS A  1 4   ? -84.016  -58.913 89.380  1.00 71.46  ? 3   LYS A NZ  1 
ATOM   22    N  N   . ALA A  1 5   ? -82.785  -53.746 92.893  1.00 37.06  ? 4   ALA A N   1 
ATOM   23    C  CA  . ALA A  1 5   ? -82.646  -52.393 92.413  1.00 34.80  ? 4   ALA A CA  1 
ATOM   24    C  C   . ALA A  1 5   ? -82.124  -52.428 90.978  1.00 33.52  ? 4   ALA A C   1 
ATOM   25    O  O   . ALA A  1 5   ? -81.654  -53.470 90.477  1.00 30.97  ? 4   ALA A O   1 
ATOM   26    C  CB  . ALA A  1 5   ? -81.731  -51.618 93.324  1.00 36.33  ? 4   ALA A CB  1 
ATOM   27    N  N   . VAL A  1 6   ? -82.221  -51.272 90.324  1.00 30.74  ? 5   VAL A N   1 
ATOM   28    C  CA  . VAL A  1 6   ? -81.855  -51.141 88.931  1.00 30.19  ? 5   VAL A CA  1 
ATOM   29    C  C   . VAL A  1 6   ? -81.436  -49.697 88.682  1.00 29.41  ? 5   VAL A C   1 
ATOM   30    O  O   . VAL A  1 6   ? -81.870  -48.774 89.390  1.00 29.31  ? 5   VAL A O   1 
ATOM   31    C  CB  . VAL A  1 6   ? -83.013  -51.560 88.011  1.00 31.48  ? 5   VAL A CB  1 
ATOM   32    C  CG1 . VAL A  1 6   ? -84.151  -50.553 88.053  1.00 30.91  ? 5   VAL A CG1 1 
ATOM   33    C  CG2 . VAL A  1 6   ? -82.552  -51.813 86.584  1.00 33.63  ? 5   VAL A CG2 1 
ATOM   34    N  N   . CYS A  1 7   ? -80.572  -49.543 87.684  1.00 28.53  ? 6   CYS A N   1 
ATOM   35    C  CA  . CYS A  1 7   ? -80.033  -48.284 87.289  1.00 28.91  ? 6   CYS A CA  1 
ATOM   36    C  C   . CYS A  1 7   ? -79.920  -48.266 85.758  1.00 27.24  ? 6   CYS A C   1 
ATOM   37    O  O   . CYS A  1 7   ? -79.384  -49.220 85.161  1.00 27.32  ? 6   CYS A O   1 
ATOM   38    C  CB  . CYS A  1 7   ? -78.664  -48.106 87.923  1.00 30.68  ? 6   CYS A CB  1 
ATOM   39    S  SG  . CYS A  1 7   ? -77.964  -46.471 87.613  1.00 33.73  ? 6   CYS A SG  1 
ATOM   40    N  N   . VAL A  1 8   ? -80.469  -47.216 85.146  1.00 26.88  ? 7   VAL A N   1 
ATOM   41    C  CA  . VAL A  1 8   ? -80.253  -46.898 83.747  1.00 26.72  ? 7   VAL A CA  1 
ATOM   42    C  C   . VAL A  1 8   ? -79.152  -45.826 83.663  1.00 26.40  ? 7   VAL A C   1 
ATOM   43    O  O   . VAL A  1 8   ? -79.317  -44.709 84.135  1.00 26.80  ? 7   VAL A O   1 
ATOM   44    C  CB  . VAL A  1 8   ? -81.562  -46.425 83.100  1.00 29.98  ? 7   VAL A CB  1 
ATOM   45    C  CG1 . VAL A  1 8   ? -81.390  -46.155 81.612  1.00 31.76  ? 7   VAL A CG1 1 
ATOM   46    C  CG2 . VAL A  1 8   ? -82.687  -47.418 83.332  1.00 30.34  ? 7   VAL A CG2 1 
ATOM   47    N  N   . LEU A  1 9   ? -78.026  -46.167 83.041  1.00 27.76  ? 8   LEU A N   1 
ATOM   48    C  CA  . LEU A  1 9   ? -76.908  -45.244 82.877  1.00 29.33  ? 8   LEU A CA  1 
ATOM   49    C  C   . LEU A  1 9   ? -77.068  -44.509 81.543  1.00 28.49  ? 8   LEU A C   1 
ATOM   50    O  O   . LEU A  1 9   ? -77.255  -45.140 80.511  1.00 25.18  ? 8   LEU A O   1 
ATOM   51    C  CB  . LEU A  1 9   ? -75.578  -46.003 82.902  1.00 32.87  ? 8   LEU A CB  1 
ATOM   52    C  CG  . LEU A  1 9   ? -75.101  -46.502 84.270  1.00 38.03  ? 8   LEU A CG  1 
ATOM   53    C  CD1 A LEU A  1 9   ? -76.211  -47.245 84.977  0.60 42.39  ? 8   LEU A CD1 1 
ATOM   54    C  CD1 B LEU A  1 9   ? -76.208  -47.250 84.981  0.40 40.62  ? 8   LEU A CD1 1 
ATOM   55    C  CD2 A LEU A  1 9   ? -73.898  -47.420 84.116  0.60 40.71  ? 8   LEU A CD2 1 
ATOM   56    C  CD2 B LEU A  1 9   ? -73.890  -47.409 84.114  0.40 39.48  ? 8   LEU A CD2 1 
ATOM   57    N  N   . LYS A  1 10  ? -76.943  -43.181 81.600  1.00 30.24  ? 9   LYS A N   1 
ATOM   58    C  CA  . LYS A  1 10  ? -76.943  -42.299 80.438  1.00 34.40  ? 9   LYS A CA  1 
ATOM   59    C  C   . LYS A  1 10  ? -75.913  -41.194 80.688  1.00 34.02  ? 9   LYS A C   1 
ATOM   60    O  O   . LYS A  1 10  ? -75.608  -40.859 81.838  1.00 29.01  ? 9   LYS A O   1 
ATOM   61    C  CB  . LYS A  1 10  ? -78.335  -41.696 80.227  1.00 37.58  ? 9   LYS A CB  1 
ATOM   62    C  CG  . LYS A  1 10  ? -79.433  -42.678 79.843  1.00 46.13  ? 9   LYS A CG  1 
ATOM   63    C  CD  . LYS A  1 10  ? -79.479  -42.987 78.362  1.00 55.66  ? 9   LYS A CD  1 
ATOM   64    C  CE  . LYS A  1 10  ? -80.714  -43.751 77.918  1.00 60.97  ? 9   LYS A CE  1 
ATOM   65    N  NZ  . LYS A  1 10  ? -80.527  -45.217 78.054  1.00 66.88  ? 9   LYS A NZ  1 
ATOM   66    N  N   . GLY A  1 11  ? -75.386  -40.616 79.603  1.00 33.15  ? 10  GLY A N   1 
ATOM   67    C  CA  . GLY A  1 11  ? -74.513  -39.443 79.699  1.00 34.39  ? 10  GLY A CA  1 
ATOM   68    C  C   . GLY A  1 11  ? -74.617  -38.556 78.474  1.00 32.68  ? 10  GLY A C   1 
ATOM   69    O  O   . GLY A  1 11  ? -75.507  -38.709 77.671  1.00 33.59  ? 10  GLY A O   1 
ATOM   70    N  N   . ASP A  1 12  ? -73.662  -37.642 78.344  1.00 37.45  ? 11  ASP A N   1 
ATOM   71    C  CA  . ASP A  1 12  ? -73.636  -36.638 77.294  1.00 42.84  ? 11  ASP A CA  1 
ATOM   72    C  C   . ASP A  1 12  ? -73.140  -37.266 75.994  1.00 42.60  ? 11  ASP A C   1 
ATOM   73    O  O   . ASP A  1 12  ? -73.453  -36.768 74.938  1.00 44.99  ? 11  ASP A O   1 
ATOM   74    C  CB  . ASP A  1 12  ? -72.780  -35.450 77.726  1.00 47.03  ? 11  ASP A CB  1 
ATOM   75    C  CG  . ASP A  1 12  ? -73.430  -34.693 78.873  1.00 57.01  ? 11  ASP A CG  1 
ATOM   76    O  OD1 . ASP A  1 12  ? -74.688  -34.605 78.883  1.00 61.40  ? 11  ASP A OD1 1 
ATOM   77    O  OD2 . ASP A  1 12  ? -72.691  -34.225 79.766  1.00 70.62  ? 11  ASP A OD2 1 
ATOM   78    N  N   . GLY A  1 13  ? -72.381  -38.363 76.112  1.00 36.36  ? 12  GLY A N   1 
ATOM   79    C  CA  . GLY A  1 13  ? -71.882  -39.124 74.991  1.00 33.26  ? 12  GLY A CA  1 
ATOM   80    C  C   . GLY A  1 13  ? -72.698  -40.391 74.745  1.00 31.55  ? 12  GLY A C   1 
ATOM   81    O  O   . GLY A  1 13  ? -73.886  -40.460 75.055  1.00 30.58  ? 12  GLY A O   1 
ATOM   82    N  N   . PRO A  1 14  ? -72.059  -41.422 74.142  1.00 30.54  ? 13  PRO A N   1 
ATOM   83    C  CA  . PRO A  1 14  ? -72.733  -42.651 73.745  1.00 29.35  ? 13  PRO A CA  1 
ATOM   84    C  C   . PRO A  1 14  ? -72.807  -43.774 74.796  1.00 28.91  ? 13  PRO A C   1 
ATOM   85    O  O   . PRO A  1 14  ? -73.372  -44.816 74.534  1.00 32.01  ? 13  PRO A O   1 
ATOM   86    C  CB  . PRO A  1 14  ? -71.831  -43.056 72.580  1.00 29.23  ? 13  PRO A CB  1 
ATOM   87    C  CG  . PRO A  1 14  ? -70.467  -42.740 73.072  1.00 30.13  ? 13  PRO A CG  1 
ATOM   88    C  CD  . PRO A  1 14  ? -70.630  -41.419 73.787  1.00 30.66  ? 13  PRO A CD  1 
ATOM   89    N  N   . VAL A  1 15  ? -72.243  -43.556 75.983  1.00 30.55  ? 14  VAL A N   1 
ATOM   90    C  CA  . VAL A  1 15  ? -72.245  -44.602 77.022  1.00 31.53  ? 14  VAL A CA  1 
ATOM   91    C  C   . VAL A  1 15  ? -73.668  -44.742 77.581  1.00 31.37  ? 14  VAL A C   1 
ATOM   92    O  O   . VAL A  1 15  ? -74.272  -43.760 78.049  1.00 30.19  ? 14  VAL A O   1 
ATOM   93    C  CB  . VAL A  1 15  ? -71.224  -44.316 78.137  1.00 32.70  ? 14  VAL A CB  1 
ATOM   94    C  CG1 . VAL A  1 15  ? -71.279  -45.391 79.223  1.00 34.41  ? 14  VAL A CG1 1 
ATOM   95    C  CG2 . VAL A  1 15  ? -69.814  -44.192 77.583  1.00 32.49  ? 14  VAL A CG2 1 
ATOM   96    N  N   . GLN A  1 16  ? -74.191  -45.969 77.526  1.00 32.14  ? 15  GLN A N   1 
ATOM   97    C  CA  . GLN A  1 16  ? -75.458  -46.294 78.116  1.00 33.83  ? 15  GLN A CA  1 
ATOM   98    C  C   . GLN A  1 16  ? -75.492  -47.763 78.528  1.00 32.65  ? 15  GLN A C   1 
ATOM   99    O  O   . GLN A  1 16  ? -74.821  -48.624 77.950  1.00 32.71  ? 15  GLN A O   1 
ATOM   100   C  CB  . GLN A  1 16  ? -76.612  -45.977 77.167  1.00 36.87  ? 15  GLN A CB  1 
ATOM   101   C  CG  . GLN A  1 16  ? -76.447  -46.529 75.766  1.00 39.95  ? 15  GLN A CG  1 
ATOM   102   C  CD  . GLN A  1 16  ? -77.540  -46.051 74.832  1.00 44.69  ? 15  GLN A CD  1 
ATOM   103   O  OE1 . GLN A  1 16  ? -77.305  -45.777 73.654  1.00 48.09  ? 15  GLN A OE1 1 
ATOM   104   N  NE2 . GLN A  1 16  ? -78.756  -45.959 75.345  1.00 40.75  ? 15  GLN A NE2 1 
ATOM   105   N  N   . GLY A  1 17  ? -76.299  -48.029 79.549  1.00 31.79  ? 16  GLY A N   1 
ATOM   106   C  CA  . GLY A  1 17  ? -76.448  -49.356 80.063  1.00 35.30  ? 16  GLY A CA  1 
ATOM   107   C  C   . GLY A  1 17  ? -77.544  -49.456 81.098  1.00 32.39  ? 16  GLY A C   1 
ATOM   108   O  O   . GLY A  1 17  ? -78.136  -48.450 81.517  1.00 31.77  ? 16  GLY A O   1 
ATOM   109   N  N   . ILE A  1 18  ? -77.787  -50.702 81.494  1.00 30.63  ? 17  ILE A N   1 
ATOM   110   C  CA  . ILE A  1 18  ? -78.684  -51.077 82.541  1.00 33.27  ? 17  ILE A CA  1 
ATOM   111   C  C   . ILE A  1 18  ? -77.913  -51.990 83.502  1.00 34.96  ? 17  ILE A C   1 
ATOM   112   O  O   . ILE A  1 18  ? -77.358  -53.018 83.066  1.00 33.87  ? 17  ILE A O   1 
ATOM   113   C  CB  . ILE A  1 18  ? -79.923  -51.779 81.958  1.00 33.27  ? 17  ILE A CB  1 
ATOM   114   C  CG1 . ILE A  1 18  ? -80.751  -50.801 81.123  1.00 36.23  ? 17  ILE A CG1 1 
ATOM   115   C  CG2 . ILE A  1 18  ? -80.750  -52.438 83.058  1.00 34.41  ? 17  ILE A CG2 1 
ATOM   116   C  CD1 . ILE A  1 18  ? -81.852  -51.459 80.326  1.00 37.49  ? 17  ILE A CD1 1 
ATOM   117   N  N   . ILE A  1 19  ? -77.906  -51.629 84.790  1.00 32.24  ? 18  ILE A N   1 
ATOM   118   C  CA  . ILE A  1 19  ? -77.265  -52.438 85.814  1.00 32.78  ? 18  ILE A CA  1 
ATOM   119   C  C   . ILE A  1 19  ? -78.324  -52.855 86.835  1.00 34.63  ? 18  ILE A C   1 
ATOM   120   O  O   . ILE A  1 19  ? -79.053  -52.012 87.352  1.00 33.61  ? 18  ILE A O   1 
ATOM   121   C  CB  . ILE A  1 19  ? -76.088  -51.688 86.476  1.00 34.95  ? 18  ILE A CB  1 
ATOM   122   C  CG1 . ILE A  1 19  ? -74.986  -51.338 85.468  1.00 33.87  ? 18  ILE A CG1 1 
ATOM   123   C  CG2 . ILE A  1 19  ? -75.523  -52.489 87.640  1.00 31.85  ? 18  ILE A CG2 1 
ATOM   124   C  CD1 . ILE A  1 19  ? -74.312  -52.546 84.846  1.00 36.25  ? 18  ILE A CD1 1 
ATOM   125   N  N   . ASN A  1 20  ? -78.370  -54.164 87.116  1.00 33.67  ? 19  ASN A N   1 
ATOM   126   C  CA  . ASN A  1 20  ? -79.283  -54.771 88.091  1.00 34.63  ? 19  ASN A CA  1 
ATOM   127   C  C   . ASN A  1 20  ? -78.539  -55.054 89.398  1.00 34.64  ? 19  ASN A C   1 
ATOM   128   O  O   . ASN A  1 20  ? -77.334  -55.332 89.390  1.00 35.46  ? 19  ASN A O   1 
ATOM   129   C  CB  . ASN A  1 20  ? -79.868  -56.081 87.573  1.00 34.06  ? 19  ASN A CB  1 
ATOM   130   C  CG  . ASN A  1 20  ? -80.524  -55.892 86.232  1.00 38.15  ? 19  ASN A CG  1 
ATOM   131   O  OD1 . ASN A  1 20  ? -81.603  -55.320 86.160  1.00 39.91  ? 19  ASN A OD1 1 
ATOM   132   N  ND2 . ASN A  1 20  ? -79.853  -56.315 85.170  1.00 38.58  ? 19  ASN A ND2 1 
ATOM   133   N  N   . PHE A  1 21  ? -79.274  -54.958 90.511  1.00 36.28  ? 20  PHE A N   1 
ATOM   134   C  CA  . PHE A  1 21  ? -78.765  -55.289 91.831  1.00 37.51  ? 20  PHE A CA  1 
ATOM   135   C  C   . PHE A  1 21  ? -79.766  -56.230 92.512  1.00 42.82  ? 20  PHE A C   1 
ATOM   136   O  O   . PHE A  1 21  ? -80.983  -56.062 92.379  1.00 36.30  ? 20  PHE A O   1 
ATOM   137   C  CB  . PHE A  1 21  ? -78.557  -54.056 92.709  1.00 37.26  ? 20  PHE A CB  1 
ATOM   138   C  CG  . PHE A  1 21  ? -77.751  -52.924 92.122  1.00 36.94  ? 20  PHE A CG  1 
ATOM   139   C  CD1 . PHE A  1 21  ? -76.455  -52.687 92.536  1.00 36.18  ? 20  PHE A CD1 1 
ATOM   140   C  CD2 . PHE A  1 21  ? -78.316  -52.053 91.198  1.00 38.78  ? 20  PHE A CD2 1 
ATOM   141   C  CE1 . PHE A  1 21  ? -75.733  -51.616 92.030  1.00 38.00  ? 20  PHE A CE1 1 
ATOM   142   C  CE2 . PHE A  1 21  ? -77.587  -50.988 90.681  1.00 37.29  ? 20  PHE A CE2 1 
ATOM   143   C  CZ  . PHE A  1 21  ? -76.300  -50.766 91.104  1.00 36.42  ? 20  PHE A CZ  1 
ATOM   144   N  N   . GLU A  1 22  ? -79.237  -57.232 93.226  1.00 43.75  ? 21  GLU A N   1 
ATOM   145   C  CA  . GLU A  1 22  ? -80.061  -58.177 93.963  1.00 47.41  ? 21  GLU A CA  1 
ATOM   146   C  C   . GLU A  1 22  ? -79.381  -58.500 95.294  1.00 45.63  ? 21  GLU A C   1 
ATOM   147   O  O   . GLU A  1 22  ? -78.197  -58.836 95.318  1.00 42.56  ? 21  GLU A O   1 
ATOM   148   C  CB  . GLU A  1 22  ? -80.271  -59.435 93.132  1.00 52.43  ? 21  GLU A CB  1 
ATOM   149   C  CG  . GLU A  1 22  ? -81.260  -60.410 93.734  1.00 59.12  ? 21  GLU A CG  1 
ATOM   150   C  CD  . GLU A  1 22  ? -81.778  -61.381 92.689  1.00 65.81  ? 21  GLU A CD  1 
ATOM   151   O  OE1 . GLU A  1 22  ? -81.410  -62.574 92.748  1.00 74.09  ? 21  GLU A OE1 1 
ATOM   152   O  OE2 . GLU A  1 22  ? -82.515  -60.925 91.787  1.00 76.64  ? 21  GLU A OE2 1 
ATOM   153   N  N   . GLN A  1 23  ? -80.138  -58.346 96.384  1.00 48.22  ? 22  GLN A N   1 
ATOM   154   C  CA  . GLN A  1 23  ? -79.686  -58.667 97.727  1.00 52.63  ? 22  GLN A CA  1 
ATOM   155   C  C   . GLN A  1 23  ? -80.779  -59.475 98.437  1.00 57.06  ? 22  GLN A C   1 
ATOM   156   O  O   . GLN A  1 23  ? -81.730  -58.884 98.952  1.00 54.47  ? 22  GLN A O   1 
ATOM   157   C  CB  . GLN A  1 23  ? -79.362  -57.395 98.508  1.00 50.61  ? 22  GLN A CB  1 
ATOM   158   C  CG  . GLN A  1 23  ? -78.737  -57.682 99.863  1.00 50.39  ? 22  GLN A CG  1 
ATOM   159   C  CD  . GLN A  1 23  ? -78.462  -56.437 100.662 1.00 49.79  ? 22  GLN A CD  1 
ATOM   160   O  OE1 . GLN A  1 23  ? -79.216  -55.466 100.622 1.00 51.27  ? 22  GLN A OE1 1 
ATOM   161   N  NE2 . GLN A  1 23  ? -77.379  -56.468 101.422 1.00 52.39  ? 22  GLN A NE2 1 
ATOM   162   N  N   . LYS A  1 24  ? -80.608  -60.807 98.459  1.00 66.40  ? 23  LYS A N   1 
ATOM   163   C  CA  . LYS A  1 24  ? -81.604  -61.767 98.988  1.00 76.05  ? 23  LYS A CA  1 
ATOM   164   C  C   . LYS A  1 24  ? -81.667  -61.715 100.520 1.00 72.76  ? 23  LYS A C   1 
ATOM   165   O  O   . LYS A  1 24  ? -82.754  -61.699 101.083 1.00 73.69  ? 23  LYS A O   1 
ATOM   166   C  CB  . LYS A  1 24  ? -81.301  -63.201 98.530  1.00 82.22  ? 23  LYS A CB  1 
ATOM   167   C  CG  . LYS A  1 24  ? -81.505  -63.492 97.046  1.00 90.48  ? 23  LYS A CG  1 
ATOM   168   C  CD  . LYS A  1 24  ? -82.422  -62.518 96.311  1.00 101.24 ? 23  LYS A CD  1 
ATOM   169   C  CE  . LYS A  1 24  ? -83.837  -62.442 96.855  1.00 104.67 ? 23  LYS A CE  1 
ATOM   170   N  NZ  . LYS A  1 24  ? -84.822  -63.070 95.943  1.00 107.34 ? 23  LYS A NZ  1 
ATOM   171   N  N   . GLU A  1 25  ? -80.506  -61.703 101.181 1.00 73.60  ? 24  GLU A N   1 
ATOM   172   C  CA  . GLU A  1 25  ? -80.429  -61.598 102.636 1.00 79.27  ? 24  GLU A CA  1 
ATOM   173   C  C   . GLU A  1 25  ? -80.116  -60.141 102.992 1.00 76.71  ? 24  GLU A C   1 
ATOM   174   O  O   . GLU A  1 25  ? -79.208  -59.558 102.424 1.00 73.88  ? 24  GLU A O   1 
ATOM   175   C  CB  . GLU A  1 25  ? -79.388  -62.584 103.167 1.00 85.03  ? 24  GLU A CB  1 
ATOM   176   C  CG  . GLU A  1 25  ? -79.670  -64.027 102.769 1.00 90.95  ? 24  GLU A CG  1 
ATOM   177   C  CD  . GLU A  1 25  ? -78.439  -64.915 102.655 1.00 100.76 ? 24  GLU A CD  1 
ATOM   178   O  OE1 . GLU A  1 25  ? -78.191  -65.700 103.595 1.00 106.78 ? 24  GLU A OE1 1 
ATOM   179   O  OE2 . GLU A  1 25  ? -77.734  -64.831 101.621 1.00 100.85 ? 24  GLU A OE2 1 
ATOM   180   N  N   . SER A  1 26  ? -80.853  -59.592 103.963 1.00 79.18  ? 25  SER A N   1 
ATOM   181   C  CA  . SER A  1 26  ? -81.036  -58.143 104.123 1.00 87.04  ? 25  SER A CA  1 
ATOM   182   C  C   . SER A  1 26  ? -79.713  -57.414 104.410 1.00 90.31  ? 25  SER A C   1 
ATOM   183   O  O   . SER A  1 26  ? -79.621  -56.205 104.170 1.00 100.75 ? 25  SER A O   1 
ATOM   184   C  CB  . SER A  1 26  ? -82.072  -57.834 105.176 1.00 89.56  ? 25  SER A CB  1 
ATOM   185   O  OG  . SER A  1 26  ? -81.550  -58.030 106.481 1.00 89.23  ? 25  SER A OG  1 
ATOM   186   N  N   . ASN A  1 27  ? -78.701  -58.121 104.927 1.00 84.90  ? 26  ASN A N   1 
ATOM   187   C  CA  . ASN A  1 27  ? -77.351  -57.554 104.978 1.00 85.17  ? 26  ASN A CA  1 
ATOM   188   C  C   . ASN A  1 27  ? -76.337  -58.632 104.570 1.00 79.99  ? 26  ASN A C   1 
ATOM   189   O  O   . ASN A  1 27  ? -75.254  -58.734 105.138 1.00 84.92  ? 26  ASN A O   1 
ATOM   190   C  CB  . ASN A  1 27  ? -77.060  -56.869 106.319 1.00 92.56  ? 26  ASN A CB  1 
ATOM   191   C  CG  . ASN A  1 27  ? -77.334  -57.738 107.529 1.00 99.51  ? 26  ASN A CG  1 
ATOM   192   O  OD1 . ASN A  1 27  ? -77.614  -58.927 107.401 1.00 104.66 ? 26  ASN A OD1 1 
ATOM   193   N  ND2 . ASN A  1 27  ? -77.252  -57.153 108.714 1.00 100.38 ? 26  ASN A ND2 1 
ATOM   194   N  N   . GLY A  1 28  ? -76.700  -59.400 103.537 1.00 71.39  ? 27  GLY A N   1 
ATOM   195   C  CA  . GLY A  1 28  ? -75.778  -60.248 102.789 1.00 67.28  ? 27  GLY A CA  1 
ATOM   196   C  C   . GLY A  1 28  ? -75.178  -59.508 101.590 1.00 62.24  ? 27  GLY A C   1 
ATOM   197   O  O   . GLY A  1 28  ? -75.340  -58.296 101.445 1.00 55.58  ? 27  GLY A O   1 
ATOM   198   N  N   . PRO A  1 29  ? -74.464  -60.214 100.686 1.00 56.79  ? 28  PRO A N   1 
ATOM   199   C  CA  . PRO A  1 29  ? -73.790  -59.557 99.569  1.00 54.33  ? 28  PRO A CA  1 
ATOM   200   C  C   . PRO A  1 29  ? -74.792  -59.165 98.475  1.00 51.53  ? 28  PRO A C   1 
ATOM   201   O  O   . PRO A  1 29  ? -75.861  -59.783 98.362  1.00 44.57  ? 28  PRO A O   1 
ATOM   202   C  CB  . PRO A  1 29  ? -72.801  -60.622 99.080  1.00 55.49  ? 28  PRO A CB  1 
ATOM   203   C  CG  . PRO A  1 29  ? -73.480  -61.937 99.410  1.00 55.53  ? 28  PRO A CG  1 
ATOM   204   C  CD  . PRO A  1 29  ? -74.272  -61.674 100.679 1.00 54.86  ? 28  PRO A CD  1 
ATOM   205   N  N   . VAL A  1 30  ? -74.434  -58.131 97.701  1.00 50.03  ? 29  VAL A N   1 
ATOM   206   C  CA  . VAL A  1 30  ? -75.263  -57.618 96.614  1.00 44.93  ? 29  VAL A CA  1 
ATOM   207   C  C   . VAL A  1 30  ? -74.672  -58.148 95.304  1.00 43.55  ? 29  VAL A C   1 
ATOM   208   O  O   . VAL A  1 30  ? -73.496  -57.933 95.021  1.00 42.76  ? 29  VAL A O   1 
ATOM   209   C  CB  . VAL A  1 30  ? -75.321  -56.077 96.633  1.00 45.62  ? 29  VAL A CB  1 
ATOM   210   C  CG1 . VAL A  1 30  ? -76.176  -55.533 95.498  1.00 41.58  ? 29  VAL A CG1 1 
ATOM   211   C  CG2 . VAL A  1 30  ? -75.832  -55.538 97.967  1.00 44.27  ? 29  VAL A CG2 1 
ATOM   212   N  N   . LYS A  1 31  ? -75.483  -58.891 94.550  1.00 42.08  ? 30  LYS A N   1 
ATOM   213   C  CA  . LYS A  1 31  ? -75.178  -59.260 93.178  1.00 49.61  ? 30  LYS A CA  1 
ATOM   214   C  C   . LYS A  1 31  ? -75.417  -58.025 92.294  1.00 44.52  ? 30  LYS A C   1 
ATOM   215   O  O   . LYS A  1 31  ? -76.455  -57.392 92.401  1.00 36.46  ? 30  LYS A O   1 
ATOM   216   C  CB  . LYS A  1 31  ? -76.047  -60.445 92.732  1.00 57.83  ? 30  LYS A CB  1 
ATOM   217   C  CG  . LYS A  1 31  ? -75.329  -61.783 92.602  1.00 68.09  ? 30  LYS A CG  1 
ATOM   218   C  CD  . LYS A  1 31  ? -75.089  -62.206 91.154  1.00 76.66  ? 30  LYS A CD  1 
ATOM   219   C  CE  . LYS A  1 31  ? -76.324  -62.790 90.494  1.00 80.53  ? 30  LYS A CE  1 
ATOM   220   N  NZ  . LYS A  1 31  ? -76.145  -62.994 89.034  1.00 83.51  ? 30  LYS A NZ  1 
ATOM   221   N  N   . VAL A  1 32  ? -74.426  -57.687 91.467  1.00 42.00  ? 31  VAL A N   1 
ATOM   222   C  CA  . VAL A  1 32  ? -74.485  -56.548 90.536  1.00 40.59  ? 31  VAL A CA  1 
ATOM   223   C  C   . VAL A  1 32  ? -74.197  -57.084 89.133  1.00 40.17  ? 31  VAL A C   1 
ATOM   224   O  O   . VAL A  1 32  ? -73.136  -57.665 88.908  1.00 40.72  ? 31  VAL A O   1 
ATOM   225   C  CB  . VAL A  1 32  ? -73.497  -55.433 90.938  1.00 40.03  ? 31  VAL A CB  1 
ATOM   226   C  CG1 . VAL A  1 32  ? -73.652  -54.185 90.066  1.00 38.72  ? 31  VAL A CG1 1 
ATOM   227   C  CG2 . VAL A  1 32  ? -73.633  -55.065 92.408  1.00 40.73  ? 31  VAL A CG2 1 
ATOM   228   N  N   . TRP A  1 33  ? -75.140  -56.908 88.197  1.00 39.68  ? 32  TRP A N   1 
ATOM   229   C  CA  . TRP A  1 33  ? -74.929  -57.425 86.855  1.00 38.96  ? 32  TRP A CA  1 
ATOM   230   C  C   . TRP A  1 33  ? -75.701  -56.618 85.809  1.00 41.06  ? 32  TRP A C   1 
ATOM   231   O  O   . TRP A  1 33  ? -76.753  -56.052 86.075  1.00 36.08  ? 32  TRP A O   1 
ATOM   232   C  CB  . TRP A  1 33  ? -75.311  -58.907 86.770  1.00 38.26  ? 32  TRP A CB  1 
ATOM   233   C  CG  . TRP A  1 33  ? -76.786  -59.139 86.661  1.00 38.57  ? 32  TRP A CG  1 
ATOM   234   C  CD1 . TRP A  1 33  ? -77.511  -59.347 85.526  1.00 39.25  ? 32  TRP A CD1 1 
ATOM   235   C  CD2 . TRP A  1 33  ? -77.723  -59.155 87.749  1.00 37.93  ? 32  TRP A CD2 1 
ATOM   236   N  NE1 . TRP A  1 33  ? -78.836  -59.497 85.838  1.00 42.46  ? 32  TRP A NE1 1 
ATOM   237   C  CE2 . TRP A  1 33  ? -78.992  -59.379 87.194  1.00 39.54  ? 32  TRP A CE2 1 
ATOM   238   C  CE3 . TRP A  1 33  ? -77.604  -58.991 89.131  1.00 40.67  ? 32  TRP A CE3 1 
ATOM   239   C  CZ2 . TRP A  1 33  ? -80.138  -59.456 87.980  1.00 44.42  ? 32  TRP A CZ2 1 
ATOM   240   C  CZ3 . TRP A  1 33  ? -78.736  -59.059 89.907  1.00 42.63  ? 32  TRP A CZ3 1 
ATOM   241   C  CH2 . TRP A  1 33  ? -79.984  -59.297 89.336  1.00 43.43  ? 32  TRP A CH2 1 
ATOM   242   N  N   . GLY A  1 34  ? -75.174  -56.663 84.585  1.00 39.06  ? 33  GLY A N   1 
ATOM   243   C  CA  . GLY A  1 34  ? -75.816  -56.076 83.445  1.00 37.68  ? 33  GLY A CA  1 
ATOM   244   C  C   . GLY A  1 34  ? -74.805  -55.785 82.362  1.00 37.56  ? 33  GLY A C   1 
ATOM   245   O  O   . GLY A  1 34  ? -73.809  -56.481 82.245  1.00 35.04  ? 33  GLY A O   1 
ATOM   246   N  N   . SER A  1 35  ? -75.074  -54.729 81.597  1.00 35.98  ? 34  SER A N   1 
ATOM   247   C  CA  . SER A  1 35  ? -74.366  -54.432 80.399  1.00 38.20  ? 34  SER A CA  1 
ATOM   248   C  C   . SER A  1 35  ? -74.278  -52.912 80.212  1.00 38.03  ? 34  SER A C   1 
ATOM   249   O  O   . SER A  1 35  ? -75.260  -52.204 80.441  1.00 34.63  ? 34  SER A O   1 
ATOM   250   C  CB  . SER A  1 35  ? -75.052  -55.090 79.246  1.00 42.64  ? 34  SER A CB  1 
ATOM   251   O  OG  . SER A  1 35  ? -74.117  -55.326 78.222  1.00 54.14  ? 34  SER A OG  1 
ATOM   252   N  N   . ILE A  1 36  ? -73.084  -52.429 79.847  1.00 35.22  ? 35  ILE A N   1 
ATOM   253   C  CA  . ILE A  1 36  ? -72.840  -51.053 79.442  1.00 33.41  ? 35  ILE A CA  1 
ATOM   254   C  C   . ILE A  1 36  ? -72.201  -51.070 78.054  1.00 37.11  ? 35  ILE A C   1 
ATOM   255   O  O   . ILE A  1 36  ? -71.228  -51.799 77.850  1.00 40.28  ? 35  ILE A O   1 
ATOM   256   C  CB  . ILE A  1 36  ? -71.910  -50.337 80.431  1.00 34.31  ? 35  ILE A CB  1 
ATOM   257   C  CG1 . ILE A  1 36  ? -72.329  -50.568 81.888  1.00 34.16  ? 35  ILE A CG1 1 
ATOM   258   C  CG2 . ILE A  1 36  ? -71.811  -48.860 80.072  1.00 31.74  ? 35  ILE A CG2 1 
ATOM   259   C  CD1 . ILE A  1 36  ? -71.429  -49.915 82.907  1.00 34.35  ? 35  ILE A CD1 1 
ATOM   260   N  N   . LYS A  1 37  ? -72.719  -50.253 77.131  1.00 32.02  ? 36  LYS A N   1 
ATOM   261   C  CA  . LYS A  1 37  ? -72.146  -50.140 75.794  1.00 32.44  ? 36  LYS A CA  1 
ATOM   262   C  C   . LYS A  1 37  ? -71.679  -48.706 75.541  1.00 30.11  ? 36  LYS A C   1 
ATOM   263   O  O   . LYS A  1 37  ? -71.896  -47.831 76.347  1.00 30.70  ? 36  LYS A O   1 
ATOM   264   C  CB  . LYS A  1 37  ? -73.152  -50.617 74.749  1.00 35.52  ? 36  LYS A CB  1 
ATOM   265   C  CG  . LYS A  1 37  ? -74.410  -49.783 74.639  1.00 37.12  ? 36  LYS A CG  1 
ATOM   266   C  CD  . LYS A  1 37  ? -75.393  -50.425 73.699  1.00 41.98  ? 36  LYS A CD  1 
ATOM   267   C  CE  . LYS A  1 37  ? -76.601  -49.558 73.432  1.00 40.73  ? 36  LYS A CE  1 
ATOM   268   N  NZ  . LYS A  1 37  ? -77.641  -50.337 72.729  1.00 43.27  ? 36  LYS A NZ  1 
ATOM   269   N  N   . GLY A  1 38  ? -70.997  -48.504 74.410  1.00 29.10  ? 37  GLY A N   1 
ATOM   270   C  CA  . GLY A  1 38  ? -70.464  -47.210 74.031  1.00 29.92  ? 37  GLY A CA  1 
ATOM   271   C  C   . GLY A  1 38  ? -69.177  -46.850 74.744  1.00 29.36  ? 37  GLY A C   1 
ATOM   272   O  O   . GLY A  1 38  ? -68.772  -45.659 74.737  1.00 28.36  ? 37  GLY A O   1 
ATOM   273   N  N   . LEU A  1 39  ? -68.482  -47.853 75.308  1.00 30.66  ? 38  LEU A N   1 
ATOM   274   C  CA  . LEU A  1 39  ? -67.227  -47.604 76.042  1.00 33.05  ? 38  LEU A CA  1 
ATOM   275   C  C   . LEU A  1 39  ? -66.040  -47.880 75.120  1.00 32.53  ? 38  LEU A C   1 
ATOM   276   O  O   . LEU A  1 39  ? -66.158  -48.639 74.186  1.00 33.26  ? 38  LEU A O   1 
ATOM   277   C  CB  . LEU A  1 39  ? -67.135  -48.508 77.278  1.00 35.58  ? 38  LEU A CB  1 
ATOM   278   C  CG  . LEU A  1 39  ? -68.143  -48.232 78.387  1.00 36.32  ? 38  LEU A CG  1 
ATOM   279   C  CD1 . LEU A  1 39  ? -68.193  -49.402 79.362  1.00 37.46  ? 38  LEU A CD1 1 
ATOM   280   C  CD2 . LEU A  1 39  ? -67.805  -46.936 79.105  1.00 36.73  ? 38  LEU A CD2 1 
ATOM   281   N  N   . THR A  1 40  ? -64.899  -47.246 75.409  1.00 35.28  ? 39  THR A N   1 
ATOM   282   C  CA  . THR A  1 40  ? -63.615  -47.654 74.819  1.00 36.51  ? 39  THR A CA  1 
ATOM   283   C  C   . THR A  1 40  ? -63.208  -49.005 75.428  1.00 36.11  ? 39  THR A C   1 
ATOM   284   O  O   . THR A  1 40  ? -63.434  -49.259 76.616  1.00 33.81  ? 39  THR A O   1 
ATOM   285   C  CB  . THR A  1 40  ? -62.527  -46.593 75.035  1.00 37.95  ? 39  THR A CB  1 
ATOM   286   O  OG1 . THR A  1 40  ? -62.407  -46.296 76.426  1.00 38.63  ? 39  THR A OG1 1 
ATOM   287   C  CG2 . THR A  1 40  ? -62.809  -45.297 74.304  1.00 38.89  ? 39  THR A CG2 1 
ATOM   288   N  N   . GLU A  1 41  ? -62.627  -49.875 74.598  1.00 36.99  ? 40  GLU A N   1 
ATOM   289   C  CA  . GLU A  1 41  ? -62.085  -51.173 75.041  1.00 40.15  ? 40  GLU A CA  1 
ATOM   290   C  C   . GLU A  1 41  ? -61.151  -50.929 76.226  1.00 37.77  ? 40  GLU A C   1 
ATOM   291   O  O   . GLU A  1 41  ? -60.361  -49.982 76.210  1.00 41.53  ? 40  GLU A O   1 
ATOM   292   C  CB  . GLU A  1 41  ? -61.333  -51.852 73.893  1.00 43.83  ? 40  GLU A CB  1 
ATOM   293   C  CG  . GLU A  1 41  ? -60.805  -53.236 74.234  1.00 46.73  ? 40  GLU A CG  1 
ATOM   294   C  CD  . GLU A  1 41  ? -60.064  -53.903 73.086  1.00 52.92  ? 40  GLU A CD  1 
ATOM   295   O  OE1 . GLU A  1 41  ? -59.888  -53.244 72.043  1.00 61.56  ? 40  GLU A OE1 1 
ATOM   296   O  OE2 . GLU A  1 41  ? -59.676  -55.076 73.231  1.00 55.58  ? 40  GLU A OE2 1 
ATOM   297   N  N   . GLY A  1 42  ? -61.250  -51.776 77.250  1.00 40.45  ? 41  GLY A N   1 
ATOM   298   C  CA  . GLY A  1 42  ? -60.398  -51.638 78.440  1.00 40.57  ? 41  GLY A CA  1 
ATOM   299   C  C   . GLY A  1 42  ? -61.197  -51.365 79.705  1.00 40.37  ? 41  GLY A C   1 
ATOM   300   O  O   . GLY A  1 42  ? -62.431  -51.491 79.731  1.00 38.27  ? 41  GLY A O   1 
ATOM   301   N  N   . LEU A  1 43  ? -60.470  -50.972 80.754  1.00 40.81  ? 42  LEU A N   1 
ATOM   302   C  CA  . LEU A  1 43  ? -60.987  -50.879 82.114  1.00 40.62  ? 42  LEU A CA  1 
ATOM   303   C  C   . LEU A  1 43  ? -61.564  -49.487 82.351  1.00 37.29  ? 42  LEU A C   1 
ATOM   304   O  O   . LEU A  1 43  ? -60.972  -48.495 81.945  1.00 37.48  ? 42  LEU A O   1 
ATOM   305   C  CB  . LEU A  1 43  ? -59.847  -51.146 83.102  1.00 43.74  ? 42  LEU A CB  1 
ATOM   306   C  CG  . LEU A  1 43  ? -59.233  -52.544 83.016  1.00 46.38  ? 42  LEU A CG  1 
ATOM   307   C  CD1 . LEU A  1 43  ? -57.876  -52.571 83.691  1.00 52.20  ? 42  LEU A CD1 1 
ATOM   308   C  CD2 . LEU A  1 43  ? -60.145  -53.575 83.639  1.00 48.92  ? 42  LEU A CD2 1 
ATOM   309   N  N   . HIS A  1 44  ? -62.690  -49.443 83.069  1.00 34.15  ? 43  HIS A N   1 
ATOM   310   C  CA  . HIS A  1 44  ? -63.384  -48.206 83.396  1.00 34.72  ? 43  HIS A CA  1 
ATOM   311   C  C   . HIS A  1 44  ? -63.793  -48.232 84.870  1.00 32.94  ? 43  HIS A C   1 
ATOM   312   O  O   . HIS A  1 44  ? -64.427  -49.181 85.302  1.00 34.34  ? 43  HIS A O   1 
ATOM   313   C  CB  . HIS A  1 44  ? -64.607  -48.043 82.484  1.00 34.88  ? 43  HIS A CB  1 
ATOM   314   C  CG  . HIS A  1 44  ? -64.262  -47.841 81.047  1.00 32.45  ? 43  HIS A CG  1 
ATOM   315   N  ND1 . HIS A  1 44  ? -63.985  -46.590 80.527  1.00 36.60  ? 43  HIS A ND1 1 
ATOM   316   C  CD2 . HIS A  1 44  ? -64.139  -48.719 80.029  1.00 35.75  ? 43  HIS A CD2 1 
ATOM   317   C  CE1 . HIS A  1 44  ? -63.718  -46.706 79.239  1.00 36.18  ? 43  HIS A CE1 1 
ATOM   318   N  NE2 . HIS A  1 44  ? -63.810  -48.015 78.905  1.00 33.61  ? 43  HIS A NE2 1 
ATOM   319   N  N   . GLY A  1 45  ? -63.448  -47.171 85.604  1.00 35.47  ? 44  GLY A N   1 
ATOM   320   C  CA  . GLY A  1 45  ? -63.894  -46.968 86.991  1.00 35.80  ? 44  GLY A CA  1 
ATOM   321   C  C   . GLY A  1 45  ? -65.403  -47.103 87.103  1.00 36.45  ? 44  GLY A C   1 
ATOM   322   O  O   . GLY A  1 45  ? -66.124  -46.726 86.186  1.00 35.68  ? 44  GLY A O   1 
ATOM   323   N  N   . PHE A  1 46  ? -65.878  -47.664 88.223  1.00 36.12  ? 45  PHE A N   1 
ATOM   324   C  CA  . PHE A  1 46  ? -67.282  -48.040 88.394  1.00 34.70  ? 45  PHE A CA  1 
ATOM   325   C  C   . PHE A  1 46  ? -67.643  -47.867 89.869  1.00 38.21  ? 45  PHE A C   1 
ATOM   326   O  O   . PHE A  1 46  ? -67.249  -48.685 90.710  1.00 38.28  ? 45  PHE A O   1 
ATOM   327   C  CB  . PHE A  1 46  ? -67.480  -49.463 87.873  1.00 34.34  ? 45  PHE A CB  1 
ATOM   328   C  CG  . PHE A  1 46  ? -68.897  -49.969 87.769  1.00 38.08  ? 45  PHE A CG  1 
ATOM   329   C  CD1 . PHE A  1 46  ? -69.810  -49.382 86.903  1.00 38.95  ? 45  PHE A CD1 1 
ATOM   330   C  CD2 . PHE A  1 46  ? -69.300  -51.092 88.475  1.00 38.25  ? 45  PHE A CD2 1 
ATOM   331   C  CE1 . PHE A  1 46  ? -71.095  -49.888 86.775  1.00 39.94  ? 45  PHE A CE1 1 
ATOM   332   C  CE2 . PHE A  1 46  ? -70.586  -51.594 88.347  1.00 38.63  ? 45  PHE A CE2 1 
ATOM   333   C  CZ  . PHE A  1 46  ? -71.486  -50.987 87.503  1.00 40.39  ? 45  PHE A CZ  1 
ATOM   334   N  N   . HIS A  1 47  ? -68.366  -46.787 90.174  1.00 36.29  ? 46  HIS A N   1 
ATOM   335   C  CA  . HIS A  1 47  ? -68.547  -46.345 91.535  1.00 38.11  ? 46  HIS A CA  1 
ATOM   336   C  C   . HIS A  1 47  ? -69.985  -45.909 91.795  1.00 37.84  ? 46  HIS A C   1 
ATOM   337   O  O   . HIS A  1 47  ? -70.702  -45.451 90.893  1.00 35.70  ? 46  HIS A O   1 
ATOM   338   C  CB  . HIS A  1 47  ? -67.671  -45.134 91.879  1.00 39.70  ? 46  HIS A CB  1 
ATOM   339   C  CG  . HIS A  1 47  ? -66.255  -45.237 91.437  1.00 39.46  ? 46  HIS A CG  1 
ATOM   340   N  ND1 . HIS A  1 47  ? -65.564  -44.155 90.915  1.00 40.64  ? 46  HIS A ND1 1 
ATOM   341   C  CD2 . HIS A  1 47  ? -65.388  -46.270 91.472  1.00 41.91  ? 46  HIS A CD2 1 
ATOM   342   C  CE1 . HIS A  1 47  ? -64.331  -44.535 90.634  1.00 41.93  ? 46  HIS A CE1 1 
ATOM   343   N  NE2 . HIS A  1 47  ? -64.200  -45.824 90.970  1.00 40.35  ? 46  HIS A NE2 1 
ATOM   344   N  N   . VAL A  1 48  ? -70.352  -46.005 93.075  1.00 36.56  ? 47  VAL A N   1 
ATOM   345   C  CA  . VAL A  1 48  ? -71.508  -45.364 93.619  1.00 32.80  ? 47  VAL A CA  1 
ATOM   346   C  C   . VAL A  1 48  ? -71.064  -44.035 94.214  1.00 35.96  ? 47  VAL A C   1 
ATOM   347   O  O   . VAL A  1 48  ? -70.206  -44.000 95.118  1.00 35.04  ? 47  VAL A O   1 
ATOM   348   C  CB  . VAL A  1 48  ? -72.193  -46.219 94.695  1.00 33.11  ? 47  VAL A CB  1 
ATOM   349   C  CG1 . VAL A  1 48  ? -73.393  -45.489 95.264  1.00 33.96  ? 47  VAL A CG1 1 
ATOM   350   C  CG2 . VAL A  1 48  ? -72.583  -47.590 94.173  1.00 34.12  ? 47  VAL A CG2 1 
ATOM   351   N  N   . HIS A  1 49  ? -71.678  -42.957 93.716  1.00 34.94  ? 48  HIS A N   1 
ATOM   352   C  CA  . HIS A  1 49  ? -71.491  -41.635 94.236  1.00 33.06  ? 48  HIS A CA  1 
ATOM   353   C  C   . HIS A  1 49  ? -72.669  -41.288 95.140  1.00 34.19  ? 48  HIS A C   1 
ATOM   354   O  O   . HIS A  1 49  ? -73.724  -41.902 95.056  1.00 32.14  ? 48  HIS A O   1 
ATOM   355   C  CB  . HIS A  1 49  ? -71.313  -40.633 93.091  1.00 33.08  ? 48  HIS A CB  1 
ATOM   356   C  CG  . HIS A  1 49  ? -70.008  -40.771 92.381  1.00 31.38  ? 48  HIS A CG  1 
ATOM   357   N  ND1 . HIS A  1 49  ? -69.122  -39.720 92.279  1.00 34.90  ? 48  HIS A ND1 1 
ATOM   358   C  CD2 . HIS A  1 49  ? -69.420  -41.821 91.768  1.00 32.68  ? 48  HIS A CD2 1 
ATOM   359   C  CE1 . HIS A  1 49  ? -68.072  -40.095 91.576  1.00 33.87  ? 48  HIS A CE1 1 
ATOM   360   N  NE2 . HIS A  1 49  ? -68.207  -41.386 91.276  1.00 33.61  ? 48  HIS A NE2 1 
ATOM   361   N  N   . GLU A  1 50  ? -72.471  -40.251 95.958  1.00 36.29  ? 49  GLU A N   1 
ATOM   362   C  CA  . GLU A  1 50  ? -73.230  -40.072 97.182  1.00 39.78  ? 49  GLU A CA  1 
ATOM   363   C  C   . GLU A  1 50  ? -74.692  -39.682 96.917  1.00 37.71  ? 49  GLU A C   1 
ATOM   364   O  O   . GLU A  1 50  ? -75.590  -40.168 97.615  1.00 33.99  ? 49  GLU A O   1 
ATOM   365   C  CB  . GLU A  1 50  ? -72.593  -38.996 98.056  1.00 42.36  ? 49  GLU A CB  1 
ATOM   366   C  CG  . GLU A  1 50  ? -73.460  -38.699 99.263  1.00 49.42  ? 49  GLU A CG  1 
ATOM   367   C  CD  . GLU A  1 50  ? -72.757  -38.003 100.405 1.00 52.75  ? 49  GLU A CD  1 
ATOM   368   O  OE1 . GLU A  1 50  ? -71.726  -37.348 100.148 1.00 55.22  ? 49  GLU A OE1 1 
ATOM   369   O  OE2 . GLU A  1 50  ? -73.268  -38.105 101.539 1.00 61.04  ? 49  GLU A OE2 1 
ATOM   370   N  N   . PHE A  1 51  ? -74.903  -38.740 95.990  1.00 33.66  ? 50  PHE A N   1 
ATOM   371   C  CA  . PHE A  1 51  ? -76.208  -38.145 95.740  1.00 33.58  ? 50  PHE A CA  1 
ATOM   372   C  C   . PHE A  1 51  ? -76.790  -38.702 94.433  1.00 35.37  ? 50  PHE A C   1 
ATOM   373   O  O   . PHE A  1 51  ? -76.058  -38.832 93.427  1.00 31.65  ? 50  PHE A O   1 
ATOM   374   C  CB  . PHE A  1 51  ? -76.080  -36.625 95.648  1.00 36.94  ? 50  PHE A CB  1 
ATOM   375   C  CG  . PHE A  1 51  ? -75.403  -35.989 96.834  1.00 39.67  ? 50  PHE A CG  1 
ATOM   376   C  CD1 . PHE A  1 51  ? -75.957  -36.099 98.104  1.00 43.57  ? 50  PHE A CD1 1 
ATOM   377   C  CD2 . PHE A  1 51  ? -74.213  -35.289 96.688  1.00 41.34  ? 50  PHE A CD2 1 
ATOM   378   C  CE1 . PHE A  1 51  ? -75.323  -35.534 99.205  1.00 45.55  ? 50  PHE A CE1 1 
ATOM   379   C  CE2 . PHE A  1 51  ? -73.580  -34.724 97.790  1.00 43.85  ? 50  PHE A CE2 1 
ATOM   380   C  CZ  . PHE A  1 51  ? -74.137  -34.849 99.045  1.00 43.50  ? 50  PHE A CZ  1 
ATOM   381   N  N   . GLY A  1 52  ? -78.102  -38.983 94.450  1.00 31.09  ? 51  GLY A N   1 
ATOM   382   C  CA  . GLY A  1 52  ? -78.892  -39.257 93.250  1.00 31.44  ? 51  GLY A CA  1 
ATOM   383   C  C   . GLY A  1 52  ? -79.418  -37.957 92.657  1.00 30.98  ? 51  GLY A C   1 
ATOM   384   O  O   . GLY A  1 52  ? -80.607  -37.780 92.455  1.00 31.33  ? 51  GLY A O   1 
ATOM   385   N  N   . ASP A  1 53  ? -78.506  -37.004 92.471  1.00 31.45  ? 52  ASP A N   1 
ATOM   386   C  CA  . ASP A  1 53  ? -78.811  -35.709 91.954  1.00 31.55  ? 52  ASP A CA  1 
ATOM   387   C  C   . ASP A  1 53  ? -78.128  -35.585 90.587  1.00 31.68  ? 52  ASP A C   1 
ATOM   388   O  O   . ASP A  1 53  ? -76.902  -35.522 90.493  1.00 28.76  ? 52  ASP A O   1 
ATOM   389   C  CB  . ASP A  1 53  ? -78.353  -34.646 92.944  1.00 32.02  ? 52  ASP A CB  1 
ATOM   390   C  CG  . ASP A  1 53  ? -78.622  -33.220 92.508  1.00 32.78  ? 52  ASP A CG  1 
ATOM   391   O  OD1 . ASP A  1 53  ? -78.501  -32.370 93.364  1.00 34.62  ? 52  ASP A OD1 1 
ATOM   392   O  OD2 . ASP A  1 53  ? -78.947  -32.976 91.308  1.00 31.69  ? 52  ASP A OD2 1 
ATOM   393   N  N   . ASN A  1 54  ? -78.946  -35.602 89.533  1.00 33.78  ? 53  ASN A N   1 
ATOM   394   C  CA  . ASN A  1 54  ? -78.496  -35.573 88.152  1.00 34.93  ? 53  ASN A CA  1 
ATOM   395   C  C   . ASN A  1 54  ? -78.962  -34.254 87.510  1.00 32.17  ? 53  ASN A C   1 
ATOM   396   O  O   . ASN A  1 54  ? -79.109  -34.161 86.308  1.00 32.84  ? 53  ASN A O   1 
ATOM   397   C  CB  . ASN A  1 54  ? -78.959  -36.847 87.420  1.00 39.23  ? 53  ASN A CB  1 
ATOM   398   C  CG  A ASN A  1 54  ? -78.249  -38.112 87.884  0.60 44.08  ? 53  ASN A CG  1 
ATOM   399   C  CG  B ASN A  1 54  ? -78.265  -38.122 87.876  0.40 42.49  ? 53  ASN A CG  1 
ATOM   400   O  OD1 A ASN A  1 54  ? -78.710  -39.223 87.622  0.60 44.86  ? 53  ASN A OD1 1 
ATOM   401   O  OD1 B ASN A  1 54  ? -78.367  -39.159 87.218  0.40 44.02  ? 53  ASN A OD1 1 
ATOM   402   N  ND2 A ASN A  1 54  ? -77.116  -37.975 88.563  0.60 46.17  ? 53  ASN A ND2 1 
ATOM   403   N  ND2 B ASN A  1 54  ? -77.556  -38.077 88.995  0.40 43.99  ? 53  ASN A ND2 1 
ATOM   404   N  N   . THR A  1 55  ? -79.162  -33.213 88.322  1.00 30.99  ? 54  THR A N   1 
ATOM   405   C  CA  . THR A  1 55  ? -79.625  -31.931 87.829  1.00 33.31  ? 54  THR A CA  1 
ATOM   406   C  C   . THR A  1 55  ? -78.497  -31.168 87.112  1.00 36.18  ? 54  THR A C   1 
ATOM   407   O  O   . THR A  1 55  ? -78.779  -30.224 86.390  1.00 33.75  ? 54  THR A O   1 
ATOM   408   C  CB  . THR A  1 55  ? -80.186  -31.040 88.939  1.00 33.63  ? 54  THR A CB  1 
ATOM   409   O  OG1 . THR A  1 55  ? -79.204  -30.844 89.955  1.00 34.30  ? 54  THR A OG1 1 
ATOM   410   C  CG2 . THR A  1 55  ? -81.447  -31.602 89.554  1.00 34.39  ? 54  THR A CG2 1 
ATOM   411   N  N   . ALA A  1 56  ? -77.237  -31.574 87.319  1.00 33.38  ? 55  ALA A N   1 
ATOM   412   C  CA  . ALA A  1 56  ? -76.090  -31.073 86.548  1.00 34.88  ? 55  ALA A CA  1 
ATOM   413   C  C   . ALA A  1 56  ? -75.301  -32.268 86.013  1.00 36.40  ? 55  ALA A C   1 
ATOM   414   O  O   . ALA A  1 56  ? -74.149  -32.452 86.361  1.00 41.40  ? 55  ALA A O   1 
ATOM   415   C  CB  . ALA A  1 56  ? -75.214  -30.192 87.407  1.00 35.10  ? 55  ALA A CB  1 
ATOM   416   N  N   . GLY A  1 57  ? -75.962  -33.100 85.213  1.00 36.90  ? 56  GLY A N   1 
ATOM   417   C  CA  . GLY A  1 57  ? -75.401  -34.353 84.728  1.00 38.86  ? 56  GLY A CA  1 
ATOM   418   C  C   . GLY A  1 57  ? -74.853  -35.196 85.865  1.00 36.23  ? 56  GLY A C   1 
ATOM   419   O  O   . GLY A  1 57  ? -75.426  -35.246 86.931  1.00 36.58  ? 56  GLY A O   1 
ATOM   420   N  N   . CYS A  1 58  ? -73.677  -35.787 85.651  1.00 37.16  ? 57  CYS A N   1 
ATOM   421   C  CA  . CYS A  1 58  ? -73.074  -36.693 86.600  1.00 34.89  ? 57  CYS A CA  1 
ATOM   422   C  C   . CYS A  1 58  ? -72.318  -35.903 87.688  1.00 35.54  ? 57  CYS A C   1 
ATOM   423   O  O   . CYS A  1 58  ? -71.985  -36.472 88.744  1.00 35.73  ? 57  CYS A O   1 
ATOM   424   C  CB  . CYS A  1 58  ? -72.197  -37.695 85.851  1.00 38.39  ? 57  CYS A CB  1 
ATOM   425   S  SG  . CYS A  1 58  ? -73.125  -38.709 84.658  1.00 41.09  ? 57  CYS A SG  1 
ATOM   426   N  N   . THR A  1 59  ? -72.064  -34.600 87.459  1.00 31.08  ? 58  THR A N   1 
ATOM   427   C  CA  . THR A  1 59  ? -71.266  -33.777 88.392  1.00 33.20  ? 58  THR A CA  1 
ATOM   428   C  C   . THR A  1 59  ? -71.997  -33.611 89.725  1.00 33.57  ? 58  THR A C   1 
ATOM   429   O  O   . THR A  1 59  ? -71.386  -33.647 90.789  1.00 31.68  ? 58  THR A O   1 
ATOM   430   C  CB  . THR A  1 59  ? -70.912  -32.405 87.800  1.00 33.64  ? 58  THR A CB  1 
ATOM   431   O  OG1 . THR A  1 59  ? -70.038  -32.683 86.715  1.00 35.59  ? 58  THR A OG1 1 
ATOM   432   C  CG2 . THR A  1 59  ? -70.229  -31.467 88.770  1.00 34.12  ? 58  THR A CG2 1 
ATOM   433   N  N   . SER A  1 60  ? -73.320  -33.460 89.661  1.00 34.03  ? 59  SER A N   1 
ATOM   434   C  CA  . SER A  1 60  ? -74.117  -33.181 90.852  1.00 33.39  ? 59  SER A CA  1 
ATOM   435   C  C   . SER A  1 60  ? -74.284  -34.440 91.723  1.00 31.32  ? 59  SER A C   1 
ATOM   436   O  O   . SER A  1 60  ? -74.803  -34.356 92.818  1.00 34.72  ? 59  SER A O   1 
ATOM   437   C  CB  . SER A  1 60  ? -75.429  -32.560 90.455  1.00 32.24  ? 59  SER A CB  1 
ATOM   438   O  OG  . SER A  1 60  ? -76.006  -33.277 89.377  1.00 32.23  ? 59  SER A OG  1 
ATOM   439   N  N   . ALA A  1 61  ? -73.816  -35.601 91.251  1.00 30.84  ? 60  ALA A N   1 
ATOM   440   C  CA  . ALA A  1 61  ? -73.749  -36.834 92.066  1.00 30.94  ? 60  ALA A CA  1 
ATOM   441   C  C   . ALA A  1 61  ? -72.763  -36.705 93.251  1.00 33.71  ? 60  ALA A C   1 
ATOM   442   O  O   . ALA A  1 61  ? -72.753  -37.554 94.140  1.00 32.84  ? 60  ALA A O   1 
ATOM   443   C  CB  . ALA A  1 61  ? -73.376  -38.003 91.195  1.00 30.93  ? 60  ALA A CB  1 
ATOM   444   N  N   . GLY A  1 62  ? -71.922  -35.661 93.258  1.00 35.29  ? 61  GLY A N   1 
ATOM   445   C  CA  . GLY A  1 62  ? -70.945  -35.442 94.307  1.00 36.63  ? 61  GLY A CA  1 
ATOM   446   C  C   . GLY A  1 62  ? -69.864  -36.524 94.327  1.00 38.53  ? 61  GLY A C   1 
ATOM   447   O  O   . GLY A  1 62  ? -69.606  -37.199 93.320  1.00 34.16  ? 61  GLY A O   1 
ATOM   448   N  N   . PRO A  1 63  ? -69.201  -36.727 95.489  1.00 41.67  ? 62  PRO A N   1 
ATOM   449   C  CA  . PRO A  1 63  ? -68.068  -37.648 95.582  1.00 42.64  ? 62  PRO A CA  1 
ATOM   450   C  C   . PRO A  1 63  ? -68.533  -39.101 95.735  1.00 40.37  ? 62  PRO A C   1 
ATOM   451   O  O   . PRO A  1 63  ? -69.725  -39.365 95.743  1.00 38.54  ? 62  PRO A O   1 
ATOM   452   C  CB  . PRO A  1 63  ? -67.343  -37.144 96.840  1.00 43.44  ? 62  PRO A CB  1 
ATOM   453   C  CG  . PRO A  1 63  ? -68.466  -36.642 97.723  1.00 42.44  ? 62  PRO A CG  1 
ATOM   454   C  CD  . PRO A  1 63  ? -69.507  -36.080 96.776  1.00 43.03  ? 62  PRO A CD  1 
ATOM   455   N  N   . HIS A  1 64  ? -67.575  -40.019 95.865  1.00 39.30  ? 63  HIS A N   1 
ATOM   456   C  CA  . HIS A  1 64  ? -67.872  -41.424 96.133  1.00 42.34  ? 63  HIS A CA  1 
ATOM   457   C  C   . HIS A  1 64  ? -68.699  -41.538 97.419  1.00 44.92  ? 63  HIS A C   1 
ATOM   458   O  O   . HIS A  1 64  ? -68.538  -40.738 98.338  1.00 40.59  ? 63  HIS A O   1 
ATOM   459   C  CB  . HIS A  1 64  ? -66.571  -42.225 96.182  1.00 45.17  ? 63  HIS A CB  1 
ATOM   460   C  CG  . HIS A  1 64  ? -65.904  -42.287 94.855  1.00 49.29  ? 63  HIS A CG  1 
ATOM   461   N  ND1 . HIS A  1 64  ? -64.776  -43.039 94.636  1.00 56.46  ? 63  HIS A ND1 1 
ATOM   462   C  CD2 . HIS A  1 64  ? -66.222  -41.701 93.675  1.00 54.29  ? 63  HIS A CD2 1 
ATOM   463   C  CE1 . HIS A  1 64  ? -64.413  -42.916 93.366  1.00 59.96  ? 63  HIS A CE1 1 
ATOM   464   N  NE2 . HIS A  1 64  ? -65.314  -42.113 92.732  1.00 56.54  ? 63  HIS A NE2 1 
ATOM   465   N  N   . PHE A  1 65  ? -69.643  -42.484 97.432  1.00 41.16  ? 64  PHE A N   1 
ATOM   466   C  CA  . PHE A  1 65  ? -70.419  -42.769 98.628  1.00 41.05  ? 64  PHE A CA  1 
ATOM   467   C  C   . PHE A  1 65  ? -69.485  -43.387 99.676  1.00 39.87  ? 64  PHE A C   1 
ATOM   468   O  O   . PHE A  1 65  ? -68.911  -44.452 99.414  1.00 41.30  ? 64  PHE A O   1 
ATOM   469   C  CB  . PHE A  1 65  ? -71.562  -43.722 98.304  1.00 38.57  ? 64  PHE A CB  1 
ATOM   470   C  CG  . PHE A  1 65  ? -72.377  -44.142 99.494  1.00 40.33  ? 64  PHE A CG  1 
ATOM   471   C  CD1 . PHE A  1 65  ? -72.690  -45.477 99.691  1.00 43.53  ? 64  PHE A CD1 1 
ATOM   472   C  CD2 . PHE A  1 65  ? -72.837  -43.204 100.403 1.00 41.09  ? 64  PHE A CD2 1 
ATOM   473   C  CE1 . PHE A  1 65  ? -73.467  -45.868 100.772 1.00 46.17  ? 64  PHE A CE1 1 
ATOM   474   C  CE2 . PHE A  1 65  ? -73.597  -43.598 101.493 1.00 46.54  ? 64  PHE A CE2 1 
ATOM   475   C  CZ  . PHE A  1 65  ? -73.907  -44.929 101.676 1.00 47.21  ? 64  PHE A CZ  1 
ATOM   476   N  N   . ASN A  1 66  ? -69.353  -42.707 100.828 1.00 45.42  ? 65  ASN A N   1 
ATOM   477   C  CA  . ASN A  1 66  ? -68.267  -42.946 101.804 1.00 50.57  ? 65  ASN A CA  1 
ATOM   478   C  C   . ASN A  1 66  ? -68.711  -42.562 103.216 1.00 52.60  ? 65  ASN A C   1 
ATOM   479   O  O   . ASN A  1 66  ? -68.160  -41.648 103.828 1.00 48.36  ? 65  ASN A O   1 
ATOM   480   C  CB  . ASN A  1 66  ? -67.000  -42.165 101.435 1.00 53.80  ? 65  ASN A CB  1 
ATOM   481   C  CG  . ASN A  1 66  ? -65.826  -42.425 102.364 1.00 56.29  ? 65  ASN A CG  1 
ATOM   482   O  OD1 . ASN A  1 66  ? -64.983  -41.550 102.562 1.00 56.10  ? 65  ASN A OD1 1 
ATOM   483   N  ND2 . ASN A  1 66  ? -65.757  -43.616 102.938 1.00 48.81  ? 65  ASN A ND2 1 
ATOM   484   N  N   . PRO A  1 67  ? -69.706  -43.254 103.806 1.00 54.72  ? 66  PRO A N   1 
ATOM   485   C  CA  . PRO A  1 67  ? -70.184  -42.883 105.142 1.00 59.46  ? 66  PRO A CA  1 
ATOM   486   C  C   . PRO A  1 67  ? -69.073  -42.973 106.216 1.00 63.11  ? 66  PRO A C   1 
ATOM   487   O  O   . PRO A  1 67  ? -69.097  -42.214 107.196 1.00 66.28  ? 66  PRO A O   1 
ATOM   488   C  CB  . PRO A  1 67  ? -71.357  -43.853 105.384 1.00 58.03  ? 66  PRO A CB  1 
ATOM   489   C  CG  . PRO A  1 67  ? -71.102  -45.021 104.436 1.00 60.36  ? 66  PRO A CG  1 
ATOM   490   C  CD  . PRO A  1 67  ? -70.392  -44.421 103.237 1.00 56.27  ? 66  PRO A CD  1 
ATOM   491   N  N   . LEU A  1 68  ? -68.075  -43.845 106.001 1.00 64.30  ? 67  LEU A N   1 
ATOM   492   C  CA  . LEU A  1 68  ? -67.021  -44.154 106.995 1.00 66.25  ? 67  LEU A CA  1 
ATOM   493   C  C   . LEU A  1 68  ? -65.848  -43.159 106.967 1.00 69.59  ? 67  LEU A C   1 
ATOM   494   O  O   . LEU A  1 68  ? -64.959  -43.261 107.813 1.00 75.32  ? 67  LEU A O   1 
ATOM   495   C  CB  . LEU A  1 68  ? -66.483  -45.565 106.733 1.00 62.94  ? 67  LEU A CB  1 
ATOM   496   C  CG  . LEU A  1 68  ? -67.499  -46.706 106.737 1.00 67.12  ? 67  LEU A CG  1 
ATOM   497   C  CD1 . LEU A  1 68  ? -66.794  -48.021 107.045 1.00 65.12  ? 67  LEU A CD1 1 
ATOM   498   C  CD2 . LEU A  1 68  ? -68.637  -46.458 107.721 1.00 69.58  ? 67  LEU A CD2 1 
ATOM   499   N  N   . SER A  1 69  ? -65.821  -42.223 106.009 1.00 72.30  ? 68  SER A N   1 
ATOM   500   C  CA  . SER A  1 69  ? -64.715  -41.244 105.865 1.00 74.49  ? 68  SER A CA  1 
ATOM   501   C  C   . SER A  1 69  ? -63.358  -41.966 105.793 1.00 75.17  ? 68  SER A C   1 
ATOM   502   O  O   . SER A  1 69  ? -62.393  -41.532 106.420 1.00 75.69  ? 68  SER A O   1 
ATOM   503   C  CB  . SER A  1 69  ? -64.719  -40.215 106.980 1.00 73.70  ? 68  SER A CB  1 
ATOM   504   O  OG  . SER A  1 69  ? -65.950  -39.511 107.036 1.00 72.19  ? 68  SER A OG  1 
ATOM   505   N  N   . ARG A  1 70  ? -63.298  -43.067 105.031 1.00 77.42  ? 69  ARG A N   1 
ATOM   506   C  CA  . ARG A  1 70  ? -62.050  -43.805 104.747 1.00 80.59  ? 69  ARG A CA  1 
ATOM   507   C  C   . ARG A  1 70  ? -61.441  -43.310 103.426 1.00 79.38  ? 69  ARG A C   1 
ATOM   508   O  O   . ARG A  1 70  ? -62.072  -42.560 102.688 1.00 77.62  ? 69  ARG A O   1 
ATOM   509   C  CB  . ARG A  1 70  ? -62.314  -45.315 104.717 1.00 80.86  ? 69  ARG A CB  1 
ATOM   510   C  CG  . ARG A  1 70  ? -63.204  -45.814 105.848 1.00 81.33  ? 69  ARG A CG  1 
ATOM   511   C  CD  . ARG A  1 70  ? -62.965  -47.271 106.193 1.00 82.53  ? 69  ARG A CD  1 
ATOM   512   N  NE  . ARG A  1 70  ? -61.592  -47.516 106.618 1.00 84.16  ? 69  ARG A NE  1 
ATOM   513   C  CZ  . ARG A  1 70  ? -61.078  -48.717 106.860 1.00 81.97  ? 69  ARG A CZ  1 
ATOM   514   N  NH1 . ARG A  1 70  ? -59.788  -48.838 107.127 1.00 79.55  ? 69  ARG A NH1 1 
ATOM   515   N  NH2 . ARG A  1 70  ? -61.852  -49.789 106.825 1.00 78.40  ? 69  ARG A NH2 1 
ATOM   516   N  N   . LYS A  1 71  ? -60.195  -43.718 103.157 1.00 83.29  ? 70  LYS A N   1 
ATOM   517   C  CA  . LYS A  1 71  ? -59.527  -43.424 101.881 1.00 85.06  ? 70  LYS A CA  1 
ATOM   518   C  C   . LYS A  1 71  ? -60.085  -44.373 100.810 1.00 77.58  ? 70  LYS A C   1 
ATOM   519   O  O   . LYS A  1 71  ? -60.545  -45.483 101.126 1.00 70.38  ? 70  LYS A O   1 
ATOM   520   C  CB  . LYS A  1 71  ? -58.001  -43.566 101.976 1.00 86.34  ? 70  LYS A CB  1 
ATOM   521   C  CG  . LYS A  1 71  ? -57.295  -42.755 103.060 1.00 91.36  ? 70  LYS A CG  1 
ATOM   522   C  CD  . LYS A  1 71  ? -57.895  -41.391 103.371 1.00 98.74  ? 70  LYS A CD  1 
ATOM   523   C  CE  . LYS A  1 71  ? -57.649  -40.347 102.302 1.00 103.96 ? 70  LYS A CE  1 
ATOM   524   N  NZ  . LYS A  1 71  ? -57.993  -38.987 102.787 1.00 105.19 ? 70  LYS A NZ  1 
ATOM   525   N  N   . HIS A  1 72  ? -60.038  -43.918 99.550  1.00 72.24  ? 71  HIS A N   1 
ATOM   526   C  CA  . HIS A  1 72  ? -60.479  -44.700 98.384  1.00 70.69  ? 71  HIS A CA  1 
ATOM   527   C  C   . HIS A  1 72  ? -59.665  -46.002 98.305  1.00 67.86  ? 71  HIS A C   1 
ATOM   528   O  O   . HIS A  1 72  ? -58.451  -46.017 98.566  1.00 63.55  ? 71  HIS A O   1 
ATOM   529   C  CB  . HIS A  1 72  ? -60.380  -43.863 97.092  1.00 68.50  ? 71  HIS A CB  1 
ATOM   530   C  CG  . HIS A  1 72  ? -60.671  -44.632 95.843  1.00 68.90  ? 71  HIS A CG  1 
ATOM   531   N  ND1 . HIS A  1 72  ? -61.963  -44.857 95.375  1.00 68.57  ? 71  HIS A ND1 1 
ATOM   532   C  CD2 . HIS A  1 72  ? -59.839  -45.242 94.968  1.00 68.37  ? 71  HIS A CD2 1 
ATOM   533   C  CE1 . HIS A  1 72  ? -61.902  -45.570 94.267  1.00 69.54  ? 71  HIS A CE1 1 
ATOM   534   N  NE2 . HIS A  1 72  ? -60.611  -45.822 93.999  1.00 70.31  ? 71  HIS A NE2 1 
ATOM   535   N  N   . GLY A  1 73  ? -60.354  -47.096 97.963  1.00 60.97  ? 72  GLY A N   1 
ATOM   536   C  CA  . GLY A  1 73  ? -59.723  -48.390 97.744  1.00 68.43  ? 72  GLY A CA  1 
ATOM   537   C  C   . GLY A  1 73  ? -60.440  -49.171 96.660  1.00 73.97  ? 72  GLY A C   1 
ATOM   538   O  O   . GLY A  1 73  ? -61.382  -48.665 96.044  1.00 71.02  ? 72  GLY A O   1 
ATOM   539   N  N   . GLY A  1 74  ? -59.968  -50.399 96.410  1.00 77.69  ? 73  GLY A N   1 
ATOM   540   C  CA  . GLY A  1 74  ? -60.690  -51.348 95.579  1.00 79.25  ? 73  GLY A CA  1 
ATOM   541   C  C   . GLY A  1 74  ? -61.769  -52.055 96.395  1.00 79.79  ? 73  GLY A C   1 
ATOM   542   O  O   . GLY A  1 74  ? -61.841  -51.858 97.607  1.00 78.84  ? 73  GLY A O   1 
ATOM   543   N  N   . PRO A  1 75  ? -62.635  -52.883 95.762  1.00 82.13  ? 74  PRO A N   1 
ATOM   544   C  CA  . PRO A  1 75  ? -63.701  -53.589 96.479  1.00 83.77  ? 74  PRO A CA  1 
ATOM   545   C  C   . PRO A  1 75  ? -63.194  -54.540 97.583  1.00 85.27  ? 74  PRO A C   1 
ATOM   546   O  O   . PRO A  1 75  ? -63.379  -54.252 98.763  1.00 72.08  ? 74  PRO A O   1 
ATOM   547   C  CB  . PRO A  1 75  ? -64.468  -54.359 95.387  1.00 79.65  ? 74  PRO A CB  1 
ATOM   548   C  CG  . PRO A  1 75  ? -64.034  -53.732 94.083  1.00 79.38  ? 74  PRO A CG  1 
ATOM   549   C  CD  . PRO A  1 75  ? -62.646  -53.174 94.321  1.00 79.94  ? 74  PRO A CD  1 
ATOM   550   N  N   . LYS A  1 76  ? -62.563  -55.657 97.198  1.00 96.11  ? 75  LYS A N   1 
ATOM   551   C  CA  . LYS A  1 76  ? -62.096  -56.683 98.150  1.00 100.60 ? 75  LYS A CA  1 
ATOM   552   C  C   . LYS A  1 76  ? -60.822  -56.167 98.839  1.00 101.59 ? 75  LYS A C   1 
ATOM   553   O  O   . LYS A  1 76  ? -59.716  -56.623 98.547  1.00 107.28 ? 75  LYS A O   1 
ATOM   554   C  CB  . LYS A  1 76  ? -61.873  -58.026 97.441  1.00 100.90 ? 75  LYS A CB  1 
ATOM   555   C  CG  . LYS A  1 76  ? -63.016  -58.528 96.561  1.00 102.90 ? 75  LYS A CG  1 
ATOM   556   C  CD  . LYS A  1 76  ? -64.283  -58.900 97.305  1.00 104.42 ? 75  LYS A CD  1 
ATOM   557   C  CE  . LYS A  1 76  ? -65.123  -59.911 96.549  1.00 105.11 ? 75  LYS A CE  1 
ATOM   558   N  NZ  . LYS A  1 76  ? -66.229  -60.435 97.384  1.00 101.49 ? 75  LYS A NZ  1 
ATOM   559   N  N   . ASP A  1 77  ? -61.006  -55.216 99.766  1.00 100.99 ? 76  ASP A N   1 
ATOM   560   C  CA  . ASP A  1 77  ? -59.933  -54.380 100.313 1.00 99.61  ? 76  ASP A CA  1 
ATOM   561   C  C   . ASP A  1 77  ? -60.513  -53.541 101.462 1.00 101.30 ? 76  ASP A C   1 
ATOM   562   O  O   . ASP A  1 77  ? -61.521  -52.847 101.288 1.00 95.87  ? 76  ASP A O   1 
ATOM   563   C  CB  . ASP A  1 77  ? -59.301  -53.557 99.183  1.00 99.48  ? 76  ASP A CB  1 
ATOM   564   C  CG  . ASP A  1 77  ? -58.393  -52.409 99.595  1.00 101.35 ? 76  ASP A CG  1 
ATOM   565   O  OD1 . ASP A  1 77  ? -58.441  -52.003 100.769 1.00 109.98 ? 76  ASP A OD1 1 
ATOM   566   O  OD2 . ASP A  1 77  ? -57.645  -51.921 98.721  1.00 96.36  ? 76  ASP A OD2 1 
ATOM   567   N  N   . GLU A  1 78  ? -59.847  -53.594 102.624 1.00 101.57 ? 77  GLU A N   1 
ATOM   568   C  CA  . GLU A  1 78  ? -60.418  -53.162 103.914 1.00 101.46 ? 77  GLU A CA  1 
ATOM   569   C  C   . GLU A  1 78  ? -60.579  -51.630 103.956 1.00 93.56  ? 77  GLU A C   1 
ATOM   570   O  O   . GLU A  1 78  ? -61.639  -51.136 104.352 1.00 90.27  ? 77  GLU A O   1 
ATOM   571   C  CB  . GLU A  1 78  ? -59.570  -53.711 105.066 1.00 102.77 ? 77  GLU A CB  1 
ATOM   572   C  CG  . GLU A  1 78  ? -59.566  -55.233 105.153 1.00 107.15 ? 77  GLU A CG  1 
ATOM   573   C  CD  . GLU A  1 78  ? -60.803  -55.866 105.778 1.00 113.92 ? 77  GLU A CD  1 
ATOM   574   O  OE1 . GLU A  1 78  ? -61.192  -55.443 106.887 1.00 117.80 ? 77  GLU A OE1 1 
ATOM   575   O  OE2 . GLU A  1 78  ? -61.374  -56.790 105.158 1.00 116.62 ? 77  GLU A OE2 1 
ATOM   576   N  N   . GLU A  1 79  ? -59.539  -50.885 103.555 1.00 86.76  ? 78  GLU A N   1 
ATOM   577   C  CA  . GLU A  1 79  ? -59.621  -49.417 103.434 1.00 85.87  ? 78  GLU A CA  1 
ATOM   578   C  C   . GLU A  1 79  ? -60.125  -49.044 102.030 1.00 81.88  ? 78  GLU A C   1 
ATOM   579   O  O   . GLU A  1 79  ? -59.364  -49.051 101.056 1.00 71.01  ? 78  GLU A O   1 
ATOM   580   C  CB  . GLU A  1 79  ? -58.276  -48.747 103.732 1.00 87.83  ? 78  GLU A CB  1 
ATOM   581   C  CG  . GLU A  1 79  ? -58.256  -47.262 103.387 1.00 91.85  ? 78  GLU A CG  1 
ATOM   582   C  CD  . GLU A  1 79  ? -57.949  -46.325 104.544 1.00 92.60  ? 78  GLU A CD  1 
ATOM   583   O  OE1 . GLU A  1 79  ? -58.892  -45.675 105.039 1.00 86.35  ? 78  GLU A OE1 1 
ATOM   584   O  OE2 . GLU A  1 79  ? -56.767  -46.230 104.934 1.00 95.81  ? 78  GLU A OE2 1 
ATOM   585   N  N   . ARG A  1 80  ? -61.415  -48.694 101.958 1.00 79.11  ? 79  ARG A N   1 
ATOM   586   C  CA  . ARG A  1 80  ? -62.094  -48.296 100.721 1.00 74.66  ? 79  ARG A CA  1 
ATOM   587   C  C   . ARG A  1 80  ? -63.282  -47.390 101.071 1.00 75.96  ? 79  ARG A C   1 
ATOM   588   O  O   . ARG A  1 80  ? -63.623  -47.225 102.258 1.00 78.31  ? 79  ARG A O   1 
ATOM   589   C  CB  . ARG A  1 80  ? -62.576  -49.529 99.946  1.00 70.68  ? 79  ARG A CB  1 
ATOM   590   C  CG  . ARG A  1 80  ? -63.643  -50.345 100.666 1.00 68.56  ? 79  ARG A CG  1 
ATOM   591   C  CD  . ARG A  1 80  ? -64.224  -51.467 99.822  1.00 68.38  ? 79  ARG A CD  1 
ATOM   592   N  NE  . ARG A  1 80  ? -65.447  -51.103 99.115  1.00 66.86  ? 79  ARG A NE  1 
ATOM   593   C  CZ  . ARG A  1 80  ? -66.300  -51.975 98.578  1.00 62.31  ? 79  ARG A CZ  1 
ATOM   594   N  NH1 . ARG A  1 80  ? -67.445  -51.557 98.059  1.00 56.69  ? 79  ARG A NH1 1 
ATOM   595   N  NH2 . ARG A  1 80  ? -66.018  -53.266 98.584  1.00 59.37  ? 79  ARG A NH2 1 
ATOM   596   N  N   . HIS A  1 81  ? -63.897  -46.807 100.030 1.00 71.46  ? 80  HIS A N   1 
ATOM   597   C  CA  . HIS A  1 81  ? -65.220  -46.174 100.135 1.00 64.02  ? 80  HIS A CA  1 
ATOM   598   C  C   . HIS A  1 81  ? -66.287  -47.270 100.031 1.00 56.21  ? 80  HIS A C   1 
ATOM   599   O  O   . HIS A  1 81  ? -66.064  -48.335 99.431  1.00 48.18  ? 80  HIS A O   1 
ATOM   600   C  CB  . HIS A  1 81  ? -65.406  -45.068 99.079  1.00 64.44  ? 80  HIS A CB  1 
ATOM   601   C  CG  . HIS A  1 81  ? -64.395  -43.969 99.159  1.00 64.85  ? 80  HIS A CG  1 
ATOM   602   N  ND1 . HIS A  1 81  ? -63.985  -43.242 98.053  1.00 62.95  ? 80  HIS A ND1 1 
ATOM   603   C  CD2 . HIS A  1 81  ? -63.693  -43.487 100.209 1.00 64.78  ? 80  HIS A CD2 1 
ATOM   604   C  CE1 . HIS A  1 81  ? -63.108  -42.331 98.438  1.00 63.17  ? 80  HIS A CE1 1 
ATOM   605   N  NE2 . HIS A  1 81  ? -62.897  -42.475 99.750  1.00 61.94  ? 80  HIS A NE2 1 
ATOM   606   N  N   . VAL A  1 82  ? -67.452  -47.026 100.627 1.00 50.37  ? 81  VAL A N   1 
ATOM   607   C  CA  . VAL A  1 82  ? -68.540  -47.966 100.432 1.00 53.70  ? 81  VAL A CA  1 
ATOM   608   C  C   . VAL A  1 82  ? -68.780  -48.095 98.913  1.00 51.97  ? 81  VAL A C   1 
ATOM   609   O  O   . VAL A  1 82  ? -68.874  -49.222 98.399  1.00 46.27  ? 81  VAL A O   1 
ATOM   610   C  CB  . VAL A  1 82  ? -69.791  -47.578 101.246 1.00 55.37  ? 81  VAL A CB  1 
ATOM   611   C  CG1 . VAL A  1 82  ? -71.007  -48.426 100.880 1.00 56.13  ? 81  VAL A CG1 1 
ATOM   612   C  CG2 . VAL A  1 82  ? -69.516  -47.686 102.744 1.00 56.38  ? 81  VAL A CG2 1 
ATOM   613   N  N   . GLY A  1 83  ? -68.732  -46.956 98.197  1.00 52.53  ? 82  GLY A N   1 
ATOM   614   C  CA  . GLY A  1 83  ? -69.058  -46.876 96.755  1.00 56.26  ? 82  GLY A CA  1 
ATOM   615   C  C   . GLY A  1 83  ? -67.959  -47.301 95.775  1.00 54.49  ? 82  GLY A C   1 
ATOM   616   O  O   . GLY A  1 83  ? -68.145  -47.148 94.572  1.00 54.42  ? 82  GLY A O   1 
ATOM   617   N  N   A SER A  1 84  ? -66.820  -47.801 96.275  0.70 56.33  ? 83  SER A N   1 
ATOM   618   C  CA  A SER A  1 84  ? -65.706  -48.278 95.427  0.70 53.98  ? 83  SER A CA  1 
ATOM   619   C  C   A SER A  1 84  ? -66.009  -49.683 94.910  0.70 51.98  ? 83  SER A C   1 
ATOM   620   O  O   A SER A  1 84  ? -65.708  -50.664 95.585  0.70 55.23  ? 83  SER A O   1 
ATOM   621   C  CB  A SER A  1 84  ? -64.368  -48.258 96.160  0.70 56.24  ? 83  SER A CB  1 
ATOM   622   O  OG  A SER A  1 84  ? -64.383  -47.433 97.320  0.70 57.08  ? 83  SER A OG  1 
ATOM   623   N  N   B ASP A  1 84  ? -66.862  -47.877 96.276  0.30 50.92  ? 83  ASP A N   1 
ATOM   624   C  CA  B ASP A  1 84  ? -65.741  -48.274 95.438  0.30 47.75  ? 83  ASP A CA  1 
ATOM   625   C  C   B ASP A  1 84  ? -65.959  -49.686 94.885  0.30 47.34  ? 83  ASP A C   1 
ATOM   626   O  O   B ASP A  1 84  ? -65.519  -50.659 95.496  0.30 47.42  ? 83  ASP A O   1 
ATOM   627   C  CB  B ASP A  1 84  ? -64.436  -48.227 96.232  0.30 47.10  ? 83  ASP A CB  1 
ATOM   628   C  CG  B ASP A  1 84  ? -63.970  -46.809 96.490  0.30 47.22  ? 83  ASP A CG  1 
ATOM   629   O  OD1 B ASP A  1 84  ? -64.430  -45.918 95.749  0.30 46.19  ? 83  ASP A OD1 1 
ATOM   630   O  OD2 B ASP A  1 84  ? -63.178  -46.607 97.437  0.30 43.58  ? 83  ASP A OD2 1 
ATOM   631   N  N   . LEU A  1 85  ? -66.585  -49.783 93.704  1.00 45.92  ? 84  LEU A N   1 
ATOM   632   C  CA  . LEU A  1 85  ? -66.885  -51.098 93.097  1.00 46.77  ? 84  LEU A CA  1 
ATOM   633   C  C   . LEU A  1 85  ? -65.799  -51.532 92.097  1.00 46.14  ? 84  LEU A C   1 
ATOM   634   O  O   . LEU A  1 85  ? -65.971  -52.526 91.417  1.00 47.74  ? 84  LEU A O   1 
ATOM   635   C  CB  . LEU A  1 85  ? -68.254  -51.065 92.417  1.00 49.27  ? 84  LEU A CB  1 
ATOM   636   C  CG  . LEU A  1 85  ? -69.456  -50.923 93.343  1.00 51.50  ? 84  LEU A CG  1 
ATOM   637   C  CD1 . LEU A  1 85  ? -70.747  -50.924 92.530  1.00 50.39  ? 84  LEU A CD1 1 
ATOM   638   C  CD2 . LEU A  1 85  ? -69.472  -52.040 94.376  1.00 55.97  ? 84  LEU A CD2 1 
ATOM   639   N  N   . GLY A  1 86  ? -64.672  -50.821 92.029  1.00 44.53  ? 85  GLY A N   1 
ATOM   640   C  CA  . GLY A  1 86  ? -63.555  -51.257 91.190  1.00 46.90  ? 85  GLY A CA  1 
ATOM   641   C  C   . GLY A  1 86  ? -63.750  -50.877 89.727  1.00 45.41  ? 85  GLY A C   1 
ATOM   642   O  O   . GLY A  1 86  ? -64.132  -49.743 89.413  1.00 41.20  ? 85  GLY A O   1 
ATOM   643   N  N   . ASN A  1 87  ? -63.486  -51.831 88.835  1.00 42.15  ? 86  ASN A N   1 
ATOM   644   C  CA  . ASN A  1 87  ? -63.418  -51.569 87.413  1.00 41.49  ? 86  ASN A CA  1 
ATOM   645   C  C   . ASN A  1 87  ? -64.306  -52.544 86.660  1.00 43.66  ? 86  ASN A C   1 
ATOM   646   O  O   . ASN A  1 87  ? -64.420  -53.696 87.050  1.00 42.98  ? 86  ASN A O   1 
ATOM   647   C  CB  . ASN A  1 87  ? -61.997  -51.701 86.876  1.00 44.11  ? 86  ASN A CB  1 
ATOM   648   C  CG  . ASN A  1 87  ? -61.128  -50.548 87.313  1.00 45.43  ? 86  ASN A CG  1 
ATOM   649   O  OD1 . ASN A  1 87  ? -61.320  -49.415 86.869  1.00 47.27  ? 86  ASN A OD1 1 
ATOM   650   N  ND2 . ASN A  1 87  ? -60.199  -50.822 88.208  1.00 46.13  ? 86  ASN A ND2 1 
ATOM   651   N  N   . VAL A  1 88  ? -64.931  -52.049 85.584  1.00 38.82  ? 87  VAL A N   1 
ATOM   652   C  CA  . VAL A  1 88  ? -65.539  -52.911 84.591  1.00 37.58  ? 87  VAL A CA  1 
ATOM   653   C  C   . VAL A  1 88  ? -64.623  -52.895 83.361  1.00 35.84  ? 87  VAL A C   1 
ATOM   654   O  O   . VAL A  1 88  ? -63.864  -51.938 83.153  1.00 37.37  ? 87  VAL A O   1 
ATOM   655   C  CB  . VAL A  1 88  ? -66.991  -52.487 84.270  1.00 37.35  ? 87  VAL A CB  1 
ATOM   656   C  CG1 . VAL A  1 88  ? -67.875  -52.584 85.503  1.00 35.85  ? 87  VAL A CG1 1 
ATOM   657   C  CG2 . VAL A  1 88  ? -67.077  -51.083 83.683  1.00 36.85  ? 87  VAL A CG2 1 
ATOM   658   N  N   . THR A  1 89  ? -64.713  -53.960 82.564  1.00 35.26  ? 88  THR A N   1 
ATOM   659   C  CA  . THR A  1 89  ? -63.884  -54.169 81.378  1.00 40.34  ? 88  THR A CA  1 
ATOM   660   C  C   . THR A  1 89  ? -64.773  -54.193 80.139  1.00 35.89  ? 88  THR A C   1 
ATOM   661   O  O   . THR A  1 89  ? -65.643  -55.044 80.006  1.00 36.77  ? 88  THR A O   1 
ATOM   662   C  CB  . THR A  1 89  ? -63.088  -55.484 81.453  1.00 44.28  ? 88  THR A CB  1 
ATOM   663   O  OG1 . THR A  1 89  ? -62.353  -55.469 82.674  1.00 47.20  ? 88  THR A OG1 1 
ATOM   664   C  CG2 . THR A  1 89  ? -62.129  -55.666 80.296  1.00 44.52  ? 88  THR A CG2 1 
ATOM   665   N  N   . ALA A  1 90  ? -64.534  -53.248 79.236  1.00 36.85  ? 89  ALA A N   1 
ATOM   666   C  CA  . ALA A  1 90  ? -65.226  -53.241 77.973  1.00 37.40  ? 89  ALA A CA  1 
ATOM   667   C  C   . ALA A  1 90  ? -64.375  -54.015 76.968  1.00 33.76  ? 89  ALA A C   1 
ATOM   668   O  O   . ALA A  1 90  ? -63.169  -53.813 76.908  1.00 35.56  ? 89  ALA A O   1 
ATOM   669   C  CB  . ALA A  1 90  ? -65.490  -51.824 77.510  1.00 35.85  ? 89  ALA A CB  1 
ATOM   670   N  N   . ASP A  1 91  ? -65.051  -54.870 76.200  1.00 35.24  ? 90  ASP A N   1 
ATOM   671   C  CA  . ASP A  1 91  ? -64.486  -55.697 75.152  1.00 38.25  ? 90  ASP A CA  1 
ATOM   672   C  C   . ASP A  1 91  ? -64.263  -54.833 73.902  1.00 40.85  ? 90  ASP A C   1 
ATOM   673   O  O   . ASP A  1 91  ? -64.441  -53.610 73.937  1.00 37.38  ? 90  ASP A O   1 
ATOM   674   C  CB  . ASP A  1 91  ? -65.390  -56.909 74.896  1.00 40.75  ? 90  ASP A CB  1 
ATOM   675   C  CG  . ASP A  1 91  ? -66.749  -56.611 74.270  1.00 43.89  ? 90  ASP A CG  1 
ATOM   676   O  OD1 . ASP A  1 91  ? -67.585  -57.542 74.221  1.00 46.61  ? 90  ASP A OD1 1 
ATOM   677   O  OD2 . ASP A  1 91  ? -66.959  -55.472 73.795  1.00 42.80  ? 90  ASP A OD2 1 
ATOM   678   N  N   . LYS A  1 92  ? -63.863  -55.479 72.803  1.00 40.69  ? 91  LYS A N   1 
ATOM   679   C  CA  . LYS A  1 92  ? -63.538  -54.778 71.562  1.00 44.40  ? 91  LYS A CA  1 
ATOM   680   C  C   . LYS A  1 92  ? -64.806  -54.219 70.880  1.00 39.31  ? 91  LYS A C   1 
ATOM   681   O  O   . LYS A  1 92  ? -64.682  -53.420 69.977  1.00 38.71  ? 91  LYS A O   1 
ATOM   682   C  CB  . LYS A  1 92  ? -62.732  -55.693 70.630  1.00 51.05  ? 91  LYS A CB  1 
ATOM   683   C  CG  . LYS A  1 92  ? -63.475  -56.905 70.068  1.00 62.95  ? 91  LYS A CG  1 
ATOM   684   C  CD  . LYS A  1 92  ? -63.349  -58.186 70.899  1.00 75.06  ? 91  LYS A CD  1 
ATOM   685   C  CE  . LYS A  1 92  ? -64.648  -58.645 71.539  1.00 79.97  ? 91  LYS A CE  1 
ATOM   686   N  NZ  . LYS A  1 92  ? -64.407  -59.624 72.627  1.00 79.89  ? 91  LYS A NZ  1 
ATOM   687   N  N   . ASP A  1 93  ? -66.011  -54.648 71.285  1.00 36.73  ? 92  ASP A N   1 
ATOM   688   C  CA  . ASP A  1 93  ? -67.258  -54.065 70.760  1.00 39.51  ? 92  ASP A CA  1 
ATOM   689   C  C   . ASP A  1 93  ? -67.712  -52.878 71.620  1.00 37.01  ? 92  ASP A C   1 
ATOM   690   O  O   . ASP A  1 93  ? -68.805  -52.332 71.400  1.00 38.14  ? 92  ASP A O   1 
ATOM   691   C  CB  . ASP A  1 93  ? -68.372  -55.108 70.653  1.00 44.14  ? 92  ASP A CB  1 
ATOM   692   C  CG  . ASP A  1 93  ? -68.121  -56.140 69.562  1.00 53.56  ? 92  ASP A CG  1 
ATOM   693   O  OD1 . ASP A  1 93  ? -68.259  -57.345 69.864  1.00 62.93  ? 92  ASP A OD1 1 
ATOM   694   O  OD2 . ASP A  1 93  ? -67.793  -55.735 68.413  1.00 53.78  ? 92  ASP A OD2 1 
ATOM   695   N  N   . GLY A  1 94  ? -66.873  -52.469 72.577  1.00 32.35  ? 93  GLY A N   1 
ATOM   696   C  CA  . GLY A  1 94  ? -67.187  -51.378 73.504  1.00 34.15  ? 93  GLY A CA  1 
ATOM   697   C  C   . GLY A  1 94  ? -68.229  -51.747 74.548  1.00 33.81  ? 93  GLY A C   1 
ATOM   698   O  O   . GLY A  1 94  ? -68.859  -50.852 75.144  1.00 34.48  ? 93  GLY A O   1 
ATOM   699   N  N   . VAL A  1 95  ? -68.400  -53.057 74.797  1.00 33.16  ? 94  VAL A N   1 
ATOM   700   C  CA  . VAL A  1 95  ? -69.408  -53.568 75.721  1.00 35.20  ? 94  VAL A CA  1 
ATOM   701   C  C   . VAL A  1 95  ? -68.731  -54.128 76.979  1.00 38.07  ? 94  VAL A C   1 
ATOM   702   O  O   . VAL A  1 95  ? -67.847  -54.984 76.890  1.00 37.91  ? 94  VAL A O   1 
ATOM   703   C  CB  . VAL A  1 95  ? -70.281  -54.638 75.049  1.00 36.38  ? 94  VAL A CB  1 
ATOM   704   C  CG1 . VAL A  1 95  ? -71.334  -55.201 75.996  1.00 38.82  ? 94  VAL A CG1 1 
ATOM   705   C  CG2 . VAL A  1 95  ? -70.946  -54.094 73.799  1.00 40.03  ? 94  VAL A CG2 1 
ATOM   706   N  N   . ALA A  1 96  ? -69.183  -53.657 78.147  1.00 36.30  ? 95  ALA A N   1 
ATOM   707   C  CA  . ALA A  1 96  ? -68.791  -54.190 79.447  1.00 37.02  ? 95  ALA A CA  1 
ATOM   708   C  C   . ALA A  1 96  ? -69.940  -55.033 79.996  1.00 41.63  ? 95  ALA A C   1 
ATOM   709   O  O   . ALA A  1 96  ? -71.008  -54.507 80.310  1.00 39.21  ? 95  ALA A O   1 
ATOM   710   C  CB  . ALA A  1 96  ? -68.456  -53.066 80.384  1.00 36.68  ? 95  ALA A CB  1 
ATOM   711   N  N   . ASP A  1 97  ? -69.717  -56.347 80.074  1.00 41.84  ? 96  ASP A N   1 
ATOM   712   C  CA  . ASP A  1 97  ? -70.655  -57.253 80.715  1.00 47.87  ? 96  ASP A CA  1 
ATOM   713   C  C   . ASP A  1 97  ? -70.269  -57.299 82.192  1.00 44.14  ? 96  ASP A C   1 
ATOM   714   O  O   . ASP A  1 97  ? -69.176  -57.674 82.512  1.00 48.15  ? 96  ASP A O   1 
ATOM   715   C  CB  . ASP A  1 97  ? -70.662  -58.621 80.031  1.00 49.61  ? 96  ASP A CB  1 
ATOM   716   C  CG  . ASP A  1 97  ? -71.348  -58.607 78.672  1.00 58.94  ? 96  ASP A CG  1 
ATOM   717   O  OD1 . ASP A  1 97  ? -72.433  -57.965 78.540  1.00 60.63  ? 96  ASP A OD1 1 
ATOM   718   O  OD2 . ASP A  1 97  ? -70.800  -59.233 77.744  1.00 68.83  ? 96  ASP A OD2 1 
ATOM   719   N  N   . VAL A  1 98  ? -71.157  -56.818 83.061  1.00 43.01  ? 97  VAL A N   1 
ATOM   720   C  CA  . VAL A  1 98  ? -70.847  -56.632 84.462  1.00 41.32  ? 97  VAL A CA  1 
ATOM   721   C  C   . VAL A  1 98  ? -71.401  -57.838 85.229  1.00 43.33  ? 97  VAL A C   1 
ATOM   722   O  O   . VAL A  1 98  ? -72.511  -58.279 84.987  1.00 40.51  ? 97  VAL A O   1 
ATOM   723   C  CB  . VAL A  1 98  ? -71.412  -55.297 84.982  1.00 42.88  ? 97  VAL A CB  1 
ATOM   724   C  CG1 . VAL A  1 98  ? -71.181  -55.110 86.470  1.00 43.16  ? 97  VAL A CG1 1 
ATOM   725   C  CG2 . VAL A  1 98  ? -70.848  -54.111 84.207  1.00 40.83  ? 97  VAL A CG2 1 
ATOM   726   N  N   . SER A  1 99  ? -70.575  -58.369 86.132  1.00 47.18  ? 98  SER A N   1 
ATOM   727   C  CA  . SER A  1 99  ? -70.938  -59.443 87.055  1.00 48.76  ? 98  SER A CA  1 
ATOM   728   C  C   . SER A  1 99  ? -70.069  -59.308 88.309  1.00 45.51  ? 98  SER A C   1 
ATOM   729   O  O   . SER A  1 99  ? -68.907  -59.660 88.311  1.00 49.72  ? 98  SER A O   1 
ATOM   730   C  CB  . SER A  1 99  ? -70.794  -60.796 86.410  1.00 51.26  ? 98  SER A CB  1 
ATOM   731   O  OG  . SER A  1 99  ? -71.576  -61.761 87.094  1.00 59.20  ? 98  SER A OG  1 
ATOM   732   N  N   . ILE A  1 100 ? -70.649  -58.714 89.341  1.00 45.01  ? 99  ILE A N   1 
ATOM   733   C  CA  . ILE A  1 100 ? -69.980  -58.373 90.567  1.00 51.39  ? 99  ILE A CA  1 
ATOM   734   C  C   . ILE A  1 100 ? -70.801  -58.966 91.709  1.00 53.15  ? 99  ILE A C   1 
ATOM   735   O  O   . ILE A  1 100 ? -72.034  -59.085 91.624  1.00 45.57  ? 99  ILE A O   1 
ATOM   736   C  CB  . ILE A  1 100 ? -69.845  -56.843 90.738  1.00 50.72  ? 99  ILE A CB  1 
ATOM   737   C  CG1 . ILE A  1 100 ? -68.844  -56.238 89.759  1.00 53.64  ? 99  ILE A CG1 1 
ATOM   738   C  CG2 . ILE A  1 100 ? -69.493  -56.473 92.170  1.00 53.38  ? 99  ILE A CG2 1 
ATOM   739   C  CD1 . ILE A  1 100 ? -68.752  -54.734 89.840  1.00 56.69  ? 99  ILE A CD1 1 
ATOM   740   N  N   . GLU A  1 101 ? -70.090  -59.305 92.781  1.00 55.29  ? 100 GLU A N   1 
ATOM   741   C  CA  . GLU A  1 101 ? -70.682  -59.570 94.054  1.00 58.53  ? 100 GLU A CA  1 
ATOM   742   C  C   . GLU A  1 101 ? -69.917  -58.719 95.062  1.00 54.08  ? 100 GLU A C   1 
ATOM   743   O  O   . GLU A  1 101 ? -68.695  -58.717 95.067  1.00 58.26  ? 100 GLU A O   1 
ATOM   744   C  CB  . GLU A  1 101 ? -70.628  -61.069 94.344  1.00 64.50  ? 100 GLU A CB  1 
ATOM   745   C  CG  . GLU A  1 101 ? -71.710  -61.536 95.296  1.00 72.67  ? 100 GLU A CG  1 
ATOM   746   C  CD  . GLU A  1 101 ? -71.971  -63.030 95.238  1.00 74.63  ? 100 GLU A CD  1 
ATOM   747   O  OE1 . GLU A  1 101 ? -72.802  -63.453 94.407  1.00 80.68  ? 100 GLU A OE1 1 
ATOM   748   O  OE2 . GLU A  1 101 ? -71.327  -63.762 96.008  1.00 78.66  ? 100 GLU A OE2 1 
ATOM   749   N  N   . ASP A  1 102 ? -70.644  -57.938 95.856  1.00 54.78  ? 101 ASP A N   1 
ATOM   750   C  CA  . ASP A  1 102 ? -70.011  -57.033 96.788  1.00 54.13  ? 101 ASP A CA  1 
ATOM   751   C  C   . ASP A  1 102 ? -70.764  -57.076 98.115  1.00 53.67  ? 101 ASP A C   1 
ATOM   752   O  O   . ASP A  1 102 ? -71.987  -57.078 98.124  1.00 49.17  ? 101 ASP A O   1 
ATOM   753   C  CB  . ASP A  1 102 ? -69.966  -55.605 96.249  1.00 53.99  ? 101 ASP A CB  1 
ATOM   754   C  CG  . ASP A  1 102 ? -69.080  -54.711 97.093  1.00 56.27  ? 101 ASP A CG  1 
ATOM   755   O  OD1 . ASP A  1 102 ? -69.629  -53.947 97.912  1.00 56.35  ? 101 ASP A OD1 1 
ATOM   756   O  OD2 . ASP A  1 102 ? -67.846  -54.801 96.932  1.00 61.41  ? 101 ASP A OD2 1 
ATOM   757   N  N   . SER A  1 103 ? -69.994  -57.080 99.210  1.00 57.77  ? 102 SER A N   1 
ATOM   758   C  CA  . SER A  1 103 ? -70.499  -57.247 100.578 1.00 61.27  ? 102 SER A CA  1 
ATOM   759   C  C   . SER A  1 103 ? -70.574  -55.909 101.315 1.00 56.08  ? 102 SER A C   1 
ATOM   760   O  O   . SER A  1 103 ? -71.216  -55.836 102.360 1.00 61.15  ? 102 SER A O   1 
ATOM   761   C  CB  . SER A  1 103 ? -69.642  -58.216 101.362 1.00 60.33  ? 102 SER A CB  1 
ATOM   762   O  OG  . SER A  1 103 ? -69.847  -59.543 100.911 1.00 65.88  ? 102 SER A OG  1 
ATOM   763   N  N   . VAL A  1 104 ? -69.906  -54.873 100.797 1.00 51.05  ? 103 VAL A N   1 
ATOM   764   C  CA  . VAL A  1 104 ? -69.827  -53.588 101.493 1.00 49.53  ? 103 VAL A CA  1 
ATOM   765   C  C   . VAL A  1 104 ? -71.040  -52.705 101.155 1.00 51.72  ? 103 VAL A C   1 
ATOM   766   O  O   . VAL A  1 104 ? -71.533  -51.990 102.035 1.00 50.71  ? 103 VAL A O   1 
ATOM   767   C  CB  . VAL A  1 104 ? -68.505  -52.864 101.193 1.00 52.83  ? 103 VAL A CB  1 
ATOM   768   C  CG1 . VAL A  1 104 ? -68.419  -51.514 101.900 1.00 52.64  ? 103 VAL A CG1 1 
ATOM   769   C  CG2 . VAL A  1 104 ? -67.315  -53.740 101.550 1.00 57.30  ? 103 VAL A CG2 1 
ATOM   770   N  N   . ILE A  1 105 ? -71.477  -52.696 99.885  1.00 49.28  ? 104 ILE A N   1 
ATOM   771   C  CA  . ILE A  1 105 ? -72.696  -51.963 99.510  1.00 46.87  ? 104 ILE A CA  1 
ATOM   772   C  C   . ILE A  1 105 ? -73.886  -52.758 100.044 1.00 46.03  ? 104 ILE A C   1 
ATOM   773   O  O   . ILE A  1 105 ? -73.782  -53.975 100.206 1.00 46.85  ? 104 ILE A O   1 
ATOM   774   C  CB  . ILE A  1 105 ? -72.804  -51.750 97.983  1.00 42.64  ? 104 ILE A CB  1 
ATOM   775   C  CG1 . ILE A  1 105 ? -72.856  -53.078 97.224  1.00 43.53  ? 104 ILE A CG1 1 
ATOM   776   C  CG2 . ILE A  1 105 ? -71.675  -50.850 97.504  1.00 46.51  ? 104 ILE A CG2 1 
ATOM   777   C  CD1 . ILE A  1 105 ? -73.284  -52.967 95.776  1.00 45.71  ? 104 ILE A CD1 1 
ATOM   778   N  N   . SER A  1 106 ? -75.006  -52.071 100.286 1.00 43.85  ? 105 SER A N   1 
ATOM   779   C  CA  . SER A  1 106 ? -76.284  -52.743 100.566 1.00 43.40  ? 105 SER A CA  1 
ATOM   780   C  C   . SER A  1 106 ? -77.433  -52.059 99.815  1.00 40.05  ? 105 SER A C   1 
ATOM   781   O  O   . SER A  1 106 ? -77.293  -50.934 99.326  1.00 39.06  ? 105 SER A O   1 
ATOM   782   C  CB  . SER A  1 106 ? -76.571  -52.773 102.060 1.00 44.71  ? 105 SER A CB  1 
ATOM   783   O  OG  . SER A  1 106 ? -77.623  -53.693 102.334 1.00 46.47  ? 105 SER A OG  1 
ATOM   784   N  N   . LEU A  1 107 ? -78.574  -52.753 99.754  1.00 38.68  ? 106 LEU A N   1 
ATOM   785   C  CA  . LEU A  1 107 ? -79.830  -52.196 99.269  1.00 40.13  ? 106 LEU A CA  1 
ATOM   786   C  C   . LEU A  1 107 ? -80.747  -51.801 100.435 1.00 41.82  ? 106 LEU A C   1 
ATOM   787   O  O   . LEU A  1 107 ? -81.901  -51.447 100.222 1.00 42.51  ? 106 LEU A O   1 
ATOM   788   C  CB  . LEU A  1 107 ? -80.495  -53.227 98.361  1.00 38.99  ? 106 LEU A CB  1 
ATOM   789   C  CG  . LEU A  1 107 ? -79.641  -53.677 97.180  1.00 37.83  ? 106 LEU A CG  1 
ATOM   790   C  CD1 . LEU A  1 107 ? -80.423  -54.619 96.291  1.00 37.13  ? 106 LEU A CD1 1 
ATOM   791   C  CD2 . LEU A  1 107 ? -79.130  -52.482 96.392  1.00 38.70  ? 106 LEU A CD2 1 
ATOM   792   N  N   . SER A  1 108 ? -80.227  -51.861 101.666 1.00 46.21  ? 107 SER A N   1 
ATOM   793   C  CA  . SER A  1 108 ? -80.966  -51.421 102.847 1.00 49.67  ? 107 SER A CA  1 
ATOM   794   C  C   . SER A  1 108 ? -79.980  -51.002 103.931 1.00 47.84  ? 107 SER A C   1 
ATOM   795   O  O   . SER A  1 108 ? -78.824  -51.390 103.880 1.00 58.21  ? 107 SER A O   1 
ATOM   796   C  CB  . SER A  1 108 ? -81.912  -52.484 103.346 1.00 52.36  ? 107 SER A CB  1 
ATOM   797   O  OG  . SER A  1 108 ? -81.245  -53.723 103.490 1.00 56.33  ? 107 SER A OG  1 
ATOM   798   N  N   . GLY A  1 109 ? -80.471  -50.190 104.874 1.00 50.53  ? 108 GLY A N   1 
ATOM   799   C  CA  . GLY A  1 109 ? -79.706  -49.654 105.991 1.00 54.92  ? 108 GLY A CA  1 
ATOM   800   C  C   . GLY A  1 109 ? -79.063  -48.324 105.634 1.00 60.51  ? 108 GLY A C   1 
ATOM   801   O  O   . GLY A  1 109 ? -79.268  -47.799 104.547 1.00 56.43  ? 108 GLY A O   1 
ATOM   802   N  N   . ASP A  1 110 ? -78.265  -47.777 106.557 1.00 67.07  ? 109 ASP A N   1 
ATOM   803   C  CA  . ASP A  1 110 ? -77.616  -46.466 106.353 1.00 70.93  ? 109 ASP A CA  1 
ATOM   804   C  C   . ASP A  1 110 ? -76.519  -46.568 105.276 1.00 61.27  ? 109 ASP A C   1 
ATOM   805   O  O   . ASP A  1 110 ? -76.072  -45.524 104.793 1.00 59.62  ? 109 ASP A O   1 
ATOM   806   C  CB  . ASP A  1 110 ? -77.077  -45.892 107.669 1.00 77.42  ? 109 ASP A CB  1 
ATOM   807   C  CG  . ASP A  1 110 ? -78.156  -45.460 108.655 1.00 81.65  ? 109 ASP A CG  1 
ATOM   808   O  OD1 . ASP A  1 110 ? -79.338  -45.346 108.235 1.00 82.28  ? 109 ASP A OD1 1 
ATOM   809   O  OD2 . ASP A  1 110 ? -77.806  -45.227 109.839 1.00 76.73  ? 109 ASP A OD2 1 
ATOM   810   N  N   . HIS A  1 111 ? -76.113  -47.804 104.916 1.00 52.14  ? 110 HIS A N   1 
ATOM   811   C  CA  . HIS A  1 111 ? -75.168  -48.122 103.803 1.00 54.76  ? 110 HIS A CA  1 
ATOM   812   C  C   . HIS A  1 111 ? -75.887  -48.484 102.481 1.00 52.98  ? 110 HIS A C   1 
ATOM   813   O  O   . HIS A  1 111 ? -75.275  -49.045 101.539 1.00 49.80  ? 110 HIS A O   1 
ATOM   814   C  CB  . HIS A  1 111 ? -74.217  -49.240 104.240 1.00 56.37  ? 110 HIS A CB  1 
ATOM   815   C  CG  . HIS A  1 111 ? -73.157  -48.752 105.168 1.00 62.42  ? 110 HIS A CG  1 
ATOM   816   N  ND1 . HIS A  1 111 ? -71.872  -49.244 105.137 1.00 58.80  ? 110 HIS A ND1 1 
ATOM   817   C  CD2 . HIS A  1 111 ? -73.178  -47.784 106.116 1.00 69.34  ? 110 HIS A CD2 1 
ATOM   818   C  CE1 . HIS A  1 111 ? -71.148  -48.619 106.044 1.00 70.39  ? 110 HIS A CE1 1 
ATOM   819   N  NE2 . HIS A  1 111 ? -71.926  -47.713 106.662 1.00 68.46  ? 110 HIS A NE2 1 
ATOM   820   N  N   . SER A  1 112 ? -77.175  -48.140 102.384 1.00 48.41  ? 111 SER A N   1 
ATOM   821   C  CA  . SER A  1 112 ? -77.965  -48.419 101.193 1.00 45.78  ? 111 SER A CA  1 
ATOM   822   C  C   . SER A  1 112 ? -77.533  -47.488 100.048 1.00 36.75  ? 111 SER A C   1 
ATOM   823   O  O   . SER A  1 112 ? -77.403  -46.282 100.224 1.00 36.74  ? 111 SER A O   1 
ATOM   824   C  CB  . SER A  1 112 ? -79.432  -48.269 101.463 1.00 40.34  ? 111 SER A CB  1 
ATOM   825   O  OG  . SER A  1 112 ? -80.169  -48.439 100.262 1.00 39.84  ? 111 SER A OG  1 
ATOM   826   N  N   . ILE A  1 113 ? -77.413  -48.064 98.853  1.00 38.04  ? 112 ILE A N   1 
ATOM   827   C  CA  . ILE A  1 113 ? -77.113  -47.304 97.638  1.00 35.11  ? 112 ILE A CA  1 
ATOM   828   C  C   . ILE A  1 113 ? -78.400  -46.887 96.889  1.00 34.06  ? 112 ILE A C   1 
ATOM   829   O  O   . ILE A  1 113 ? -78.311  -46.224 95.863  1.00 30.45  ? 112 ILE A O   1 
ATOM   830   C  CB  . ILE A  1 113 ? -76.159  -48.122 96.754  1.00 35.47  ? 112 ILE A CB  1 
ATOM   831   C  CG1 . ILE A  1 113 ? -76.816  -49.398 96.227  1.00 34.60  ? 112 ILE A CG1 1 
ATOM   832   C  CG2 . ILE A  1 113 ? -74.871  -48.407 97.515  1.00 38.31  ? 112 ILE A CG2 1 
ATOM   833   C  CD1 . ILE A  1 113 ? -75.953  -50.175 95.268  1.00 36.11  ? 112 ILE A CD1 1 
ATOM   834   N  N   . ILE A  1 114 ? -79.585  -47.240 97.405  1.00 33.44  ? 113 ILE A N   1 
ATOM   835   C  CA  . ILE A  1 114 ? -80.852  -46.841 96.799  1.00 32.89  ? 113 ILE A CA  1 
ATOM   836   C  C   . ILE A  1 114 ? -80.959  -45.316 96.868  1.00 31.67  ? 113 ILE A C   1 
ATOM   837   O  O   . ILE A  1 114 ? -80.806  -44.740 97.927  1.00 28.62  ? 113 ILE A O   1 
ATOM   838   C  CB  . ILE A  1 114 ? -82.058  -47.489 97.510  1.00 36.51  ? 113 ILE A CB  1 
ATOM   839   C  CG1 . ILE A  1 114 ? -81.981  -49.021 97.559  1.00 37.23  ? 113 ILE A CG1 1 
ATOM   840   C  CG2 . ILE A  1 114 ? -83.369  -47.000 96.900  1.00 34.95  ? 113 ILE A CG2 1 
ATOM   841   C  CD1 . ILE A  1 114 ? -82.112  -49.707 96.235  1.00 40.38  ? 113 ILE A CD1 1 
ATOM   842   N  N   . GLY A  1 115 ? -81.268  -44.672 95.736  1.00 29.10  ? 114 GLY A N   1 
ATOM   843   C  CA  . GLY A  1 115 ? -81.419  -43.234 95.671  1.00 27.35  ? 114 GLY A CA  1 
ATOM   844   C  C   . GLY A  1 115 ? -80.089  -42.500 95.495  1.00 27.11  ? 114 GLY A C   1 
ATOM   845   O  O   . GLY A  1 115 ? -80.056  -41.282 95.524  1.00 27.78  ? 114 GLY A O   1 
ATOM   846   N  N   . ARG A  1 116 ? -78.995  -43.245 95.344  1.00 26.97  ? 115 ARG A N   1 
ATOM   847   C  CA  . ARG A  1 116 ? -77.679  -42.692 95.054  1.00 30.43  ? 115 ARG A CA  1 
ATOM   848   C  C   . ARG A  1 116 ? -77.397  -42.892 93.552  1.00 30.51  ? 115 ARG A C   1 
ATOM   849   O  O   . ARG A  1 116 ? -78.248  -43.393 92.850  1.00 32.79  ? 115 ARG A O   1 
ATOM   850   C  CB  . ARG A  1 116 ? -76.653  -43.333 95.993  1.00 32.91  ? 115 ARG A CB  1 
ATOM   851   C  CG  . ARG A  1 116 ? -76.961  -43.065 97.463  1.00 33.39  ? 115 ARG A CG  1 
ATOM   852   C  CD  . ARG A  1 116 ? -75.870  -43.507 98.427  1.00 35.84  ? 115 ARG A CD  1 
ATOM   853   N  NE  . ARG A  1 116 ? -76.322  -43.466 99.812  1.00 34.75  ? 115 ARG A NE  1 
ATOM   854   C  CZ  . ARG A  1 116 ? -76.548  -42.360 100.514 1.00 37.17  ? 115 ARG A CZ  1 
ATOM   855   N  NH1 . ARG A  1 116 ? -77.128  -42.470 101.697 1.00 39.76  ? 115 ARG A NH1 1 
ATOM   856   N  NH2 . ARG A  1 116 ? -76.202  -41.160 100.061 1.00 34.75  ? 115 ARG A NH2 1 
ATOM   857   N  N   . THR A  1 117 ? -76.228  -42.452 93.065  1.00 32.57  ? 116 THR A N   1 
ATOM   858   C  CA  . THR A  1 117 ? -75.880  -42.506 91.629  1.00 30.89  ? 116 THR A CA  1 
ATOM   859   C  C   . THR A  1 117 ? -74.775  -43.530 91.361  1.00 31.62  ? 116 THR A C   1 
ATOM   860   O  O   . THR A  1 117 ? -73.730  -43.525 92.012  1.00 32.25  ? 116 THR A O   1 
ATOM   861   C  CB  . THR A  1 117 ? -75.411  -41.137 91.134  1.00 29.90  ? 116 THR A CB  1 
ATOM   862   O  OG1 . THR A  1 117 ? -76.511  -40.253 91.322  1.00 29.13  ? 116 THR A OG1 1 
ATOM   863   C  CG2 . THR A  1 117 ? -74.983  -41.125 89.683  1.00 31.14  ? 116 THR A CG2 1 
ATOM   864   N  N   . LEU A  1 118 ? -75.017  -44.396 90.377  1.00 28.62  ? 117 LEU A N   1 
ATOM   865   C  CA  . LEU A  1 118 ? -73.996  -45.252 89.799  1.00 29.48  ? 117 LEU A CA  1 
ATOM   866   C  C   . LEU A  1 118 ? -73.323  -44.479 88.655  1.00 31.66  ? 117 LEU A C   1 
ATOM   867   O  O   . LEU A  1 118 ? -74.038  -43.866 87.827  1.00 26.53  ? 117 LEU A O   1 
ATOM   868   C  CB  . LEU A  1 118 ? -74.671  -46.530 89.301  1.00 30.11  ? 117 LEU A CB  1 
ATOM   869   C  CG  . LEU A  1 118 ? -73.732  -47.643 88.839  1.00 32.08  ? 117 LEU A CG  1 
ATOM   870   C  CD1 . LEU A  1 118 ? -72.886  -48.181 89.991  1.00 32.44  ? 117 LEU A CD1 1 
ATOM   871   C  CD2 . LEU A  1 118 ? -74.522  -48.770 88.193  1.00 32.24  ? 117 LEU A CD2 1 
ATOM   872   N  N   . VAL A  1 119 ? -71.979  -44.485 88.639  1.00 29.83  ? 118 VAL A N   1 
ATOM   873   C  CA  . VAL A  1 119 ? -71.168  -43.776 87.651  1.00 32.05  ? 118 VAL A CA  1 
ATOM   874   C  C   . VAL A  1 119 ? -70.190  -44.747 86.989  1.00 33.99  ? 118 VAL A C   1 
ATOM   875   O  O   . VAL A  1 119 ? -69.500  -45.533 87.661  1.00 32.92  ? 118 VAL A O   1 
ATOM   876   C  CB  . VAL A  1 119 ? -70.394  -42.611 88.291  1.00 33.37  ? 118 VAL A CB  1 
ATOM   877   C  CG1 . VAL A  1 119 ? -69.537  -41.881 87.269  1.00 34.60  ? 118 VAL A CG1 1 
ATOM   878   C  CG2 . VAL A  1 119 ? -71.317  -41.641 89.009  1.00 30.18  ? 118 VAL A CG2 1 
ATOM   879   N  N   . VAL A  1 120 ? -70.083  -44.651 85.667  1.00 30.83  ? 119 VAL A N   1 
ATOM   880   C  CA  . VAL A  1 120 ? -68.992  -45.283 84.963  1.00 31.75  ? 119 VAL A CA  1 
ATOM   881   C  C   . VAL A  1 120 ? -68.069  -44.183 84.421  1.00 33.43  ? 119 VAL A C   1 
ATOM   882   O  O   . VAL A  1 120 ? -68.542  -43.158 83.900  1.00 33.58  ? 119 VAL A O   1 
ATOM   883   C  CB  . VAL A  1 120 ? -69.486  -46.260 83.884  1.00 32.52  ? 119 VAL A CB  1 
ATOM   884   C  CG1 . VAL A  1 120 ? -70.301  -45.564 82.812  1.00 34.14  ? 119 VAL A CG1 1 
ATOM   885   C  CG2 . VAL A  1 120 ? -68.331  -47.044 83.273  1.00 34.41  ? 119 VAL A CG2 1 
ATOM   886   N  N   . HIS A  1 121 ? -66.755  -44.415 84.561  1.00 31.31  ? 120 HIS A N   1 
ATOM   887   C  CA  . HIS A  1 121 ? -65.719  -43.411 84.354  1.00 33.00  ? 120 HIS A CA  1 
ATOM   888   C  C   . HIS A  1 121 ? -64.952  -43.656 83.048  1.00 32.77  ? 120 HIS A C   1 
ATOM   889   O  O   . HIS A  1 121 ? -65.004  -44.715 82.430  1.00 31.76  ? 120 HIS A O   1 
ATOM   890   C  CB  . HIS A  1 121 ? -64.755  -43.364 85.542  1.00 33.44  ? 120 HIS A CB  1 
ATOM   891   C  CG  . HIS A  1 121 ? -65.258  -42.646 86.743  1.00 34.44  ? 120 HIS A CG  1 
ATOM   892   N  ND1 . HIS A  1 121 ? -65.034  -41.290 86.935  1.00 36.06  ? 120 HIS A ND1 1 
ATOM   893   C  CD2 . HIS A  1 121 ? -65.935  -43.085 87.833  1.00 33.69  ? 120 HIS A CD2 1 
ATOM   894   C  CE1 . HIS A  1 121 ? -65.553  -40.920 88.087  1.00 35.40  ? 120 HIS A CE1 1 
ATOM   895   N  NE2 . HIS A  1 121 ? -66.101  -42.008 88.669  1.00 39.15  ? 120 HIS A NE2 1 
ATOM   896   N  N   . GLU A  1 122 ? -64.280  -42.593 82.620  1.00 36.78  ? 121 GLU A N   1 
ATOM   897   C  CA  . GLU A  1 122 ? -63.474  -42.546 81.414  1.00 39.27  ? 121 GLU A CA  1 
ATOM   898   C  C   . GLU A  1 122 ? -62.314  -43.552 81.507  1.00 41.59  ? 121 GLU A C   1 
ATOM   899   O  O   . GLU A  1 122 ? -62.049  -44.282 80.559  1.00 38.32  ? 121 GLU A O   1 
ATOM   900   C  CB  . GLU A  1 122 ? -62.973  -41.113 81.278  1.00 44.04  ? 121 GLU A CB  1 
ATOM   901   C  CG  . GLU A  1 122 ? -62.113  -40.832 80.069  1.00 50.63  ? 121 GLU A CG  1 
ATOM   902   C  CD  . GLU A  1 122 ? -61.501  -39.441 80.149  1.00 57.91  ? 121 GLU A CD  1 
ATOM   903   O  OE1 . GLU A  1 122 ? -61.464  -38.752 79.117  1.00 68.95  ? 121 GLU A OE1 1 
ATOM   904   O  OE2 . GLU A  1 122 ? -61.089  -39.039 81.258  1.00 57.62  ? 121 GLU A OE2 1 
ATOM   905   N  N   . LYS A  1 123 ? -61.640  -43.586 82.662  1.00 43.04  ? 122 LYS A N   1 
ATOM   906   C  CA  . LYS A  1 123 ? -60.391  -44.312 82.807  1.00 48.53  ? 122 LYS A CA  1 
ATOM   907   C  C   . LYS A  1 123 ? -60.520  -45.369 83.903  1.00 49.66  ? 122 LYS A C   1 
ATOM   908   O  O   . LYS A  1 123 ? -61.501  -45.393 84.656  1.00 41.68  ? 122 LYS A O   1 
ATOM   909   C  CB  . LYS A  1 123 ? -59.260  -43.351 83.179  1.00 53.99  ? 122 LYS A CB  1 
ATOM   910   C  CG  . LYS A  1 123 ? -59.034  -42.206 82.197  1.00 59.01  ? 122 LYS A CG  1 
ATOM   911   C  CD  . LYS A  1 123 ? -57.857  -41.319 82.542  1.00 62.60  ? 122 LYS A CD  1 
ATOM   912   C  CE  . LYS A  1 123 ? -57.647  -41.158 84.034  1.00 70.79  ? 122 LYS A CE  1 
ATOM   913   N  NZ  . LYS A  1 123 ? -56.722  -40.043 84.352  1.00 77.87  ? 122 LYS A NZ  1 
ATOM   914   N  N   . ALA A  1 124 ? -59.490  -46.220 83.992  1.00 47.77  ? 123 ALA A N   1 
ATOM   915   C  CA  . ALA A  1 124 ? -59.425  -47.248 85.013  1.00 46.67  ? 123 ALA A CA  1 
ATOM   916   C  C   . ALA A  1 124 ? -59.289  -46.585 86.388  1.00 42.93  ? 123 ALA A C   1 
ATOM   917   O  O   . ALA A  1 124 ? -58.702  -45.517 86.549  1.00 44.09  ? 123 ALA A O   1 
ATOM   918   C  CB  . ALA A  1 124 ? -58.279  -48.195 84.735  1.00 49.25  ? 123 ALA A CB  1 
ATOM   919   N  N   . ASP A  1 125 ? -59.921  -47.215 87.367  1.00 44.46  ? 124 ASP A N   1 
ATOM   920   C  CA  . ASP A  1 125 ? -59.716  -46.936 88.749  1.00 49.50  ? 124 ASP A CA  1 
ATOM   921   C  C   . ASP A  1 125 ? -58.417  -47.637 89.155  1.00 48.97  ? 124 ASP A C   1 
ATOM   922   O  O   . ASP A  1 125 ? -58.338  -48.850 89.034  1.00 48.06  ? 124 ASP A O   1 
ATOM   923   C  CB  . ASP A  1 125 ? -60.910  -47.471 89.548  1.00 54.28  ? 124 ASP A CB  1 
ATOM   924   C  CG  . ASP A  1 125 ? -60.924  -47.045 91.001  1.00 56.12  ? 124 ASP A CG  1 
ATOM   925   O  OD1 . ASP A  1 125 ? -59.889  -46.528 91.461  1.00 59.58  ? 124 ASP A OD1 1 
ATOM   926   O  OD2 . ASP A  1 125 ? -61.964  -47.249 91.660  1.00 55.93  ? 124 ASP A OD2 1 
ATOM   927   N  N   . ASP A  1 126 ? -57.422  -46.882 89.632  1.00 57.80  ? 125 ASP A N   1 
ATOM   928   C  CA  . ASP A  1 126 ? -56.128  -47.463 90.075  1.00 65.28  ? 125 ASP A CA  1 
ATOM   929   C  C   . ASP A  1 126 ? -56.283  -48.142 91.449  1.00 66.60  ? 125 ASP A C   1 
ATOM   930   O  O   . ASP A  1 126 ? -55.341  -48.755 91.927  1.00 74.22  ? 125 ASP A O   1 
ATOM   931   C  CB  . ASP A  1 126 ? -54.996  -46.426 90.040  1.00 62.40  ? 125 ASP A CB  1 
ATOM   932   C  CG  . ASP A  1 126 ? -55.104  -45.264 91.018  1.00 67.84  ? 125 ASP A CG  1 
ATOM   933   O  OD1 . ASP A  1 126 ? -54.405  -44.248 90.792  1.00 68.50  ? 125 ASP A OD1 1 
ATOM   934   O  OD2 . ASP A  1 126 ? -55.870  -45.373 91.999  1.00 71.17  ? 125 ASP A OD2 1 
ATOM   935   N  N   . LEU A  1 127 ? -57.461  -47.994 92.077  1.00 68.99  ? 126 LEU A N   1 
ATOM   936   C  CA  . LEU A  1 127 ? -57.880  -48.677 93.321  1.00 72.25  ? 126 LEU A CA  1 
ATOM   937   C  C   . LEU A  1 127 ? -57.115  -48.152 94.548  1.00 77.36  ? 126 LEU A C   1 
ATOM   938   O  O   . LEU A  1 127 ? -57.015  -48.858 95.556  1.00 74.61  ? 126 LEU A O   1 
ATOM   939   C  CB  . LEU A  1 127 ? -57.718  -50.194 93.157  1.00 73.88  ? 126 LEU A CB  1 
ATOM   940   C  CG  . LEU A  1 127 ? -58.536  -50.827 92.031  1.00 75.48  ? 126 LEU A CG  1 
ATOM   941   C  CD1 . LEU A  1 127 ? -58.699  -52.323 92.241  1.00 78.32  ? 126 LEU A CD1 1 
ATOM   942   C  CD2 . LEU A  1 127 ? -59.911  -50.187 91.917  1.00 75.84  ? 126 LEU A CD2 1 
ATOM   943   N  N   . GLY A  1 128 ? -56.618  -46.908 94.479  1.00 82.66  ? 127 GLY A N   1 
ATOM   944   C  CA  . GLY A  1 128 ? -55.984  -46.222 95.620  1.00 86.30  ? 127 GLY A CA  1 
ATOM   945   C  C   . GLY A  1 128 ? -54.462  -46.352 95.667  1.00 92.57  ? 127 GLY A C   1 
ATOM   946   O  O   . GLY A  1 128 ? -53.839  -45.737 96.537  1.00 92.01  ? 127 GLY A O   1 
ATOM   947   N  N   . LYS A  1 129 ? -53.860  -47.103 94.727  1.00 95.16  ? 128 LYS A N   1 
ATOM   948   C  CA  . LYS A  1 129 ? -52.410  -47.444 94.768  1.00 94.79  ? 128 LYS A CA  1 
ATOM   949   C  C   . LYS A  1 129 ? -51.627  -46.617 93.729  1.00 94.64  ? 128 LYS A C   1 
ATOM   950   O  O   . LYS A  1 129 ? -50.626  -47.081 93.175  1.00 89.76  ? 128 LYS A O   1 
ATOM   951   C  CB  . LYS A  1 129 ? -52.196  -48.959 94.614  1.00 96.13  ? 128 LYS A CB  1 
ATOM   952   C  CG  . LYS A  1 129 ? -52.853  -49.651 93.417  1.00 97.50  ? 128 LYS A CG  1 
ATOM   953   C  CD  . LYS A  1 129 ? -52.183  -49.377 92.077  1.00 92.64  ? 128 LYS A CD  1 
ATOM   954   C  CE  . LYS A  1 129 ? -52.383  -50.454 91.029  1.00 90.17  ? 128 LYS A CE  1 
ATOM   955   N  NZ  . LYS A  1 129 ? -53.583  -50.220 90.191  1.00 85.53  ? 128 LYS A NZ  1 
ATOM   956   N  N   . GLY A  1 130 ? -52.061  -45.371 93.504  1.00 89.72  ? 129 GLY A N   1 
ATOM   957   C  CA  . GLY A  1 130 ? -51.385  -44.433 92.605  1.00 89.81  ? 129 GLY A CA  1 
ATOM   958   C  C   . GLY A  1 130 ? -50.278  -43.655 93.304  1.00 87.42  ? 129 GLY A C   1 
ATOM   959   O  O   . GLY A  1 130 ? -49.448  -43.037 92.646  1.00 80.04  ? 129 GLY A O   1 
ATOM   960   N  N   . GLY A  1 131 ? -50.283  -43.672 94.643  1.00 89.48  ? 130 GLY A N   1 
ATOM   961   C  CA  . GLY A  1 131 ? -49.278  -43.001 95.464  1.00 92.79  ? 130 GLY A CA  1 
ATOM   962   C  C   . GLY A  1 131 ? -49.704  -41.591 95.839  1.00 99.86  ? 130 GLY A C   1 
ATOM   963   O  O   . GLY A  1 131 ? -49.662  -41.218 97.017  1.00 100.18 ? 130 GLY A O   1 
ATOM   964   N  N   . ASN A  1 132 ? -50.130  -40.821 94.827  1.00 100.37 ? 131 ASN A N   1 
ATOM   965   C  CA  . ASN A  1 132 ? -50.549  -39.413 94.963  1.00 99.28  ? 131 ASN A CA  1 
ATOM   966   C  C   . ASN A  1 132 ? -51.875  -39.307 95.745  1.00 101.21 ? 131 ASN A C   1 
ATOM   967   O  O   . ASN A  1 132 ? -52.450  -40.310 96.190  1.00 94.47  ? 131 ASN A O   1 
ATOM   968   C  CB  . ASN A  1 132 ? -50.606  -38.728 93.589  1.00 91.29  ? 131 ASN A CB  1 
ATOM   969   C  CG  . ASN A  1 132 ? -51.796  -39.136 92.745  1.00 91.21  ? 131 ASN A CG  1 
ATOM   970   O  OD1 . ASN A  1 132 ? -52.711  -38.345 92.541  1.00 93.00  ? 131 ASN A OD1 1 
ATOM   971   N  ND2 . ASN A  1 132 ? -51.798  -40.362 92.250  1.00 90.02  ? 131 ASN A ND2 1 
ATOM   972   N  N   . GLU A  1 133 ? -52.348  -38.063 95.910  1.00 104.30 ? 132 GLU A N   1 
ATOM   973   C  CA  . GLU A  1 133 ? -53.513  -37.711 96.741  1.00 102.01 ? 132 GLU A CA  1 
ATOM   974   C  C   . GLU A  1 133 ? -54.822  -38.034 96.003  1.00 92.12  ? 132 GLU A C   1 
ATOM   975   O  O   . GLU A  1 133 ? -55.752  -38.595 96.595  1.00 79.48  ? 132 GLU A O   1 
ATOM   976   C  CB  . GLU A  1 133 ? -53.449  -36.224 97.100  1.00 103.78 ? 132 GLU A CB  1 
ATOM   977   C  CG  . GLU A  1 133 ? -54.234  -35.856 98.343  1.00 106.33 ? 132 GLU A CG  1 
ATOM   978   C  CD  . GLU A  1 133 ? -54.291  -34.361 98.607  1.00 111.02 ? 132 GLU A CD  1 
ATOM   979   O  OE1 . GLU A  1 133 ? -55.304  -33.903 99.173  1.00 116.53 ? 132 GLU A OE1 1 
ATOM   980   O  OE2 . GLU A  1 133 ? -53.324  -33.657 98.242  1.00 107.34 ? 132 GLU A OE2 1 
ATOM   981   N  N   . GLU A  1 134 ? -54.877  -37.672 94.714  1.00 85.23  ? 133 GLU A N   1 
ATOM   982   C  CA  . GLU A  1 134 ? -56.041  -37.903 93.840  1.00 87.03  ? 133 GLU A CA  1 
ATOM   983   C  C   . GLU A  1 134 ? -56.438  -39.392 93.854  1.00 83.73  ? 133 GLU A C   1 
ATOM   984   O  O   . GLU A  1 134 ? -57.630  -39.723 93.797  1.00 69.24  ? 133 GLU A O   1 
ATOM   985   C  CB  . GLU A  1 134 ? -55.732  -37.408 92.421  1.00 88.38  ? 133 GLU A CB  1 
ATOM   986   C  CG  . GLU A  1 134 ? -56.920  -37.433 91.474  1.00 92.66  ? 133 GLU A CG  1 
ATOM   987   C  CD  . GLU A  1 134 ? -58.131  -36.642 91.941  1.00 99.33  ? 133 GLU A CD  1 
ATOM   988   O  OE1 . GLU A  1 134 ? -59.261  -37.133 91.746  1.00 99.57  ? 133 GLU A OE1 1 
ATOM   989   O  OE2 . GLU A  1 134 ? -57.945  -35.539 92.502  1.00 98.66  ? 133 GLU A OE2 1 
ATOM   990   N  N   . SER A  1 135 ? -55.438  -40.282 93.933  1.00 76.88  ? 134 SER A N   1 
ATOM   991   C  CA  . SER A  1 135 ? -55.653  -41.738 93.961  1.00 78.97  ? 134 SER A CA  1 
ATOM   992   C  C   . SER A  1 135 ? -56.468  -42.169 95.194  1.00 80.20  ? 134 SER A C   1 
ATOM   993   O  O   . SER A  1 135 ? -57.200  -43.159 95.126  1.00 73.00  ? 134 SER A O   1 
ATOM   994   C  CB  . SER A  1 135 ? -54.340  -42.484 93.900  1.00 77.55  ? 134 SER A CB  1 
ATOM   995   O  OG  . SER A  1 135 ? -54.554  -43.886 94.019  1.00 69.46  ? 134 SER A OG  1 
ATOM   996   N  N   . THR A  1 136 ? -56.341  -41.438 96.312  1.00 84.80  ? 135 THR A N   1 
ATOM   997   C  CA  . THR A  1 136 ? -56.997  -41.817 97.581  1.00 88.33  ? 135 THR A CA  1 
ATOM   998   C  C   . THR A  1 136 ? -58.376  -41.140 97.705  1.00 87.88  ? 135 THR A C   1 
ATOM   999   O  O   . THR A  1 136 ? -58.968  -41.144 98.795  1.00 81.56  ? 135 THR A O   1 
ATOM   1000  C  CB  . THR A  1 136 ? -56.091  -41.527 98.790  1.00 84.73  ? 135 THR A CB  1 
ATOM   1001  O  OG1 . THR A  1 136 ? -56.122  -40.130 99.085  1.00 85.93  ? 135 THR A OG1 1 
ATOM   1002  C  CG2 . THR A  1 136 ? -54.657  -41.962 98.580  1.00 84.28  ? 135 THR A CG2 1 
ATOM   1003  N  N   . LYS A  1 137 ? -58.899  -40.595 96.594  1.00 88.78  ? 136 LYS A N   1 
ATOM   1004  C  CA  . LYS A  1 137 ? -60.220  -39.932 96.582  1.00 94.26  ? 136 LYS A CA  1 
ATOM   1005  C  C   . LYS A  1 137 ? -61.080  -40.449 95.405  1.00 90.23  ? 136 LYS A C   1 
ATOM   1006  O  O   . LYS A  1 137 ? -62.263  -40.757 95.614  1.00 86.84  ? 136 LYS A O   1 
ATOM   1007  C  CB  . LYS A  1 137 ? -60.015  -38.409 96.676  1.00 94.83  ? 136 LYS A CB  1 
ATOM   1008  C  CG  . LYS A  1 137 ? -60.115  -37.586 95.394  1.00 98.27  ? 136 LYS A CG  1 
ATOM   1009  C  CD  . LYS A  1 137 ? -61.429  -36.815 95.264  1.00 101.70 ? 136 LYS A CD  1 
ATOM   1010  C  CE  . LYS A  1 137 ? -61.429  -35.769 94.166  1.00 97.25  ? 136 LYS A CE  1 
ATOM   1011  N  NZ  . LYS A  1 137 ? -60.502  -34.651 94.463  1.00 97.89  ? 136 LYS A NZ  1 
ATOM   1012  N  N   . THR A  1 138 ? -60.501  -40.571 94.195  1.00 87.45  ? 137 THR A N   1 
ATOM   1013  C  CA  . THR A  1 138 ? -61.239  -41.000 92.970  1.00 85.29  ? 137 THR A CA  1 
ATOM   1014  C  C   . THR A  1 138 ? -60.634  -42.239 92.293  1.00 83.30  ? 137 THR A C   1 
ATOM   1015  O  O   . THR A  1 138 ? -61.266  -42.807 91.397  1.00 83.74  ? 137 THR A O   1 
ATOM   1016  C  CB  . THR A  1 138 ? -61.254  -39.912 91.886  1.00 87.13  ? 137 THR A CB  1 
ATOM   1017  O  OG1 . THR A  1 138 ? -59.904  -39.644 91.490  1.00 76.79  ? 137 THR A OG1 1 
ATOM   1018  C  CG2 . THR A  1 138 ? -61.946  -38.646 92.340  1.00 86.03  ? 137 THR A CG2 1 
ATOM   1019  N  N   . GLY A  1 139 ? -59.404  -42.616 92.666  1.00 79.02  ? 138 GLY A N   1 
ATOM   1020  C  CA  . GLY A  1 139 ? -58.638  -43.652 91.953  1.00 73.77  ? 138 GLY A CA  1 
ATOM   1021  C  C   . GLY A  1 139 ? -58.104  -43.176 90.606  1.00 66.02  ? 138 GLY A C   1 
ATOM   1022  O  O   . GLY A  1 139 ? -57.727  -43.995 89.762  1.00 61.21  ? 138 GLY A O   1 
ATOM   1023  N  N   . ASN A  1 140 ? -58.059  -41.848 90.415  1.00 64.68  ? 139 ASN A N   1 
ATOM   1024  C  CA  . ASN A  1 140 ? -57.611  -41.216 89.171  1.00 68.36  ? 139 ASN A CA  1 
ATOM   1025  C  C   . ASN A  1 140 ? -58.444  -41.729 87.982  1.00 61.41  ? 139 ASN A C   1 
ATOM   1026  O  O   . ASN A  1 140 ? -57.883  -41.966 86.911  1.00 58.74  ? 139 ASN A O   1 
ATOM   1027  C  CB  . ASN A  1 140 ? -56.114  -41.459 88.927  1.00 69.32  ? 139 ASN A CB  1 
ATOM   1028  C  CG  . ASN A  1 140 ? -55.219  -40.679 89.867  1.00 72.43  ? 139 ASN A CG  1 
ATOM   1029  O  OD1 . ASN A  1 140 ? -55.170  -39.451 89.801  1.00 72.91  ? 139 ASN A OD1 1 
ATOM   1030  N  ND2 . ASN A  1 140 ? -54.493  -41.382 90.724  1.00 68.23  ? 139 ASN A ND2 1 
ATOM   1031  N  N   . ALA A  1 141 ? -59.765  -41.887 88.175  1.00 53.15  ? 140 ALA A N   1 
ATOM   1032  C  CA  . ALA A  1 141 ? -60.653  -42.576 87.197  1.00 50.35  ? 140 ALA A CA  1 
ATOM   1033  C  C   . ALA A  1 141 ? -61.145  -41.616 86.097  1.00 45.89  ? 140 ALA A C   1 
ATOM   1034  O  O   . ALA A  1 141 ? -61.717  -42.060 85.096  1.00 43.48  ? 140 ALA A O   1 
ATOM   1035  C  CB  . ALA A  1 141 ? -61.814  -43.221 87.917  1.00 48.83  ? 140 ALA A CB  1 
ATOM   1036  N  N   . GLY A  1 142 ? -60.963  -40.306 86.296  1.00 44.65  ? 141 GLY A N   1 
ATOM   1037  C  CA  . GLY A  1 142 ? -61.234  -39.310 85.252  1.00 44.58  ? 141 GLY A CA  1 
ATOM   1038  C  C   . GLY A  1 142 ? -62.713  -38.984 85.131  1.00 43.80  ? 141 GLY A C   1 
ATOM   1039  O  O   . GLY A  1 142 ? -63.450  -39.098 86.100  1.00 42.90  ? 141 GLY A O   1 
ATOM   1040  N  N   . SER A  1 143 ? -63.120  -38.572 83.924  1.00 41.21  ? 142 SER A N   1 
ATOM   1041  C  CA  . SER A  1 143 ? -64.453  -38.065 83.613  1.00 41.47  ? 142 SER A CA  1 
ATOM   1042  C  C   . SER A  1 143 ? -65.531  -39.098 83.942  1.00 36.79  ? 142 SER A C   1 
ATOM   1043  O  O   . SER A  1 143 ? -65.325  -40.312 83.773  1.00 36.23  ? 142 SER A O   1 
ATOM   1044  C  CB  . SER A  1 143 ? -64.578  -37.686 82.154  1.00 43.02  ? 142 SER A CB  1 
ATOM   1045  O  OG  . SER A  1 143 ? -64.116  -36.368 81.943  1.00 57.96  ? 142 SER A OG  1 
ATOM   1046  N  N   . ARG A  1 144 ? -66.707  -38.567 84.290  1.00 34.39  ? 143 ARG A N   1 
ATOM   1047  C  CA  . ARG A  1 144 ? -67.910  -39.335 84.467  1.00 35.38  ? 143 ARG A CA  1 
ATOM   1048  C  C   . ARG A  1 144 ? -68.626  -39.447 83.115  1.00 35.85  ? 143 ARG A C   1 
ATOM   1049  O  O   . ARG A  1 144 ? -69.170  -38.480 82.622  1.00 34.58  ? 143 ARG A O   1 
ATOM   1050  C  CB  . ARG A  1 144 ? -68.767  -38.668 85.541  1.00 32.80  ? 143 ARG A CB  1 
ATOM   1051  C  CG  . ARG A  1 144 ? -68.008  -38.457 86.843  1.00 33.10  ? 143 ARG A CG  1 
ATOM   1052  C  CD  . ARG A  1 144 ? -68.805  -37.689 87.870  1.00 35.14  ? 143 ARG A CD  1 
ATOM   1053  N  NE  . ARG A  1 144 ? -67.976  -37.339 89.009  1.00 34.74  ? 143 ARG A NE  1 
ATOM   1054  C  CZ  . ARG A  1 144 ? -68.417  -36.964 90.212  1.00 35.63  ? 143 ARG A CZ  1 
ATOM   1055  N  NH1 . ARG A  1 144 ? -67.532  -36.793 91.179  1.00 31.31  ? 143 ARG A NH1 1 
ATOM   1056  N  NH2 . ARG A  1 144 ? -69.709  -36.770 90.449  1.00 30.25  ? 143 ARG A NH2 1 
ATOM   1057  N  N   . LEU A  1 145 ? -68.618  -40.646 82.531  1.00 33.15  ? 144 LEU A N   1 
ATOM   1058  C  CA  . LEU A  1 145 ? -69.105  -40.854 81.162  1.00 34.09  ? 144 LEU A CA  1 
ATOM   1059  C  C   . LEU A  1 145 ? -70.630  -41.021 81.140  1.00 34.78  ? 144 LEU A C   1 
ATOM   1060  O  O   . LEU A  1 145 ? -71.309  -40.639 80.171  1.00 31.42  ? 144 LEU A O   1 
ATOM   1061  C  CB  . LEU A  1 145 ? -68.423  -42.094 80.586  1.00 35.19  ? 144 LEU A CB  1 
ATOM   1062  C  CG  . LEU A  1 145 ? -67.244  -41.846 79.648  1.00 39.64  ? 144 LEU A CG  1 
ATOM   1063  C  CD1 . LEU A  1 145 ? -66.397  -40.668 80.070  1.00 39.49  ? 144 LEU A CD1 1 
ATOM   1064  C  CD2 . LEU A  1 145 ? -66.405  -43.100 79.524  1.00 43.48  ? 144 LEU A CD2 1 
ATOM   1065  N  N   . ALA A  1 146 ? -71.158  -41.667 82.177  1.00 30.34  ? 145 ALA A N   1 
ATOM   1066  C  CA  . ALA A  1 146 ? -72.568  -41.959 82.265  1.00 28.84  ? 145 ALA A CA  1 
ATOM   1067  C  C   . ALA A  1 146 ? -72.904  -42.283 83.718  1.00 31.21  ? 145 ALA A C   1 
ATOM   1068  O  O   . ALA A  1 146 ? -72.032  -42.730 84.491  1.00 30.47  ? 145 ALA A O   1 
ATOM   1069  C  CB  . ALA A  1 146 ? -72.958  -43.098 81.368  1.00 29.06  ? 145 ALA A CB  1 
ATOM   1070  N  N   . CYS A  1 147 ? -74.152  -42.001 84.080  1.00 30.22  ? 146 CYS A N   1 
ATOM   1071  C  CA  . CYS A  1 147 ? -74.624  -42.235 85.407  1.00 32.26  ? 146 CYS A CA  1 
ATOM   1072  C  C   . CYS A  1 147 ? -76.143  -42.394 85.404  1.00 33.23  ? 146 CYS A C   1 
ATOM   1073  O  O   . CYS A  1 147 ? -76.826  -42.112 84.421  1.00 27.73  ? 146 CYS A O   1 
ATOM   1074  C  CB  . CYS A  1 147 ? -74.226  -41.091 86.330  1.00 34.60  ? 146 CYS A CB  1 
ATOM   1075  S  SG  . CYS A  1 147 ? -74.798  -39.463 85.786  1.00 38.61  ? 146 CYS A SG  1 
ATOM   1076  N  N   . GLY A  1 148 ? -76.656  -42.863 86.536  1.00 29.07  ? 147 GLY A N   1 
ATOM   1077  C  CA  . GLY A  1 148 ? -78.069  -42.961 86.756  1.00 30.35  ? 147 GLY A CA  1 
ATOM   1078  C  C   . GLY A  1 148 ? -78.346  -43.087 88.237  1.00 29.03  ? 147 GLY A C   1 
ATOM   1079  O  O   . GLY A  1 148 ? -77.466  -43.485 88.982  1.00 29.48  ? 147 GLY A O   1 
ATOM   1080  N  N   . VAL A  1 149 ? -79.560  -42.734 88.637  1.00 26.47  ? 148 VAL A N   1 
ATOM   1081  C  CA  . VAL A  1 149 ? -80.008  -42.942 89.986  1.00 28.98  ? 148 VAL A CA  1 
ATOM   1082  C  C   . VAL A  1 149 ? -80.431  -44.417 90.149  1.00 30.47  ? 148 VAL A C   1 
ATOM   1083  O  O   . VAL A  1 149 ? -81.147  -45.001 89.291  1.00 29.39  ? 148 VAL A O   1 
ATOM   1084  C  CB  . VAL A  1 149 ? -81.156  -41.984 90.338  1.00 29.66  ? 148 VAL A CB  1 
ATOM   1085  C  CG1 . VAL A  1 149 ? -81.557  -42.113 91.794  1.00 30.92  ? 148 VAL A CG1 1 
ATOM   1086  C  CG2 . VAL A  1 149 ? -80.815  -40.538 90.006  1.00 30.80  ? 148 VAL A CG2 1 
ATOM   1087  N  N   . ILE A  1 150 ? -79.991  -45.017 91.262  1.00 29.39  ? 149 ILE A N   1 
ATOM   1088  C  CA  . ILE A  1 150 ? -80.299  -46.412 91.603  1.00 30.11  ? 149 ILE A CA  1 
ATOM   1089  C  C   . ILE A  1 150 ? -81.703  -46.468 92.214  1.00 29.98  ? 149 ILE A C   1 
ATOM   1090  O  O   . ILE A  1 150 ? -81.998  -45.839 93.230  1.00 30.26  ? 149 ILE A O   1 
ATOM   1091  C  CB  . ILE A  1 150 ? -79.210  -47.006 92.515  1.00 32.71  ? 149 ILE A CB  1 
ATOM   1092  C  CG1 . ILE A  1 150 ? -77.831  -46.933 91.851  1.00 35.82  ? 149 ILE A CG1 1 
ATOM   1093  C  CG2 . ILE A  1 150 ? -79.540  -48.437 92.922  1.00 33.19  ? 149 ILE A CG2 1 
ATOM   1094  C  CD1 . ILE A  1 150 ? -76.660  -47.111 92.805  1.00 36.76  ? 149 ILE A CD1 1 
ATOM   1095  N  N   . GLY A  1 151 ? -82.596  -47.188 91.535  1.00 28.69  ? 150 GLY A N   1 
ATOM   1096  C  CA  . GLY A  1 151 ? -84.003  -47.222 91.889  1.00 27.92  ? 150 GLY A CA  1 
ATOM   1097  C  C   . GLY A  1 151 ? -84.417  -48.588 92.387  1.00 28.66  ? 150 GLY A C   1 
ATOM   1098  O  O   . GLY A  1 151 ? -83.751  -49.566 92.114  1.00 30.47  ? 150 GLY A O   1 
ATOM   1099  N  N   . ILE A  1 152 ? -85.516  -48.632 93.133  1.00 31.36  ? 151 ILE A N   1 
ATOM   1100  C  CA  . ILE A  1 152 ? -86.125  -49.890 93.587  1.00 33.55  ? 151 ILE A CA  1 
ATOM   1101  C  C   . ILE A  1 152 ? -86.736  -50.593 92.371  1.00 34.24  ? 151 ILE A C   1 
ATOM   1102  O  O   . ILE A  1 152 ? -87.497  -49.996 91.611  1.00 34.80  ? 151 ILE A O   1 
ATOM   1103  C  CB  . ILE A  1 152 ? -87.176  -49.625 94.687  1.00 36.08  ? 151 ILE A CB  1 
ATOM   1104  C  CG1 . ILE A  1 152 ? -86.512  -49.156 95.980  1.00 36.77  ? 151 ILE A CG1 1 
ATOM   1105  C  CG2 . ILE A  1 152 ? -88.052  -50.840 94.941  1.00 36.82  ? 151 ILE A CG2 1 
ATOM   1106  C  CD1 . ILE A  1 152 ? -87.432  -48.374 96.879  1.00 37.92  ? 151 ILE A CD1 1 
ATOM   1107  N  N   . ALA A  1 153 ? -86.369  -51.860 92.182  1.00 33.79  ? 152 ALA A N   1 
ATOM   1108  C  CA  . ALA A  1 153 ? -86.909  -52.676 91.105  1.00 40.23  ? 152 ALA A CA  1 
ATOM   1109  C  C   . ALA A  1 153 ? -87.892  -53.695 91.710  1.00 42.59  ? 152 ALA A C   1 
ATOM   1110  O  O   . ALA A  1 153 ? -87.860  -53.938 92.921  1.00 44.46  ? 152 ALA A O   1 
ATOM   1111  C  CB  . ALA A  1 153 ? -85.772  -53.337 90.375  1.00 38.71  ? 152 ALA A CB  1 
ATOM   1112  N  N   . GLN A  1 154 ? -88.743  -54.287 90.873  1.00 49.96  ? 153 GLN A N   1 
ATOM   1113  C  CA  . GLN A  1 154 ? -89.824  -55.177 91.326  1.00 59.36  ? 153 GLN A CA  1 
ATOM   1114  C  C   . GLN A  1 154 ? -89.283  -56.341 92.171  1.00 67.47  ? 153 GLN A C   1 
ATOM   1115  O  O   . GLN A  1 154 ? -88.848  -57.354 91.643  1.00 77.88  ? 153 GLN A O   1 
ATOM   1116  C  CB  . GLN A  1 154 ? -90.613  -55.718 90.139  1.00 60.94  ? 153 GLN A CB  1 
ATOM   1117  C  CG  . GLN A  1 154 ? -91.723  -56.677 90.558  1.00 67.78  ? 153 GLN A CG  1 
ATOM   1118  C  CD  . GLN A  1 154 ? -92.923  -56.618 89.642  1.00 73.06  ? 153 GLN A CD  1 
ATOM   1119  O  OE1 . GLN A  1 154 ? -94.038  -56.341 90.078  1.00 79.12  ? 153 GLN A OE1 1 
ATOM   1120  N  NE2 . GLN A  1 154 ? -92.703  -56.863 88.357  1.00 70.46  ? 153 GLN A NE2 1 
ATOM   1121  N  N   . GLY A  1 155 ? -89.340  -56.165 93.495  1.00 73.69  ? 154 GLY A N   1 
ATOM   1122  C  CA  . GLY A  1 155 ? -89.035  -57.187 94.488  1.00 79.96  ? 154 GLY A CA  1 
ATOM   1123  C  C   . GLY A  1 155 ? -89.401  -56.694 95.883  1.00 84.93  ? 154 GLY A C   1 
ATOM   1124  O  O   . GLY A  1 155 ? -90.485  -56.134 96.065  1.00 84.91  ? 154 GLY A O   1 
ATOM   1125  N  N   . ALA A  1 156 ? -88.479  -56.881 96.842  1.00 86.06  ? 155 ALA A N   1 
ATOM   1126  C  CA  . ALA A  1 156 ? -88.572  -56.417 98.246  1.00 83.84  ? 155 ALA A CA  1 
ATOM   1127  C  C   . ALA A  1 156 ? -89.682  -57.165 98.986  1.00 83.21  ? 155 ALA A C   1 
ATOM   1128  O  O   . ALA A  1 156 ? -90.021  -56.787 100.102 1.00 85.08  ? 155 ALA A O   1 
ATOM   1129  C  CB  . ALA A  1 156 ? -88.785  -54.923 98.317  1.00 84.68  ? 155 ALA A CB  1 
ATOM   1130  N  N   . GLY A  1 167 ? -88.773  -50.975 101.434 1.00 74.86  ? 166 GLY A N   1 
ATOM   1131  C  CA  . GLY A  1 167 ? -87.303  -50.899 101.178 1.00 77.52  ? 166 GLY A CA  1 
ATOM   1132  C  C   . GLY A  1 167 ? -86.875  -49.517 100.710 1.00 76.31  ? 166 GLY A C   1 
ATOM   1133  O  O   . GLY A  1 167 ? -87.716  -48.672 100.392 1.00 81.28  ? 166 GLY A O   1 
ATOM   1134  N  N   . GLY A  1 168 ? -85.559  -49.274 100.701 1.00 72.90  ? 167 GLY A N   1 
ATOM   1135  C  CA  . GLY A  1 168 ? -85.001  -48.131 99.988  1.00 71.69  ? 167 GLY A CA  1 
ATOM   1136  C  C   . GLY A  1 168 ? -83.968  -47.357 100.784 1.00 65.80  ? 167 GLY A C   1 
ATOM   1137  O  O   . GLY A  1 168 ? -82.965  -47.953 101.205 1.00 57.40  ? 167 GLY A O   1 
ATOM   1138  N  N   . GLY A  1 169 ? -84.203  -46.036 100.943 1.00 64.82  ? 168 GLY A N   1 
ATOM   1139  C  CA  . GLY A  1 169 ? -83.170  -45.074 101.403 1.00 61.96  ? 168 GLY A CA  1 
ATOM   1140  C  C   . GLY A  1 169 ? -83.709  -43.829 102.111 1.00 63.73  ? 168 GLY A C   1 
ATOM   1141  O  O   . GLY A  1 169 ? -84.938  -43.608 102.211 1.00 53.49  ? 168 GLY A O   1 
ATOM   1142  N  N   . SER A  1 170 ? -82.768  -42.973 102.557 1.00 60.71  ? 169 SER A N   1 
ATOM   1143  C  CA  . SER A  1 170 ? -83.004  -42.004 103.654 1.00 65.72  ? 169 SER A CA  1 
ATOM   1144  C  C   . SER A  1 170 ? -82.245  -40.682 103.450 1.00 58.26  ? 169 SER A C   1 
ATOM   1145  O  O   . SER A  1 170 ? -81.041  -40.694 103.204 1.00 58.63  ? 169 SER A O   1 
ATOM   1146  C  CB  . SER A  1 170 ? -82.624  -42.623 104.976 1.00 69.41  ? 169 SER A CB  1 
ATOM   1147  O  OG  . SER A  1 170 ? -83.780  -43.030 105.687 1.00 75.94  ? 169 SER A OG  1 
ATOM   1148  N  N   . ALA A  1 171 ? -82.949  -39.554 103.643 1.00 47.97  ? 170 ALA A N   1 
ATOM   1149  C  CA  . ALA A  1 171 ? -82.424  -38.202 103.380 1.00 47.16  ? 170 ALA A CA  1 
ATOM   1150  C  C   . ALA A  1 171 ? -83.396  -37.126 103.890 1.00 44.16  ? 170 ALA A C   1 
ATOM   1151  O  O   . ALA A  1 171 ? -84.541  -37.429 104.196 1.00 45.83  ? 170 ALA A O   1 
ATOM   1152  C  CB  . ALA A  1 171 ? -82.206  -38.048 101.898 1.00 46.11  ? 170 ALA A CB  1 
ATOM   1153  N  N   . THR A  1 172 ? -82.923  -35.872 103.946 1.00 42.97  ? 171 THR A N   1 
ATOM   1154  C  CA  . THR A  1 172 ? -83.744  -34.685 104.271 1.00 42.85  ? 171 THR A CA  1 
ATOM   1155  C  C   . THR A  1 172 ? -84.040  -33.825 103.025 1.00 38.05  ? 171 THR A C   1 
ATOM   1156  O  O   . THR A  1 172 ? -84.887  -32.954 103.075 1.00 32.63  ? 171 THR A O   1 
ATOM   1157  C  CB  . THR A  1 172 ? -83.056  -33.813 105.330 1.00 46.57  ? 171 THR A CB  1 
ATOM   1158  O  OG1 A THR A  1 172 ? -81.821  -33.351 104.783 0.60 47.61  ? 171 THR A OG1 1 
ATOM   1159  O  OG1 B THR A  1 172 ? -81.820  -33.350 104.785 0.40 46.96  ? 171 THR A OG1 1 
ATOM   1160  C  CG2 A THR A  1 172 ? -82.800  -34.553 106.624 0.60 49.05  ? 171 THR A CG2 1 
ATOM   1161  C  CG2 B THR A  1 172 ? -82.800  -34.552 106.625 0.40 47.98  ? 171 THR A CG2 1 
ATOM   1162  N  N   . LYS A  1 173 ? -83.330  -34.052 101.912 1.00 38.16  ? 172 LYS A N   1 
ATOM   1163  C  CA  . LYS A  1 173 ? -83.646  -33.408 100.614 1.00 38.94  ? 172 LYS A CA  1 
ATOM   1164  C  C   . LYS A  1 173 ? -83.533  -34.471 99.525  1.00 34.14  ? 172 LYS A C   1 
ATOM   1165  O  O   . LYS A  1 173 ? -82.660  -35.339 99.601  1.00 30.78  ? 172 LYS A O   1 
ATOM   1166  C  CB  . LYS A  1 173 ? -82.685  -32.266 100.258 1.00 45.51  ? 172 LYS A CB  1 
ATOM   1167  C  CG  . LYS A  1 173 ? -82.788  -31.009 101.108 1.00 51.04  ? 172 LYS A CG  1 
ATOM   1168  C  CD  . LYS A  1 173 ? -83.271  -29.804 100.340 1.00 58.91  ? 172 LYS A CD  1 
ATOM   1169  C  CE  . LYS A  1 173 ? -82.143  -28.940 99.816  1.00 63.21  ? 172 LYS A CE  1 
ATOM   1170  N  NZ  . LYS A  1 173 ? -81.818  -27.851 100.771 1.00 66.14  ? 172 LYS A NZ  1 
ATOM   1171  N  N   . ALA A  1 174 ? -84.425  -34.403 98.530  1.00 30.24  ? 173 ALA A N   1 
ATOM   1172  C  CA  . ALA A  1 174 ? -84.322  -35.283 97.395  1.00 29.42  ? 173 ALA A CA  1 
ATOM   1173  C  C   . ALA A  1 174 ? -84.623  -34.493 96.123  1.00 27.69  ? 173 ALA A C   1 
ATOM   1174  O  O   . ALA A  1 174 ? -85.124  -33.397 96.175  1.00 25.69  ? 173 ALA A O   1 
ATOM   1175  C  CB  . ALA A  1 174 ? -85.243  -36.462 97.550  1.00 30.16  ? 173 ALA A CB  1 
ATOM   1176  N  N   . VAL A  1 175 ? -84.336  -35.102 94.972  1.00 27.10  ? 174 VAL A N   1 
ATOM   1177  C  CA  . VAL A  1 175 ? -84.529  -34.392 93.745  1.00 27.90  ? 174 VAL A CA  1 
ATOM   1178  C  C   . VAL A  1 175 ? -84.865  -35.420 92.680  1.00 26.15  ? 174 VAL A C   1 
ATOM   1179  O  O   . VAL A  1 175 ? -84.461  -36.601 92.784  1.00 25.73  ? 174 VAL A O   1 
ATOM   1180  C  CB  . VAL A  1 175 ? -83.281  -33.555 93.396  1.00 28.67  ? 174 VAL A CB  1 
ATOM   1181  C  CG1 . VAL A  1 175 ? -82.103  -34.444 93.040  1.00 29.79  ? 174 VAL A CG1 1 
ATOM   1182  C  CG2 . VAL A  1 175 ? -83.546  -32.532 92.305  1.00 31.82  ? 174 VAL A CG2 1 
ATOM   1183  N  N   . CYS A  1 176 ? -85.582  -34.947 91.662  1.00 26.81  ? 175 CYS A N   1 
ATOM   1184  C  CA  . CYS A  1 176 ? -86.014  -35.787 90.579  1.00 25.73  ? 175 CYS A CA  1 
ATOM   1185  C  C   . CYS A  1 176 ? -85.880  -35.005 89.277  1.00 25.10  ? 175 CYS A C   1 
ATOM   1186  O  O   . CYS A  1 176 ? -86.437  -33.913 89.173  1.00 23.61  ? 175 CYS A O   1 
ATOM   1187  C  CB  . CYS A  1 176 ? -87.477  -36.181 90.757  1.00 27.39  ? 175 CYS A CB  1 
ATOM   1188  S  SG  . CYS A  1 176 ? -88.008  -37.388 89.520  1.00 30.26  ? 175 CYS A SG  1 
ATOM   1189  N  N   . VAL A  1 177 ? -85.197  -35.601 88.299  1.00 25.83  ? 176 VAL A N   1 
ATOM   1190  C  CA  . VAL A  1 177 ? -85.141  -35.045 86.938  1.00 26.60  ? 176 VAL A CA  1 
ATOM   1191  C  C   . VAL A  1 177 ? -86.168  -35.797 86.098  1.00 25.57  ? 176 VAL A C   1 
ATOM   1192  O  O   . VAL A  1 177 ? -85.983  -36.972 85.880  1.00 23.17  ? 176 VAL A O   1 
ATOM   1193  C  CB  . VAL A  1 177 ? -83.740  -35.160 86.311  1.00 27.22  ? 176 VAL A CB  1 
ATOM   1194  C  CG1 . VAL A  1 177 ? -83.739  -34.616 84.889  1.00 29.26  ? 176 VAL A CG1 1 
ATOM   1195  C  CG2 . VAL A  1 177 ? -82.698  -34.427 87.144  1.00 29.36  ? 176 VAL A CG2 1 
ATOM   1196  N  N   . LEU A  1 178 ? -87.240  -35.115 85.674  1.00 25.20  ? 177 LEU A N   1 
ATOM   1197  C  CA  . LEU A  1 178 ? -88.288  -35.740 84.855  1.00 28.31  ? 177 LEU A CA  1 
ATOM   1198  C  C   . LEU A  1 178 ? -87.930  -35.621 83.366  1.00 28.02  ? 177 LEU A C   1 
ATOM   1199  O  O   . LEU A  1 178 ? -87.613  -34.536 82.906  1.00 27.81  ? 177 LEU A O   1 
ATOM   1200  C  CB  . LEU A  1 178 ? -89.621  -35.049 85.126  1.00 30.02  ? 177 LEU A CB  1 
ATOM   1201  C  CG  . LEU A  1 178 ? -90.123  -35.161 86.566  1.00 33.50  ? 177 LEU A CG  1 
ATOM   1202  C  CD1 A LEU A  1 178 ? -91.091  -34.048 86.890  0.60 36.66  ? 177 LEU A CD1 1 
ATOM   1203  C  CD1 B LEU A  1 178 ? -91.090  -34.042 86.891  0.40 35.42  ? 177 LEU A CD1 1 
ATOM   1204  C  CD2 A LEU A  1 178 ? -90.788  -36.499 86.793  0.60 35.66  ? 177 LEU A CD2 1 
ATOM   1205  C  CD2 B LEU A  1 178 ? -90.786  -36.502 86.799  0.40 34.71  ? 177 LEU A CD2 1 
ATOM   1206  N  N   . LYS A  1 179 ? -88.017  -36.742 82.649  1.00 27.40  ? 178 LYS A N   1 
ATOM   1207  C  CA  . LYS A  1 179 ? -87.833  -36.821 81.200  1.00 33.37  ? 178 LYS A CA  1 
ATOM   1208  C  C   . LYS A  1 179 ? -88.831  -37.839 80.641  1.00 32.09  ? 178 LYS A C   1 
ATOM   1209  O  O   . LYS A  1 179 ? -89.240  -38.741 81.359  1.00 30.69  ? 178 LYS A O   1 
ATOM   1210  C  CB  . LYS A  1 179 ? -86.384  -37.211 80.877  1.00 37.96  ? 178 LYS A CB  1 
ATOM   1211  C  CG  . LYS A  1 179 ? -85.399  -36.052 81.008  1.00 49.00  ? 178 LYS A CG  1 
ATOM   1212  C  CD  . LYS A  1 179 ? -83.957  -36.361 80.629  1.00 59.40  ? 178 LYS A CD  1 
ATOM   1213  C  CE  . LYS A  1 179 ? -83.107  -36.872 81.779  1.00 66.72  ? 178 LYS A CE  1 
ATOM   1214  N  NZ  . LYS A  1 179 ? -81.747  -36.268 81.780  1.00 67.59  ? 178 LYS A NZ  1 
ATOM   1215  N  N   . GLY A  1 180 ? -89.194  -37.704 79.357  1.00 31.27  ? 179 GLY A N   1 
ATOM   1216  C  CA  . GLY A  1 180 ? -90.018  -38.718 78.688  1.00 36.20  ? 179 GLY A CA  1 
ATOM   1217  C  C   . GLY A  1 180 ? -89.735  -38.832 77.196  1.00 37.88  ? 179 GLY A C   1 
ATOM   1218  O  O   . GLY A  1 180 ? -88.723  -38.343 76.710  1.00 34.33  ? 179 GLY A O   1 
ATOM   1219  N  N   . ASP A  1 181 ? -90.654  -39.486 76.480  1.00 43.84  ? 180 ASP A N   1 
ATOM   1220  C  CA  . ASP A  1 181 ? -90.545  -39.674 75.022  1.00 51.72  ? 180 ASP A CA  1 
ATOM   1221  C  C   . ASP A  1 181 ? -90.669  -38.311 74.323  1.00 48.69  ? 180 ASP A C   1 
ATOM   1222  O  O   . ASP A  1 181 ? -89.892  -37.981 73.439  1.00 61.69  ? 180 ASP A O   1 
ATOM   1223  C  CB  . ASP A  1 181 ? -91.583  -40.682 74.524  1.00 58.25  ? 180 ASP A CB  1 
ATOM   1224  C  CG  . ASP A  1 181 ? -91.048  -42.102 74.480  1.00 66.35  ? 180 ASP A CG  1 
ATOM   1225  O  OD1 . ASP A  1 181 ? -90.062  -42.330 73.749  1.00 74.06  ? 180 ASP A OD1 1 
ATOM   1226  O  OD2 . ASP A  1 181 ? -91.610  -42.964 75.183  1.00 77.75  ? 180 ASP A OD2 1 
ATOM   1227  N  N   . GLY A  1 182 ? -91.620  -37.505 74.792  1.00 42.44  ? 181 GLY A N   1 
ATOM   1228  C  CA  . GLY A  1 182 ? -91.985  -36.264 74.186  1.00 36.35  ? 181 GLY A CA  1 
ATOM   1229  C  C   . GLY A  1 182 ? -91.218  -35.082 74.760  1.00 33.63  ? 181 GLY A C   1 
ATOM   1230  O  O   . GLY A  1 182 ? -90.092  -35.218 75.225  1.00 34.72  ? 181 GLY A O   1 
ATOM   1231  N  N   . PRO A  1 183 ? -91.823  -33.878 74.712  1.00 31.31  ? 182 PRO A N   1 
ATOM   1232  C  CA  . PRO A  1 183 ? -91.164  -32.654 75.152  1.00 30.43  ? 182 PRO A CA  1 
ATOM   1233  C  C   . PRO A  1 183 ? -91.249  -32.325 76.644  1.00 29.39  ? 182 PRO A C   1 
ATOM   1234  O  O   . PRO A  1 183 ? -90.708  -31.321 77.082  1.00 28.13  ? 182 PRO A O   1 
ATOM   1235  C  CB  . PRO A  1 183 ? -91.958  -31.593 74.383  1.00 30.22  ? 182 PRO A CB  1 
ATOM   1236  C  CG  . PRO A  1 183 ? -93.358  -32.131 74.348  1.00 30.44  ? 182 PRO A CG  1 
ATOM   1237  C  CD  . PRO A  1 183 ? -93.186  -33.634 74.211  1.00 31.20  ? 182 PRO A CD  1 
ATOM   1238  N  N   . VAL A  1 184 ? -91.929  -33.151 77.442  1.00 27.18  ? 183 VAL A N   1 
ATOM   1239  C  CA  . VAL A  1 184 ? -92.086  -32.810 78.846  1.00 27.00  ? 183 VAL A CA  1 
ATOM   1240  C  C   . VAL A  1 184 ? -90.776  -33.102 79.564  1.00 26.36  ? 183 VAL A C   1 
ATOM   1241  O  O   . VAL A  1 184 ? -90.195  -34.172 79.409  1.00 29.95  ? 183 VAL A O   1 
ATOM   1242  C  CB  . VAL A  1 184 ? -93.256  -33.558 79.509  1.00 28.52  ? 183 VAL A CB  1 
ATOM   1243  C  CG1 . VAL A  1 184 ? -93.396  -33.176 80.977  1.00 29.72  ? 183 VAL A CG1 1 
ATOM   1244  C  CG2 . VAL A  1 184 ? -94.559  -33.311 78.760  1.00 29.05  ? 183 VAL A CG2 1 
ATOM   1245  N  N   . GLN A  1 185 ? -90.321  -32.132 80.354  1.00 29.49  ? 184 GLN A N   1 
ATOM   1246  C  CA  . GLN A  1 185 ? -89.116  -32.313 81.159  1.00 30.95  ? 184 GLN A CA  1 
ATOM   1247  C  C   . GLN A  1 185 ? -89.146  -31.317 82.314  1.00 27.37  ? 184 GLN A C   1 
ATOM   1248  O  O   . GLN A  1 185 ? -89.777  -30.268 82.233  1.00 24.86  ? 184 GLN A O   1 
ATOM   1249  C  CB  . GLN A  1 185 ? -87.839  -32.145 80.333  1.00 36.06  ? 184 GLN A CB  1 
ATOM   1250  C  CG  . GLN A  1 185 ? -87.574  -30.728 79.862  1.00 42.34  ? 184 GLN A CG  1 
ATOM   1251  C  CD  . GLN A  1 185 ? -86.345  -30.651 78.981  1.00 50.74  ? 184 GLN A CD  1 
ATOM   1252  O  OE1 . GLN A  1 185 ? -86.391  -30.112 77.876  1.00 55.02  ? 184 GLN A OE1 1 
ATOM   1253  N  NE2 . GLN A  1 185 ? -85.235  -31.208 79.451  1.00 51.43  ? 184 GLN A NE2 1 
ATOM   1254  N  N   . GLY A  1 186 ? -88.472  -31.677 83.400  1.00 25.49  ? 185 GLY A N   1 
ATOM   1255  C  CA  . GLY A  1 186 ? -88.402  -30.767 84.504  1.00 26.59  ? 185 GLY A CA  1 
ATOM   1256  C  C   . GLY A  1 186 ? -87.606  -31.326 85.646  1.00 25.05  ? 185 GLY A C   1 
ATOM   1257  O  O   . GLY A  1 186 ? -87.056  -32.411 85.560  1.00 25.81  ? 185 GLY A O   1 
ATOM   1258  N  N   . ILE A  1 187 ? -87.557  -30.523 86.702  1.00 25.85  ? 186 ILE A N   1 
ATOM   1259  C  CA  . ILE A  1 187 ? -86.840  -30.827 87.896  1.00 26.27  ? 186 ILE A CA  1 
ATOM   1260  C  C   . ILE A  1 187 ? -87.748  -30.536 89.091  1.00 24.75  ? 186 ILE A C   1 
ATOM   1261  O  O   . ILE A  1 187 ? -88.346  -29.459 89.197  1.00 24.91  ? 186 ILE A O   1 
ATOM   1262  C  CB  . ILE A  1 187 ? -85.525  -30.030 87.984  1.00 26.80  ? 186 ILE A CB  1 
ATOM   1263  C  CG1 . ILE A  1 187 ? -84.569  -30.376 86.839  1.00 28.72  ? 186 ILE A CG1 1 
ATOM   1264  C  CG2 . ILE A  1 187 ? -84.872  -30.240 89.342  1.00 27.87  ? 186 ILE A CG2 1 
ATOM   1265  C  CD1 . ILE A  1 187 ? -83.317  -29.495 86.807  1.00 30.77  ? 186 ILE A CD1 1 
ATOM   1266  N  N   . ILE A  1 188 ? -87.834  -31.524 89.983  1.00 24.46  ? 187 ILE A N   1 
ATOM   1267  C  CA  . ILE A  1 188 ? -88.667  -31.414 91.175  1.00 25.90  ? 187 ILE A CA  1 
ATOM   1268  C  C   . ILE A  1 188 ? -87.788  -31.692 92.393  1.00 23.62  ? 187 ILE A C   1 
ATOM   1269  O  O   . ILE A  1 188 ? -87.076  -32.696 92.452  1.00 26.38  ? 187 ILE A O   1 
ATOM   1270  C  CB  . ILE A  1 188 ? -89.876  -32.381 91.116  1.00 25.27  ? 187 ILE A CB  1 
ATOM   1271  C  CG1 . ILE A  1 188 ? -90.778  -32.087 89.916  1.00 25.24  ? 187 ILE A CG1 1 
ATOM   1272  C  CG2 . ILE A  1 188 ? -90.662  -32.323 92.420  1.00 25.48  ? 187 ILE A CG2 1 
ATOM   1273  C  CD1 . ILE A  1 188 ? -91.551  -30.801 90.023  1.00 26.33  ? 187 ILE A CD1 1 
ATOM   1274  N  N   . ASN A  1 189 ? -87.902  -30.792 93.358  1.00 25.17  ? 188 ASN A N   1 
ATOM   1275  C  CA  . ASN A  1 189 ? -87.178  -30.808 94.614  1.00 26.96  ? 188 ASN A CA  1 
ATOM   1276  C  C   . ASN A  1 189 ? -88.113  -31.265 95.728  1.00 27.49  ? 188 ASN A C   1 
ATOM   1277  O  O   . ASN A  1 189 ? -89.296  -30.910 95.727  1.00 27.96  ? 188 ASN A O   1 
ATOM   1278  C  CB  . ASN A  1 189 ? -86.659  -29.405 94.958  1.00 26.72  ? 188 ASN A CB  1 
ATOM   1279  C  CG  . ASN A  1 189 ? -85.780  -28.898 93.843  1.00 26.76  ? 188 ASN A CG  1 
ATOM   1280  O  OD1 . ASN A  1 189 ? -84.703  -29.436 93.676  1.00 28.50  ? 188 ASN A OD1 1 
ATOM   1281  N  ND2 . ASN A  1 189 ? -86.296  -28.024 92.989  1.00 26.51  ? 188 ASN A ND2 1 
ATOM   1282  N  N   . PHE A  1 190 ? -87.564  -32.062 96.644  1.00 29.06  ? 189 PHE A N   1 
ATOM   1283  C  CA  . PHE A  1 190 ? -88.271  -32.524 97.844  1.00 29.99  ? 189 PHE A CA  1 
ATOM   1284  C  C   . PHE A  1 190 ? -87.454  -32.118 99.078  1.00 31.66  ? 189 PHE A C   1 
ATOM   1285  O  O   . PHE A  1 190 ? -86.241  -32.331 99.111  1.00 33.12  ? 189 PHE A O   1 
ATOM   1286  C  CB  . PHE A  1 190 ? -88.425  -34.044 97.850  1.00 29.30  ? 189 PHE A CB  1 
ATOM   1287  C  CG  . PHE A  1 190 ? -89.190  -34.631 96.684  1.00 29.63  ? 189 PHE A CG  1 
ATOM   1288  C  CD1 . PHE A  1 190 ? -90.551  -34.886 96.784  1.00 28.25  ? 189 PHE A CD1 1 
ATOM   1289  C  CD2 . PHE A  1 190 ? -88.555  -34.900 95.482  1.00 29.66  ? 189 PHE A CD2 1 
ATOM   1290  C  CE1 . PHE A  1 190 ? -91.252  -35.418 95.713  1.00 30.15  ? 189 PHE A CE1 1 
ATOM   1291  C  CE2 . PHE A  1 190 ? -89.256  -35.459 94.416  1.00 28.09  ? 189 PHE A CE2 1 
ATOM   1292  C  CZ  . PHE A  1 190 ? -90.600  -35.709 94.537  1.00 27.73  ? 189 PHE A CZ  1 
ATOM   1293  N  N   . GLU A  1 191 ? -88.126  -31.552 100.086 1.00 34.52  ? 190 GLU A N   1 
ATOM   1294  C  CA  . GLU A  1 191 ? -87.460  -31.155 101.337 1.00 40.52  ? 190 GLU A CA  1 
ATOM   1295  C  C   . GLU A  1 191 ? -88.349  -31.570 102.518 1.00 37.90  ? 190 GLU A C   1 
ATOM   1296  O  O   . GLU A  1 191 ? -89.545  -31.276 102.533 1.00 34.54  ? 190 GLU A O   1 
ATOM   1297  C  CB  . GLU A  1 191 ? -87.174  -29.651 101.331 1.00 42.22  ? 190 GLU A CB  1 
ATOM   1298  C  CG  . GLU A  1 191 ? -86.435  -29.172 102.574 1.00 53.19  ? 190 GLU A CG  1 
ATOM   1299  C  CD  . GLU A  1 191 ? -86.713  -27.728 102.969 1.00 63.75  ? 190 GLU A CD  1 
ATOM   1300  O  OE1 . GLU A  1 191 ? -87.541  -27.512 103.895 1.00 74.91  ? 190 GLU A OE1 1 
ATOM   1301  O  OE2 . GLU A  1 191 ? -86.116  -26.826 102.350 1.00 61.96  ? 190 GLU A OE2 1 
ATOM   1302  N  N   . GLN A  1 192 ? -87.743  -32.279 103.475 1.00 36.64  ? 191 GLN A N   1 
ATOM   1303  C  CA  . GLN A  1 192 ? -88.390  -32.723 104.704 1.00 39.22  ? 191 GLN A CA  1 
ATOM   1304  C  C   . GLN A  1 192 ? -87.468  -32.422 105.896 1.00 42.09  ? 191 GLN A C   1 
ATOM   1305  O  O   . GLN A  1 192 ? -86.644  -33.264 106.269 1.00 38.94  ? 191 GLN A O   1 
ATOM   1306  C  CB  . GLN A  1 192 ? -88.658  -34.220 104.629 1.00 35.97  ? 191 GLN A CB  1 
ATOM   1307  C  CG  . GLN A  1 192 ? -89.503  -34.710 105.782 1.00 37.09  ? 191 GLN A CG  1 
ATOM   1308  C  CD  . GLN A  1 192 ? -89.790  -36.178 105.650 1.00 38.30  ? 191 GLN A CD  1 
ATOM   1309  O  OE1 . GLN A  1 192 ? -88.970  -36.938 105.143 1.00 37.50  ? 191 GLN A OE1 1 
ATOM   1310  N  NE2 . GLN A  1 192 ? -90.950  -36.586 106.137 1.00 39.05  ? 191 GLN A NE2 1 
ATOM   1311  N  N   . LYS A  1 193 ? -87.615  -31.229 106.474 1.00 49.31  ? 192 LYS A N   1 
ATOM   1312  C  CA  . LYS A  1 193 ? -86.660  -30.722 107.483 1.00 60.98  ? 192 LYS A CA  1 
ATOM   1313  C  C   . LYS A  1 193 ? -86.851  -31.413 108.845 1.00 57.21  ? 192 LYS A C   1 
ATOM   1314  O  O   . LYS A  1 193 ? -85.940  -31.375 109.647 1.00 67.87  ? 192 LYS A O   1 
ATOM   1315  C  CB  . LYS A  1 193 ? -86.751  -29.198 107.627 1.00 68.03  ? 192 LYS A CB  1 
ATOM   1316  C  CG  . LYS A  1 193 ? -88.027  -28.671 108.268 1.00 74.82  ? 192 LYS A CG  1 
ATOM   1317  C  CD  . LYS A  1 193 ? -88.936  -27.955 107.297 1.00 83.06  ? 192 LYS A CD  1 
ATOM   1318  C  CE  . LYS A  1 193 ? -90.375  -27.920 107.763 1.00 84.04  ? 192 LYS A CE  1 
ATOM   1319  N  NZ  . LYS A  1 193 ? -91.151  -29.111 107.339 1.00 86.94  ? 192 LYS A NZ  1 
ATOM   1320  N  N   . GLU A  1 194 ? -88.017  -32.019 109.106 1.00 56.90  ? 193 GLU A N   1 
ATOM   1321  C  CA  . GLU A  1 194 ? -88.221  -32.889 110.284 1.00 60.66  ? 193 GLU A CA  1 
ATOM   1322  C  C   . GLU A  1 194 ? -88.787  -34.233 109.814 1.00 60.72  ? 193 GLU A C   1 
ATOM   1323  O  O   . GLU A  1 194 ? -89.620  -34.271 108.909 1.00 59.50  ? 193 GLU A O   1 
ATOM   1324  C  CB  . GLU A  1 194 ? -89.120  -32.232 111.339 1.00 66.99  ? 193 GLU A CB  1 
ATOM   1325  C  CG  . GLU A  1 194 ? -90.250  -31.389 110.773 1.00 71.75  ? 193 GLU A CG  1 
ATOM   1326  C  CD  . GLU A  1 194 ? -91.310  -30.954 111.775 1.00 75.66  ? 193 GLU A CD  1 
ATOM   1327  O  OE1 . GLU A  1 194 ? -92.010  -29.954 111.497 1.00 72.76  ? 193 GLU A OE1 1 
ATOM   1328  O  OE2 . GLU A  1 194 ? -91.453  -31.622 112.820 1.00 75.99  ? 193 GLU A OE2 1 
ATOM   1329  N  N   . SER A  1 195 ? -88.377  -35.311 110.495 1.00 61.07  ? 194 SER A N   1 
ATOM   1330  C  CA  . SER A  1 195 ? -88.281  -36.664 109.924 1.00 69.88  ? 194 SER A CA  1 
ATOM   1331  C  C   . SER A  1 195 ? -89.574  -37.483 110.067 1.00 73.33  ? 194 SER A C   1 
ATOM   1332  O  O   . SER A  1 195 ? -89.555  -38.705 109.931 1.00 92.16  ? 194 SER A O   1 
ATOM   1333  C  CB  . SER A  1 195 ? -87.115  -37.397 110.537 1.00 74.35  ? 194 SER A CB  1 
ATOM   1334  O  OG  . SER A  1 195 ? -87.250  -37.447 111.950 1.00 80.12  ? 194 SER A OG  1 
ATOM   1335  N  N   . ASN A  1 196 ? -90.691  -36.833 110.368 1.00 70.85  ? 195 ASN A N   1 
ATOM   1336  C  CA  . ASN A  1 196 ? -91.984  -37.364 109.966 1.00 76.90  ? 195 ASN A CA  1 
ATOM   1337  C  C   . ASN A  1 196 ? -92.933  -36.183 109.736 1.00 76.55  ? 195 ASN A C   1 
ATOM   1338  O  O   . ASN A  1 196 ? -94.159  -36.335 109.774 1.00 88.18  ? 195 ASN A O   1 
ATOM   1339  C  CB  . ASN A  1 196 ? -92.515  -38.410 110.954 1.00 85.58  ? 195 ASN A CB  1 
ATOM   1340  C  CG  . ASN A  1 196 ? -92.801  -37.864 112.340 1.00 90.78  ? 195 ASN A CG  1 
ATOM   1341  O  OD1 . ASN A  1 196 ? -92.550  -36.694 112.626 1.00 92.28  ? 195 ASN A OD1 1 
ATOM   1342  N  ND2 . ASN A  1 196 ? -93.335  -38.707 113.210 1.00 94.20  ? 195 ASN A ND2 1 
ATOM   1343  N  N   . GLY A  1 197 ? -92.342  -35.011 109.466 1.00 60.96  ? 196 GLY A N   1 
ATOM   1344  C  CA  . GLY A  1 197 ? -93.077  -33.817 109.156 1.00 57.00  ? 196 GLY A CA  1 
ATOM   1345  C  C   . GLY A  1 197 ? -93.446  -33.795 107.679 1.00 48.16  ? 196 GLY A C   1 
ATOM   1346  O  O   . GLY A  1 197 ? -93.193  -34.760 106.962 1.00 45.35  ? 196 GLY A O   1 
ATOM   1347  N  N   . PRO A  1 198 ? -94.054  -32.698 107.186 1.00 43.28  ? 197 PRO A N   1 
ATOM   1348  C  CA  . PRO A  1 198 ? -94.439  -32.615 105.784 1.00 46.07  ? 197 PRO A CA  1 
ATOM   1349  C  C   . PRO A  1 198 ? -93.214  -32.562 104.854 1.00 41.47  ? 197 PRO A C   1 
ATOM   1350  O  O   . PRO A  1 198 ? -92.122  -32.138 105.259 1.00 38.24  ? 197 PRO A O   1 
ATOM   1351  C  CB  . PRO A  1 198 ? -95.257  -31.321 105.701 1.00 46.10  ? 197 PRO A CB  1 
ATOM   1352  C  CG  . PRO A  1 198 ? -94.781  -30.490 106.870 1.00 46.55  ? 197 PRO A CG  1 
ATOM   1353  C  CD  . PRO A  1 198 ? -94.387  -31.483 107.939 1.00 45.73  ? 197 PRO A CD  1 
ATOM   1354  N  N   . VAL A  1 199 ? -93.416  -33.040 103.623 1.00 38.30  ? 198 VAL A N   1 
ATOM   1355  C  CA  . VAL A  1 199 ? -92.454  -32.909 102.543 1.00 33.70  ? 198 VAL A CA  1 
ATOM   1356  C  C   . VAL A  1 199 ? -92.917  -31.764 101.645 1.00 33.48  ? 198 VAL A C   1 
ATOM   1357  O  O   . VAL A  1 199 ? -94.039  -31.801 101.136 1.00 36.44  ? 198 VAL A O   1 
ATOM   1358  C  CB  . VAL A  1 199 ? -92.328  -34.230 101.761 1.00 33.66  ? 198 VAL A CB  1 
ATOM   1359  C  CG1 . VAL A  1 199 ? -91.240  -34.166 100.697 1.00 32.48  ? 198 VAL A CG1 1 
ATOM   1360  C  CG2 . VAL A  1 199 ? -92.092  -35.408 102.690 1.00 34.64  ? 198 VAL A CG2 1 
ATOM   1361  N  N   . LYS A  1 200 ? -92.066  -30.747 101.474 1.00 32.38  ? 199 LYS A N   1 
ATOM   1362  C  CA  . LYS A  1 200 ? -92.312  -29.681 100.510 1.00 35.34  ? 199 LYS A CA  1 
ATOM   1363  C  C   . LYS A  1 200 ? -91.855  -30.208 99.153  1.00 30.72  ? 199 LYS A C   1 
ATOM   1364  O  O   . LYS A  1 200 ? -90.820  -30.831 99.053  1.00 31.37  ? 199 LYS A O   1 
ATOM   1365  C  CB  . LYS A  1 200 ? -91.570  -28.377 100.834 1.00 40.75  ? 199 LYS A CB  1 
ATOM   1366  C  CG  . LYS A  1 200 ? -92.035  -27.669 102.101 1.00 54.37  ? 199 LYS A CG  1 
ATOM   1367  C  CD  . LYS A  1 200 ? -91.340  -26.339 102.360 1.00 63.83  ? 199 LYS A CD  1 
ATOM   1368  C  CE  . LYS A  1 200 ? -91.829  -25.631 103.610 1.00 69.48  ? 199 LYS A CE  1 
ATOM   1369  N  NZ  . LYS A  1 200 ? -91.512  -26.395 104.840 1.00 74.06  ? 199 LYS A NZ  1 
ATOM   1370  N  N   . VAL A  1 201 ? -92.656  -29.942 98.129  1.00 30.22  ? 200 VAL A N   1 
ATOM   1371  C  CA  . VAL A  1 201 ? -92.402  -30.456 96.788  1.00 29.92  ? 200 VAL A CA  1 
ATOM   1372  C  C   . VAL A  1 201 ? -92.462  -29.248 95.871  1.00 29.61  ? 200 VAL A C   1 
ATOM   1373  O  O   . VAL A  1 201 ? -93.506  -28.567 95.833  1.00 29.65  ? 200 VAL A O   1 
ATOM   1374  C  CB  . VAL A  1 201 ? -93.418  -31.538 96.371  1.00 29.05  ? 200 VAL A CB  1 
ATOM   1375  C  CG1 . VAL A  1 201 ? -93.114  -32.098 94.987  1.00 27.22  ? 200 VAL A CG1 1 
ATOM   1376  C  CG2 . VAL A  1 201 ? -93.488  -32.671 97.384  1.00 29.32  ? 200 VAL A CG2 1 
ATOM   1377  N  N   . TRP A  1 202 ? -91.347  -28.932 95.199  1.00 26.45  ? 201 TRP A N   1 
ATOM   1378  C  CA  . TRP A  1 202 ? -91.359  -27.719 94.378  1.00 27.43  ? 201 TRP A CA  1 
ATOM   1379  C  C   . TRP A  1 202 ? -90.416  -27.870 93.183  1.00 25.49  ? 201 TRP A C   1 
ATOM   1380  O  O   . TRP A  1 202 ? -89.455  -28.632 93.225  1.00 27.51  ? 201 TRP A O   1 
ATOM   1381  C  CB  . TRP A  1 202 ? -91.039  -26.479 95.241  1.00 30.00  ? 201 TRP A CB  1 
ATOM   1382  C  CG  . TRP A  1 202 ? -89.618  -26.413 95.706  1.00 31.39  ? 201 TRP A CG  1 
ATOM   1383  C  CD1 . TRP A  1 202 ? -89.088  -26.978 96.829  1.00 33.21  ? 201 TRP A CD1 1 
ATOM   1384  C  CD2 . TRP A  1 202 ? -88.526  -25.776 95.022  1.00 33.55  ? 201 TRP A CD2 1 
ATOM   1385  N  NE1 . TRP A  1 202 ? -87.743  -26.733 96.888  1.00 34.82  ? 201 TRP A NE1 1 
ATOM   1386  C  CE2 . TRP A  1 202 ? -87.368  -26.005 95.789  1.00 36.43  ? 201 TRP A CE2 1 
ATOM   1387  C  CE3 . TRP A  1 202 ? -88.412  -25.058 93.824  1.00 40.75  ? 201 TRP A CE3 1 
ATOM   1388  C  CZ2 . TRP A  1 202 ? -86.113  -25.504 95.417  1.00 41.01  ? 201 TRP A CZ2 1 
ATOM   1389  C  CZ3 . TRP A  1 202 ? -87.170  -24.579 93.445  1.00 43.19  ? 201 TRP A CZ3 1 
ATOM   1390  C  CH2 . TRP A  1 202 ? -86.033  -24.802 94.234  1.00 40.08  ? 201 TRP A CH2 1 
ATOM   1391  N  N   . GLY A  1 203 ? -90.741  -27.160 92.105  1.00 25.68  ? 202 GLY A N   1 
ATOM   1392  C  CA  . GLY A  1 203 ? -89.912  -27.125 90.923  1.00 26.56  ? 202 GLY A CA  1 
ATOM   1393  C  C   . GLY A  1 203 ? -90.711  -26.735 89.710  1.00 25.98  ? 202 GLY A C   1 
ATOM   1394  O  O   . GLY A  1 203 ? -91.783  -26.183 89.847  1.00 30.60  ? 202 GLY A O   1 
ATOM   1395  N  N   . SER A  1 204 ? -90.190  -27.076 88.530  1.00 28.57  ? 203 SER A N   1 
ATOM   1396  C  CA  . SER A  1 204 ? -90.784  -26.691 87.268  1.00 27.86  ? 203 SER A CA  1 
ATOM   1397  C  C   . SER A  1 204 ? -90.739  -27.865 86.310  1.00 25.47  ? 203 SER A C   1 
ATOM   1398  O  O   . SER A  1 204 ? -89.769  -28.598 86.280  1.00 27.78  ? 203 SER A O   1 
ATOM   1399  C  CB  . SER A  1 204 ? -90.086  -25.511 86.638  1.00 33.72  ? 203 SER A CB  1 
ATOM   1400  O  OG  . SER A  1 204 ? -90.332  -24.344 87.391  1.00 41.26  ? 203 SER A OG  1 
ATOM   1401  N  N   . ILE A  1 205 ? -91.832  -28.012 85.558  1.00 24.49  ? 204 ILE A N   1 
ATOM   1402  C  CA  . ILE A  1 205 ? -91.967  -28.958 84.480  1.00 25.62  ? 204 ILE A CA  1 
ATOM   1403  C  C   . ILE A  1 205 ? -92.453  -28.168 83.267  1.00 27.15  ? 204 ILE A C   1 
ATOM   1404  O  O   . ILE A  1 205 ? -93.411  -27.387 83.374  1.00 27.30  ? 204 ILE A O   1 
ATOM   1405  C  CB  . ILE A  1 205 ? -92.977  -30.069 84.853  1.00 27.45  ? 204 ILE A CB  1 
ATOM   1406  C  CG1 . ILE A  1 205 ? -92.661  -30.738 86.191  1.00 28.50  ? 204 ILE A CG1 1 
ATOM   1407  C  CG2 . ILE A  1 205 ? -93.070  -31.089 83.741  1.00 26.57  ? 204 ILE A CG2 1 
ATOM   1408  C  CD1 . ILE A  1 205 ? -93.822  -31.495 86.768  1.00 30.86  ? 204 ILE A CD1 1 
ATOM   1409  N  N   . LYS A  1 206 ? -91.816  -28.373 82.113  1.00 28.16  ? 205 LYS A N   1 
ATOM   1410  C  CA  . LYS A  1 206 ? -92.216  -27.635 80.935  1.00 28.78  ? 205 LYS A CA  1 
ATOM   1411  C  C   . LYS A  1 206 ? -92.627  -28.633 79.860  1.00 26.03  ? 205 LYS A C   1 
ATOM   1412  O  O   . LYS A  1 206 ? -92.402  -29.829 79.986  1.00 27.47  ? 205 LYS A O   1 
ATOM   1413  C  CB  . LYS A  1 206 ? -91.080  -26.716 80.458  1.00 32.98  ? 205 LYS A CB  1 
ATOM   1414  C  CG  . LYS A  1 206 ? -89.893  -27.451 79.864  1.00 35.72  ? 205 LYS A CG  1 
ATOM   1415  C  CD  . LYS A  1 206 ? -88.736  -26.537 79.494  1.00 44.67  ? 205 LYS A CD  1 
ATOM   1416  C  CE  . LYS A  1 206 ? -87.505  -27.310 79.055  1.00 48.97  ? 205 LYS A CE  1 
ATOM   1417  N  NZ  . LYS A  1 206 ? -86.494  -26.411 78.446  1.00 54.91  ? 205 LYS A NZ  1 
ATOM   1418  N  N   . GLY A  1 207 ? -93.208  -28.099 78.785  1.00 25.45  ? 206 GLY A N   1 
ATOM   1419  C  CA  . GLY A  1 207 ? -93.592  -28.900 77.640  1.00 25.22  ? 206 GLY A CA  1 
ATOM   1420  C  C   . GLY A  1 207 ? -94.963  -29.537 77.816  1.00 25.79  ? 206 GLY A C   1 
ATOM   1421  O  O   . GLY A  1 207 ? -95.336  -30.395 77.034  1.00 26.68  ? 206 GLY A O   1 
ATOM   1422  N  N   . LEU A  1 208 ? -95.738  -29.082 78.812  1.00 28.65  ? 207 LEU A N   1 
ATOM   1423  C  CA  . LEU A  1 208 ? -97.064  -29.647 79.097  1.00 27.68  ? 207 LEU A CA  1 
ATOM   1424  C  C   . LEU A  1 208 ? -98.133  -28.856 78.358  1.00 29.67  ? 207 LEU A C   1 
ATOM   1425  O  O   . LEU A  1 208 ? -97.963  -27.685 78.095  1.00 28.99  ? 207 LEU A O   1 
ATOM   1426  C  CB  . LEU A  1 208 ? -97.358  -29.582 80.601  1.00 27.99  ? 207 LEU A CB  1 
ATOM   1427  C  CG  . LEU A  1 208 ? -96.505  -30.485 81.474  1.00 26.04  ? 207 LEU A CG  1 
ATOM   1428  C  CD1 . LEU A  1 208 ? -96.491  -29.967 82.900  1.00 27.04  ? 207 LEU A CD1 1 
ATOM   1429  C  CD2 . LEU A  1 208 ? -96.991  -31.930 81.412  1.00 28.20  ? 207 LEU A CD2 1 
ATOM   1430  N  N   . THR A  1 209 ? -99.281  -29.503 78.120  1.00 30.01  ? 208 THR A N   1 
ATOM   1431  C  CA  . THR A  1 209 ? -100.489 -28.790 77.706  1.00 30.23  ? 208 THR A CA  1 
ATOM   1432  C  C   . THR A  1 209 ? -101.034 -28.005 78.892  1.00 29.39  ? 208 THR A C   1 
ATOM   1433  O  O   . THR A  1 209 ? -101.017 -28.475 80.041  1.00 29.82  ? 208 THR A O   1 
ATOM   1434  C  CB  . THR A  1 209 ? -101.568 -29.766 77.221  1.00 32.57  ? 208 THR A CB  1 
ATOM   1435  O  OG1 . THR A  1 209 ? -101.815 -30.661 78.309  1.00 31.64  ? 208 THR A OG1 1 
ATOM   1436  C  CG2 . THR A  1 209 ? -101.156 -30.541 75.991  1.00 31.76  ? 208 THR A CG2 1 
ATOM   1437  N  N   . GLU A  1 210 ? -101.571 -26.825 78.601  1.00 29.08  ? 209 GLU A N   1 
ATOM   1438  C  CA  . GLU A  1 210 ? -102.168 -25.979 79.587  1.00 30.08  ? 209 GLU A CA  1 
ATOM   1439  C  C   . GLU A  1 210 ? -103.221 -26.760 80.390  1.00 32.29  ? 209 GLU A C   1 
ATOM   1440  O  O   . GLU A  1 210 ? -104.002 -27.497 79.823  1.00 31.59  ? 209 GLU A O   1 
ATOM   1441  C  CB  . GLU A  1 210 ? -102.817 -24.797 78.880  1.00 31.64  ? 209 GLU A CB  1 
ATOM   1442  C  CG  . GLU A  1 210 ? -103.339 -23.762 79.842  1.00 34.77  ? 209 GLU A CG  1 
ATOM   1443  C  CD  . GLU A  1 210 ? -103.993 -22.573 79.171  1.00 37.54  ? 209 GLU A CD  1 
ATOM   1444  O  OE1 . GLU A  1 210 ? -104.679 -21.838 79.870  1.00 44.82  ? 209 GLU A OE1 1 
ATOM   1445  O  OE2 . GLU A  1 210 ? -103.788 -22.379 77.960  1.00 44.00  ? 209 GLU A OE2 1 
ATOM   1446  N  N   . GLY A  1 211 ? -103.220 -26.589 81.714  1.00 32.72  ? 210 GLY A N   1 
ATOM   1447  C  CA  . GLY A  1 211 ? -104.243 -27.169 82.586  1.00 31.84  ? 210 GLY A CA  1 
ATOM   1448  C  C   . GLY A  1 211 ? -103.684 -28.235 83.515  1.00 31.78  ? 210 GLY A C   1 
ATOM   1449  O  O   . GLY A  1 211 ? -102.450 -28.273 83.797  1.00 29.25  ? 210 GLY A O   1 
ATOM   1450  N  N   . LEU A  1 212 ? -104.591 -29.122 83.976  1.00 30.13  ? 211 LEU A N   1 
ATOM   1451  C  CA  . LEU A  1 212 ? -104.324 -30.066 85.075  1.00 30.00  ? 211 LEU A CA  1 
ATOM   1452  C  C   . LEU A  1 212 ? -103.637 -31.327 84.547  1.00 27.53  ? 211 LEU A C   1 
ATOM   1453  O  O   . LEU A  1 212 ? -104.027 -31.885 83.524  1.00 28.44  ? 211 LEU A O   1 
ATOM   1454  C  CB  . LEU A  1 212 ? -105.643 -30.434 85.775  1.00 32.90  ? 211 LEU A CB  1 
ATOM   1455  C  CG  . LEU A  1 212 ? -106.364 -29.305 86.507  1.00 33.83  ? 211 LEU A CG  1 
ATOM   1456  C  CD1 . LEU A  1 212 ? -107.789 -29.727 86.857  1.00 36.61  ? 211 LEU A CD1 1 
ATOM   1457  C  CD2 . LEU A  1 212 ? -105.611 -28.880 87.755  1.00 33.90  ? 211 LEU A CD2 1 
ATOM   1458  N  N   . HIS A  1 213 ? -102.642 -31.793 85.301  1.00 24.56  ? 212 HIS A N   1 
ATOM   1459  C  CA  . HIS A  1 213 ? -101.908 -33.003 85.022  1.00 24.63  ? 212 HIS A CA  1 
ATOM   1460  C  C   . HIS A  1 213 ? -101.711 -33.792 86.315  1.00 25.81  ? 212 HIS A C   1 
ATOM   1461  O  O   . HIS A  1 213 ? -101.192 -33.252 87.302  1.00 23.37  ? 212 HIS A O   1 
ATOM   1462  C  CB  . HIS A  1 213 ? -100.546 -32.722 84.380  1.00 25.19  ? 212 HIS A CB  1 
ATOM   1463  C  CG  . HIS A  1 213 ? -100.666 -32.122 83.019  1.00 25.31  ? 212 HIS A CG  1 
ATOM   1464  N  ND1 . HIS A  1 213 ? -100.677 -32.893 81.889  1.00 27.31  ? 212 HIS A ND1 1 
ATOM   1465  C  CD2 . HIS A  1 213 ? -100.877 -30.858 82.613  1.00 27.46  ? 212 HIS A CD2 1 
ATOM   1466  C  CE1 . HIS A  1 213 ? -100.840 -32.120 80.836  1.00 27.27  ? 212 HIS A CE1 1 
ATOM   1467  N  NE2 . HIS A  1 213 ? -101.003 -30.883 81.254  1.00 27.38  ? 212 HIS A NE2 1 
ATOM   1468  N  N   . GLY A  1 214 ? -102.070 -35.088 86.262  1.00 25.98  ? 213 GLY A N   1 
ATOM   1469  C  CA  . GLY A  1 214 ? -101.860 -35.992 87.393  1.00 26.70  ? 213 GLY A CA  1 
ATOM   1470  C  C   . GLY A  1 214 ? -100.378 -36.089 87.726  1.00 27.36  ? 213 GLY A C   1 
ATOM   1471  O  O   . GLY A  1 214 ? -99.530  -36.021 86.829  1.00 24.98  ? 213 GLY A O   1 
ATOM   1472  N  N   . PHE A  1 215 ? -100.086 -36.229 89.022  1.00 25.64  ? 214 PHE A N   1 
ATOM   1473  C  CA  . PHE A  1 215 ? -98.750  -36.124 89.552  1.00 25.07  ? 214 PHE A CA  1 
ATOM   1474  C  C   . PHE A  1 215 ? -98.621  -37.119 90.701  1.00 24.25  ? 214 PHE A C   1 
ATOM   1475  O  O   . PHE A  1 215 ? -99.220  -36.883 91.761  1.00 24.93  ? 214 PHE A O   1 
ATOM   1476  C  CB  . PHE A  1 215 ? -98.527  -34.676 90.000  1.00 26.00  ? 214 PHE A CB  1 
ATOM   1477  C  CG  . PHE A  1 215 ? -97.118  -34.278 90.376  1.00 26.20  ? 214 PHE A CG  1 
ATOM   1478  C  CD1 . PHE A  1 215 ? -96.118  -34.206 89.415  1.00 28.55  ? 214 PHE A CD1 1 
ATOM   1479  C  CD2 . PHE A  1 215 ? -96.813  -33.875 91.672  1.00 26.98  ? 214 PHE A CD2 1 
ATOM   1480  C  CE1 . PHE A  1 215 ? -94.833  -33.788 89.745  1.00 26.51  ? 214 PHE A CE1 1 
ATOM   1481  C  CE2 . PHE A  1 215 ? -95.523  -33.473 92.007  1.00 28.03  ? 214 PHE A CE2 1 
ATOM   1482  C  CZ  . PHE A  1 215 ? -94.540  -33.418 91.039  1.00 27.06  ? 214 PHE A CZ  1 
ATOM   1483  N  N   . HIS A  1 216 ? -97.839  -38.190 90.516  1.00 23.07  ? 215 HIS A N   1 
ATOM   1484  C  CA  . HIS A  1 216 ? -97.811  -39.290 91.511  1.00 24.09  ? 215 HIS A CA  1 
ATOM   1485  C  C   . HIS A  1 216 ? -96.417  -39.893 91.654  1.00 24.42  ? 215 HIS A C   1 
ATOM   1486  O  O   . HIS A  1 216 ? -95.615  -39.904 90.707  1.00 24.33  ? 215 HIS A O   1 
ATOM   1487  C  CB  . HIS A  1 216 ? -98.745  -40.459 91.137  1.00 23.75  ? 215 HIS A CB  1 
ATOM   1488  C  CG  . HIS A  1 216 ? -100.037 -40.047 90.539  1.00 23.64  ? 215 HIS A CG  1 
ATOM   1489  N  ND1 . HIS A  1 216 ? -100.408 -40.447 89.255  1.00 27.19  ? 215 HIS A ND1 1 
ATOM   1490  C  CD2 . HIS A  1 216 ? -101.015 -39.248 91.002  1.00 22.72  ? 215 HIS A CD2 1 
ATOM   1491  C  CE1 . HIS A  1 216 ? -101.593 -39.935 88.989  1.00 27.40  ? 215 HIS A CE1 1 
ATOM   1492  N  NE2 . HIS A  1 216 ? -101.974 -39.169 90.026  1.00 24.86  ? 215 HIS A NE2 1 
ATOM   1493  N  N   . VAL A  1 217 ? -96.182  -40.473 92.833  1.00 24.32  ? 216 VAL A N   1 
ATOM   1494  C  CA  . VAL A  1 217 ? -95.064  -41.348 93.042  1.00 24.52  ? 216 VAL A CA  1 
ATOM   1495  C  C   . VAL A  1 217 ? -95.507  -42.780 92.737  1.00 25.92  ? 216 VAL A C   1 
ATOM   1496  O  O   . VAL A  1 217 ? -96.450  -43.271 93.353  1.00 26.68  ? 216 VAL A O   1 
ATOM   1497  C  CB  . VAL A  1 217 ? -94.512  -41.232 94.471  1.00 25.35  ? 216 VAL A CB  1 
ATOM   1498  C  CG1 . VAL A  1 217 ? -93.335  -42.160 94.684  1.00 26.13  ? 216 VAL A CG1 1 
ATOM   1499  C  CG2 . VAL A  1 217 ? -94.140  -39.805 94.817  1.00 27.82  ? 216 VAL A CG2 1 
ATOM   1500  N  N   . HIS A  1 218 ? -94.791  -43.439 91.817  1.00 23.03  ? 217 HIS A N   1 
ATOM   1501  C  CA  . HIS A  1 218 ? -95.021  -44.827 91.450  1.00 25.75  ? 217 HIS A CA  1 
ATOM   1502  C  C   . HIS A  1 218 ? -94.021  -45.707 92.193  1.00 26.55  ? 217 HIS A C   1 
ATOM   1503  O  O   . HIS A  1 218 ? -92.992  -45.258 92.672  1.00 27.33  ? 217 HIS A O   1 
ATOM   1504  C  CB  . HIS A  1 218 ? -94.947  -45.040 89.928  1.00 25.08  ? 217 HIS A CB  1 
ATOM   1505  C  CG  . HIS A  1 218 ? -96.080  -44.418 89.193  1.00 24.07  ? 217 HIS A CG  1 
ATOM   1506  N  ND1 . HIS A  1 218 ? -96.888  -45.139 88.335  1.00 25.48  ? 217 HIS A ND1 1 
ATOM   1507  C  CD2 . HIS A  1 218 ? -96.604  -43.177 89.245  1.00 24.22  ? 217 HIS A CD2 1 
ATOM   1508  C  CE1 . HIS A  1 218 ? -97.831  -44.352 87.860  1.00 24.00  ? 217 HIS A CE1 1 
ATOM   1509  N  NE2 . HIS A  1 218 ? -97.681  -43.153 88.405  1.00 24.39  ? 217 HIS A NE2 1 
ATOM   1510  N  N   . GLU A  1 219 ? -94.336  -46.993 92.255  1.00 28.38  ? 218 GLU A N   1 
ATOM   1511  C  CA  . GLU A  1 219 ? -93.698  -47.881 93.191  1.00 29.89  ? 218 GLU A CA  1 
ATOM   1512  C  C   . GLU A  1 219 ? -92.225  -48.125 92.858  1.00 29.83  ? 218 GLU A C   1 
ATOM   1513  O  O   . GLU A  1 219 ? -91.410  -48.170 93.779  1.00 30.35  ? 218 GLU A O   1 
ATOM   1514  C  CB  . GLU A  1 219 ? -94.449  -49.209 93.227  1.00 33.45  ? 218 GLU A CB  1 
ATOM   1515  C  CG  . GLU A  1 219 ? -93.845  -50.185 94.197  1.00 35.58  ? 218 GLU A CG  1 
ATOM   1516  C  CD  . GLU A  1 219 ? -94.631  -51.474 94.352  1.00 40.20  ? 218 GLU A CD  1 
ATOM   1517  O  OE1 . GLU A  1 219 ? -94.176  -52.311 95.141  1.00 44.30  ? 218 GLU A OE1 1 
ATOM   1518  O  OE2 . GLU A  1 219 ? -95.655  -51.646 93.648  1.00 38.81  ? 218 GLU A OE2 1 
ATOM   1519  N  N   . PHE A  1 220 ? -91.891  -48.323 91.574  1.00 29.07  ? 219 PHE A N   1 
ATOM   1520  C  CA  . PHE A  1 220 ? -90.540  -48.758 91.192  1.00 30.50  ? 219 PHE A CA  1 
ATOM   1521  C  C   . PHE A  1 220 ? -89.750  -47.594 90.594  1.00 30.39  ? 219 PHE A C   1 
ATOM   1522  O  O   . PHE A  1 220 ? -90.277  -46.808 89.801  1.00 32.47  ? 219 PHE A O   1 
ATOM   1523  C  CB  . PHE A  1 220 ? -90.627  -49.942 90.237  1.00 31.47  ? 219 PHE A CB  1 
ATOM   1524  C  CG  . PHE A  1 220 ? -91.453  -51.070 90.801  1.00 34.09  ? 219 PHE A CG  1 
ATOM   1525  C  CD1 . PHE A  1 220 ? -91.118  -51.642 92.019  1.00 36.29  ? 219 PHE A CD1 1 
ATOM   1526  C  CD2 . PHE A  1 220 ? -92.555  -51.561 90.128  1.00 38.64  ? 219 PHE A CD2 1 
ATOM   1527  C  CE1 . PHE A  1 220 ? -91.880  -52.670 92.556  1.00 37.10  ? 219 PHE A CE1 1 
ATOM   1528  C  CE2 . PHE A  1 220 ? -93.314  -52.594 90.667  1.00 36.83  ? 219 PHE A CE2 1 
ATOM   1529  C  CZ  . PHE A  1 220 ? -92.978  -53.136 91.880  1.00 35.81  ? 219 PHE A CZ  1 
ATOM   1530  N  N   . GLY A  1 221 ? -88.488  -47.491 91.011  1.00 29.79  ? 220 GLY A N   1 
ATOM   1531  C  CA  . GLY A  1 221 ? -87.504  -46.597 90.406  1.00 30.47  ? 220 GLY A CA  1 
ATOM   1532  C  C   . GLY A  1 221 ? -86.844  -47.286 89.230  1.00 30.30  ? 220 GLY A C   1 
ATOM   1533  O  O   . GLY A  1 221 ? -85.633  -47.299 89.106  1.00 31.39  ? 220 GLY A O   1 
ATOM   1534  N  N   . ASP A  1 222 ? -87.680  -47.885 88.379  1.00 30.31  ? 221 ASP A N   1 
ATOM   1535  C  CA  . ASP A  1 222 ? -87.259  -48.695 87.261  1.00 32.22  ? 221 ASP A CA  1 
ATOM   1536  C  C   . ASP A  1 222 ? -87.695  -47.979 85.979  1.00 32.02  ? 221 ASP A C   1 
ATOM   1537  O  O   . ASP A  1 222 ? -88.891  -47.869 85.716  1.00 30.78  ? 221 ASP A O   1 
ATOM   1538  C  CB  . ASP A  1 222 ? -87.877  -50.087 87.359  1.00 33.30  ? 221 ASP A CB  1 
ATOM   1539  C  CG  . ASP A  1 222 ? -87.342  -51.062 86.330  1.00 35.03  ? 221 ASP A CG  1 
ATOM   1540  O  OD1 . ASP A  1 222 ? -87.357  -52.267 86.629  1.00 37.16  ? 221 ASP A OD1 1 
ATOM   1541  O  OD2 . ASP A  1 222 ? -86.926  -50.602 85.239  1.00 33.07  ? 221 ASP A OD2 1 
ATOM   1542  N  N   . ASN A  1 223 ? -86.728  -47.451 85.230  1.00 32.32  ? 222 ASN A N   1 
ATOM   1543  C  CA  . ASN A  1 223 ? -87.037  -46.722 84.009  1.00 35.49  ? 222 ASN A CA  1 
ATOM   1544  C  C   . ASN A  1 223 ? -86.423  -47.480 82.824  1.00 34.95  ? 222 ASN A C   1 
ATOM   1545  O  O   . ASN A  1 223 ? -86.086  -46.893 81.811  1.00 32.88  ? 222 ASN A O   1 
ATOM   1546  C  CB  . ASN A  1 223 ? -86.616  -45.248 84.123  1.00 39.66  ? 222 ASN A CB  1 
ATOM   1547  C  CG  . ASN A  1 223 ? -87.463  -44.445 85.103  1.00 46.63  ? 222 ASN A CG  1 
ATOM   1548  O  OD1 . ASN A  1 223 ? -88.495  -44.913 85.597  1.00 51.42  ? 222 ASN A OD1 1 
ATOM   1549  N  ND2 . ASN A  1 223 ? -87.043  -43.221 85.396  1.00 43.75  ? 222 ASN A ND2 1 
ATOM   1550  N  N   . THR A  1 224 ? -86.297  -48.805 82.941  1.00 32.79  ? 223 THR A N   1 
ATOM   1551  C  CA  . THR A  1 224 ? -85.635  -49.579 81.906  1.00 35.48  ? 223 THR A CA  1 
ATOM   1552  C  C   . THR A  1 224 ? -86.485  -49.616 80.633  1.00 37.74  ? 223 THR A C   1 
ATOM   1553  O  O   . THR A  1 224 ? -85.920  -49.713 79.566  1.00 41.35  ? 223 THR A O   1 
ATOM   1554  C  CB  . THR A  1 224 ? -85.324  -51.007 82.347  1.00 34.89  ? 223 THR A CB  1 
ATOM   1555  O  OG1 . THR A  1 224 ? -86.528  -51.559 82.856  1.00 33.58  ? 223 THR A OG1 1 
ATOM   1556  C  CG2 . THR A  1 224 ? -84.227  -51.067 83.381  1.00 36.76  ? 223 THR A CG2 1 
ATOM   1557  N  N   . ALA A  1 225 ? -87.816  -49.510 80.768  1.00 37.23  ? 224 ALA A N   1 
ATOM   1558  C  CA  . ALA A  1 225 ? -88.745  -49.434 79.645  1.00 40.22  ? 224 ALA A CA  1 
ATOM   1559  C  C   . ALA A  1 225 ? -89.446  -48.069 79.622  1.00 41.17  ? 224 ALA A C   1 
ATOM   1560  O  O   . ALA A  1 225 ? -90.625  -47.993 79.333  1.00 47.79  ? 224 ALA A O   1 
ATOM   1561  C  CB  . ALA A  1 225 ? -89.755  -50.547 79.773  1.00 43.24  ? 224 ALA A CB  1 
ATOM   1562  N  N   . GLY A  1 226 ? -88.719  -46.999 79.953  1.00 36.83  ? 225 GLY A N   1 
ATOM   1563  C  CA  . GLY A  1 226 ? -89.326  -45.699 80.135  1.00 36.91  ? 225 GLY A CA  1 
ATOM   1564  C  C   . GLY A  1 226 ? -90.205  -45.694 81.380  1.00 38.68  ? 225 GLY A C   1 
ATOM   1565  O  O   . GLY A  1 226 ? -89.982  -46.472 82.315  1.00 35.65  ? 225 GLY A O   1 
ATOM   1566  N  N   . CYS A  1 227 ? -91.241  -44.857 81.353  1.00 34.65  ? 226 CYS A N   1 
ATOM   1567  C  CA  . CYS A  1 227 ? -92.100  -44.610 82.492  1.00 33.93  ? 226 CYS A CA  1 
ATOM   1568  C  C   . CYS A  1 227 ? -92.983  -45.834 82.792  1.00 31.90  ? 226 CYS A C   1 
ATOM   1569  O  O   . CYS A  1 227 ? -93.450  -46.005 83.924  1.00 28.68  ? 226 CYS A O   1 
ATOM   1570  C  CB  . CYS A  1 227 ? -92.895  -43.341 82.229  1.00 32.82  ? 226 CYS A CB  1 
ATOM   1571  S  SG  . CYS A  1 227 ? -91.801  -41.898 82.050  1.00 37.71  ? 226 CYS A SG  1 
ATOM   1572  N  N   . THR A  1 228 ? -93.166  -46.702 81.794  1.00 31.19  ? 227 THR A N   1 
ATOM   1573  C  CA  . THR A  1 228 ? -94.011  -47.917 81.923  1.00 35.76  ? 227 THR A CA  1 
ATOM   1574  C  C   . THR A  1 228 ? -93.486  -48.836 83.027  1.00 35.61  ? 227 THR A C   1 
ATOM   1575  O  O   . THR A  1 228 ? -94.260  -49.438 83.755  1.00 38.34  ? 227 THR A O   1 
ATOM   1576  C  CB  . THR A  1 228 ? -94.062  -48.749 80.633  1.00 40.24  ? 227 THR A CB  1 
ATOM   1577  O  OG1 . THR A  1 228 ? -94.267  -47.875 79.524  1.00 48.88  ? 227 THR A OG1 1 
ATOM   1578  C  CG2 . THR A  1 228 ? -95.160  -49.789 80.668  1.00 43.98  ? 227 THR A CG2 1 
ATOM   1579  N  N   . SER A  1 229 ? -92.162  -48.929 83.167  1.00 31.71  ? 228 SER A N   1 
ATOM   1580  C  CA  . SER A  1 229 ? -91.576  -49.907 84.082  1.00 33.20  ? 228 SER A CA  1 
ATOM   1581  C  C   . SER A  1 229 ? -91.647  -49.428 85.542  1.00 29.43  ? 228 SER A C   1 
ATOM   1582  O  O   . SER A  1 229 ? -91.325  -50.171 86.458  1.00 30.75  ? 228 SER A O   1 
ATOM   1583  C  CB  . SER A  1 229 ? -90.181  -50.261 83.640  1.00 33.36  ? 228 SER A CB  1 
ATOM   1584  O  OG  . SER A  1 229 ? -89.512  -49.135 83.108  1.00 37.15  ? 228 SER A OG  1 
ATOM   1585  N  N   . ALA A  1 230 ? -92.133  -48.208 85.766  1.00 27.97  ? 229 ALA A N   1 
ATOM   1586  C  CA  . ALA A  1 230 ? -92.233  -47.634 87.133  1.00 29.08  ? 229 ALA A CA  1 
ATOM   1587  C  C   . ALA A  1 230 ? -93.354  -48.313 87.929  1.00 31.22  ? 229 ALA A C   1 
ATOM   1588  O  O   . ALA A  1 230 ? -93.466  -48.133 89.158  1.00 30.61  ? 229 ALA A O   1 
ATOM   1589  C  CB  . ALA A  1 230 ? -92.464  -46.148 87.046  1.00 27.70  ? 229 ALA A CB  1 
ATOM   1590  N  N   . GLY A  1 231 ? -94.231  -49.026 87.215  1.00 30.52  ? 230 GLY A N   1 
ATOM   1591  C  CA  . GLY A  1 231 ? -95.273  -49.824 87.841  1.00 31.49  ? 230 GLY A CA  1 
ATOM   1592  C  C   . GLY A  1 231 ? -96.424  -48.946 88.310  1.00 31.80  ? 230 GLY A C   1 
ATOM   1593  O  O   . GLY A  1 231 ? -96.585  -47.820 87.824  1.00 31.87  ? 230 GLY A O   1 
ATOM   1594  N  N   . PRO A  1 232 ? -97.264  -49.432 89.253  1.00 32.25  ? 231 PRO A N   1 
ATOM   1595  C  CA  . PRO A  1 232 ? -98.434  -48.673 89.699  1.00 31.16  ? 231 PRO A CA  1 
ATOM   1596  C  C   . PRO A  1 232 ? -98.050  -47.598 90.726  1.00 28.38  ? 231 PRO A C   1 
ATOM   1597  O  O   . PRO A  1 232 ? -96.881  -47.466 91.090  1.00 28.95  ? 231 PRO A O   1 
ATOM   1598  C  CB  . PRO A  1 232 ? -99.286  -49.771 90.356  1.00 33.29  ? 231 PRO A CB  1 
ATOM   1599  C  CG  . PRO A  1 232 ? -98.235  -50.682 90.987  1.00 34.15  ? 231 PRO A CG  1 
ATOM   1600  C  CD  . PRO A  1 232 ? -97.138  -50.734 89.940  1.00 32.40  ? 231 PRO A CD  1 
ATOM   1601  N  N   . HIS A  1 233 ? -99.045  -46.875 91.220  1.00 27.26  ? 232 HIS A N   1 
ATOM   1602  C  CA  . HIS A  1 233 ? -98.856  -45.918 92.292  1.00 28.84  ? 232 HIS A CA  1 
ATOM   1603  C  C   . HIS A  1 233 ? -98.282  -46.599 93.535  1.00 29.29  ? 232 HIS A C   1 
ATOM   1604  O  O   . HIS A  1 233 ? -98.663  -47.702 93.889  1.00 26.21  ? 232 HIS A O   1 
ATOM   1605  C  CB  . HIS A  1 233 ? -100.168 -45.215 92.631  1.00 29.38  ? 232 HIS A CB  1 
ATOM   1606  C  CG  . HIS A  1 233 ? -100.677 -44.396 91.503  1.00 30.99  ? 232 HIS A CG  1 
ATOM   1607  N  ND1 . HIS A  1 233 ? -101.781 -43.574 91.614  1.00 28.87  ? 232 HIS A ND1 1 
ATOM   1608  C  CD2 . HIS A  1 233 ? -100.217 -44.261 90.234  1.00 31.08  ? 232 HIS A CD2 1 
ATOM   1609  C  CE1 . HIS A  1 233 ? -101.984 -42.968 90.456  1.00 30.90  ? 232 HIS A CE1 1 
ATOM   1610  N  NE2 . HIS A  1 233 ? -101.027 -43.367 89.591  1.00 31.64  ? 232 HIS A NE2 1 
ATOM   1611  N  N   . PHE A  1 234 ? -97.344  -45.910 94.189  1.00 25.94  ? 233 PHE A N   1 
ATOM   1612  C  CA  . PHE A  1 234 ? -96.755  -46.419 95.403  1.00 27.45  ? 233 PHE A CA  1 
ATOM   1613  C  C   . PHE A  1 234 ? -97.850  -46.524 96.469  1.00 27.97  ? 233 PHE A C   1 
ATOM   1614  O  O   . PHE A  1 234 ? -98.445  -45.510 96.842  1.00 27.00  ? 233 PHE A O   1 
ATOM   1615  C  CB  . PHE A  1 234 ? -95.635  -45.497 95.861  1.00 26.15  ? 233 PHE A CB  1 
ATOM   1616  C  CG  . PHE A  1 234 ? -95.002  -45.886 97.170  1.00 28.53  ? 233 PHE A CG  1 
ATOM   1617  C  CD1 . PHE A  1 234 ? -94.758  -44.924 98.137  1.00 29.36  ? 233 PHE A CD1 1 
ATOM   1618  C  CD2 . PHE A  1 234 ? -94.654  -47.204 97.432  1.00 29.05  ? 233 PHE A CD2 1 
ATOM   1619  C  CE1 . PHE A  1 234 ? -94.138  -45.270 99.326  1.00 32.14  ? 233 PHE A CE1 1 
ATOM   1620  C  CE2 . PHE A  1 234 ? -94.039  -47.546 98.631  1.00 31.83  ? 233 PHE A CE2 1 
ATOM   1621  C  CZ  . PHE A  1 234 ? -93.786  -46.579 99.569  1.00 30.03  ? 233 PHE A CZ  1 
ATOM   1622  N  N   . ASN A  1 235 ? -98.159  -47.760 96.886  1.00 31.07  ? 234 ASN A N   1 
ATOM   1623  C  CA  . ASN A  1 235 ? -99.372  -48.011 97.670  1.00 32.76  ? 234 ASN A CA  1 
ATOM   1624  C  C   . ASN A  1 235 ? -99.108  -49.078 98.732  1.00 34.69  ? 234 ASN A C   1 
ATOM   1625  O  O   . ASN A  1 235 ? -99.674  -50.163 98.692  1.00 33.53  ? 234 ASN A O   1 
ATOM   1626  C  CB  . ASN A  1 235 ? -100.518 -48.424 96.752  1.00 32.90  ? 234 ASN A CB  1 
ATOM   1627  C  CG  . ASN A  1 235 ? -101.836 -48.624 97.472  1.00 33.64  ? 234 ASN A CG  1 
ATOM   1628  O  OD1 . ASN A  1 235 ? -102.109 -48.000 98.506  1.00 32.09  ? 234 ASN A OD1 1 
ATOM   1629  N  ND2 . ASN A  1 235 ? -102.700 -49.407 96.854  1.00 33.16  ? 234 ASN A ND2 1 
ATOM   1630  N  N   . PRO A  1 236 ? -98.241  -48.805 99.721  1.00 34.53  ? 235 PRO A N   1 
ATOM   1631  C  CA  . PRO A  1 236 ? -97.883  -49.817 100.714 1.00 36.74  ? 235 PRO A CA  1 
ATOM   1632  C  C   . PRO A  1 236 ? -99.050  -50.218 101.639 1.00 37.22  ? 235 PRO A C   1 
ATOM   1633  O  O   . PRO A  1 236 ? -99.046  -51.332 102.126 1.00 40.26  ? 235 PRO A O   1 
ATOM   1634  C  CB  . PRO A  1 236 ? -96.731  -49.138 101.486 1.00 35.07  ? 235 PRO A CB  1 
ATOM   1635  C  CG  . PRO A  1 236 ? -97.025  -47.668 101.354 1.00 35.15  ? 235 PRO A CG  1 
ATOM   1636  C  CD  . PRO A  1 236 ? -97.559  -47.523 99.944  1.00 35.09  ? 235 PRO A CD  1 
ATOM   1637  N  N   . LEU A  1 237 ? -100.042 -49.337 101.827 1.00 38.68  ? 236 LEU A N   1 
ATOM   1638  C  CA  . LEU A  1 237 ? -101.190 -49.589 102.711 1.00 41.62  ? 236 LEU A CA  1 
ATOM   1639  C  C   . LEU A  1 237 ? -102.377 -50.208 101.949 1.00 46.16  ? 236 LEU A C   1 
ATOM   1640  O  O   . LEU A  1 237 ? -103.457 -50.339 102.528 1.00 46.09  ? 236 LEU A O   1 
ATOM   1641  C  CB  . LEU A  1 237 ? -101.624 -48.276 103.366 1.00 40.09  ? 236 LEU A CB  1 
ATOM   1642  C  CG  . LEU A  1 237 ? -100.610 -47.589 104.278 1.00 43.86  ? 236 LEU A CG  1 
ATOM   1643  C  CD1 . LEU A  1 237 ? -101.246 -46.386 104.958 1.00 45.48  ? 236 LEU A CD1 1 
ATOM   1644  C  CD2 . LEU A  1 237 ? -100.049 -48.540 105.314 1.00 46.06  ? 236 LEU A CD2 1 
ATOM   1645  N  N   . SER A  1 238 ? -102.200 -50.545 100.662 1.00 42.27  ? 237 SER A N   1 
ATOM   1646  C  CA  . SER A  1 238 ? -103.223 -51.206 99.834  1.00 42.07  ? 237 SER A CA  1 
ATOM   1647  C  C   . SER A  1 238 ? -104.566 -50.474 99.860  1.00 41.65  ? 237 SER A C   1 
ATOM   1648  O  O   . SER A  1 238 ? -105.614 -51.105 99.987  1.00 41.88  ? 237 SER A O   1 
ATOM   1649  C  CB  . SER A  1 238 ? -103.434 -52.627 100.255 1.00 42.47  ? 237 SER A CB  1 
ATOM   1650  O  OG  . SER A  1 238 ? -102.299 -53.393 99.943  1.00 45.45  ? 237 SER A OG  1 
ATOM   1651  N  N   . ARG A  1 239 ? -104.544 -49.160 99.665  1.00 39.59  ? 238 ARG A N   1 
ATOM   1652  C  CA  . ARG A  1 239 ? -105.768 -48.387 99.580  1.00 38.91  ? 238 ARG A CA  1 
ATOM   1653  C  C   . ARG A  1 239 ? -106.110 -48.097 98.117  1.00 36.79  ? 238 ARG A C   1 
ATOM   1654  O  O   . ARG A  1 239 ? -105.358 -48.416 97.200  1.00 37.90  ? 238 ARG A O   1 
ATOM   1655  C  CB  . ARG A  1 239 ? -105.616 -47.137 100.438 1.00 40.92  ? 238 ARG A CB  1 
ATOM   1656  C  CG  . ARG A  1 239 ? -105.324 -47.492 101.887 1.00 48.19  ? 238 ARG A CG  1 
ATOM   1657  C  CD  . ARG A  1 239 ? -105.597 -46.384 102.874 1.00 53.89  ? 238 ARG A CD  1 
ATOM   1658  N  NE  . ARG A  1 239 ? -105.040 -46.743 104.166 1.00 58.89  ? 238 ARG A NE  1 
ATOM   1659  C  CZ  . ARG A  1 239 ? -105.190 -46.030 105.271 1.00 63.46  ? 238 ARG A CZ  1 
ATOM   1660  N  NH1 . ARG A  1 239 ? -104.675 -46.467 106.409 1.00 61.77  ? 238 ARG A NH1 1 
ATOM   1661  N  NH2 . ARG A  1 239 ? -105.868 -44.894 105.236 1.00 64.14  ? 238 ARG A NH2 1 
ATOM   1662  N  N   . LYS A  1 240 ? -107.304 -47.546 97.929  1.00 37.69  ? 239 LYS A N   1 
ATOM   1663  C  CA  . LYS A  1 240 ? -107.753 -47.035 96.671  1.00 40.24  ? 239 LYS A CA  1 
ATOM   1664  C  C   . LYS A  1 240 ? -107.092 -45.671 96.435  1.00 36.44  ? 239 LYS A C   1 
ATOM   1665  O  O   . LYS A  1 240 ? -106.668 -44.997 97.376  1.00 31.32  ? 239 LYS A O   1 
ATOM   1666  C  CB  . LYS A  1 240 ? -109.280 -46.906 96.640  1.00 43.64  ? 239 LYS A CB  1 
ATOM   1667  C  CG  . LYS A  1 240 ? -110.061 -48.217 96.658  1.00 53.39  ? 239 LYS A CG  1 
ATOM   1668  C  CD  . LYS A  1 240 ? -109.345 -49.364 95.957  1.00 64.59  ? 239 LYS A CD  1 
ATOM   1669  C  CE  . LYS A  1 240 ? -110.257 -50.470 95.455  1.00 75.38  ? 239 LYS A CE  1 
ATOM   1670  N  NZ  . LYS A  1 240 ? -110.935 -51.189 96.561  1.00 78.72  ? 239 LYS A NZ  1 
ATOM   1671  N  N   . HIS A  1 241 ? -107.043 -45.290 95.155  1.00 36.81  ? 240 HIS A N   1 
ATOM   1672  C  CA  . HIS A  1 241 ? -106.516 -44.003 94.708  1.00 33.29  ? 240 HIS A CA  1 
ATOM   1673  C  C   . HIS A  1 241 ? -107.418 -42.883 95.225  1.00 32.58  ? 240 HIS A C   1 
ATOM   1674  O  O   . HIS A  1 241 ? -108.643 -42.969 95.178  1.00 33.55  ? 240 HIS A O   1 
ATOM   1675  C  CB  . HIS A  1 241 ? -106.410 -43.973 93.174  1.00 32.06  ? 240 HIS A CB  1 
ATOM   1676  C  CG  . HIS A  1 241 ? -105.929 -42.656 92.653  1.00 30.78  ? 240 HIS A CG  1 
ATOM   1677  N  ND1 . HIS A  1 241 ? -104.589 -42.260 92.711  1.00 29.44  ? 240 HIS A ND1 1 
ATOM   1678  C  CD2 . HIS A  1 241 ? -106.612 -41.609 92.142  1.00 31.54  ? 240 HIS A CD2 1 
ATOM   1679  C  CE1 . HIS A  1 241 ? -104.487 -41.042 92.190  1.00 31.87  ? 240 HIS A CE1 1 
ATOM   1680  N  NE2 . HIS A  1 241 ? -105.709 -40.615 91.853  1.00 29.94  ? 240 HIS A NE2 1 
ATOM   1681  N  N   . GLY A  1 242 ? -106.807 -41.789 95.671  1.00 30.08  ? 241 GLY A N   1 
ATOM   1682  C  CA  . GLY A  1 242 ? -107.556 -40.610 96.028  1.00 29.70  ? 241 GLY A CA  1 
ATOM   1683  C  C   . GLY A  1 242 ? -106.765 -39.337 95.769  1.00 31.45  ? 241 GLY A C   1 
ATOM   1684  O  O   . GLY A  1 242 ? -105.708 -39.367 95.160  1.00 32.16  ? 241 GLY A O   1 
ATOM   1685  N  N   . GLY A  1 243 ? -107.314 -38.218 96.232  1.00 31.66  ? 242 GLY A N   1 
ATOM   1686  C  CA  . GLY A  1 243 ? -106.630 -36.958 96.251  1.00 31.84  ? 242 GLY A CA  1 
ATOM   1687  C  C   . GLY A  1 243 ? -105.698 -36.888 97.449  1.00 32.47  ? 242 GLY A C   1 
ATOM   1688  O  O   . GLY A  1 243 ? -105.831 -37.669 98.385  1.00 32.81  ? 242 GLY A O   1 
ATOM   1689  N  N   . PRO A  1 244 ? -104.720 -35.958 97.457  1.00 31.80  ? 243 PRO A N   1 
ATOM   1690  C  CA  . PRO A  1 244 ? -103.798 -35.859 98.579  1.00 33.12  ? 243 PRO A CA  1 
ATOM   1691  C  C   . PRO A  1 244 ? -104.474 -35.574 99.932  1.00 36.13  ? 243 PRO A C   1 
ATOM   1692  O  O   . PRO A  1 244 ? -103.937 -35.986 100.945 1.00 36.68  ? 243 PRO A O   1 
ATOM   1693  C  CB  . PRO A  1 244 ? -102.820 -34.747 98.181  1.00 31.87  ? 243 PRO A CB  1 
ATOM   1694  C  CG  . PRO A  1 244 ? -103.496 -33.999 97.051  1.00 32.95  ? 243 PRO A CG  1 
ATOM   1695  C  CD  . PRO A  1 244 ? -104.437 -34.986 96.392  1.00 31.42  ? 243 PRO A CD  1 
ATOM   1696  N  N   . LYS A  1 245 ? -105.631 -34.907 99.924  1.00 41.23  ? 244 LYS A N   1 
ATOM   1697  C  CA  . LYS A  1 245 ? -106.339 -34.500 101.146 1.00 46.41  ? 244 LYS A CA  1 
ATOM   1698  C  C   . LYS A  1 245 ? -107.224 -35.625 101.695 1.00 44.94  ? 244 LYS A C   1 
ATOM   1699  O  O   . LYS A  1 245 ? -107.826 -35.450 102.730 1.00 46.91  ? 244 LYS A O   1 
ATOM   1700  C  CB  . LYS A  1 245 ? -107.230 -33.284 100.869 1.00 49.47  ? 244 LYS A CB  1 
ATOM   1701  C  CG  . LYS A  1 245 ? -106.596 -31.928 101.126 1.00 60.86  ? 244 LYS A CG  1 
ATOM   1702  C  CD  . LYS A  1 245 ? -105.499 -31.553 100.153 1.00 71.54  ? 244 LYS A CD  1 
ATOM   1703  C  CE  . LYS A  1 245 ? -104.111 -32.024 100.549 1.00 78.45  ? 244 LYS A CE  1 
ATOM   1704  N  NZ  . LYS A  1 245 ? -103.685 -31.489 101.865 1.00 82.20  ? 244 LYS A NZ  1 
ATOM   1705  N  N   . ASP A  1 246 ? -107.333 -36.756 100.992 1.00 42.50  ? 245 ASP A N   1 
ATOM   1706  C  CA  . ASP A  1 246 ? -108.226 -37.830 101.412 1.00 43.16  ? 245 ASP A CA  1 
ATOM   1707  C  C   . ASP A  1 246 ? -107.502 -38.798 102.341 1.00 45.87  ? 245 ASP A C   1 
ATOM   1708  O  O   . ASP A  1 246 ? -106.296 -38.979 102.249 1.00 42.70  ? 245 ASP A O   1 
ATOM   1709  C  CB  . ASP A  1 246 ? -108.764 -38.637 100.232 1.00 41.77  ? 245 ASP A CB  1 
ATOM   1710  C  CG  . ASP A  1 246 ? -109.597 -37.805 99.284  1.00 47.66  ? 245 ASP A CG  1 
ATOM   1711  O  OD1 . ASP A  1 246 ? -109.521 -38.062 98.068  1.00 49.60  ? 245 ASP A OD1 1 
ATOM   1712  O  OD2 . ASP A  1 246 ? -110.289 -36.885 99.767  1.00 50.24  ? 245 ASP A OD2 1 
ATOM   1713  N  N   . GLU A  1 247 ? -108.293 -39.455 103.195 1.00 47.93  ? 246 GLU A N   1 
ATOM   1714  C  CA  . GLU A  1 247 ? -107.818 -40.531 104.060 1.00 50.47  ? 246 GLU A CA  1 
ATOM   1715  C  C   . GLU A  1 247 ? -107.554 -41.751 103.179 1.00 43.69  ? 246 GLU A C   1 
ATOM   1716  O  O   . GLU A  1 247 ? -106.502 -42.393 103.269 1.00 46.32  ? 246 GLU A O   1 
ATOM   1717  C  CB  . GLU A  1 247 ? -108.848 -40.786 105.169 1.00 60.23  ? 246 GLU A CB  1 
ATOM   1718  C  CG  . GLU A  1 247 ? -108.652 -42.085 105.938 1.00 71.62  ? 246 GLU A CG  1 
ATOM   1719  C  CD  . GLU A  1 247 ? -107.832 -41.977 107.214 1.00 82.25  ? 246 GLU A CD  1 
ATOM   1720  O  OE1 . GLU A  1 247 ? -108.184 -42.666 108.198 1.00 92.84  ? 246 GLU A OE1 1 
ATOM   1721  O  OE2 . GLU A  1 247 ? -106.841 -41.214 107.224 1.00 81.20  ? 246 GLU A OE2 1 
ATOM   1722  N  N   . GLU A  1 248 ? -108.512 -42.055 102.299 1.00 40.92  ? 247 GLU A N   1 
ATOM   1723  C  CA  . GLU A  1 248 ? -108.355 -43.136 101.342 1.00 39.56  ? 247 GLU A CA  1 
ATOM   1724  C  C   . GLU A  1 248 ? -107.536 -42.603 100.153 1.00 35.51  ? 247 GLU A C   1 
ATOM   1725  O  O   . GLU A  1 248 ? -108.067 -41.951 99.273  1.00 36.55  ? 247 GLU A O   1 
ATOM   1726  C  CB  . GLU A  1 248 ? -109.723 -43.668 100.892 1.00 39.95  ? 247 GLU A CB  1 
ATOM   1727  C  CG  . GLU A  1 248 ? -109.673 -44.977 100.109 1.00 43.19  ? 247 GLU A CG  1 
ATOM   1728  C  CD  . GLU A  1 248 ? -109.293 -46.215 100.899 1.00 45.27  ? 247 GLU A CD  1 
ATOM   1729  O  OE1 . GLU A  1 248 ? -109.033 -47.273 100.285 1.00 46.10  ? 247 GLU A OE1 1 
ATOM   1730  O  OE2 . GLU A  1 248 ? -109.236 -46.119 102.133 1.00 57.31  ? 247 GLU A OE2 1 
ATOM   1731  N  N   . ARG A  1 249 ? -106.237 -42.904 100.149 1.00 33.68  ? 248 ARG A N   1 
ATOM   1732  C  CA  . ARG A  1 249 ? -105.351 -42.542 99.048  1.00 33.31  ? 248 ARG A CA  1 
ATOM   1733  C  C   . ARG A  1 249 ? -104.181 -43.514 99.044  1.00 34.63  ? 248 ARG A C   1 
ATOM   1734  O  O   . ARG A  1 249 ? -103.907 -44.214 100.051 1.00 33.16  ? 248 ARG A O   1 
ATOM   1735  C  CB  . ARG A  1 249 ? -104.876 -41.087 99.163  1.00 31.17  ? 248 ARG A CB  1 
ATOM   1736  C  CG  . ARG A  1 249 ? -104.094 -40.773 100.436 1.00 33.12  ? 248 ARG A CG  1 
ATOM   1737  C  CD  . ARG A  1 249 ? -103.401 -39.412 100.432 1.00 32.92  ? 248 ARG A CD  1 
ATOM   1738  N  NE  . ARG A  1 249 ? -102.098 -39.451 99.774  1.00 31.96  ? 248 ARG A NE  1 
ATOM   1739  C  CZ  . ARG A  1 249 ? -101.150 -38.527 99.914  1.00 31.92  ? 248 ARG A CZ  1 
ATOM   1740  N  NH1 . ARG A  1 249 ? -99.931  -38.740 99.433  1.00 32.33  ? 248 ARG A NH1 1 
ATOM   1741  N  NH2 . ARG A  1 249 ? -101.414 -37.411 100.569 1.00 33.89  ? 248 ARG A NH2 1 
ATOM   1742  N  N   . HIS A  1 250 ? -103.492 -43.550 97.900  1.00 30.62  ? 249 HIS A N   1 
ATOM   1743  C  CA  . HIS A  1 250 ? -102.170 -44.147 97.822  1.00 30.69  ? 249 HIS A CA  1 
ATOM   1744  C  C   . HIS A  1 250 ? -101.172 -43.192 98.491  1.00 28.82  ? 249 HIS A C   1 
ATOM   1745  O  O   . HIS A  1 250 ? -101.365 -41.984 98.490  1.00 29.13  ? 249 HIS A O   1 
ATOM   1746  C  CB  . HIS A  1 250 ? -101.783 -44.411 96.363  1.00 32.10  ? 249 HIS A CB  1 
ATOM   1747  C  CG  . HIS A  1 250 ? -102.745 -45.266 95.608  1.00 34.77  ? 249 HIS A CG  1 
ATOM   1748  N  ND1 . HIS A  1 250 ? -102.954 -45.142 94.229  1.00 33.44  ? 249 HIS A ND1 1 
ATOM   1749  C  CD2 . HIS A  1 250 ? -103.506 -46.300 96.022  1.00 34.40  ? 249 HIS A CD2 1 
ATOM   1750  C  CE1 . HIS A  1 250 ? -103.814 -46.070 93.851  1.00 34.69  ? 249 HIS A CE1 1 
ATOM   1751  N  NE2 . HIS A  1 250 ? -104.157 -46.794 94.928  1.00 34.65  ? 249 HIS A NE2 1 
ATOM   1752  N  N   . VAL A  1 251 ? -100.083 -43.733 99.036  1.00 28.79  ? 250 VAL A N   1 
ATOM   1753  C  CA  . VAL A  1 251 ? -99.010  -42.870 99.521  1.00 30.92  ? 250 VAL A CA  1 
ATOM   1754  C  C   . VAL A  1 251 ? -98.553  -41.940 98.390  1.00 31.13  ? 250 VAL A C   1 
ATOM   1755  O  O   . VAL A  1 251 ? -98.388  -40.755 98.630  1.00 32.61  ? 250 VAL A O   1 
ATOM   1756  C  CB  . VAL A  1 251 ? -97.831  -43.667 100.107 1.00 31.61  ? 250 VAL A CB  1 
ATOM   1757  C  CG1 . VAL A  1 251 ? -96.623  -42.764 100.340 1.00 32.68  ? 250 VAL A CG1 1 
ATOM   1758  C  CG2 . VAL A  1 251 ? -98.239  -44.378 101.399 1.00 33.46  ? 250 VAL A CG2 1 
ATOM   1759  N  N   . GLY A  1 252 ? -98.446  -42.469 97.159  1.00 30.63  ? 251 GLY A N   1 
ATOM   1760  C  CA  . GLY A  1 252 ? -97.902  -41.694 96.030  1.00 30.72  ? 251 GLY A CA  1 
ATOM   1761  C  C   . GLY A  1 252 ? -98.867  -40.694 95.391  1.00 30.64  ? 251 GLY A C   1 
ATOM   1762  O  O   . GLY A  1 252 ? -98.518  -40.082 94.376  1.00 29.44  ? 251 GLY A O   1 
ATOM   1763  N  N   A SER A  1 253 ? -100.080 -40.516 95.927  0.30 31.55  ? 252 SER A N   1 
ATOM   1764  C  CA  A SER A  1 253 ? -101.110 -39.751 95.209  0.30 31.48  ? 252 SER A CA  1 
ATOM   1765  C  C   A SER A  1 253 ? -101.079 -38.267 95.610  0.30 31.50  ? 252 SER A C   1 
ATOM   1766  O  O   A SER A  1 253 ? -101.820 -37.835 96.494  0.30 31.20  ? 252 SER A O   1 
ATOM   1767  C  CB  A SER A  1 253 ? -102.465 -40.412 95.371  0.30 32.26  ? 252 SER A CB  1 
ATOM   1768  O  OG  A SER A  1 253 ? -102.599 -41.548 94.497  0.30 33.99  ? 252 SER A OG  1 
ATOM   1769  N  N   B ASP A  1 253 ? -100.047 -40.507 96.003  0.70 30.08  ? 252 ASP A N   1 
ATOM   1770  C  CA  B ASP A  1 253 ? -101.104 -39.687 95.437  0.70 28.50  ? 252 ASP A CA  1 
ATOM   1771  C  C   B ASP A  1 253 ? -100.910 -38.213 95.788  0.70 30.64  ? 252 ASP A C   1 
ATOM   1772  O  O   B ASP A  1 253 ? -101.417 -37.721 96.815  0.70 32.05  ? 252 ASP A O   1 
ATOM   1773  C  CB  B ASP A  1 253 ? -102.480 -40.145 95.905  0.70 28.37  ? 252 ASP A CB  1 
ATOM   1774  C  CG  B ASP A  1 253 ? -102.900 -41.423 95.222  0.70 30.54  ? 252 ASP A CG  1 
ATOM   1775  O  OD1 B ASP A  1 253 ? -102.286 -41.746 94.175  0.70 32.27  ? 252 ASP A OD1 1 
ATOM   1776  O  OD2 B ASP A  1 253 ? -103.832 -42.062 95.712  0.70 26.93  ? 252 ASP A OD2 1 
ATOM   1777  N  N   . LEU A  1 254 ? -100.254 -37.485 94.886  1.00 29.65  ? 253 LEU A N   1 
ATOM   1778  C  CA  . LEU A  1 254 ? -100.004 -36.067 95.126  1.00 29.26  ? 253 LEU A CA  1 
ATOM   1779  C  C   . LEU A  1 254 ? -100.966 -35.149 94.360  1.00 29.25  ? 253 LEU A C   1 
ATOM   1780  O  O   . LEU A  1 254 ? -100.816 -33.929 94.395  1.00 30.36  ? 253 LEU A O   1 
ATOM   1781  C  CB  . LEU A  1 254 ? -98.553  -35.764 94.745  1.00 30.19  ? 253 LEU A CB  1 
ATOM   1782  C  CG  . LEU A  1 254 ? -97.509  -36.443 95.621  1.00 32.57  ? 253 LEU A CG  1 
ATOM   1783  C  CD1 . LEU A  1 254 ? -96.109  -36.184 95.101  1.00 33.01  ? 253 LEU A CD1 1 
ATOM   1784  C  CD2 . LEU A  1 254 ? -97.643  -35.972 97.066  1.00 34.74  ? 253 LEU A CD2 1 
ATOM   1785  N  N   . GLY A  1 255 ? -101.963 -35.701 93.675  1.00 25.17  ? 254 GLY A N   1 
ATOM   1786  C  CA  . GLY A  1 255 ? -102.978 -34.857 93.074  1.00 24.85  ? 254 GLY A CA  1 
ATOM   1787  C  C   . GLY A  1 255 ? -102.568 -34.396 91.678  1.00 24.46  ? 254 GLY A C   1 
ATOM   1788  O  O   . GLY A  1 255 ? -102.035 -35.170 90.876  1.00 26.55  ? 254 GLY A O   1 
ATOM   1789  N  N   . ASN A  1 256 ? -102.889 -33.143 91.389  1.00 24.17  ? 255 ASN A N   1 
ATOM   1790  C  CA  . ASN A  1 256 ? -102.665 -32.516 90.121  1.00 26.16  ? 255 ASN A CA  1 
ATOM   1791  C  C   . ASN A  1 256 ? -101.617 -31.404 90.280  1.00 25.49  ? 255 ASN A C   1 
ATOM   1792  O  O   . ASN A  1 256 ? -101.502 -30.797 91.339  1.00 26.01  ? 255 ASN A O   1 
ATOM   1793  C  CB  . ASN A  1 256 ? -103.952 -31.898 89.575  1.00 27.63  ? 255 ASN A CB  1 
ATOM   1794  C  CG  . ASN A  1 256 ? -104.900 -32.945 89.034  1.00 29.42  ? 255 ASN A CG  1 
ATOM   1795  O  OD1 . ASN A  1 256 ? -104.562 -33.654 88.081  1.00 27.74  ? 255 ASN A OD1 1 
ATOM   1796  N  ND2 . ASN A  1 256 ? -106.037 -33.099 89.696  1.00 27.75  ? 255 ASN A ND2 1 
ATOM   1797  N  N   . VAL A  1 257 ? -100.901 -31.150 89.190  1.00 24.79  ? 256 VAL A N   1 
ATOM   1798  C  CA  . VAL A  1 257 ? -100.151 -29.902 88.978  1.00 26.38  ? 256 VAL A CA  1 
ATOM   1799  C  C   . VAL A  1 257 ? -100.775 -29.207 87.773  1.00 28.45  ? 256 VAL A C   1 
ATOM   1800  O  O   . VAL A  1 257 ? -101.390 -29.868 86.946  1.00 30.60  ? 256 VAL A O   1 
ATOM   1801  C  CB  . VAL A  1 257 ? -98.647  -30.176 88.791  1.00 25.09  ? 256 VAL A CB  1 
ATOM   1802  C  CG1 . VAL A  1 257 ? -98.083  -30.818 90.047  1.00 24.82  ? 256 VAL A CG1 1 
ATOM   1803  C  CG2 . VAL A  1 257 ? -98.356  -31.045 87.590  1.00 25.69  ? 256 VAL A CG2 1 
ATOM   1804  N  N   . THR A  1 258 ? -100.614 -27.883 87.702  1.00 26.48  ? 257 THR A N   1 
ATOM   1805  C  CA  . THR A  1 258 ? -101.233 -27.065 86.703  1.00 28.97  ? 257 THR A CA  1 
ATOM   1806  C  C   . THR A  1 258 ? -100.159 -26.399 85.838  1.00 30.81  ? 257 THR A C   1 
ATOM   1807  O  O   . THR A  1 258 ? -99.302  -25.671 86.366  1.00 25.02  ? 257 THR A O   1 
ATOM   1808  C  CB  . THR A  1 258 ? -102.099 -25.981 87.354  1.00 32.02  ? 257 THR A CB  1 
ATOM   1809  O  OG1 . THR A  1 258 ? -103.118 -26.606 88.138  1.00 33.23  ? 257 THR A OG1 1 
ATOM   1810  C  CG2 . THR A  1 258 ? -102.747 -25.051 86.351  1.00 32.78  ? 257 THR A CG2 1 
ATOM   1811  N  N   . ALA A  1 259 ? -100.258 -26.632 84.522  1.00 30.03  ? 258 ALA A N   1 
ATOM   1812  C  CA  . ALA A  1 259 ? -99.446  -25.997 83.530  1.00 29.29  ? 258 ALA A CA  1 
ATOM   1813  C  C   . ALA A  1 259 ? -100.149 -24.709 83.080  1.00 31.62  ? 258 ALA A C   1 
ATOM   1814  O  O   . ALA A  1 259 ? -101.349 -24.689 82.911  1.00 30.14  ? 258 ALA A O   1 
ATOM   1815  C  CB  . ALA A  1 259 ? -99.199  -26.944 82.383  1.00 29.72  ? 258 ALA A CB  1 
ATOM   1816  N  N   . ASP A  1 260 ? -99.370  -23.632 82.926  1.00 32.33  ? 259 ASP A N   1 
ATOM   1817  C  CA  . ASP A  1 260 ? -99.864  -22.331 82.495  1.00 32.91  ? 259 ASP A CA  1 
ATOM   1818  C  C   . ASP A  1 260 ? -99.937  -22.320 80.964  1.00 32.01  ? 259 ASP A C   1 
ATOM   1819  O  O   . ASP A  1 260 ? -99.613  -23.320 80.335  1.00 26.26  ? 259 ASP A O   1 
ATOM   1820  C  CB  . ASP A  1 260 ? -98.982  -21.219 83.067  1.00 32.20  ? 259 ASP A CB  1 
ATOM   1821  C  CG  . ASP A  1 260 ? -97.563  -21.155 82.524  1.00 33.90  ? 259 ASP A CG  1 
ATOM   1822  O  OD1 . ASP A  1 260 ? -96.744  -20.488 83.186  1.00 35.92  ? 259 ASP A OD1 1 
ATOM   1823  O  OD2 . ASP A  1 260 ? -97.279  -21.773 81.456  1.00 28.82  ? 259 ASP A OD2 1 
ATOM   1824  N  N   . LYS A  1 261 ? -100.321 -21.175 80.375  1.00 38.07  ? 260 LYS A N   1 
ATOM   1825  C  CA  . LYS A  1 261 ? -100.524 -21.083 78.911  1.00 40.50  ? 260 LYS A CA  1 
ATOM   1826  C  C   . LYS A  1 261 ? -99.212  -21.300 78.135  1.00 36.78  ? 260 LYS A C   1 
ATOM   1827  O  O   . LYS A  1 261 ? -99.264  -21.604 76.936  1.00 35.19  ? 260 LYS A O   1 
ATOM   1828  C  CB  . LYS A  1 261 ? -101.245 -19.804 78.469  1.00 46.78  ? 260 LYS A CB  1 
ATOM   1829  C  CG  . LYS A  1 261 ? -100.781 -18.459 79.016  1.00 57.85  ? 260 LYS A CG  1 
ATOM   1830  C  CD  . LYS A  1 261 ? -99.291  -18.148 78.974  1.00 68.93  ? 260 LYS A CD  1 
ATOM   1831  C  CE  . LYS A  1 261 ? -98.599  -18.204 80.330  1.00 75.48  ? 260 LYS A CE  1 
ATOM   1832  N  NZ  . LYS A  1 261 ? -99.107  -17.192 81.291  1.00 76.71  ? 260 LYS A NZ  1 
ATOM   1833  N  N   . ASP A  1 262 ? -98.058  -21.202 78.806  1.00 34.41  ? 261 ASP A N   1 
ATOM   1834  C  CA  . ASP A  1 262 ? -96.763  -21.456 78.176  1.00 35.33  ? 261 ASP A CA  1 
ATOM   1835  C  C   . ASP A  1 262 ? -96.331  -22.918 78.322  1.00 31.66  ? 261 ASP A C   1 
ATOM   1836  O  O   . ASP A  1 262 ? -95.236  -23.273 77.890  1.00 31.40  ? 261 ASP A O   1 
ATOM   1837  C  CB  . ASP A  1 262 ? -95.685  -20.526 78.733  1.00 38.09  ? 261 ASP A CB  1 
ATOM   1838  C  CG  . ASP A  1 262 ? -95.908  -19.072 78.340  1.00 43.53  ? 261 ASP A CG  1 
ATOM   1839  O  OD1 . ASP A  1 262 ? -95.651  -18.199 79.194  1.00 46.25  ? 261 ASP A OD1 1 
ATOM   1840  O  OD2 . ASP A  1 262 ? -96.350  -18.830 77.188  1.00 42.36  ? 261 ASP A OD2 1 
ATOM   1841  N  N   . GLY A  1 263 ? -97.161  -23.743 78.964  1.00 29.45  ? 262 GLY A N   1 
ATOM   1842  C  CA  . GLY A  1 263 ? -96.886  -25.167 79.131  1.00 28.85  ? 262 GLY A CA  1 
ATOM   1843  C  C   . GLY A  1 263 ? -96.009  -25.457 80.339  1.00 25.56  ? 262 GLY A C   1 
ATOM   1844  O  O   . GLY A  1 263 ? -95.415  -26.516 80.421  1.00 27.05  ? 262 GLY A O   1 
ATOM   1845  N  N   . VAL A  1 264 ? -95.939  -24.514 81.280  1.00 26.54  ? 263 VAL A N   1 
ATOM   1846  C  CA  . VAL A  1 264 ? -95.065  -24.636 82.430  1.00 28.08  ? 263 VAL A CA  1 
ATOM   1847  C  C   . VAL A  1 264 ? -95.903  -24.848 83.696  1.00 25.77  ? 263 VAL A C   1 
ATOM   1848  O  O   . VAL A  1 264 ? -96.764  -24.053 84.023  1.00 24.94  ? 263 VAL A O   1 
ATOM   1849  C  CB  . VAL A  1 264 ? -94.154  -23.405 82.595  1.00 30.19  ? 263 VAL A CB  1 
ATOM   1850  C  CG1 . VAL A  1 264 ? -93.314  -23.528 83.846  1.00 31.13  ? 263 VAL A CG1 1 
ATOM   1851  C  CG2 . VAL A  1 264 ? -93.262  -23.194 81.380  1.00 31.89  ? 263 VAL A CG2 1 
ATOM   1852  N  N   . ALA A  1 265 ? -95.585  -25.912 84.430  1.00 26.26  ? 264 ALA A N   1 
ATOM   1853  C  CA  . ALA A  1 265 ? -96.149  -26.143 85.756  1.00 27.13  ? 264 ALA A CA  1 
ATOM   1854  C  C   . ALA A  1 265 ? -95.097  -25.770 86.797  1.00 26.91  ? 264 ALA A C   1 
ATOM   1855  O  O   . ALA A  1 265 ? -94.108  -26.484 86.937  1.00 26.18  ? 264 ALA A O   1 
ATOM   1856  C  CB  . ALA A  1 265 ? -96.544  -27.590 85.909  1.00 26.71  ? 264 ALA A CB  1 
ATOM   1857  N  N   . ASP A  1 266 ? -95.325  -24.660 87.499  1.00 28.63  ? 265 ASP A N   1 
ATOM   1858  C  CA  . ASP A  1 266 ? -94.497  -24.284 88.650  1.00 30.12  ? 265 ASP A CA  1 
ATOM   1859  C  C   . ASP A  1 266 ? -95.097  -24.980 89.869  1.00 28.32  ? 265 ASP A C   1 
ATOM   1860  O  O   . ASP A  1 266 ? -96.003  -24.460 90.498  1.00 28.17  ? 265 ASP A O   1 
ATOM   1861  C  CB  . ASP A  1 266 ? -94.381  -22.758 88.772  1.00 30.65  ? 265 ASP A CB  1 
ATOM   1862  C  CG  . ASP A  1 266 ? -93.555  -22.160 87.631  1.00 31.60  ? 265 ASP A CG  1 
ATOM   1863  O  OD1 . ASP A  1 266 ? -92.503  -22.739 87.299  1.00 31.65  ? 265 ASP A OD1 1 
ATOM   1864  O  OD2 . ASP A  1 266 ? -94.019  -21.191 87.021  1.00 38.06  ? 265 ASP A OD2 1 
ATOM   1865  N  N   . VAL A  1 267 ? -94.586  -26.176 90.152  1.00 28.39  ? 266 VAL A N   1 
ATOM   1866  C  CA  . VAL A  1 267 ? -95.096  -27.054 91.200  1.00 28.10  ? 266 VAL A CA  1 
ATOM   1867  C  C   . VAL A  1 267 ? -94.785  -26.462 92.586  1.00 30.29  ? 266 VAL A C   1 
ATOM   1868  O  O   . VAL A  1 267 ? -93.641  -26.082 92.915  1.00 27.77  ? 266 VAL A O   1 
ATOM   1869  C  CB  . VAL A  1 267 ? -94.519  -28.470 91.040  1.00 28.55  ? 266 VAL A CB  1 
ATOM   1870  C  CG1 . VAL A  1 267 ? -94.941  -29.401 92.169  1.00 29.67  ? 266 VAL A CG1 1 
ATOM   1871  C  CG2 . VAL A  1 267 ? -94.890  -29.067 89.683  1.00 28.71  ? 266 VAL A CG2 1 
ATOM   1872  N  N   . SER A  1 268 ? -95.823  -26.393 93.424  1.00 31.39  ? 267 SER A N   1 
ATOM   1873  C  CA  . SER A  1 268 ? -95.647  -26.030 94.821  1.00 32.53  ? 267 SER A CA  1 
ATOM   1874  C  C   . SER A  1 268 ? -96.661  -26.803 95.663  1.00 32.84  ? 267 SER A C   1 
ATOM   1875  O  O   . SER A  1 268 ? -97.819  -26.451 95.664  1.00 34.31  ? 267 SER A O   1 
ATOM   1876  C  CB  . SER A  1 268 ? -95.774  -24.552 95.022  1.00 33.77  ? 267 SER A CB  1 
ATOM   1877  O  OG  . SER A  1 268 ? -95.422  -24.207 96.356  1.00 36.25  ? 267 SER A OG  1 
ATOM   1878  N  N   . ILE A  1 269 ? -96.190  -27.864 96.321  1.00 32.15  ? 268 ILE A N   1 
ATOM   1879  C  CA  . ILE A  1 269 ? -97.028  -28.815 97.020  1.00 36.32  ? 268 ILE A CA  1 
ATOM   1880  C  C   . ILE A  1 269 ? -96.392  -29.078 98.389  1.00 35.94  ? 268 ILE A C   1 
ATOM   1881  O  O   . ILE A  1 269 ? -95.172  -29.022 98.529  1.00 34.49  ? 268 ILE A O   1 
ATOM   1882  C  CB  . ILE A  1 269 ? -97.188  -30.089 96.156  1.00 37.64  ? 268 ILE A CB  1 
ATOM   1883  C  CG1 . ILE A  1 269 ? -98.243  -29.893 95.067  1.00 39.22  ? 268 ILE A CG1 1 
ATOM   1884  C  CG2 . ILE A  1 269 ? -97.499  -31.321 96.978  1.00 40.78  ? 268 ILE A CG2 1 
ATOM   1885  C  CD1 . ILE A  1 269 ? -98.330  -31.073 94.103  1.00 43.35  ? 268 ILE A CD1 1 
ATOM   1886  N  N   . GLU A  1 270 ? -97.236  -29.355 99.391  1.00 35.26  ? 269 GLU A N   1 
ATOM   1887  C  CA  . GLU A  1 270 ? -96.785  -29.850 100.686 1.00 36.38  ? 269 GLU A CA  1 
ATOM   1888  C  C   . GLU A  1 270 ? -97.626  -31.079 101.045 1.00 33.68  ? 269 GLU A C   1 
ATOM   1889  O  O   . GLU A  1 270 ? -98.838  -31.031 101.008 1.00 34.81  ? 269 GLU A O   1 
ATOM   1890  C  CB  . GLU A  1 270 ? -96.924  -28.724 101.711 1.00 43.14  ? 269 GLU A CB  1 
ATOM   1891  C  CG  . GLU A  1 270 ? -96.340  -29.032 103.070 1.00 52.32  ? 269 GLU A CG  1 
ATOM   1892  C  CD  . GLU A  1 270 ? -96.329  -27.815 103.989 1.00 63.26  ? 269 GLU A CD  1 
ATOM   1893  O  OE1 . GLU A  1 270 ? -95.359  -27.023 103.909 1.00 71.80  ? 269 GLU A OE1 1 
ATOM   1894  O  OE2 . GLU A  1 270 ? -97.314  -27.637 104.750 1.00 65.54  ? 269 GLU A OE2 1 
ATOM   1895  N  N   . ASP A  1 271 ? -96.969  -32.199 101.327 1.00 32.35  ? 270 ASP A N   1 
ATOM   1896  C  CA  . ASP A  1 271 ? -97.662  -33.426 101.619 1.00 35.20  ? 270 ASP A CA  1 
ATOM   1897  C  C   . ASP A  1 271 ? -97.067  -34.048 102.883 1.00 37.93  ? 270 ASP A C   1 
ATOM   1898  O  O   . ASP A  1 271 ? -95.847  -34.111 103.029 1.00 39.02  ? 270 ASP A O   1 
ATOM   1899  C  CB  . ASP A  1 271 ? -97.572  -34.431 100.467 1.00 32.65  ? 270 ASP A CB  1 
ATOM   1900  C  CG  . ASP A  1 271 ? -98.600  -35.554 100.588 1.00 34.97  ? 270 ASP A CG  1 
ATOM   1901  O  OD1 . ASP A  1 271 ? -98.215  -36.711 100.906 1.00 31.94  ? 270 ASP A OD1 1 
ATOM   1902  O  OD2 . ASP A  1 271 ? -99.783  -35.263 100.387 1.00 39.03  ? 270 ASP A OD2 1 
ATOM   1903  N  N   . SER A  1 272 ? -97.942  -34.597 103.734 1.00 41.08  ? 271 SER A N   1 
ATOM   1904  C  CA  . SER A  1 272 ? -97.522  -35.232 104.986 1.00 43.37  ? 271 SER A CA  1 
ATOM   1905  C  C   . SER A  1 272 ? -97.649  -36.761 104.933 1.00 42.11  ? 271 SER A C   1 
ATOM   1906  O  O   . SER A  1 272 ? -97.370  -37.410 105.934 1.00 40.61  ? 271 SER A O   1 
ATOM   1907  C  CB  . SER A  1 272 ? -98.309  -34.671 106.147 1.00 50.20  ? 271 SER A CB  1 
ATOM   1908  O  OG  . SER A  1 272 ? -97.860  -33.357 106.460 1.00 53.93  ? 271 SER A OG  1 
ATOM   1909  N  N   . VAL A  1 273 ? -98.060  -37.343 103.794 1.00 34.03  ? 272 VAL A N   1 
ATOM   1910  C  CA  . VAL A  1 273 ? -98.190  -38.793 103.719 1.00 33.19  ? 272 VAL A CA  1 
ATOM   1911  C  C   . VAL A  1 273 ? -96.912  -39.398 103.127 1.00 35.53  ? 272 VAL A C   1 
ATOM   1912  O  O   . VAL A  1 273 ? -96.435  -40.432 103.580 1.00 33.90  ? 272 VAL A O   1 
ATOM   1913  C  CB  . VAL A  1 273 ? -99.452  -39.209 102.946 1.00 33.01  ? 272 VAL A CB  1 
ATOM   1914  C  CG1 . VAL A  1 273 ? -99.497  -40.712 102.688 1.00 34.89  ? 272 VAL A CG1 1 
ATOM   1915  C  CG2 . VAL A  1 273 ? -100.703 -38.769 103.681 1.00 36.45  ? 272 VAL A CG2 1 
ATOM   1916  N  N   . ILE A  1 274 ? -96.356  -38.752 102.092 1.00 34.86  ? 273 ILE A N   1 
ATOM   1917  C  CA  . ILE A  1 274 ? -95.073  -39.167 101.596 1.00 33.00  ? 273 ILE A CA  1 
ATOM   1918  C  C   . ILE A  1 274 ? -94.025  -38.829 102.664 1.00 32.93  ? 273 ILE A C   1 
ATOM   1919  O  O   . ILE A  1 274 ? -94.228  -37.942 103.491 1.00 31.33  ? 273 ILE A O   1 
ATOM   1920  C  CB  . ILE A  1 274 ? -94.743  -38.524 100.225 1.00 31.69  ? 273 ILE A CB  1 
ATOM   1921  C  CG1 . ILE A  1 274 ? -94.679  -36.996 100.286 1.00 30.04  ? 273 ILE A CG1 1 
ATOM   1922  C  CG2 . ILE A  1 274 ? -95.713  -39.007 99.156  1.00 31.31  ? 273 ILE A CG2 1 
ATOM   1923  C  CD1 . ILE A  1 274 ? -93.895  -36.366 99.119  1.00 31.26  ? 273 ILE A CD1 1 
ATOM   1924  N  N   . SER A  1 275 ? -92.877  -39.490 102.550 1.00 31.84  ? 274 SER A N   1 
ATOM   1925  C  CA  . SER A  1 275 ? -91.733  -39.275 103.398 1.00 34.26  ? 274 SER A CA  1 
ATOM   1926  C  C   . SER A  1 275 ? -90.435  -39.505 102.604 1.00 30.49  ? 274 SER A C   1 
ATOM   1927  O  O   . SER A  1 275 ? -90.451  -40.176 101.588 1.00 32.41  ? 274 SER A O   1 
ATOM   1928  C  CB  . SER A  1 275 ? -91.811  -40.189 104.592 1.00 37.81  ? 274 SER A CB  1 
ATOM   1929  O  OG  . SER A  1 275 ? -90.757  -39.897 105.489 1.00 38.54  ? 274 SER A OG  1 
ATOM   1930  N  N   . LEU A  1 276 ? -89.328  -38.909 103.069 1.00 31.67  ? 275 LEU A N   1 
ATOM   1931  C  CA  . LEU A  1 276 ? -88.006  -39.178 102.527 1.00 32.59  ? 275 LEU A CA  1 
ATOM   1932  C  C   . LEU A  1 276 ? -87.229  -40.170 103.403 1.00 36.84  ? 275 LEU A C   1 
ATOM   1933  O  O   . LEU A  1 276 ? -86.054  -40.405 103.157 1.00 34.53  ? 275 LEU A O   1 
ATOM   1934  C  CB  . LEU A  1 276 ? -87.254  -37.859 102.377 1.00 33.52  ? 275 LEU A CB  1 
ATOM   1935  C  CG  . LEU A  1 276 ? -87.977  -36.790 101.562 1.00 33.47  ? 275 LEU A CG  1 
ATOM   1936  C  CD1 . LEU A  1 276 ? -87.107  -35.549 101.438 1.00 34.56  ? 275 LEU A CD1 1 
ATOM   1937  C  CD2 . LEU A  1 276 ? -88.370  -37.312 100.182 1.00 33.52  ? 275 LEU A CD2 1 
ATOM   1938  N  N   . SER A  1 277 ? -87.892  -40.776 104.395 1.00 36.38  ? 276 SER A N   1 
ATOM   1939  C  CA  . SER A  1 277 ? -87.306  -41.889 105.135 1.00 39.17  ? 276 SER A CA  1 
ATOM   1940  C  C   . SER A  1 277 ? -88.406  -42.782 105.715 1.00 37.81  ? 276 SER A C   1 
ATOM   1941  O  O   . SER A  1 277 ? -89.572  -42.429 105.714 1.00 38.18  ? 276 SER A O   1 
ATOM   1942  C  CB  . SER A  1 277 ? -86.370  -41.386 106.215 1.00 42.57  ? 276 SER A CB  1 
ATOM   1943  O  OG  . SER A  1 277 ? -87.045  -40.479 107.058 1.00 40.96  ? 276 SER A OG  1 
ATOM   1944  N  N   . GLY A  1 278 ? -88.001  -43.954 106.202 1.00 41.41  ? 277 GLY A N   1 
ATOM   1945  C  CA  . GLY A  1 278 ? -88.922  -44.938 106.751 1.00 45.55  ? 277 GLY A CA  1 
ATOM   1946  C  C   . GLY A  1 278 ? -89.584  -45.741 105.651 1.00 49.49  ? 277 GLY A C   1 
ATOM   1947  O  O   . GLY A  1 278 ? -89.164  -45.698 104.487 1.00 44.66  ? 277 GLY A O   1 
ATOM   1948  N  N   . ASP A  1 279 ? -90.658  -46.450 105.999 1.00 49.59  ? 278 ASP A N   1 
ATOM   1949  C  CA  . ASP A  1 279 ? -91.221  -47.437 105.084 1.00 53.71  ? 278 ASP A CA  1 
ATOM   1950  C  C   . ASP A  1 279 ? -92.096  -46.763 104.013 1.00 44.61  ? 278 ASP A C   1 
ATOM   1951  O  O   . ASP A  1 279 ? -92.380  -47.380 103.016 1.00 45.32  ? 278 ASP A O   1 
ATOM   1952  C  CB  . ASP A  1 279 ? -91.940  -48.549 105.855 1.00 62.98  ? 278 ASP A CB  1 
ATOM   1953  C  CG  . ASP A  1 279 ? -91.066  -49.769 106.130 1.00 69.92  ? 278 ASP A CG  1 
ATOM   1954  O  OD1 . ASP A  1 279 ? -91.639  -50.866 106.293 1.00 80.16  ? 278 ASP A OD1 1 
ATOM   1955  O  OD2 . ASP A  1 279 ? -89.816  -49.623 106.173 1.00 72.10  ? 278 ASP A OD2 1 
ATOM   1956  N  N   . HIS A  1 280 ? -92.507  -45.508 104.225 1.00 41.18  ? 279 HIS A N   1 
ATOM   1957  C  CA  . HIS A  1 280 ? -93.208  -44.711 103.209 1.00 41.80  ? 279 HIS A CA  1 
ATOM   1958  C  C   . HIS A  1 280 ? -92.245  -43.776 102.453 1.00 37.20  ? 279 HIS A C   1 
ATOM   1959  O  O   . HIS A  1 280 ? -92.680  -42.777 101.827 1.00 35.79  ? 279 HIS A O   1 
ATOM   1960  C  CB  . HIS A  1 280 ? -94.356  -43.942 103.866 1.00 39.98  ? 279 HIS A CB  1 
ATOM   1961  C  CG  . HIS A  1 280 ? -95.439  -44.870 104.308 1.00 42.71  ? 279 HIS A CG  1 
ATOM   1962  N  ND1 . HIS A  1 280 ? -96.622  -44.416 104.835 1.00 38.69  ? 279 HIS A ND1 1 
ATOM   1963  C  CD2 . HIS A  1 280 ? -95.518  -46.225 104.277 1.00 41.58  ? 279 HIS A CD2 1 
ATOM   1964  C  CE1 . HIS A  1 280 ? -97.398  -45.450 105.115 1.00 43.41  ? 279 HIS A CE1 1 
ATOM   1965  N  NE2 . HIS A  1 280 ? -96.730  -46.578 104.797 1.00 42.18  ? 279 HIS A NE2 1 
ATOM   1966  N  N   . SER A  1 281 ? -90.948  -44.094 102.498 1.00 34.28  ? 280 SER A N   1 
ATOM   1967  C  CA  . SER A  1 281 ? -89.955  -43.322 101.766 1.00 33.23  ? 280 SER A CA  1 
ATOM   1968  C  C   . SER A  1 281 ? -90.179  -43.461 100.249 1.00 29.76  ? 280 SER A C   1 
ATOM   1969  O  O   . SER A  1 281 ? -90.321  -44.565 99.732  1.00 29.58  ? 280 SER A O   1 
ATOM   1970  C  CB  . SER A  1 281 ? -88.566  -43.747 102.088 1.00 33.45  ? 280 SER A CB  1 
ATOM   1971  O  OG  . SER A  1 281 ? -87.657  -43.035 101.257 1.00 33.56  ? 280 SER A OG  1 
ATOM   1972  N  N   . ILE A  1 282 ? -90.059  -42.334 99.555  1.00 31.32  ? 281 ILE A N   1 
ATOM   1973  C  CA  . ILE A  1 282 ? -90.178  -42.271 98.088  1.00 32.42  ? 281 ILE A CA  1 
ATOM   1974  C  C   . ILE A  1 282 ? -88.793  -42.228 97.423  1.00 33.17  ? 281 ILE A C   1 
ATOM   1975  O  O   . ILE A  1 282 ? -88.717  -42.168 96.193  1.00 32.67  ? 281 ILE A O   1 
ATOM   1976  C  CB  . ILE A  1 282 ? -91.042  -41.066 97.700  1.00 31.10  ? 281 ILE A CB  1 
ATOM   1977  C  CG1 . ILE A  1 282 ? -90.395  -39.732 98.080  1.00 30.64  ? 281 ILE A CG1 1 
ATOM   1978  C  CG2 . ILE A  1 282 ? -92.423  -41.232 98.309  1.00 32.01  ? 281 ILE A CG2 1 
ATOM   1979  C  CD1 . ILE A  1 282 ? -91.180  -38.521 97.621  1.00 30.52  ? 281 ILE A CD1 1 
ATOM   1980  N  N   . ILE A  1 283 ? -87.717  -42.320 98.218  1.00 29.60  ? 282 ILE A N   1 
ATOM   1981  C  CA  . ILE A  1 283 ? -86.363  -42.365 97.682  1.00 30.39  ? 282 ILE A CA  1 
ATOM   1982  C  C   . ILE A  1 283 ? -86.239  -43.665 96.889  1.00 30.93  ? 282 ILE A C   1 
ATOM   1983  O  O   . ILE A  1 283 ? -86.585  -44.738 97.391  1.00 29.25  ? 282 ILE A O   1 
ATOM   1984  C  CB  . ILE A  1 283 ? -85.289  -42.275 98.792  1.00 31.22  ? 282 ILE A CB  1 
ATOM   1985  C  CG1 . ILE A  1 283 ? -85.408  -41.007 99.639  1.00 33.05  ? 282 ILE A CG1 1 
ATOM   1986  C  CG2 . ILE A  1 283 ? -83.890  -42.431 98.212  1.00 29.07  ? 282 ILE A CG2 1 
ATOM   1987  C  CD1 . ILE A  1 283 ? -85.048  -39.750 98.926  1.00 35.38  ? 282 ILE A CD1 1 
ATOM   1988  N  N   . GLY A  1 284 ? -85.766  -43.553 95.642  1.00 28.61  ? 283 GLY A N   1 
ATOM   1989  C  CA  . GLY A  1 284 ? -85.522  -44.705 94.796  1.00 27.97  ? 283 GLY A CA  1 
ATOM   1990  C  C   . GLY A  1 284 ? -86.788  -45.193 94.096  1.00 26.82  ? 283 GLY A C   1 
ATOM   1991  O  O   . GLY A  1 284 ? -86.771  -46.239 93.460  1.00 27.90  ? 283 GLY A O   1 
ATOM   1992  N  N   . ARG A  1 285 ? -87.867  -44.413 94.197  1.00 24.71  ? 284 ARG A N   1 
ATOM   1993  C  CA  . ARG A  1 285 ? -89.126  -44.661 93.488  1.00 26.67  ? 284 ARG A CA  1 
ATOM   1994  C  C   . ARG A  1 285 ? -89.243  -43.624 92.359  1.00 25.77  ? 284 ARG A C   1 
ATOM   1995  O  O   . ARG A  1 285 ? -88.323  -42.850 92.187  1.00 27.46  ? 284 ARG A O   1 
ATOM   1996  C  CB  . ARG A  1 285 ? -90.271  -44.645 94.503  1.00 28.30  ? 284 ARG A CB  1 
ATOM   1997  C  CG  . ARG A  1 285 ? -90.074  -45.683 95.601  1.00 28.73  ? 284 ARG A CG  1 
ATOM   1998  C  CD  . ARG A  1 285 ? -91.326  -45.956 96.403  1.00 33.42  ? 284 ARG A CD  1 
ATOM   1999  N  NE  . ARG A  1 285 ? -91.002  -46.766 97.574  1.00 33.42  ? 284 ARG A NE  1 
ATOM   2000  C  CZ  . ARG A  1 285 ? -90.986  -48.092 97.601  1.00 32.77  ? 284 ARG A CZ  1 
ATOM   2001  N  NH1 . ARG A  1 285 ? -90.667  -48.719 98.724  1.00 34.15  ? 284 ARG A NH1 1 
ATOM   2002  N  NH2 . ARG A  1 285 ? -91.339  -48.784 96.538  1.00 28.77  ? 284 ARG A NH2 1 
ATOM   2003  N  N   . THR A  1 286 ? -90.308  -43.674 91.549  1.00 25.46  ? 285 THR A N   1 
ATOM   2004  C  CA  . THR A  1 286 ? -90.402  -42.830 90.351  1.00 25.91  ? 285 THR A CA  1 
ATOM   2005  C  C   . THR A  1 286 ? -91.498  -41.793 90.548  1.00 25.50  ? 285 THR A C   1 
ATOM   2006  O  O   . THR A  1 286 ? -92.592  -42.110 90.967  1.00 28.10  ? 285 THR A O   1 
ATOM   2007  C  CB  . THR A  1 286 ? -90.652  -43.651 89.082  1.00 28.00  ? 285 THR A CB  1 
ATOM   2008  O  OG1 . THR A  1 286 ? -89.522  -44.497 88.888  1.00 27.99  ? 285 THR A OG1 1 
ATOM   2009  C  CG2 . THR A  1 286 ? -90.867  -42.805 87.843  1.00 28.64  ? 285 THR A CG2 1 
ATOM   2010  N  N   . LEU A  1 287 ? -91.176  -40.540 90.238  1.00 23.82  ? 286 LEU A N   1 
ATOM   2011  C  CA  . LEU A  1 287 ? -92.165  -39.508 90.126  1.00 23.09  ? 286 LEU A CA  1 
ATOM   2012  C  C   . LEU A  1 287 ? -92.644  -39.453 88.662  1.00 24.89  ? 286 LEU A C   1 
ATOM   2013  O  O   . LEU A  1 287 ? -91.829  -39.462 87.747  1.00 23.58  ? 286 LEU A O   1 
ATOM   2014  C  CB  . LEU A  1 287 ? -91.516  -38.197 90.580  1.00 22.97  ? 286 LEU A CB  1 
ATOM   2015  C  CG  . LEU A  1 287 ? -92.433  -36.990 90.533  1.00 23.91  ? 286 LEU A CG  1 
ATOM   2016  C  CD1 . LEU A  1 287 ? -93.602  -37.149 91.507  1.00 25.24  ? 286 LEU A CD1 1 
ATOM   2017  C  CD2 . LEU A  1 287 ? -91.666  -35.702 90.791  1.00 24.26  ? 286 LEU A CD2 1 
ATOM   2018  N  N   . VAL A  1 288 ? -93.961  -39.388 88.447  1.00 23.94  ? 287 VAL A N   1 
ATOM   2019  C  CA  . VAL A  1 288 ? -94.560  -39.403 87.109  1.00 25.11  ? 287 VAL A CA  1 
ATOM   2020  C  C   . VAL A  1 288 ? -95.477  -38.199 86.961  1.00 24.80  ? 287 VAL A C   1 
ATOM   2021  O  O   . VAL A  1 288 ? -96.295  -37.933 87.833  1.00 25.51  ? 287 VAL A O   1 
ATOM   2022  C  CB  . VAL A  1 288 ? -95.352  -40.702 86.855  1.00 26.38  ? 287 VAL A CB  1 
ATOM   2023  C  CG1 . VAL A  1 288 ? -96.027  -40.710 85.482  1.00 27.24  ? 287 VAL A CG1 1 
ATOM   2024  C  CG2 . VAL A  1 288 ? -94.471  -41.916 87.032  1.00 25.82  ? 287 VAL A CG2 1 
ATOM   2025  N  N   . VAL A  1 289 ? -95.369  -37.498 85.822  1.00 24.24  ? 288 VAL A N   1 
ATOM   2026  C  CA  . VAL A  1 289 ? -96.380  -36.547 85.447  1.00 23.50  ? 288 VAL A CA  1 
ATOM   2027  C  C   . VAL A  1 289 ? -97.175  -37.107 84.256  1.00 25.00  ? 288 VAL A C   1 
ATOM   2028  O  O   . VAL A  1 289 ? -96.591  -37.672 83.330  1.00 22.53  ? 288 VAL A O   1 
ATOM   2029  C  CB  . VAL A  1 289 ? -95.789  -35.153 85.159  1.00 24.57  ? 288 VAL A CB  1 
ATOM   2030  C  CG1 . VAL A  1 289 ? -94.867  -35.134 83.944  1.00 25.32  ? 288 VAL A CG1 1 
ATOM   2031  C  CG2 . VAL A  1 289 ? -96.892  -34.127 85.027  1.00 23.24  ? 288 VAL A CG2 1 
ATOM   2032  N  N   . HIS A  1 290 ? -98.493  -36.877 84.288  1.00 25.32  ? 289 HIS A N   1 
ATOM   2033  C  CA  . HIS A  1 290 ? -99.459  -37.553 83.429  1.00 27.46  ? 289 HIS A CA  1 
ATOM   2034  C  C   . HIS A  1 290 ? -100.056 -36.627 82.356  1.00 26.64  ? 289 HIS A C   1 
ATOM   2035  O  O   . HIS A  1 290 ? -100.081 -35.404 82.466  1.00 25.42  ? 289 HIS A O   1 
ATOM   2036  C  CB  . HIS A  1 290 ? -100.596 -38.137 84.278  1.00 26.16  ? 289 HIS A CB  1 
ATOM   2037  C  CG  . HIS A  1 290 ? -100.222 -39.401 84.959  1.00 26.83  ? 289 HIS A CG  1 
ATOM   2038  N  ND1 . HIS A  1 290 ? -100.291 -40.625 84.325  1.00 25.98  ? 289 HIS A ND1 1 
ATOM   2039  C  CD2 . HIS A  1 290 ? -99.762  -39.632 86.210  1.00 26.41  ? 289 HIS A CD2 1 
ATOM   2040  C  CE1 . HIS A  1 290 ? -99.887  -41.565 85.174  1.00 27.24  ? 289 HIS A CE1 1 
ATOM   2041  N  NE2 . HIS A  1 290 ? -99.596  -40.984 86.347  1.00 29.37  ? 289 HIS A NE2 1 
ATOM   2042  N  N   . GLU A  1 291 ? -100.623 -37.285 81.345  1.00 30.46  ? 290 GLU A N   1 
ATOM   2043  C  CA  . GLU A  1 291 ? -101.273 -36.692 80.171  1.00 33.22  ? 290 GLU A CA  1 
ATOM   2044  C  C   . GLU A  1 291 ? -102.486 -35.850 80.573  1.00 30.58  ? 290 GLU A C   1 
ATOM   2045  O  O   . GLU A  1 291 ? -102.691 -34.772 80.040  1.00 29.46  ? 290 GLU A O   1 
ATOM   2046  C  CB  . GLU A  1 291 ? -101.687 -37.856 79.261  1.00 38.16  ? 290 GLU A CB  1 
ATOM   2047  C  CG  . GLU A  1 291 ? -102.579 -37.486 78.093  1.00 42.10  ? 290 GLU A CG  1 
ATOM   2048  C  CD  . GLU A  1 291 ? -103.178 -38.693 77.365  1.00 47.58  ? 290 GLU A CD  1 
ATOM   2049  O  OE1 . GLU A  1 291 ? -103.626 -38.492 76.216  1.00 54.26  ? 290 GLU A OE1 1 
ATOM   2050  O  OE2 . GLU A  1 291 ? -103.197 -39.843 77.938  1.00 39.54  ? 290 GLU A OE2 1 
ATOM   2051  N  N   . LYS A  1 292 ? -103.294 -36.368 81.501  1.00 30.07  ? 291 LYS A N   1 
ATOM   2052  C  CA  . LYS A  1 292 ? -104.618 -35.830 81.807  1.00 32.25  ? 291 LYS A CA  1 
ATOM   2053  C  C   . LYS A  1 292 ? -104.717 -35.492 83.296  1.00 28.74  ? 291 LYS A C   1 
ATOM   2054  O  O   . LYS A  1 292 ? -103.888 -35.919 84.095  1.00 27.46  ? 291 LYS A O   1 
ATOM   2055  C  CB  . LYS A  1 292 ? -105.712 -36.856 81.465  1.00 38.01  ? 291 LYS A CB  1 
ATOM   2056  C  CG  . LYS A  1 292 ? -105.622 -37.438 80.059  1.00 45.19  ? 291 LYS A CG  1 
ATOM   2057  C  CD  . LYS A  1 292 ? -106.886 -38.108 79.550  1.00 48.74  ? 291 LYS A CD  1 
ATOM   2058  C  CE  . LYS A  1 292 ? -107.398 -39.187 80.475  1.00 56.73  ? 291 LYS A CE  1 
ATOM   2059  N  NZ  . LYS A  1 292 ? -108.466 -40.009 79.854  1.00 64.60  ? 291 LYS A NZ  1 
ATOM   2060  N  N   . ALA A  1 293 ? -105.770 -34.751 83.636  1.00 26.77  ? 292 ALA A N   1 
ATOM   2061  C  CA  . ALA A  1 293 ? -106.147 -34.459 85.015  1.00 30.76  ? 292 ALA A CA  1 
ATOM   2062  C  C   . ALA A  1 293 ? -106.413 -35.756 85.802  1.00 30.40  ? 292 ALA A C   1 
ATOM   2063  O  O   . ALA A  1 293 ? -106.933 -36.737 85.281  1.00 28.40  ? 292 ALA A O   1 
ATOM   2064  C  CB  . ALA A  1 293 ? -107.359 -33.566 85.006  1.00 30.63  ? 292 ALA A CB  1 
ATOM   2065  N  N   . ASP A  1 294 ? -105.980 -35.752 87.063  1.00 29.36  ? 293 ASP A N   1 
ATOM   2066  C  CA  . ASP A  1 294 ? -106.281 -36.778 88.026  1.00 30.30  ? 293 ASP A CA  1 
ATOM   2067  C  C   . ASP A  1 294 ? -107.670 -36.435 88.588  1.00 29.08  ? 293 ASP A C   1 
ATOM   2068  O  O   . ASP A  1 294 ? -107.874 -35.321 89.065  1.00 27.72  ? 293 ASP A O   1 
ATOM   2069  C  CB  . ASP A  1 294 ? -105.163 -36.834 89.075  1.00 29.84  ? 293 ASP A CB  1 
ATOM   2070  C  CG  . ASP A  1 294 ? -105.282 -37.905 90.152  1.00 31.41  ? 293 ASP A CG  1 
ATOM   2071  O  OD1 . ASP A  1 294 ? -106.388 -38.424 90.367  1.00 31.20  ? 293 ASP A OD1 1 
ATOM   2072  O  OD2 . ASP A  1 294 ? -104.252 -38.212 90.780  1.00 34.89  ? 293 ASP A OD2 1 
ATOM   2073  N  N   . ASP A  1 295 ? -108.613 -37.390 88.524  1.00 28.43  ? 294 ASP A N   1 
ATOM   2074  C  CA  . ASP A  1 295 ? -109.987 -37.181 89.016  1.00 30.68  ? 294 ASP A CA  1 
ATOM   2075  C  C   . ASP A  1 295 ? -110.060 -37.390 90.540  1.00 30.06  ? 294 ASP A C   1 
ATOM   2076  O  O   . ASP A  1 295 ? -111.138 -37.245 91.149  1.00 31.69  ? 294 ASP A O   1 
ATOM   2077  C  CB  . ASP A  1 295 ? -110.993 -38.035 88.237  1.00 30.72  ? 294 ASP A CB  1 
ATOM   2078  C  CG  . ASP A  1 295 ? -110.898 -39.536 88.449  1.00 31.91  ? 294 ASP A CG  1 
ATOM   2079  O  OD1 . ASP A  1 295 ? -111.393 -40.275 87.553  1.00 30.41  ? 294 ASP A OD1 1 
ATOM   2080  O  OD2 . ASP A  1 295 ? -110.302 -39.962 89.467  1.00 30.03  ? 294 ASP A OD2 1 
ATOM   2081  N  N   . LEU A  1 296 ? -108.915 -37.696 91.148  1.00 28.83  ? 295 LEU A N   1 
ATOM   2082  C  CA  . LEU A  1 296 ? -108.710 -37.775 92.598  1.00 29.43  ? 295 LEU A CA  1 
ATOM   2083  C  C   . LEU A  1 296 ? -109.598 -38.886 93.178  1.00 29.87  ? 295 LEU A C   1 
ATOM   2084  O  O   . LEU A  1 296 ? -109.995 -38.854 94.336  1.00 29.70  ? 295 LEU A O   1 
ATOM   2085  C  CB  . LEU A  1 296 ? -108.980 -36.412 93.247  1.00 29.92  ? 295 LEU A CB  1 
ATOM   2086  C  CG  . LEU A  1 296 ? -108.248 -35.213 92.622  1.00 30.77  ? 295 LEU A CG  1 
ATOM   2087  C  CD1 . LEU A  1 296 ? -108.619 -33.930 93.335  1.00 31.45  ? 295 LEU A CD1 1 
ATOM   2088  C  CD2 . LEU A  1 296 ? -106.745 -35.402 92.650  1.00 28.85  ? 295 LEU A CD2 1 
ATOM   2089  N  N   . GLY A  1 297 ? -109.854 -39.893 92.350  1.00 32.33  ? 296 GLY A N   1 
ATOM   2090  C  CA  . GLY A  1 297 ? -110.595 -41.071 92.747  1.00 33.69  ? 296 GLY A CA  1 
ATOM   2091  C  C   . GLY A  1 297 ? -112.095 -40.849 92.791  1.00 33.55  ? 296 GLY A C   1 
ATOM   2092  O  O   . GLY A  1 297 ? -112.793 -41.695 93.350  1.00 34.97  ? 296 GLY A O   1 
ATOM   2093  N  N   . LYS A  1 298 ? -112.583 -39.770 92.159  1.00 30.75  ? 297 LYS A N   1 
ATOM   2094  C  CA  . LYS A  1 298 ? -113.993 -39.408 92.155  1.00 31.66  ? 297 LYS A CA  1 
ATOM   2095  C  C   . LYS A  1 298 ? -114.673 -39.662 90.803  1.00 29.61  ? 297 LYS A C   1 
ATOM   2096  O  O   . LYS A  1 298 ? -115.747 -39.121 90.549  1.00 30.88  ? 297 LYS A O   1 
ATOM   2097  C  CB  . LYS A  1 298 ? -114.119 -37.937 92.534  1.00 34.03  ? 297 LYS A CB  1 
ATOM   2098  C  CG  . LYS A  1 298 ? -113.516 -37.621 93.888  1.00 36.02  ? 297 LYS A CG  1 
ATOM   2099  C  CD  . LYS A  1 298 ? -113.848 -36.239 94.340  1.00 45.59  ? 297 LYS A CD  1 
ATOM   2100  C  CE  . LYS A  1 298 ? -113.274 -35.917 95.699  1.00 55.77  ? 297 LYS A CE  1 
ATOM   2101  N  NZ  . LYS A  1 298 ? -113.939 -34.725 96.272  1.00 66.90  ? 297 LYS A NZ  1 
ATOM   2102  N  N   . GLY A  1 299 ? -114.067 -40.496 89.961  1.00 28.66  ? 298 GLY A N   1 
ATOM   2103  C  CA  . GLY A  1 299 ? -114.562 -40.737 88.618  1.00 31.45  ? 298 GLY A CA  1 
ATOM   2104  C  C   . GLY A  1 299 ? -115.607 -41.851 88.513  1.00 30.24  ? 298 GLY A C   1 
ATOM   2105  O  O   . GLY A  1 299 ? -116.183 -42.040 87.438  1.00 27.82  ? 298 GLY A O   1 
ATOM   2106  N  N   . GLY A  1 300 ? -115.781 -42.641 89.579  1.00 30.08  ? 299 GLY A N   1 
ATOM   2107  C  CA  . GLY A  1 300 ? -116.850 -43.651 89.645  1.00 30.07  ? 299 GLY A CA  1 
ATOM   2108  C  C   . GLY A  1 300 ? -116.564 -44.908 88.850  1.00 30.16  ? 299 GLY A C   1 
ATOM   2109  O  O   . GLY A  1 300 ? -117.388 -45.827 88.833  1.00 33.09  ? 299 GLY A O   1 
ATOM   2110  N  N   . ASN A  1 301 ? -115.420 -44.984 88.163  1.00 31.68  ? 300 ASN A N   1 
ATOM   2111  C  CA  . ASN A  1 301 ? -115.102 -46.183 87.380  1.00 31.20  ? 300 ASN A CA  1 
ATOM   2112  C  C   . ASN A  1 301 ? -113.911 -46.856 88.035  1.00 29.44  ? 300 ASN A C   1 
ATOM   2113  O  O   . ASN A  1 301 ? -113.284 -46.295 88.907  1.00 30.36  ? 300 ASN A O   1 
ATOM   2114  C  CB  . ASN A  1 301 ? -114.895 -45.932 85.876  1.00 32.62  ? 300 ASN A CB  1 
ATOM   2115  C  CG  . ASN A  1 301 ? -113.740 -45.002 85.548  1.00 36.87  ? 300 ASN A CG  1 
ATOM   2116  O  OD1 . ASN A  1 301 ? -113.117 -44.430 86.448  1.00 32.31  ? 300 ASN A OD1 1 
ATOM   2117  N  ND2 . ASN A  1 301 ? -113.442 -44.866 84.263  1.00 37.09  ? 300 ASN A ND2 1 
ATOM   2118  N  N   . GLU A  1 302 ? -113.627 -48.076 87.600  1.00 31.39  ? 301 GLU A N   1 
ATOM   2119  C  CA  . GLU A  1 302 ? -112.560 -48.860 88.174  1.00 35.91  ? 301 GLU A CA  1 
ATOM   2120  C  C   . GLU A  1 302 ? -111.217 -48.116 88.041  1.00 35.65  ? 301 GLU A C   1 
ATOM   2121  O  O   . GLU A  1 302 ? -110.405 -48.130 88.967  1.00 34.60  ? 301 GLU A O   1 
ATOM   2122  C  CB  . GLU A  1 302 ? -112.466 -50.217 87.483  1.00 40.33  ? 301 GLU A CB  1 
ATOM   2123  C  CG  . GLU A  1 302 ? -111.578 -51.192 88.238  1.00 51.91  ? 301 GLU A CG  1 
ATOM   2124  C  CD  . GLU A  1 302 ? -111.527 -52.604 87.668  1.00 61.78  ? 301 GLU A CD  1 
ATOM   2125  O  OE1 . GLU A  1 302 ? -112.320 -52.893 86.724  1.00 65.55  ? 301 GLU A OE1 1 
ATOM   2126  O  OE2 . GLU A  1 302 ? -110.691 -53.413 88.166  1.00 67.90  ? 301 GLU A OE2 1 
ATOM   2127  N  N   . GLU A  1 303 ? -110.990 -47.503 86.870  1.00 36.28  ? 302 GLU A N   1 
ATOM   2128  C  CA  . GLU A  1 303 ? -109.731 -46.797 86.552  1.00 37.16  ? 302 GLU A CA  1 
ATOM   2129  C  C   . GLU A  1 303 ? -109.507 -45.647 87.547  1.00 32.62  ? 302 GLU A C   1 
ATOM   2130  O  O   . GLU A  1 303 ? -108.385 -45.428 87.990  1.00 33.87  ? 302 GLU A O   1 
ATOM   2131  C  CB  . GLU A  1 303 ? -109.738 -46.334 85.090  1.00 39.03  ? 302 GLU A CB  1 
ATOM   2132  C  CG  . GLU A  1 303 ? -108.372 -45.908 84.575  1.00 45.46  ? 302 GLU A CG  1 
ATOM   2133  C  CD  . GLU A  1 303 ? -107.327 -47.002 84.681  1.00 48.09  ? 302 GLU A CD  1 
ATOM   2134  O  OE1 . GLU A  1 303 ? -107.566 -48.097 84.140  1.00 51.20  ? 302 GLU A OE1 1 
ATOM   2135  O  OE2 . GLU A  1 303 ? -106.302 -46.774 85.345  1.00 54.53  ? 302 GLU A OE2 1 
ATOM   2136  N  N   . SER A  1 304 ? -110.581 -44.956 87.939  1.00 29.70  ? 303 SER A N   1 
ATOM   2137  C  CA  . SER A  1 304 ? -110.509 -43.856 88.891  1.00 30.35  ? 303 SER A CA  1 
ATOM   2138  C  C   . SER A  1 304 ? -109.853 -44.313 90.192  1.00 32.62  ? 303 SER A C   1 
ATOM   2139  O  O   . SER A  1 304 ? -109.039 -43.570 90.750  1.00 29.12  ? 303 SER A O   1 
ATOM   2140  C  CB  . SER A  1 304 ? -111.852 -43.246 89.144  1.00 29.72  ? 303 SER A CB  1 
ATOM   2141  O  OG  . SER A  1 304 ? -111.774 -42.175 90.079  1.00 30.85  ? 303 SER A OG  1 
ATOM   2142  N  N   . THR A  1 305 ? -110.199 -45.529 90.643  1.00 31.83  ? 304 THR A N   1 
ATOM   2143  C  CA  . THR A  1 305 ? -109.759 -46.096 91.933  1.00 32.21  ? 304 THR A CA  1 
ATOM   2144  C  C   . THR A  1 305 ? -108.303 -46.575 91.856  1.00 32.41  ? 304 THR A C   1 
ATOM   2145  O  O   . THR A  1 305 ? -107.711 -46.932 92.871  1.00 31.44  ? 304 THR A O   1 
ATOM   2146  C  CB  . THR A  1 305 ? -110.660 -47.282 92.345  1.00 35.92  ? 304 THR A CB  1 
ATOM   2147  O  OG1 . THR A  1 305 ? -110.481 -48.365 91.429  1.00 37.44  ? 304 THR A OG1 1 
ATOM   2148  C  CG2 . THR A  1 305 ? -112.136 -46.960 92.340  1.00 36.72  ? 304 THR A CG2 1 
ATOM   2149  N  N   . LYS A  1 306 ? -107.741 -46.638 90.644  1.00 32.25  ? 305 LYS A N   1 
ATOM   2150  C  CA  . LYS A  1 306 ? -106.351 -47.090 90.429  1.00 35.40  ? 305 LYS A CA  1 
ATOM   2151  C  C   . LYS A  1 306 ? -105.416 -45.914 90.084  1.00 33.89  ? 305 LYS A C   1 
ATOM   2152  O  O   . LYS A  1 306 ? -104.349 -45.781 90.660  1.00 32.11  ? 305 LYS A O   1 
ATOM   2153  C  CB  . LYS A  1 306 ? -106.318 -48.126 89.304  1.00 41.81  ? 305 LYS A CB  1 
ATOM   2154  C  CG  . LYS A  1 306 ? -107.032 -49.440 89.592  1.00 46.88  ? 305 LYS A CG  1 
ATOM   2155  C  CD  . LYS A  1 306 ? -107.145 -50.308 88.354  1.00 56.05  ? 305 LYS A CD  1 
ATOM   2156  C  CE  . LYS A  1 306 ? -107.788 -51.654 88.609  1.00 65.85  ? 305 LYS A CE  1 
ATOM   2157  N  NZ  . LYS A  1 306 ? -106.847 -52.598 89.261  1.00 72.04  ? 305 LYS A NZ  1 
ATOM   2158  N  N   . THR A  1 307 ? -105.811 -45.095 89.108  1.00 32.96  ? 306 THR A N   1 
ATOM   2159  C  CA  . THR A  1 307 ? -104.919 -44.121 88.507  1.00 32.16  ? 306 THR A CA  1 
ATOM   2160  C  C   . THR A  1 307 ? -105.553 -42.739 88.439  1.00 32.34  ? 306 THR A C   1 
ATOM   2161  O  O   . THR A  1 307 ? -104.902 -41.796 87.987  1.00 32.49  ? 306 THR A O   1 
ATOM   2162  C  CB  . THR A  1 307 ? -104.520 -44.542 87.089  1.00 32.52  ? 306 THR A CB  1 
ATOM   2163  O  OG1 . THR A  1 307 ? -105.685 -44.444 86.271  1.00 30.53  ? 306 THR A OG1 1 
ATOM   2164  C  CG2 . THR A  1 307 ? -103.920 -45.927 87.037  1.00 34.45  ? 306 THR A CG2 1 
ATOM   2165  N  N   . GLY A  1 308 ? -106.809 -42.602 88.872  1.00 26.42  ? 307 GLY A N   1 
ATOM   2166  C  CA  . GLY A  1 308 ? -107.491 -41.333 88.733  1.00 26.95  ? 307 GLY A CA  1 
ATOM   2167  C  C   . GLY A  1 308 ? -107.812 -40.957 87.287  1.00 25.86  ? 307 GLY A C   1 
ATOM   2168  O  O   . GLY A  1 308 ? -108.194 -39.783 87.030  1.00 27.84  ? 307 GLY A O   1 
ATOM   2169  N  N   . ASN A  1 309 ? -107.752 -41.921 86.351  1.00 25.55  ? 308 ASN A N   1 
ATOM   2170  C  CA  . ASN A  1 309 ? -108.028 -41.637 84.913  1.00 27.26  ? 308 ASN A CA  1 
ATOM   2171  C  C   . ASN A  1 309 ? -107.038 -40.575 84.368  1.00 28.50  ? 308 ASN A C   1 
ATOM   2172  O  O   . ASN A  1 309 ? -107.386 -39.789 83.461  1.00 29.56  ? 308 ASN A O   1 
ATOM   2173  C  CB  . ASN A  1 309 ? -109.473 -41.177 84.680  1.00 29.45  ? 308 ASN A CB  1 
ATOM   2174  C  CG  . ASN A  1 309 ? -110.482 -42.305 84.833  1.00 32.60  ? 308 ASN A CG  1 
ATOM   2175  O  OD1 . ASN A  1 309 ? -110.437 -43.268 84.082  1.00 34.88  ? 308 ASN A OD1 1 
ATOM   2176  N  ND2 . ASN A  1 309 ? -111.339 -42.229 85.842  1.00 31.29  ? 308 ASN A ND2 1 
ATOM   2177  N  N   . ALA A  1 310 ? -105.818 -40.530 84.922  1.00 25.04  ? 309 ALA A N   1 
ATOM   2178  C  CA  . ALA A  1 310 ? -104.805 -39.488 84.553  1.00 28.30  ? 309 ALA A CA  1 
ATOM   2179  C  C   . ALA A  1 310 ? -104.117 -39.807 83.206  1.00 27.76  ? 309 ALA A C   1 
ATOM   2180  O  O   . ALA A  1 310 ? -103.380 -38.975 82.662  1.00 29.65  ? 309 ALA A O   1 
ATOM   2181  C  CB  . ALA A  1 310 ? -103.793 -39.356 85.674  1.00 28.31  ? 309 ALA A CB  1 
ATOM   2182  N  N   . GLY A  1 311 ? -104.331 -41.011 82.668  1.00 28.01  ? 310 GLY A N   1 
ATOM   2183  C  CA  . GLY A  1 311 ? -103.877 -41.346 81.335  1.00 30.36  ? 310 GLY A CA  1 
ATOM   2184  C  C   . GLY A  1 311 ? -102.374 -41.603 81.294  1.00 30.12  ? 310 GLY A C   1 
ATOM   2185  O  O   . GLY A  1 311 ? -101.781 -42.004 82.284  1.00 30.13  ? 310 GLY A O   1 
ATOM   2186  N  N   . SER A  1 312 ? -101.743 -41.340 80.146  1.00 28.85  ? 311 SER A N   1 
ATOM   2187  C  CA  . SER A  1 312 ? -100.406 -41.843 79.915  1.00 30.87  ? 311 SER A CA  1 
ATOM   2188  C  C   . SER A  1 312 ? -99.363  -41.021 80.706  1.00 26.48  ? 311 SER A C   1 
ATOM   2189  O  O   . SER A  1 312 ? -99.620  -39.944 81.208  1.00 23.83  ? 311 SER A O   1 
ATOM   2190  C  CB  . SER A  1 312 ? -100.097 -41.926 78.436  1.00 34.84  ? 311 SER A CB  1 
ATOM   2191  O  OG  A SER A  1 312 ? -100.324 -40.683 77.813  0.60 41.58  ? 311 SER A OG  1 
ATOM   2192  O  OG  B SER A  1 312 ? -100.323 -40.680 77.811  0.40 39.20  ? 311 SER A OG  1 
ATOM   2193  N  N   . ARG A  1 313 ? -98.171  -41.596 80.808  1.00 25.96  ? 312 ARG A N   1 
ATOM   2194  C  CA  . ARG A  1 313 ? -97.075  -41.078 81.560  1.00 28.17  ? 312 ARG A CA  1 
ATOM   2195  C  C   . ARG A  1 313 ? -96.195  -40.266 80.605  1.00 28.28  ? 312 ARG A C   1 
ATOM   2196  O  O   . ARG A  1 313 ? -95.516  -40.826 79.769  1.00 28.58  ? 312 ARG A O   1 
ATOM   2197  C  CB  . ARG A  1 313 ? -96.334  -42.265 82.176  1.00 27.63  ? 312 ARG A CB  1 
ATOM   2198  C  CG  . ARG A  1 313 ? -97.254  -43.230 82.916  1.00 28.53  ? 312 ARG A CG  1 
ATOM   2199  C  CD  . ARG A  1 313 ? -96.567  -44.472 83.437  1.00 28.29  ? 312 ARG A CD  1 
ATOM   2200  N  NE  . ARG A  1 313 ? -97.524  -45.312 84.144  1.00 29.82  ? 312 ARG A NE  1 
ATOM   2201  C  CZ  . ARG A  1 313 ? -97.216  -46.272 85.009  1.00 29.63  ? 312 ARG A CZ  1 
ATOM   2202  N  NH1 . ARG A  1 313 ? -98.177  -46.973 85.591  1.00 29.63  ? 312 ARG A NH1 1 
ATOM   2203  N  NH2 . ARG A  1 313 ? -95.954  -46.541 85.280  1.00 29.78  ? 312 ARG A NH2 1 
ATOM   2204  N  N   . LEU A  1 314 ? -96.237  -38.944 80.737  1.00 27.12  ? 313 LEU A N   1 
ATOM   2205  C  CA  . LEU A  1 314 ? -95.534  -38.055 79.817  1.00 27.99  ? 313 LEU A CA  1 
ATOM   2206  C  C   . LEU A  1 314 ? -94.052  -37.961 80.160  1.00 28.93  ? 313 LEU A C   1 
ATOM   2207  O  O   . LEU A  1 314 ? -93.229  -37.762 79.278  1.00 27.33  ? 313 LEU A O   1 
ATOM   2208  C  CB  . LEU A  1 314 ? -96.168  -36.664 79.876  1.00 28.70  ? 313 LEU A CB  1 
ATOM   2209  C  CG  . LEU A  1 314 ? -97.621  -36.605 79.426  1.00 31.05  ? 313 LEU A CG  1 
ATOM   2210  C  CD1 . LEU A  1 314 ? -98.101  -35.168 79.320  1.00 32.09  ? 313 LEU A CD1 1 
ATOM   2211  C  CD2 . LEU A  1 314 ? -97.830  -37.335 78.117  1.00 33.43  ? 313 LEU A CD2 1 
ATOM   2212  N  N   . ALA A  1 315 ? -93.724  -37.989 81.455  1.00 25.57  ? 314 ALA A N   1 
ATOM   2213  C  CA  . ALA A  1 315 ? -92.352  -37.898 81.859  1.00 26.16  ? 314 ALA A CA  1 
ATOM   2214  C  C   . ALA A  1 315 ? -92.229  -38.438 83.282  1.00 26.72  ? 314 ALA A C   1 
ATOM   2215  O  O   . ALA A  1 315 ? -93.191  -38.414 84.059  1.00 23.39  ? 314 ALA A O   1 
ATOM   2216  C  CB  . ALA A  1 315 ? -91.868  -36.468 81.790  1.00 25.37  ? 314 ALA A CB  1 
ATOM   2217  N  N   . CYS A  1 316 ? -91.030  -38.910 83.589  1.00 25.77  ? 315 CYS A N   1 
ATOM   2218  C  CA  . CYS A  1 316 ? -90.771  -39.461 84.872  1.00 28.35  ? 315 CYS A CA  1 
ATOM   2219  C  C   . CYS A  1 316 ? -89.278  -39.407 85.174  1.00 27.97  ? 315 CYS A C   1 
ATOM   2220  O  O   . CYS A  1 316 ? -88.436  -39.151 84.279  1.00 24.01  ? 315 CYS A O   1 
ATOM   2221  C  CB  . CYS A  1 316 ? -91.255  -40.906 84.940  1.00 30.08  ? 315 CYS A CB  1 
ATOM   2222  S  SG  . CYS A  1 316 ? -90.460  -42.013 83.754  1.00 32.76  ? 315 CYS A SG  1 
ATOM   2223  N  N   . GLY A  1 317 ? -88.965  -39.688 86.442  1.00 25.54  ? 316 GLY A N   1 
ATOM   2224  C  CA  . GLY A  1 317 ? -87.603  -39.906 86.867  1.00 27.28  ? 316 GLY A CA  1 
ATOM   2225  C  C   . GLY A  1 317 ? -87.549  -40.531 88.256  1.00 27.28  ? 316 GLY A C   1 
ATOM   2226  O  O   . GLY A  1 317 ? -88.530  -40.490 89.032  1.00 25.46  ? 316 GLY A O   1 
ATOM   2227  N  N   . VAL A  1 318 ? -86.373  -41.055 88.571  1.00 25.01  ? 317 VAL A N   1 
ATOM   2228  C  CA  . VAL A  1 318 ? -86.106  -41.703 89.826  1.00 27.32  ? 317 VAL A CA  1 
ATOM   2229  C  C   . VAL A  1 318 ? -85.747  -40.636 90.864  1.00 26.44  ? 317 VAL A C   1 
ATOM   2230  O  O   . VAL A  1 318 ? -85.001  -39.703 90.589  1.00 27.88  ? 317 VAL A O   1 
ATOM   2231  C  CB  . VAL A  1 318 ? -85.005  -42.751 89.658  1.00 27.96  ? 317 VAL A CB  1 
ATOM   2232  C  CG1 . VAL A  1 318 ? -84.718  -43.477 90.974  1.00 29.46  ? 317 VAL A CG1 1 
ATOM   2233  C  CG2 . VAL A  1 318 ? -85.350  -43.739 88.556  1.00 28.46  ? 317 VAL A CG2 1 
ATOM   2234  N  N   . ILE A  1 319 ? -86.357  -40.756 92.044  1.00 26.94  ? 318 ILE A N   1 
ATOM   2235  C  CA  . ILE A  1 319 ? -86.207  -39.794 93.117  1.00 26.32  ? 318 ILE A CA  1 
ATOM   2236  C  C   . ILE A  1 319 ? -84.925  -40.156 93.869  1.00 29.17  ? 318 ILE A C   1 
ATOM   2237  O  O   . ILE A  1 319 ? -84.809  -41.260 94.427  1.00 29.12  ? 318 ILE A O   1 
ATOM   2238  C  CB  . ILE A  1 319 ? -87.442  -39.796 94.036  1.00 27.08  ? 318 ILE A CB  1 
ATOM   2239  C  CG1 . ILE A  1 319 ? -88.704  -39.361 93.288  1.00 27.23  ? 318 ILE A CG1 1 
ATOM   2240  C  CG2 . ILE A  1 319 ? -87.208  -38.927 95.253  1.00 27.77  ? 318 ILE A CG2 1 
ATOM   2241  C  CD1 . ILE A  1 319 ? -89.991  -39.802 93.944  1.00 26.14  ? 318 ILE A CD1 1 
ATOM   2242  N  N   . GLY A  1 320 ? -83.973  -39.220 93.854  1.00 27.32  ? 319 GLY A N   1 
ATOM   2243  C  CA  . GLY A  1 320 ? -82.644  -39.417 94.372  1.00 28.99  ? 319 GLY A CA  1 
ATOM   2244  C  C   . GLY A  1 320 ? -82.382  -38.562 95.601  1.00 26.37  ? 319 GLY A C   1 
ATOM   2245  O  O   . GLY A  1 320 ? -82.911  -37.454 95.740  1.00 26.51  ? 319 GLY A O   1 
ATOM   2246  N  N   . ILE A  1 321 ? -81.475  -39.056 96.438  1.00 27.15  ? 320 ILE A N   1 
ATOM   2247  C  CA  . ILE A  1 321 ? -80.971  -38.299 97.592  1.00 29.26  ? 320 ILE A CA  1 
ATOM   2248  C  C   . ILE A  1 321 ? -80.212  -37.068 97.083  1.00 30.01  ? 320 ILE A C   1 
ATOM   2249  O  O   . ILE A  1 321 ? -79.272  -37.191 96.300  1.00 31.13  ? 320 ILE A O   1 
ATOM   2250  C  CB  . ILE A  1 321 ? -80.075  -39.191 98.478  1.00 30.81  ? 320 ILE A CB  1 
ATOM   2251  C  CG1 . ILE A  1 321 ? -80.811  -40.455 98.937  1.00 32.97  ? 320 ILE A CG1 1 
ATOM   2252  C  CG2 . ILE A  1 321 ? -79.517  -38.382 99.651  1.00 31.79  ? 320 ILE A CG2 1 
ATOM   2253  C  CD1 . ILE A  1 321 ? -79.929  -41.526 99.574  1.00 34.47  ? 320 ILE A CD1 1 
ATOM   2254  N  N   . ALA A  1 322 ? -80.596  -35.903 97.601  1.00 30.70  ? 321 ALA A N   1 
ATOM   2255  C  CA  . ALA A  1 322 ? -79.997  -34.615 97.262  1.00 36.41  ? 321 ALA A CA  1 
ATOM   2256  C  C   . ALA A  1 322 ? -79.152  -34.028 98.403  1.00 42.45  ? 321 ALA A C   1 
ATOM   2257  O  O   . ALA A  1 322 ? -78.190  -33.338 98.138  1.00 49.94  ? 321 ALA A O   1 
ATOM   2258  C  CB  . ALA A  1 322 ? -81.089  -33.651 96.903  1.00 33.74  ? 321 ALA A CB  1 
ATOM   2259  N  N   . GLN A  1 323 ? -79.550  -34.287 99.651  1.00 54.98  ? 322 GLN A N   1 
ATOM   2260  C  CA  . GLN A  1 323 ? -79.299  -33.395 100.829 1.00 66.03  ? 322 GLN A CA  1 
ATOM   2261  C  C   . GLN A  1 323 ? -77.807  -33.194 101.093 1.00 69.43  ? 322 GLN A C   1 
ATOM   2262  O  O   . GLN A  1 323 ? -77.441  -32.221 101.751 1.00 81.41  ? 322 GLN A O   1 
ATOM   2263  C  CB  . GLN A  1 323 ? -79.966  -33.946 102.095 1.00 66.31  ? 322 GLN A CB  1 
ATOM   2264  C  CG  . GLN A  1 323 ? -79.701  -35.424 102.339 1.00 68.25  ? 322 GLN A CG  1 
ATOM   2265  C  CD  . GLN A  1 323 ? -78.301  -35.659 102.844 1.00 77.26  ? 322 GLN A CD  1 
ATOM   2266  O  OE1 . GLN A  1 323 ? -77.857  -35.014 103.794 1.00 86.64  ? 322 GLN A OE1 1 
ATOM   2267  N  NE2 . GLN A  1 323 ? -77.594  -36.582 102.207 1.00 71.74  ? 322 GLN A NE2 1 
ATOM   2268  N  N   . ALA B  1 2   ? -50.050  -2.861  34.086  1.00 60.91  ? 1   ALA C N   1 
ATOM   2269  C  CA  . ALA B  1 2   ? -51.361  -2.947  33.354  1.00 59.79  ? 1   ALA C CA  1 
ATOM   2270  C  C   . ALA B  1 2   ? -51.936  -4.371  33.425  1.00 57.86  ? 1   ALA C C   1 
ATOM   2271  O  O   . ALA B  1 2   ? -51.256  -5.311  33.826  1.00 55.39  ? 1   ALA C O   1 
ATOM   2272  C  CB  . ALA B  1 2   ? -51.179  -2.512  31.920  1.00 60.66  ? 1   ALA C CB  1 
ATOM   2273  N  N   . THR B  1 3   ? -53.189  -4.497  32.974  1.00 55.04  ? 2   THR C N   1 
ATOM   2274  C  CA  . THR B  1 3   ? -54.009  -5.715  33.040  1.00 57.90  ? 2   THR C CA  1 
ATOM   2275  C  C   . THR B  1 3   ? -54.013  -6.441  31.680  1.00 55.22  ? 2   THR C C   1 
ATOM   2276  O  O   . THR B  1 3   ? -54.199  -7.670  31.609  1.00 50.74  ? 2   THR C O   1 
ATOM   2277  C  CB  . THR B  1 3   ? -55.408  -5.317  33.534  1.00 55.03  ? 2   THR C CB  1 
ATOM   2278  O  OG1 . THR B  1 3   ? -55.770  -6.245  34.548  1.00 60.70  ? 2   THR C OG1 1 
ATOM   2279  C  CG2 . THR B  1 3   ? -56.462  -5.257  32.452  1.00 55.38  ? 2   THR C CG2 1 
ATOM   2280  N  N   . LYS B  1 4   ? -53.864  -5.664  30.602  1.00 49.40  ? 3   LYS C N   1 
ATOM   2281  C  CA  . LYS B  1 4   ? -53.712  -6.164  29.247  1.00 50.45  ? 3   LYS C CA  1 
ATOM   2282  C  C   . LYS B  1 4   ? -52.498  -5.482  28.611  1.00 46.08  ? 3   LYS C C   1 
ATOM   2283  O  O   . LYS B  1 4   ? -52.228  -4.313  28.865  1.00 46.97  ? 3   LYS C O   1 
ATOM   2284  C  CB  . LYS B  1 4   ? -54.963  -5.878  28.411  1.00 58.39  ? 3   LYS C CB  1 
ATOM   2285  C  CG  . LYS B  1 4   ? -56.255  -6.510  28.923  1.00 66.09  ? 3   LYS C CG  1 
ATOM   2286  C  CD  . LYS B  1 4   ? -57.493  -6.187  28.094  1.00 74.05  ? 3   LYS C CD  1 
ATOM   2287  C  CE  . LYS B  1 4   ? -57.340  -6.433  26.601  1.00 81.58  ? 3   LYS C CE  1 
ATOM   2288  N  NZ  . LYS B  1 4   ? -56.898  -7.815  26.284  1.00 85.17  ? 3   LYS C NZ  1 
ATOM   2289  N  N   . ALA B  1 5   ? -51.780  -6.228  27.776  1.00 41.28  ? 4   ALA C N   1 
ATOM   2290  C  CA  . ALA B  1 5   ? -50.709  -5.693  26.954  1.00 40.81  ? 4   ALA C CA  1 
ATOM   2291  C  C   . ALA B  1 5   ? -50.774  -6.354  25.578  1.00 42.40  ? 4   ALA C C   1 
ATOM   2292  O  O   . ALA B  1 5   ? -51.482  -7.356  25.389  1.00 39.76  ? 4   ALA C O   1 
ATOM   2293  C  CB  . ALA B  1 5   ? -49.368  -5.903  27.624  1.00 38.80  ? 4   ALA C CB  1 
ATOM   2294  N  N   . VAL B  1 6   ? -50.061  -5.757  24.620  1.00 38.69  ? 5   VAL C N   1 
ATOM   2295  C  CA  . VAL B  1 6   ? -50.034  -6.230  23.266  1.00 38.56  ? 5   VAL C CA  1 
ATOM   2296  C  C   . VAL B  1 6   ? -48.664  -5.904  22.660  1.00 40.93  ? 5   VAL C C   1 
ATOM   2297  O  O   . VAL B  1 6   ? -47.976  -4.957  23.058  1.00 37.74  ? 5   VAL C O   1 
ATOM   2298  C  CB  . VAL B  1 6   ? -51.194  -5.632  22.447  1.00 40.86  ? 5   VAL C CB  1 
ATOM   2299  C  CG1 . VAL B  1 6   ? -51.065  -4.128  22.254  1.00 44.03  ? 5   VAL C CG1 1 
ATOM   2300  C  CG2 . VAL B  1 6   ? -51.357  -6.325  21.104  1.00 40.34  ? 5   VAL C CG2 1 
ATOM   2301  N  N   . CYS B  1 7   ? -48.276  -6.706  21.679  1.00 38.21  ? 6   CYS C N   1 
ATOM   2302  C  CA  . CYS B  1 7   ? -47.018  -6.545  21.031  1.00 39.50  ? 6   CYS C CA  1 
ATOM   2303  C  C   . CYS B  1 7   ? -47.219  -6.831  19.548  1.00 39.12  ? 6   CYS C C   1 
ATOM   2304  O  O   . CYS B  1 7   ? -47.804  -7.855  19.182  1.00 36.82  ? 6   CYS C O   1 
ATOM   2305  C  CB  . CYS B  1 7   ? -45.974  -7.465  21.659  1.00 42.26  ? 6   CYS C CB  1 
ATOM   2306  S  SG  . CYS B  1 7   ? -44.328  -7.290  20.923  1.00 44.47  ? 6   CYS C SG  1 
ATOM   2307  N  N   . VAL B  1 8   ? -46.769  -5.897  18.708  1.00 35.74  ? 7   VAL C N   1 
ATOM   2308  C  CA  . VAL B  1 8   ? -46.735  -6.083  17.291  1.00 36.21  ? 7   VAL C CA  1 
ATOM   2309  C  C   . VAL B  1 8   ? -45.297  -6.449  16.899  1.00 40.79  ? 7   VAL C C   1 
ATOM   2310  O  O   . VAL B  1 8   ? -44.386  -5.629  17.062  1.00 40.08  ? 7   VAL C O   1 
ATOM   2311  C  CB  . VAL B  1 8   ? -47.221  -4.833  16.542  1.00 36.03  ? 7   VAL C CB  1 
ATOM   2312  C  CG1 . VAL B  1 8   ? -47.117  -5.009  15.043  1.00 37.57  ? 7   VAL C CG1 1 
ATOM   2313  C  CG2 . VAL B  1 8   ? -48.633  -4.443  16.936  1.00 37.15  ? 7   VAL C CG2 1 
ATOM   2314  N  N   . LEU B  1 9   ? -45.115  -7.666  16.363  1.00 40.35  ? 8   LEU C N   1 
ATOM   2315  C  CA  . LEU B  1 9   ? -43.799  -8.197  16.004  1.00 43.27  ? 8   LEU C CA  1 
ATOM   2316  C  C   . LEU B  1 9   ? -43.557  -7.948  14.516  1.00 45.11  ? 8   LEU C C   1 
ATOM   2317  O  O   . LEU B  1 9   ? -44.396  -8.291  13.671  1.00 39.09  ? 8   LEU C O   1 
ATOM   2318  C  CB  . LEU B  1 9   ? -43.710  -9.689  16.353  1.00 45.10  ? 8   LEU C CB  1 
ATOM   2319  C  CG  . LEU B  1 9   ? -43.639  -9.994  17.852  1.00 46.17  ? 8   LEU C CG  1 
ATOM   2320  C  CD1 . LEU B  1 9   ? -44.996  -10.424 18.363  1.00 51.92  ? 8   LEU C CD1 1 
ATOM   2321  C  CD2 . LEU B  1 9   ? -42.601  -11.061 18.167  1.00 50.54  ? 8   LEU C CD2 1 
ATOM   2322  N  N   . LYS B  1 10  ? -42.422  -7.302  14.218  1.00 46.10  ? 9   LYS C N   1 
ATOM   2323  C  CA  . LYS B  1 10  ? -41.995  -7.016  12.842  1.00 53.18  ? 9   LYS C CA  1 
ATOM   2324  C  C   . LYS B  1 10  ? -40.494  -7.300  12.709  1.00 50.96  ? 9   LYS C C   1 
ATOM   2325  O  O   . LYS B  1 10  ? -39.763  -7.316  13.706  1.00 44.74  ? 9   LYS C O   1 
ATOM   2326  C  CB  . LYS B  1 10  ? -42.253  -5.551  12.470  1.00 58.88  ? 9   LYS C CB  1 
ATOM   2327  C  CG  . LYS B  1 10  ? -43.682  -5.058  12.652  1.00 65.72  ? 9   LYS C CG  1 
ATOM   2328  C  CD  . LYS B  1 10  ? -44.475  -4.970  11.372  1.00 72.77  ? 9   LYS C CD  1 
ATOM   2329  C  CE  . LYS B  1 10  ? -45.677  -4.059  11.508  1.00 78.37  ? 9   LYS C CE  1 
ATOM   2330  N  NZ  . LYS B  1 10  ? -46.298  -3.790  10.190  1.00 87.77  ? 9   LYS C NZ  1 
ATOM   2331  N  N   . GLY B  1 11  ? -40.036  -7.481  11.469  1.00 54.50  ? 10  GLY C N   1 
ATOM   2332  C  CA  . GLY B  1 11  ? -38.619  -7.685  11.215  1.00 60.52  ? 10  GLY C CA  1 
ATOM   2333  C  C   . GLY B  1 11  ? -38.208  -7.269  9.816   1.00 60.85  ? 10  GLY C C   1 
ATOM   2334  O  O   . GLY B  1 11  ? -39.031  -6.829  9.014   1.00 65.00  ? 10  GLY C O   1 
ATOM   2335  N  N   . ASP B  1 12  ? -36.905  -7.412  9.550   1.00 66.13  ? 11  ASP C N   1 
ATOM   2336  C  CA  . ASP B  1 12  ? -36.321  -7.250  8.228   1.00 70.80  ? 11  ASP C CA  1 
ATOM   2337  C  C   . ASP B  1 12  ? -37.057  -8.164  7.243   1.00 72.20  ? 11  ASP C C   1 
ATOM   2338  O  O   . ASP B  1 12  ? -37.521  -7.710  6.200   1.00 71.69  ? 11  ASP C O   1 
ATOM   2339  C  CB  . ASP B  1 12  ? -34.825  -7.584  8.237   1.00 77.58  ? 11  ASP C CB  1 
ATOM   2340  C  CG  . ASP B  1 12  ? -33.934  -6.517  8.855   1.00 84.37  ? 11  ASP C CG  1 
ATOM   2341  O  OD1 . ASP B  1 12  ? -34.414  -5.379  9.048   1.00 85.71  ? 11  ASP C OD1 1 
ATOM   2342  O  OD2 . ASP B  1 12  ? -32.756  -6.833  9.134   1.00 94.90  ? 11  ASP C OD2 1 
ATOM   2343  N  N   . GLY B  1 13  ? -37.154  -9.449  7.609   1.00 68.14  ? 12  GLY C N   1 
ATOM   2344  C  CA  . GLY B  1 13  ? -37.756  -10.492 6.792   1.00 65.25  ? 12  GLY C CA  1 
ATOM   2345  C  C   . GLY B  1 13  ? -39.277  -10.383 6.765   1.00 66.88  ? 12  GLY C C   1 
ATOM   2346  O  O   . GLY B  1 13  ? -39.830  -9.343  7.120   1.00 63.92  ? 12  GLY C O   1 
ATOM   2347  N  N   . PRO B  1 14  ? -39.994  -11.451 6.342   1.00 64.89  ? 13  PRO C N   1 
ATOM   2348  C  CA  . PRO B  1 14  ? -41.455  -11.424 6.258   1.00 58.39  ? 13  PRO C CA  1 
ATOM   2349  C  C   . PRO B  1 14  ? -42.167  -11.849 7.555   1.00 54.35  ? 13  PRO C C   1 
ATOM   2350  O  O   . PRO B  1 14  ? -43.385  -11.963 7.560   1.00 56.31  ? 13  PRO C O   1 
ATOM   2351  C  CB  . PRO B  1 14  ? -41.711  -12.422 5.119   1.00 60.69  ? 13  PRO C CB  1 
ATOM   2352  C  CG  . PRO B  1 14  ? -40.620  -13.470 5.291   1.00 60.44  ? 13  PRO C CG  1 
ATOM   2353  C  CD  . PRO B  1 14  ? -39.440  -12.746 5.914   1.00 63.82  ? 13  PRO C CD  1 
ATOM   2354  N  N   . VAL B  1 15  ? -41.412  -12.043 8.645   1.00 49.62  ? 14  VAL C N   1 
ATOM   2355  C  CA  . VAL B  1 15  ? -41.992  -12.443 9.929   1.00 51.89  ? 14  VAL C CA  1 
ATOM   2356  C  C   . VAL B  1 15  ? -42.765  -11.260 10.526  1.00 51.91  ? 14  VAL C C   1 
ATOM   2357  O  O   . VAL B  1 15  ? -42.193  -10.203 10.776  1.00 54.72  ? 14  VAL C O   1 
ATOM   2358  C  CB  . VAL B  1 15  ? -40.932  -12.957 10.921  1.00 50.06  ? 14  VAL C CB  1 
ATOM   2359  C  CG1 . VAL B  1 15  ? -41.554  -13.363 12.252  1.00 48.83  ? 14  VAL C CG1 1 
ATOM   2360  C  CG2 . VAL B  1 15  ? -40.127  -14.109 10.343  1.00 54.70  ? 14  VAL C CG2 1 
ATOM   2361  N  N   . GLN B  1 16  ? -44.061  -11.463 10.782  1.00 47.95  ? 15  GLN C N   1 
ATOM   2362  C  CA  . GLN B  1 16  ? -44.869  -10.491 11.524  1.00 49.73  ? 15  GLN C CA  1 
ATOM   2363  C  C   . GLN B  1 16  ? -45.910  -11.222 12.374  1.00 49.54  ? 15  GLN C C   1 
ATOM   2364  O  O   . GLN B  1 16  ? -46.329  -12.329 12.029  1.00 44.28  ? 15  GLN C O   1 
ATOM   2365  C  CB  . GLN B  1 16  ? -45.563  -9.518  10.578  1.00 52.65  ? 15  GLN C CB  1 
ATOM   2366  C  CG  . GLN B  1 16  ? -46.262  -10.195 9.415   1.00 57.89  ? 15  GLN C CG  1 
ATOM   2367  C  CD  . GLN B  1 16  ? -46.303  -9.290  8.211   1.00 63.42  ? 15  GLN C CD  1 
ATOM   2368  O  OE1 . GLN B  1 16  ? -47.368  -8.889  7.757   1.00 69.23  ? 15  GLN C OE1 1 
ATOM   2369  N  NE2 . GLN B  1 16  ? -45.134  -8.947  7.691   1.00 70.36  ? 15  GLN C NE2 1 
ATOM   2370  N  N   . GLY B  1 17  ? -46.321  -10.586 13.476  1.00 44.08  ? 16  GLY C N   1 
ATOM   2371  C  CA  . GLY B  1 17  ? -47.364  -11.130 14.318  1.00 44.69  ? 16  GLY C CA  1 
ATOM   2372  C  C   . GLY B  1 17  ? -47.920  -10.117 15.294  1.00 42.64  ? 16  GLY C C   1 
ATOM   2373  O  O   . GLY B  1 17  ? -47.433  -8.982  15.397  1.00 41.55  ? 16  GLY C O   1 
ATOM   2374  N  N   . ILE B  1 18  ? -48.981  -10.532 15.988  1.00 35.35  ? 17  ILE C N   1 
ATOM   2375  C  CA  . ILE B  1 18  ? -49.524  -9.822  17.098  1.00 36.71  ? 17  ILE C CA  1 
ATOM   2376  C  C   . ILE B  1 18  ? -49.667  -10.808 18.249  1.00 38.13  ? 17  ILE C C   1 
ATOM   2377  O  O   . ILE B  1 18  ? -50.259  -11.882 18.083  1.00 37.55  ? 17  ILE C O   1 
ATOM   2378  C  CB  . ILE B  1 18  ? -50.870  -9.176  16.733  1.00 37.14  ? 17  ILE C CB  1 
ATOM   2379  C  CG1 . ILE B  1 18  ? -50.700  -8.115  15.640  1.00 41.57  ? 17  ILE C CG1 1 
ATOM   2380  C  CG2 . ILE B  1 18  ? -51.533  -8.637  17.989  1.00 39.66  ? 17  ILE C CG2 1 
ATOM   2381  C  CD1 . ILE B  1 18  ? -51.998  -7.522  15.119  1.00 43.14  ? 17  ILE C CD1 1 
ATOM   2382  N  N   . ILE B  1 19  ? -49.156  -10.409 19.412  1.00 35.38  ? 18  ILE C N   1 
ATOM   2383  C  CA  . ILE B  1 19  ? -49.224  -11.192 20.609  1.00 36.93  ? 18  ILE C CA  1 
ATOM   2384  C  C   . ILE B  1 19  ? -49.866  -10.336 21.698  1.00 39.62  ? 18  ILE C C   1 
ATOM   2385  O  O   . ILE B  1 19  ? -49.420  -9.205  21.956  1.00 38.94  ? 18  ILE C O   1 
ATOM   2386  C  CB  . ILE B  1 19  ? -47.830  -11.682 21.056  1.00 35.14  ? 18  ILE C CB  1 
ATOM   2387  C  CG1 . ILE B  1 19  ? -47.154  -12.597 20.031  1.00 37.72  ? 18  ILE C CG1 1 
ATOM   2388  C  CG2 . ILE B  1 19  ? -47.923  -12.326 22.422  1.00 37.20  ? 18  ILE C CG2 1 
ATOM   2389  C  CD1 . ILE B  1 19  ? -47.870  -13.908 19.795  1.00 41.65  ? 18  ILE C CD1 1 
ATOM   2390  N  N   . ASN B  1 20  ? -50.857  -10.931 22.369  1.00 36.40  ? 19  ASN C N   1 
ATOM   2391  C  CA  . ASN B  1 20  ? -51.618  -10.332 23.441  1.00 35.55  ? 19  ASN C CA  1 
ATOM   2392  C  C   . ASN B  1 20  ? -51.180  -10.918 24.787  1.00 36.47  ? 19  ASN C C   1 
ATOM   2393  O  O   . ASN B  1 20  ? -50.756  -12.076 24.872  1.00 38.86  ? 19  ASN C O   1 
ATOM   2394  C  CB  . ASN B  1 20  ? -53.112  -10.588 23.251  1.00 38.60  ? 19  ASN C CB  1 
ATOM   2395  C  CG  . ASN B  1 20  ? -53.600  -10.175 21.883  1.00 41.72  ? 19  ASN C CG  1 
ATOM   2396  O  OD1 . ASN B  1 20  ? -53.811  -8.989  21.632  1.00 45.76  ? 19  ASN C OD1 1 
ATOM   2397  N  ND2 . ASN B  1 20  ? -53.794  -11.146 21.001  1.00 41.08  ? 19  ASN C ND2 1 
ATOM   2398  N  N   . PHE B  1 21  ? -51.314  -10.110 25.838  1.00 32.85  ? 20  PHE C N   1 
ATOM   2399  C  CA  . PHE B  1 21  ? -51.059  -10.501 27.206  1.00 38.08  ? 20  PHE C CA  1 
ATOM   2400  C  C   . PHE B  1 21  ? -52.252  -10.075 28.063  1.00 40.91  ? 20  PHE C C   1 
ATOM   2401  O  O   . PHE B  1 21  ? -52.874  -9.032  27.821  1.00 40.36  ? 20  PHE C O   1 
ATOM   2402  C  CB  . PHE B  1 21  ? -49.776  -9.868  27.759  1.00 39.06  ? 20  PHE C CB  1 
ATOM   2403  C  CG  . PHE B  1 21  ? -48.548  -10.065 26.910  1.00 38.60  ? 20  PHE C CG  1 
ATOM   2404  C  CD1 . PHE B  1 21  ? -47.551  -10.947 27.301  1.00 38.42  ? 20  PHE C CD1 1 
ATOM   2405  C  CD2 . PHE B  1 21  ? -48.392  -9.373  25.718  1.00 38.64  ? 20  PHE C CD2 1 
ATOM   2406  C  CE1 . PHE B  1 21  ? -46.421  -11.132 26.520  1.00 38.47  ? 20  PHE C CE1 1 
ATOM   2407  C  CE2 . PHE B  1 21  ? -47.262  -9.565  24.935  1.00 40.66  ? 20  PHE C CE2 1 
ATOM   2408  C  CZ  . PHE B  1 21  ? -46.278  -10.443 25.338  1.00 38.86  ? 20  PHE C CZ  1 
ATOM   2409  N  N   . GLU B  1 22  ? -52.561  -10.880 29.082  1.00 44.65  ? 21  GLU C N   1 
ATOM   2410  C  CA  . GLU B  1 22  ? -53.610  -10.530 30.001  1.00 48.40  ? 21  GLU C CA  1 
ATOM   2411  C  C   . GLU B  1 22  ? -53.306  -11.131 31.369  1.00 48.03  ? 21  GLU C C   1 
ATOM   2412  O  O   . GLU B  1 22  ? -52.873  -12.280 31.457  1.00 50.41  ? 21  GLU C O   1 
ATOM   2413  C  CB  . GLU B  1 22  ? -54.959  -11.005 29.472  1.00 51.38  ? 21  GLU C CB  1 
ATOM   2414  C  CG  . GLU B  1 22  ? -56.094  -10.657 30.405  1.00 57.74  ? 21  GLU C CG  1 
ATOM   2415  C  CD  . GLU B  1 22  ? -57.461  -10.919 29.809  1.00 66.83  ? 21  GLU C CD  1 
ATOM   2416  O  OE1 . GLU B  1 22  ? -58.169  -11.799 30.351  1.00 71.98  ? 21  GLU C OE1 1 
ATOM   2417  O  OE2 . GLU B  1 22  ? -57.805  -10.249 28.804  1.00 71.72  ? 21  GLU C OE2 1 
ATOM   2418  N  N   . GLN B  1 23  ? -53.550  -10.332 32.412  1.00 48.80  ? 22  GLN C N   1 
ATOM   2419  C  CA  . GLN B  1 23  ? -53.278  -10.689 33.794  1.00 52.05  ? 22  GLN C CA  1 
ATOM   2420  C  C   . GLN B  1 23  ? -54.361  -10.063 34.680  1.00 63.23  ? 22  GLN C C   1 
ATOM   2421  O  O   . GLN B  1 23  ? -54.418  -8.841  34.810  1.00 66.44  ? 22  GLN C O   1 
ATOM   2422  C  CB  . GLN B  1 23  ? -51.877  -10.217 34.184  1.00 48.55  ? 22  GLN C CB  1 
ATOM   2423  C  CG  . GLN B  1 23  ? -51.466  -10.594 35.601  1.00 48.98  ? 22  GLN C CG  1 
ATOM   2424  C  CD  . GLN B  1 23  ? -50.070  -10.114 35.920  1.00 51.71  ? 22  GLN C CD  1 
ATOM   2425  O  OE1 . GLN B  1 23  ? -49.645  -9.052  35.469  1.00 53.20  ? 22  GLN C OE1 1 
ATOM   2426  N  NE2 . GLN B  1 23  ? -49.332  -10.899 36.690  1.00 45.94  ? 22  GLN C NE2 1 
ATOM   2427  N  N   . LYS B  1 24  ? -55.192  -10.916 35.293  1.00 73.74  ? 23  LYS C N   1 
ATOM   2428  C  CA  . LYS B  1 24  ? -56.371  -10.499 36.065  1.00 77.22  ? 23  LYS C CA  1 
ATOM   2429  C  C   . LYS B  1 24  ? -55.942  -9.784  37.351  1.00 77.11  ? 23  LYS C C   1 
ATOM   2430  O  O   . LYS B  1 24  ? -56.588  -8.817  37.755  1.00 81.34  ? 23  LYS C O   1 
ATOM   2431  C  CB  . LYS B  1 24  ? -57.269  -11.699 36.390  1.00 85.39  ? 23  LYS C CB  1 
ATOM   2432  C  CG  . LYS B  1 24  ? -57.770  -12.504 35.193  1.00 89.40  ? 23  LYS C CG  1 
ATOM   2433  C  CD  . LYS B  1 24  ? -58.128  -11.670 33.970  1.00 93.29  ? 23  LYS C CD  1 
ATOM   2434  C  CE  . LYS B  1 24  ? -59.205  -10.635 34.230  1.00 91.93  ? 23  LYS C CE  1 
ATOM   2435  N  NZ  . LYS B  1 24  ? -59.503  -9.841  33.016  1.00 89.83  ? 23  LYS C NZ  1 
ATOM   2436  N  N   . GLU B  1 25  ? -54.873  -10.266 37.996  1.00 77.10  ? 24  GLU C N   1 
ATOM   2437  C  CA  . GLU B  1 25  ? -54.169  -9.455  38.997  1.00 86.13  ? 24  GLU C CA  1 
ATOM   2438  C  C   . GLU B  1 25  ? -52.721  -9.945  39.136  1.00 83.91  ? 24  GLU C C   1 
ATOM   2439  O  O   . GLU B  1 25  ? -52.344  -10.995 38.607  1.00 77.15  ? 24  GLU C O   1 
ATOM   2440  C  CB  . GLU B  1 25  ? -54.927  -9.412  40.329  1.00 96.32  ? 24  GLU C CB  1 
ATOM   2441  C  CG  . GLU B  1 25  ? -54.814  -10.679 41.153  1.00 102.28 ? 24  GLU C CG  1 
ATOM   2442  C  CD  . GLU B  1 25  ? -55.703  -11.819 40.693  1.00 104.01 ? 24  GLU C CD  1 
ATOM   2443  O  OE1 . GLU B  1 25  ? -55.741  -12.086 39.474  1.00 96.81  ? 24  GLU C OE1 1 
ATOM   2444  O  OE2 . GLU B  1 25  ? -56.355  -12.436 41.559  1.00 109.15 ? 24  GLU C OE2 1 
ATOM   2445  N  N   . SER B  1 26  ? -51.933  -9.154  39.873  1.00 84.98  ? 25  SER C N   1 
ATOM   2446  C  CA  . SER B  1 26  ? -50.473  -9.116  39.788  1.00 85.88  ? 25  SER C CA  1 
ATOM   2447  C  C   . SER B  1 26  ? -49.840  -10.368 40.405  1.00 83.21  ? 25  SER C C   1 
ATOM   2448  O  O   . SER B  1 26  ? -48.706  -10.711 40.083  1.00 77.59  ? 25  SER C O   1 
ATOM   2449  C  CB  . SER B  1 26  ? -49.940  -7.849  40.425  1.00 92.26  ? 25  SER C CB  1 
ATOM   2450  O  OG  . SER B  1 26  ? -50.638  -7.537  41.626  1.00 90.60  ? 25  SER C OG  1 
ATOM   2451  N  N   . ASN B  1 27  ? -50.563  -11.029 41.310  1.00 88.82  ? 26  ASN C N   1 
ATOM   2452  C  CA  . ASN B  1 27  ? -50.170  -12.358 41.771  1.00 94.62  ? 26  ASN C CA  1 
ATOM   2453  C  C   . ASN B  1 27  ? -50.324  -13.346 40.604  1.00 91.96  ? 26  ASN C C   1 
ATOM   2454  O  O   . ASN B  1 27  ? -49.432  -14.161 40.358  1.00 98.66  ? 26  ASN C O   1 
ATOM   2455  C  CB  . ASN B  1 27  ? -50.951  -12.807 43.013  1.00 102.39 ? 26  ASN C CB  1 
ATOM   2456  C  CG  . ASN B  1 27  ? -52.414  -12.407 43.003  1.00 110.28 ? 26  ASN C CG  1 
ATOM   2457  O  OD1 . ASN B  1 27  ? -52.753  -11.266 43.315  1.00 115.76 ? 26  ASN C OD1 1 
ATOM   2458  N  ND2 . ASN B  1 27  ? -53.289  -13.341 42.665  1.00 110.67 ? 26  ASN C ND2 1 
ATOM   2459  N  N   . GLY B  1 28  ? -51.442  -13.219 39.873  1.00 83.86  ? 27  GLY C N   1 
ATOM   2460  C  CA  . GLY B  1 28  ? -51.939  -14.219 38.925  1.00 72.14  ? 27  GLY C CA  1 
ATOM   2461  C  C   . GLY B  1 28  ? -50.994  -14.478 37.754  1.00 66.37  ? 27  GLY C C   1 
ATOM   2462  O  O   . GLY B  1 28  ? -50.104  -13.683 37.462  1.00 60.37  ? 27  GLY C O   1 
ATOM   2463  N  N   . PRO B  1 29  ? -51.169  -15.612 37.039  1.00 62.59  ? 28  PRO C N   1 
ATOM   2464  C  CA  . PRO B  1 29  ? -50.415  -15.876 35.816  1.00 58.48  ? 28  PRO C CA  1 
ATOM   2465  C  C   . PRO B  1 29  ? -50.844  -14.952 34.662  1.00 52.69  ? 28  PRO C C   1 
ATOM   2466  O  O   . PRO B  1 29  ? -51.912  -14.333 34.715  1.00 47.36  ? 28  PRO C O   1 
ATOM   2467  C  CB  . PRO B  1 29  ? -50.754  -17.342 35.502  1.00 61.37  ? 28  PRO C CB  1 
ATOM   2468  C  CG  . PRO B  1 29  ? -52.131  -17.539 36.101  1.00 60.68  ? 28  PRO C CG  1 
ATOM   2469  C  CD  . PRO B  1 29  ? -52.109  -16.700 37.362  1.00 65.03  ? 28  PRO C CD  1 
ATOM   2470  N  N   . VAL B  1 30  ? -49.998  -14.893 33.628  1.00 47.09  ? 29  VAL C N   1 
ATOM   2471  C  CA  . VAL B  1 30  ? -50.214  -14.064 32.446  1.00 48.23  ? 29  VAL C CA  1 
ATOM   2472  C  C   . VAL B  1 30  ? -50.552  -14.984 31.274  1.00 46.17  ? 29  VAL C C   1 
ATOM   2473  O  O   . VAL B  1 30  ? -49.743  -15.851 30.907  1.00 43.91  ? 29  VAL C O   1 
ATOM   2474  C  CB  . VAL B  1 30  ? -48.974  -13.202 32.127  1.00 48.18  ? 29  VAL C CB  1 
ATOM   2475  C  CG1 . VAL B  1 30  ? -49.117  -12.442 30.812  1.00 49.12  ? 29  VAL C CG1 1 
ATOM   2476  C  CG2 . VAL B  1 30  ? -48.635  -12.258 33.275  1.00 49.76  ? 29  VAL C CG2 1 
ATOM   2477  N  N   . LYS B  1 31  ? -51.738  -14.765 30.699  1.00 45.77  ? 30  LYS C N   1 
ATOM   2478  C  CA  . LYS B  1 31  ? -52.163  -15.385 29.454  1.00 47.12  ? 30  LYS C CA  1 
ATOM   2479  C  C   . LYS B  1 31  ? -51.483  -14.665 28.283  1.00 43.32  ? 30  LYS C C   1 
ATOM   2480  O  O   . LYS B  1 31  ? -51.601  -13.445 28.148  1.00 40.70  ? 30  LYS C O   1 
ATOM   2481  C  CB  . LYS B  1 31  ? -53.690  -15.316 29.305  1.00 53.30  ? 30  LYS C CB  1 
ATOM   2482  C  CG  . LYS B  1 31  ? -54.283  -16.361 28.365  1.00 62.16  ? 30  LYS C CG  1 
ATOM   2483  C  CD  . LYS B  1 31  ? -55.694  -16.065 27.857  1.00 69.56  ? 30  LYS C CD  1 
ATOM   2484  C  CE  . LYS B  1 31  ? -56.021  -16.790 26.560  1.00 69.49  ? 30  LYS C CE  1 
ATOM   2485  N  NZ  . LYS B  1 31  ? -57.305  -16.337 25.968  1.00 65.86  ? 30  LYS C NZ  1 
ATOM   2486  N  N   . VAL B  1 32  ? -50.826  -15.444 27.414  1.00 41.24  ? 31  VAL C N   1 
ATOM   2487  C  CA  . VAL B  1 32  ? -50.108  -14.955 26.240  1.00 39.32  ? 31  VAL C CA  1 
ATOM   2488  C  C   . VAL B  1 32  ? -50.657  -15.668 25.005  1.00 41.53  ? 31  VAL C C   1 
ATOM   2489  O  O   . VAL B  1 32  ? -50.535  -16.894 24.903  1.00 43.13  ? 31  VAL C O   1 
ATOM   2490  C  CB  . VAL B  1 32  ? -48.597  -15.222 26.378  1.00 41.53  ? 31  VAL C CB  1 
ATOM   2491  C  CG1 . VAL B  1 32  ? -47.817  -14.683 25.196  1.00 40.39  ? 31  VAL C CG1 1 
ATOM   2492  C  CG2 . VAL B  1 32  ? -48.043  -14.702 27.695  1.00 43.26  ? 31  VAL C CG2 1 
ATOM   2493  N  N   . TRP B  1 33  ? -51.213  -14.920 24.051  1.00 37.92  ? 32  TRP C N   1 
ATOM   2494  C  CA  . TRP B  1 33  ? -51.785  -15.563 22.887  1.00 38.75  ? 32  TRP C CA  1 
ATOM   2495  C  C   . TRP B  1 33  ? -51.765  -14.650 21.667  1.00 38.25  ? 32  TRP C C   1 
ATOM   2496  O  O   . TRP B  1 33  ? -51.807  -13.409 21.758  1.00 40.29  ? 32  TRP C O   1 
ATOM   2497  C  CB  . TRP B  1 33  ? -53.216  -16.041 23.185  1.00 37.45  ? 32  TRP C CB  1 
ATOM   2498  C  CG  . TRP B  1 33  ? -54.253  -14.971 23.084  1.00 36.91  ? 32  TRP C CG  1 
ATOM   2499  C  CD1 . TRP B  1 33  ? -55.037  -14.687 22.006  1.00 38.05  ? 32  TRP C CD1 1 
ATOM   2500  C  CD2 . TRP B  1 33  ? -54.610  -14.028 24.109  1.00 36.95  ? 32  TRP C CD2 1 
ATOM   2501  N  NE1 . TRP B  1 33  ? -55.866  -13.637 22.295  1.00 38.75  ? 32  TRP C NE1 1 
ATOM   2502  C  CE2 . TRP B  1 33  ? -55.622  -13.211 23.578  1.00 38.53  ? 32  TRP C CE2 1 
ATOM   2503  C  CE3 . TRP B  1 33  ? -54.159  -13.790 25.413  1.00 42.24  ? 32  TRP C CE3 1 
ATOM   2504  C  CZ2 . TRP B  1 33  ? -56.203  -12.180 24.316  1.00 42.00  ? 32  TRP C CZ2 1 
ATOM   2505  C  CZ3 . TRP B  1 33  ? -54.735  -12.773 26.147  1.00 43.20  ? 32  TRP C CZ3 1 
ATOM   2506  C  CH2 . TRP B  1 33  ? -55.748  -11.984 25.604  1.00 43.60  ? 32  TRP C CH2 1 
ATOM   2507  N  N   . GLY B  1 34  ? -51.777  -15.297 20.510  1.00 35.18  ? 33  GLY C N   1 
ATOM   2508  C  CA  . GLY B  1 34  ? -51.903  -14.617 19.248  1.00 35.90  ? 33  GLY C CA  1 
ATOM   2509  C  C   . GLY B  1 34  ? -51.282  -15.444 18.150  1.00 37.11  ? 33  GLY C C   1 
ATOM   2510  O  O   . GLY B  1 34  ? -51.334  -16.667 18.184  1.00 37.37  ? 33  GLY C O   1 
ATOM   2511  N  N   . SER B  1 35  ? -50.703  -14.772 17.161  1.00 37.25  ? 34  SER C N   1 
ATOM   2512  C  CA  . SER B  1 35  ? -50.295  -15.435 15.951  1.00 40.17  ? 34  SER C CA  1 
ATOM   2513  C  C   . SER B  1 35  ? -49.082  -14.720 15.351  1.00 41.88  ? 34  SER C C   1 
ATOM   2514  O  O   . SER B  1 35  ? -49.025  -13.479 15.361  1.00 40.48  ? 34  SER C O   1 
ATOM   2515  C  CB  . SER B  1 35  ? -51.454  -15.468 14.968  1.00 42.99  ? 34  SER C CB  1 
ATOM   2516  O  OG  . SER B  1 35  ? -51.247  -16.477 13.997  1.00 48.89  ? 34  SER C OG  1 
ATOM   2517  N  N   . ILE B  1 36  ? -48.146  -15.518 14.826  1.00 38.52  ? 35  ILE C N   1 
ATOM   2518  C  CA  . ILE B  1 36  ? -46.959  -15.060 14.110  1.00 41.85  ? 35  ILE C CA  1 
ATOM   2519  C  C   . ILE B  1 36  ? -46.933  -15.808 12.777  1.00 43.71  ? 35  ILE C C   1 
ATOM   2520  O  O   . ILE B  1 36  ? -47.061  -17.043 12.749  1.00 44.31  ? 35  ILE C O   1 
ATOM   2521  C  CB  . ILE B  1 36  ? -45.681  -15.305 14.944  1.00 41.21  ? 35  ILE C CB  1 
ATOM   2522  C  CG1 . ILE B  1 36  ? -45.796  -14.674 16.335  1.00 40.93  ? 35  ILE C CG1 1 
ATOM   2523  C  CG2 . ILE B  1 36  ? -44.447  -14.812 14.196  1.00 43.18  ? 35  ILE C CG2 1 
ATOM   2524  C  CD1 . ILE B  1 36  ? -44.695  -15.058 17.298  1.00 43.73  ? 35  ILE C CD1 1 
ATOM   2525  N  N   . LYS B  1 37  ? -46.798  -15.064 11.681  1.00 40.69  ? 36  LYS C N   1 
ATOM   2526  C  CA  . LYS B  1 37  ? -46.742  -15.649 10.354  1.00 44.72  ? 36  LYS C CA  1 
ATOM   2527  C  C   . LYS B  1 37  ? -45.387  -15.330 9.706   1.00 45.56  ? 36  LYS C C   1 
ATOM   2528  O  O   . LYS B  1 37  ? -44.592  -14.583 10.262  1.00 48.06  ? 36  LYS C O   1 
ATOM   2529  C  CB  . LYS B  1 37  ? -47.931  -15.167 9.517   1.00 50.08  ? 36  LYS C CB  1 
ATOM   2530  C  CG  . LYS B  1 37  ? -47.904  -13.707 9.081   1.00 56.90  ? 36  LYS C CG  1 
ATOM   2531  C  CD  . LYS B  1 37  ? -48.519  -13.473 7.707   1.00 64.27  ? 36  LYS C CD  1 
ATOM   2532  C  CE  . LYS B  1 37  ? -47.894  -14.350 6.635   1.00 72.61  ? 36  LYS C CE  1 
ATOM   2533  N  NZ  . LYS B  1 37  ? -47.812  -13.680 5.314   1.00 73.75  ? 36  LYS C NZ  1 
ATOM   2534  N  N   . GLY B  1 38  ? -45.148  -15.925 8.535   1.00 44.94  ? 37  GLY C N   1 
ATOM   2535  C  CA  . GLY B  1 38  ? -43.909  -15.796 7.780   1.00 45.73  ? 37  GLY C CA  1 
ATOM   2536  C  C   . GLY B  1 38  ? -42.725  -16.529 8.399   1.00 46.20  ? 37  GLY C C   1 
ATOM   2537  O  O   . GLY B  1 38  ? -41.581  -16.208 8.073   1.00 48.05  ? 37  GLY C O   1 
ATOM   2538  N  N   . LEU B  1 39  ? -42.968  -17.524 9.263   1.00 42.12  ? 38  LEU C N   1 
ATOM   2539  C  CA  . LEU B  1 39  ? -41.871  -18.303 9.875   1.00 41.68  ? 38  LEU C CA  1 
ATOM   2540  C  C   . LEU B  1 39  ? -41.535  -19.518 9.005   1.00 42.18  ? 38  LEU C C   1 
ATOM   2541  O  O   . LEU B  1 39  ? -42.341  -19.947 8.169   1.00 45.91  ? 38  LEU C O   1 
ATOM   2542  C  CB  . LEU B  1 39  ? -42.262  -18.747 11.286  1.00 44.29  ? 38  LEU C CB  1 
ATOM   2543  C  CG  . LEU B  1 39  ? -42.315  -17.635 12.326  1.00 46.61  ? 38  LEU C CG  1 
ATOM   2544  C  CD1 . LEU B  1 39  ? -43.125  -18.058 13.546  1.00 46.75  ? 38  LEU C CD1 1 
ATOM   2545  C  CD2 . LEU B  1 39  ? -40.908  -17.214 12.733  1.00 45.97  ? 38  LEU C CD2 1 
ATOM   2546  N  N   . THR B  1 40  ? -40.324  -20.053 9.194   1.00 40.94  ? 39  THR C N   1 
ATOM   2547  C  CA  . THR B  1 40  ? -39.989  -21.394 8.720   1.00 46.20  ? 39  THR C CA  1 
ATOM   2548  C  C   . THR B  1 40  ? -40.692  -22.423 9.618   1.00 43.43  ? 39  THR C C   1 
ATOM   2549  O  O   . THR B  1 40  ? -40.781  -22.230 10.819  1.00 43.38  ? 39  THR C O   1 
ATOM   2550  C  CB  . THR B  1 40  ? -38.475  -21.657 8.730   1.00 44.57  ? 39  THR C CB  1 
ATOM   2551  O  OG1 . THR B  1 40  ? -37.985  -21.426 10.049  1.00 47.77  ? 39  THR C OG1 1 
ATOM   2552  C  CG2 . THR B  1 40  ? -37.715  -20.789 7.757   1.00 47.44  ? 39  THR C CG2 1 
ATOM   2553  N  N   . GLU B  1 41  ? -41.157  -23.520 9.022   1.00 46.71  ? 40  GLU C N   1 
ATOM   2554  C  CA  . GLU B  1 41  ? -41.658  -24.698 9.744   1.00 47.24  ? 40  GLU C CA  1 
ATOM   2555  C  C   . GLU B  1 41  ? -40.829  -24.986 10.994  1.00 42.30  ? 40  GLU C C   1 
ATOM   2556  O  O   . GLU B  1 41  ? -39.634  -25.055 10.904  1.00 45.43  ? 40  GLU C O   1 
ATOM   2557  C  CB  . GLU B  1 41  ? -41.493  -25.944 8.880   1.00 51.43  ? 40  GLU C CB  1 
ATOM   2558  C  CG  . GLU B  1 41  ? -42.552  -26.100 7.822   1.00 57.49  ? 40  GLU C CG  1 
ATOM   2559  C  CD  . GLU B  1 41  ? -42.560  -27.503 7.241   1.00 58.27  ? 40  GLU C CD  1 
ATOM   2560  O  OE1 . GLU B  1 41  ? -41.497  -28.164 7.297   1.00 55.76  ? 40  GLU C OE1 1 
ATOM   2561  O  OE2 . GLU B  1 41  ? -43.631  -27.944 6.786   1.00 65.66  ? 40  GLU C OE2 1 
ATOM   2562  N  N   . GLY B  1 42  ? -41.474  -25.202 12.141  1.00 40.53  ? 41  GLY C N   1 
ATOM   2563  C  CA  . GLY B  1 42  ? -40.796  -25.809 13.287  1.00 38.88  ? 41  GLY C CA  1 
ATOM   2564  C  C   . GLY B  1 42  ? -40.756  -24.899 14.493  1.00 38.34  ? 41  GLY C C   1 
ATOM   2565  O  O   . GLY B  1 42  ? -41.544  -23.930 14.573  1.00 37.19  ? 41  GLY C O   1 
ATOM   2566  N  N   . LEU B  1 43  ? -39.895  -25.260 15.458  1.00 35.45  ? 42  LEU C N   1 
ATOM   2567  C  CA  . LEU B  1 43  ? -39.836  -24.566 16.730  1.00 42.24  ? 42  LEU C CA  1 
ATOM   2568  C  C   . LEU B  1 43  ? -39.001  -23.278 16.561  1.00 44.61  ? 42  LEU C C   1 
ATOM   2569  O  O   . LEU B  1 43  ? -37.965  -23.267 15.888  1.00 47.57  ? 42  LEU C O   1 
ATOM   2570  C  CB  . LEU B  1 43  ? -39.239  -25.457 17.828  1.00 44.03  ? 42  LEU C CB  1 
ATOM   2571  C  CG  . LEU B  1 43  ? -39.722  -26.908 17.954  1.00 48.19  ? 42  LEU C CG  1 
ATOM   2572  C  CD1 . LEU B  1 43  ? -39.431  -27.433 19.355  1.00 46.13  ? 42  LEU C CD1 1 
ATOM   2573  C  CD2 . LEU B  1 43  ? -41.195  -27.074 17.626  1.00 49.68  ? 42  LEU C CD2 1 
ATOM   2574  N  N   . HIS B  1 44  ? -39.464  -22.192 17.181  1.00 43.04  ? 43  HIS C N   1 
ATOM   2575  C  CA  . HIS B  1 44  ? -38.729  -20.913 17.219  1.00 41.57  ? 43  HIS C CA  1 
ATOM   2576  C  C   . HIS B  1 44  ? -38.695  -20.399 18.655  1.00 42.58  ? 43  HIS C C   1 
ATOM   2577  O  O   . HIS B  1 44  ? -39.741  -20.307 19.316  1.00 39.76  ? 43  HIS C O   1 
ATOM   2578  C  CB  . HIS B  1 44  ? -39.370  -19.888 16.293  1.00 37.29  ? 43  HIS C CB  1 
ATOM   2579  C  CG  . HIS B  1 44  ? -39.199  -20.182 14.847  1.00 39.38  ? 43  HIS C CG  1 
ATOM   2580  N  ND1 . HIS B  1 44  ? -40.130  -20.908 14.131  1.00 44.44  ? 43  HIS C ND1 1 
ATOM   2581  C  CD2 . HIS B  1 44  ? -38.228  -19.847 13.969  1.00 42.48  ? 43  HIS C CD2 1 
ATOM   2582  C  CE1 . HIS B  1 44  ? -39.737  -20.999 12.875  1.00 42.01  ? 43  HIS C CE1 1 
ATOM   2583  N  NE2 . HIS B  1 44  ? -38.575  -20.343 12.743  1.00 41.38  ? 43  HIS C NE2 1 
ATOM   2584  N  N   . GLY B  1 45  ? -37.487  -20.076 19.134  1.00 40.32  ? 44  GLY C N   1 
ATOM   2585  C  CA  . GLY B  1 45  ? -37.325  -19.443 20.428  1.00 41.22  ? 44  GLY C CA  1 
ATOM   2586  C  C   . GLY B  1 45  ? -38.173  -18.183 20.523  1.00 40.16  ? 44  GLY C C   1 
ATOM   2587  O  O   . GLY B  1 45  ? -38.404  -17.495 19.526  1.00 39.20  ? 44  GLY C O   1 
ATOM   2588  N  N   . PHE B  1 46  ? -38.666  -17.925 21.731  1.00 40.65  ? 45  PHE C N   1 
ATOM   2589  C  CA  . PHE B  1 46  ? -39.680  -16.932 21.985  1.00 44.78  ? 45  PHE C CA  1 
ATOM   2590  C  C   . PHE B  1 46  ? -39.436  -16.413 23.400  1.00 43.06  ? 45  PHE C C   1 
ATOM   2591  O  O   . PHE B  1 46  ? -39.673  -17.143 24.355  1.00 40.49  ? 45  PHE C O   1 
ATOM   2592  C  CB  . PHE B  1 46  ? -41.058  -17.576 21.802  1.00 43.36  ? 45  PHE C CB  1 
ATOM   2593  C  CG  . PHE B  1 46  ? -42.271  -16.688 21.923  1.00 38.32  ? 45  PHE C CG  1 
ATOM   2594  C  CD1 . PHE B  1 46  ? -42.610  -15.796 20.917  1.00 42.14  ? 45  PHE C CD1 1 
ATOM   2595  C  CD2 . PHE B  1 46  ? -43.132  -16.817 22.998  1.00 36.58  ? 45  PHE C CD2 1 
ATOM   2596  C  CE1 . PHE B  1 46  ? -43.761  -15.024 21.001  1.00 37.92  ? 45  PHE C CE1 1 
ATOM   2597  C  CE2 . PHE B  1 46  ? -44.288  -16.056 23.078  1.00 36.85  ? 45  PHE C CE2 1 
ATOM   2598  C  CZ  . PHE B  1 46  ? -44.599  -15.158 22.080  1.00 38.76  ? 45  PHE C CZ  1 
ATOM   2599  N  N   . HIS B  1 47  ? -38.882  -15.192 23.509  1.00 45.43  ? 46  HIS C N   1 
ATOM   2600  C  CA  . HIS B  1 47  ? -38.446  -14.652 24.813  1.00 45.57  ? 46  HIS C CA  1 
ATOM   2601  C  C   . HIS B  1 47  ? -38.750  -13.154 24.948  1.00 44.13  ? 46  HIS C C   1 
ATOM   2602  O  O   . HIS B  1 47  ? -38.866  -12.414 23.959  1.00 42.93  ? 46  HIS C O   1 
ATOM   2603  C  CB  . HIS B  1 47  ? -36.940  -14.837 25.046  1.00 49.94  ? 46  HIS C CB  1 
ATOM   2604  C  CG  . HIS B  1 47  ? -36.353  -16.080 24.478  1.00 52.05  ? 46  HIS C CG  1 
ATOM   2605  N  ND1 . HIS B  1 47  ? -35.581  -16.056 23.332  1.00 55.30  ? 46  HIS C ND1 1 
ATOM   2606  C  CD2 . HIS B  1 47  ? -36.387  -17.365 24.898  1.00 50.70  ? 46  HIS C CD2 1 
ATOM   2607  C  CE1 . HIS B  1 47  ? -35.168  -17.279 23.062  1.00 51.89  ? 46  HIS C CE1 1 
ATOM   2608  N  NE2 . HIS B  1 47  ? -35.653  -18.101 24.004  1.00 52.48  ? 46  HIS C NE2 1 
ATOM   2609  N  N   . VAL B  1 48  ? -38.852  -12.720 26.205  1.00 43.53  ? 47  VAL C N   1 
ATOM   2610  C  CA  . VAL B  1 48  ? -38.884  -11.298 26.559  1.00 48.77  ? 47  VAL C CA  1 
ATOM   2611  C  C   . VAL B  1 48  ? -37.436  -10.847 26.796  1.00 46.45  ? 47  VAL C C   1 
ATOM   2612  O  O   . VAL B  1 48  ? -36.764  -11.367 27.692  1.00 44.45  ? 47  VAL C O   1 
ATOM   2613  C  CB  . VAL B  1 48  ? -39.769  -11.044 27.796  1.00 47.89  ? 47  VAL C CB  1 
ATOM   2614  C  CG1 . VAL B  1 48  ? -39.689  -9.593  28.268  1.00 49.20  ? 47  VAL C CG1 1 
ATOM   2615  C  CG2 . VAL B  1 48  ? -41.214  -11.444 27.539  1.00 50.54  ? 47  VAL C CG2 1 
ATOM   2616  N  N   . HIS B  1 49  ? -36.971  -9.900  25.979  1.00 49.49  ? 48  HIS C N   1 
ATOM   2617  C  CA  . HIS B  1 49  ? -35.643  -9.272  26.144  1.00 47.35  ? 48  HIS C CA  1 
ATOM   2618  C  C   . HIS B  1 49  ? -35.743  -8.034  27.052  1.00 48.71  ? 48  HIS C C   1 
ATOM   2619  O  O   . HIS B  1 49  ? -36.814  -7.448  27.238  1.00 41.89  ? 48  HIS C O   1 
ATOM   2620  C  CB  . HIS B  1 49  ? -35.032  -9.010  24.764  1.00 47.45  ? 48  HIS C CB  1 
ATOM   2621  C  CG  . HIS B  1 49  ? -34.611  -10.281 24.112  1.00 54.09  ? 48  HIS C CG  1 
ATOM   2622  N  ND1 . HIS B  1 49  ? -33.301  -10.537 23.740  1.00 56.27  ? 48  HIS C ND1 1 
ATOM   2623  C  CD2 . HIS B  1 49  ? -35.311  -11.404 23.833  1.00 53.55  ? 48  HIS C CD2 1 
ATOM   2624  C  CE1 . HIS B  1 49  ? -33.218  -11.745 23.217  1.00 53.28  ? 48  HIS C CE1 1 
ATOM   2625  N  NE2 . HIS B  1 49  ? -34.444  -12.304 23.267  1.00 56.64  ? 48  HIS C NE2 1 
ATOM   2626  N  N   . GLU B  1 50  ? -34.606  -7.648  27.646  1.00 50.17  ? 49  GLU C N   1 
ATOM   2627  C  CA  . GLU B  1 50  ? -34.593  -6.676  28.755  1.00 52.66  ? 49  GLU C CA  1 
ATOM   2628  C  C   . GLU B  1 50  ? -35.123  -5.304  28.304  1.00 44.68  ? 49  GLU C C   1 
ATOM   2629  O  O   . GLU B  1 50  ? -35.919  -4.692  29.025  1.00 44.98  ? 49  GLU C O   1 
ATOM   2630  C  CB  . GLU B  1 50  ? -33.182  -6.505  29.326  1.00 55.25  ? 49  GLU C CB  1 
ATOM   2631  C  CG  . GLU B  1 50  ? -33.161  -5.672  30.596  1.00 57.11  ? 49  GLU C CG  1 
ATOM   2632  C  CD  . GLU B  1 50  ? -31.837  -5.690  31.338  1.00 59.97  ? 49  GLU C CD  1 
ATOM   2633  O  OE1 . GLU B  1 50  ? -30.816  -6.084  30.724  1.00 55.30  ? 49  GLU C OE1 1 
ATOM   2634  O  OE2 . GLU B  1 50  ? -31.836  -5.314  32.526  1.00 61.00  ? 49  GLU C OE2 1 
ATOM   2635  N  N   . PHE B  1 51  ? -34.680  -4.850  27.128  1.00 42.58  ? 50  PHE C N   1 
ATOM   2636  C  CA  . PHE B  1 51  ? -34.846  -3.454  26.706  1.00 49.44  ? 50  PHE C CA  1 
ATOM   2637  C  C   . PHE B  1 51  ? -35.891  -3.348  25.591  1.00 47.19  ? 50  PHE C C   1 
ATOM   2638  O  O   . PHE B  1 51  ? -35.846  -4.102  24.634  1.00 48.60  ? 50  PHE C O   1 
ATOM   2639  C  CB  . PHE B  1 51  ? -33.498  -2.855  26.277  1.00 49.85  ? 50  PHE C CB  1 
ATOM   2640  C  CG  . PHE B  1 51  ? -32.461  -2.888  27.373  1.00 52.82  ? 50  PHE C CG  1 
ATOM   2641  C  CD1 . PHE B  1 51  ? -32.754  -2.386  28.636  1.00 53.88  ? 50  PHE C CD1 1 
ATOM   2642  C  CD2 . PHE B  1 51  ? -31.223  -3.480  27.169  1.00 53.27  ? 50  PHE C CD2 1 
ATOM   2643  C  CE1 . PHE B  1 51  ? -31.820  -2.447  29.658  1.00 53.74  ? 50  PHE C CE1 1 
ATOM   2644  C  CE2 . PHE B  1 51  ? -30.289  -3.537  28.194  1.00 54.06  ? 50  PHE C CE2 1 
ATOM   2645  C  CZ  . PHE B  1 51  ? -30.592  -3.027  29.436  1.00 52.54  ? 50  PHE C CZ  1 
ATOM   2646  N  N   . GLY B  1 52  ? -36.806  -2.378  25.753  1.00 47.64  ? 51  GLY C N   1 
ATOM   2647  C  CA  . GLY B  1 52  ? -37.797  -1.963  24.757  1.00 46.49  ? 51  GLY C CA  1 
ATOM   2648  C  C   . GLY B  1 52  ? -37.218  -0.981  23.758  1.00 46.78  ? 51  GLY C C   1 
ATOM   2649  O  O   . GLY B  1 52  ? -37.835  0.063   23.415  1.00 45.45  ? 51  GLY C O   1 
ATOM   2650  N  N   . ASP B  1 53  ? -36.049  -1.355  23.241  1.00 47.29  ? 52  ASP C N   1 
ATOM   2651  C  CA  . ASP B  1 53  ? -35.228  -0.517  22.409  1.00 45.33  ? 52  ASP C CA  1 
ATOM   2652  C  C   . ASP B  1 53  ? -35.054  -1.224  21.072  1.00 40.90  ? 52  ASP C C   1 
ATOM   2653  O  O   . ASP B  1 53  ? -34.394  -2.238  21.012  1.00 45.71  ? 52  ASP C O   1 
ATOM   2654  C  CB  . ASP B  1 53  ? -33.884  -0.269  23.095  1.00 47.77  ? 52  ASP C CB  1 
ATOM   2655  C  CG  . ASP B  1 53  ? -32.930  0.679   22.382  1.00 48.82  ? 52  ASP C CG  1 
ATOM   2656  O  OD1 . ASP B  1 53  ? -32.051  1.211   23.093  1.00 48.39  ? 52  ASP C OD1 1 
ATOM   2657  O  OD2 . ASP B  1 53  ? -33.054  0.866   21.128  1.00 46.35  ? 52  ASP C OD2 1 
ATOM   2658  N  N   . ASN B  1 54  ? -35.650  -0.671  20.020  1.00 39.43  ? 53  ASN C N   1 
ATOM   2659  C  CA  . ASN B  1 54  ? -35.565  -1.249  18.698  1.00 47.18  ? 53  ASN C CA  1 
ATOM   2660  C  C   . ASN B  1 54  ? -34.866  -0.260  17.749  1.00 46.79  ? 53  ASN C C   1 
ATOM   2661  O  O   . ASN B  1 54  ? -35.048  -0.336  16.543  1.00 47.75  ? 53  ASN C O   1 
ATOM   2662  C  CB  . ASN B  1 54  ? -36.951  -1.715  18.209  1.00 51.33  ? 53  ASN C CB  1 
ATOM   2663  C  CG  . ASN B  1 54  ? -37.532  -2.878  19.010  1.00 58.64  ? 53  ASN C CG  1 
ATOM   2664  O  OD1 . ASN B  1 54  ? -36.862  -3.503  19.844  1.00 59.53  ? 53  ASN C OD1 1 
ATOM   2665  N  ND2 . ASN B  1 54  ? -38.796  -3.193  18.768  1.00 55.61  ? 53  ASN C ND2 1 
ATOM   2666  N  N   . THR B  1 55  ? -34.028  0.634   18.298  1.00 51.08  ? 54  THR C N   1 
ATOM   2667  C  CA  . THR B  1 55  ? -33.296  1.657   17.503  1.00 52.69  ? 54  THR C CA  1 
ATOM   2668  C  C   . THR B  1 55  ? -32.439  0.995   16.414  1.00 54.52  ? 54  THR C C   1 
ATOM   2669  O  O   . THR B  1 55  ? -32.436  1.468   15.285  1.00 55.34  ? 54  THR C O   1 
ATOM   2670  C  CB  . THR B  1 55  ? -32.446  2.569   18.399  1.00 50.16  ? 54  THR C CB  1 
ATOM   2671  O  OG1 . THR B  1 55  ? -31.680  1.768   19.297  1.00 51.66  ? 54  THR C OG1 1 
ATOM   2672  C  CG2 . THR B  1 55  ? -33.288  3.529   19.208  1.00 51.35  ? 54  THR C CG2 1 
ATOM   2673  N  N   . ALA B  1 56  ? -31.742  -0.099  16.758  1.00 60.00  ? 55  ALA C N   1 
ATOM   2674  C  CA  . ALA B  1 56  ? -30.919  -0.889  15.809  1.00 64.93  ? 55  ALA C CA  1 
ATOM   2675  C  C   . ALA B  1 56  ? -31.604  -2.225  15.470  1.00 65.78  ? 55  ALA C C   1 
ATOM   2676  O  O   . ALA B  1 56  ? -30.946  -3.272  15.399  1.00 69.99  ? 55  ALA C O   1 
ATOM   2677  C  CB  . ALA B  1 56  ? -29.550  -1.120  16.408  1.00 64.09  ? 55  ALA C CB  1 
ATOM   2678  N  N   . GLY B  1 57  ? -32.923  -2.186  15.249  1.00 62.53  ? 56  GLY C N   1 
ATOM   2679  C  CA  . GLY B  1 57  ? -33.738  -3.395  15.127  1.00 54.76  ? 56  GLY C CA  1 
ATOM   2680  C  C   . GLY B  1 57  ? -33.780  -4.163  16.439  1.00 52.56  ? 56  GLY C C   1 
ATOM   2681  O  O   . GLY B  1 57  ? -33.596  -3.588  17.507  1.00 49.79  ? 56  GLY C O   1 
ATOM   2682  N  N   . CYS B  1 58  ? -33.958  -5.487  16.345  1.00 50.71  ? 57  CYS C N   1 
ATOM   2683  C  CA  . CYS B  1 58  ? -34.111  -6.372  17.509  1.00 49.74  ? 57  CYS C CA  1 
ATOM   2684  C  C   . CYS B  1 58  ? -32.802  -6.487  18.310  1.00 45.83  ? 57  CYS C C   1 
ATOM   2685  O  O   . CYS B  1 58  ? -32.822  -6.781  19.508  1.00 46.99  ? 57  CYS C O   1 
ATOM   2686  C  CB  . CYS B  1 58  ? -34.609  -7.745  17.056  1.00 53.36  ? 57  CYS C CB  1 
ATOM   2687  S  SG  . CYS B  1 58  ? -36.167  -7.685  16.120  1.00 54.25  ? 57  CYS C SG  1 
ATOM   2688  N  N   . THR B  1 59  ? -31.659  -6.236  17.665  1.00 49.53  ? 58  THR C N   1 
ATOM   2689  C  CA  . THR B  1 59  ? -30.344  -6.269  18.345  1.00 52.19  ? 58  THR C CA  1 
ATOM   2690  C  C   . THR B  1 59  ? -30.320  -5.373  19.589  1.00 51.94  ? 58  THR C C   1 
ATOM   2691  O  O   . THR B  1 59  ? -29.798  -5.770  20.631  1.00 49.19  ? 58  THR C O   1 
ATOM   2692  C  CB  . THR B  1 59  ? -29.200  -5.819  17.432  1.00 59.99  ? 58  THR C CB  1 
ATOM   2693  O  OG1 . THR B  1 59  ? -29.556  -6.059  16.069  1.00 61.65  ? 58  THR C OG1 1 
ATOM   2694  C  CG2 . THR B  1 59  ? -27.904  -6.525  17.772  1.00 63.38  ? 58  THR C CG2 1 
ATOM   2695  N  N   . SER B  1 60  ? -30.884  -4.162  19.480  1.00 50.79  ? 59  SER C N   1 
ATOM   2696  C  CA  . SER B  1 60  ? -30.842  -3.202  20.587  1.00 49.02  ? 59  SER C CA  1 
ATOM   2697  C  C   . SER B  1 60  ? -31.657  -3.685  21.793  1.00 47.40  ? 59  SER C C   1 
ATOM   2698  O  O   . SER B  1 60  ? -31.518  -3.111  22.872  1.00 44.51  ? 59  SER C O   1 
ATOM   2699  C  CB  . SER B  1 60  ? -31.264  -1.812  20.160  1.00 49.13  ? 59  SER C CB  1 
ATOM   2700  O  OG  . SER B  1 60  ? -31.765  -1.799  18.832  1.00 53.49  ? 59  SER C OG  1 
ATOM   2701  N  N   . ALA B  1 61  ? -32.477  -4.742  21.639  1.00 51.20  ? 60  ALA C N   1 
ATOM   2702  C  CA  . ALA B  1 61  ? -33.331  -5.262  22.744  1.00 49.28  ? 60  ALA C CA  1 
ATOM   2703  C  C   . ALA B  1 61  ? -32.492  -5.827  23.899  1.00 48.13  ? 60  ALA C C   1 
ATOM   2704  O  O   . ALA B  1 61  ? -33.000  -6.008  25.023  1.00 45.08  ? 60  ALA C O   1 
ATOM   2705  C  CB  . ALA B  1 61  ? -34.274  -6.319  22.217  1.00 55.43  ? 60  ALA C CB  1 
ATOM   2706  N  N   . GLY B  1 62  ? -31.221  -6.133  23.612  1.00 53.04  ? 61  GLY C N   1 
ATOM   2707  C  CA  . GLY B  1 62  ? -30.291  -6.667  24.607  1.00 53.84  ? 61  GLY C CA  1 
ATOM   2708  C  C   . GLY B  1 62  ? -30.540  -8.152  24.874  1.00 56.84  ? 61  GLY C C   1 
ATOM   2709  O  O   . GLY B  1 62  ? -31.091  -8.860  24.021  1.00 46.20  ? 61  GLY C O   1 
ATOM   2710  N  N   . PRO B  1 63  ? -30.137  -8.654  26.069  1.00 60.11  ? 62  PRO C N   1 
ATOM   2711  C  CA  . PRO B  1 63  ? -30.303  -10.063 26.434  1.00 57.83  ? 62  PRO C CA  1 
ATOM   2712  C  C   . PRO B  1 63  ? -31.704  -10.375 26.973  1.00 58.87  ? 62  PRO C C   1 
ATOM   2713  O  O   . PRO B  1 63  ? -32.519  -9.467  27.119  1.00 55.21  ? 62  PRO C O   1 
ATOM   2714  C  CB  . PRO B  1 63  ? -29.302  -10.225 27.588  1.00 57.11  ? 62  PRO C CB  1 
ATOM   2715  C  CG  . PRO B  1 63  ? -29.376  -8.882  28.292  1.00 58.48  ? 62  PRO C CG  1 
ATOM   2716  C  CD  . PRO B  1 63  ? -29.499  -7.882  27.154  1.00 58.99  ? 62  PRO C CD  1 
ATOM   2717  N  N   . HIS B  1 64  ? -31.931  -11.643 27.330  1.00 54.64  ? 63  HIS C N   1 
ATOM   2718  C  CA  . HIS B  1 64  ? -33.192  -12.074 27.912  1.00 53.95  ? 63  HIS C CA  1 
ATOM   2719  C  C   . HIS B  1 64  ? -33.428  -11.252 29.185  1.00 54.39  ? 63  HIS C C   1 
ATOM   2720  O  O   . HIS B  1 64  ? -32.489  -11.027 29.944  1.00 53.67  ? 63  HIS C O   1 
ATOM   2721  C  CB  . HIS B  1 64  ? -33.191  -13.604 28.150  1.00 54.01  ? 63  HIS C CB  1 
ATOM   2722  C  CG  . HIS B  1 64  ? -33.031  -14.429 26.909  1.00 54.45  ? 63  HIS C CG  1 
ATOM   2723  N  ND1 . HIS B  1 64  ? -32.907  -15.821 26.928  1.00 52.58  ? 63  HIS C ND1 1 
ATOM   2724  C  CD2 . HIS B  1 64  ? -32.943  -14.069 25.608  1.00 56.12  ? 63  HIS C CD2 1 
ATOM   2725  C  CE1 . HIS B  1 64  ? -32.775  -16.261 25.692  1.00 54.83  ? 63  HIS C CE1 1 
ATOM   2726  N  NE2 . HIS B  1 64  ? -32.784  -15.208 24.861  1.00 54.99  ? 63  HIS C NE2 1 
ATOM   2727  N  N   . PHE B  1 65  ? -34.664  -10.774 29.393  1.00 48.77  ? 64  PHE C N   1 
ATOM   2728  C  CA  . PHE B  1 65  ? -35.043  -10.205 30.670  1.00 50.66  ? 64  PHE C CA  1 
ATOM   2729  C  C   . PHE B  1 65  ? -34.743  -11.236 31.764  1.00 57.87  ? 64  PHE C C   1 
ATOM   2730  O  O   . PHE B  1 65  ? -35.376  -12.299 31.818  1.00 58.80  ? 64  PHE C O   1 
ATOM   2731  C  CB  . PHE B  1 65  ? -36.513  -9.776  30.691  1.00 50.27  ? 64  PHE C CB  1 
ATOM   2732  C  CG  . PHE B  1 65  ? -36.988  -9.131  31.974  1.00 50.08  ? 64  PHE C CG  1 
ATOM   2733  C  CD1 . PHE B  1 65  ? -38.193  -9.504  32.549  1.00 48.40  ? 64  PHE C CD1 1 
ATOM   2734  C  CD2 . PHE B  1 65  ? -36.259  -8.119  32.591  1.00 50.10  ? 64  PHE C CD2 1 
ATOM   2735  C  CE1 . PHE B  1 65  ? -38.650  -8.907  33.715  1.00 50.03  ? 64  PHE C CE1 1 
ATOM   2736  C  CE2 . PHE B  1 65  ? -36.722  -7.517  33.754  1.00 46.53  ? 64  PHE C CE2 1 
ATOM   2737  C  CZ  . PHE B  1 65  ? -37.918  -7.908  34.314  1.00 49.61  ? 64  PHE C CZ  1 
ATOM   2738  N  N   . ASN B  1 66  ? -33.782  -10.896 32.636  1.00 58.77  ? 65  ASN C N   1 
ATOM   2739  C  CA  . ASN B  1 66  ? -33.206  -11.835 33.593  1.00 61.74  ? 65  ASN C CA  1 
ATOM   2740  C  C   . ASN B  1 66  ? -32.946  -11.114 34.915  1.00 63.29  ? 65  ASN C C   1 
ATOM   2741  O  O   . ASN B  1 66  ? -31.808  -11.022 35.369  1.00 62.08  ? 65  ASN C O   1 
ATOM   2742  C  CB  . ASN B  1 66  ? -31.952  -12.492 33.002  1.00 61.49  ? 65  ASN C CB  1 
ATOM   2743  C  CG  . ASN B  1 66  ? -31.256  -13.471 33.931  1.00 63.75  ? 65  ASN C CG  1 
ATOM   2744  O  OD1 . ASN B  1 66  ? -30.085  -13.788 33.722  1.00 60.53  ? 65  ASN C OD1 1 
ATOM   2745  N  ND2 . ASN B  1 66  ? -31.953  -13.949 34.952  1.00 53.82  ? 65  ASN C ND2 1 
ATOM   2746  N  N   . PRO B  1 67  ? -33.994  -10.590 35.586  1.00 64.11  ? 66  PRO C N   1 
ATOM   2747  C  CA  . PRO B  1 67  ? -33.823  -9.900  36.868  1.00 66.44  ? 66  PRO C CA  1 
ATOM   2748  C  C   . PRO B  1 67  ? -33.444  -10.746 38.101  1.00 71.01  ? 66  PRO C C   1 
ATOM   2749  O  O   . PRO B  1 67  ? -33.482  -10.222 39.212  1.00 74.50  ? 66  PRO C O   1 
ATOM   2750  C  CB  . PRO B  1 67  ? -35.224  -9.300  37.099  1.00 64.57  ? 66  PRO C CB  1 
ATOM   2751  C  CG  . PRO B  1 67  ? -36.149  -10.274 36.409  1.00 62.91  ? 66  PRO C CG  1 
ATOM   2752  C  CD  . PRO B  1 67  ? -35.396  -10.631 35.145  1.00 63.85  ? 66  PRO C CD  1 
ATOM   2753  N  N   . LEU B  1 68  ? -33.109  -12.034 37.929  1.00 75.77  ? 67  LEU C N   1 
ATOM   2754  C  CA  . LEU B  1 68  ? -32.677  -12.888 39.059  1.00 75.65  ? 67  LEU C CA  1 
ATOM   2755  C  C   . LEU B  1 68  ? -31.314  -13.549 38.774  1.00 74.74  ? 67  LEU C C   1 
ATOM   2756  O  O   . LEU B  1 68  ? -30.889  -14.435 39.517  1.00 77.98  ? 67  LEU C O   1 
ATOM   2757  C  CB  . LEU B  1 68  ? -33.770  -13.927 39.348  1.00 78.97  ? 67  LEU C CB  1 
ATOM   2758  C  CG  . LEU B  1 68  ? -35.117  -13.374 39.824  1.00 79.28  ? 67  LEU C CG  1 
ATOM   2759  C  CD1 . LEU B  1 68  ? -36.136  -14.492 39.987  1.00 77.77  ? 67  LEU C CD1 1 
ATOM   2760  C  CD2 . LEU B  1 68  ? -34.975  -12.603 41.130  1.00 79.38  ? 67  LEU C CD2 1 
ATOM   2761  N  N   . SER B  1 69  ? -30.628  -13.104 37.711  1.00 74.94  ? 68  SER C N   1 
ATOM   2762  C  CA  . SER B  1 69  ? -29.215  -13.431 37.428  1.00 82.29  ? 68  SER C CA  1 
ATOM   2763  C  C   . SER B  1 69  ? -29.017  -14.921 37.105  1.00 82.94  ? 68  SER C C   1 
ATOM   2764  O  O   . SER B  1 69  ? -27.879  -15.401 37.157  1.00 83.93  ? 68  SER C O   1 
ATOM   2765  C  CB  . SER B  1 69  ? -28.318  -13.021 38.578  1.00 84.02  ? 68  SER C CB  1 
ATOM   2766  O  OG  . SER B  1 69  ? -28.753  -11.805 39.174  1.00 87.17  ? 68  SER C OG  1 
ATOM   2767  N  N   . ARG B  1 70  ? -30.100  -15.629 36.745  1.00 79.90  ? 69  ARG C N   1 
ATOM   2768  C  CA  . ARG B  1 70  ? -30.104  -17.099 36.592  1.00 73.60  ? 69  ARG C CA  1 
ATOM   2769  C  C   . ARG B  1 70  ? -29.662  -17.502 35.179  1.00 71.09  ? 69  ARG C C   1 
ATOM   2770  O  O   . ARG B  1 70  ? -29.464  -16.658 34.311  1.00 67.14  ? 69  ARG C O   1 
ATOM   2771  C  CB  . ARG B  1 70  ? -31.490  -17.659 36.920  1.00 68.34  ? 69  ARG C CB  1 
ATOM   2772  C  CG  . ARG B  1 70  ? -32.026  -17.180 38.261  1.00 70.12  ? 69  ARG C CG  1 
ATOM   2773  C  CD  . ARG B  1 70  ? -32.900  -18.212 38.935  1.00 72.74  ? 69  ARG C CD  1 
ATOM   2774  N  NE  . ARG B  1 70  ? -33.523  -17.702 40.147  1.00 72.75  ? 69  ARG C NE  1 
ATOM   2775  C  CZ  . ARG B  1 70  ? -34.593  -18.242 40.721  1.00 77.67  ? 69  ARG C CZ  1 
ATOM   2776  N  NH1 . ARG B  1 70  ? -35.088  -17.722 41.831  1.00 79.74  ? 69  ARG C NH1 1 
ATOM   2777  N  NH2 . ARG B  1 70  ? -35.169  -19.303 40.184  1.00 78.40  ? 69  ARG C NH2 1 
ATOM   2778  N  N   . LYS B  1 71  ? -29.482  -18.815 34.986  1.00 75.83  ? 70  LYS C N   1 
ATOM   2779  C  CA  . LYS B  1 71  ? -29.125  -19.411 33.690  1.00 79.04  ? 70  LYS C CA  1 
ATOM   2780  C  C   . LYS B  1 71  ? -30.398  -19.539 32.836  1.00 72.44  ? 70  LYS C C   1 
ATOM   2781  O  O   . LYS B  1 71  ? -31.524  -19.643 33.374  1.00 60.80  ? 70  LYS C O   1 
ATOM   2782  C  CB  . LYS B  1 71  ? -28.465  -20.784 33.882  1.00 88.97  ? 70  LYS C CB  1 
ATOM   2783  C  CG  . LYS B  1 71  ? -27.365  -20.868 34.938  1.00 92.39  ? 70  LYS C CG  1 
ATOM   2784  C  CD  . LYS B  1 71  ? -26.197  -19.936 34.699  1.00 98.35  ? 70  LYS C CD  1 
ATOM   2785  C  CE  . LYS B  1 71  ? -25.395  -20.302 33.470  1.00 102.62 ? 70  LYS C CE  1 
ATOM   2786  N  NZ  . LYS B  1 71  ? -24.189  -19.452 33.332  1.00 108.09 ? 70  LYS C NZ  1 
ATOM   2787  N  N   . HIS B  1 72  ? -30.222  -19.527 31.507  1.00 66.87  ? 71  HIS C N   1 
ATOM   2788  C  CA  . HIS B  1 72  ? -31.340  -19.721 30.581  1.00 65.83  ? 71  HIS C CA  1 
ATOM   2789  C  C   . HIS B  1 72  ? -31.940  -21.117 30.797  1.00 64.12  ? 71  HIS C C   1 
ATOM   2790  O  O   . HIS B  1 72  ? -31.217  -22.085 31.045  1.00 61.33  ? 71  HIS C O   1 
ATOM   2791  C  CB  . HIS B  1 72  ? -30.912  -19.526 29.117  1.00 64.61  ? 71  HIS C CB  1 
ATOM   2792  C  CG  . HIS B  1 72  ? -31.998  -19.838 28.138  1.00 67.80  ? 71  HIS C CG  1 
ATOM   2793  N  ND1 . HIS B  1 72  ? -33.090  -19.002 27.924  1.00 67.28  ? 71  HIS C ND1 1 
ATOM   2794  C  CD2 . HIS B  1 72  ? -32.180  -20.908 27.333  1.00 68.72  ? 71  HIS C CD2 1 
ATOM   2795  C  CE1 . HIS B  1 72  ? -33.879  -19.544 27.021  1.00 66.26  ? 71  HIS C CE1 1 
ATOM   2796  N  NE2 . HIS B  1 72  ? -33.344  -20.710 26.644  1.00 69.19  ? 71  HIS C NE2 1 
ATOM   2797  N  N   . GLY B  1 73  ? -33.270  -21.202 30.706  1.00 59.47  ? 72  GLY C N   1 
ATOM   2798  C  CA  . GLY B  1 73  ? -33.978  -22.477 30.719  1.00 60.49  ? 72  GLY C CA  1 
ATOM   2799  C  C   . GLY B  1 73  ? -35.253  -22.430 29.894  1.00 58.06  ? 72  GLY C C   1 
ATOM   2800  O  O   . GLY B  1 73  ? -35.507  -21.466 29.161  1.00 57.61  ? 72  GLY C O   1 
ATOM   2801  N  N   . GLY B  1 74  ? -36.045  -23.502 30.005  1.00 59.82  ? 73  GLY C N   1 
ATOM   2802  C  CA  . GLY B  1 74  ? -37.391  -23.553 29.448  1.00 59.26  ? 73  GLY C CA  1 
ATOM   2803  C  C   . GLY B  1 74  ? -38.408  -22.986 30.433  1.00 57.18  ? 73  GLY C C   1 
ATOM   2804  O  O   . GLY B  1 74  ? -38.145  -22.916 31.634  1.00 58.17  ? 73  GLY C O   1 
ATOM   2805  N  N   . PRO B  1 75  ? -39.599  -22.560 29.962  1.00 54.39  ? 74  PRO C N   1 
ATOM   2806  C  CA  . PRO B  1 75  ? -40.591  -21.941 30.840  1.00 57.01  ? 74  PRO C CA  1 
ATOM   2807  C  C   . PRO B  1 75  ? -40.928  -22.756 32.106  1.00 60.33  ? 74  PRO C C   1 
ATOM   2808  O  O   . PRO B  1 75  ? -41.210  -22.163 33.150  1.00 56.43  ? 74  PRO C O   1 
ATOM   2809  C  CB  . PRO B  1 75  ? -41.832  -21.748 29.942  1.00 55.19  ? 74  PRO C CB  1 
ATOM   2810  C  CG  . PRO B  1 75  ? -41.560  -22.551 28.686  1.00 53.40  ? 74  PRO C CG  1 
ATOM   2811  C  CD  . PRO B  1 75  ? -40.052  -22.644 28.568  1.00 55.18  ? 74  PRO C CD  1 
ATOM   2812  N  N   . LYS B  1 76  ? -40.883  -24.093 32.027  1.00 63.77  ? 75  LYS C N   1 
ATOM   2813  C  CA  . LYS B  1 76  ? -41.299  -24.944 33.152  1.00 70.85  ? 75  LYS C CA  1 
ATOM   2814  C  C   . LYS B  1 76  ? -40.137  -25.168 34.138  1.00 68.43  ? 75  LYS C C   1 
ATOM   2815  O  O   . LYS B  1 76  ? -40.361  -25.646 35.249  1.00 65.23  ? 75  LYS C O   1 
ATOM   2816  C  CB  . LYS B  1 76  ? -41.873  -26.257 32.616  1.00 79.32  ? 75  LYS C CB  1 
ATOM   2817  C  CG  . LYS B  1 76  ? -42.630  -27.109 33.632  1.00 92.08  ? 75  LYS C CG  1 
ATOM   2818  C  CD  . LYS B  1 76  ? -43.777  -26.395 34.331  1.00 98.70  ? 75  LYS C CD  1 
ATOM   2819  C  CE  . LYS B  1 76  ? -43.422  -25.928 35.729  1.00 100.12 ? 75  LYS C CE  1 
ATOM   2820  N  NZ  . LYS B  1 76  ? -44.584  -25.324 36.420  1.00 102.27 ? 75  LYS C NZ  1 
ATOM   2821  N  N   . ASP B  1 77  ? -38.909  -24.802 33.744  1.00 68.56  ? 76  ASP C N   1 
ATOM   2822  C  CA  . ASP B  1 77  ? -37.719  -24.883 34.615  1.00 68.80  ? 76  ASP C CA  1 
ATOM   2823  C  C   . ASP B  1 77  ? -37.814  -23.852 35.751  1.00 73.02  ? 76  ASP C C   1 
ATOM   2824  O  O   . ASP B  1 77  ? -38.341  -22.750 35.571  1.00 71.71  ? 76  ASP C O   1 
ATOM   2825  C  CB  . ASP B  1 77  ? -36.424  -24.687 33.818  1.00 65.32  ? 76  ASP C CB  1 
ATOM   2826  C  CG  . ASP B  1 77  ? -36.234  -25.721 32.721  1.00 65.63  ? 76  ASP C CG  1 
ATOM   2827  O  OD1 . ASP B  1 77  ? -35.435  -25.471 31.793  1.00 65.35  ? 76  ASP C OD1 1 
ATOM   2828  O  OD2 . ASP B  1 77  ? -36.897  -26.765 32.800  1.00 66.88  ? 76  ASP C OD2 1 
ATOM   2829  N  N   . GLU B  1 78  ? -37.287  -24.236 36.922  1.00 80.67  ? 77  GLU C N   1 
ATOM   2830  C  CA  . GLU B  1 78  ? -37.062  -23.336 38.061  1.00 79.62  ? 77  GLU C CA  1 
ATOM   2831  C  C   . GLU B  1 78  ? -35.887  -22.407 37.718  1.00 72.53  ? 77  GLU C C   1 
ATOM   2832  O  O   . GLU B  1 78  ? -35.954  -21.212 37.964  1.00 70.52  ? 77  GLU C O   1 
ATOM   2833  C  CB  . GLU B  1 78  ? -36.799  -24.150 39.333  1.00 89.50  ? 77  GLU C CB  1 
ATOM   2834  C  CG  . GLU B  1 78  ? -37.985  -24.208 40.285  1.00 99.19  ? 77  GLU C CG  1 
ATOM   2835  C  CD  . GLU B  1 78  ? -37.919  -23.237 41.456  1.00 110.10 ? 77  GLU C CD  1 
ATOM   2836  O  OE1 . GLU B  1 78  ? -38.816  -22.368 41.564  1.00 110.98 ? 77  GLU C OE1 1 
ATOM   2837  O  OE2 . GLU B  1 78  ? -36.974  -23.354 42.266  1.00 114.77 ? 77  GLU C OE2 1 
ATOM   2838  N  N   . GLU B  1 79  ? -34.836  -22.982 37.118  1.00 72.34  ? 78  GLU C N   1 
ATOM   2839  C  CA  . GLU B  1 79  ? -33.665  -22.255 36.599  1.00 74.38  ? 78  GLU C CA  1 
ATOM   2840  C  C   . GLU B  1 79  ? -33.949  -21.761 35.171  1.00 70.72  ? 78  GLU C C   1 
ATOM   2841  O  O   . GLU B  1 79  ? -33.627  -22.434 34.180  1.00 67.84  ? 78  GLU C O   1 
ATOM   2842  C  CB  . GLU B  1 79  ? -32.423  -23.151 36.638  1.00 74.77  ? 78  GLU C CB  1 
ATOM   2843  C  CG  . GLU B  1 79  ? -31.130  -22.424 36.313  1.00 76.45  ? 78  GLU C CG  1 
ATOM   2844  C  CD  . GLU B  1 79  ? -30.678  -21.401 37.346  1.00 78.00  ? 78  GLU C CD  1 
ATOM   2845  O  OE1 . GLU B  1 79  ? -31.316  -21.297 38.418  1.00 75.44  ? 78  GLU C OE1 1 
ATOM   2846  O  OE2 . GLU B  1 79  ? -29.681  -20.706 37.073  1.00 77.69  ? 78  GLU C OE2 1 
ATOM   2847  N  N   . ARG B  1 80  ? -34.536  -20.560 35.093  1.00 68.54  ? 79  ARG C N   1 
ATOM   2848  C  CA  . ARG B  1 80  ? -34.843  -19.862 33.841  1.00 65.15  ? 79  ARG C CA  1 
ATOM   2849  C  C   . ARG B  1 80  ? -34.673  -18.350 34.044  1.00 62.29  ? 79  ARG C C   1 
ATOM   2850  O  O   . ARG B  1 80  ? -34.756  -17.856 35.168  1.00 64.89  ? 79  ARG C O   1 
ATOM   2851  C  CB  . ARG B  1 80  ? -36.286  -20.166 33.418  1.00 61.24  ? 79  ARG C CB  1 
ATOM   2852  C  CG  . ARG B  1 80  ? -37.328  -19.787 34.465  1.00 58.43  ? 79  ARG C CG  1 
ATOM   2853  C  CD  . ARG B  1 80  ? -38.762  -19.843 33.961  1.00 59.40  ? 79  ARG C CD  1 
ATOM   2854  N  NE  . ARG B  1 80  ? -39.193  -18.657 33.227  1.00 56.09  ? 79  ARG C NE  1 
ATOM   2855  C  CZ  . ARG B  1 80  ? -40.440  -18.447 32.808  1.00 58.77  ? 79  ARG C CZ  1 
ATOM   2856  N  NH1 . ARG B  1 80  ? -40.755  -17.333 32.161  1.00 53.07  ? 79  ARG C NH1 1 
ATOM   2857  N  NH2 . ARG B  1 80  ? -41.372  -19.357 33.042  1.00 54.62  ? 79  ARG C NH2 1 
ATOM   2858  N  N   . HIS B  1 81  ? -34.459  -17.623 32.941  1.00 59.96  ? 80  HIS C N   1 
ATOM   2859  C  CA  . HIS B  1 81  ? -34.681  -16.172 32.896  1.00 57.91  ? 80  HIS C CA  1 
ATOM   2860  C  C   . HIS B  1 81  ? -36.184  -15.901 33.028  1.00 59.56  ? 80  HIS C C   1 
ATOM   2861  O  O   . HIS B  1 81  ? -36.995  -16.753 32.645  1.00 62.28  ? 80  HIS C O   1 
ATOM   2862  C  CB  . HIS B  1 81  ? -34.141  -15.583 31.590  1.00 57.55  ? 80  HIS C CB  1 
ATOM   2863  C  CG  . HIS B  1 81  ? -32.719  -15.928 31.307  1.00 59.41  ? 80  HIS C CG  1 
ATOM   2864  N  ND1 . HIS B  1 81  ? -32.214  -16.047 30.018  1.00 60.11  ? 80  HIS C ND1 1 
ATOM   2865  C  CD2 . HIS B  1 81  ? -31.691  -16.178 32.147  1.00 58.80  ? 80  HIS C CD2 1 
ATOM   2866  C  CE1 . HIS B  1 81  ? -30.919  -16.294 30.090  1.00 58.58  ? 80  HIS C CE1 1 
ATOM   2867  N  NE2 . HIS B  1 81  ? -30.582  -16.410 31.379  1.00 59.52  ? 80  HIS C NE2 1 
ATOM   2868  N  N   . VAL B  1 82  ? -36.566  -14.726 33.548  1.00 56.66  ? 81  VAL C N   1 
ATOM   2869  C  CA  . VAL B  1 82  ? -37.993  -14.350 33.601  1.00 56.37  ? 81  VAL C CA  1 
ATOM   2870  C  C   . VAL B  1 82  ? -38.549  -14.352 32.162  1.00 52.95  ? 81  VAL C C   1 
ATOM   2871  O  O   . VAL B  1 82  ? -39.694  -14.775 31.915  1.00 51.93  ? 81  VAL C O   1 
ATOM   2872  C  CB  . VAL B  1 82  ? -38.221  -13.008 34.327  1.00 57.14  ? 81  VAL C CB  1 
ATOM   2873  C  CG1 . VAL B  1 82  ? -39.553  -12.365 33.959  1.00 56.23  ? 81  VAL C CG1 1 
ATOM   2874  C  CG2 . VAL B  1 82  ? -38.151  -13.181 35.838  1.00 58.52  ? 81  VAL C CG2 1 
ATOM   2875  N  N   . GLY B  1 83  ? -37.708  -13.948 31.202  1.00 49.51  ? 82  GLY C N   1 
ATOM   2876  C  CA  . GLY B  1 83  ? -38.106  -13.821 29.806  1.00 51.94  ? 82  GLY C CA  1 
ATOM   2877  C  C   . GLY B  1 83  ? -38.080  -15.120 28.996  1.00 52.31  ? 82  GLY C C   1 
ATOM   2878  O  O   . GLY B  1 83  ? -38.297  -15.067 27.795  1.00 47.37  ? 82  GLY C O   1 
ATOM   2879  N  N   A SER B  1 84  ? -37.800  -16.275 29.614  0.70 55.35  ? 83  SER C N   1 
ATOM   2880  C  CA  A SER B  1 84  ? -37.574  -17.512 28.836  0.70 57.08  ? 83  SER C CA  1 
ATOM   2881  C  C   A SER B  1 84  ? -38.916  -18.214 28.582  0.70 55.83  ? 83  SER C C   1 
ATOM   2882  O  O   A SER B  1 84  ? -39.708  -18.542 29.266  0.70 57.91  ? 83  SER C O   1 
ATOM   2883  C  CB  A SER B  1 84  ? -36.501  -18.379 29.489  0.70 59.72  ? 83  SER C CB  1 
ATOM   2884  O  OG  A SER B  1 84  ? -35.175  -17.913 29.158  0.70 62.48  ? 83  SER C OG  1 
ATOM   2885  N  N   B ASP B  1 84  ? -37.848  -16.254 29.675  0.30 48.53  ? 83  ASP C N   1 
ATOM   2886  C  CA  B ASP B  1 84  ? -37.706  -17.555 29.039  0.30 47.87  ? 83  ASP C CA  1 
ATOM   2887  C  C   B ASP B  1 84  ? -39.079  -18.176 28.811  0.30 49.39  ? 83  ASP C C   1 
ATOM   2888  O  O   B ASP B  1 84  ? -39.618  -18.809 29.724  0.30 49.70  ? 83  ASP C O   1 
ATOM   2889  C  CB  B ASP B  1 84  ? -36.914  -18.522 29.918  0.30 45.92  ? 83  ASP C CB  1 
ATOM   2890  C  CG  B ASP B  1 84  ? -35.437  -18.211 29.888  0.30 46.13  ? 83  ASP C CG  1 
ATOM   2891  O  OD1 B ASP B  1 84  ? -35.084  -17.278 29.158  0.30 50.21  ? 83  ASP C OD1 1 
ATOM   2892  O  OD2 B ASP B  1 84  ? -34.669  -18.889 30.586  0.30 43.51  ? 83  ASP C OD2 1 
ATOM   2893  N  N   . LEU B  1 85  ? -39.637  -17.998 27.610  1.00 49.82  ? 84  LEU C N   1 
ATOM   2894  C  CA  . LEU B  1 85  ? -41.013  -18.523 27.346  1.00 52.85  ? 84  LEU C CA  1 
ATOM   2895  C  C   . LEU B  1 85  ? -40.996  -19.686 26.344  1.00 51.25  ? 84  LEU C C   1 
ATOM   2896  O  O   . LEU B  1 85  ? -42.039  -20.018 25.789  1.00 50.51  ? 84  LEU C O   1 
ATOM   2897  C  CB  . LEU B  1 85  ? -41.898  -17.393 26.798  1.00 51.42  ? 84  LEU C CB  1 
ATOM   2898  C  CG  . LEU B  1 85  ? -42.174  -16.223 27.737  1.00 49.07  ? 84  LEU C CG  1 
ATOM   2899  C  CD1 . LEU B  1 85  ? -42.941  -15.124 27.012  1.00 51.22  ? 84  LEU C CD1 1 
ATOM   2900  C  CD2 . LEU B  1 85  ? -42.929  -16.677 28.975  1.00 52.53  ? 84  LEU C CD2 1 
ATOM   2901  N  N   . GLY B  1 86  ? -39.819  -20.261 26.078  1.00 50.08  ? 85  GLY C N   1 
ATOM   2902  C  CA  . GLY B  1 86  ? -39.710  -21.521 25.344  1.00 46.30  ? 85  GLY C CA  1 
ATOM   2903  C  C   . GLY B  1 86  ? -39.822  -21.333 23.843  1.00 48.46  ? 85  GLY C C   1 
ATOM   2904  O  O   . GLY B  1 86  ? -39.164  -20.466 23.247  1.00 44.05  ? 85  GLY C O   1 
ATOM   2905  N  N   . ASN B  1 87  ? -40.665  -22.172 23.225  1.00 46.06  ? 86  ASN C N   1 
ATOM   2906  C  CA  . ASN B  1 87  ? -40.761  -22.264 21.781  1.00 41.66  ? 86  ASN C CA  1 
ATOM   2907  C  C   . ASN B  1 87  ? -42.210  -22.037 21.351  1.00 37.30  ? 86  ASN C C   1 
ATOM   2908  O  O   . ASN B  1 87  ? -43.123  -22.420 22.038  1.00 38.47  ? 86  ASN C O   1 
ATOM   2909  C  CB  . ASN B  1 87  ? -40.287  -23.623 21.259  1.00 43.66  ? 86  ASN C CB  1 
ATOM   2910  C  CG  . ASN B  1 87  ? -38.787  -23.789 21.341  1.00 46.97  ? 86  ASN C CG  1 
ATOM   2911  O  OD1 . ASN B  1 87  ? -38.062  -23.215 20.531  1.00 45.45  ? 86  ASN C OD1 1 
ATOM   2912  N  ND2 . ASN B  1 87  ? -38.322  -24.569 22.307  1.00 45.17  ? 86  ASN C ND2 1 
ATOM   2913  N  N   . VAL B  1 88  ? -42.372  -21.419 20.186  1.00 34.19  ? 87  VAL C N   1 
ATOM   2914  C  CA  . VAL B  1 88  ? -43.602  -21.426 19.452  1.00 38.20  ? 87  VAL C CA  1 
ATOM   2915  C  C   . VAL B  1 88  ? -43.333  -22.300 18.232  1.00 38.61  ? 87  VAL C C   1 
ATOM   2916  O  O   . VAL B  1 88  ? -42.201  -22.345 17.754  1.00 38.79  ? 87  VAL C O   1 
ATOM   2917  C  CB  . VAL B  1 88  ? -44.072  -20.003 19.082  1.00 38.21  ? 87  VAL C CB  1 
ATOM   2918  C  CG1 . VAL B  1 88  ? -44.194  -19.137 20.326  1.00 38.83  ? 87  VAL C CG1 1 
ATOM   2919  C  CG2 . VAL B  1 88  ? -43.176  -19.330 18.054  1.00 39.08  ? 87  VAL C CG2 1 
ATOM   2920  N  N   . THR B  1 89  ? -44.378  -22.981 17.755  1.00 37.95  ? 88  THR C N   1 
ATOM   2921  C  CA  . THR B  1 89  ? -44.273  -23.911 16.649  1.00 38.38  ? 88  THR C CA  1 
ATOM   2922  C  C   . THR B  1 89  ? -45.006  -23.356 15.426  1.00 35.86  ? 88  THR C C   1 
ATOM   2923  O  O   . THR B  1 89  ? -46.213  -23.100 15.472  1.00 36.57  ? 88  THR C O   1 
ATOM   2924  C  CB  . THR B  1 89  ? -44.797  -25.293 17.072  1.00 39.21  ? 88  THR C CB  1 
ATOM   2925  O  OG1 . THR B  1 89  ? -44.002  -25.703 18.187  1.00 39.00  ? 88  THR C OG1 1 
ATOM   2926  C  CG2 . THR B  1 89  ? -44.718  -26.317 15.958  1.00 38.84  ? 88  THR C CG2 1 
ATOM   2927  N  N   . ALA B  1 90  ? -44.263  -23.178 14.331  1.00 34.63  ? 89  ALA C N   1 
ATOM   2928  C  CA  . ALA B  1 90  ? -44.819  -22.778 13.067  1.00 36.79  ? 89  ALA C CA  1 
ATOM   2929  C  C   . ALA B  1 90  ? -45.214  -24.038 12.298  1.00 40.24  ? 89  ALA C C   1 
ATOM   2930  O  O   . ALA B  1 90  ? -44.423  -24.960 12.192  1.00 37.53  ? 89  ALA C O   1 
ATOM   2931  C  CB  . ALA B  1 90  ? -43.834  -21.970 12.268  1.00 37.63  ? 89  ALA C CB  1 
ATOM   2932  N  N   . ASP B  1 91  ? -46.431  -24.027 11.753  1.00 40.49  ? 90  ASP C N   1 
ATOM   2933  C  CA  . ASP B  1 91  ? -46.927  -25.101 10.906  1.00 44.21  ? 90  ASP C CA  1 
ATOM   2934  C  C   . ASP B  1 91  ? -46.285  -24.981 9.520   1.00 44.31  ? 90  ASP C C   1 
ATOM   2935  O  O   . ASP B  1 91  ? -45.434  -24.129 9.279   1.00 42.24  ? 90  ASP C O   1 
ATOM   2936  C  CB  . ASP B  1 91  ? -48.460  -25.097 10.834  1.00 42.33  ? 90  ASP C CB  1 
ATOM   2937  C  CG  . ASP B  1 91  ? -49.084  -23.904 10.118  1.00 43.67  ? 90  ASP C CG  1 
ATOM   2938  O  OD1 . ASP B  1 91  ? -50.254  -23.608 10.418  1.00 44.65  ? 90  ASP C OD1 1 
ATOM   2939  O  OD2 . ASP B  1 91  ? -48.416  -23.293 9.257   1.00 42.42  ? 90  ASP C OD2 1 
ATOM   2940  N  N   . LYS B  1 92  ? -46.750  -25.838 8.614   1.00 46.28  ? 91  LYS C N   1 
ATOM   2941  C  CA  . LYS B  1 92  ? -46.215  -25.995 7.266   1.00 51.51  ? 91  LYS C CA  1 
ATOM   2942  C  C   . LYS B  1 92  ? -46.499  -24.746 6.415   1.00 49.19  ? 91  LYS C C   1 
ATOM   2943  O  O   . LYS B  1 92  ? -45.888  -24.581 5.381   1.00 48.82  ? 91  LYS C O   1 
ATOM   2944  C  CB  . LYS B  1 92  ? -46.764  -27.303 6.678   1.00 57.75  ? 91  LYS C CB  1 
ATOM   2945  C  CG  . LYS B  1 92  ? -47.550  -27.199 5.375   1.00 69.17  ? 91  LYS C CG  1 
ATOM   2946  C  CD  . LYS B  1 92  ? -49.058  -27.250 5.561   1.00 75.50  ? 91  LYS C CD  1 
ATOM   2947  C  CE  . LYS B  1 92  ? -49.779  -27.943 4.425   1.00 76.88  ? 91  LYS C CE  1 
ATOM   2948  N  NZ  . LYS B  1 92  ? -51.195  -27.516 4.350   1.00 80.42  ? 91  LYS C NZ  1 
ATOM   2949  N  N   . ASP B  1 93  ? -47.418  -23.872 6.838   1.00 49.26  ? 92  ASP C N   1 
ATOM   2950  C  CA  . ASP B  1 93  ? -47.688  -22.624 6.098   1.00 50.49  ? 92  ASP C CA  1 
ATOM   2951  C  C   . ASP B  1 93  ? -46.910  -21.440 6.695   1.00 44.97  ? 92  ASP C C   1 
ATOM   2952  O  O   . ASP B  1 93  ? -47.063  -20.329 6.231   1.00 44.49  ? 92  ASP C O   1 
ATOM   2953  C  CB  . ASP B  1 93  ? -49.177  -22.282 6.098   1.00 56.31  ? 92  ASP C CB  1 
ATOM   2954  C  CG  . ASP B  1 93  ? -50.055  -23.327 5.431   1.00 60.20  ? 92  ASP C CG  1 
ATOM   2955  O  OD1 . ASP B  1 93  ? -51.110  -23.636 6.006   1.00 62.85  ? 92  ASP C OD1 1 
ATOM   2956  O  OD2 . ASP B  1 93  ? -49.688  -23.808 4.340   1.00 60.08  ? 92  ASP C OD2 1 
ATOM   2957  N  N   . GLY B  1 94  ? -46.129  -21.684 7.748   1.00 43.24  ? 93  GLY C N   1 
ATOM   2958  C  CA  . GLY B  1 94  ? -45.284  -20.665 8.376   1.00 45.03  ? 93  GLY C CA  1 
ATOM   2959  C  C   . GLY B  1 94  ? -45.978  -19.920 9.503   1.00 44.76  ? 93  GLY C C   1 
ATOM   2960  O  O   . GLY B  1 94  ? -45.442  -18.914 10.008  1.00 41.80  ? 93  GLY C O   1 
ATOM   2961  N  N   . VAL B  1 95  ? -47.144  -20.435 9.925   1.00 41.09  ? 94  VAL C N   1 
ATOM   2962  C  CA  . VAL B  1 95  ? -47.986  -19.808 10.935  1.00 38.93  ? 94  VAL C CA  1 
ATOM   2963  C  C   . VAL B  1 95  ? -47.801  -20.528 12.269  1.00 38.47  ? 94  VAL C C   1 
ATOM   2964  O  O   . VAL B  1 95  ? -48.017  -21.742 12.369  1.00 36.58  ? 94  VAL C O   1 
ATOM   2965  C  CB  . VAL B  1 95  ? -49.470  -19.808 10.526  1.00 42.56  ? 94  VAL C CB  1 
ATOM   2966  C  CG1 . VAL B  1 95  ? -50.339  -19.131 11.584  1.00 43.17  ? 94  VAL C CG1 1 
ATOM   2967  C  CG2 . VAL B  1 95  ? -49.675  -19.163 9.171   1.00 41.36  ? 94  VAL C CG2 1 
ATOM   2968  N  N   . ALA B  1 96  ? -47.404  -19.759 13.289  1.00 35.85  ? 95  ALA C N   1 
ATOM   2969  C  CA  . ALA B  1 96  ? -47.403  -20.203 14.649  1.00 37.88  ? 95  ALA C CA  1 
ATOM   2970  C  C   . ALA B  1 96  ? -48.535  -19.487 15.381  1.00 40.64  ? 95  ALA C C   1 
ATOM   2971  O  O   . ALA B  1 96  ? -48.474  -18.266 15.566  1.00 39.23  ? 95  ALA C O   1 
ATOM   2972  C  CB  . ALA B  1 96  ? -46.071  -19.920 15.293  1.00 39.97  ? 95  ALA C CB  1 
ATOM   2973  N  N   . ASP B  1 97  ? -49.565  -20.247 15.773  1.00 39.92  ? 96  ASP C N   1 
ATOM   2974  C  CA  . ASP B  1 97  ? -50.550  -19.770 16.717  1.00 40.29  ? 96  ASP C CA  1 
ATOM   2975  C  C   . ASP B  1 97  ? -49.943  -19.942 18.107  1.00 40.34  ? 96  ASP C C   1 
ATOM   2976  O  O   . ASP B  1 97  ? -49.281  -20.932 18.391  1.00 42.21  ? 96  ASP C O   1 
ATOM   2977  C  CB  . ASP B  1 97  ? -51.897  -20.469 16.521  1.00 46.81  ? 96  ASP C CB  1 
ATOM   2978  C  CG  . ASP B  1 97  ? -52.571  -20.125 15.201  1.00 50.87  ? 96  ASP C CG  1 
ATOM   2979  O  OD1 . ASP B  1 97  ? -53.225  -21.021 14.647  1.00 56.93  ? 96  ASP C OD1 1 
ATOM   2980  O  OD2 . ASP B  1 97  ? -52.431  -18.959 14.718  1.00 52.46  ? 96  ASP C OD2 1 
ATOM   2981  N  N   . VAL B  1 98  ? -50.121  -18.934 18.955  1.00 37.54  ? 97  VAL C N   1 
ATOM   2982  C  CA  . VAL B  1 98  ? -49.490  -18.924 20.235  1.00 37.55  ? 97  VAL C CA  1 
ATOM   2983  C  C   . VAL B  1 98  ? -50.563  -18.981 21.319  1.00 36.25  ? 97  VAL C C   1 
ATOM   2984  O  O   . VAL B  1 98  ? -51.520  -18.219 21.288  1.00 38.36  ? 97  VAL C O   1 
ATOM   2985  C  CB  . VAL B  1 98  ? -48.609  -17.673 20.393  1.00 38.77  ? 97  VAL C CB  1 
ATOM   2986  C  CG1 . VAL B  1 98  ? -48.023  -17.600 21.793  1.00 39.28  ? 97  VAL C CG1 1 
ATOM   2987  C  CG2 . VAL B  1 98  ? -47.520  -17.629 19.330  1.00 39.18  ? 97  VAL C CG2 1 
ATOM   2988  N  N   . SER B  1 99  ? -50.367  -19.865 22.299  1.00 38.48  ? 98  SER C N   1 
ATOM   2989  C  CA  . SER B  1 99  ? -51.235  -19.928 23.455  1.00 42.72  ? 98  SER C CA  1 
ATOM   2990  C  C   . SER B  1 99  ? -50.455  -20.504 24.638  1.00 47.53  ? 98  SER C C   1 
ATOM   2991  O  O   . SER B  1 99  ? -50.222  -21.709 24.729  1.00 45.91  ? 98  SER C O   1 
ATOM   2992  C  CB  . SER B  1 99  ? -52.502  -20.707 23.172  1.00 43.42  ? 98  SER C CB  1 
ATOM   2993  O  OG  . SER B  1 99  ? -53.447  -20.492 24.211  1.00 43.18  ? 98  SER C OG  1 
ATOM   2994  N  N   . ILE B  1 100 ? -50.058  -19.597 25.532  1.00 48.21  ? 99  ILE C N   1 
ATOM   2995  C  CA  . ILE B  1 100 ? -49.148  -19.852 26.629  1.00 49.30  ? 99  ILE C CA  1 
ATOM   2996  C  C   . ILE B  1 100 ? -49.793  -19.265 27.886  1.00 46.43  ? 99  ILE C C   1 
ATOM   2997  O  O   . ILE B  1 100 ? -50.547  -18.305 27.823  1.00 43.84  ? 99  ILE C O   1 
ATOM   2998  C  CB  . ILE B  1 100 ? -47.776  -19.202 26.328  1.00 53.72  ? 99  ILE C CB  1 
ATOM   2999  C  CG1 . ILE B  1 100 ? -47.018  -19.938 25.224  1.00 56.78  ? 99  ILE C CG1 1 
ATOM   3000  C  CG2 . ILE B  1 100 ? -46.932  -19.058 27.585  1.00 56.18  ? 99  ILE C CG2 1 
ATOM   3001  C  CD1 . ILE B  1 100 ? -45.801  -19.175 24.708  1.00 60.69  ? 99  ILE C CD1 1 
ATOM   3002  N  N   . GLU B  1 101 ? -49.485  -19.859 29.033  1.00 46.90  ? 100 GLU C N   1 
ATOM   3003  C  CA  . GLU B  1 101 ? -49.752  -19.241 30.301  1.00 52.79  ? 100 GLU C CA  1 
ATOM   3004  C  C   . GLU B  1 101 ? -48.472  -19.354 31.126  1.00 52.79  ? 100 GLU C C   1 
ATOM   3005  O  O   . GLU B  1 101 ? -47.816  -20.399 31.115  1.00 50.95  ? 100 GLU C O   1 
ATOM   3006  C  CB  . GLU B  1 101 ? -50.972  -19.878 30.960  1.00 54.72  ? 100 GLU C CB  1 
ATOM   3007  C  CG  . GLU B  1 101 ? -51.210  -19.394 32.368  1.00 60.66  ? 100 GLU C CG  1 
ATOM   3008  C  CD  . GLU B  1 101 ? -52.517  -19.889 32.957  1.00 65.94  ? 100 GLU C CD  1 
ATOM   3009  O  OE1 . GLU B  1 101 ? -53.578  -19.382 32.533  1.00 71.33  ? 100 GLU C OE1 1 
ATOM   3010  O  OE2 . GLU B  1 101 ? -52.468  -20.791 33.821  1.00 66.95  ? 100 GLU C OE2 1 
ATOM   3011  N  N   . ASP B  1 102 ? -48.093  -18.246 31.771  1.00 53.43  ? 101 ASP C N   1 
ATOM   3012  C  CA  . ASP B  1 102 ? -46.828  -18.164 32.501  1.00 52.05  ? 101 ASP C CA  1 
ATOM   3013  C  C   . ASP B  1 102 ? -47.058  -17.387 33.806  1.00 53.50  ? 101 ASP C C   1 
ATOM   3014  O  O   . ASP B  1 102 ? -47.793  -16.386 33.824  1.00 56.24  ? 101 ASP C O   1 
ATOM   3015  C  CB  . ASP B  1 102 ? -45.743  -17.563 31.613  1.00 51.63  ? 101 ASP C CB  1 
ATOM   3016  C  CG  . ASP B  1 102 ? -44.335  -17.842 32.108  1.00 57.17  ? 101 ASP C CG  1 
ATOM   3017  O  OD1 . ASP B  1 102 ? -43.778  -16.973 32.814  1.00 55.88  ? 101 ASP C OD1 1 
ATOM   3018  O  OD2 . ASP B  1 102 ? -43.800  -18.921 31.775  1.00 58.59  ? 101 ASP C OD2 1 
ATOM   3019  N  N   . SER B  1 103 ? -46.446  -17.881 34.892  1.00 52.38  ? 102 SER C N   1 
ATOM   3020  C  CA  . SER B  1 103 ? -46.600  -17.332 36.244  1.00 58.79  ? 102 SER C CA  1 
ATOM   3021  C  C   . SER B  1 103 ? -45.343  -16.565 36.671  1.00 53.45  ? 102 SER C C   1 
ATOM   3022  O  O   . SER B  1 103 ? -45.312  -16.024 37.783  1.00 55.19  ? 102 SER C O   1 
ATOM   3023  C  CB  . SER B  1 103 ? -46.911  -18.426 37.238  1.00 63.80  ? 102 SER C CB  1 
ATOM   3024  O  OG  . SER B  1 103 ? -47.980  -19.239 36.781  1.00 71.89  ? 102 SER C OG  1 
ATOM   3025  N  N   . VAL B  1 104 ? -44.324  -16.527 35.799  1.00 51.32  ? 103 VAL C N   1 
ATOM   3026  C  CA  . VAL B  1 104 ? -43.033  -15.894 36.118  1.00 56.23  ? 103 VAL C CA  1 
ATOM   3027  C  C   . VAL B  1 104 ? -43.021  -14.441 35.617  1.00 57.66  ? 103 VAL C C   1 
ATOM   3028  O  O   . VAL B  1 104 ? -42.741  -13.540 36.399  1.00 54.05  ? 103 VAL C O   1 
ATOM   3029  C  CB  . VAL B  1 104 ? -41.842  -16.691 35.557  1.00 56.43  ? 103 VAL C CB  1 
ATOM   3030  C  CG1 . VAL B  1 104 ? -40.525  -15.963 35.791  1.00 58.92  ? 103 VAL C CG1 1 
ATOM   3031  C  CG2 . VAL B  1 104 ? -41.789  -18.093 36.145  1.00 58.54  ? 103 VAL C CG2 1 
ATOM   3032  N  N   . ILE B  1 105 ? -43.298  -14.233 34.318  1.00 55.44  ? 104 ILE C N   1 
ATOM   3033  C  CA  . ILE B  1 105 ? -43.513  -12.888 33.756  1.00 49.72  ? 104 ILE C CA  1 
ATOM   3034  C  C   . ILE B  1 105 ? -44.685  -12.244 34.500  1.00 49.85  ? 104 ILE C C   1 
ATOM   3035  O  O   . ILE B  1 105 ? -45.519  -12.933 35.086  1.00 49.02  ? 104 ILE C O   1 
ATOM   3036  C  CB  . ILE B  1 105 ? -43.776  -12.895 32.235  1.00 47.70  ? 104 ILE C CB  1 
ATOM   3037  C  CG1 . ILE B  1 105 ? -45.062  -13.647 31.865  1.00 47.95  ? 104 ILE C CG1 1 
ATOM   3038  C  CG2 . ILE B  1 105 ? -42.561  -13.404 31.475  1.00 46.91  ? 104 ILE C CG2 1 
ATOM   3039  C  CD1 . ILE B  1 105 ? -45.446  -13.556 30.401  1.00 45.61  ? 104 ILE C CD1 1 
ATOM   3040  N  N   . SER B  1 106 ? -44.726  -10.910 34.467  1.00 45.57  ? 105 SER C N   1 
ATOM   3041  C  CA  . SER B  1 106 ? -45.829  -10.151 35.015  1.00 45.62  ? 105 SER C CA  1 
ATOM   3042  C  C   . SER B  1 106 ? -46.048  -8.923  34.132  1.00 45.13  ? 105 SER C C   1 
ATOM   3043  O  O   . SER B  1 106 ? -45.180  -8.575  33.338  1.00 41.57  ? 105 SER C O   1 
ATOM   3044  C  CB  . SER B  1 106 ? -45.592  -9.764  36.461  1.00 44.65  ? 105 SER C CB  1 
ATOM   3045  O  OG  . SER B  1 106 ? -46.819  -9.385  37.082  1.00 46.17  ? 105 SER C OG  1 
ATOM   3046  N  N   . LEU B  1 107 ? -47.223  -8.311  34.267  1.00 43.44  ? 106 LEU C N   1 
ATOM   3047  C  CA  . LEU B  1 107 ? -47.504  -7.044  33.619  1.00 49.89  ? 106 LEU C CA  1 
ATOM   3048  C  C   . LEU B  1 107 ? -47.445  -5.902  34.646  1.00 52.37  ? 106 LEU C C   1 
ATOM   3049  O  O   . LEU B  1 107 ? -47.876  -4.792  34.349  1.00 53.13  ? 106 LEU C O   1 
ATOM   3050  C  CB  . LEU B  1 107 ? -48.876  -7.124  32.944  1.00 47.93  ? 106 LEU C CB  1 
ATOM   3051  C  CG  . LEU B  1 107 ? -49.015  -8.174  31.844  1.00 43.47  ? 106 LEU C CG  1 
ATOM   3052  C  CD1 . LEU B  1 107 ? -50.401  -8.079  31.217  1.00 46.10  ? 106 LEU C CD1 1 
ATOM   3053  C  CD2 . LEU B  1 107 ? -47.926  -8.028  30.787  1.00 44.34  ? 106 LEU C CD2 1 
ATOM   3054  N  N   . SER B  1 108 ? -46.912  -6.184  35.843  1.00 56.60  ? 107 SER C N   1 
ATOM   3055  C  CA  . SER B  1 108 ? -46.628  -5.159  36.863  1.00 59.50  ? 107 SER C CA  1 
ATOM   3056  C  C   . SER B  1 108 ? -45.574  -5.674  37.851  1.00 60.91  ? 107 SER C C   1 
ATOM   3057  O  O   . SER B  1 108 ? -45.261  -6.869  37.880  1.00 52.88  ? 107 SER C O   1 
ATOM   3058  C  CB  . SER B  1 108 ? -47.878  -4.716  37.570  1.00 56.70  ? 107 SER C CB  1 
ATOM   3059  O  OG  . SER B  1 108 ? -48.418  -5.766  38.347  1.00 62.02  ? 107 SER C OG  1 
ATOM   3060  N  N   . GLY B  1 109 ? -44.997  -4.738  38.618  1.00 61.89  ? 108 GLY C N   1 
ATOM   3061  C  CA  . GLY B  1 109 ? -44.005  -5.039  39.655  1.00 56.34  ? 108 GLY C CA  1 
ATOM   3062  C  C   . GLY B  1 109 ? -42.617  -5.220  39.070  1.00 56.48  ? 108 GLY C C   1 
ATOM   3063  O  O   . GLY B  1 109 ? -42.344  -4.770  37.957  1.00 52.87  ? 108 GLY C O   1 
ATOM   3064  N  N   . ASP B  1 110 ? -41.768  -5.938  39.818  1.00 61.53  ? 109 ASP C N   1 
ATOM   3065  C  CA  . ASP B  1 110 ? -40.327  -6.070  39.566  1.00 67.19  ? 109 ASP C CA  1 
ATOM   3066  C  C   . ASP B  1 110 ? -40.059  -6.951  38.339  1.00 67.01  ? 109 ASP C C   1 
ATOM   3067  O  O   . ASP B  1 110 ? -39.000  -6.833  37.728  1.00 69.24  ? 109 ASP C O   1 
ATOM   3068  C  CB  . ASP B  1 110 ? -39.603  -6.644  40.792  1.00 73.72  ? 109 ASP C CB  1 
ATOM   3069  C  CG  . ASP B  1 110 ? -39.958  -5.959  42.105  1.00 77.28  ? 109 ASP C CG  1 
ATOM   3070  O  OD1 . ASP B  1 110 ? -39.999  -6.657  43.140  1.00 79.87  ? 109 ASP C OD1 1 
ATOM   3071  O  OD2 . ASP B  1 110 ? -40.201  -4.735  42.086  1.00 79.43  ? 109 ASP C OD2 1 
ATOM   3072  N  N   . HIS B  1 111 ? -41.007  -7.840  38.005  1.00 70.35  ? 110 HIS C N   1 
ATOM   3073  C  CA  . HIS B  1 111 ? -40.891  -8.756  36.860  1.00 68.73  ? 110 HIS C CA  1 
ATOM   3074  C  C   . HIS B  1 111 ? -41.700  -8.259  35.648  1.00 65.58  ? 110 HIS C C   1 
ATOM   3075  O  O   . HIS B  1 111 ? -41.795  -8.994  34.650  1.00 65.60  ? 110 HIS C O   1 
ATOM   3076  C  CB  . HIS B  1 111 ? -41.330  -10.180 37.253  1.00 73.11  ? 110 HIS C CB  1 
ATOM   3077  C  CG  . HIS B  1 111 ? -40.396  -10.893 38.175  1.00 79.57  ? 110 HIS C CG  1 
ATOM   3078  N  ND1 . HIS B  1 111 ? -40.838  -11.827 39.094  1.00 82.56  ? 110 HIS C ND1 1 
ATOM   3079  C  CD2 . HIS B  1 111 ? -39.056  -10.813 38.333  1.00 83.90  ? 110 HIS C CD2 1 
ATOM   3080  C  CE1 . HIS B  1 111 ? -39.811  -12.290 39.775  1.00 82.99  ? 110 HIS C CE1 1 
ATOM   3081  N  NE2 . HIS B  1 111 ? -38.705  -11.686 39.327  1.00 83.94  ? 110 HIS C NE2 1 
ATOM   3082  N  N   . SER B  1 112 ? -42.274  -7.042  35.718  1.00 57.27  ? 111 SER C N   1 
ATOM   3083  C  CA  . SER B  1 112 ? -43.130  -6.499  34.636  1.00 50.64  ? 111 SER C CA  1 
ATOM   3084  C  C   . SER B  1 112 ? -42.378  -6.523  33.302  1.00 45.07  ? 111 SER C C   1 
ATOM   3085  O  O   . SER B  1 112 ? -41.188  -6.240  33.251  1.00 44.26  ? 111 SER C O   1 
ATOM   3086  C  CB  . SER B  1 112 ? -43.623  -5.110  34.943  1.00 51.28  ? 111 SER C CB  1 
ATOM   3087  O  OG  . SER B  1 112 ? -44.365  -4.597  33.844  1.00 51.83  ? 111 SER C OG  1 
ATOM   3088  N  N   . ILE B  1 113 ? -43.081  -6.899  32.228  1.00 42.04  ? 112 ILE C N   1 
ATOM   3089  C  CA  . ILE B  1 113 ? -42.495  -6.956  30.887  1.00 40.40  ? 112 ILE C CA  1 
ATOM   3090  C  C   . ILE B  1 113 ? -42.994  -5.772  30.044  1.00 38.89  ? 112 ILE C C   1 
ATOM   3091  O  O   . ILE B  1 113 ? -42.670  -5.660  28.873  1.00 39.98  ? 112 ILE C O   1 
ATOM   3092  C  CB  . ILE B  1 113 ? -42.791  -8.314  30.209  1.00 45.14  ? 112 ILE C CB  1 
ATOM   3093  C  CG1 . ILE B  1 113 ? -44.291  -8.595  30.072  1.00 44.89  ? 112 ILE C CG1 1 
ATOM   3094  C  CG2 . ILE B  1 113 ? -42.078  -9.437  30.950  1.00 47.37  ? 112 ILE C CG2 1 
ATOM   3095  C  CD1 . ILE B  1 113 ? -44.630  -9.732  29.112  1.00 45.10  ? 112 ILE C CD1 1 
ATOM   3096  N  N   . ILE B  1 114 ? -43.811  -4.899  30.635  1.00 41.75  ? 113 ILE C N   1 
ATOM   3097  C  CA  . ILE B  1 114 ? -44.301  -3.720  29.931  1.00 43.55  ? 113 ILE C CA  1 
ATOM   3098  C  C   . ILE B  1 114 ? -43.112  -2.810  29.629  1.00 41.64  ? 113 ILE C C   1 
ATOM   3099  O  O   . ILE B  1 114 ? -42.261  -2.611  30.466  1.00 48.19  ? 113 ILE C O   1 
ATOM   3100  C  CB  . ILE B  1 114 ? -45.429  -3.044  30.728  1.00 45.10  ? 113 ILE C CB  1 
ATOM   3101  C  CG1 . ILE B  1 114 ? -46.678  -3.933  30.670  1.00 48.54  ? 113 ILE C CG1 1 
ATOM   3102  C  CG2 . ILE B  1 114 ? -45.708  -1.640  30.208  1.00 46.01  ? 113 ILE C CG2 1 
ATOM   3103  C  CD1 . ILE B  1 114 ? -47.732  -3.574  31.654  1.00 53.18  ? 113 ILE C CD1 1 
ATOM   3104  N  N   . GLY B  1 115 ? -43.036  -2.360  28.378  1.00 42.96  ? 114 GLY C N   1 
ATOM   3105  C  CA  . GLY B  1 115 ? -41.938  -1.533  27.902  1.00 46.27  ? 114 GLY C CA  1 
ATOM   3106  C  C   . GLY B  1 115 ? -40.700  -2.343  27.558  1.00 46.85  ? 114 GLY C C   1 
ATOM   3107  O  O   . GLY B  1 115 ? -39.649  -1.769  27.290  1.00 41.34  ? 114 GLY C O   1 
ATOM   3108  N  N   . ARG B  1 116 ? -40.813  -3.680  27.546  1.00 45.92  ? 115 ARG C N   1 
ATOM   3109  C  CA  . ARG B  1 116 ? -39.693  -4.542  27.128  1.00 45.45  ? 115 ARG C CA  1 
ATOM   3110  C  C   . ARG B  1 116 ? -39.987  -5.083  25.724  1.00 45.51  ? 115 ARG C C   1 
ATOM   3111  O  O   . ARG B  1 116 ? -40.989  -4.722  25.122  1.00 47.09  ? 115 ARG C O   1 
ATOM   3112  C  CB  . ARG B  1 116 ? -39.455  -5.614  28.192  1.00 47.88  ? 115 ARG C CB  1 
ATOM   3113  C  CG  . ARG B  1 116 ? -39.148  -5.019  29.561  1.00 48.21  ? 115 ARG C CG  1 
ATOM   3114  C  CD  . ARG B  1 116 ? -38.535  -6.010  30.529  1.00 49.98  ? 115 ARG C CD  1 
ATOM   3115  N  NE  . ARG B  1 116 ? -38.409  -5.426  31.857  1.00 51.61  ? 115 ARG C NE  1 
ATOM   3116  C  CZ  . ARG B  1 116 ? -37.430  -4.598  32.230  1.00 51.87  ? 115 ARG C CZ  1 
ATOM   3117  N  NH1 . ARG B  1 116 ? -37.487  -4.046  33.431  1.00 44.31  ? 115 ARG C NH1 1 
ATOM   3118  N  NH2 . ARG B  1 116 ? -36.406  -4.342  31.417  1.00 43.58  ? 115 ARG C NH2 1 
ATOM   3119  N  N   . THR B  1 117 ? -39.086  -5.917  25.196  1.00 43.42  ? 116 THR C N   1 
ATOM   3120  C  CA  . THR B  1 117 ? -39.201  -6.391  23.834  1.00 44.13  ? 116 THR C CA  1 
ATOM   3121  C  C   . THR B  1 117 ? -39.545  -7.888  23.839  1.00 46.71  ? 116 THR C C   1 
ATOM   3122  O  O   . THR B  1 117 ? -38.983  -8.663  24.628  1.00 45.19  ? 116 THR C O   1 
ATOM   3123  C  CB  . THR B  1 117 ? -37.922  -6.107  23.036  1.00 43.61  ? 116 THR C CB  1 
ATOM   3124  O  OG1 . THR B  1 117 ? -37.732  -4.693  22.924  1.00 45.10  ? 116 THR C OG1 1 
ATOM   3125  C  CG2 . THR B  1 117 ? -37.956  -6.687  21.639  1.00 42.38  ? 116 THR C CG2 1 
ATOM   3126  N  N   . LEU B  1 118 ? -40.470  -8.272  22.947  1.00 44.08  ? 117 LEU C N   1 
ATOM   3127  C  CA  . LEU B  1 118 ? -40.776  -9.662  22.688  1.00 42.25  ? 117 LEU C CA  1 
ATOM   3128  C  C   . LEU B  1 118 ? -40.048  -10.049 21.396  1.00 41.25  ? 117 LEU C C   1 
ATOM   3129  O  O   . LEU B  1 118 ? -40.144  -9.338  20.384  1.00 37.72  ? 117 LEU C O   1 
ATOM   3130  C  CB  . LEU B  1 118 ? -42.297  -9.858  22.575  1.00 41.93  ? 117 LEU C CB  1 
ATOM   3131  C  CG  . LEU B  1 118 ? -42.768  -11.316 22.530  1.00 41.02  ? 117 LEU C CG  1 
ATOM   3132  C  CD1 . LEU B  1 118 ? -42.520  -12.011 23.860  1.00 40.95  ? 117 LEU C CD1 1 
ATOM   3133  C  CD2 . LEU B  1 118 ? -44.240  -11.410 22.177  1.00 40.83  ? 117 LEU C CD2 1 
ATOM   3134  N  N   . VAL B  1 119 ? -39.301  -11.164 21.446  1.00 38.15  ? 118 VAL C N   1 
ATOM   3135  C  CA  . VAL B  1 119 ? -38.488  -11.590 20.323  1.00 39.27  ? 118 VAL C CA  1 
ATOM   3136  C  C   . VAL B  1 119 ? -38.883  -13.021 19.928  1.00 39.53  ? 118 VAL C C   1 
ATOM   3137  O  O   . VAL B  1 119 ? -39.022  -13.886 20.805  1.00 37.92  ? 118 VAL C O   1 
ATOM   3138  C  CB  . VAL B  1 119 ? -36.991  -11.510 20.683  1.00 42.68  ? 118 VAL C CB  1 
ATOM   3139  C  CG1 . VAL B  1 119 ? -36.107  -12.009 19.548  1.00 42.72  ? 118 VAL C CG1 1 
ATOM   3140  C  CG2 . VAL B  1 119 ? -36.590  -10.095 21.100  1.00 43.84  ? 118 VAL C CG2 1 
ATOM   3141  N  N   . VAL B  1 120 ? -39.028  -13.247 18.619  1.00 38.63  ? 119 VAL C N   1 
ATOM   3142  C  CA  . VAL B  1 120 ? -39.148  -14.595 18.039  1.00 42.52  ? 119 VAL C CA  1 
ATOM   3143  C  C   . VAL B  1 120 ? -37.870  -14.877 17.226  1.00 44.07  ? 119 VAL C C   1 
ATOM   3144  O  O   . VAL B  1 120 ? -37.461  -14.073 16.375  1.00 45.53  ? 119 VAL C O   1 
ATOM   3145  C  CB  . VAL B  1 120 ? -40.430  -14.771 17.198  1.00 40.59  ? 119 VAL C CB  1 
ATOM   3146  C  CG1 . VAL B  1 120 ? -40.536  -13.764 16.056  1.00 40.62  ? 119 VAL C CG1 1 
ATOM   3147  C  CG2 . VAL B  1 120 ? -40.551  -16.191 16.651  1.00 43.61  ? 119 VAL C CG2 1 
ATOM   3148  N  N   . HIS B  1 121 ? -37.278  -16.050 17.471  1.00 45.63  ? 120 HIS C N   1 
ATOM   3149  C  CA  . HIS B  1 121 ? -35.926  -16.393 17.023  1.00 46.15  ? 120 HIS C CA  1 
ATOM   3150  C  C   . HIS B  1 121 ? -35.945  -17.286 15.782  1.00 51.11  ? 120 HIS C C   1 
ATOM   3151  O  O   . HIS B  1 121 ? -36.969  -17.872 15.430  1.00 50.72  ? 120 HIS C O   1 
ATOM   3152  C  CB  . HIS B  1 121 ? -35.150  -17.042 18.172  1.00 45.15  ? 120 HIS C CB  1 
ATOM   3153  C  CG  . HIS B  1 121 ? -34.582  -16.032 19.105  1.00 49.23  ? 120 HIS C CG  1 
ATOM   3154  N  ND1 . HIS B  1 121 ? -33.400  -15.372 18.834  1.00 50.47  ? 120 HIS C ND1 1 
ATOM   3155  C  CD2 . HIS B  1 121 ? -35.033  -15.538 20.275  1.00 52.54  ? 120 HIS C CD2 1 
ATOM   3156  C  CE1 . HIS B  1 121 ? -33.137  -14.535 19.813  1.00 50.54  ? 120 HIS C CE1 1 
ATOM   3157  N  NE2 . HIS B  1 121 ? -34.118  -14.610 20.703  1.00 46.23  ? 120 HIS C NE2 1 
ATOM   3158  N  N   . GLU B  1 122 ? -34.761  -17.386 15.163  1.00 52.19  ? 121 GLU C N   1 
ATOM   3159  C  CA  . GLU B  1 122 ? -34.482  -18.102 13.914  1.00 51.99  ? 121 GLU C CA  1 
ATOM   3160  C  C   . GLU B  1 122 ? -34.642  -19.614 14.108  1.00 48.74  ? 121 GLU C C   1 
ATOM   3161  O  O   . GLU B  1 122 ? -35.175  -20.295 13.240  1.00 47.95  ? 121 GLU C O   1 
ATOM   3162  C  CB  . GLU B  1 122 ? -33.048  -17.779 13.499  1.00 58.09  ? 121 GLU C CB  1 
ATOM   3163  C  CG  . GLU B  1 122 ? -32.644  -18.281 12.127  1.00 61.29  ? 121 GLU C CG  1 
ATOM   3164  C  CD  . GLU B  1 122 ? -31.137  -18.280 11.909  1.00 67.27  ? 121 GLU C CD  1 
ATOM   3165  O  OE1 . GLU B  1 122 ? -30.721  -18.508 10.756  1.00 73.00  ? 121 GLU C OE1 1 
ATOM   3166  O  OE2 . GLU B  1 122 ? -30.378  -18.062 12.894  1.00 62.90  ? 121 GLU C OE2 1 
ATOM   3167  N  N   . LYS B  1 123 ? -34.158  -20.099 15.254  1.00 50.29  ? 122 LYS C N   1 
ATOM   3168  C  CA  . LYS B  1 123 ? -34.000  -21.505 15.568  1.00 54.35  ? 122 LYS C CA  1 
ATOM   3169  C  C   . LYS B  1 123 ? -34.767  -21.819 16.848  1.00 51.91  ? 122 LYS C C   1 
ATOM   3170  O  O   . LYS B  1 123 ? -35.172  -20.915 17.585  1.00 52.67  ? 122 LYS C O   1 
ATOM   3171  C  CB  . LYS B  1 123 ? -32.542  -21.874 15.878  1.00 57.21  ? 122 LYS C CB  1 
ATOM   3172  C  CG  . LYS B  1 123 ? -31.510  -21.651 14.782  1.00 63.37  ? 122 LYS C CG  1 
ATOM   3173  C  CD  . LYS B  1 123 ? -30.084  -21.681 15.336  1.00 70.32  ? 122 LYS C CD  1 
ATOM   3174  C  CE  . LYS B  1 123 ? -29.053  -22.230 14.371  1.00 76.44  ? 122 LYS C CE  1 
ATOM   3175  N  NZ  . LYS B  1 123 ? -28.901  -21.383 13.164  1.00 78.25  ? 122 LYS C NZ  1 
ATOM   3176  N  N   . ALA B  1 124 ? -34.873  -23.118 17.129  1.00 48.82  ? 123 ALA C N   1 
ATOM   3177  C  CA  . ALA B  1 124 ? -35.462  -23.630 18.340  1.00 51.97  ? 123 ALA C CA  1 
ATOM   3178  C  C   . ALA B  1 124 ? -34.586  -23.262 19.541  1.00 51.98  ? 123 ALA C C   1 
ATOM   3179  O  O   . ALA B  1 124 ? -33.358  -23.210 19.454  1.00 60.64  ? 123 ALA C O   1 
ATOM   3180  C  CB  . ALA B  1 124 ? -35.632  -25.132 18.225  1.00 50.63  ? 123 ALA C CB  1 
ATOM   3181  N  N   . ASP B  1 125 ? -35.254  -23.007 20.661  1.00 51.07  ? 124 ASP C N   1 
ATOM   3182  C  CA  . ASP B  1 125 ? -34.667  -22.862 21.965  1.00 50.92  ? 124 ASP C CA  1 
ATOM   3183  C  C   . ASP B  1 125 ? -34.438  -24.270 22.531  1.00 55.39  ? 124 ASP C C   1 
ATOM   3184  O  O   . ASP B  1 125 ? -35.386  -25.057 22.604  1.00 51.11  ? 124 ASP C O   1 
ATOM   3185  C  CB  . ASP B  1 125 ? -35.617  -22.027 22.827  1.00 52.48  ? 124 ASP C CB  1 
ATOM   3186  C  CG  . ASP B  1 125 ? -35.085  -21.603 24.180  1.00 55.34  ? 124 ASP C CG  1 
ATOM   3187  O  OD1 . ASP B  1 125 ? -34.048  -22.142 24.591  1.00 57.79  ? 124 ASP C OD1 1 
ATOM   3188  O  OD2 . ASP B  1 125 ? -35.738  -20.748 24.823  1.00 53.83  ? 124 ASP C OD2 1 
ATOM   3189  N  N   . ASP B  1 126 ? -33.191  -24.582 22.919  1.00 52.40  ? 125 ASP C N   1 
ATOM   3190  C  CA  . ASP B  1 126 ? -32.836  -25.906 23.448  1.00 55.63  ? 125 ASP C CA  1 
ATOM   3191  C  C   . ASP B  1 126 ? -33.153  -25.964 24.947  1.00 55.76  ? 125 ASP C C   1 
ATOM   3192  O  O   . ASP B  1 126 ? -32.919  -26.982 25.579  1.00 57.95  ? 125 ASP C O   1 
ATOM   3193  C  CB  . ASP B  1 126 ? -31.386  -26.298 23.119  1.00 58.35  ? 125 ASP C CB  1 
ATOM   3194  C  CG  . ASP B  1 126 ? -30.275  -25.451 23.738  1.00 60.43  ? 125 ASP C CG  1 
ATOM   3195  O  OD1 . ASP B  1 126 ? -29.212  -25.329 23.083  1.00 63.23  ? 125 ASP C OD1 1 
ATOM   3196  O  OD2 . ASP B  1 126 ? -30.455  -24.943 24.877  1.00 59.00  ? 125 ASP C OD2 1 
ATOM   3197  N  N   . LEU B  1 127 ? -33.662  -24.854 25.496  1.00 55.84  ? 126 LEU C N   1 
ATOM   3198  C  CA  . LEU B  1 127 ? -34.218  -24.745 26.851  1.00 57.35  ? 126 LEU C CA  1 
ATOM   3199  C  C   . LEU B  1 127 ? -33.122  -24.917 27.914  1.00 62.33  ? 126 LEU C C   1 
ATOM   3200  O  O   . LEU B  1 127 ? -33.417  -25.306 29.059  1.00 59.16  ? 126 LEU C O   1 
ATOM   3201  C  CB  . LEU B  1 127 ? -35.350  -25.765 27.018  1.00 57.18  ? 126 LEU C CB  1 
ATOM   3202  C  CG  . LEU B  1 127 ? -36.473  -25.681 25.979  1.00 58.46  ? 126 LEU C CG  1 
ATOM   3203  C  CD1 . LEU B  1 127 ? -37.536  -26.737 26.239  1.00 58.54  ? 126 LEU C CD1 1 
ATOM   3204  C  CD2 . LEU B  1 127 ? -37.110  -24.299 25.964  1.00 57.36  ? 126 LEU C CD2 1 
ATOM   3205  N  N   . GLY B  1 128 ? -31.879  -24.568 27.550  1.00 66.37  ? 127 GLY C N   1 
ATOM   3206  C  CA  . GLY B  1 128 ? -30.710  -24.684 28.434  1.00 74.99  ? 127 GLY C CA  1 
ATOM   3207  C  C   . GLY B  1 128 ? -30.272  -26.129 28.624  1.00 79.04  ? 127 GLY C C   1 
ATOM   3208  O  O   . GLY B  1 128 ? -29.834  -26.494 29.711  1.00 81.91  ? 127 GLY C O   1 
ATOM   3209  N  N   . LYS B  1 129 ? -30.397  -26.937 27.559  1.00 81.23  ? 128 LYS C N   1 
ATOM   3210  C  CA  . LYS B  1 129 ? -30.204  -28.405 27.585  1.00 87.03  ? 128 LYS C CA  1 
ATOM   3211  C  C   . LYS B  1 129 ? -29.118  -28.826 26.581  1.00 84.77  ? 128 LYS C C   1 
ATOM   3212  O  O   . LYS B  1 129 ? -28.848  -30.019 26.424  1.00 85.30  ? 128 LYS C O   1 
ATOM   3213  C  CB  . LYS B  1 129 ? -31.513  -29.117 27.212  1.00 90.42  ? 128 LYS C CB  1 
ATOM   3214  C  CG  . LYS B  1 129 ? -31.975  -30.222 28.153  1.00 92.03  ? 128 LYS C CG  1 
ATOM   3215  C  CD  . LYS B  1 129 ? -33.051  -29.776 29.114  1.00 90.31  ? 128 LYS C CD  1 
ATOM   3216  C  CE  . LYS B  1 129 ? -32.660  -28.543 29.898  1.00 92.27  ? 128 LYS C CE  1 
ATOM   3217  N  NZ  . LYS B  1 129 ? -33.681  -28.191 30.912  1.00 98.43  ? 128 LYS C NZ  1 
ATOM   3218  N  N   . GLY B  1 130 ? -28.503  -27.843 25.910  1.00 82.20  ? 129 GLY C N   1 
ATOM   3219  C  CA  . GLY B  1 130 ? -27.636  -28.065 24.756  1.00 84.13  ? 129 GLY C CA  1 
ATOM   3220  C  C   . GLY B  1 130 ? -26.211  -28.436 25.146  1.00 88.97  ? 129 GLY C C   1 
ATOM   3221  O  O   . GLY B  1 130 ? -25.410  -28.787 24.268  1.00 81.26  ? 129 GLY C O   1 
ATOM   3222  N  N   . GLY B  1 131 ? -25.895  -28.332 26.447  1.00 89.29  ? 130 GLY C N   1 
ATOM   3223  C  CA  . GLY B  1 131 ? -24.595  -28.706 27.003  1.00 93.82  ? 130 GLY C CA  1 
ATOM   3224  C  C   . GLY B  1 131 ? -23.692  -27.499 27.206  1.00 99.19  ? 130 GLY C C   1 
ATOM   3225  O  O   . GLY B  1 131 ? -23.253  -27.235 28.328  1.00 105.32 ? 130 GLY C O   1 
ATOM   3226  N  N   . ASN B  1 132 ? -23.431  -26.770 26.111  1.00 102.36 ? 131 ASN C N   1 
ATOM   3227  C  CA  . ASN B  1 132 ? -22.502  -25.624 26.076  1.00 101.44 ? 131 ASN C CA  1 
ATOM   3228  C  C   . ASN B  1 132 ? -23.050  -24.474 26.939  1.00 102.13 ? 131 ASN C C   1 
ATOM   3229  O  O   . ASN B  1 132 ? -24.136  -24.574 27.527  1.00 100.53 ? 131 ASN C O   1 
ATOM   3230  C  CB  . ASN B  1 132 ? -22.180  -25.194 24.634  1.00 97.16  ? 131 ASN C CB  1 
ATOM   3231  C  CG  . ASN B  1 132 ? -23.379  -24.743 23.822  1.00 97.62  ? 131 ASN C CG  1 
ATOM   3232  O  OD1 . ASN B  1 132 ? -24.518  -24.829 24.270  1.00 92.34  ? 131 ASN C OD1 1 
ATOM   3233  N  ND2 . ASN B  1 132 ? -23.132  -24.256 22.618  1.00 93.95  ? 131 ASN C ND2 1 
ATOM   3234  N  N   . GLU B  1 133 ? -22.264  -23.394 27.030  1.00 101.44 ? 132 GLU C N   1 
ATOM   3235  C  CA  . GLU B  1 133 ? -22.604  -22.209 27.823  1.00 96.57  ? 132 GLU C CA  1 
ATOM   3236  C  C   . GLU B  1 133 ? -23.554  -21.303 27.030  1.00 88.46  ? 132 GLU C C   1 
ATOM   3237  O  O   . GLU B  1 133 ? -24.373  -20.604 27.630  1.00 79.19  ? 132 GLU C O   1 
ATOM   3238  C  CB  . GLU B  1 133 ? -21.334  -21.462 28.237  1.00 100.17 ? 132 GLU C CB  1 
ATOM   3239  C  CG  . GLU B  1 133 ? -20.690  -22.029 29.489  1.00 107.87 ? 132 GLU C CG  1 
ATOM   3240  C  CD  . GLU B  1 133 ? -19.174  -22.106 29.445  1.00 115.24 ? 132 GLU C CD  1 
ATOM   3241  O  OE1 . GLU B  1 133 ? -18.618  -23.072 30.006  1.00 119.95 ? 132 GLU C OE1 1 
ATOM   3242  O  OE2 . GLU B  1 133 ? -18.552  -21.201 28.851  1.00 117.04 ? 132 GLU C OE2 1 
ATOM   3243  N  N   . GLU B  1 134 ? -23.437  -21.321 25.695  1.00 81.81  ? 133 GLU C N   1 
ATOM   3244  C  CA  . GLU B  1 134 ? -24.337  -20.590 24.802  1.00 82.01  ? 133 GLU C CA  1 
ATOM   3245  C  C   . GLU B  1 134 ? -25.791  -20.978 25.110  1.00 83.09  ? 133 GLU C C   1 
ATOM   3246  O  O   . GLU B  1 134 ? -26.648  -20.107 25.273  1.00 76.86  ? 133 GLU C O   1 
ATOM   3247  C  CB  . GLU B  1 134 ? -24.004  -20.882 23.338  1.00 87.09  ? 133 GLU C CB  1 
ATOM   3248  C  CG  . GLU B  1 134 ? -24.876  -20.127 22.345  1.00 91.05  ? 133 GLU C CG  1 
ATOM   3249  C  CD  . GLU B  1 134 ? -24.895  -18.617 22.522  1.00 95.14  ? 133 GLU C CD  1 
ATOM   3250  O  OE1 . GLU B  1 134 ? -24.190  -17.927 21.761  1.00 94.29  ? 133 GLU C OE1 1 
ATOM   3251  O  OE2 . GLU B  1 134 ? -25.623  -18.131 23.412  1.00 99.96  ? 133 GLU C OE2 1 
ATOM   3252  N  N   . SER B  1 135 ? -26.038  -22.292 25.208  1.00 76.36  ? 134 SER C N   1 
ATOM   3253  C  CA  . SER B  1 135 ? -27.340  -22.860 25.580  1.00 72.62  ? 134 SER C CA  1 
ATOM   3254  C  C   . SER B  1 135 ? -27.859  -22.268 26.901  1.00 71.18  ? 134 SER C C   1 
ATOM   3255  O  O   . SER B  1 135 ? -29.066  -22.128 27.093  1.00 72.73  ? 134 SER C O   1 
ATOM   3256  C  CB  . SER B  1 135 ? -27.261  -24.365 25.662  1.00 66.68  ? 134 SER C CB  1 
ATOM   3257  O  OG  . SER B  1 135 ? -28.346  -24.892 26.412  1.00 60.14  ? 134 SER C OG  1 
ATOM   3258  N  N   . THR B  1 136 ? -26.953  -21.931 27.822  1.00 68.08  ? 135 THR C N   1 
ATOM   3259  C  CA  . THR B  1 136 ? -27.347  -21.414 29.136  1.00 70.94  ? 135 THR C CA  1 
ATOM   3260  C  C   . THR B  1 136 ? -27.525  -19.881 29.081  1.00 67.06  ? 135 THR C C   1 
ATOM   3261  O  O   . THR B  1 136 ? -27.873  -19.268 30.090  1.00 61.92  ? 135 THR C O   1 
ATOM   3262  C  CB  . THR B  1 136 ? -26.359  -21.901 30.208  1.00 76.11  ? 135 THR C CB  1 
ATOM   3263  O  OG1 . THR B  1 136 ? -25.113  -21.225 30.034  1.00 76.76  ? 135 THR C OG1 1 
ATOM   3264  C  CG2 . THR B  1 136 ? -26.125  -23.396 30.156  1.00 76.78  ? 135 THR C CG2 1 
ATOM   3265  N  N   . LYS B  1 137 ? -27.347  -19.277 27.895  1.00 65.54  ? 136 LYS C N   1 
ATOM   3266  C  CA  . LYS B  1 137 ? -27.511  -17.834 27.678  1.00 75.22  ? 136 LYS C CA  1 
ATOM   3267  C  C   . LYS B  1 137 ? -28.757  -17.559 26.820  1.00 73.55  ? 136 LYS C C   1 
ATOM   3268  O  O   . LYS B  1 137 ? -29.664  -16.833 27.246  1.00 71.18  ? 136 LYS C O   1 
ATOM   3269  C  CB  . LYS B  1 137 ? -26.255  -17.262 27.008  1.00 80.39  ? 136 LYS C CB  1 
ATOM   3270  C  CG  . LYS B  1 137 ? -24.941  -17.624 27.690  1.00 85.78  ? 136 LYS C CG  1 
ATOM   3271  C  CD  . LYS B  1 137 ? -24.229  -16.467 28.350  1.00 90.82  ? 136 LYS C CD  1 
ATOM   3272  C  CE  . LYS B  1 137 ? -23.300  -15.738 27.401  1.00 94.46  ? 136 LYS C CE  1 
ATOM   3273  N  NZ  . LYS B  1 137 ? -22.303  -14.929 28.138  1.00 97.94  ? 136 LYS C NZ  1 
ATOM   3274  N  N   . THR B  1 138 ? -28.771  -18.119 25.602  1.00 71.01  ? 137 THR C N   1 
ATOM   3275  C  CA  . THR B  1 138 ? -29.809  -17.870 24.601  1.00 72.89  ? 137 THR C CA  1 
ATOM   3276  C  C   . THR B  1 138 ? -30.521  -19.165 24.167  1.00 74.17  ? 137 THR C C   1 
ATOM   3277  O  O   . THR B  1 138 ? -31.378  -19.123 23.267  1.00 61.95  ? 137 THR C O   1 
ATOM   3278  C  CB  . THR B  1 138 ? -29.212  -17.200 23.359  1.00 71.66  ? 137 THR C CB  1 
ATOM   3279  O  OG1 . THR B  1 138 ? -28.393  -18.176 22.715  1.00 69.94  ? 137 THR C OG1 1 
ATOM   3280  C  CG2 . THR B  1 138 ? -28.421  -15.953 23.689  1.00 72.97  ? 137 THR C CG2 1 
ATOM   3281  N  N   . GLY B  1 139 ? -30.149  -20.303 24.774  1.00 69.16  ? 138 GLY C N   1 
ATOM   3282  C  CA  . GLY B  1 139 ? -30.635  -21.626 24.369  1.00 67.23  ? 138 GLY C CA  1 
ATOM   3283  C  C   . GLY B  1 139 ? -30.368  -21.940 22.903  1.00 65.16  ? 138 GLY C C   1 
ATOM   3284  O  O   . GLY B  1 139 ? -31.076  -22.752 22.306  1.00 66.63  ? 138 GLY C O   1 
ATOM   3285  N  N   . ASN B  1 140 ? -29.345  -21.300 22.326  1.00 60.06  ? 139 ASN C N   1 
ATOM   3286  C  CA  . ASN B  1 140 ? -28.921  -21.497 20.940  1.00 60.26  ? 139 ASN C CA  1 
ATOM   3287  C  C   . ASN B  1 140 ? -30.051  -21.133 19.963  1.00 58.21  ? 139 ASN C C   1 
ATOM   3288  O  O   . ASN B  1 140 ? -30.162  -21.732 18.890  1.00 57.73  ? 139 ASN C O   1 
ATOM   3289  C  CB  . ASN B  1 140 ? -28.377  -22.915 20.726  1.00 62.17  ? 139 ASN C CB  1 
ATOM   3290  C  CG  . ASN B  1 140 ? -26.996  -23.082 21.324  1.00 63.92  ? 139 ASN C CG  1 
ATOM   3291  O  OD1 . ASN B  1 140 ? -26.842  -23.633 22.415  1.00 64.27  ? 139 ASN C OD1 1 
ATOM   3292  N  ND2 . ASN B  1 140 ? -25.997  -22.556 20.635  1.00 62.00  ? 139 ASN C ND2 1 
ATOM   3293  N  N   . ALA B  1 141 ? -30.825  -20.091 20.293  1.00 58.26  ? 140 ALA C N   1 
ATOM   3294  C  CA  . ALA B  1 141 ? -32.025  -19.728 19.517  1.00 56.17  ? 140 ALA C CA  1 
ATOM   3295  C  C   . ALA B  1 141 ? -31.658  -18.998 18.210  1.00 53.57  ? 140 ALA C C   1 
ATOM   3296  O  O   . ALA B  1 141 ? -32.474  -18.936 17.282  1.00 49.98  ? 140 ALA C O   1 
ATOM   3297  C  CB  . ALA B  1 141 ? -32.962  -18.920 20.383  1.00 57.42  ? 140 ALA C CB  1 
ATOM   3298  N  N   . GLY B  1 142 ? -30.433  -18.461 18.113  1.00 51.05  ? 141 GLY C N   1 
ATOM   3299  C  CA  . GLY B  1 142 ? -29.947  -17.888 16.844  1.00 50.25  ? 141 GLY C CA  1 
ATOM   3300  C  C   . GLY B  1 142 ? -30.472  -16.479 16.608  1.00 49.00  ? 141 GLY C C   1 
ATOM   3301  O  O   . GLY B  1 142 ? -30.749  -15.770 17.564  1.00 47.51  ? 141 GLY C O   1 
ATOM   3302  N  N   . SER B  1 143 ? -30.616  -16.092 15.329  1.00 50.98  ? 142 SER C N   1 
ATOM   3303  C  CA  . SER B  1 143 ? -30.975  -14.715 14.930  1.00 55.83  ? 142 SER C CA  1 
ATOM   3304  C  C   . SER B  1 143 ? -32.314  -14.289 15.547  1.00 59.48  ? 142 SER C C   1 
ATOM   3305  O  O   . SER B  1 143 ? -33.158  -15.121 15.925  1.00 54.16  ? 142 SER C O   1 
ATOM   3306  C  CB  . SER B  1 143 ? -31.049  -14.550 13.429  1.00 58.92  ? 142 SER C CB  1 
ATOM   3307  O  OG  . SER B  1 143 ? -29.879  -15.031 12.794  1.00 68.74  ? 142 SER C OG  1 
ATOM   3308  N  N   . ARG B  1 144 ? -32.495  -12.965 15.609  1.00 57.64  ? 143 ARG C N   1 
ATOM   3309  C  CA  . ARG B  1 144 ? -33.740  -12.326 15.996  1.00 53.30  ? 143 ARG C CA  1 
ATOM   3310  C  C   . ARG B  1 144 ? -34.513  -11.999 14.714  1.00 53.09  ? 143 ARG C C   1 
ATOM   3311  O  O   . ARG B  1 144 ? -34.072  -11.185 13.913  1.00 54.67  ? 143 ARG C O   1 
ATOM   3312  C  CB  . ARG B  1 144 ? -33.436  -11.092 16.847  1.00 54.29  ? 143 ARG C CB  1 
ATOM   3313  C  CG  . ARG B  1 144 ? -32.695  -11.419 18.136  1.00 53.62  ? 143 ARG C CG  1 
ATOM   3314  C  CD  . ARG B  1 144 ? -32.281  -10.207 18.953  1.00 52.63  ? 143 ARG C CD  1 
ATOM   3315  N  NE  . ARG B  1 144 ? -31.282  -10.584 19.946  1.00 51.74  ? 143 ARG C NE  1 
ATOM   3316  C  CZ  . ARG B  1 144 ? -31.030  -9.914  21.063  1.00 52.50  ? 143 ARG C CZ  1 
ATOM   3317  N  NH1 . ARG B  1 144 ? -30.296  -10.476 22.008  1.00 46.24  ? 143 ARG C NH1 1 
ATOM   3318  N  NH2 . ARG B  1 144 ? -31.527  -8.699  21.244  1.00 53.03  ? 143 ARG C NH2 1 
ATOM   3319  N  N   . LEU B  1 145 ? -35.650  -12.677 14.515  1.00 47.43  ? 144 LEU C N   1 
ATOM   3320  C  CA  . LEU B  1 145 ? -36.378  -12.634 13.241  1.00 46.37  ? 144 LEU C CA  1 
ATOM   3321  C  C   . LEU B  1 145 ? -37.375  -11.471 13.250  1.00 42.98  ? 144 LEU C C   1 
ATOM   3322  O  O   . LEU B  1 145 ? -37.655  -10.876 12.210  1.00 43.63  ? 144 LEU C O   1 
ATOM   3323  C  CB  . LEU B  1 145 ? -37.118  -13.962 13.041  1.00 50.65  ? 144 LEU C CB  1 
ATOM   3324  C  CG  . LEU B  1 145 ? -36.446  -15.008 12.155  1.00 51.45  ? 144 LEU C CG  1 
ATOM   3325  C  CD1 . LEU B  1 145 ? -34.962  -15.126 12.444  1.00 55.66  ? 144 LEU C CD1 1 
ATOM   3326  C  CD2 . LEU B  1 145 ? -37.138  -16.347 12.337  1.00 53.78  ? 144 LEU C CD2 1 
ATOM   3327  N  N   . ALA B  1 146 ? -37.961  -11.221 14.424  1.00 43.57  ? 145 ALA C N   1 
ATOM   3328  C  CA  . ALA B  1 146 ? -38.927  -10.166 14.611  1.00 43.67  ? 145 ALA C CA  1 
ATOM   3329  C  C   . ALA B  1 146 ? -39.028  -9.855  16.101  1.00 42.86  ? 145 ALA C C   1 
ATOM   3330  O  O   . ALA B  1 146 ? -38.743  -10.711 16.967  1.00 43.99  ? 145 ALA C O   1 
ATOM   3331  C  CB  . ALA B  1 146 ? -40.271  -10.550 14.026  1.00 46.71  ? 145 ALA C CB  1 
ATOM   3332  N  N   . CYS B  1 147 ? -39.425  -8.611  16.384  1.00 38.12  ? 146 CYS C N   1 
ATOM   3333  C  CA  . CYS B  1 147 ? -39.585  -8.163  17.729  1.00 39.29  ? 146 CYS C CA  1 
ATOM   3334  C  C   . CYS B  1 147 ? -40.556  -6.986  17.760  1.00 35.41  ? 146 CYS C C   1 
ATOM   3335  O  O   . CYS B  1 147 ? -40.908  -6.418  16.734  1.00 38.03  ? 146 CYS C O   1 
ATOM   3336  C  CB  . CYS B  1 147 ? -38.250  -7.729  18.327  1.00 48.66  ? 146 CYS C CB  1 
ATOM   3337  S  SG  . CYS B  1 147 ? -37.392  -6.489  17.318  1.00 49.93  ? 146 CYS C SG  1 
ATOM   3338  N  N   . GLY B  1 148 ? -40.965  -6.638  18.971  1.00 37.19  ? 147 GLY C N   1 
ATOM   3339  C  CA  . GLY B  1 148 ? -41.737  -5.467  19.206  1.00 38.04  ? 147 GLY C CA  1 
ATOM   3340  C  C   . GLY B  1 148 ? -41.710  -5.131  20.669  1.00 36.58  ? 147 GLY C C   1 
ATOM   3341  O  O   . GLY B  1 148 ? -41.348  -5.968  21.490  1.00 39.81  ? 147 GLY C O   1 
ATOM   3342  N  N   . VAL B  1 149 ? -42.115  -3.902  20.983  1.00 38.28  ? 148 VAL C N   1 
ATOM   3343  C  CA  . VAL B  1 149 ? -42.180  -3.454  22.332  1.00 37.80  ? 148 VAL C CA  1 
ATOM   3344  C  C   . VAL B  1 149 ? -43.563  -3.828  22.857  1.00 39.40  ? 148 VAL C C   1 
ATOM   3345  O  O   . VAL B  1 149 ? -44.583  -3.701  22.146  1.00 43.89  ? 148 VAL C O   1 
ATOM   3346  C  CB  . VAL B  1 149 ? -41.897  -1.940  22.445  1.00 39.53  ? 148 VAL C CB  1 
ATOM   3347  C  CG1 . VAL B  1 149 ? -41.874  -1.479  23.890  1.00 37.63  ? 148 VAL C CG1 1 
ATOM   3348  C  CG2 . VAL B  1 149 ? -40.608  -1.556  21.726  1.00 39.82  ? 148 VAL C CG2 1 
ATOM   3349  N  N   . ILE B  1 150 ? -43.575  -4.296  24.106  1.00 40.30  ? 149 ILE C N   1 
ATOM   3350  C  CA  . ILE B  1 150 ? -44.781  -4.710  24.770  1.00 42.08  ? 149 ILE C CA  1 
ATOM   3351  C  C   . ILE B  1 150 ? -45.425  -3.460  25.380  1.00 42.57  ? 149 ILE C C   1 
ATOM   3352  O  O   . ILE B  1 150 ? -44.894  -2.892  26.347  1.00 40.20  ? 149 ILE C O   1 
ATOM   3353  C  CB  . ILE B  1 150 ? -44.476  -5.795  25.821  1.00 41.29  ? 149 ILE C CB  1 
ATOM   3354  C  CG1 . ILE B  1 150 ? -43.781  -7.006  25.184  1.00 43.82  ? 149 ILE C CG1 1 
ATOM   3355  C  CG2 . ILE B  1 150 ? -45.745  -6.178  26.567  1.00 42.83  ? 149 ILE C CG2 1 
ATOM   3356  C  CD1 . ILE B  1 150 ? -43.096  -7.920  26.173  1.00 44.47  ? 149 ILE C CD1 1 
ATOM   3357  N  N   . GLY B  1 151 ? -46.559  -3.052  24.802  1.00 39.32  ? 150 GLY C N   1 
ATOM   3358  C  CA  . GLY B  1 151 ? -47.267  -1.840  25.205  1.00 41.10  ? 150 GLY C CA  1 
ATOM   3359  C  C   . GLY B  1 151 ? -48.519  -2.148  26.003  1.00 44.20  ? 150 GLY C C   1 
ATOM   3360  O  O   . GLY B  1 151 ? -49.074  -3.264  25.919  1.00 39.69  ? 150 GLY C O   1 
ATOM   3361  N  N   . ILE B  1 152 ? -48.960  -1.158  26.785  1.00 40.22  ? 151 ILE C N   1 
ATOM   3362  C  CA  . ILE B  1 152 ? -50.201  -1.231  27.545  1.00 43.87  ? 151 ILE C CA  1 
ATOM   3363  C  C   . ILE B  1 152 ? -51.360  -1.273  26.543  1.00 42.14  ? 151 ILE C C   1 
ATOM   3364  O  O   . ILE B  1 152 ? -51.374  -0.502  25.558  1.00 38.00  ? 151 ILE C O   1 
ATOM   3365  C  CB  . ILE B  1 152 ? -50.326  -0.058  28.535  1.00 43.88  ? 151 ILE C CB  1 
ATOM   3366  C  CG1 . ILE B  1 152 ? -49.194  -0.073  29.569  1.00 46.58  ? 151 ILE C CG1 1 
ATOM   3367  C  CG2 . ILE B  1 152 ? -51.699  -0.072  29.195  1.00 45.13  ? 151 ILE C CG2 1 
ATOM   3368  C  CD1 . ILE B  1 152 ? -49.132  1.159   30.470  1.00 46.30  ? 151 ILE C CD1 1 
ATOM   3369  N  N   . ALA B  1 153 ? -52.296  -2.208  26.760  1.00 42.30  ? 152 ALA C N   1 
ATOM   3370  C  CA  . ALA B  1 153 ? -53.279  -2.541  25.723  1.00 45.19  ? 152 ALA C CA  1 
ATOM   3371  C  C   . ALA B  1 153 ? -54.619  -1.897  26.048  1.00 46.71  ? 152 ALA C C   1 
ATOM   3372  O  O   . ALA B  1 153 ? -55.077  -1.898  27.195  1.00 42.23  ? 152 ALA C O   1 
ATOM   3373  C  CB  . ALA B  1 153 ? -53.440  -4.028  25.523  1.00 47.54  ? 152 ALA C CB  1 
ATOM   3374  N  N   . GLN B  1 154 ? -55.135  -1.283  24.984  1.00 56.89  ? 153 GLN C N   1 
ATOM   3375  C  CA  . GLN B  1 154 ? -56.497  -0.942  24.711  1.00 68.36  ? 153 GLN C CA  1 
ATOM   3376  C  C   . GLN B  1 154 ? -57.454  -1.553  25.749  1.00 73.34  ? 153 GLN C C   1 
ATOM   3377  O  O   . GLN B  1 154 ? -57.438  -2.771  26.042  1.00 70.10  ? 153 GLN C O   1 
ATOM   3378  C  CB  . GLN B  1 154 ? -56.786  -1.394  23.274  1.00 75.58  ? 153 GLN C CB  1 
ATOM   3379  C  CG  . GLN B  1 154 ? -58.066  -0.826  22.670  1.00 84.94  ? 153 GLN C CG  1 
ATOM   3380  C  CD  . GLN B  1 154 ? -57.835  0.461   21.911  1.00 85.51  ? 153 GLN C CD  1 
ATOM   3381  O  OE1 . GLN B  1 154 ? -57.267  1.415   22.433  1.00 88.74  ? 153 GLN C OE1 1 
ATOM   3382  N  NE2 . GLN B  1 154 ? -58.286  0.499   20.666  1.00 82.62  ? 153 GLN C NE2 1 
ATOM   3383  N  N   . GLY B  1 155 ? -58.270  -0.656  26.315  1.00 77.44  ? 154 GLY C N   1 
ATOM   3384  C  CA  . GLY B  1 155 ? -59.556  -0.961  26.914  1.00 81.20  ? 154 GLY C CA  1 
ATOM   3385  C  C   . GLY B  1 155 ? -60.677  -0.275  26.147  1.00 81.79  ? 154 GLY C C   1 
ATOM   3386  O  O   . GLY B  1 155 ? -60.427  0.452   25.179  1.00 70.74  ? 154 GLY C O   1 
ATOM   3387  N  N   . GLY B  1 167 ? -49.928  1.976   35.666  1.00 76.57  ? 166 GLY C N   1 
ATOM   3388  C  CA  . GLY B  1 167 ? -49.033  1.859   34.481  1.00 76.52  ? 166 GLY C CA  1 
ATOM   3389  C  C   . GLY B  1 167 ? -48.667  0.413   34.180  1.00 80.80  ? 166 GLY C C   1 
ATOM   3390  O  O   . GLY B  1 167 ? -49.453  -0.340  33.608  1.00 85.13  ? 166 GLY C O   1 
ATOM   3391  N  N   . GLY B  1 168 ? -47.459  0.018   34.583  1.00 76.92  ? 167 GLY C N   1 
ATOM   3392  C  CA  . GLY B  1 168 ? -46.917  -1.267  34.231  1.00 73.55  ? 167 GLY C CA  1 
ATOM   3393  C  C   . GLY B  1 168 ? -45.402  -1.278  34.309  1.00 74.35  ? 167 GLY C C   1 
ATOM   3394  O  O   . GLY B  1 168 ? -44.841  -2.159  34.941  1.00 70.21  ? 167 GLY C O   1 
ATOM   3395  N  N   . GLY B  1 169 ? -44.757  -0.282  33.678  1.00 77.21  ? 168 GLY C N   1 
ATOM   3396  C  CA  . GLY B  1 169 ? -43.289  -0.218  33.531  1.00 77.24  ? 168 GLY C CA  1 
ATOM   3397  C  C   . GLY B  1 169 ? -42.661  0.968   34.256  1.00 77.84  ? 168 GLY C C   1 
ATOM   3398  O  O   . GLY B  1 169 ? -43.285  2.017   34.420  1.00 66.45  ? 168 GLY C O   1 
ATOM   3399  N  N   . SER B  1 170 ? -41.404  0.786   34.685  1.00 82.73  ? 169 SER C N   1 
ATOM   3400  C  CA  . SER B  1 170 ? -40.590  1.831   35.331  1.00 87.69  ? 169 SER C CA  1 
ATOM   3401  C  C   . SER B  1 170 ? -39.149  1.757   34.795  1.00 85.10  ? 169 SER C C   1 
ATOM   3402  O  O   . SER B  1 170 ? -38.691  0.658   34.444  1.00 84.46  ? 169 SER C O   1 
ATOM   3403  C  CB  . SER B  1 170 ? -40.646  1.722   36.845  1.00 89.94  ? 169 SER C CB  1 
ATOM   3404  O  OG  . SER B  1 170 ? -40.245  0.434   37.291  1.00 93.24  ? 169 SER C OG  1 
ATOM   3405  N  N   . ALA B  1 171 ? -38.461  2.916   34.716  1.00 73.87  ? 170 ALA C N   1 
ATOM   3406  C  CA  . ALA B  1 171 ? -37.098  3.015   34.128  1.00 68.43  ? 170 ALA C CA  1 
ATOM   3407  C  C   . ALA B  1 171 ? -36.457  4.403   34.340  1.00 66.78  ? 170 ALA C C   1 
ATOM   3408  O  O   . ALA B  1 171 ? -37.076  5.339   34.830  1.00 63.29  ? 170 ALA C O   1 
ATOM   3409  C  CB  . ALA B  1 171 ? -37.158  2.676   32.658  1.00 69.17  ? 170 ALA C CB  1 
ATOM   3410  N  N   . THR B  1 172 ? -35.183  4.503   33.949  1.00 58.55  ? 171 THR C N   1 
ATOM   3411  C  CA  . THR B  1 172 ? -34.340  5.681   34.115  1.00 60.49  ? 171 THR C CA  1 
ATOM   3412  C  C   . THR B  1 172 ? -34.085  6.303   32.734  1.00 58.94  ? 171 THR C C   1 
ATOM   3413  O  O   . THR B  1 172 ? -33.914  7.529   32.593  1.00 55.12  ? 171 THR C O   1 
ATOM   3414  C  CB  . THR B  1 172 ? -33.053  5.281   34.859  1.00 58.76  ? 171 THR C CB  1 
ATOM   3415  O  OG1 . THR B  1 172 ? -32.921  6.156   35.972  1.00 59.12  ? 171 THR C OG1 1 
ATOM   3416  C  CG2 . THR B  1 172 ? -31.792  5.325   34.022  1.00 58.33  ? 171 THR C CG2 1 
ATOM   3417  N  N   . LYS B  1 173 ? -34.020  5.428   31.727  1.00 54.53  ? 172 LYS C N   1 
ATOM   3418  C  CA  . LYS B  1 173 ? -33.996  5.797   30.333  1.00 56.84  ? 172 LYS C CA  1 
ATOM   3419  C  C   . LYS B  1 173 ? -35.099  5.035   29.587  1.00 54.59  ? 172 LYS C C   1 
ATOM   3420  O  O   . LYS B  1 173 ? -35.512  3.928   29.988  1.00 53.23  ? 172 LYS C O   1 
ATOM   3421  C  CB  . LYS B  1 173 ? -32.634  5.486   29.708  1.00 62.29  ? 172 LYS C CB  1 
ATOM   3422  C  CG  . LYS B  1 173 ? -31.489  6.388   30.147  1.00 71.24  ? 172 LYS C CG  1 
ATOM   3423  C  CD  . LYS B  1 173 ? -30.162  6.027   29.503  1.00 75.74  ? 172 LYS C CD  1 
ATOM   3424  C  CE  . LYS B  1 173 ? -30.114  6.280   28.007  1.00 77.77  ? 172 LYS C CE  1 
ATOM   3425  N  NZ  . LYS B  1 173 ? -30.236  7.723   27.678  1.00 80.41  ? 172 LYS C NZ  1 
ATOM   3426  N  N   . ALA B  1 174 ? -35.551  5.641   28.488  1.00 46.55  ? 173 ALA C N   1 
ATOM   3427  C  CA  . ALA B  1 174 ? -36.527  5.055   27.614  1.00 46.78  ? 173 ALA C CA  1 
ATOM   3428  C  C   . ALA B  1 174 ? -36.255  5.557   26.197  1.00 43.47  ? 173 ALA C C   1 
ATOM   3429  O  O   . ALA B  1 174 ? -35.456  6.469   25.970  1.00 45.75  ? 173 ALA C O   1 
ATOM   3430  C  CB  . ALA B  1 174 ? -37.923  5.378   28.105  1.00 46.14  ? 173 ALA C CB  1 
ATOM   3431  N  N   . VAL B  1 175 ? -36.897  4.921   25.228  1.00 39.76  ? 174 VAL C N   1 
ATOM   3432  C  CA  . VAL B  1 175 ? -36.686  5.258   23.846  1.00 39.32  ? 174 VAL C CA  1 
ATOM   3433  C  C   . VAL B  1 175 ? -37.922  4.824   23.058  1.00 39.26  ? 174 VAL C C   1 
ATOM   3434  O  O   . VAL B  1 175 ? -38.631  3.906   23.461  1.00 44.66  ? 174 VAL C O   1 
ATOM   3435  C  CB  . VAL B  1 175 ? -35.404  4.599   23.304  1.00 38.03  ? 174 VAL C CB  1 
ATOM   3436  C  CG1 . VAL B  1 175 ? -35.517  3.075   23.256  1.00 42.42  ? 174 VAL C CG1 1 
ATOM   3437  C  CG2 . VAL B  1 175 ? -35.019  5.142   21.940  1.00 38.39  ? 174 VAL C CG2 1 
ATOM   3438  N  N   . CYS B  1 176 ? -38.125  5.466   21.912  1.00 41.00  ? 175 CYS C N   1 
ATOM   3439  C  CA  . CYS B  1 176 ? -39.272  5.237   21.092  1.00 42.28  ? 175 CYS C CA  1 
ATOM   3440  C  C   . CYS B  1 176 ? -38.897  5.422   19.622  1.00 42.60  ? 175 CYS C C   1 
ATOM   3441  O  O   . CYS B  1 176 ? -38.338  6.456   19.228  1.00 40.59  ? 175 CYS C O   1 
ATOM   3442  C  CB  . CYS B  1 176 ? -40.385  6.197   21.494  1.00 45.43  ? 175 CYS C CB  1 
ATOM   3443  S  SG  . CYS B  1 176 ? -41.847  6.065   20.438  1.00 46.91  ? 175 CYS C SG  1 
ATOM   3444  N  N   . VAL B  1 177 ? -39.203  4.410   18.805  1.00 39.13  ? 176 VAL C N   1 
ATOM   3445  C  CA  . VAL B  1 177 ? -38.995  4.496   17.365  1.00 41.22  ? 176 VAL C CA  1 
ATOM   3446  C  C   . VAL B  1 177 ? -40.340  4.851   16.734  1.00 44.58  ? 176 VAL C C   1 
ATOM   3447  O  O   . VAL B  1 177 ? -41.278  4.058   16.808  1.00 43.52  ? 176 VAL C O   1 
ATOM   3448  C  CB  . VAL B  1 177 ? -38.442  3.173   16.792  1.00 44.32  ? 176 VAL C CB  1 
ATOM   3449  C  CG1 . VAL B  1 177 ? -38.350  3.214   15.275  1.00 45.34  ? 176 VAL C CG1 1 
ATOM   3450  C  CG2 . VAL B  1 177 ? -37.102  2.798   17.411  1.00 45.18  ? 176 VAL C CG2 1 
ATOM   3451  N  N   . LEU B  1 178 ? -40.428  6.036   16.123  1.00 43.92  ? 177 LEU C N   1 
ATOM   3452  C  CA  . LEU B  1 178 ? -41.642  6.480   15.474  1.00 44.03  ? 177 LEU C CA  1 
ATOM   3453  C  C   . LEU B  1 178 ? -41.653  5.953   14.039  1.00 44.28  ? 177 LEU C C   1 
ATOM   3454  O  O   . LEU B  1 178 ? -40.680  6.125   13.330  1.00 42.87  ? 177 LEU C O   1 
ATOM   3455  C  CB  . LEU B  1 178 ? -41.694  8.013   15.490  1.00 48.35  ? 177 LEU C CB  1 
ATOM   3456  C  CG  . LEU B  1 178 ? -41.715  8.666   16.871  1.00 47.22  ? 177 LEU C CG  1 
ATOM   3457  C  CD1 . LEU B  1 178 ? -41.594  10.175  16.760  1.00 54.55  ? 177 LEU C CD1 1 
ATOM   3458  C  CD2 . LEU B  1 178 ? -42.981  8.319   17.617  1.00 52.12  ? 177 LEU C CD2 1 
ATOM   3459  N  N   . LYS B  1 179 ? -42.752  5.298   13.642  1.00 42.58  ? 178 LYS C N   1 
ATOM   3460  C  CA  . LYS B  1 179 ? -42.984  4.858   12.264  1.00 47.16  ? 178 LYS C CA  1 
ATOM   3461  C  C   . LYS B  1 179 ? -44.438  5.149   11.909  1.00 44.82  ? 178 LYS C C   1 
ATOM   3462  O  O   . LYS B  1 179 ? -45.305  5.176   12.786  1.00 44.14  ? 178 LYS C O   1 
ATOM   3463  C  CB  . LYS B  1 179 ? -42.738  3.353   12.079  1.00 54.10  ? 178 LYS C CB  1 
ATOM   3464  C  CG  . LYS B  1 179 ? -41.425  2.814   12.632  1.00 59.18  ? 178 LYS C CG  1 
ATOM   3465  C  CD  . LYS B  1 179 ? -40.202  3.330   11.894  1.00 71.28  ? 178 LYS C CD  1 
ATOM   3466  C  CE  . LYS B  1 179 ? -39.616  2.334   10.915  1.00 75.29  ? 178 LYS C CE  1 
ATOM   3467  N  NZ  . LYS B  1 179 ? -38.624  1.451   11.576  1.00 77.13  ? 178 LYS C NZ  1 
ATOM   3468  N  N   . GLY B  1 180 ? -44.685  5.345   10.617  1.00 48.85  ? 179 GLY C N   1 
ATOM   3469  C  CA  . GLY B  1 180 ? -46.020  5.519   10.088  1.00 53.74  ? 179 GLY C CA  1 
ATOM   3470  C  C   . GLY B  1 180 ? -46.136  4.915   8.704   1.00 57.56  ? 179 GLY C C   1 
ATOM   3471  O  O   . GLY B  1 180 ? -45.166  4.391   8.171   1.00 58.73  ? 179 GLY C O   1 
ATOM   3472  N  N   . ASP B  1 181 ? -47.337  5.002   8.130   1.00 65.10  ? 180 ASP C N   1 
ATOM   3473  C  CA  . ASP B  1 181 ? -47.600  4.500   6.787   1.00 70.38  ? 180 ASP C CA  1 
ATOM   3474  C  C   . ASP B  1 181 ? -46.849  5.342   5.751   1.00 67.75  ? 180 ASP C C   1 
ATOM   3475  O  O   . ASP B  1 181 ? -46.436  4.808   4.730   1.00 79.20  ? 180 ASP C O   1 
ATOM   3476  C  CB  . ASP B  1 181 ? -49.101  4.451   6.486   1.00 77.85  ? 180 ASP C CB  1 
ATOM   3477  C  CG  . ASP B  1 181 ? -49.725  3.108   6.828   1.00 85.43  ? 180 ASP C CG  1 
ATOM   3478  O  OD1 . ASP B  1 181 ? -49.290  2.091   6.238   1.00 86.94  ? 180 ASP C OD1 1 
ATOM   3479  O  OD2 . ASP B  1 181 ? -50.620  3.082   7.699   1.00 88.07  ? 180 ASP C OD2 1 
ATOM   3480  N  N   . GLY B  1 182 ? -46.674  6.641   6.028   1.00 62.51  ? 181 GLY C N   1 
ATOM   3481  C  CA  . GLY B  1 182 ? -45.970  7.569   5.139   1.00 56.75  ? 181 GLY C CA  1 
ATOM   3482  C  C   . GLY B  1 182 ? -44.473  7.642   5.435   1.00 55.89  ? 181 GLY C C   1 
ATOM   3483  O  O   . GLY B  1 182 ? -43.906  6.732   6.032   1.00 55.66  ? 181 GLY C O   1 
ATOM   3484  N  N   . PRO B  1 183 ? -43.789  8.742   5.037   1.00 59.69  ? 182 PRO C N   1 
ATOM   3485  C  CA  . PRO B  1 183 ? -42.333  8.850   5.168   1.00 57.98  ? 182 PRO C CA  1 
ATOM   3486  C  C   . PRO B  1 183 ? -41.823  9.285   6.544   1.00 54.92  ? 182 PRO C C   1 
ATOM   3487  O  O   . PRO B  1 183 ? -40.621  9.309   6.780   1.00 55.76  ? 182 PRO C O   1 
ATOM   3488  C  CB  . PRO B  1 183 ? -41.987  9.934   4.132   1.00 56.35  ? 182 PRO C CB  1 
ATOM   3489  C  CG  . PRO B  1 183 ? -43.202  10.844  4.116   1.00 56.46  ? 182 PRO C CG  1 
ATOM   3490  C  CD  . PRO B  1 183 ? -44.386  9.953   4.443   1.00 58.67  ? 182 PRO C CD  1 
ATOM   3491  N  N   . VAL B  1 184 ? -42.732  9.631   7.459   1.00 53.96  ? 183 VAL C N   1 
ATOM   3492  C  CA  . VAL B  1 184 ? -42.322  10.159  8.747   1.00 48.00  ? 183 VAL C CA  1 
ATOM   3493  C  C   . VAL B  1 184 ? -41.728  9.028   9.591   1.00 46.99  ? 183 VAL C C   1 
ATOM   3494  O  O   . VAL B  1 184 ? -42.348  7.980   9.782   1.00 52.00  ? 183 VAL C O   1 
ATOM   3495  C  CB  . VAL B  1 184 ? -43.494  10.842  9.471   1.00 48.28  ? 183 VAL C CB  1 
ATOM   3496  C  CG1 . VAL B  1 184 ? -43.091  11.273  10.872  1.00 47.97  ? 183 VAL C CG1 1 
ATOM   3497  C  CG2 . VAL B  1 184 ? -44.046  12.022  8.682   1.00 49.51  ? 183 VAL C CG2 1 
ATOM   3498  N  N   . GLN B  1 185 ? -40.523  9.249   10.115  1.00 44.91  ? 184 GLN C N   1 
ATOM   3499  C  CA  . GLN B  1 185 ? -39.968  8.346   11.092  1.00 46.68  ? 184 GLN C CA  1 
ATOM   3500  C  C   . GLN B  1 185 ? -38.914  9.061   11.931  1.00 43.37  ? 184 GLN C C   1 
ATOM   3501  O  O   . GLN B  1 185 ? -38.358  10.070  11.520  1.00 44.04  ? 184 GLN C O   1 
ATOM   3502  C  CB  . GLN B  1 185 ? -39.371  7.113   10.420  1.00 54.09  ? 184 GLN C CB  1 
ATOM   3503  C  CG  . GLN B  1 185 ? -38.280  7.429   9.418   1.00 59.30  ? 184 GLN C CG  1 
ATOM   3504  C  CD  . GLN B  1 185 ? -37.762  6.164   8.778   1.00 67.12  ? 184 GLN C CD  1 
ATOM   3505  O  OE1 . GLN B  1 185 ? -38.018  5.054   9.249   1.00 72.76  ? 184 GLN C OE1 1 
ATOM   3506  N  NE2 . GLN B  1 185 ? -37.032  6.327   7.687   1.00 63.26  ? 184 GLN C NE2 1 
ATOM   3507  N  N   . GLY B  1 186 ? -38.655  8.513   13.117  1.00 41.65  ? 185 GLY C N   1 
ATOM   3508  C  CA  . GLY B  1 186 ? -37.686  9.091   14.001  1.00 43.91  ? 185 GLY C CA  1 
ATOM   3509  C  C   . GLY B  1 186 ? -37.417  8.250   15.225  1.00 42.47  ? 185 GLY C C   1 
ATOM   3510  O  O   . GLY B  1 186 ? -37.957  7.149   15.401  1.00 42.53  ? 185 GLY C O   1 
ATOM   3511  N  N   . ILE B  1 187 ? -36.559  8.804   16.079  1.00 39.93  ? 186 ILE C N   1 
ATOM   3512  C  CA  . ILE B  1 187 ? -36.157  8.208   17.327  1.00 40.99  ? 186 ILE C CA  1 
ATOM   3513  C  C   . ILE B  1 187 ? -36.243  9.294   18.391  1.00 41.16  ? 186 ILE C C   1 
ATOM   3514  O  O   . ILE B  1 187 ? -35.751  10.406  18.180  1.00 43.18  ? 186 ILE C O   1 
ATOM   3515  C  CB  . ILE B  1 187 ? -34.733  7.626   17.214  1.00 42.65  ? 186 ILE C CB  1 
ATOM   3516  C  CG1 . ILE B  1 187 ? -34.670  6.530   16.144  1.00 47.72  ? 186 ILE C CG1 1 
ATOM   3517  C  CG2 . ILE B  1 187 ? -34.240  7.144   18.572  1.00 44.33  ? 186 ILE C CG2 1 
ATOM   3518  C  CD1 . ILE B  1 187 ? -33.299  5.895   15.965  1.00 50.85  ? 186 ILE C CD1 1 
ATOM   3519  N  N   . ILE B  1 188 ? -36.854  8.965   19.525  1.00 37.77  ? 187 ILE C N   1 
ATOM   3520  C  CA  . ILE B  1 188 ? -36.967  9.888   20.616  1.00 38.78  ? 187 ILE C CA  1 
ATOM   3521  C  C   . ILE B  1 188 ? -36.482  9.180   21.874  1.00 41.36  ? 187 ILE C C   1 
ATOM   3522  O  O   . ILE B  1 188 ? -36.932  8.070   22.183  1.00 40.57  ? 187 ILE C O   1 
ATOM   3523  C  CB  . ILE B  1 188 ? -38.407  10.419  20.765  1.00 36.68  ? 187 ILE C CB  1 
ATOM   3524  C  CG1 . ILE B  1 188 ? -38.868  11.216  19.540  1.00 36.90  ? 187 ILE C CG1 1 
ATOM   3525  C  CG2 . ILE B  1 188 ? -38.549  11.216  22.046  1.00 38.11  ? 187 ILE C CG2 1 
ATOM   3526  C  CD1 . ILE B  1 188 ? -38.129  12.533  19.320  1.00 41.22  ? 187 ILE C CD1 1 
ATOM   3527  N  N   . ASN B  1 189 ? -35.574  9.851   22.593  1.00 36.83  ? 188 ASN C N   1 
ATOM   3528  C  CA  . ASN B  1 189 ? -35.016  9.348   23.827  1.00 38.58  ? 188 ASN C CA  1 
ATOM   3529  C  C   . ASN B  1 189 ? -35.662  10.077  24.991  1.00 36.48  ? 188 ASN C C   1 
ATOM   3530  O  O   . ASN B  1 189 ? -36.101  11.227  24.858  1.00 40.26  ? 188 ASN C O   1 
ATOM   3531  C  CB  . ASN B  1 189 ? -33.497  9.528   23.897  1.00 43.31  ? 188 ASN C CB  1 
ATOM   3532  C  CG  . ASN B  1 189 ? -32.802  8.983   22.673  1.00 44.07  ? 188 ASN C CG  1 
ATOM   3533  O  OD1 . ASN B  1 189 ? -32.567  9.711   21.706  1.00 52.41  ? 188 ASN C OD1 1 
ATOM   3534  N  ND2 . ASN B  1 189 ? -32.528  7.691   22.687  1.00 47.15  ? 188 ASN C ND2 1 
ATOM   3535  N  N   . PHE B  1 190 ? -35.706  9.385   26.124  1.00 35.53  ? 189 PHE C N   1 
ATOM   3536  C  CA  . PHE B  1 190 ? -36.202  9.923   27.353  1.00 39.64  ? 189 PHE C CA  1 
ATOM   3537  C  C   . PHE B  1 190 ? -35.200  9.549   28.450  1.00 46.20  ? 189 PHE C C   1 
ATOM   3538  O  O   . PHE B  1 190 ? -34.616  8.444   28.424  1.00 42.13  ? 189 PHE C O   1 
ATOM   3539  C  CB  . PHE B  1 190 ? -37.590  9.394   27.734  1.00 40.57  ? 189 PHE C CB  1 
ATOM   3540  C  CG  . PHE B  1 190 ? -38.677  9.507   26.693  1.00 41.01  ? 189 PHE C CG  1 
ATOM   3541  C  CD1 . PHE B  1 190 ? -39.748  10.372  26.885  1.00 39.12  ? 189 PHE C CD1 1 
ATOM   3542  C  CD2 . PHE B  1 190 ? -38.663  8.703   25.559  1.00 38.78  ? 189 PHE C CD2 1 
ATOM   3543  C  CE1 . PHE B  1 190 ? -40.762  10.459  25.943  1.00 42.62  ? 189 PHE C CE1 1 
ATOM   3544  C  CE2 . PHE B  1 190 ? -39.691  8.779   24.630  1.00 41.76  ? 189 PHE C CE2 1 
ATOM   3545  C  CZ  . PHE B  1 190 ? -40.734  9.658   24.820  1.00 41.07  ? 189 PHE C CZ  1 
ATOM   3546  N  N   . GLU B  1 191 ? -35.009  10.478  29.395  1.00 49.58  ? 190 GLU C N   1 
ATOM   3547  C  CA  . GLU B  1 191 ? -34.115  10.288  30.526  1.00 53.51  ? 190 GLU C CA  1 
ATOM   3548  C  C   . GLU B  1 191 ? -34.690  11.021  31.736  1.00 50.00  ? 190 GLU C C   1 
ATOM   3549  O  O   . GLU B  1 191 ? -35.146  12.157  31.631  1.00 55.01  ? 190 GLU C O   1 
ATOM   3550  C  CB  . GLU B  1 191 ? -32.718  10.792  30.183  1.00 58.73  ? 190 GLU C CB  1 
ATOM   3551  C  CG  . GLU B  1 191 ? -31.694  10.499  31.261  1.00 64.95  ? 190 GLU C CG  1 
ATOM   3552  C  CD  . GLU B  1 191 ? -30.300  10.922  30.837  1.00 72.51  ? 190 GLU C CD  1 
ATOM   3553  O  OE1 . GLU B  1 191 ? -29.846  11.996  31.295  1.00 78.46  ? 190 GLU C OE1 1 
ATOM   3554  O  OE2 . GLU B  1 191 ? -29.693  10.195  30.021  1.00 73.11  ? 190 GLU C OE2 1 
ATOM   3555  N  N   . GLN B  1 192 ? -34.693  10.339  32.874  1.00 47.44  ? 191 GLN C N   1 
ATOM   3556  C  CA  . GLN B  1 192 ? -35.192  10.871  34.108  1.00 53.78  ? 191 GLN C CA  1 
ATOM   3557  C  C   . GLN B  1 192 ? -34.257  10.403  35.229  1.00 66.71  ? 191 GLN C C   1 
ATOM   3558  O  O   . GLN B  1 192 ? -33.969  9.208   35.343  1.00 65.50  ? 191 GLN C O   1 
ATOM   3559  C  CB  . GLN B  1 192 ? -36.630  10.410  34.340  1.00 51.68  ? 191 GLN C CB  1 
ATOM   3560  C  CG  . GLN B  1 192 ? -37.257  11.015  35.584  1.00 52.04  ? 191 GLN C CG  1 
ATOM   3561  C  CD  . GLN B  1 192 ? -38.644  10.486  35.841  1.00 55.49  ? 191 GLN C CD  1 
ATOM   3562  O  OE1 . GLN B  1 192 ? -38.946  9.333   35.531  1.00 51.88  ? 191 GLN C OE1 1 
ATOM   3563  N  NE2 . GLN B  1 192 ? -39.496  11.325  36.419  1.00 50.94  ? 191 GLN C NE2 1 
ATOM   3564  N  N   . LYS B  1 193 ? -33.800  11.356  36.050  1.00 77.59  ? 192 LYS C N   1 
ATOM   3565  C  CA  . LYS B  1 193 ? -32.806  11.103  37.093  1.00 76.11  ? 192 LYS C CA  1 
ATOM   3566  C  C   . LYS B  1 193 ? -33.465  10.584  38.377  1.00 75.26  ? 192 LYS C C   1 
ATOM   3567  O  O   . LYS B  1 193 ? -32.824  9.847   39.109  1.00 77.41  ? 192 LYS C O   1 
ATOM   3568  C  CB  . LYS B  1 193 ? -31.965  12.358  37.351  1.00 81.63  ? 192 LYS C CB  1 
ATOM   3569  C  CG  . LYS B  1 193 ? -30.593  12.379  36.684  1.00 84.22  ? 192 LYS C CG  1 
ATOM   3570  C  CD  . LYS B  1 193 ? -30.528  11.730  35.309  1.00 87.32  ? 192 LYS C CD  1 
ATOM   3571  C  CE  . LYS B  1 193 ? -30.392  10.220  35.350  1.00 88.43  ? 192 LYS C CE  1 
ATOM   3572  N  NZ  . LYS B  1 193 ? -29.407  9.732   34.359  1.00 91.70  ? 192 LYS C NZ  1 
ATOM   3573  N  N   . GLU B  1 194 ? -34.727  10.933  38.650  1.00 76.84  ? 193 GLU C N   1 
ATOM   3574  C  CA  . GLU B  1 194 ? -35.348  10.440  39.879  1.00 82.59  ? 193 GLU C CA  1 
ATOM   3575  C  C   . GLU B  1 194 ? -36.872  10.602  39.868  1.00 85.36  ? 193 GLU C C   1 
ATOM   3576  O  O   . GLU B  1 194 ? -37.421  11.362  39.078  1.00 88.62  ? 193 GLU C O   1 
ATOM   3577  C  CB  . GLU B  1 194 ? -34.749  11.177  41.077  1.00 89.32  ? 193 GLU C CB  1 
ATOM   3578  C  CG  . GLU B  1 194 ? -34.590  12.672  40.857  1.00 89.87  ? 193 GLU C CG  1 
ATOM   3579  C  CD  . GLU B  1 194 ? -33.441  13.280  41.638  1.00 91.47  ? 193 GLU C CD  1 
ATOM   3580  O  OE1 . GLU B  1 194 ? -33.156  12.780  42.745  1.00 88.76  ? 193 GLU C OE1 1 
ATOM   3581  O  OE2 . GLU B  1 194 ? -32.828  14.238  41.131  1.00 90.61  ? 193 GLU C OE2 1 
ATOM   3582  N  N   . SER B  1 195 ? -37.518  9.849   40.770  1.00 86.90  ? 194 SER C N   1 
ATOM   3583  C  CA  . SER B  1 195 ? -38.928  9.992   41.151  1.00 91.68  ? 194 SER C CA  1 
ATOM   3584  C  C   . SER B  1 195 ? -39.373  11.449  40.995  1.00 91.77  ? 194 SER C C   1 
ATOM   3585  O  O   . SER B  1 195 ? -38.715  12.352  41.506  1.00 97.66  ? 194 SER C O   1 
ATOM   3586  C  CB  . SER B  1 195 ? -39.146  9.517   42.568  1.00 93.45  ? 194 SER C CB  1 
ATOM   3587  O  OG  . SER B  1 195 ? -39.273  8.104   42.620  1.00 93.54  ? 194 SER C OG  1 
ATOM   3588  N  N   . ASN B  1 196 ? -40.518  11.640  40.331  1.00 92.29  ? 195 ASN C N   1 
ATOM   3589  C  CA  . ASN B  1 196 ? -40.897  12.899  39.666  1.00 96.38  ? 195 ASN C CA  1 
ATOM   3590  C  C   . ASN B  1 196 ? -39.802  13.958  39.861  1.00 91.73  ? 195 ASN C C   1 
ATOM   3591  O  O   . ASN B  1 196 ? -39.935  14.892  40.661  1.00 93.44  ? 195 ASN C O   1 
ATOM   3592  C  CB  . ASN B  1 196 ? -42.285  13.406  40.075  1.00 97.67  ? 195 ASN C CB  1 
ATOM   3593  C  CG  . ASN B  1 196 ? -42.906  14.282  39.003  1.00 99.76  ? 195 ASN C CG  1 
ATOM   3594  O  OD1 . ASN B  1 196 ? -42.642  15.482  38.934  1.00 92.08  ? 195 ASN C OD1 1 
ATOM   3595  N  ND2 . ASN B  1 196 ? -43.712  13.686  38.137  1.00 97.30  ? 195 ASN C ND2 1 
ATOM   3596  N  N   . GLY B  1 197 ? -38.696  13.742  39.143  1.00 82.42  ? 196 GLY C N   1 
ATOM   3597  C  CA  . GLY B  1 197 ? -37.830  14.780  38.641  1.00 74.69  ? 196 GLY C CA  1 
ATOM   3598  C  C   . GLY B  1 197 ? -38.169  15.001  37.173  1.00 68.33  ? 196 GLY C C   1 
ATOM   3599  O  O   . GLY B  1 197 ? -38.915  14.209  36.601  1.00 68.32  ? 196 GLY C O   1 
ATOM   3600  N  N   . PRO B  1 198 ? -37.653  16.058  36.512  1.00 59.90  ? 197 PRO C N   1 
ATOM   3601  C  CA  . PRO B  1 198 ? -38.000  16.309  35.115  1.00 58.63  ? 197 PRO C CA  1 
ATOM   3602  C  C   . PRO B  1 198 ? -37.565  15.136  34.221  1.00 53.96  ? 197 PRO C C   1 
ATOM   3603  O  O   . PRO B  1 198 ? -36.622  14.394  34.569  1.00 53.56  ? 197 PRO C O   1 
ATOM   3604  C  CB  . PRO B  1 198 ? -37.224  17.593  34.768  1.00 59.96  ? 197 PRO C CB  1 
ATOM   3605  C  CG  . PRO B  1 198 ? -36.090  17.624  35.779  1.00 60.06  ? 197 PRO C CG  1 
ATOM   3606  C  CD  . PRO B  1 198 ? -36.704  17.050  37.042  1.00 60.61  ? 197 PRO C CD  1 
ATOM   3607  N  N   . VAL B  1 199 ? -38.243  14.999  33.077  1.00 45.75  ? 198 VAL C N   1 
ATOM   3608  C  CA  . VAL B  1 199 ? -37.874  14.056  32.037  1.00 44.35  ? 198 VAL C CA  1 
ATOM   3609  C  C   . VAL B  1 199 ? -37.372  14.841  30.829  1.00 42.45  ? 198 VAL C C   1 
ATOM   3610  O  O   . VAL B  1 199 ? -38.107  15.651  30.273  1.00 45.69  ? 198 VAL C O   1 
ATOM   3611  C  CB  . VAL B  1 199 ? -39.050  13.152  31.612  1.00 42.47  ? 198 VAL C CB  1 
ATOM   3612  C  CG1 . VAL B  1 199 ? -38.626  12.187  30.514  1.00 42.84  ? 198 VAL C CG1 1 
ATOM   3613  C  CG2 . VAL B  1 199 ? -39.660  12.409  32.789  1.00 43.83  ? 198 VAL C CG2 1 
ATOM   3614  N  N   . LYS B  1 200 ? -36.139  14.544  30.418  1.00 42.96  ? 199 LYS C N   1 
ATOM   3615  C  CA  . LYS B  1 200 ? -35.538  15.064  29.208  1.00 46.45  ? 199 LYS C CA  1 
ATOM   3616  C  C   . LYS B  1 200 ? -35.979  14.183  28.036  1.00 45.24  ? 199 LYS C C   1 
ATOM   3617  O  O   . LYS B  1 200 ? -35.870  12.953  28.100  1.00 48.03  ? 199 LYS C O   1 
ATOM   3618  C  CB  . LYS B  1 200 ? -34.012  15.100  29.338  1.00 50.39  ? 199 LYS C CB  1 
ATOM   3619  C  CG  . LYS B  1 200 ? -33.482  15.987  30.464  1.00 58.65  ? 199 LYS C CG  1 
ATOM   3620  C  CD  . LYS B  1 200 ? -32.545  15.286  31.460  1.00 69.41  ? 199 LYS C CD  1 
ATOM   3621  C  CE  . LYS B  1 200 ? -33.226  14.830  32.741  1.00 73.11  ? 199 LYS C CE  1 
ATOM   3622  N  NZ  . LYS B  1 200 ? -32.473  13.750  33.431  1.00 71.15  ? 199 LYS C NZ  1 
ATOM   3623  N  N   . VAL B  1 201 ? -36.462  14.842  26.980  1.00 40.05  ? 200 VAL C N   1 
ATOM   3624  C  CA  . VAL B  1 201 ? -37.008  14.235  25.786  1.00 40.87  ? 200 VAL C CA  1 
ATOM   3625  C  C   . VAL B  1 201 ? -36.276  14.844  24.592  1.00 38.24  ? 200 VAL C C   1 
ATOM   3626  O  O   . VAL B  1 201 ? -36.441  16.027  24.296  1.00 41.90  ? 200 VAL C O   1 
ATOM   3627  C  CB  . VAL B  1 201 ? -38.526  14.480  25.667  1.00 39.68  ? 200 VAL C CB  1 
ATOM   3628  C  CG1 . VAL B  1 201 ? -39.129  13.729  24.487  1.00 42.68  ? 200 VAL C CG1 1 
ATOM   3629  C  CG2 . VAL B  1 201 ? -39.258  14.156  26.955  1.00 39.27  ? 200 VAL C CG2 1 
ATOM   3630  N  N   . TRP B  1 202 ? -35.478  14.038  23.901  1.00 36.46  ? 201 TRP C N   1 
ATOM   3631  C  CA  . TRP B  1 202 ? -34.704  14.548  22.797  1.00 38.21  ? 201 TRP C CA  1 
ATOM   3632  C  C   . TRP B  1 202 ? -34.570  13.482  21.724  1.00 37.17  ? 201 TRP C C   1 
ATOM   3633  O  O   . TRP B  1 202 ? -34.566  12.303  22.028  1.00 42.42  ? 201 TRP C O   1 
ATOM   3634  C  CB  . TRP B  1 202 ? -33.324  15.024  23.282  1.00 40.10  ? 201 TRP C CB  1 
ATOM   3635  C  CG  . TRP B  1 202 ? -32.348  13.921  23.544  1.00 35.47  ? 201 TRP C CG  1 
ATOM   3636  C  CD1 . TRP B  1 202 ? -31.412  13.437  22.678  1.00 36.36  ? 201 TRP C CD1 1 
ATOM   3637  C  CD2 . TRP B  1 202 ? -32.235  13.134  24.743  1.00 37.37  ? 201 TRP C CD2 1 
ATOM   3638  N  NE1 . TRP B  1 202 ? -30.720  12.405  23.258  1.00 38.52  ? 201 TRP C NE1 1 
ATOM   3639  C  CE2 . TRP B  1 202 ? -31.197  12.204  24.527  1.00 36.67  ? 201 TRP C CE2 1 
ATOM   3640  C  CE3 . TRP B  1 202 ? -32.921  13.106  25.964  1.00 40.63  ? 201 TRP C CE3 1 
ATOM   3641  C  CZ2 . TRP B  1 202 ? -30.825  11.268  25.493  1.00 41.99  ? 201 TRP C CZ2 1 
ATOM   3642  C  CZ3 . TRP B  1 202 ? -32.548  12.189  26.923  1.00 42.69  ? 201 TRP C CZ3 1 
ATOM   3643  C  CH2 . TRP B  1 202 ? -31.515  11.279  26.688  1.00 42.35  ? 201 TRP C CH2 1 
ATOM   3644  N  N   . GLY B  1 203 ? -34.420  13.939  20.486  1.00 36.10  ? 202 GLY C N   1 
ATOM   3645  C  CA  . GLY B  1 203 ? -34.141  13.086  19.372  1.00 36.62  ? 202 GLY C CA  1 
ATOM   3646  C  C   . GLY B  1 203 ? -34.467  13.801  18.092  1.00 36.78  ? 202 GLY C C   1 
ATOM   3647  O  O   . GLY B  1 203 ? -34.462  15.018  18.057  1.00 40.71  ? 202 GLY C O   1 
ATOM   3648  N  N   . SER B  1 204 ? -34.754  13.037  17.040  1.00 37.82  ? 203 SER C N   1 
ATOM   3649  C  CA  . SER B  1 204 ? -34.966  13.590  15.738  1.00 42.17  ? 203 SER C CA  1 
ATOM   3650  C  C   . SER B  1 204 ? -36.063  12.813  15.000  1.00 44.70  ? 203 SER C C   1 
ATOM   3651  O  O   . SER B  1 204 ? -36.195  11.610  15.155  1.00 45.55  ? 203 SER C O   1 
ATOM   3652  C  CB  . SER B  1 204 ? -33.684  13.579  14.956  1.00 46.91  ? 203 SER C CB  1 
ATOM   3653  O  OG  . SER B  1 204 ? -33.879  14.225  13.709  1.00 57.65  ? 203 SER C OG  1 
ATOM   3654  N  N   . ILE B  1 205 ? -36.817  13.538  14.178  1.00 42.03  ? 204 ILE C N   1 
ATOM   3655  C  CA  . ILE B  1 205 ? -37.875  13.010  13.361  1.00 46.34  ? 204 ILE C CA  1 
ATOM   3656  C  C   . ILE B  1 205 ? -37.689  13.614  11.973  1.00 49.30  ? 204 ILE C C   1 
ATOM   3657  O  O   . ILE B  1 205 ? -37.487  14.820  11.865  1.00 50.80  ? 204 ILE C O   1 
ATOM   3658  C  CB  . ILE B  1 205 ? -39.256  13.373  13.953  1.00 43.90  ? 204 ILE C CB  1 
ATOM   3659  C  CG1 . ILE B  1 205 ? -39.410  12.914  15.405  1.00 41.57  ? 204 ILE C CG1 1 
ATOM   3660  C  CG2 . ILE B  1 205 ? -40.380  12.859  13.057  1.00 45.52  ? 204 ILE C CG2 1 
ATOM   3661  C  CD1 . ILE B  1 205 ? -40.678  13.410  16.075  1.00 43.55  ? 204 ILE C CD1 1 
ATOM   3662  N  N   . LYS B  1 206 ? -37.764  12.782  10.932  1.00 47.22  ? 205 LYS C N   1 
ATOM   3663  C  CA  . LYS B  1 206 ? -37.634  13.255  9.572   1.00 50.28  ? 205 LYS C CA  1 
ATOM   3664  C  C   . LYS B  1 206 ? -38.906  12.902  8.819   1.00 48.73  ? 205 LYS C C   1 
ATOM   3665  O  O   . LYS B  1 206 ? -39.757  12.182  9.332   1.00 50.89  ? 205 LYS C O   1 
ATOM   3666  C  CB  . LYS B  1 206 ? -36.385  12.698  8.876   1.00 60.61  ? 205 LYS C CB  1 
ATOM   3667  C  CG  . LYS B  1 206 ? -36.060  11.229  9.123   1.00 69.98  ? 205 LYS C CG  1 
ATOM   3668  C  CD  . LYS B  1 206 ? -34.571  10.902  9.069   1.00 76.88  ? 205 LYS C CD  1 
ATOM   3669  C  CE  . LYS B  1 206 ? -33.739  11.609  10.127  1.00 82.44  ? 205 LYS C CE  1 
ATOM   3670  N  NZ  . LYS B  1 206 ? -34.225  11.342  11.505  1.00 82.45  ? 205 LYS C NZ  1 
ATOM   3671  N  N   . GLY B  1 207 ? -39.035  13.476  7.623   1.00 44.95  ? 206 GLY C N   1 
ATOM   3672  C  CA  . GLY B  1 207 ? -40.124  13.176  6.724   1.00 46.95  ? 206 GLY C CA  1 
ATOM   3673  C  C   . GLY B  1 207 ? -41.343  14.040  6.966   1.00 47.30  ? 206 GLY C C   1 
ATOM   3674  O  O   . GLY B  1 207 ? -42.379  13.774  6.384   1.00 44.19  ? 206 GLY C O   1 
ATOM   3675  N  N   . LEU B  1 208 ? -41.210  15.081  7.801   1.00 46.31  ? 207 LEU C N   1 
ATOM   3676  C  CA  . LEU B  1 208 ? -42.341  15.959  8.160   1.00 46.32  ? 207 LEU C CA  1 
ATOM   3677  C  C   . LEU B  1 208 ? -42.417  17.131  7.185   1.00 47.27  ? 207 LEU C C   1 
ATOM   3678  O  O   . LEU B  1 208 ? -41.407  17.547  6.655   1.00 49.95  ? 207 LEU C O   1 
ATOM   3679  C  CB  . LEU B  1 208 ? -42.139  16.498  9.577   1.00 43.24  ? 207 LEU C CB  1 
ATOM   3680  C  CG  . LEU B  1 208 ? -42.180  15.449  10.676  1.00 41.80  ? 207 LEU C CG  1 
ATOM   3681  C  CD1 . LEU B  1 208 ? -41.554  15.986  11.950  1.00 41.12  ? 207 LEU C CD1 1 
ATOM   3682  C  CD2 . LEU B  1 208 ? -43.618  15.000  10.921  1.00 42.69  ? 207 LEU C CD2 1 
ATOM   3683  N  N   . THR B  1 209 ? -43.614  17.701  7.034   1.00 48.04  ? 208 THR C N   1 
ATOM   3684  C  CA  . THR B  1 209 ? -43.774  19.015  6.409   1.00 51.29  ? 208 THR C CA  1 
ATOM   3685  C  C   . THR B  1 209 ? -43.192  20.094  7.337   1.00 53.41  ? 208 THR C C   1 
ATOM   3686  O  O   . THR B  1 209 ? -43.254  19.983  8.573   1.00 50.86  ? 208 THR C O   1 
ATOM   3687  C  CB  . THR B  1 209 ? -45.242  19.307  6.084   1.00 51.37  ? 208 THR C CB  1 
ATOM   3688  O  OG1 . THR B  1 209 ? -45.975  19.312  7.310   1.00 51.17  ? 208 THR C OG1 1 
ATOM   3689  C  CG2 . THR B  1 209 ? -45.828  18.298  5.123   1.00 53.47  ? 208 THR C CG2 1 
ATOM   3690  N  N   . GLU B  1 210 ? -42.623  21.138  6.731   1.00 52.34  ? 209 GLU C N   1 
ATOM   3691  C  CA  . GLU B  1 210 ? -41.981  22.218  7.468   1.00 50.40  ? 209 GLU C CA  1 
ATOM   3692  C  C   . GLU B  1 210 ? -42.994  22.867  8.422   1.00 46.76  ? 209 GLU C C   1 
ATOM   3693  O  O   . GLU B  1 210 ? -44.123  23.158  8.047   1.00 45.59  ? 209 GLU C O   1 
ATOM   3694  C  CB  . GLU B  1 210 ? -41.437  23.257  6.484   1.00 55.31  ? 209 GLU C CB  1 
ATOM   3695  C  CG  . GLU B  1 210 ? -40.723  24.421  7.156   1.00 60.73  ? 209 GLU C CG  1 
ATOM   3696  C  CD  . GLU B  1 210 ? -40.247  25.508  6.205   1.00 65.10  ? 209 GLU C CD  1 
ATOM   3697  O  OE1 . GLU B  1 210 ? -39.674  26.497  6.699   1.00 64.01  ? 209 GLU C OE1 1 
ATOM   3698  O  OE2 . GLU B  1 210 ? -40.454  25.365  4.975   1.00 64.81  ? 209 GLU C OE2 1 
ATOM   3699  N  N   . GLY B  1 211 ? -42.573  23.109  9.663   1.00 44.23  ? 210 GLY C N   1 
ATOM   3700  C  CA  . GLY B  1 211 ? -43.410  23.813  10.620  1.00 43.69  ? 210 GLY C CA  1 
ATOM   3701  C  C   . GLY B  1 211 ? -43.738  22.958  11.833  1.00 40.76  ? 210 GLY C C   1 
ATOM   3702  O  O   . GLY B  1 211 ? -43.029  22.002  12.129  1.00 39.68  ? 210 GLY C O   1 
ATOM   3703  N  N   . LEU B  1 212 ? -44.821  23.345  12.523  1.00 38.97  ? 211 LEU C N   1 
ATOM   3704  C  CA  . LEU B  1 212 ? -45.199  22.831  13.835  1.00 38.94  ? 211 LEU C CA  1 
ATOM   3705  C  C   . LEU B  1 212 ? -46.028  21.547  13.669  1.00 35.87  ? 211 LEU C C   1 
ATOM   3706  O  O   . LEU B  1 212 ? -46.884  21.473  12.797  1.00 36.72  ? 211 LEU C O   1 
ATOM   3707  C  CB  . LEU B  1 212 ? -46.015  23.902  14.571  1.00 38.91  ? 211 LEU C CB  1 
ATOM   3708  C  CG  . LEU B  1 212 ? -45.243  25.140  15.030  1.00 44.17  ? 211 LEU C CG  1 
ATOM   3709  C  CD1 . LEU B  1 212 ? -46.182  26.184  15.622  1.00 45.49  ? 211 LEU C CD1 1 
ATOM   3710  C  CD2 . LEU B  1 212 ? -44.169  24.779  16.035  1.00 43.71  ? 211 LEU C CD2 1 
ATOM   3711  N  N   . HIS B  1 213 ? -45.787  20.570  14.547  1.00 35.02  ? 212 HIS C N   1 
ATOM   3712  C  CA  . HIS B  1 213 ? -46.566  19.318  14.602  1.00 34.68  ? 212 HIS C CA  1 
ATOM   3713  C  C   . HIS B  1 213 ? -46.823  18.950  16.063  1.00 31.75  ? 212 HIS C C   1 
ATOM   3714  O  O   . HIS B  1 213 ? -45.909  18.981  16.855  1.00 30.08  ? 212 HIS C O   1 
ATOM   3715  C  CB  . HIS B  1 213 ? -45.810  18.191  13.900  1.00 35.05  ? 212 HIS C CB  1 
ATOM   3716  C  CG  . HIS B  1 213 ? -45.599  18.419  12.448  1.00 38.73  ? 212 HIS C CG  1 
ATOM   3717  N  ND1 . HIS B  1 213 ? -46.517  18.000  11.505  1.00 37.58  ? 212 HIS C ND1 1 
ATOM   3718  C  CD2 . HIS B  1 213 ? -44.574  18.995  11.772  1.00 40.20  ? 212 HIS C CD2 1 
ATOM   3719  C  CE1 . HIS B  1 213 ? -46.070  18.321  10.305  1.00 42.66  ? 212 HIS C CE1 1 
ATOM   3720  N  NE2 . HIS B  1 213 ? -44.874  18.928  10.439  1.00 38.16  ? 212 HIS C NE2 1 
ATOM   3721  N  N   . GLY B  1 214 ? -48.081  18.627  16.397  1.00 30.28  ? 213 GLY C N   1 
ATOM   3722  C  CA  . GLY B  1 214 ? -48.437  18.155  17.723  1.00 30.46  ? 213 GLY C CA  1 
ATOM   3723  C  C   . GLY B  1 214 ? -47.677  16.885  18.054  1.00 29.50  ? 213 GLY C C   1 
ATOM   3724  O  O   . GLY B  1 214 ? -47.343  16.112  17.170  1.00 31.08  ? 213 GLY C O   1 
ATOM   3725  N  N   . PHE B  1 215 ? -47.395  16.697  19.338  1.00 30.72  ? 214 PHE C N   1 
ATOM   3726  C  CA  . PHE B  1 215 ? -46.445  15.702  19.823  1.00 33.10  ? 214 PHE C CA  1 
ATOM   3727  C  C   . PHE B  1 215 ? -46.931  15.316  21.221  1.00 34.33  ? 214 PHE C C   1 
ATOM   3728  O  O   . PHE B  1 215 ? -46.891  16.150  22.140  1.00 33.81  ? 214 PHE C O   1 
ATOM   3729  C  CB  . PHE B  1 215 ? -45.033  16.300  19.758  1.00 35.30  ? 214 PHE C CB  1 
ATOM   3730  C  CG  . PHE B  1 215 ? -43.872  15.441  20.202  1.00 34.17  ? 214 PHE C CG  1 
ATOM   3731  C  CD1 . PHE B  1 215 ? -43.346  14.465  19.368  1.00 34.91  ? 214 PHE C CD1 1 
ATOM   3732  C  CD2 . PHE B  1 215 ? -43.258  15.662  21.427  1.00 34.58  ? 214 PHE C CD2 1 
ATOM   3733  C  CE1 . PHE B  1 215 ? -42.246  13.711  19.759  1.00 33.49  ? 214 PHE C CE1 1 
ATOM   3734  C  CE2 . PHE B  1 215 ? -42.157  14.910  21.816  1.00 34.74  ? 214 PHE C CE2 1 
ATOM   3735  C  CZ  . PHE B  1 215 ? -41.648  13.946  20.975  1.00 35.80  ? 214 PHE C CZ  1 
ATOM   3736  N  N   . HIS B  1 216 ? -47.499  14.105  21.348  1.00 32.38  ? 215 HIS C N   1 
ATOM   3737  C  CA  . HIS B  1 216 ? -48.207  13.729  22.565  1.00 33.61  ? 215 HIS C CA  1 
ATOM   3738  C  C   . HIS B  1 216 ? -47.938  12.274  22.955  1.00 33.72  ? 215 HIS C C   1 
ATOM   3739  O  O   . HIS B  1 216 ? -47.669  11.429  22.118  1.00 33.44  ? 215 HIS C O   1 
ATOM   3740  C  CB  . HIS B  1 216 ? -49.717  13.899  22.422  1.00 35.83  ? 215 HIS C CB  1 
ATOM   3741  C  CG  . HIS B  1 216 ? -50.184  15.132  21.725  1.00 37.84  ? 215 HIS C CG  1 
ATOM   3742  N  ND1 . HIS B  1 216 ? -51.005  15.068  20.637  1.00 37.13  ? 215 HIS C ND1 1 
ATOM   3743  C  CD2 . HIS B  1 216 ? -50.018  16.446  22.003  1.00 38.99  ? 215 HIS C CD2 1 
ATOM   3744  C  CE1 . HIS B  1 216 ? -51.309  16.289  20.244  1.00 36.37  ? 215 HIS C CE1 1 
ATOM   3745  N  NE2 . HIS B  1 216 ? -50.714  17.152  21.063  1.00 37.94  ? 215 HIS C NE2 1 
ATOM   3746  N  N   . VAL B  1 217 ? -48.072  11.996  24.250  1.00 33.81  ? 216 VAL C N   1 
ATOM   3747  C  CA  . VAL B  1 217 ? -48.114  10.633  24.721  1.00 36.67  ? 216 VAL C CA  1 
ATOM   3748  C  C   . VAL B  1 217 ? -49.590  10.215  24.784  1.00 34.27  ? 216 VAL C C   1 
ATOM   3749  O  O   . VAL B  1 217 ? -50.415  10.887  25.400  1.00 32.74  ? 216 VAL C O   1 
ATOM   3750  C  CB  . VAL B  1 217 ? -47.378  10.440  26.061  1.00 37.01  ? 216 VAL C CB  1 
ATOM   3751  C  CG1 . VAL B  1 217 ? -47.499  9.003   26.559  1.00 38.19  ? 216 VAL C CG1 1 
ATOM   3752  C  CG2 . VAL B  1 217 ? -45.915  10.826  25.943  1.00 37.80  ? 216 VAL C CG2 1 
ATOM   3753  N  N   . HIS B  1 218 ? -49.917  9.138   24.065  1.00 34.25  ? 217 HIS C N   1 
ATOM   3754  C  CA  . HIS B  1 218 ? -51.273  8.600   24.022  1.00 34.55  ? 217 HIS C CA  1 
ATOM   3755  C  C   . HIS B  1 218 ? -51.337  7.375   24.947  1.00 36.20  ? 217 HIS C C   1 
ATOM   3756  O  O   . HIS B  1 218 ? -50.318  6.769   25.275  1.00 35.54  ? 217 HIS C O   1 
ATOM   3757  C  CB  . HIS B  1 218 ? -51.681  8.294   22.577  1.00 33.44  ? 217 HIS C CB  1 
ATOM   3758  C  CG  . HIS B  1 218 ? -52.020  9.484   21.736  1.00 35.72  ? 217 HIS C CG  1 
ATOM   3759  N  ND1 . HIS B  1 218 ? -53.239  9.600   21.095  1.00 35.53  ? 217 HIS C ND1 1 
ATOM   3760  C  CD2 . HIS B  1 218 ? -51.307  10.585  21.377  1.00 35.44  ? 217 HIS C CD2 1 
ATOM   3761  C  CE1 . HIS B  1 218 ? -53.264  10.708  20.370  1.00 33.65  ? 217 HIS C CE1 1 
ATOM   3762  N  NE2 . HIS B  1 218 ? -52.111  11.350  20.561  1.00 34.32  ? 217 HIS C NE2 1 
ATOM   3763  N  N   . GLU B  1 219 ? -52.560  7.011   25.343  1.00 37.27  ? 218 GLU C N   1 
ATOM   3764  C  CA  . GLU B  1 219 ? -52.803  6.162   26.509  1.00 38.39  ? 218 GLU C CA  1 
ATOM   3765  C  C   . GLU B  1 219 ? -52.232  4.747   26.317  1.00 33.65  ? 218 GLU C C   1 
ATOM   3766  O  O   . GLU B  1 219 ? -51.613  4.212   27.226  1.00 37.27  ? 218 GLU C O   1 
ATOM   3767  C  CB  . GLU B  1 219 ? -54.301  6.095   26.805  1.00 43.10  ? 218 GLU C CB  1 
ATOM   3768  C  CG  . GLU B  1 219 ? -54.604  5.303   28.058  1.00 44.88  ? 218 GLU C CG  1 
ATOM   3769  C  CD  . GLU B  1 219 ? -56.015  5.407   28.600  1.00 46.70  ? 218 GLU C CD  1 
ATOM   3770  O  OE1 . GLU B  1 219 ? -56.221  4.874   29.697  1.00 51.63  ? 218 GLU C OE1 1 
ATOM   3771  O  OE2 . GLU B  1 219 ? -56.897  6.012   27.938  1.00 44.83  ? 218 GLU C OE2 1 
ATOM   3772  N  N   . PHE B  1 220 ? -52.408  4.178   25.128  1.00 31.74  ? 219 PHE C N   1 
ATOM   3773  C  CA  . PHE B  1 220 ? -52.169  2.751   24.901  1.00 36.59  ? 219 PHE C CA  1 
ATOM   3774  C  C   . PHE B  1 220 ? -50.952  2.551   23.996  1.00 36.37  ? 219 PHE C C   1 
ATOM   3775  O  O   . PHE B  1 220 ? -50.802  3.241   22.971  1.00 38.47  ? 219 PHE C O   1 
ATOM   3776  C  CB  . PHE B  1 220 ? -53.428  2.090   24.326  1.00 35.84  ? 219 PHE C CB  1 
ATOM   3777  C  CG  . PHE B  1 220 ? -54.659  2.283   25.175  1.00 35.62  ? 219 PHE C CG  1 
ATOM   3778  C  CD1 . PHE B  1 220 ? -54.682  1.857   26.494  1.00 39.87  ? 219 PHE C CD1 1 
ATOM   3779  C  CD2 . PHE B  1 220 ? -55.790  2.894   24.666  1.00 39.75  ? 219 PHE C CD2 1 
ATOM   3780  C  CE1 . PHE B  1 220 ? -55.810  2.032   27.283  1.00 39.91  ? 219 PHE C CE1 1 
ATOM   3781  C  CE2 . PHE B  1 220 ? -56.921  3.066   25.456  1.00 40.48  ? 219 PHE C CE2 1 
ATOM   3782  C  CZ  . PHE B  1 220 ? -56.922  2.649   26.767  1.00 40.99  ? 219 PHE C CZ  1 
ATOM   3783  N  N   . GLY B  1 221 ? -50.085  1.614   24.406  1.00 35.86  ? 220 GLY C N   1 
ATOM   3784  C  CA  . GLY B  1 221 ? -48.962  1.126   23.591  1.00 39.24  ? 220 GLY C CA  1 
ATOM   3785  C  C   . GLY B  1 221 ? -49.403  0.039   22.625  1.00 40.64  ? 220 GLY C C   1 
ATOM   3786  O  O   . GLY B  1 221 ? -48.792  -1.052  22.525  1.00 36.79  ? 220 GLY C O   1 
ATOM   3787  N  N   . ASP B  1 222 ? -50.477  0.347   21.894  1.00 40.19  ? 221 ASP C N   1 
ATOM   3788  C  CA  . ASP B  1 222 ? -51.160  -0.611  21.043  1.00 36.45  ? 221 ASP C CA  1 
ATOM   3789  C  C   . ASP B  1 222 ? -51.126  -0.067  19.622  1.00 31.68  ? 221 ASP C C   1 
ATOM   3790  O  O   . ASP B  1 222 ? -51.809  0.894   19.328  1.00 35.61  ? 221 ASP C O   1 
ATOM   3791  C  CB  . ASP B  1 222 ? -52.584  -0.841  21.556  1.00 38.24  ? 221 ASP C CB  1 
ATOM   3792  C  CG  . ASP B  1 222 ? -53.414  -1.821  20.739  1.00 39.09  ? 221 ASP C CG  1 
ATOM   3793  O  OD1 . ASP B  1 222 ? -54.433  -2.299  21.292  1.00 43.01  ? 221 ASP C OD1 1 
ATOM   3794  O  OD2 . ASP B  1 222 ? -53.050  -2.085  19.566  1.00 35.99  ? 221 ASP C OD2 1 
ATOM   3795  N  N   . ASN B  1 223 ? -50.297  -0.668  18.771  1.00 33.13  ? 222 ASN C N   1 
ATOM   3796  C  CA  . ASN B  1 223 ? -50.192  -0.260  17.375  1.00 38.67  ? 222 ASN C CA  1 
ATOM   3797  C  C   . ASN B  1 223 ? -50.754  -1.367  16.464  1.00 37.97  ? 222 ASN C C   1 
ATOM   3798  O  O   . ASN B  1 223 ? -50.427  -1.412  15.273  1.00 35.21  ? 222 ASN C O   1 
ATOM   3799  C  CB  . ASN B  1 223 ? -48.749  0.137   17.005  1.00 44.55  ? 222 ASN C CB  1 
ATOM   3800  C  CG  . ASN B  1 223 ? -48.200  1.292   17.832  1.00 52.54  ? 222 ASN C CG  1 
ATOM   3801  O  OD1 . ASN B  1 223 ? -48.943  2.023   18.506  1.00 52.79  ? 222 ASN C OD1 1 
ATOM   3802  N  ND2 . ASN B  1 223 ? -46.885  1.462   17.797  1.00 54.67  ? 222 ASN C ND2 1 
ATOM   3803  N  N   . THR B  1 224 ? -51.647  -2.213  17.000  1.00 40.19  ? 223 THR C N   1 
ATOM   3804  C  CA  . THR B  1 224 ? -52.270  -3.321  16.203  1.00 44.27  ? 223 THR C CA  1 
ATOM   3805  C  C   . THR B  1 224 ? -53.001  -2.773  14.966  1.00 43.52  ? 223 THR C C   1 
ATOM   3806  O  O   . THR B  1 224 ? -52.932  -3.387  13.919  1.00 48.26  ? 223 THR C O   1 
ATOM   3807  C  CB  . THR B  1 224 ? -53.205  -4.199  17.047  1.00 42.61  ? 223 THR C CB  1 
ATOM   3808  O  OG1 . THR B  1 224 ? -54.206  -3.373  17.635  1.00 39.96  ? 223 THR C OG1 1 
ATOM   3809  C  CG2 . THR B  1 224 ? -52.483  -4.965  18.137  1.00 41.86  ? 223 THR C CG2 1 
ATOM   3810  N  N   . ALA B  1 225 ? -53.660  -1.609  15.068  1.00 44.32  ? 224 ALA C N   1 
ATOM   3811  C  CA  . ALA B  1 225 ? -54.215  -0.927  13.878  1.00 46.58  ? 224 ALA C CA  1 
ATOM   3812  C  C   . ALA B  1 225 ? -53.418  0.351   13.549  1.00 50.84  ? 224 ALA C C   1 
ATOM   3813  O  O   . ALA B  1 225 ? -53.983  1.371   13.146  1.00 50.31  ? 224 ALA C O   1 
ATOM   3814  C  CB  . ALA B  1 225 ? -55.677  -0.627  14.110  1.00 47.50  ? 224 ALA C CB  1 
ATOM   3815  N  N   . GLY B  1 226 ? -52.089  0.286   13.685  1.00 51.40  ? 225 GLY C N   1 
ATOM   3816  C  CA  . GLY B  1 226 ? -51.244  1.473   13.579  1.00 48.30  ? 225 GLY C CA  1 
ATOM   3817  C  C   . GLY B  1 226 ? -51.557  2.478   14.681  1.00 45.61  ? 225 GLY C C   1 
ATOM   3818  O  O   . GLY B  1 226 ? -51.926  2.093   15.786  1.00 39.69  ? 225 GLY C O   1 
ATOM   3819  N  N   . CYS B  1 227 ? -51.448  3.777   14.363  1.00 42.34  ? 226 CYS C N   1 
ATOM   3820  C  CA  . CYS B  1 227 ? -51.439  4.839   15.394  1.00 41.69  ? 226 CYS C CA  1 
ATOM   3821  C  C   . CYS B  1 227 ? -52.846  5.047   15.997  1.00 39.60  ? 226 CYS C C   1 
ATOM   3822  O  O   . CYS B  1 227 ? -52.974  5.436   17.157  1.00 35.95  ? 226 CYS C O   1 
ATOM   3823  C  CB  . CYS B  1 227 ? -50.800  6.106   14.822  1.00 41.80  ? 226 CYS C CB  1 
ATOM   3824  S  SG  . CYS B  1 227 ? -49.074  5.831   14.314  1.00 44.27  ? 226 CYS C SG  1 
ATOM   3825  N  N   . THR B  1 228 ? -53.899  4.685   15.258  1.00 39.08  ? 227 THR C N   1 
ATOM   3826  C  CA  . THR B  1 228 ? -55.278  4.790   15.756  1.00 42.22  ? 227 THR C CA  1 
ATOM   3827  C  C   . THR B  1 228 ? -55.492  4.001   17.046  1.00 40.37  ? 227 THR C C   1 
ATOM   3828  O  O   . THR B  1 228 ? -56.214  4.471   17.918  1.00 38.74  ? 227 THR C O   1 
ATOM   3829  C  CB  . THR B  1 228 ? -56.329  4.253   14.783  1.00 46.08  ? 227 THR C CB  1 
ATOM   3830  O  OG1 . THR B  1 228 ? -56.027  4.766   13.492  1.00 47.58  ? 227 THR C OG1 1 
ATOM   3831  C  CG2 . THR B  1 228 ? -57.732  4.664   15.178  1.00 51.24  ? 227 THR C CG2 1 
ATOM   3832  N  N   . SER B  1 229 ? -54.882  2.815   17.169  1.00 38.63  ? 228 SER C N   1 
ATOM   3833  C  CA  . SER B  1 229 ? -55.134  1.957   18.352  1.00 39.27  ? 228 SER C CA  1 
ATOM   3834  C  C   . SER B  1 229 ? -54.476  2.522   19.616  1.00 38.73  ? 228 SER C C   1 
ATOM   3835  O  O   . SER B  1 229 ? -54.657  1.958   20.690  1.00 35.29  ? 228 SER C O   1 
ATOM   3836  C  CB  . SER B  1 229 ? -54.683  0.514   18.150  1.00 40.90  ? 228 SER C CB  1 
ATOM   3837  O  OG  . SER B  1 229 ? -54.162  0.287   16.855  1.00 43.16  ? 228 SER C OG  1 
ATOM   3838  N  N   . ALA B  1 230 ? -53.699  3.610   19.503  1.00 36.80  ? 229 ALA C N   1 
ATOM   3839  C  CA  . ALA B  1 230 ? -53.027  4.200   20.663  1.00 36.18  ? 229 ALA C CA  1 
ATOM   3840  C  C   . ALA B  1 230 ? -54.033  4.861   21.620  1.00 35.47  ? 229 ALA C C   1 
ATOM   3841  O  O   . ALA B  1 230 ? -53.719  5.113   22.792  1.00 36.52  ? 229 ALA C O   1 
ATOM   3842  C  CB  . ALA B  1 230 ? -51.984  5.180   20.183  1.00 39.17  ? 229 ALA C CB  1 
ATOM   3843  N  N   . GLY B  1 231 ? -55.247  5.129   21.129  1.00 35.86  ? 230 GLY C N   1 
ATOM   3844  C  CA  . GLY B  1 231 ? -56.296  5.766   21.913  1.00 36.47  ? 230 GLY C CA  1 
ATOM   3845  C  C   . GLY B  1 231 ? -56.065  7.272   22.041  1.00 38.06  ? 230 GLY C C   1 
ATOM   3846  O  O   . GLY B  1 231 ? -55.341  7.861   21.240  1.00 35.16  ? 230 GLY C O   1 
ATOM   3847  N  N   . PRO B  1 232 ? -56.688  7.922   23.047  1.00 40.18  ? 231 PRO C N   1 
ATOM   3848  C  CA  . PRO B  1 232 ? -56.591  9.373   23.232  1.00 41.52  ? 231 PRO C CA  1 
ATOM   3849  C  C   . PRO B  1 232 ? -55.313  9.764   23.990  1.00 40.09  ? 231 PRO C C   1 
ATOM   3850  O  O   . PRO B  1 232 ? -54.462  8.910   24.237  1.00 38.67  ? 231 PRO C O   1 
ATOM   3851  C  CB  . PRO B  1 232 ? -57.846  9.662   24.064  1.00 41.82  ? 231 PRO C CB  1 
ATOM   3852  C  CG  . PRO B  1 232 ? -57.958  8.438   24.953  1.00 41.55  ? 231 PRO C CG  1 
ATOM   3853  C  CD  . PRO B  1 232 ? -57.532  7.285   24.069  1.00 40.52  ? 231 PRO C CD  1 
ATOM   3854  N  N   . HIS B  1 233 ? -55.179  11.048  24.337  1.00 38.32  ? 232 HIS C N   1 
ATOM   3855  C  CA  . HIS B  1 233 ? -54.002  11.515  25.051  1.00 39.38  ? 232 HIS C CA  1 
ATOM   3856  C  C   . HIS B  1 233 ? -53.981  10.828  26.420  1.00 38.82  ? 232 HIS C C   1 
ATOM   3857  O  O   . HIS B  1 233 ? -55.030  10.616  27.014  1.00 40.90  ? 232 HIS C O   1 
ATOM   3858  C  CB  . HIS B  1 233 ? -53.980  13.055  25.128  1.00 39.34  ? 232 HIS C CB  1 
ATOM   3859  C  CG  . HIS B  1 233 ? -53.811  13.711  23.802  1.00 37.60  ? 232 HIS C CG  1 
ATOM   3860  N  ND1 . HIS B  1 233 ? -53.901  15.076  23.627  1.00 39.01  ? 232 HIS C ND1 1 
ATOM   3861  C  CD2 . HIS B  1 233 ? -53.562  13.183  22.582  1.00 41.37  ? 232 HIS C CD2 1 
ATOM   3862  C  CE1 . HIS B  1 233 ? -53.700  15.365  22.352  1.00 39.34  ? 232 HIS C CE1 1 
ATOM   3863  N  NE2 . HIS B  1 233 ? -53.475  14.213  21.678  1.00 42.06  ? 232 HIS C NE2 1 
ATOM   3864  N  N   . PHE B  1 234 ? -52.789  10.453  26.896  1.00 37.60  ? 233 PHE C N   1 
ATOM   3865  C  CA  . PHE B  1 234 ? -52.664  9.935   28.246  1.00 37.20  ? 233 PHE C CA  1 
ATOM   3866  C  C   . PHE B  1 234 ? -53.122  11.028  29.221  1.00 40.65  ? 233 PHE C C   1 
ATOM   3867  O  O   . PHE B  1 234 ? -52.526  12.105  29.278  1.00 39.50  ? 233 PHE C O   1 
ATOM   3868  C  CB  . PHE B  1 234 ? -51.240  9.439   28.482  1.00 37.77  ? 233 PHE C CB  1 
ATOM   3869  C  CG  . PHE B  1 234 ? -50.997  8.889   29.861  1.00 39.69  ? 233 PHE C CG  1 
ATOM   3870  C  CD1 . PHE B  1 234 ? -49.864  9.248   30.576  1.00 40.42  ? 233 PHE C CD1 1 
ATOM   3871  C  CD2 . PHE B  1 234 ? -51.898  8.009   30.445  1.00 40.04  ? 233 PHE C CD2 1 
ATOM   3872  C  CE1 . PHE B  1 234 ? -49.630  8.732   31.844  1.00 41.36  ? 233 PHE C CE1 1 
ATOM   3873  C  CE2 . PHE B  1 234 ? -51.671  7.507   31.720  1.00 38.23  ? 233 PHE C CE2 1 
ATOM   3874  C  CZ  . PHE B  1 234 ? -50.539  7.868   32.418  1.00 39.96  ? 233 PHE C CZ  1 
ATOM   3875  N  N   . ASN B  1 235 ? -54.215  10.760  29.944  1.00 36.42  ? 234 ASN C N   1 
ATOM   3876  C  CA  . ASN B  1 235 ? -54.914  11.788  30.715  1.00 39.67  ? 234 ASN C CA  1 
ATOM   3877  C  C   . ASN B  1 235 ? -55.388  11.234  32.059  1.00 42.59  ? 234 ASN C C   1 
ATOM   3878  O  O   . ASN B  1 235 ? -56.583  11.273  32.345  1.00 39.02  ? 234 ASN C O   1 
ATOM   3879  C  CB  . ASN B  1 235 ? -56.087  12.377  29.923  1.00 39.20  ? 234 ASN C CB  1 
ATOM   3880  C  CG  . ASN B  1 235 ? -56.746  13.555  30.615  1.00 39.76  ? 234 ASN C CG  1 
ATOM   3881  O  OD1 . ASN B  1 235 ? -56.151  14.192  31.485  1.00 40.28  ? 234 ASN C OD1 1 
ATOM   3882  N  ND2 . ASN B  1 235 ? -57.967  13.872  30.221  1.00 38.71  ? 234 ASN C ND2 1 
ATOM   3883  N  N   . PRO B  1 236 ? -54.484  10.731  32.934  1.00 43.55  ? 235 PRO C N   1 
ATOM   3884  C  CA  . PRO B  1 236 ? -54.894  10.136  34.207  1.00 48.95  ? 235 PRO C CA  1 
ATOM   3885  C  C   . PRO B  1 236 ? -55.619  11.068  35.193  1.00 54.89  ? 235 PRO C C   1 
ATOM   3886  O  O   . PRO B  1 236 ? -56.230  10.573  36.130  1.00 57.69  ? 235 PRO C O   1 
ATOM   3887  C  CB  . PRO B  1 236 ? -53.580  9.666   34.847  1.00 47.67  ? 235 PRO C CB  1 
ATOM   3888  C  CG  . PRO B  1 236 ? -52.510  10.487  34.156  1.00 48.44  ? 235 PRO C CG  1 
ATOM   3889  C  CD  . PRO B  1 236 ? -53.027  10.707  32.750  1.00 43.70  ? 235 PRO C CD  1 
ATOM   3890  N  N   . LEU B  1 237 ? -55.567  12.390  34.983  1.00 58.86  ? 236 LEU C N   1 
ATOM   3891  C  CA  . LEU B  1 237 ? -56.176  13.347  35.926  1.00 55.92  ? 236 LEU C CA  1 
ATOM   3892  C  C   . LEU B  1 237 ? -57.450  13.980  35.347  1.00 55.84  ? 236 LEU C C   1 
ATOM   3893  O  O   . LEU B  1 237 ? -57.983  14.915  35.940  1.00 62.10  ? 236 LEU C O   1 
ATOM   3894  C  CB  . LEU B  1 237 ? -55.128  14.402  36.296  1.00 57.57  ? 236 LEU C CB  1 
ATOM   3895  C  CG  . LEU B  1 237 ? -53.845  13.838  36.910  1.00 58.19  ? 236 LEU C CG  1 
ATOM   3896  C  CD1 . LEU B  1 237 ? -52.821  14.934  37.147  1.00 55.69  ? 236 LEU C CD1 1 
ATOM   3897  C  CD2 . LEU B  1 237 ? -54.141  13.090  38.208  1.00 59.12  ? 236 LEU C CD2 1 
ATOM   3898  N  N   . SER B  1 238 ? -57.952  13.445  34.224  1.00 52.65  ? 237 SER C N   1 
ATOM   3899  C  CA  . SER B  1 238 ? -59.203  13.902  33.576  1.00 56.29  ? 237 SER C CA  1 
ATOM   3900  C  C   . SER B  1 238 ? -59.219  15.423  33.380  1.00 55.94  ? 237 SER C C   1 
ATOM   3901  O  O   . SER B  1 238 ? -60.244  16.063  33.628  1.00 53.45  ? 237 SER C O   1 
ATOM   3902  C  CB  . SER B  1 238 ? -60.413  13.484  34.365  1.00 58.70  ? 237 SER C CB  1 
ATOM   3903  O  OG  . SER B  1 238 ? -60.381  12.095  34.621  1.00 62.48  ? 237 SER C OG  1 
ATOM   3904  N  N   . ARG B  1 239 ? -58.091  15.992  32.939  1.00 52.41  ? 238 ARG C N   1 
ATOM   3905  C  CA  . ARG B  1 239 ? -58.026  17.412  32.646  1.00 53.83  ? 238 ARG C CA  1 
ATOM   3906  C  C   . ARG B  1 239 ? -58.368  17.622  31.171  1.00 47.62  ? 238 ARG C C   1 
ATOM   3907  O  O   . ARG B  1 239 ? -58.405  16.666  30.405  1.00 48.28  ? 238 ARG C O   1 
ATOM   3908  C  CB  . ARG B  1 239 ? -56.637  17.962  32.966  1.00 55.71  ? 238 ARG C CB  1 
ATOM   3909  C  CG  . ARG B  1 239 ? -56.143  17.622  34.363  1.00 62.68  ? 238 ARG C CG  1 
ATOM   3910  C  CD  . ARG B  1 239 ? -56.586  18.595  35.434  1.00 64.40  ? 238 ARG C CD  1 
ATOM   3911  N  NE  . ARG B  1 239 ? -55.770  18.412  36.627  1.00 71.25  ? 238 ARG C NE  1 
ATOM   3912  C  CZ  . ARG B  1 239 ? -54.574  18.958  36.824  1.00 74.61  ? 238 ARG C CZ  1 
ATOM   3913  N  NH1 . ARG B  1 239 ? -53.817  18.545  37.826  1.00 76.03  ? 238 ARG C NH1 1 
ATOM   3914  N  NH2 . ARG B  1 239 ? -54.134  19.910  36.020  1.00 83.55  ? 238 ARG C NH2 1 
ATOM   3915  N  N   . LYS B  1 240 ? -58.623  18.880  30.801  1.00 44.62  ? 239 LYS C N   1 
ATOM   3916  C  CA  . LYS B  1 240 ? -58.711  19.296  29.402  1.00 44.45  ? 239 LYS C CA  1 
ATOM   3917  C  C   . LYS B  1 240 ? -57.297  19.394  28.818  1.00 39.16  ? 239 LYS C C   1 
ATOM   3918  O  O   . LYS B  1 240 ? -56.298  19.486  29.545  1.00 39.40  ? 239 LYS C O   1 
ATOM   3919  C  CB  . LYS B  1 240 ? -59.454  20.629  29.277  1.00 50.54  ? 239 LYS C CB  1 
ATOM   3920  C  CG  . LYS B  1 240 ? -60.962  20.511  29.424  1.00 57.68  ? 239 LYS C CG  1 
ATOM   3921  C  CD  . LYS B  1 240 ? -61.672  21.832  29.508  1.00 64.86  ? 239 LYS C CD  1 
ATOM   3922  C  CE  . LYS B  1 240 ? -63.120  21.667  29.919  1.00 71.43  ? 239 LYS C CE  1 
ATOM   3923  N  NZ  . LYS B  1 240 ? -63.855  22.953  29.847  1.00 73.88  ? 239 LYS C NZ  1 
ATOM   3924  N  N   . HIS B  1 241 ? -57.229  19.353  27.487  1.00 38.61  ? 240 HIS C N   1 
ATOM   3925  C  CA  . HIS B  1 241 ? -55.976  19.460  26.760  1.00 35.74  ? 240 HIS C CA  1 
ATOM   3926  C  C   . HIS B  1 241 ? -55.394  20.875  26.934  1.00 35.35  ? 240 HIS C C   1 
ATOM   3927  O  O   . HIS B  1 241 ? -56.126  21.851  26.994  1.00 34.74  ? 240 HIS C O   1 
ATOM   3928  C  CB  . HIS B  1 241 ? -56.200  19.107  25.285  1.00 35.23  ? 240 HIS C CB  1 
ATOM   3929  C  CG  . HIS B  1 241 ? -54.993  19.303  24.440  1.00 36.38  ? 240 HIS C CG  1 
ATOM   3930  N  ND1 . HIS B  1 241 ? -53.887  18.476  24.514  1.00 36.23  ? 240 HIS C ND1 1 
ATOM   3931  C  CD2 . HIS B  1 241 ? -54.710  20.254  23.524  1.00 35.01  ? 240 HIS C CD2 1 
ATOM   3932  C  CE1 . HIS B  1 241 ? -52.976  18.915  23.674  1.00 37.14  ? 240 HIS C CE1 1 
ATOM   3933  N  NE2 . HIS B  1 241 ? -53.460  19.997  23.047  1.00 37.30  ? 240 HIS C NE2 1 
ATOM   3934  N  N   . GLY B  1 242 ? -54.068  20.977  27.006  1.00 33.06  ? 241 GLY C N   1 
ATOM   3935  C  CA  . GLY B  1 242 ? -53.409  22.294  26.978  1.00 35.76  ? 241 GLY C CA  1 
ATOM   3936  C  C   . GLY B  1 242 ? -51.979  22.143  26.532  1.00 35.95  ? 241 GLY C C   1 
ATOM   3937  O  O   . GLY B  1 242 ? -51.582  21.055  26.143  1.00 35.06  ? 241 GLY C O   1 
ATOM   3938  N  N   . GLY B  1 243 ? -51.217  23.239  26.562  1.00 36.40  ? 242 GLY C N   1 
ATOM   3939  C  CA  . GLY B  1 243 ? -49.791  23.170  26.257  1.00 33.51  ? 242 GLY C CA  1 
ATOM   3940  C  C   . GLY B  1 243 ? -49.017  22.661  27.467  1.00 32.25  ? 242 GLY C C   1 
ATOM   3941  O  O   . GLY B  1 243 ? -49.515  22.668  28.585  1.00 32.43  ? 242 GLY C O   1 
ATOM   3942  N  N   . PRO B  1 244 ? -47.772  22.193  27.290  1.00 33.28  ? 243 PRO C N   1 
ATOM   3943  C  CA  . PRO B  1 244 ? -47.020  21.617  28.398  1.00 36.48  ? 243 PRO C CA  1 
ATOM   3944  C  C   . PRO B  1 244 ? -46.810  22.574  29.583  1.00 42.01  ? 243 PRO C C   1 
ATOM   3945  O  O   . PRO B  1 244 ? -46.679  22.095  30.715  1.00 36.51  ? 243 PRO C O   1 
ATOM   3946  C  CB  . PRO B  1 244 ? -45.677  21.188  27.778  1.00 36.95  ? 243 PRO C CB  1 
ATOM   3947  C  CG  . PRO B  1 244 ? -45.627  21.840  26.407  1.00 35.62  ? 243 PRO C CG  1 
ATOM   3948  C  CD  . PRO B  1 244 ? -47.051  22.160  26.019  1.00 33.62  ? 243 PRO C CD  1 
ATOM   3949  N  N   . LYS B  1 245 ? -46.831  23.893  29.323  1.00 45.11  ? 244 LYS C N   1 
ATOM   3950  C  CA  . LYS B  1 245 ? -46.561  24.905  30.351  1.00 49.82  ? 244 LYS C CA  1 
ATOM   3951  C  C   . LYS B  1 245 ? -47.845  25.287  31.092  1.00 50.24  ? 244 LYS C C   1 
ATOM   3952  O  O   . LYS B  1 245 ? -47.767  25.994  32.079  1.00 52.52  ? 244 LYS C O   1 
ATOM   3953  C  CB  . LYS B  1 245 ? -45.890  26.141  29.745  1.00 52.72  ? 244 LYS C CB  1 
ATOM   3954  C  CG  . LYS B  1 245 ? -44.373  26.072  29.643  1.00 58.24  ? 244 LYS C CG  1 
ATOM   3955  C  CD  . LYS B  1 245 ? -43.853  25.186  28.519  1.00 69.53  ? 244 LYS C CD  1 
ATOM   3956  C  CE  . LYS B  1 245 ? -42.608  25.735  27.844  1.00 72.96  ? 244 LYS C CE  1 
ATOM   3957  N  NZ  . LYS B  1 245 ? -42.934  26.834  26.903  1.00 75.42  ? 244 LYS C NZ  1 
ATOM   3958  N  N   . ASP B  1 246 ? -49.010  24.798  30.643  1.00 47.99  ? 245 ASP C N   1 
ATOM   3959  C  CA  . ASP B  1 246 ? -50.275  25.079  31.332  1.00 49.92  ? 245 ASP C CA  1 
ATOM   3960  C  C   . ASP B  1 246 ? -50.451  24.137  32.524  1.00 51.83  ? 245 ASP C C   1 
ATOM   3961  O  O   . ASP B  1 246 ? -49.931  23.025  32.531  1.00 51.97  ? 245 ASP C O   1 
ATOM   3962  C  CB  . ASP B  1 246 ? -51.473  24.939  30.395  1.00 48.12  ? 245 ASP C CB  1 
ATOM   3963  C  CG  . ASP B  1 246 ? -51.350  25.850  29.197  1.00 49.58  ? 245 ASP C CG  1 
ATOM   3964  O  OD1 . ASP B  1 246 ? -51.890  25.503  28.130  1.00 46.72  ? 245 ASP C OD1 1 
ATOM   3965  O  OD2 . ASP B  1 246 ? -50.685  26.889  29.345  1.00 54.02  ? 245 ASP C OD2 1 
ATOM   3966  N  N   . GLU B  1 247 ? -51.221  24.596  33.512  1.00 56.02  ? 246 GLU C N   1 
ATOM   3967  C  CA  . GLU B  1 247 ? -51.639  23.759  34.626  1.00 62.27  ? 246 GLU C CA  1 
ATOM   3968  C  C   . GLU B  1 247 ? -52.746  22.805  34.156  1.00 57.23  ? 246 GLU C C   1 
ATOM   3969  O  O   . GLU B  1 247 ? -52.710  21.616  34.473  1.00 55.23  ? 246 GLU C O   1 
ATOM   3970  C  CB  . GLU B  1 247 ? -52.109  24.609  35.807  1.00 73.36  ? 246 GLU C CB  1 
ATOM   3971  C  CG  . GLU B  1 247 ? -52.626  23.773  36.969  1.00 82.20  ? 246 GLU C CG  1 
ATOM   3972  C  CD  . GLU B  1 247 ? -52.163  24.222  38.342  1.00 89.19  ? 246 GLU C CD  1 
ATOM   3973  O  OE1 . GLU B  1 247 ? -52.083  25.447  38.569  1.00 94.11  ? 246 GLU C OE1 1 
ATOM   3974  O  OE2 . GLU B  1 247 ? -51.878  23.341  39.180  1.00 97.42  ? 246 GLU C OE2 1 
ATOM   3975  N  N   . GLU B  1 248 ? -53.724  23.334  33.410  1.00 49.79  ? 247 GLU C N   1 
ATOM   3976  C  CA  . GLU B  1 248 ? -54.749  22.505  32.763  1.00 47.56  ? 247 GLU C CA  1 
ATOM   3977  C  C   . GLU B  1 248 ? -54.149  21.899  31.479  1.00 41.63  ? 247 GLU C C   1 
ATOM   3978  O  O   . GLU B  1 248 ? -54.155  22.522  30.420  1.00 38.78  ? 247 GLU C O   1 
ATOM   3979  C  CB  . GLU B  1 248 ? -56.008  23.329  32.491  1.00 50.36  ? 247 GLU C CB  1 
ATOM   3980  C  CG  . GLU B  1 248 ? -57.210  22.506  32.037  1.00 56.40  ? 247 GLU C CG  1 
ATOM   3981  C  CD  . GLU B  1 248 ? -57.894  21.655  33.101  1.00 57.81  ? 247 GLU C CD  1 
ATOM   3982  O  OE1 . GLU B  1 248 ? -57.543  21.790  34.292  1.00 63.06  ? 247 GLU C OE1 1 
ATOM   3983  O  OE2 . GLU B  1 248 ? -58.785  20.850  32.736  1.00 54.89  ? 247 GLU C OE2 1 
ATOM   3984  N  N   . ARG B  1 249 ? -53.606  20.682  31.602  1.00 39.20  ? 248 ARG C N   1 
ATOM   3985  C  CA  . ARG B  1 249 ? -53.090  19.882  30.475  1.00 39.78  ? 248 ARG C CA  1 
ATOM   3986  C  C   . ARG B  1 249 ? -53.276  18.382  30.766  1.00 41.59  ? 248 ARG C C   1 
ATOM   3987  O  O   . ARG B  1 249 ? -53.447  17.980  31.926  1.00 39.60  ? 248 ARG C O   1 
ATOM   3988  C  CB  . ARG B  1 249 ? -51.606  20.179  30.265  1.00 37.49  ? 248 ARG C CB  1 
ATOM   3989  C  CG  . ARG B  1 249 ? -50.751  19.868  31.481  1.00 37.42  ? 248 ARG C CG  1 
ATOM   3990  C  CD  . ARG B  1 249 ? -49.265  19.858  31.186  1.00 39.14  ? 248 ARG C CD  1 
ATOM   3991  N  NE  . ARG B  1 249 ? -48.795  18.606  30.616  1.00 38.66  ? 248 ARG C NE  1 
ATOM   3992  C  CZ  . ARG B  1 249 ? -47.515  18.300  30.467  1.00 41.25  ? 248 ARG C CZ  1 
ATOM   3993  N  NH1 . ARG B  1 249 ? -47.150  17.078  30.099  1.00 36.24  ? 248 ARG C NH1 1 
ATOM   3994  N  NH2 . ARG B  1 249 ? -46.595  19.221  30.708  1.00 38.25  ? 248 ARG C NH2 1 
ATOM   3995  N  N   . HIS B  1 250 ? -53.249  17.565  29.706  1.00 40.16  ? 249 HIS C N   1 
ATOM   3996  C  CA  . HIS B  1 250 ? -53.118  16.112  29.844  1.00 38.45  ? 249 HIS C CA  1 
ATOM   3997  C  C   . HIS B  1 250 ? -51.681  15.793  30.280  1.00 37.53  ? 249 HIS C C   1 
ATOM   3998  O  O   . HIS B  1 250 ? -50.730  16.537  29.971  1.00 35.01  ? 249 HIS C O   1 
ATOM   3999  C  CB  . HIS B  1 250 ? -53.475  15.382  28.538  1.00 37.68  ? 249 HIS C CB  1 
ATOM   4000  C  CG  . HIS B  1 250 ? -54.841  15.668  28.004  1.00 35.24  ? 249 HIS C CG  1 
ATOM   4001  N  ND1 . HIS B  1 250 ? -55.134  15.689  26.645  1.00 33.34  ? 249 HIS C ND1 1 
ATOM   4002  C  CD2 . HIS B  1 250 ? -55.998  15.932  28.646  1.00 35.65  ? 249 HIS C CD2 1 
ATOM   4003  C  CE1 . HIS B  1 250 ? -56.421  15.922  26.492  1.00 33.05  ? 249 HIS C CE1 1 
ATOM   4004  N  NE2 . HIS B  1 250 ? -56.967  16.095  27.701  1.00 33.81  ? 249 HIS C NE2 1 
ATOM   4005  N  N   . VAL B  1 251 ? -51.488  14.658  30.953  1.00 34.90  ? 250 VAL C N   1 
ATOM   4006  C  CA  . VAL B  1 251 ? -50.129  14.274  31.257  1.00 34.48  ? 250 VAL C CA  1 
ATOM   4007  C  C   . VAL B  1 251 ? -49.371  14.159  29.935  1.00 33.92  ? 250 VAL C C   1 
ATOM   4008  O  O   . VAL B  1 251 ? -48.207  14.528  29.875  1.00 36.85  ? 250 VAL C O   1 
ATOM   4009  C  CB  . VAL B  1 251 ? -50.025  12.991  32.094  1.00 35.63  ? 250 VAL C CB  1 
ATOM   4010  C  CG1 . VAL B  1 251 ? -48.641  12.360  31.983  1.00 37.61  ? 250 VAL C CG1 1 
ATOM   4011  C  CG2 . VAL B  1 251 ? -50.357  13.265  33.554  1.00 37.06  ? 250 VAL C CG2 1 
ATOM   4012  N  N   . GLY B  1 252 ? -50.040  13.672  28.877  1.00 34.57  ? 251 GLY C N   1 
ATOM   4013  C  CA  . GLY B  1 252 ? -49.374  13.400  27.582  1.00 35.09  ? 251 GLY C CA  1 
ATOM   4014  C  C   . GLY B  1 252 ? -49.192  14.610  26.653  1.00 35.51  ? 251 GLY C C   1 
ATOM   4015  O  O   . GLY B  1 252 ? -48.639  14.453  25.567  1.00 35.64  ? 251 GLY C O   1 
ATOM   4016  N  N   A SER B  1 253 ? -49.650  15.805  27.048  0.30 36.11  ? 252 SER C N   1 
ATOM   4017  C  CA  A SER B  1 253 ? -49.648  16.977  26.152  0.30 36.43  ? 252 SER C CA  1 
ATOM   4018  C  C   A SER B  1 253 ? -48.280  17.672  26.159  0.30 35.22  ? 252 SER C C   1 
ATOM   4019  O  O   A SER B  1 253 ? -48.068  18.618  26.918  0.30 36.54  ? 252 SER C O   1 
ATOM   4020  C  CB  A SER B  1 253 ? -50.781  17.918  26.509  0.30 36.03  ? 252 SER C CB  1 
ATOM   4021  O  OG  A SER B  1 253 ? -52.032  17.443  26.004  0.30 37.47  ? 252 SER C OG  1 
ATOM   4022  N  N   B ASP B  1 253 ? -49.619  15.798  27.112  0.70 34.71  ? 252 ASP C N   1 
ATOM   4023  C  CA  B ASP B  1 253 ? -49.538  17.027  26.338  0.70 34.99  ? 252 ASP C CA  1 
ATOM   4024  C  C   B ASP B  1 253 ? -48.111  17.561  26.318  0.70 34.07  ? 252 ASP C C   1 
ATOM   4025  O  O   B ASP B  1 253 ? -47.683  18.280  27.226  0.70 37.11  ? 252 ASP C O   1 
ATOM   4026  C  CB  B ASP B  1 253 ? -50.458  18.104  26.900  0.70 33.77  ? 252 ASP C CB  1 
ATOM   4027  C  CG  B ASP B  1 253 ? -51.900  17.707  26.733  0.70 35.08  ? 252 ASP C CG  1 
ATOM   4028  O  OD1 B ASP B  1 253 ? -52.116  16.628  26.154  0.70 42.54  ? 252 ASP C OD1 1 
ATOM   4029  O  OD2 B ASP B  1 253 ? -52.775  18.456  27.176  0.70 36.11  ? 252 ASP C OD2 1 
ATOM   4030  N  N   . LEU B  1 254 ? -47.381  17.231  25.260  1.00 32.64  ? 253 LEU C N   1 
ATOM   4031  C  CA  . LEU B  1 254 ? -46.007  17.711  25.180  1.00 34.64  ? 253 LEU C CA  1 
ATOM   4032  C  C   . LEU B  1 254 ? -45.874  18.818  24.125  1.00 32.59  ? 253 LEU C C   1 
ATOM   4033  O  O   . LEU B  1 254 ? -44.777  19.104  23.713  1.00 36.23  ? 253 LEU C O   1 
ATOM   4034  C  CB  . LEU B  1 254 ? -45.076  16.542  24.849  1.00 35.45  ? 253 LEU C CB  1 
ATOM   4035  C  CG  . LEU B  1 254 ? -44.918  15.473  25.928  1.00 37.20  ? 253 LEU C CG  1 
ATOM   4036  C  CD1 . LEU B  1 254 ? -43.999  14.370  25.428  1.00 40.03  ? 253 LEU C CD1 1 
ATOM   4037  C  CD2 . LEU B  1 254 ? -44.408  16.051  27.235  1.00 39.15  ? 253 LEU C CD2 1 
ATOM   4038  N  N   . GLY B  1 255 ? -46.987  19.387  23.662  1.00 31.17  ? 254 GLY C N   1 
ATOM   4039  C  CA  . GLY B  1 255 ? -46.949  20.558  22.809  1.00 33.58  ? 254 GLY C CA  1 
ATOM   4040  C  C   . GLY B  1 255 ? -46.604  20.217  21.370  1.00 37.48  ? 254 GLY C C   1 
ATOM   4041  O  O   . GLY B  1 255 ? -47.143  19.252  20.790  1.00 34.65  ? 254 GLY C O   1 
ATOM   4042  N  N   . ASN B  1 256 ? -45.713  21.025  20.784  1.00 32.29  ? 255 ASN C N   1 
ATOM   4043  C  CA  . ASN B  1 256 ? -45.395  20.968  19.375  1.00 32.59  ? 255 ASN C CA  1 
ATOM   4044  C  C   . ASN B  1 256 ? -43.909  20.666  19.198  1.00 32.64  ? 255 ASN C C   1 
ATOM   4045  O  O   . ASN B  1 256 ? -43.090  21.038  20.053  1.00 33.61  ? 255 ASN C O   1 
ATOM   4046  C  CB  . ASN B  1 256 ? -45.719  22.287  18.676  1.00 34.84  ? 255 ASN C CB  1 
ATOM   4047  C  CG  . ASN B  1 256 ? -47.187  22.440  18.356  1.00 34.65  ? 255 ASN C CG  1 
ATOM   4048  O  OD1 . ASN B  1 256 ? -47.700  21.737  17.488  1.00 32.80  ? 255 ASN C OD1 1 
ATOM   4049  N  ND2 . ASN B  1 256 ? -47.850  23.370  19.024  1.00 33.02  ? 255 ASN C ND2 1 
ATOM   4050  N  N   . VAL B  1 257 ? -43.583  20.017  18.076  1.00 31.99  ? 256 VAL C N   1 
ATOM   4051  C  CA  . VAL B  1 257 ? -42.218  19.942  17.581  1.00 31.60  ? 256 VAL C CA  1 
ATOM   4052  C  C   . VAL B  1 257 ? -42.174  20.723  16.268  1.00 33.23  ? 256 VAL C C   1 
ATOM   4053  O  O   . VAL B  1 257 ? -43.221  20.945  15.636  1.00 35.81  ? 256 VAL C O   1 
ATOM   4054  C  CB  . VAL B  1 257 ? -41.710  18.499  17.395  1.00 32.38  ? 256 VAL C CB  1 
ATOM   4055  C  CG1 . VAL B  1 257 ? -41.656  17.750  18.713  1.00 35.60  ? 256 VAL C CG1 1 
ATOM   4056  C  CG2 . VAL B  1 257 ? -42.518  17.730  16.363  1.00 32.12  ? 256 VAL C CG2 1 
ATOM   4057  N  N   . THR B  1 258 ? -40.961  21.108  15.846  1.00 34.85  ? 257 THR C N   1 
ATOM   4058  C  CA  . THR B  1 258 ? -40.791  21.963  14.673  1.00 37.02  ? 257 THR C CA  1 
ATOM   4059  C  C   . THR B  1 258 ? -39.906  21.268  13.637  1.00 37.44  ? 257 THR C C   1 
ATOM   4060  O  O   . THR B  1 258 ? -38.772  20.888  13.944  1.00 38.73  ? 257 THR C O   1 
ATOM   4061  C  CB  . THR B  1 258 ? -40.188  23.326  15.048  1.00 40.72  ? 257 THR C CB  1 
ATOM   4062  O  OG1 . THR B  1 258 ? -41.016  23.911  16.058  1.00 39.78  ? 257 THR C OG1 1 
ATOM   4063  C  CG2 . THR B  1 258 ? -40.077  24.243  13.846  1.00 38.25  ? 257 THR C CG2 1 
ATOM   4064  N  N   . ALA B  1 259 ? -40.454  21.115  12.430  1.00 37.85  ? 258 ALA C N   1 
ATOM   4065  C  CA  . ALA B  1 259 ? -39.740  20.579  11.282  1.00 43.50  ? 258 ALA C CA  1 
ATOM   4066  C  C   . ALA B  1 259 ? -39.191  21.740  10.436  1.00 44.88  ? 258 ALA C C   1 
ATOM   4067  O  O   . ALA B  1 259 ? -39.930  22.668  10.082  1.00 41.79  ? 258 ALA C O   1 
ATOM   4068  C  CB  . ALA B  1 259 ? -40.645  19.701  10.455  1.00 44.04  ? 258 ALA C CB  1 
ATOM   4069  N  N   . ASP B  1 260 ? -37.898  21.653  10.112  1.00 47.90  ? 259 ASP C N   1 
ATOM   4070  C  CA  . ASP B  1 260 ? -37.218  22.612  9.241   1.00 51.28  ? 259 ASP C CA  1 
ATOM   4071  C  C   . ASP B  1 260 ? -37.648  22.364  7.789   1.00 55.29  ? 259 ASP C C   1 
ATOM   4072  O  O   . ASP B  1 260 ? -38.523  21.534  7.513   1.00 55.57  ? 259 ASP C O   1 
ATOM   4073  C  CB  . ASP B  1 260 ? -35.708  22.576  9.506   1.00 52.11  ? 259 ASP C CB  1 
ATOM   4074  C  CG  . ASP B  1 260 ? -35.004  21.303  9.062   1.00 54.36  ? 259 ASP C CG  1 
ATOM   4075  O  OD1 . ASP B  1 260 ? -34.023  20.923  9.736   1.00 52.67  ? 259 ASP C OD1 1 
ATOM   4076  O  OD2 . ASP B  1 260 ? -35.444  20.695  8.058   1.00 54.97  ? 259 ASP C OD2 1 
ATOM   4077  N  N   . LYS B  1 261 ? -37.062  23.144  6.875   1.00 62.34  ? 260 LYS C N   1 
ATOM   4078  C  CA  . LYS B  1 261 ? -37.356  23.108  5.428   1.00 63.92  ? 260 LYS C CA  1 
ATOM   4079  C  C   . LYS B  1 261 ? -36.956  21.760  4.801   1.00 58.89  ? 260 LYS C C   1 
ATOM   4080  O  O   . LYS B  1 261 ? -37.496  21.406  3.758   1.00 53.99  ? 260 LYS C O   1 
ATOM   4081  C  CB  . LYS B  1 261 ? -36.703  24.299  4.707   1.00 71.10  ? 260 LYS C CB  1 
ATOM   4082  C  CG  . LYS B  1 261 ? -35.179  24.305  4.561   1.00 76.93  ? 260 LYS C CG  1 
ATOM   4083  C  CD  . LYS B  1 261 ? -34.376  24.118  5.848   1.00 85.25  ? 260 LYS C CD  1 
ATOM   4084  C  CE  . LYS B  1 261 ? -34.485  25.275  6.828   1.00 90.15  ? 260 LYS C CE  1 
ATOM   4085  N  NZ  . LYS B  1 261 ? -33.330  26.200  6.749   1.00 94.11  ? 260 LYS C NZ  1 
ATOM   4086  N  N   . ASP B  1 262 ? -36.046  21.009  5.443   1.00 59.54  ? 261 ASP C N   1 
ATOM   4087  C  CA  . ASP B  1 262 ? -35.682  19.634  5.016   1.00 61.99  ? 261 ASP C CA  1 
ATOM   4088  C  C   . ASP B  1 262 ? -36.594  18.583  5.677   1.00 62.95  ? 261 ASP C C   1 
ATOM   4089  O  O   . ASP B  1 262 ? -36.264  17.392  5.684   1.00 58.80  ? 261 ASP C O   1 
ATOM   4090  C  CB  . ASP B  1 262 ? -34.221  19.315  5.352   1.00 63.78  ? 261 ASP C CB  1 
ATOM   4091  C  CG  . ASP B  1 262 ? -33.204  20.253  4.716   1.00 69.11  ? 261 ASP C CG  1 
ATOM   4092  O  OD1 . ASP B  1 262 ? -33.511  20.828  3.645   1.00 62.34  ? 261 ASP C OD1 1 
ATOM   4093  O  OD2 . ASP B  1 262 ? -32.110  20.406  5.301   1.00 70.33  ? 261 ASP C OD2 1 
ATOM   4094  N  N   . GLY B  1 263 ? -37.718  19.021  6.259   1.00 59.86  ? 262 GLY C N   1 
ATOM   4095  C  CA  . GLY B  1 263 ? -38.673  18.149  6.938   1.00 53.31  ? 262 GLY C CA  1 
ATOM   4096  C  C   . GLY B  1 263 ? -38.083  17.418  8.133   1.00 52.96  ? 262 GLY C C   1 
ATOM   4097  O  O   . GLY B  1 263 ? -38.579  16.357  8.508   1.00 52.98  ? 262 GLY C O   1 
ATOM   4098  N  N   . VAL B  1 264 ? -37.056  17.995  8.769   1.00 49.12  ? 263 VAL C N   1 
ATOM   4099  C  CA  . VAL B  1 264 ? -36.448  17.386  9.936   1.00 46.96  ? 263 VAL C CA  1 
ATOM   4100  C  C   . VAL B  1 264 ? -36.818  18.200  11.176  1.00 49.48  ? 263 VAL C C   1 
ATOM   4101  O  O   . VAL B  1 264 ? -36.687  19.433  11.174  1.00 48.54  ? 263 VAL C O   1 
ATOM   4102  C  CB  . VAL B  1 264 ? -34.922  17.286  9.796   1.00 49.93  ? 263 VAL C CB  1 
ATOM   4103  C  CG1 . VAL B  1 264 ? -34.273  16.831  11.097  1.00 48.42  ? 263 VAL C CG1 1 
ATOM   4104  C  CG2 . VAL B  1 264 ? -34.528  16.380  8.633   1.00 52.56  ? 263 VAL C CG2 1 
ATOM   4105  N  N   . ALA B  1 265 ? -37.252  17.490  12.227  1.00 45.64  ? 264 ALA C N   1 
ATOM   4106  C  CA  . ALA B  1 265 ? -37.475  18.054  13.541  1.00 44.16  ? 264 ALA C CA  1 
ATOM   4107  C  C   . ALA B  1 265 ? -36.430  17.476  14.489  1.00 46.30  ? 264 ALA C C   1 
ATOM   4108  O  O   . ALA B  1 265 ? -36.427  16.283  14.758  1.00 43.75  ? 264 ALA C O   1 
ATOM   4109  C  CB  . ALA B  1 265 ? -38.874  17.764  14.036  1.00 43.23  ? 264 ALA C CB  1 
ATOM   4110  N  N   . ASP B  1 266 ? -35.528  18.342  14.957  1.00 44.15  ? 265 ASP C N   1 
ATOM   4111  C  CA  . ASP B  1 266 ? -34.752  18.066  16.136  1.00 45.96  ? 265 ASP C CA  1 
ATOM   4112  C  C   . ASP B  1 266 ? -35.678  18.344  17.312  1.00 44.98  ? 265 ASP C C   1 
ATOM   4113  O  O   . ASP B  1 266 ? -36.393  19.333  17.301  1.00 51.29  ? 265 ASP C O   1 
ATOM   4114  C  CB  . ASP B  1 266 ? -33.469  18.904  16.175  1.00 52.83  ? 265 ASP C CB  1 
ATOM   4115  C  CG  . ASP B  1 266 ? -32.484  18.550  15.072  1.00 56.13  ? 265 ASP C CG  1 
ATOM   4116  O  OD1 . ASP B  1 266 ? -32.086  19.471  14.334  1.00 65.20  ? 265 ASP C OD1 1 
ATOM   4117  O  OD2 . ASP B  1 266 ? -32.138  17.349  14.947  1.00 62.58  ? 265 ASP C OD2 1 
ATOM   4118  N  N   . VAL B  1 267 ? -35.695  17.444  18.289  1.00 41.41  ? 266 VAL C N   1 
ATOM   4119  C  CA  . VAL B  1 267 ? -36.588  17.556  19.398  1.00 40.06  ? 266 VAL C CA  1 
ATOM   4120  C  C   . VAL B  1 267 ? -35.741  17.681  20.658  1.00 39.67  ? 266 VAL C C   1 
ATOM   4121  O  O   . VAL B  1 267 ? -34.813  16.921  20.875  1.00 36.99  ? 266 VAL C O   1 
ATOM   4122  C  CB  . VAL B  1 267 ? -37.557  16.353  19.490  1.00 42.08  ? 266 VAL C CB  1 
ATOM   4123  C  CG1 . VAL B  1 267 ? -38.360  16.371  20.778  1.00 39.44  ? 266 VAL C CG1 1 
ATOM   4124  C  CG2 . VAL B  1 267 ? -38.486  16.287  18.294  1.00 40.64  ? 266 VAL C CG2 1 
ATOM   4125  N  N   . SER B  1 268 ? -36.111  18.640  21.500  1.00 40.58  ? 267 SER C N   1 
ATOM   4126  C  CA  . SER B  1 268 ? -35.506  18.793  22.780  1.00 43.23  ? 267 SER C CA  1 
ATOM   4127  C  C   . SER B  1 268 ? -36.477  19.552  23.683  1.00 45.02  ? 267 SER C C   1 
ATOM   4128  O  O   . SER B  1 268 ? -36.768  20.748  23.480  1.00 46.78  ? 267 SER C O   1 
ATOM   4129  C  CB  . SER B  1 268 ? -34.165  19.481  22.689  1.00 47.63  ? 267 SER C CB  1 
ATOM   4130  O  OG  . SER B  1 268 ? -33.486  19.365  23.928  1.00 47.25  ? 267 SER C OG  1 
ATOM   4131  N  N   . ILE B  1 269 ? -36.959  18.819  24.683  1.00 42.62  ? 268 ILE C N   1 
ATOM   4132  C  CA  . ILE B  1 269 ? -38.017  19.211  25.552  1.00 45.57  ? 268 ILE C CA  1 
ATOM   4133  C  C   . ILE B  1 269 ? -37.627  18.733  26.954  1.00 45.24  ? 268 ILE C C   1 
ATOM   4134  O  O   . ILE B  1 269 ? -36.958  17.718  27.101  1.00 44.40  ? 268 ILE C O   1 
ATOM   4135  C  CB  . ILE B  1 269 ? -39.331  18.588  25.025  1.00 49.41  ? 268 ILE C CB  1 
ATOM   4136  C  CG1 . ILE B  1 269 ? -39.868  19.352  23.809  1.00 51.24  ? 268 ILE C CG1 1 
ATOM   4137  C  CG2 . ILE B  1 269 ? -40.373  18.465  26.120  1.00 47.86  ? 268 ILE C CG2 1 
ATOM   4138  C  CD1 . ILE B  1 269 ? -40.949  18.608  23.035  1.00 53.89  ? 268 ILE C CD1 1 
ATOM   4139  N  N   . GLU B  1 270 ? -38.035  19.475  27.978  1.00 45.16  ? 269 GLU C N   1 
ATOM   4140  C  CA  . GLU B  1 270 ? -37.944  19.008  29.335  1.00 47.92  ? 269 GLU C CA  1 
ATOM   4141  C  C   . GLU B  1 270 ? -39.336  19.141  29.943  1.00 45.69  ? 269 GLU C C   1 
ATOM   4142  O  O   . GLU B  1 270 ? -39.976  20.172  29.787  1.00 44.28  ? 269 GLU C O   1 
ATOM   4143  C  CB  . GLU B  1 270 ? -36.883  19.799  30.107  1.00 54.01  ? 269 GLU C CB  1 
ATOM   4144  C  CG  . GLU B  1 270 ? -36.450  19.118  31.392  1.00 57.91  ? 269 GLU C CG  1 
ATOM   4145  C  CD  . GLU B  1 270 ? -35.295  19.781  32.134  1.00 64.67  ? 269 GLU C CD  1 
ATOM   4146  O  OE1 . GLU B  1 270 ? -35.432  19.995  33.359  1.00 64.56  ? 269 GLU C OE1 1 
ATOM   4147  O  OE2 . GLU B  1 270 ? -34.255  20.061  31.493  1.00 64.12  ? 269 GLU C OE2 1 
ATOM   4148  N  N   . ASP B  1 271 ? -39.829  18.073  30.571  1.00 41.75  ? 270 ASP C N   1 
ATOM   4149  C  CA  . ASP B  1 271 ? -41.181  18.087  31.110  1.00 42.73  ? 270 ASP C CA  1 
ATOM   4150  C  C   . ASP B  1 271 ? -41.154  17.378  32.457  1.00 44.28  ? 270 ASP C C   1 
ATOM   4151  O  O   . ASP B  1 271 ? -40.429  16.392  32.630  1.00 47.14  ? 270 ASP C O   1 
ATOM   4152  C  CB  . ASP B  1 271 ? -42.188  17.449  30.142  1.00 43.06  ? 270 ASP C CB  1 
ATOM   4153  C  CG  . ASP B  1 271 ? -43.631  17.625  30.581  1.00 45.58  ? 270 ASP C CG  1 
ATOM   4154  O  OD1 . ASP B  1 271 ? -44.167  16.712  31.256  1.00 44.97  ? 270 ASP C OD1 1 
ATOM   4155  O  OD2 . ASP B  1 271 ? -44.206  18.690  30.286  1.00 50.35  ? 270 ASP C OD2 1 
ATOM   4156  N  N   . SER B  1 272 ? -41.932  17.894  33.408  1.00 44.55  ? 271 SER C N   1 
ATOM   4157  C  CA  . SER B  1 272 ? -41.901  17.363  34.762  1.00 51.63  ? 271 SER C CA  1 
ATOM   4158  C  C   . SER B  1 272 ? -43.259  16.755  35.140  1.00 51.58  ? 271 SER C C   1 
ATOM   4159  O  O   . SER B  1 272 ? -43.436  16.320  36.282  1.00 52.56  ? 271 SER C O   1 
ATOM   4160  C  CB  . SER B  1 272 ? -41.460  18.425  35.740  1.00 54.37  ? 271 SER C CB  1 
ATOM   4161  O  OG  . SER B  1 272 ? -42.354  19.524  35.699  1.00 59.68  ? 271 SER C OG  1 
ATOM   4162  N  N   . VAL B  1 273 ? -44.190  16.684  34.175  1.00 45.26  ? 272 VAL C N   1 
ATOM   4163  C  CA  . VAL B  1 273 ? -45.507  16.091  34.415  1.00 46.79  ? 272 VAL C CA  1 
ATOM   4164  C  C   . VAL B  1 273 ? -45.482  14.612  33.992  1.00 45.01  ? 272 VAL C C   1 
ATOM   4165  O  O   . VAL B  1 273 ? -45.957  13.744  34.718  1.00 42.65  ? 272 VAL C O   1 
ATOM   4166  C  CB  . VAL B  1 273 ? -46.632  16.881  33.721  1.00 46.20  ? 272 VAL C CB  1 
ATOM   4167  C  CG1 . VAL B  1 273 ? -47.990  16.212  33.907  1.00 46.23  ? 272 VAL C CG1 1 
ATOM   4168  C  CG2 . VAL B  1 273 ? -46.678  18.324  34.213  1.00 46.59  ? 272 VAL C CG2 1 
ATOM   4169  N  N   . ILE B  1 274 ? -44.927  14.324  32.817  1.00 43.84  ? 273 ILE C N   1 
ATOM   4170  C  CA  . ILE B  1 274 ? -44.665  12.950  32.477  1.00 44.56  ? 273 ILE C CA  1 
ATOM   4171  C  C   . ILE B  1 274 ? -43.674  12.410  33.507  1.00 45.83  ? 273 ILE C C   1 
ATOM   4172  O  O   . ILE B  1 274 ? -43.016  13.172  34.222  1.00 48.13  ? 273 ILE C O   1 
ATOM   4173  C  CB  . ILE B  1 274 ? -44.156  12.774  31.034  1.00 41.92  ? 273 ILE C CB  1 
ATOM   4174  C  CG1 . ILE B  1 274 ? -42.865  13.556  30.766  1.00 42.65  ? 273 ILE C CG1 1 
ATOM   4175  C  CG2 . ILE B  1 274 ? -45.260  13.125  30.049  1.00 42.26  ? 273 ILE C CG2 1 
ATOM   4176  C  CD1 . ILE B  1 274 ? -42.113  13.121  29.528  1.00 40.38  ? 273 ILE C CD1 1 
ATOM   4177  N  N   . SER B  1 275 ? -43.608  11.083  33.572  1.00 45.93  ? 274 SER C N   1 
ATOM   4178  C  CA  . SER B  1 275 ? -42.664  10.358  34.384  1.00 45.52  ? 274 SER C CA  1 
ATOM   4179  C  C   . SER B  1 275 ? -42.318  9.066   33.649  1.00 48.60  ? 274 SER C C   1 
ATOM   4180  O  O   . SER B  1 275 ? -43.065  8.662   32.736  1.00 46.20  ? 274 SER C O   1 
ATOM   4181  C  CB  . SER B  1 275 ? -43.217  10.089  35.761  1.00 46.13  ? 274 SER C CB  1 
ATOM   4182  O  OG  . SER B  1 275 ? -42.202  9.578   36.613  1.00 51.77  ? 274 SER C OG  1 
ATOM   4183  N  N   . LEU B  1 276 ? -41.187  8.460   34.027  1.00 46.56  ? 275 LEU C N   1 
ATOM   4184  C  CA  . LEU B  1 276 ? -40.787  7.149   33.517  1.00 47.95  ? 275 LEU C CA  1 
ATOM   4185  C  C   . LEU B  1 276 ? -41.066  6.054   34.557  1.00 49.70  ? 275 LEU C C   1 
ATOM   4186  O  O   . LEU B  1 276 ? -40.663  4.918   34.353  1.00 53.93  ? 275 LEU C O   1 
ATOM   4187  C  CB  . LEU B  1 276 ? -39.302  7.169   33.141  1.00 46.41  ? 275 LEU C CB  1 
ATOM   4188  C  CG  . LEU B  1 276 ? -38.898  8.090   31.991  1.00 44.22  ? 275 LEU C CG  1 
ATOM   4189  C  CD1 . LEU B  1 276 ? -37.526  7.695   31.473  1.00 42.77  ? 275 LEU C CD1 1 
ATOM   4190  C  CD2 . LEU B  1 276 ? -39.912  8.077   30.851  1.00 42.03  ? 275 LEU C CD2 1 
ATOM   4191  N  N   . SER B  1 277 ? -41.736  6.405   35.661  1.00 51.05  ? 276 SER C N   1 
ATOM   4192  C  CA  . SER B  1 277 ? -42.201  5.434   36.637  1.00 54.67  ? 276 SER C CA  1 
ATOM   4193  C  C   . SER B  1 277 ? -43.400  6.009   37.399  1.00 53.13  ? 276 SER C C   1 
ATOM   4194  O  O   . SER B  1 277 ? -43.643  7.205   37.359  1.00 54.47  ? 276 SER C O   1 
ATOM   4195  C  CB  . SER B  1 277 ? -41.084  5.017   37.563  1.00 59.85  ? 276 SER C CB  1 
ATOM   4196  O  OG  . SER B  1 277 ? -40.719  6.074   38.438  1.00 58.85  ? 276 SER C OG  1 
ATOM   4197  N  N   . GLY B  1 278 ? -44.175  5.129   38.040  1.00 53.12  ? 277 GLY C N   1 
ATOM   4198  C  CA  . GLY B  1 278 ? -45.312  5.521   38.881  1.00 50.91  ? 277 GLY C CA  1 
ATOM   4199  C  C   . GLY B  1 278 ? -46.582  5.757   38.081  1.00 49.30  ? 277 GLY C C   1 
ATOM   4200  O  O   . GLY B  1 278 ? -46.661  5.391   36.923  1.00 51.90  ? 277 GLY C O   1 
ATOM   4201  N  N   . ASP B  1 279 ? -47.566  6.390   38.733  1.00 51.36  ? 278 ASP C N   1 
ATOM   4202  C  CA  . ASP B  1 279 ? -48.901  6.683   38.198  1.00 59.30  ? 278 ASP C CA  1 
ATOM   4203  C  C   . ASP B  1 279 ? -48.847  7.392   36.836  1.00 58.17  ? 278 ASP C C   1 
ATOM   4204  O  O   . ASP B  1 279 ? -49.745  7.217   36.013  1.00 61.86  ? 278 ASP C O   1 
ATOM   4205  C  CB  . ASP B  1 279 ? -49.694  7.585   39.150  1.00 66.60  ? 278 ASP C CB  1 
ATOM   4206  C  CG  . ASP B  1 279 ? -50.167  6.907   40.427  1.00 76.37  ? 278 ASP C CG  1 
ATOM   4207  O  OD1 . ASP B  1 279 ? -50.867  7.578   41.221  1.00 80.03  ? 278 ASP C OD1 1 
ATOM   4208  O  OD2 . ASP B  1 279 ? -49.834  5.718   40.623  1.00 82.65  ? 278 ASP C OD2 1 
ATOM   4209  N  N   . HIS B  1 280 ? -47.842  8.249   36.633  1.00 53.90  ? 279 HIS C N   1 
ATOM   4210  C  CA  . HIS B  1 280 ? -47.724  9.044   35.411  1.00 51.65  ? 279 HIS C CA  1 
ATOM   4211  C  C   . HIS B  1 280 ? -46.695  8.426   34.448  1.00 51.42  ? 279 HIS C C   1 
ATOM   4212  O  O   . HIS B  1 280 ? -46.288  9.089   33.480  1.00 47.25  ? 279 HIS C O   1 
ATOM   4213  C  CB  . HIS B  1 280 ? -47.392  10.501  35.769  1.00 53.45  ? 279 HIS C CB  1 
ATOM   4214  C  CG  . HIS B  1 280 ? -48.529  11.244  36.386  1.00 53.44  ? 279 HIS C CG  1 
ATOM   4215  N  ND1 . HIS B  1 280 ? -48.546  12.626  36.467  1.00 56.37  ? 279 HIS C ND1 1 
ATOM   4216  C  CD2 . HIS B  1 280 ? -49.692  10.813  36.927  1.00 55.28  ? 279 HIS C CD2 1 
ATOM   4217  C  CE1 . HIS B  1 280 ? -49.664  13.013  37.052  1.00 54.80  ? 279 HIS C CE1 1 
ATOM   4218  N  NE2 . HIS B  1 280 ? -50.390  11.916  37.336  1.00 54.49  ? 279 HIS C NE2 1 
ATOM   4219  N  N   . SER B  1 281 ? -46.269  7.173   34.696  1.00 46.80  ? 280 SER C N   1 
ATOM   4220  C  CA  . SER B  1 281 ? -45.307  6.529   33.796  1.00 43.12  ? 280 SER C CA  1 
ATOM   4221  C  C   . SER B  1 281 ? -45.896  6.474   32.384  1.00 40.61  ? 280 SER C C   1 
ATOM   4222  O  O   . SER B  1 281 ? -47.087  6.231   32.213  1.00 42.07  ? 280 SER C O   1 
ATOM   4223  C  CB  . SER B  1 281 ? -44.898  5.158   34.252  1.00 44.76  ? 280 SER C CB  1 
ATOM   4224  O  OG  . SER B  1 281 ? -43.893  4.633   33.391  1.00 42.87  ? 280 SER C OG  1 
ATOM   4225  N  N   . ILE B  1 282 ? -45.035  6.713   31.392  1.00 41.07  ? 281 ILE C N   1 
ATOM   4226  C  CA  . ILE B  1 282 ? -45.366  6.615   29.973  1.00 42.21  ? 281 ILE C CA  1 
ATOM   4227  C  C   . ILE B  1 282 ? -44.691  5.376   29.370  1.00 37.25  ? 281 ILE C C   1 
ATOM   4228  O  O   . ILE B  1 282 ? -44.774  5.147   28.180  1.00 37.06  ? 281 ILE C O   1 
ATOM   4229  C  CB  . ILE B  1 282 ? -44.957  7.911   29.240  1.00 43.81  ? 281 ILE C CB  1 
ATOM   4230  C  CG1 . ILE B  1 282 ? -43.438  8.133   29.252  1.00 43.52  ? 281 ILE C CG1 1 
ATOM   4231  C  CG2 . ILE B  1 282 ? -45.714  9.102   29.817  1.00 43.07  ? 281 ILE C CG2 1 
ATOM   4232  C  CD1 . ILE B  1 282 ? -42.987  9.344   28.447  1.00 44.19  ? 281 ILE C CD1 1 
ATOM   4233  N  N   . ILE B  1 283 ? -43.989  4.590   30.193  1.00 41.10  ? 282 ILE C N   1 
ATOM   4234  C  CA  . ILE B  1 283 ? -43.432  3.327   29.732  1.00 40.42  ? 282 ILE C CA  1 
ATOM   4235  C  C   . ILE B  1 283 ? -44.611  2.450   29.255  1.00 39.57  ? 282 ILE C C   1 
ATOM   4236  O  O   . ILE B  1 283 ? -45.648  2.328   29.940  1.00 38.57  ? 282 ILE C O   1 
ATOM   4237  C  CB  . ILE B  1 283 ? -42.584  2.648   30.827  1.00 43.98  ? 282 ILE C CB  1 
ATOM   4238  C  CG1 . ILE B  1 283 ? -41.434  3.546   31.308  1.00 46.64  ? 282 ILE C CG1 1 
ATOM   4239  C  CG2 . ILE B  1 283 ? -42.077  1.291   30.351  1.00 43.59  ? 282 ILE C CG2 1 
ATOM   4240  C  CD1 . ILE B  1 283 ? -40.445  3.954   30.222  1.00 44.23  ? 282 ILE C CD1 1 
ATOM   4241  N  N   . GLY B  1 284 ? -44.477  1.927   28.034  1.00 38.96  ? 283 GLY C N   1 
ATOM   4242  C  CA  . GLY B  1 284 ? -45.481  1.065   27.425  1.00 42.00  ? 283 GLY C CA  1 
ATOM   4243  C  C   . GLY B  1 284 ? -46.646  1.825   26.803  1.00 41.92  ? 283 GLY C C   1 
ATOM   4244  O  O   . GLY B  1 284 ? -47.604  1.206   26.321  1.00 38.51  ? 283 GLY C O   1 
ATOM   4245  N  N   . ARG B  1 285 ? -46.589  3.161   26.791  1.00 38.08  ? 284 ARG C N   1 
ATOM   4246  C  CA  . ARG B  1 285 ? -47.601  3.966   26.098  1.00 36.47  ? 284 ARG C CA  1 
ATOM   4247  C  C   . ARG B  1 285 ? -47.059  4.344   24.725  1.00 34.26  ? 284 ARG C C   1 
ATOM   4248  O  O   . ARG B  1 285 ? -45.984  3.881   24.353  1.00 38.37  ? 284 ARG C O   1 
ATOM   4249  C  CB  . ARG B  1 285 ? -47.996  5.138   26.990  1.00 38.10  ? 284 ARG C CB  1 
ATOM   4250  C  CG  . ARG B  1 285 ? -48.488  4.669   28.350  1.00 40.67  ? 284 ARG C CG  1 
ATOM   4251  C  CD  . ARG B  1 285 ? -49.225  5.725   29.129  1.00 40.97  ? 284 ARG C CD  1 
ATOM   4252  N  NE  . ARG B  1 285 ? -49.440  5.244   30.483  1.00 40.63  ? 284 ARG C NE  1 
ATOM   4253  C  CZ  . ARG B  1 285 ? -50.495  4.543   30.879  1.00 41.89  ? 284 ARG C CZ  1 
ATOM   4254  N  NH1 . ARG B  1 285 ? -50.595  4.179   32.147  1.00 43.80  ? 284 ARG C NH1 1 
ATOM   4255  N  NH2 . ARG B  1 285 ? -51.446  4.216   30.015  1.00 39.05  ? 284 ARG C NH2 1 
ATOM   4256  N  N   . THR B  1 286 ? -47.833  5.124   23.959  1.00 35.32  ? 285 THR C N   1 
ATOM   4257  C  CA  . THR B  1 286 ? -47.471  5.458   22.578  1.00 35.60  ? 285 THR C CA  1 
ATOM   4258  C  C   . THR B  1 286 ? -47.082  6.943   22.495  1.00 37.32  ? 285 THR C C   1 
ATOM   4259  O  O   . THR B  1 286 ? -47.765  7.796   23.072  1.00 38.21  ? 285 THR C O   1 
ATOM   4260  C  CB  . THR B  1 286 ? -48.593  5.092   21.597  1.00 36.53  ? 285 THR C CB  1 
ATOM   4261  O  OG1 . THR B  1 286 ? -48.711  3.669   21.567  1.00 40.59  ? 285 THR C OG1 1 
ATOM   4262  C  CG2 . THR B  1 286 ? -48.342  5.533   20.172  1.00 35.26  ? 285 THR C CG2 1 
ATOM   4263  N  N   . LEU B  1 287 ? -45.990  7.235   21.770  1.00 38.03  ? 286 LEU C N   1 
ATOM   4264  C  CA  . LEU B  1 287 ? -45.647  8.592   21.383  1.00 36.05  ? 286 LEU C CA  1 
ATOM   4265  C  C   . LEU B  1 287 ? -46.151  8.825   19.957  1.00 33.92  ? 286 LEU C C   1 
ATOM   4266  O  O   . LEU B  1 287 ? -45.862  8.032   19.061  1.00 33.26  ? 286 LEU C O   1 
ATOM   4267  C  CB  . LEU B  1 287 ? -44.130  8.772   21.485  1.00 38.56  ? 286 LEU C CB  1 
ATOM   4268  C  CG  . LEU B  1 287 ? -43.613  10.191  21.220  1.00 40.37  ? 286 LEU C CG  1 
ATOM   4269  C  CD1 . LEU B  1 287 ? -44.095  11.156  22.293  1.00 40.34  ? 286 LEU C CD1 1 
ATOM   4270  C  CD2 . LEU B  1 287 ? -42.092  10.203  21.149  1.00 40.11  ? 286 LEU C CD2 1 
ATOM   4271  N  N   . VAL B  1 288 ? -46.862  9.941   19.743  1.00 32.49  ? 287 VAL C N   1 
ATOM   4272  C  CA  . VAL B  1 288 ? -47.458  10.261  18.452  1.00 32.11  ? 287 VAL C CA  1 
ATOM   4273  C  C   . VAL B  1 288 ? -46.979  11.638  17.974  1.00 33.92  ? 287 VAL C C   1 
ATOM   4274  O  O   . VAL B  1 288 ? -46.959  12.579  18.761  1.00 33.34  ? 287 VAL C O   1 
ATOM   4275  C  CB  . VAL B  1 288 ? -48.991  10.234  18.560  1.00 33.27  ? 287 VAL C CB  1 
ATOM   4276  C  CG1 . VAL B  1 288 ? -49.654  10.608  17.249  1.00 32.97  ? 287 VAL C CG1 1 
ATOM   4277  C  CG2 . VAL B  1 288 ? -49.486  8.881   19.069  1.00 35.09  ? 287 VAL C CG2 1 
ATOM   4278  N  N   . VAL B  1 289 ? -46.658  11.743  16.678  1.00 31.97  ? 288 VAL C N   1 
ATOM   4279  C  CA  . VAL B  1 289 ? -46.446  13.026  16.009  1.00 34.58  ? 288 VAL C CA  1 
ATOM   4280  C  C   . VAL B  1 289 ? -47.576  13.227  14.997  1.00 33.19  ? 288 VAL C C   1 
ATOM   4281  O  O   . VAL B  1 289 ? -47.902  12.341  14.205  1.00 34.16  ? 288 VAL C O   1 
ATOM   4282  C  CB  . VAL B  1 289 ? -45.042  13.150  15.371  1.00 37.60  ? 288 VAL C CB  1 
ATOM   4283  C  CG1 . VAL B  1 289 ? -44.769  12.087  14.316  1.00 35.86  ? 288 VAL C CG1 1 
ATOM   4284  C  CG2 . VAL B  1 289 ? -44.818  14.539  14.786  1.00 37.94  ? 288 VAL C CG2 1 
ATOM   4285  N  N   . HIS B  1 290 ? -48.168  14.424  15.031  1.00 33.86  ? 289 HIS C N   1 
ATOM   4286  C  CA  . HIS B  1 290 ? -49.373  14.730  14.305  1.00 31.79  ? 289 HIS C CA  1 
ATOM   4287  C  C   . HIS B  1 290 ? -49.083  15.514  13.022  1.00 36.89  ? 289 HIS C C   1 
ATOM   4288  O  O   . HIS B  1 290 ? -47.998  16.070  12.803  1.00 38.51  ? 289 HIS C O   1 
ATOM   4289  C  CB  . HIS B  1 290 ? -50.355  15.486  15.196  1.00 32.35  ? 289 HIS C CB  1 
ATOM   4290  C  CG  . HIS B  1 290 ? -51.000  14.648  16.248  1.00 32.01  ? 289 HIS C CG  1 
ATOM   4291  N  ND1 . HIS B  1 290 ? -52.222  14.053  16.044  1.00 31.17  ? 289 HIS C ND1 1 
ATOM   4292  C  CD2 . HIS B  1 290 ? -50.636  14.353  17.518  1.00 33.07  ? 289 HIS C CD2 1 
ATOM   4293  C  CE1 . HIS B  1 290 ? -52.581  13.394  17.126  1.00 33.94  ? 289 HIS C CE1 1 
ATOM   4294  N  NE2 . HIS B  1 290 ? -51.639  13.585  18.064  1.00 31.79  ? 289 HIS C NE2 1 
ATOM   4295  N  N   . GLU B  1 291 ? -50.121  15.542  12.190  1.00 37.71  ? 290 GLU C N   1 
ATOM   4296  C  CA  . GLU B  1 291 ? -50.174  16.172  10.886  1.00 43.42  ? 290 GLU C CA  1 
ATOM   4297  C  C   . GLU B  1 291 ? -50.082  17.701  11.013  1.00 41.64  ? 290 GLU C C   1 
ATOM   4298  O  O   . GLU B  1 291 ? -49.371  18.325  10.234  1.00 41.48  ? 290 GLU C O   1 
ATOM   4299  C  CB  . GLU B  1 291 ? -51.488  15.745  10.228  1.00 45.19  ? 290 GLU C CB  1 
ATOM   4300  C  CG  . GLU B  1 291 ? -51.732  16.323  8.851   1.00 50.94  ? 290 GLU C CG  1 
ATOM   4301  C  CD  . GLU B  1 291 ? -53.170  16.153  8.385   1.00 58.18  ? 290 GLU C CD  1 
ATOM   4302  O  OE1 . GLU B  1 291 ? -53.365  16.041  7.167   1.00 67.14  ? 290 GLU C OE1 1 
ATOM   4303  O  OE2 . GLU B  1 291 ? -54.093  16.135  9.247   1.00 60.77  ? 290 GLU C OE2 1 
ATOM   4304  N  N   . LYS B  1 292 ? -50.836  18.285  11.961  1.00 39.26  ? 291 LYS C N   1 
ATOM   4305  C  CA  . LYS B  1 292 ? -50.958  19.756  12.091  1.00 42.28  ? 291 LYS C CA  1 
ATOM   4306  C  C   . LYS B  1 292 ? -50.412  20.219  13.456  1.00 38.24  ? 291 LYS C C   1 
ATOM   4307  O  O   . LYS B  1 292 ? -50.122  19.422  14.336  1.00 35.00  ? 291 LYS C O   1 
ATOM   4308  C  CB  . LYS B  1 292 ? -52.413  20.213  11.899  1.00 46.83  ? 291 LYS C CB  1 
ATOM   4309  C  CG  . LYS B  1 292 ? -53.273  19.371  10.957  1.00 52.88  ? 291 LYS C CG  1 
ATOM   4310  C  CD  . LYS B  1 292 ? -54.014  20.127  9.859   1.00 61.72  ? 291 LYS C CD  1 
ATOM   4311  C  CE  . LYS B  1 292 ? -54.697  21.408  10.298  1.00 70.44  ? 291 LYS C CE  1 
ATOM   4312  N  NZ  . LYS B  1 292 ? -55.510  21.228  11.527  1.00 78.12  ? 291 LYS C NZ  1 
ATOM   4313  N  N   . ALA B  1 293 ? -50.285  21.540  13.626  1.00 36.23  ? 292 ALA C N   1 
ATOM   4314  C  CA  . ALA B  1 293 ? -49.861  22.114  14.891  1.00 34.06  ? 292 ALA C CA  1 
ATOM   4315  C  C   . ALA B  1 293 ? -50.918  21.824  15.964  1.00 32.51  ? 292 ALA C C   1 
ATOM   4316  O  O   . ALA B  1 293 ? -52.113  21.757  15.677  1.00 31.72  ? 292 ALA C O   1 
ATOM   4317  C  CB  . ALA B  1 293 ? -49.647  23.604  14.745  1.00 34.51  ? 292 ALA C CB  1 
ATOM   4318  N  N   . ASP B  1 294 ? -50.441  21.646  17.198  1.00 30.52  ? 293 ASP C N   1 
ATOM   4319  C  CA  . ASP B  1 294 ? -51.244  21.636  18.369  1.00 30.42  ? 293 ASP C CA  1 
ATOM   4320  C  C   . ASP B  1 294 ? -51.525  23.095  18.763  1.00 34.16  ? 293 ASP C C   1 
ATOM   4321  O  O   . ASP B  1 294 ? -50.587  23.861  19.004  1.00 32.43  ? 293 ASP C O   1 
ATOM   4322  C  CB  . ASP B  1 294 ? -50.495  20.833  19.431  1.00 30.91  ? 293 ASP C CB  1 
ATOM   4323  C  CG  . ASP B  1 294 ? -51.193  20.647  20.764  1.00 30.96  ? 293 ASP C CG  1 
ATOM   4324  O  OD1 . ASP B  1 294 ? -52.177  21.381  21.048  1.00 29.81  ? 293 ASP C OD1 1 
ATOM   4325  O  OD2 . ASP B  1 294 ? -50.703  19.792  21.535  1.00 32.45  ? 293 ASP C OD2 1 
ATOM   4326  N  N   . ASP B  1 295 ? -52.807  23.457  18.889  1.00 30.51  ? 294 ASP C N   1 
ATOM   4327  C  CA  . ASP B  1 295 ? -53.199  24.831  19.254  1.00 30.33  ? 294 ASP C CA  1 
ATOM   4328  C  C   . ASP B  1 295 ? -53.158  25.052  20.774  1.00 28.77  ? 294 ASP C C   1 
ATOM   4329  O  O   . ASP B  1 295 ? -53.549  26.114  21.248  1.00 27.39  ? 294 ASP C O   1 
ATOM   4330  C  CB  . ASP B  1 295 ? -54.562  25.202  18.666  1.00 30.01  ? 294 ASP C CB  1 
ATOM   4331  C  CG  . ASP B  1 295 ? -55.781  24.486  19.243  1.00 31.39  ? 294 ASP C CG  1 
ATOM   4332  O  OD1 . ASP B  1 295 ? -56.812  24.485  18.534  1.00 30.76  ? 294 ASP C OD1 1 
ATOM   4333  O  OD2 . ASP B  1 295 ? -55.710  23.969  20.402  1.00 29.06  ? 294 ASP C OD2 1 
ATOM   4334  N  N   . LEU B  1 296 ? -52.716  24.048  21.541  1.00 31.09  ? 295 LEU C N   1 
ATOM   4335  C  CA  . LEU B  1 296 ? -52.468  24.186  23.010  1.00 30.41  ? 295 LEU C CA  1 
ATOM   4336  C  C   . LEU B  1 296 ? -53.754  24.572  23.756  1.00 31.83  ? 295 LEU C C   1 
ATOM   4337  O  O   . LEU B  1 296 ? -53.719  25.214  24.820  1.00 31.36  ? 295 LEU C O   1 
ATOM   4338  C  CB  . LEU B  1 296 ? -51.361  25.229  23.226  1.00 32.02  ? 295 LEU C CB  1 
ATOM   4339  C  CG  . LEU B  1 296 ? -50.129  25.072  22.332  1.00 31.54  ? 295 LEU C CG  1 
ATOM   4340  C  CD1 . LEU B  1 296 ? -49.075  26.115  22.673  1.00 33.59  ? 295 LEU C CD1 1 
ATOM   4341  C  CD2 . LEU B  1 296 ? -49.541  23.671  22.452  1.00 31.55  ? 295 LEU C CD2 1 
ATOM   4342  N  N   . GLY B  1 297 ? -54.900  24.134  23.229  1.00 31.72  ? 296 GLY C N   1 
ATOM   4343  C  CA  . GLY B  1 297 ? -56.163  24.324  23.887  1.00 32.09  ? 296 GLY C CA  1 
ATOM   4344  C  C   . GLY B  1 297 ? -56.723  25.721  23.685  1.00 31.22  ? 296 GLY C C   1 
ATOM   4345  O  O   . GLY B  1 297 ? -57.671  26.081  24.331  1.00 31.79  ? 296 GLY C O   1 
ATOM   4346  N  N   . LYS B  1 298 ? -56.191  26.476  22.724  1.00 30.11  ? 297 LYS C N   1 
ATOM   4347  C  CA  . LYS B  1 298 ? -56.610  27.887  22.536  1.00 34.98  ? 297 LYS C CA  1 
ATOM   4348  C  C   . LYS B  1 298 ? -57.395  28.068  21.224  1.00 31.63  ? 297 LYS C C   1 
ATOM   4349  O  O   . LYS B  1 298 ? -57.527  29.176  20.708  1.00 30.85  ? 297 LYS C O   1 
ATOM   4350  C  CB  . LYS B  1 298 ? -55.351  28.757  22.614  1.00 38.45  ? 297 LYS C CB  1 
ATOM   4351  C  CG  . LYS B  1 298 ? -54.638  28.671  23.962  1.00 41.85  ? 297 LYS C CG  1 
ATOM   4352  C  CD  . LYS B  1 298 ? -53.303  29.390  24.013  1.00 55.44  ? 297 LYS C CD  1 
ATOM   4353  C  CE  . LYS B  1 298 ? -53.421  30.899  23.930  1.00 59.65  ? 297 LYS C CE  1 
ATOM   4354  N  NZ  . LYS B  1 298 ? -52.135  31.556  24.270  1.00 67.09  ? 297 LYS C NZ  1 
ATOM   4355  N  N   . GLY B  1 299 ? -57.945  26.977  20.690  1.00 29.84  ? 298 GLY C N   1 
ATOM   4356  C  CA  . GLY B  1 299 ? -58.566  27.002  19.368  1.00 28.26  ? 298 GLY C CA  1 
ATOM   4357  C  C   . GLY B  1 299 ? -60.030  27.416  19.398  1.00 30.36  ? 298 GLY C C   1 
ATOM   4358  O  O   . GLY B  1 299 ? -60.623  27.647  18.337  1.00 30.73  ? 298 GLY C O   1 
ATOM   4359  N  N   . GLY B  1 300 ? -60.632  27.481  20.585  1.00 26.83  ? 299 GLY C N   1 
ATOM   4360  C  CA  . GLY B  1 300 ? -62.025  27.961  20.734  1.00 31.53  ? 299 GLY C CA  1 
ATOM   4361  C  C   . GLY B  1 300 ? -63.118  26.973  20.299  1.00 31.07  ? 299 GLY C C   1 
ATOM   4362  O  O   . GLY B  1 300 ? -64.302  27.309  20.308  1.00 28.13  ? 299 GLY C O   1 
ATOM   4363  N  N   . ASN B  1 301 ? -62.749  25.758  19.918  1.00 35.94  ? 300 ASN C N   1 
ATOM   4364  C  CA  . ASN B  1 301 ? -63.746  24.714  19.590  1.00 40.73  ? 300 ASN C CA  1 
ATOM   4365  C  C   . ASN B  1 301 ? -63.574  23.570  20.583  1.00 41.06  ? 300 ASN C C   1 
ATOM   4366  O  O   . ASN B  1 301 ? -62.606  23.548  21.325  1.00 41.09  ? 300 ASN C O   1 
ATOM   4367  C  CB  . ASN B  1 301 ? -63.649  24.248  18.132  1.00 41.20  ? 300 ASN C CB  1 
ATOM   4368  C  CG  . ASN B  1 301 ? -62.376  23.495  17.809  1.00 39.95  ? 300 ASN C CG  1 
ATOM   4369  O  OD1 . ASN B  1 301 ? -61.485  23.368  18.649  1.00 39.79  ? 300 ASN C OD1 1 
ATOM   4370  N  ND2 . ASN B  1 301 ? -62.300  22.964  16.597  1.00 36.72  ? 300 ASN C ND2 1 
ATOM   4371  N  N   . GLU B  1 302 ? -64.510  22.613  20.579  1.00 44.28  ? 301 GLU C N   1 
ATOM   4372  C  CA  . GLU B  1 302 ? -64.455  21.493  21.519  1.00 43.65  ? 301 GLU C CA  1 
ATOM   4373  C  C   . GLU B  1 302 ? -63.190  20.655  21.287  1.00 37.59  ? 301 GLU C C   1 
ATOM   4374  O  O   . GLU B  1 302 ? -62.528  20.237  22.239  1.00 39.46  ? 301 GLU C O   1 
ATOM   4375  C  CB  . GLU B  1 302 ? -65.709  20.618  21.415  1.00 52.02  ? 301 GLU C CB  1 
ATOM   4376  C  CG  . GLU B  1 302 ? -65.887  19.682  22.599  1.00 58.22  ? 301 GLU C CG  1 
ATOM   4377  C  CD  . GLU B  1 302 ? -65.953  20.368  23.957  1.00 67.37  ? 301 GLU C CD  1 
ATOM   4378  O  OE1 . GLU B  1 302 ? -65.202  19.955  24.869  1.00 79.79  ? 301 GLU C OE1 1 
ATOM   4379  O  OE2 . GLU B  1 302 ? -66.746  21.319  24.103  1.00 70.18  ? 301 GLU C OE2 1 
ATOM   4380  N  N   . GLU B  1 303 ? -62.846  20.427  20.015  1.00 39.45  ? 302 GLU C N   1 
ATOM   4381  C  CA  . GLU B  1 303 ? -61.673  19.622  19.635  1.00 40.61  ? 302 GLU C CA  1 
ATOM   4382  C  C   . GLU B  1 303 ? -60.386  20.182  20.269  1.00 39.94  ? 302 GLU C C   1 
ATOM   4383  O  O   . GLU B  1 303 ? -59.487  19.409  20.627  1.00 38.63  ? 302 GLU C O   1 
ATOM   4384  C  CB  . GLU B  1 303 ? -61.530  19.567  18.113  1.00 43.24  ? 302 GLU C CB  1 
ATOM   4385  C  CG  . GLU B  1 303 ? -60.571  18.494  17.638  1.00 47.13  ? 302 GLU C CG  1 
ATOM   4386  C  CD  . GLU B  1 303 ? -60.956  17.090  18.094  1.00 51.58  ? 302 GLU C CD  1 
ATOM   4387  O  OE1 . GLU B  1 303 ? -62.156  16.762  18.021  1.00 50.41  ? 302 GLU C OE1 1 
ATOM   4388  O  OE2 . GLU B  1 303 ? -60.068  16.343  18.553  1.00 50.64  ? 302 GLU C OE2 1 
ATOM   4389  N  N   . SER B  1 304 ? -60.298  21.516  20.397  1.00 37.26  ? 303 SER C N   1 
ATOM   4390  C  CA  . SER B  1 304 ? -59.108  22.163  20.960  1.00 37.89  ? 303 SER C CA  1 
ATOM   4391  C  C   . SER B  1 304 ? -58.803  21.588  22.348  1.00 37.91  ? 303 SER C C   1 
ATOM   4392  O  O   . SER B  1 304 ? -57.656  21.311  22.656  1.00 35.67  ? 303 SER C O   1 
ATOM   4393  C  CB  . SER B  1 304 ? -59.252  23.661  21.011  1.00 37.50  ? 303 SER C CB  1 
ATOM   4394  O  OG  . SER B  1 304 ? -58.039  24.251  21.458  1.00 34.45  ? 303 SER C OG  1 
ATOM   4395  N  N   . THR B  1 305 ? -59.856  21.368  23.146  1.00 38.54  ? 304 THR C N   1 
ATOM   4396  C  CA  . THR B  1 305 ? -59.753  20.949  24.552  1.00 40.64  ? 304 THR C CA  1 
ATOM   4397  C  C   . THR B  1 305 ? -59.524  19.433  24.679  1.00 37.65  ? 304 THR C C   1 
ATOM   4398  O  O   . THR B  1 305 ? -59.411  18.942  25.789  1.00 37.55  ? 304 THR C O   1 
ATOM   4399  C  CB  . THR B  1 305 ? -61.028  21.296  25.335  1.00 44.87  ? 304 THR C CB  1 
ATOM   4400  O  OG1 . THR B  1 305 ? -62.072  20.474  24.813  1.00 57.42  ? 304 THR C OG1 1 
ATOM   4401  C  CG2 . THR B  1 305 ? -61.452  22.744  25.228  1.00 46.95  ? 304 THR C CG2 1 
ATOM   4402  N  N   . LYS B  1 306 ? -59.446  18.709  23.557  1.00 41.33  ? 305 LYS C N   1 
ATOM   4403  C  CA  . LYS B  1 306 ? -59.250  17.232  23.549  1.00 44.32  ? 305 LYS C CA  1 
ATOM   4404  C  C   . LYS B  1 306 ? -57.923  16.863  22.873  1.00 39.43  ? 305 LYS C C   1 
ATOM   4405  O  O   . LYS B  1 306 ? -57.122  16.117  23.456  1.00 37.32  ? 305 LYS C O   1 
ATOM   4406  C  CB  . LYS B  1 306 ? -60.428  16.547  22.848  1.00 49.55  ? 305 LYS C CB  1 
ATOM   4407  C  CG  . LYS B  1 306 ? -61.753  16.650  23.599  1.00 55.03  ? 305 LYS C CG  1 
ATOM   4408  C  CD  . LYS B  1 306 ? -62.898  15.927  22.931  1.00 63.02  ? 305 LYS C CD  1 
ATOM   4409  C  CE  . LYS B  1 306 ? -63.170  16.450  21.536  1.00 69.43  ? 305 LYS C CE  1 
ATOM   4410  N  NZ  . LYS B  1 306 ? -64.524  16.078  21.056  1.00 74.88  ? 305 LYS C NZ  1 
ATOM   4411  N  N   . THR B  1 307 ? -57.696  17.393  21.660  1.00 36.87  ? 306 THR C N   1 
ATOM   4412  C  CA  . THR B  1 307 ? -56.525  17.054  20.849  1.00 36.83  ? 306 THR C CA  1 
ATOM   4413  C  C   . THR B  1 307 ? -55.724  18.284  20.382  1.00 36.23  ? 306 THR C C   1 
ATOM   4414  O  O   . THR B  1 307 ? -54.733  18.114  19.682  1.00 33.32  ? 306 THR C O   1 
ATOM   4415  C  CB  . THR B  1 307 ? -56.946  16.316  19.576  1.00 37.02  ? 306 THR C CB  1 
ATOM   4416  O  OG1 . THR B  1 307 ? -57.654  17.266  18.764  1.00 33.83  ? 306 THR C OG1 1 
ATOM   4417  C  CG2 . THR B  1 307 ? -57.774  15.081  19.873  1.00 37.95  ? 306 THR C CG2 1 
ATOM   4418  N  N   . GLY B  1 308 ? -56.183  19.498  20.709  1.00 35.75  ? 307 GLY C N   1 
ATOM   4419  C  CA  . GLY B  1 308 ? -55.580  20.741  20.218  1.00 37.65  ? 307 GLY C CA  1 
ATOM   4420  C  C   . GLY B  1 308 ? -55.645  20.871  18.699  1.00 37.74  ? 307 GLY C C   1 
ATOM   4421  O  O   . GLY B  1 308 ? -54.847  21.592  18.117  1.00 31.32  ? 307 GLY C O   1 
ATOM   4422  N  N   . ASN B  1 309 ? -56.594  20.169  18.055  1.00 33.19  ? 308 ASN C N   1 
ATOM   4423  C  CA  . ASN B  1 309 ? -56.823  20.227  16.592  1.00 32.10  ? 308 ASN C CA  1 
ATOM   4424  C  C   . ASN B  1 309 ? -55.576  19.765  15.821  1.00 29.67  ? 308 ASN C C   1 
ATOM   4425  O  O   . ASN B  1 309 ? -55.353  20.179  14.685  1.00 33.57  ? 308 ASN C O   1 
ATOM   4426  C  CB  . ASN B  1 309 ? -57.291  21.615  16.153  1.00 33.92  ? 308 ASN C CB  1 
ATOM   4427  C  CG  . ASN B  1 309 ? -58.690  21.930  16.643  1.00 37.09  ? 308 ASN C CG  1 
ATOM   4428  O  OD1 . ASN B  1 309 ? -59.653  21.324  16.185  1.00 37.91  ? 308 ASN C OD1 1 
ATOM   4429  N  ND2 . ASN B  1 309 ? -58.818  22.835  17.598  1.00 33.63  ? 308 ASN C ND2 1 
ATOM   4430  N  N   . ALA B  1 310 ? -54.786  18.876  16.426  1.00 30.50  ? 309 ALA C N   1 
ATOM   4431  C  CA  . ALA B  1 310 ? -53.502  18.415  15.860  1.00 33.61  ? 309 ALA C CA  1 
ATOM   4432  C  C   . ALA B  1 310 ? -53.707  17.522  14.627  1.00 35.83  ? 309 ALA C C   1 
ATOM   4433  O  O   . ALA B  1 310 ? -52.769  17.304  13.861  1.00 36.68  ? 309 ALA C O   1 
ATOM   4434  C  CB  . ALA B  1 310 ? -52.694  17.686  16.908  1.00 34.47  ? 309 ALA C CB  1 
ATOM   4435  N  N   . GLY B  1 311 ? -54.918  16.995  14.438  1.00 36.48  ? 310 GLY C N   1 
ATOM   4436  C  CA  . GLY B  1 311 ? -55.229  16.237  13.221  1.00 36.77  ? 310 GLY C CA  1 
ATOM   4437  C  C   . GLY B  1 311 ? -54.669  14.825  13.281  1.00 34.66  ? 310 GLY C C   1 
ATOM   4438  O  O   . GLY B  1 311 ? -54.438  14.271  14.371  1.00 31.47  ? 310 GLY C O   1 
ATOM   4439  N  N   . SER B  1 312 ? -54.435  14.244  12.099  1.00 36.93  ? 311 SER C N   1 
ATOM   4440  C  CA  . SER B  1 312 ? -54.173  12.819  11.982  1.00 40.61  ? 311 SER C CA  1 
ATOM   4441  C  C   . SER B  1 312 ? -52.789  12.499  12.552  1.00 39.78  ? 311 SER C C   1 
ATOM   4442  O  O   . SER B  1 312 ? -51.957  13.392  12.759  1.00 41.80  ? 311 SER C O   1 
ATOM   4443  C  CB  . SER B  1 312 ? -54.344  12.348  10.552  1.00 42.75  ? 311 SER C CB  1 
ATOM   4444  O  OG  . SER B  1 312 ? -53.469  13.039  9.687   1.00 48.90  ? 311 SER C OG  1 
ATOM   4445  N  N   . ARG B  1 313 ? -52.580  11.213  12.829  1.00 38.66  ? 312 ARG C N   1 
ATOM   4446  C  CA  . ARG B  1 313 ? -51.382  10.674  13.463  1.00 38.13  ? 312 ARG C CA  1 
ATOM   4447  C  C   . ARG B  1 313 ? -50.407  10.208  12.377  1.00 40.16  ? 312 ARG C C   1 
ATOM   4448  O  O   . ARG B  1 313 ? -50.668  9.222   11.721  1.00 41.95  ? 312 ARG C O   1 
ATOM   4449  C  CB  . ARG B  1 313 ? -51.777  9.519   14.387  1.00 36.13  ? 312 ARG C CB  1 
ATOM   4450  C  CG  . ARG B  1 313 ? -52.903  9.892   15.339  1.00 38.21  ? 312 ARG C CG  1 
ATOM   4451  C  CD  . ARG B  1 313 ? -53.466  8.757   16.171  1.00 38.60  ? 312 ARG C CD  1 
ATOM   4452  N  NE  . ARG B  1 313 ? -54.515  9.255   17.050  1.00 35.47  ? 312 ARG C NE  1 
ATOM   4453  C  CZ  . ARG B  1 313 ? -54.908  8.673   18.173  1.00 38.74  ? 312 ARG C CZ  1 
ATOM   4454  N  NH1 . ARG B  1 313 ? -55.798  9.282   18.938  1.00 36.62  ? 312 ARG C NH1 1 
ATOM   4455  N  NH2 . ARG B  1 313 ? -54.416  7.496   18.530  1.00 36.25  ? 312 ARG C NH2 1 
ATOM   4456  N  N   . LEU B  1 314 ? -49.286  10.915  12.194  1.00 38.59  ? 313 LEU C N   1 
ATOM   4457  C  CA  . LEU B  1 314 ? -48.377  10.636  11.072  1.00 38.40  ? 313 LEU C CA  1 
ATOM   4458  C  C   . LEU B  1 314 ? -47.467  9.458   11.392  1.00 34.16  ? 313 LEU C C   1 
ATOM   4459  O  O   . LEU B  1 314 ? -47.071  8.730   10.506  1.00 37.64  ? 313 LEU C O   1 
ATOM   4460  C  CB  . LEU B  1 314 ? -47.527  11.864  10.743  1.00 43.16  ? 313 LEU C CB  1 
ATOM   4461  C  CG  . LEU B  1 314 ? -48.292  13.082  10.235  1.00 48.87  ? 313 LEU C CG  1 
ATOM   4462  C  CD1 . LEU B  1 314 ? -47.320  14.126  9.706   1.00 52.05  ? 313 LEU C CD1 1 
ATOM   4463  C  CD2 . LEU B  1 314 ? -49.305  12.699  9.161   1.00 50.79  ? 313 LEU C CD2 1 
ATOM   4464  N  N   . ALA B  1 315 ? -47.050  9.346   12.644  1.00 34.24  ? 314 ALA C N   1 
ATOM   4465  C  CA  . ALA B  1 315 ? -46.172  8.291   13.042  1.00 35.97  ? 314 ALA C CA  1 
ATOM   4466  C  C   . ALA B  1 315 ? -46.268  8.127   14.550  1.00 34.71  ? 314 ALA C C   1 
ATOM   4467  O  O   . ALA B  1 315 ? -46.670  9.065   15.265  1.00 35.06  ? 314 ALA C O   1 
ATOM   4468  C  CB  . ALA B  1 315 ? -44.753  8.581   12.611  1.00 38.83  ? 314 ALA C CB  1 
ATOM   4469  N  N   . CYS B  1 316 ? -45.878  6.944   15.014  1.00 31.65  ? 315 CYS C N   1 
ATOM   4470  C  CA  . CYS B  1 316 ? -45.975  6.622   16.404  1.00 33.79  ? 315 CYS C CA  1 
ATOM   4471  C  C   . CYS B  1 316 ? -45.086  5.428   16.718  1.00 32.25  ? 315 CYS C C   1 
ATOM   4472  O  O   . CYS B  1 316 ? -44.622  4.728   15.821  1.00 34.65  ? 315 CYS C O   1 
ATOM   4473  C  CB  . CYS B  1 316 ? -47.414  6.316   16.823  1.00 39.14  ? 315 CYS C CB  1 
ATOM   4474  S  SG  . CYS B  1 316 ? -48.146  4.896   15.964  1.00 42.70  ? 315 CYS C SG  1 
ATOM   4475  N  N   . GLY B  1 317 ? -44.870  5.228   18.011  1.00 33.04  ? 316 GLY C N   1 
ATOM   4476  C  CA  . GLY B  1 317 ? -44.169  4.091   18.511  1.00 33.69  ? 316 GLY C CA  1 
ATOM   4477  C  C   . GLY B  1 317 ? -44.435  3.905   19.982  1.00 35.54  ? 316 GLY C C   1 
ATOM   4478  O  O   . GLY B  1 317 ? -44.926  4.820   20.679  1.00 34.01  ? 316 GLY C O   1 
ATOM   4479  N  N   . VAL B  1 318 ? -44.118  2.702   20.457  1.00 35.47  ? 317 VAL C N   1 
ATOM   4480  C  CA  . VAL B  1 318 ? -44.318  2.362   21.824  1.00 34.95  ? 317 VAL C CA  1 
ATOM   4481  C  C   . VAL B  1 318 ? -43.061  2.778   22.593  1.00 35.86  ? 317 VAL C C   1 
ATOM   4482  O  O   . VAL B  1 318 ? -41.955  2.579   22.115  1.00 39.17  ? 317 VAL C O   1 
ATOM   4483  C  CB  . VAL B  1 318 ? -44.606  0.853   21.976  1.00 36.24  ? 317 VAL C CB  1 
ATOM   4484  C  CG1 . VAL B  1 318 ? -44.914  0.492   23.418  1.00 36.49  ? 317 VAL C CG1 1 
ATOM   4485  C  CG2 . VAL B  1 318 ? -45.737  0.389   21.067  1.00 36.54  ? 317 VAL C CG2 1 
ATOM   4486  N  N   . ILE B  1 319 ? -43.256  3.304   23.802  1.00 37.47  ? 318 ILE C N   1 
ATOM   4487  C  CA  . ILE B  1 319 ? -42.168  3.823   24.614  1.00 39.97  ? 318 ILE C CA  1 
ATOM   4488  C  C   . ILE B  1 319 ? -41.629  2.681   25.477  1.00 40.68  ? 318 ILE C C   1 
ATOM   4489  O  O   . ILE B  1 319 ? -42.320  2.224   26.394  1.00 43.98  ? 318 ILE C O   1 
ATOM   4490  C  CB  . ILE B  1 319 ? -42.653  5.013   25.464  1.00 38.02  ? 318 ILE C CB  1 
ATOM   4491  C  CG1 . ILE B  1 319 ? -43.144  6.159   24.577  1.00 38.50  ? 318 ILE C CG1 1 
ATOM   4492  C  CG2 . ILE B  1 319 ? -41.574  5.473   26.426  1.00 39.14  ? 318 ILE C CG2 1 
ATOM   4493  C  CD1 . ILE B  1 319 ? -44.031  7.146   25.307  1.00 38.02  ? 318 ILE C CD1 1 
ATOM   4494  N  N   . GLY B  1 320 ? -40.396  2.254   25.177  1.00 40.54  ? 319 GLY C N   1 
ATOM   4495  C  CA  . GLY B  1 320 ? -39.775  1.120   25.825  1.00 45.79  ? 319 GLY C CA  1 
ATOM   4496  C  C   . GLY B  1 320 ? -38.620  1.508   26.738  1.00 47.88  ? 319 GLY C C   1 
ATOM   4497  O  O   . GLY B  1 320 ? -38.096  2.632   26.685  1.00 37.76  ? 319 GLY C O   1 
ATOM   4498  N  N   . ILE B  1 321 ? -38.225  0.547   27.579  1.00 44.72  ? 320 ILE C N   1 
ATOM   4499  C  CA  . ILE B  1 321 ? -37.146  0.708   28.530  1.00 47.89  ? 320 ILE C CA  1 
ATOM   4500  C  C   . ILE B  1 321 ? -35.818  0.594   27.775  1.00 51.26  ? 320 ILE C C   1 
ATOM   4501  O  O   . ILE B  1 321 ? -35.636  -0.279  26.922  1.00 45.68  ? 320 ILE C O   1 
ATOM   4502  C  CB  . ILE B  1 321 ? -37.268  -0.310  29.679  1.00 48.26  ? 320 ILE C CB  1 
ATOM   4503  C  CG1 . ILE B  1 321 ? -38.584  -0.123  30.435  1.00 50.04  ? 320 ILE C CG1 1 
ATOM   4504  C  CG2 . ILE B  1 321 ? -36.065  -0.234  30.608  1.00 48.97  ? 320 ILE C CG2 1 
ATOM   4505  C  CD1 . ILE B  1 321 ? -38.911  -1.236  31.412  1.00 53.25  ? 320 ILE C CD1 1 
ATOM   4506  N  N   . ALA B  1 322 ? -34.908  1.531   28.067  1.00 53.18  ? 321 ALA C N   1 
ATOM   4507  C  CA  . ALA B  1 322 ? -33.583  1.564   27.466  1.00 54.31  ? 321 ALA C CA  1 
ATOM   4508  C  C   . ALA B  1 322 ? -32.524  1.514   28.581  1.00 58.48  ? 321 ALA C C   1 
ATOM   4509  O  O   . ALA B  1 322 ? -32.855  1.567   29.778  1.00 54.53  ? 321 ALA C O   1 
ATOM   4510  C  CB  . ALA B  1 322 ? -33.479  2.810   26.617  1.00 56.18  ? 321 ALA C CB  1 
ATOM   4511  N  N   . GLN B  1 323 ? -31.249  1.387   28.199  1.00 72.54  ? 322 GLN C N   1 
ATOM   4512  C  CA  . GLN B  1 323 ? -30.137  1.857   29.064  1.00 80.40  ? 322 GLN C CA  1 
ATOM   4513  C  C   . GLN B  1 323 ? -28.898  2.070   28.196  1.00 82.14  ? 322 GLN C C   1 
ATOM   4514  O  O   . GLN B  1 323 ? -29.030  2.538   27.068  1.00 87.31  ? 322 GLN C O   1 
ATOM   4515  C  CB  . GLN B  1 323 ? -29.843  0.897   30.219  1.00 79.69  ? 322 GLN C CB  1 
ATOM   4516  C  CG  . GLN B  1 323 ? -29.622  1.608   31.553  1.00 79.35  ? 322 GLN C CG  1 
ATOM   4517  C  CD  . GLN B  1 323 ? -30.760  1.449   32.536  1.00 81.86  ? 322 GLN C CD  1 
ATOM   4518  O  OE1 . GLN B  1 323 ? -31.034  2.330   33.350  1.00 82.91  ? 322 GLN C OE1 1 
ATOM   4519  N  NE2 . GLN B  1 323 ? -31.427  0.307   32.491  1.00 77.35  ? 322 GLN C NE2 1 
ATOM   4520  N  N   . ALA C  1 2   ? -82.686  5.791   43.463  1.00 33.18  ? 1   ALA E N   1 
ATOM   4521  C  CA  . ALA C  1 2   ? -83.950  5.909   44.267  1.00 34.79  ? 1   ALA E CA  1 
ATOM   4522  C  C   . ALA C  1 2   ? -84.597  7.307   44.117  1.00 33.88  ? 1   ALA E C   1 
ATOM   4523  O  O   . ALA C  1 2   ? -83.959  8.249   43.678  1.00 39.17  ? 1   ALA E O   1 
ATOM   4524  C  CB  . ALA C  1 2   ? -83.618  5.632   45.714  1.00 37.80  ? 1   ALA E CB  1 
ATOM   4525  N  N   . THR C  1 3   ? -85.865  7.434   44.525  1.00 33.11  ? 2   THR E N   1 
ATOM   4526  C  CA  . THR C  1 3   ? -86.597  8.719   44.569  1.00 33.46  ? 2   THR E CA  1 
ATOM   4527  C  C   . THR C  1 3   ? -86.592  9.306   45.985  1.00 27.28  ? 2   THR E C   1 
ATOM   4528  O  O   . THR C  1 3   ? -86.815  10.502  46.151  1.00 25.73  ? 2   THR E O   1 
ATOM   4529  C  CB  . THR C  1 3   ? -88.047  8.564   44.110  1.00 36.66  ? 2   THR E CB  1 
ATOM   4530  O  OG1 A THR C  1 3   ? -88.698  7.676   45.023  0.60 40.64  ? 2   THR E OG1 1 
ATOM   4531  O  OG1 B THR C  1 3   ? -88.700  7.675   45.019  0.40 39.12  ? 2   THR E OG1 1 
ATOM   4532  C  CG2 A THR C  1 3   ? -88.148  8.029   42.697  0.60 38.22  ? 2   THR E CG2 1 
ATOM   4533  C  CG2 B THR C  1 3   ? -88.153  8.030   42.698  0.40 37.53  ? 2   THR E CG2 1 
ATOM   4534  N  N   . LYS C  1 4   ? -86.362  8.467   46.997  1.00 26.94  ? 3   LYS E N   1 
ATOM   4535  C  CA  . LYS C  1 4   ? -86.255  8.922   48.374  1.00 25.79  ? 3   LYS E CA  1 
ATOM   4536  C  C   . LYS C  1 4   ? -85.026  8.265   49.014  1.00 24.45  ? 3   LYS E C   1 
ATOM   4537  O  O   . LYS C  1 4   ? -84.738  7.091   48.761  1.00 22.07  ? 3   LYS E O   1 
ATOM   4538  C  CB  . LYS C  1 4   ? -87.504  8.556   49.182  1.00 33.78  ? 3   LYS E CB  1 
ATOM   4539  C  CG  . LYS C  1 4   ? -88.753  9.401   48.974  1.00 42.49  ? 3   LYS E CG  1 
ATOM   4540  C  CD  . LYS C  1 4   ? -89.766  9.244   50.110  1.00 48.97  ? 3   LYS E CD  1 
ATOM   4541  C  CE  . LYS C  1 4   ? -89.710  10.319  51.186  1.00 58.18  ? 3   LYS E CE  1 
ATOM   4542  N  NZ  . LYS C  1 4   ? -88.335  10.571  51.694  1.00 64.84  ? 3   LYS E NZ  1 
ATOM   4543  N  N   . ALA C  1 5   ? -84.324  9.010   49.879  1.00 22.22  ? 4   ALA E N   1 
ATOM   4544  C  CA  . ALA C  1 5   ? -83.181  8.483   50.613  1.00 20.63  ? 4   ALA E CA  1 
ATOM   4545  C  C   . ALA C  1 5   ? -83.197  9.093   52.008  1.00 20.73  ? 4   ALA E C   1 
ATOM   4546  O  O   . ALA C  1 5   ? -83.936  10.064  52.290  1.00 20.04  ? 4   ALA E O   1 
ATOM   4547  C  CB  . ALA C  1 5   ? -81.885  8.767   49.898  1.00 19.27  ? 4   ALA E CB  1 
ATOM   4548  N  N   . VAL C  1 6   ? -82.396  8.505   52.880  1.00 20.63  ? 5   VAL E N   1 
ATOM   4549  C  CA  . VAL C  1 6   ? -82.333  8.922   54.267  1.00 20.09  ? 5   VAL E CA  1 
ATOM   4550  C  C   . VAL C  1 6   ? -80.937  8.606   54.794  1.00 20.59  ? 5   VAL E C   1 
ATOM   4551  O  O   . VAL C  1 6   ? -80.263  7.697   54.309  1.00 20.79  ? 5   VAL E O   1 
ATOM   4552  C  CB  . VAL C  1 6   ? -83.449  8.265   55.099  1.00 21.80  ? 5   VAL E CB  1 
ATOM   4553  C  CG1 . VAL C  1 6   ? -83.246  6.765   55.265  1.00 22.75  ? 5   VAL E CG1 1 
ATOM   4554  C  CG2 . VAL C  1 6   ? -83.600  8.935   56.464  1.00 22.98  ? 5   VAL E CG2 1 
ATOM   4555  N  N   . CYS C  1 7   ? -80.503  9.407   55.773  1.00 20.12  ? 6   CYS E N   1 
ATOM   4556  C  CA  . CYS C  1 7   ? -79.234  9.265   56.385  1.00 20.38  ? 6   CYS E CA  1 
ATOM   4557  C  C   . CYS C  1 7   ? -79.381  9.515   57.889  1.00 20.53  ? 6   CYS E C   1 
ATOM   4558  O  O   . CYS C  1 7   ? -79.948  10.548  58.292  1.00 20.51  ? 6   CYS E O   1 
ATOM   4559  C  CB  . CYS C  1 7   ? -78.254  10.260  55.786  1.00 21.54  ? 6   CYS E CB  1 
ATOM   4560  S  SG  . CYS C  1 7   ? -76.604  10.096  56.487  1.00 25.02  ? 6   CYS E SG  1 
ATOM   4561  N  N   . VAL C  1 8   ? -78.896  8.568   58.698  1.00 18.74  ? 7   VAL E N   1 
ATOM   4562  C  CA  . VAL C  1 8   ? -78.831  8.727   60.161  1.00 20.21  ? 7   VAL E CA  1 
ATOM   4563  C  C   . VAL C  1 8   ? -77.401  9.122   60.505  1.00 20.19  ? 7   VAL E C   1 
ATOM   4564  O  O   . VAL C  1 8   ? -76.474  8.354   60.282  1.00 20.38  ? 7   VAL E O   1 
ATOM   4565  C  CB  . VAL C  1 8   ? -79.238  7.442   60.908  1.00 21.70  ? 7   VAL E CB  1 
ATOM   4566  C  CG1 . VAL C  1 8   ? -79.160  7.621   62.415  1.00 23.00  ? 7   VAL E CG1 1 
ATOM   4567  C  CG2 . VAL C  1 8   ? -80.623  6.970   60.507  1.00 22.64  ? 7   VAL E CG2 1 
ATOM   4568  N  N   . LEU C  1 9   ? -77.227  10.336  61.008  1.00 20.09  ? 8   LEU E N   1 
ATOM   4569  C  CA  . LEU C  1 9   ? -75.930  10.844  61.362  1.00 21.95  ? 8   LEU E CA  1 
ATOM   4570  C  C   . LEU C  1 9   ? -75.622  10.446  62.807  1.00 22.81  ? 8   LEU E C   1 
ATOM   4571  O  O   . LEU C  1 9   ? -76.438  10.714  63.683  1.00 21.28  ? 8   LEU E O   1 
ATOM   4572  C  CB  . LEU C  1 9   ? -75.959  12.368  61.223  1.00 24.96  ? 8   LEU E CB  1 
ATOM   4573  C  CG  . LEU C  1 9   ? -76.139  12.900  59.796  1.00 26.26  ? 8   LEU E CG  1 
ATOM   4574  C  CD1 . LEU C  1 9   ? -76.521  14.370  59.821  1.00 33.46  ? 8   LEU E CD1 1 
ATOM   4575  C  CD2 . LEU C  1 9   ? -74.857  12.744  59.026  1.00 27.71  ? 8   LEU E CD2 1 
ATOM   4576  N  N   . LYS C  1 10  ? -74.441  9.862   63.024  1.00 22.57  ? 9   LYS E N   1 
ATOM   4577  C  CA  . LYS C  1 10  ? -73.943  9.516   64.344  1.00 25.58  ? 9   LYS E CA  1 
ATOM   4578  C  C   . LYS C  1 10  ? -72.439  9.768   64.372  1.00 23.99  ? 9   LYS E C   1 
ATOM   4579  O  O   . LYS C  1 10  ? -71.782  9.728   63.350  1.00 20.90  ? 9   LYS E O   1 
ATOM   4580  C  CB  . LYS C  1 10  ? -74.185  8.034   64.654  1.00 29.86  ? 9   LYS E CB  1 
ATOM   4581  C  CG  . LYS C  1 10  ? -75.643  7.627   64.776  1.00 34.70  ? 9   LYS E CG  1 
ATOM   4582  C  CD  . LYS C  1 10  ? -75.791  6.117   64.898  1.00 42.18  ? 9   LYS E CD  1 
ATOM   4583  C  CE  . LYS C  1 10  ? -77.223  5.623   64.984  1.00 45.91  ? 9   LYS E CE  1 
ATOM   4584  N  NZ  . LYS C  1 10  ? -77.947  6.262   66.108  1.00 50.59  ? 9   LYS E NZ  1 
ATOM   4585  N  N   . GLY C  1 11  ? -71.896  9.943   65.574  1.00 23.36  ? 10  GLY E N   1 
ATOM   4586  C  CA  . GLY C  1 11  ? -70.459  10.043  65.735  1.00 25.14  ? 10  GLY E CA  1 
ATOM   4587  C  C   . GLY C  1 11  ? -70.025  9.617   67.126  1.00 26.33  ? 10  GLY E C   1 
ATOM   4588  O  O   . GLY C  1 11  ? -70.794  9.070   67.875  1.00 28.05  ? 10  GLY E O   1 
ATOM   4589  N  N   . ASP C  1 12  ? -68.784  9.936   67.443  1.00 32.66  ? 11  ASP E N   1 
ATOM   4590  C  CA  . ASP C  1 12  ? -68.137  9.624   68.709  1.00 39.80  ? 11  ASP E CA  1 
ATOM   4591  C  C   . ASP C  1 12  ? -68.783  10.419  69.859  1.00 41.25  ? 11  ASP E C   1 
ATOM   4592  O  O   . ASP C  1 12  ? -68.887  9.934   70.996  1.00 50.99  ? 11  ASP E O   1 
ATOM   4593  C  CB  . ASP C  1 12  ? -66.652  9.951   68.567  1.00 47.68  ? 11  ASP E CB  1 
ATOM   4594  C  CG  . ASP C  1 12  ? -65.741  9.170   69.488  1.00 58.54  ? 11  ASP E CG  1 
ATOM   4595  O  OD1 . ASP C  1 12  ? -66.275  8.448   70.364  1.00 63.06  ? 11  ASP E OD1 1 
ATOM   4596  O  OD2 . ASP C  1 12  ? -64.497  9.295   69.318  1.00 65.29  ? 11  ASP E OD2 1 
ATOM   4597  N  N   . GLY C  1 13  ? -69.244  11.628  69.546  1.00 30.98  ? 12  GLY E N   1 
ATOM   4598  C  CA  . GLY C  1 13  ? -69.775  12.572  70.480  1.00 27.56  ? 12  GLY E CA  1 
ATOM   4599  C  C   . GLY C  1 13  ? -71.284  12.697  70.411  1.00 24.53  ? 12  GLY E C   1 
ATOM   4600  O  O   . GLY C  1 13  ? -71.976  11.771  70.001  1.00 25.27  ? 12  GLY E O   1 
ATOM   4601  N  N   . PRO C  1 14  ? -71.848  13.850  70.841  1.00 22.62  ? 13  PRO E N   1 
ATOM   4602  C  CA  . PRO C  1 14  ? -73.296  13.996  70.950  1.00 24.17  ? 13  PRO E CA  1 
ATOM   4603  C  C   . PRO C  1 14  ? -74.049  14.355  69.660  1.00 23.30  ? 13  PRO E C   1 
ATOM   4604  O  O   . PRO C  1 14  ? -75.272  14.466  69.686  1.00 25.60  ? 13  PRO E O   1 
ATOM   4605  C  CB  . PRO C  1 14  ? -73.448  15.183  71.899  1.00 23.33  ? 13  PRO E CB  1 
ATOM   4606  C  CG  . PRO C  1 14  ? -72.239  16.030  71.575  1.00 23.66  ? 13  PRO E CG  1 
ATOM   4607  C  CD  . PRO C  1 14  ? -71.128  15.055  71.261  1.00 23.76  ? 13  PRO E CD  1 
ATOM   4608  N  N   . VAL C  1 15  ? -73.333  14.543  68.557  1.00 24.18  ? 14  VAL E N   1 
ATOM   4609  C  CA  . VAL C  1 15  ? -74.003  15.028  67.342  1.00 24.36  ? 14  VAL E CA  1 
ATOM   4610  C  C   . VAL C  1 15  ? -74.773  13.865  66.716  1.00 23.68  ? 14  VAL E C   1 
ATOM   4611  O  O   . VAL C  1 15  ? -74.202  12.799  66.464  1.00 22.78  ? 14  VAL E O   1 
ATOM   4612  C  CB  . VAL C  1 15  ? -73.025  15.670  66.354  1.00 24.81  ? 14  VAL E CB  1 
ATOM   4613  C  CG1 . VAL C  1 15  ? -73.765  16.157  65.101  1.00 26.39  ? 14  VAL E CG1 1 
ATOM   4614  C  CG2 . VAL C  1 15  ? -72.283  16.820  67.011  1.00 25.86  ? 14  VAL E CG2 1 
ATOM   4615  N  N   . GLN C  1 16  ? -76.076  14.073  66.529  1.00 23.03  ? 15  GLN E N   1 
ATOM   4616  C  CA  . GLN C  1 16  ? -76.954  13.072  65.984  1.00 26.84  ? 15  GLN E CA  1 
ATOM   4617  C  C   . GLN C  1 16  ? -77.978  13.775  65.106  1.00 26.43  ? 15  GLN E C   1 
ATOM   4618  O  O   . GLN C  1 16  ? -78.392  14.859  65.462  1.00 24.40  ? 15  GLN E O   1 
ATOM   4619  C  CB  . GLN C  1 16  ? -77.769  12.358  67.055  1.00 32.09  ? 15  GLN E CB  1 
ATOM   4620  C  CG  . GLN C  1 16  ? -76.937  11.636  68.093  1.00 38.57  ? 15  GLN E CG  1 
ATOM   4621  C  CD  . GLN C  1 16  ? -77.835  10.729  68.896  1.00 39.05  ? 15  GLN E CD  1 
ATOM   4622  O  OE1 . GLN C  1 16  ? -78.055  9.583   68.527  1.00 46.71  ? 15  GLN E OE1 1 
ATOM   4623  N  NE2 . GLN C  1 16  ? -78.353  11.244  69.994  1.00 35.42  ? 15  GLN E NE2 1 
ATOM   4624  N  N   . GLY C  1 17  ? -78.405  13.123  64.018  1.00 23.58  ? 16  GLY E N   1 
ATOM   4625  C  CA  . GLY C  1 17  ? -79.430  13.697  63.165  1.00 26.20  ? 16  GLY E CA  1 
ATOM   4626  C  C   . GLY C  1 17  ? -80.015  12.701  62.187  1.00 25.76  ? 16  GLY E C   1 
ATOM   4627  O  O   . GLY C  1 17  ? -79.481  11.607  61.999  1.00 24.84  ? 16  GLY E O   1 
ATOM   4628  N  N   . ILE C  1 18  ? -81.136  13.094  61.570  1.00 23.83  ? 17  ILE E N   1 
ATOM   4629  C  CA  . ILE C  1 18  ? -81.729  12.390  60.454  1.00 22.70  ? 17  ILE E CA  1 
ATOM   4630  C  C   . ILE C  1 18  ? -81.934  13.373  59.306  1.00 23.65  ? 17  ILE E C   1 
ATOM   4631  O  O   . ILE C  1 18  ? -82.597  14.418  59.486  1.00 22.32  ? 17  ILE E O   1 
ATOM   4632  C  CB  . ILE C  1 18  ? -83.058  11.747  60.866  1.00 24.38  ? 17  ILE E CB  1 
ATOM   4633  C  CG1 . ILE C  1 18  ? -82.863  10.696  61.962  1.00 26.09  ? 17  ILE E CG1 1 
ATOM   4634  C  CG2 . ILE C  1 18  ? -83.785  11.188  59.655  1.00 25.74  ? 17  ILE E CG2 1 
ATOM   4635  C  CD1 . ILE C  1 18  ? -84.156  10.245  62.589  1.00 28.25  ? 17  ILE E CD1 1 
ATOM   4636  N  N   . ILE C  1 19  ? -81.357  13.046  58.148  1.00 21.86  ? 18  ILE E N   1 
ATOM   4637  C  CA  . ILE C  1 19  ? -81.496  13.840  56.945  1.00 20.90  ? 18  ILE E CA  1 
ATOM   4638  C  C   . ILE C  1 19  ? -82.219  13.011  55.879  1.00 23.20  ? 18  ILE E C   1 
ATOM   4639  O  O   . ILE C  1 19  ? -81.851  11.855  55.606  1.00 22.97  ? 18  ILE E O   1 
ATOM   4640  C  CB  . ILE C  1 19  ? -80.139  14.364  56.465  1.00 21.07  ? 18  ILE E CB  1 
ATOM   4641  C  CG1 . ILE C  1 19  ? -79.431  15.230  57.518  1.00 23.37  ? 18  ILE E CG1 1 
ATOM   4642  C  CG2 . ILE C  1 19  ? -80.309  15.121  55.157  1.00 20.25  ? 18  ILE E CG2 1 
ATOM   4643  C  CD1 . ILE C  1 19  ? -80.161  16.535  57.859  1.00 24.43  ? 18  ILE E CD1 1 
ATOM   4644  N  N   . ASN C  1 20  ? -83.270  13.608  55.312  1.00 20.45  ? 19  ASN E N   1 
ATOM   4645  C  CA  . ASN C  1 20  ? -84.076  13.037  54.258  1.00 22.69  ? 19  ASN E CA  1 
ATOM   4646  C  C   . ASN C  1 20  ? -83.710  13.675  52.916  1.00 22.25  ? 19  ASN E C   1 
ATOM   4647  O  O   . ASN C  1 20  ? -83.308  14.852  52.844  1.00 21.60  ? 19  ASN E O   1 
ATOM   4648  C  CB  . ASN C  1 20  ? -85.563  13.275  54.526  1.00 24.27  ? 19  ASN E CB  1 
ATOM   4649  C  CG  . ASN C  1 20  ? -85.986  12.752  55.877  1.00 27.41  ? 19  ASN E CG  1 
ATOM   4650  O  OD1 . ASN C  1 20  ? -86.154  11.554  56.021  1.00 25.10  ? 19  ASN E OD1 1 
ATOM   4651  N  ND2 . ASN C  1 20  ? -86.145  13.639  56.856  1.00 25.46  ? 19  ASN E ND2 1 
ATOM   4652  N  N   . PHE C  1 21  ? -83.903  12.909  51.841  1.00 21.55  ? 20  PHE E N   1 
ATOM   4653  C  CA  . PHE C  1 21  ? -83.652  13.386  50.474  1.00 21.49  ? 20  PHE E CA  1 
ATOM   4654  C  C   . PHE C  1 21  ? -84.824  12.926  49.615  1.00 23.16  ? 20  PHE E C   1 
ATOM   4655  O  O   . PHE C  1 21  ? -85.327  11.806  49.789  1.00 20.44  ? 20  PHE E O   1 
ATOM   4656  C  CB  . PHE C  1 21  ? -82.365  12.812  49.876  1.00 21.85  ? 20  PHE E CB  1 
ATOM   4657  C  CG  . PHE C  1 21  ? -81.109  13.016  50.672  1.00 22.81  ? 20  PHE E CG  1 
ATOM   4658  C  CD1 . PHE C  1 21  ? -80.175  13.954  50.289  1.00 22.95  ? 20  PHE E CD1 1 
ATOM   4659  C  CD2 . PHE C  1 21  ? -80.837  12.238  51.789  1.00 23.93  ? 20  PHE E CD2 1 
ATOM   4660  C  CE1 . PHE C  1 21  ? -79.005  14.133  51.010  1.00 22.61  ? 20  PHE E CE1 1 
ATOM   4661  C  CE2 . PHE C  1 21  ? -79.648  12.395  52.484  1.00 22.59  ? 20  PHE E CE2 1 
ATOM   4662  C  CZ  . PHE C  1 21  ? -78.738  13.342  52.101  1.00 21.87  ? 20  PHE E CZ  1 
ATOM   4663  N  N   . GLU C  1 22  ? -85.255  13.770  48.686  1.00 22.89  ? 21  GLU E N   1 
ATOM   4664  C  CA  . GLU C  1 22  ? -86.326  13.384  47.786  1.00 24.03  ? 21  GLU E CA  1 
ATOM   4665  C  C   . GLU C  1 22  ? -86.103  14.020  46.418  1.00 23.01  ? 21  GLU E C   1 
ATOM   4666  O  O   . GLU C  1 22  ? -85.712  15.168  46.293  1.00 21.90  ? 21  GLU E O   1 
ATOM   4667  C  CB  . GLU C  1 22  ? -87.684  13.752  48.381  1.00 28.94  ? 21  GLU E CB  1 
ATOM   4668  C  CG  . GLU C  1 22  ? -88.847  13.277  47.543  1.00 36.22  ? 21  GLU E CG  1 
ATOM   4669  C  CD  . GLU C  1 22  ? -90.183  13.209  48.283  1.00 44.24  ? 21  GLU E CD  1 
ATOM   4670  O  OE1 . GLU C  1 22  ? -90.201  13.384  49.514  1.00 48.31  ? 21  GLU E OE1 1 
ATOM   4671  O  OE2 . GLU C  1 22  ? -91.200  12.962  47.621  1.00 54.65  ? 21  GLU E OE2 1 
ATOM   4672  N  N   . GLN C  1 23  ? -86.321  13.216  45.388  1.00 23.31  ? 22  GLN E N   1 
ATOM   4673  C  CA  . GLN C  1 23  ? -86.086  13.626  44.036  1.00 24.95  ? 22  GLN E CA  1 
ATOM   4674  C  C   . GLN C  1 23  ? -87.249  13.105  43.190  1.00 29.18  ? 22  GLN E C   1 
ATOM   4675  O  O   . GLN C  1 23  ? -87.407  11.901  43.064  1.00 29.15  ? 22  GLN E O   1 
ATOM   4676  C  CB  . GLN C  1 23  ? -84.749  13.079  43.552  1.00 22.59  ? 22  GLN E CB  1 
ATOM   4677  C  CG  . GLN C  1 23  ? -84.370  13.601  42.183  1.00 23.24  ? 22  GLN E CG  1 
ATOM   4678  C  CD  . GLN C  1 23  ? -83.034  13.100  41.712  1.00 22.00  ? 22  GLN E CD  1 
ATOM   4679  O  OE1 . GLN C  1 23  ? -82.602  12.020  42.094  1.00 21.69  ? 22  GLN E OE1 1 
ATOM   4680  N  NE2 . GLN C  1 23  ? -82.369  13.880  40.870  1.00 19.97  ? 22  GLN E NE2 1 
ATOM   4681  N  N   . LYS C  1 24  ? -88.032  14.029  42.644  1.00 30.72  ? 23  LYS E N   1 
ATOM   4682  C  CA  . LYS C  1 24  ? -89.295  13.719  41.969  1.00 37.64  ? 23  LYS E CA  1 
ATOM   4683  C  C   . LYS C  1 24  ? -89.027  13.164  40.563  1.00 31.60  ? 23  LYS E C   1 
ATOM   4684  O  O   . LYS C  1 24  ? -89.663  12.220  40.150  1.00 33.70  ? 23  LYS E O   1 
ATOM   4685  C  CB  . LYS C  1 24  ? -90.179  14.976  41.923  1.00 44.97  ? 23  LYS E CB  1 
ATOM   4686  C  CG  . LYS C  1 24  ? -91.223  15.128  43.033  1.00 58.09  ? 23  LYS E CG  1 
ATOM   4687  C  CD  . LYS C  1 24  ? -91.103  14.174  44.232  1.00 65.50  ? 23  LYS E CD  1 
ATOM   4688  C  CE  . LYS C  1 24  ? -91.757  12.816  44.013  1.00 71.98  ? 23  LYS E CE  1 
ATOM   4689  N  NZ  . LYS C  1 24  ? -90.999  11.705  44.652  1.00 72.73  ? 23  LYS E NZ  1 
ATOM   4690  N  N   . GLU C  1 25  ? -88.085  13.763  39.840  1.00 30.66  ? 24  GLU E N   1 
ATOM   4691  C  CA  . GLU C  1 25  ? -87.653  13.249  38.544  1.00 31.73  ? 24  GLU E CA  1 
ATOM   4692  C  C   . GLU C  1 25  ? -86.135  13.079  38.567  1.00 28.15  ? 24  GLU E C   1 
ATOM   4693  O  O   . GLU C  1 25  ? -85.422  13.864  39.209  1.00 24.48  ? 24  GLU E O   1 
ATOM   4694  C  CB  . GLU C  1 25  ? -88.097  14.127  37.365  1.00 37.47  ? 24  GLU E CB  1 
ATOM   4695  C  CG  . GLU C  1 25  ? -88.697  15.471  37.737  1.00 47.95  ? 24  GLU E CG  1 
ATOM   4696  C  CD  . GLU C  1 25  ? -90.173  15.435  38.085  1.00 52.57  ? 24  GLU E CD  1 
ATOM   4697  O  OE1 . GLU C  1 25  ? -90.861  14.449  37.721  1.00 66.95  ? 24  GLU E OE1 1 
ATOM   4698  O  OE2 . GLU C  1 25  ? -90.627  16.391  38.717  1.00 69.92  ? 24  GLU E OE2 1 
ATOM   4699  N  N   . SER C  1 26  ? -85.658  12.087  37.806  1.00 24.29  ? 25  SER E N   1 
ATOM   4700  C  CA  . SER C  1 26  ? -84.254  11.720  37.752  1.00 23.99  ? 25  SER E CA  1 
ATOM   4701  C  C   . SER C  1 26  ? -83.384  12.878  37.238  1.00 22.94  ? 25  SER E C   1 
ATOM   4702  O  O   . SER C  1 26  ? -82.177  12.912  37.506  1.00 23.00  ? 25  SER E O   1 
ATOM   4703  C  CB  . SER C  1 26  ? -84.064  10.479  36.912  1.00 26.52  ? 25  SER E CB  1 
ATOM   4704  O  OG  . SER C  1 26  ? -84.442  10.735  35.562  1.00 29.04  ? 25  SER E OG  1 
ATOM   4705  N  N   . ASN C  1 27  ? -83.961  13.824  36.480  1.00 23.05  ? 26  ASN E N   1 
ATOM   4706  C  CA  . ASN C  1 27  ? -83.191  14.990  35.974  1.00 24.56  ? 26  ASN E CA  1 
ATOM   4707  C  C   . ASN C  1 27  ? -83.636  16.263  36.701  1.00 27.18  ? 26  ASN E C   1 
ATOM   4708  O  O   . ASN C  1 27  ? -83.400  17.383  36.244  1.00 32.52  ? 26  ASN E O   1 
ATOM   4709  C  CB  . ASN C  1 27  ? -83.277  15.146  34.445  1.00 25.30  ? 26  ASN E CB  1 
ATOM   4710  C  CG  . ASN C  1 27  ? -84.670  15.470  33.950  1.00 25.79  ? 26  ASN E CG  1 
ATOM   4711  O  OD1 . ASN C  1 27  ? -85.653  15.026  34.546  1.00 24.76  ? 26  ASN E OD1 1 
ATOM   4712  N  ND2 . ASN C  1 27  ? -84.746  16.231  32.862  1.00 24.53  ? 26  ASN E ND2 1 
ATOM   4713  N  N   . GLY C  1 28  ? -84.285  16.075  37.842  1.00 25.76  ? 27  GLY E N   1 
ATOM   4714  C  CA  . GLY C  1 28  ? -84.744  17.166  38.671  1.00 27.38  ? 27  GLY E CA  1 
ATOM   4715  C  C   . GLY C  1 28  ? -83.859  17.354  39.899  1.00 26.50  ? 27  GLY E C   1 
ATOM   4716  O  O   . GLY C  1 28  ? -82.968  16.555  40.188  1.00 24.31  ? 27  GLY E O   1 
ATOM   4717  N  N   . PRO C  1 29  ? -84.082  18.450  40.643  1.00 29.49  ? 28  PRO E N   1 
ATOM   4718  C  CA  . PRO C  1 29  ? -83.324  18.711  41.860  1.00 28.03  ? 28  PRO E CA  1 
ATOM   4719  C  C   . PRO C  1 29  ? -83.710  17.734  42.981  1.00 23.68  ? 28  PRO E C   1 
ATOM   4720  O  O   . PRO C  1 29  ? -84.774  17.090  42.934  1.00 21.04  ? 28  PRO E O   1 
ATOM   4721  C  CB  . PRO C  1 29  ? -83.730  20.131  42.275  1.00 29.92  ? 28  PRO E CB  1 
ATOM   4722  C  CG  . PRO C  1 29  ? -85.061  20.375  41.576  1.00 32.25  ? 28  PRO E CG  1 
ATOM   4723  C  CD  . PRO C  1 29  ? -85.076  19.492  40.343  1.00 30.45  ? 28  PRO E CD  1 
ATOM   4724  N  N   . VAL C  1 30  ? -82.842  17.685  43.991  1.00 24.11  ? 29  VAL E N   1 
ATOM   4725  C  CA  . VAL C  1 30  ? -83.037  16.916  45.201  1.00 21.65  ? 29  VAL E CA  1 
ATOM   4726  C  C   . VAL C  1 30  ? -83.352  17.874  46.352  1.00 22.72  ? 29  VAL E C   1 
ATOM   4727  O  O   . VAL C  1 30  ? -82.630  18.836  46.576  1.00 23.58  ? 29  VAL E O   1 
ATOM   4728  C  CB  . VAL C  1 30  ? -81.771  16.107  45.504  1.00 22.41  ? 29  VAL E CB  1 
ATOM   4729  C  CG1 . VAL C  1 30  ? -81.923  15.251  46.762  1.00 21.92  ? 29  VAL E CG1 1 
ATOM   4730  C  CG2 . VAL C  1 30  ? -81.372  15.262  44.306  1.00 23.40  ? 29  VAL E CG2 1 
ATOM   4731  N  N   . LYS C  1 31  ? -84.456  17.600  47.039  1.00 22.42  ? 30  LYS E N   1 
ATOM   4732  C  CA  . LYS C  1 31  ? -84.818  18.245  48.284  1.00 25.42  ? 30  LYS E CA  1 
ATOM   4733  C  C   . LYS C  1 31  ? -84.145  17.489  49.436  1.00 23.32  ? 30  LYS E C   1 
ATOM   4734  O  O   . LYS C  1 31  ? -84.181  16.258  49.483  1.00 21.56  ? 30  LYS E O   1 
ATOM   4735  C  CB  . LYS C  1 31  ? -86.343  18.279  48.426  1.00 28.69  ? 30  LYS E CB  1 
ATOM   4736  C  CG  . LYS C  1 31  ? -86.840  19.135  49.582  1.00 38.99  ? 30  LYS E CG  1 
ATOM   4737  C  CD  . LYS C  1 31  ? -88.344  19.169  49.741  1.00 46.63  ? 30  LYS E CD  1 
ATOM   4738  C  CE  . LYS C  1 31  ? -88.812  20.288  50.656  1.00 52.70  ? 30  LYS E CE  1 
ATOM   4739  N  NZ  . LYS C  1 31  ? -90.284  20.249  50.842  1.00 57.57  ? 30  LYS E NZ  1 
ATOM   4740  N  N   . VAL C  1 32  ? -83.433  18.229  50.292  1.00 23.37  ? 31  VAL E N   1 
ATOM   4741  C  CA  . VAL C  1 32  ? -82.724  17.720  51.450  1.00 23.07  ? 31  VAL E CA  1 
ATOM   4742  C  C   . VAL C  1 32  ? -83.310  18.386  52.698  1.00 25.91  ? 31  VAL E C   1 
ATOM   4743  O  O   . VAL C  1 32  ? -83.277  19.606  52.796  1.00 26.65  ? 31  VAL E O   1 
ATOM   4744  C  CB  . VAL C  1 32  ? -81.220  18.034  51.330  1.00 24.13  ? 31  VAL E CB  1 
ATOM   4745  C  CG1 . VAL C  1 32  ? -80.413  17.384  52.449  1.00 23.80  ? 31  VAL E CG1 1 
ATOM   4746  C  CG2 . VAL C  1 32  ? -80.663  17.656  49.960  1.00 24.22  ? 31  VAL E CG2 1 
ATOM   4747  N  N   . TRP C  1 33  ? -83.809  17.608  53.664  1.00 25.16  ? 32  TRP E N   1 
ATOM   4748  C  CA  . TRP C  1 33  ? -84.346  18.227  54.879  1.00 23.78  ? 32  TRP E CA  1 
ATOM   4749  C  C   . TRP C  1 33  ? -84.260  17.287  56.072  1.00 23.95  ? 32  TRP E C   1 
ATOM   4750  O  O   . TRP C  1 33  ? -84.308  16.048  55.942  1.00 21.47  ? 32  TRP E O   1 
ATOM   4751  C  CB  . TRP C  1 33  ? -85.800  18.667  54.686  1.00 25.21  ? 32  TRP E CB  1 
ATOM   4752  C  CG  . TRP C  1 33  ? -86.806  17.564  54.757  1.00 24.81  ? 32  TRP E CG  1 
ATOM   4753  C  CD1 . TRP C  1 33  ? -87.623  17.244  55.804  1.00 27.15  ? 32  TRP E CD1 1 
ATOM   4754  C  CD2 . TRP C  1 33  ? -87.106  16.633  53.712  1.00 26.04  ? 32  TRP E CD2 1 
ATOM   4755  N  NE1 . TRP C  1 33  ? -88.394  16.161  55.482  1.00 29.34  ? 32  TRP E NE1 1 
ATOM   4756  C  CE2 . TRP C  1 33  ? -88.107  15.774  54.199  1.00 28.54  ? 32  TRP E CE2 1 
ATOM   4757  C  CE3 . TRP C  1 33  ? -86.623  16.449  52.415  1.00 27.71  ? 32  TRP E CE3 1 
ATOM   4758  C  CZ2 . TRP C  1 33  ? -88.630  14.742  53.428  1.00 30.34  ? 32  TRP E CZ2 1 
ATOM   4759  C  CZ3 . TRP C  1 33  ? -87.142  15.430  51.651  1.00 29.56  ? 32  TRP E CZ3 1 
ATOM   4760  C  CH2 . TRP C  1 33  ? -88.129  14.585  52.156  1.00 30.12  ? 32  TRP E CH2 1 
ATOM   4761  N  N   . GLY C  1 34  ? -84.240  17.902  57.247  1.00 22.36  ? 33  GLY E N   1 
ATOM   4762  C  CA  . GLY C  1 34  ? -84.237  17.155  58.486  1.00 25.19  ? 33  GLY E CA  1 
ATOM   4763  C  C   . GLY C  1 34  ? -83.647  17.985  59.598  1.00 25.48  ? 33  GLY E C   1 
ATOM   4764  O  O   . GLY C  1 34  ? -83.686  19.203  59.558  1.00 26.41  ? 33  GLY E O   1 
ATOM   4765  N  N   . SER C  1 35  ? -83.042  17.315  60.559  1.00 25.86  ? 34  SER E N   1 
ATOM   4766  C  CA  . SER C  1 35  ? -82.652  17.966  61.776  1.00 29.48  ? 34  SER E CA  1 
ATOM   4767  C  C   . SER C  1 35  ? -81.401  17.288  62.331  1.00 28.09  ? 34  SER E C   1 
ATOM   4768  O  O   . SER C  1 35  ? -81.261  16.056  62.226  1.00 24.28  ? 34  SER E O   1 
ATOM   4769  C  CB  . SER C  1 35  ? -83.812  17.945  62.748  1.00 30.86  ? 34  SER E CB  1 
ATOM   4770  O  OG  . SER C  1 35  ? -83.388  18.452  63.988  1.00 46.08  ? 34  SER E OG  1 
ATOM   4771  N  N   . ILE C  1 36  ? -80.486  18.105  62.864  1.00 25.66  ? 35  ILE E N   1 
ATOM   4772  C  CA  . ILE C  1 36  ? -79.279  17.642  63.530  1.00 24.80  ? 35  ILE E CA  1 
ATOM   4773  C  C   . ILE C  1 36  ? -79.208  18.333  64.896  1.00 29.49  ? 35  ILE E C   1 
ATOM   4774  O  O   . ILE C  1 36  ? -79.446  19.552  64.985  1.00 29.92  ? 35  ILE E O   1 
ATOM   4775  C  CB  . ILE C  1 36  ? -78.024  17.955  62.713  1.00 25.59  ? 35  ILE E CB  1 
ATOM   4776  C  CG1 . ILE C  1 36  ? -78.156  17.544  61.245  1.00 26.82  ? 35  ILE E CG1 1 
ATOM   4777  C  CG2 . ILE C  1 36  ? -76.809  17.332  63.368  1.00 25.48  ? 35  ILE E CG2 1 
ATOM   4778  C  CD1 . ILE C  1 36  ? -76.998  17.976  60.407  1.00 27.26  ? 35  ILE E CD1 1 
ATOM   4779  N  N   . LYS C  1 37  ? -78.892  17.568  65.943  1.00 27.24  ? 36  LYS E N   1 
ATOM   4780  C  CA  . LYS C  1 37  ? -78.779  18.116  67.304  1.00 28.93  ? 36  LYS E CA  1 
ATOM   4781  C  C   . LYS C  1 37  ? -77.392  17.814  67.864  1.00 28.22  ? 36  LYS E C   1 
ATOM   4782  O  O   . LYS C  1 37  ? -76.620  17.034  67.284  1.00 24.26  ? 36  LYS E O   1 
ATOM   4783  C  CB  . LYS C  1 37  ? -79.909  17.598  68.194  1.00 32.90  ? 36  LYS E CB  1 
ATOM   4784  C  CG  . LYS C  1 37  ? -79.910  16.104  68.472  1.00 41.22  ? 36  LYS E CG  1 
ATOM   4785  C  CD  . LYS C  1 37  ? -81.231  15.644  69.074  1.00 47.90  ? 36  LYS E CD  1 
ATOM   4786  C  CE  . LYS C  1 37  ? -81.352  14.139  69.199  1.00 54.37  ? 36  LYS E CE  1 
ATOM   4787  N  NZ  . LYS C  1 37  ? -80.333  13.592  70.123  1.00 61.71  ? 36  LYS E NZ  1 
ATOM   4788  N  N   . GLY C  1 38  ? -77.061  18.479  68.975  1.00 24.25  ? 37  GLY E N   1 
ATOM   4789  C  CA  . GLY C  1 38  ? -75.800  18.253  69.645  1.00 23.00  ? 37  GLY E CA  1 
ATOM   4790  C  C   . GLY C  1 38  ? -74.672  19.097  69.112  1.00 23.83  ? 37  GLY E C   1 
ATOM   4791  O  O   . GLY C  1 38  ? -73.528  18.878  69.484  1.00 23.16  ? 37  GLY E O   1 
ATOM   4792  N  N   . LEU C  1 39  ? -74.994  20.068  68.246  1.00 24.32  ? 38  LEU E N   1 
ATOM   4793  C  CA  . LEU C  1 39  ? -74.006  20.926  67.591  1.00 24.77  ? 38  LEU E CA  1 
ATOM   4794  C  C   . LEU C  1 39  ? -73.735  22.170  68.452  1.00 28.49  ? 38  LEU E C   1 
ATOM   4795  O  O   . LEU C  1 39  ? -74.625  22.662  69.125  1.00 31.11  ? 38  LEU E O   1 
ATOM   4796  C  CB  . LEU C  1 39  ? -74.563  21.356  66.232  1.00 26.16  ? 38  LEU E CB  1 
ATOM   4797  C  CG  . LEU C  1 39  ? -74.668  20.245  65.180  1.00 25.43  ? 38  LEU E CG  1 
ATOM   4798  C  CD1 . LEU C  1 39  ? -75.583  20.655  64.035  1.00 27.27  ? 38  LEU E CD1 1 
ATOM   4799  C  CD2 . LEU C  1 39  ? -73.292  19.900  64.660  1.00 25.22  ? 38  LEU E CD2 1 
ATOM   4800  N  N   . THR C  1 40  ? -72.523  22.707  68.352  1.00 30.37  ? 39  THR E N   1 
ATOM   4801  C  CA  . THR C  1 40  ? -72.233  24.012  68.907  1.00 33.53  ? 39  THR E CA  1 
ATOM   4802  C  C   . THR C  1 40  ? -72.996  25.051  68.081  1.00 34.77  ? 39  THR E C   1 
ATOM   4803  O  O   . THR C  1 40  ? -73.148  24.898  66.860  1.00 31.38  ? 39  THR E O   1 
ATOM   4804  C  CB  . THR C  1 40  ? -70.730  24.309  68.885  1.00 34.00  ? 39  THR E CB  1 
ATOM   4805  O  OG1 . THR C  1 40  ? -70.306  24.279  67.524  1.00 35.36  ? 39  THR E OG1 1 
ATOM   4806  C  CG2 . THR C  1 40  ? -69.908  23.332  69.697  1.00 33.62  ? 39  THR E CG2 1 
ATOM   4807  N  N   . GLU C  1 41  ? -73.511  26.086  68.752  1.00 31.62  ? 40  GLU E N   1 
ATOM   4808  C  CA  . GLU C  1 41  ? -74.242  27.145  68.087  1.00 32.03  ? 40  GLU E CA  1 
ATOM   4809  C  C   . GLU C  1 41  ? -73.389  27.700  66.947  1.00 29.37  ? 40  GLU E C   1 
ATOM   4810  O  O   . GLU C  1 41  ? -72.196  27.934  67.105  1.00 32.26  ? 40  GLU E O   1 
ATOM   4811  C  CB  . GLU C  1 41  ? -74.577  28.263  69.074  1.00 35.11  ? 40  GLU E CB  1 
ATOM   4812  C  CG  . GLU C  1 41  ? -75.417  29.383  68.481  1.00 37.97  ? 40  GLU E CG  1 
ATOM   4813  C  CD  . GLU C  1 41  ? -75.714  30.475  69.501  1.00 42.81  ? 40  GLU E CD  1 
ATOM   4814  O  OE1 . GLU C  1 41  ? -76.554  31.342  69.218  1.00 43.85  ? 40  GLU E OE1 1 
ATOM   4815  O  OE2 . GLU C  1 41  ? -75.104  30.436  70.592  1.00 48.36  ? 40  GLU E OE2 1 
ATOM   4816  N  N   . GLY C  1 42  ? -74.021  27.925  65.795  1.00 30.92  ? 41  GLY E N   1 
ATOM   4817  C  CA  . GLY C  1 42  ? -73.341  28.540  64.662  1.00 30.21  ? 41  GLY E CA  1 
ATOM   4818  C  C   . GLY C  1 42  ? -73.287  27.618  63.452  1.00 28.35  ? 41  GLY E C   1 
ATOM   4819  O  O   . GLY C  1 42  ? -74.084  26.675  63.355  1.00 26.97  ? 41  GLY E O   1 
ATOM   4820  N  N   . LEU C  1 43  ? -72.320  27.872  62.557  1.00 27.12  ? 42  LEU E N   1 
ATOM   4821  C  CA  . LEU C  1 43  ? -72.277  27.233  61.225  1.00 29.93  ? 42  LEU E CA  1 
ATOM   4822  C  C   . LEU C  1 43  ? -71.454  25.938  61.253  1.00 29.35  ? 42  LEU E C   1 
ATOM   4823  O  O   . LEU C  1 43  ? -70.375  25.841  61.865  1.00 26.92  ? 42  LEU E O   1 
ATOM   4824  C  CB  . LEU C  1 43  ? -71.665  28.179  60.195  1.00 30.31  ? 42  LEU E CB  1 
ATOM   4825  C  CG  . LEU C  1 43  ? -72.391  29.507  59.959  1.00 34.92  ? 42  LEU E CG  1 
ATOM   4826  C  CD1 . LEU C  1 43  ? -71.805  30.203  58.752  1.00 34.62  ? 42  LEU E CD1 1 
ATOM   4827  C  CD2 . LEU C  1 43  ? -73.890  29.323  59.767  1.00 38.09  ? 42  LEU E CD2 1 
ATOM   4828  N  N   . HIS C  1 44  ? -71.898  24.971  60.452  1.00 26.18  ? 43  HIS E N   1 
ATOM   4829  C  CA  . HIS C  1 44  ? -71.213  23.682  60.363  1.00 24.66  ? 43  HIS E CA  1 
ATOM   4830  C  C   . HIS C  1 44  ? -71.228  23.232  58.908  1.00 24.64  ? 43  HIS E C   1 
ATOM   4831  O  O   . HIS C  1 44  ? -72.313  23.209  58.314  1.00 23.58  ? 43  HIS E O   1 
ATOM   4832  C  CB  . HIS C  1 44  ? -71.915  22.675  61.274  1.00 24.54  ? 43  HIS E CB  1 
ATOM   4833  C  CG  . HIS C  1 44  ? -71.810  22.997  62.726  1.00 25.52  ? 43  HIS E CG  1 
ATOM   4834  N  ND1 . HIS C  1 44  ? -70.702  22.648  63.459  1.00 26.49  ? 43  HIS E ND1 1 
ATOM   4835  C  CD2 . HIS C  1 44  ? -72.653  23.627  63.573  1.00 25.32  ? 43  HIS E CD2 1 
ATOM   4836  C  CE1 . HIS C  1 44  ? -70.852  23.082  64.698  1.00 27.79  ? 43  HIS E CE1 1 
ATOM   4837  N  NE2 . HIS C  1 44  ? -72.049  23.668  64.799  1.00 25.09  ? 43  HIS E NE2 1 
ATOM   4838  N  N   . GLY C  1 45  ? -70.047  22.911  58.370  1.00 22.32  ? 44  GLY E N   1 
ATOM   4839  C  CA  . GLY C  1 45  ? -69.906  22.344  57.067  1.00 26.02  ? 44  GLY E CA  1 
ATOM   4840  C  C   . GLY C  1 45  ? -70.727  21.068  56.942  1.00 25.14  ? 44  GLY E C   1 
ATOM   4841  O  O   . GLY C  1 45  ? -70.882  20.307  57.923  1.00 21.71  ? 44  GLY E O   1 
ATOM   4842  N  N   . PHE C  1 46  ? -71.285  20.864  55.749  1.00 23.87  ? 45  PHE E N   1 
ATOM   4843  C  CA  . PHE C  1 46  ? -72.241  19.824  55.480  1.00 22.60  ? 45  PHE E CA  1 
ATOM   4844  C  C   . PHE C  1 46  ? -71.990  19.305  54.063  1.00 23.19  ? 45  PHE E C   1 
ATOM   4845  O  O   . PHE C  1 46  ? -72.216  20.037  53.095  1.00 23.82  ? 45  PHE E O   1 
ATOM   4846  C  CB  . PHE C  1 46  ? -73.629  20.419  55.654  1.00 23.35  ? 45  PHE E CB  1 
ATOM   4847  C  CG  . PHE C  1 46  ? -74.792  19.472  55.620  1.00 23.92  ? 45  PHE E CG  1 
ATOM   4848  C  CD1 . PHE C  1 46  ? -74.943  18.498  56.590  1.00 25.28  ? 45  PHE E CD1 1 
ATOM   4849  C  CD2 . PHE C  1 46  ? -75.778  19.609  54.655  1.00 25.87  ? 45  PHE E CD2 1 
ATOM   4850  C  CE1 . PHE C  1 46  ? -76.049  17.664  56.583  1.00 25.83  ? 45  PHE E CE1 1 
ATOM   4851  C  CE2 . PHE C  1 46  ? -76.897  18.793  54.670  1.00 27.06  ? 45  PHE E CE2 1 
ATOM   4852  C  CZ  . PHE C  1 46  ? -77.024  17.813  55.627  1.00 27.79  ? 45  PHE E CZ  1 
ATOM   4853  N  N   . HIS C  1 47  ? -71.413  18.106  53.954  1.00 21.51  ? 46  HIS E N   1 
ATOM   4854  C  CA  . HIS C  1 47  ? -70.953  17.622  52.662  1.00 23.69  ? 46  HIS E CA  1 
ATOM   4855  C  C   . HIS C  1 47  ? -71.265  16.144  52.462  1.00 23.23  ? 46  HIS E C   1 
ATOM   4856  O  O   . HIS C  1 47  ? -71.340  15.364  53.437  1.00 22.33  ? 46  HIS E O   1 
ATOM   4857  C  CB  . HIS C  1 47  ? -69.440  17.763  52.492  1.00 26.99  ? 46  HIS E CB  1 
ATOM   4858  C  CG  . HIS C  1 47  ? -68.840  19.025  53.002  1.00 28.51  ? 46  HIS E CG  1 
ATOM   4859  N  ND1 . HIS C  1 47  ? -67.752  19.024  53.866  1.00 30.09  ? 46  HIS E ND1 1 
ATOM   4860  C  CD2 . HIS C  1 47  ? -69.125  20.322  52.728  1.00 32.19  ? 46  HIS E CD2 1 
ATOM   4861  C  CE1 . HIS C  1 47  ? -67.418  20.275  54.133  1.00 32.60  ? 46  HIS E CE1 1 
ATOM   4862  N  NE2 . HIS C  1 47  ? -68.253  21.094  53.440  1.00 29.27  ? 46  HIS E NE2 1 
ATOM   4863  N  N   . VAL C  1 48  ? -71.344  15.756  51.184  1.00 22.96  ? 47  VAL E N   1 
ATOM   4864  C  CA  . VAL C  1 48  ? -71.316  14.360  50.821  1.00 22.73  ? 47  VAL E CA  1 
ATOM   4865  C  C   . VAL C  1 48  ? -69.867  13.991  50.522  1.00 22.62  ? 47  VAL E C   1 
ATOM   4866  O  O   . VAL C  1 48  ? -69.188  14.628  49.702  1.00 25.31  ? 47  VAL E O   1 
ATOM   4867  C  CB  . VAL C  1 48  ? -72.239  14.029  49.638  1.00 21.90  ? 47  VAL E CB  1 
ATOM   4868  C  CG1 . VAL C  1 48  ? -72.174  12.539  49.312  1.00 21.70  ? 47  VAL E CG1 1 
ATOM   4869  C  CG2 . VAL C  1 48  ? -73.663  14.475  49.920  1.00 24.41  ? 47  VAL E CG2 1 
ATOM   4870  N  N   . HIS C  1 49  ? -69.401  12.968  51.220  1.00 21.73  ? 48  HIS E N   1 
ATOM   4871  C  CA  . HIS C  1 49  ? -68.077  12.387  51.049  1.00 22.53  ? 48  HIS E CA  1 
ATOM   4872  C  C   . HIS C  1 49  ? -68.201  11.129  50.183  1.00 22.65  ? 48  HIS E C   1 
ATOM   4873  O  O   . HIS C  1 49  ? -69.277  10.525  50.065  1.00 22.30  ? 48  HIS E O   1 
ATOM   4874  C  CB  . HIS C  1 49  ? -67.460  12.139  52.434  1.00 23.98  ? 48  HIS E CB  1 
ATOM   4875  C  CG  . HIS C  1 49  ? -66.968  13.392  53.086  1.00 24.24  ? 48  HIS E CG  1 
ATOM   4876  N  ND1 . HIS C  1 49  ? -65.637  13.588  53.351  1.00 25.00  ? 48  HIS E ND1 1 
ATOM   4877  C  CD2 . HIS C  1 49  ? -67.600  14.528  53.481  1.00 24.26  ? 48  HIS E CD2 1 
ATOM   4878  C  CE1 . HIS C  1 49  ? -65.465  14.775  53.905  1.00 25.67  ? 48  HIS E CE1 1 
ATOM   4879  N  NE2 . HIS C  1 49  ? -66.647  15.377  54.004  1.00 24.99  ? 48  HIS E NE2 1 
ATOM   4880  N  N   . GLU C  1 50  ? -67.088  10.746  49.574  1.00 24.85  ? 49  GLU E N   1 
ATOM   4881  C  CA  . GLU C  1 50  ? -67.063  9.825   48.450  1.00 25.52  ? 49  GLU E CA  1 
ATOM   4882  C  C   . GLU C  1 50  ? -67.490  8.407   48.845  1.00 23.76  ? 49  GLU E C   1 
ATOM   4883  O  O   . GLU C  1 50  ? -68.212  7.763   48.104  1.00 23.76  ? 49  GLU E O   1 
ATOM   4884  C  CB  . GLU C  1 50  ? -65.657  9.771   47.862  1.00 26.91  ? 49  GLU E CB  1 
ATOM   4885  C  CG  . GLU C  1 50  ? -65.616  8.965   46.591  1.00 30.18  ? 49  GLU E CG  1 
ATOM   4886  C  CD  . GLU C  1 50  ? -64.274  8.925   45.884  1.00 34.23  ? 49  GLU E CD  1 
ATOM   4887  O  OE1 . GLU C  1 50  ? -64.187  8.190   44.901  1.00 37.65  ? 49  GLU E OE1 1 
ATOM   4888  O  OE2 . GLU C  1 50  ? -63.335  9.629   46.316  1.00 38.70  ? 49  GLU E OE2 1 
ATOM   4889  N  N   . PHE C  1 51  ? -67.020  7.910   49.991  1.00 23.30  ? 50  PHE E N   1 
ATOM   4890  C  CA  . PHE C  1 51  ? -67.247  6.504   50.346  1.00 24.77  ? 50  PHE E CA  1 
ATOM   4891  C  C   . PHE C  1 51  ? -68.263  6.384   51.487  1.00 23.65  ? 50  PHE E C   1 
ATOM   4892  O  O   . PHE C  1 51  ? -68.200  7.131   52.460  1.00 25.33  ? 50  PHE E O   1 
ATOM   4893  C  CB  . PHE C  1 51  ? -65.920  5.842   50.723  1.00 25.41  ? 50  PHE E CB  1 
ATOM   4894  C  CG  . PHE C  1 51  ? -64.849  6.021   49.682  1.00 26.38  ? 50  PHE E CG  1 
ATOM   4895  C  CD1 . PHE C  1 51  ? -64.997  5.478   48.413  1.00 28.12  ? 50  PHE E CD1 1 
ATOM   4896  C  CD2 . PHE C  1 51  ? -63.692  6.727   49.970  1.00 30.03  ? 50  PHE E CD2 1 
ATOM   4897  C  CE1 . PHE C  1 51  ? -64.024  5.666   47.443  1.00 29.20  ? 50  PHE E CE1 1 
ATOM   4898  C  CE2 . PHE C  1 51  ? -62.718  6.907   49.001  1.00 30.13  ? 50  PHE E CE2 1 
ATOM   4899  C  CZ  . PHE C  1 51  ? -62.881  6.371   47.746  1.00 28.92  ? 50  PHE E CZ  1 
ATOM   4900  N  N   . GLY C  1 52  ? -69.146  5.389   51.375  1.00 21.21  ? 51  GLY E N   1 
ATOM   4901  C  CA  . GLY C  1 52  ? -70.059  5.001   52.411  1.00 22.13  ? 51  GLY E CA  1 
ATOM   4902  C  C   . GLY C  1 52  ? -69.425  3.996   53.353  1.00 21.94  ? 51  GLY E C   1 
ATOM   4903  O  O   . GLY C  1 52  ? -69.995  2.947   53.636  1.00 23.21  ? 51  GLY E O   1 
ATOM   4904  N  N   . ASP C  1 53  ? -68.216  4.317   53.808  1.00 24.54  ? 52  ASP E N   1 
ATOM   4905  C  CA  . ASP C  1 53  ? -67.351  3.416   54.553  1.00 22.40  ? 52  ASP E CA  1 
ATOM   4906  C  C   . ASP C  1 53  ? -67.172  4.026   55.934  1.00 23.13  ? 52  ASP E C   1 
ATOM   4907  O  O   . ASP C  1 53  ? -66.524  5.072   56.056  1.00 24.21  ? 52  ASP E O   1 
ATOM   4908  C  CB  . ASP C  1 53  ? -66.004  3.274   53.864  1.00 23.31  ? 52  ASP E CB  1 
ATOM   4909  C  CG  . ASP C  1 53  ? -65.020  2.325   54.547  1.00 25.51  ? 52  ASP E CG  1 
ATOM   4910  O  OD1 . ASP C  1 53  ? -64.144  1.829   53.838  1.00 29.14  ? 52  ASP E OD1 1 
ATOM   4911  O  OD2 . ASP C  1 53  ? -65.138  2.088   55.763  1.00 26.74  ? 52  ASP E OD2 1 
ATOM   4912  N  N   . ASN C  1 54  ? -67.784  3.411   56.939  1.00 23.51  ? 53  ASN E N   1 
ATOM   4913  C  CA  . ASN C  1 54  ? -67.732  3.933   58.298  1.00 26.73  ? 53  ASN E CA  1 
ATOM   4914  C  C   . ASN C  1 54  ? -66.955  2.958   59.200  1.00 25.12  ? 53  ASN E C   1 
ATOM   4915  O  O   . ASN C  1 54  ? -67.086  2.966   60.409  1.00 25.08  ? 53  ASN E O   1 
ATOM   4916  C  CB  . ASN C  1 54  ? -69.135  4.340   58.751  1.00 31.14  ? 53  ASN E CB  1 
ATOM   4917  C  CG  A ASN C  1 54  ? -69.668  5.582   58.051  0.60 34.98  ? 53  ASN E CG  1 
ATOM   4918  C  CG  B ASN C  1 54  ? -69.576  5.628   58.077  0.40 38.54  ? 53  ASN E CG  1 
ATOM   4919  O  OD1 A ASN C  1 54  ? -69.000  6.191   57.190  0.60 31.79  ? 53  ASN E OD1 1 
ATOM   4920  O  OD1 B ASN C  1 54  ? -70.675  5.723   57.519  0.40 44.07  ? 53  ASN E OD1 1 
ATOM   4921  N  ND2 A ASN C  1 54  ? -70.908  5.943   58.375  0.60 32.64  ? 53  ASN E ND2 1 
ATOM   4922  N  ND2 B ASN C  1 54  ? -68.700  6.631   58.087  0.40 43.17  ? 53  ASN E ND2 1 
ATOM   4923  N  N   . THR C  1 55  ? -66.041  2.188   58.607  1.00 25.52  ? 54  THR E N   1 
ATOM   4924  C  CA  . THR C  1 55  ? -65.306  1.159   59.355  1.00 27.31  ? 54  THR E CA  1 
ATOM   4925  C  C   . THR C  1 55  ? -64.354  1.788   60.374  1.00 31.42  ? 54  THR E C   1 
ATOM   4926  O  O   . THR C  1 55  ? -64.108  1.183   61.396  1.00 33.01  ? 54  THR E O   1 
ATOM   4927  C  CB  . THR C  1 55  ? -64.509  0.229   58.438  1.00 27.64  ? 54  THR E CB  1 
ATOM   4928  O  OG1 . THR C  1 55  ? -63.649  1.006   57.611  1.00 28.66  ? 54  THR E OG1 1 
ATOM   4929  C  CG2 . THR C  1 55  ? -65.422  -0.636  57.602  1.00 27.57  ? 54  THR E CG2 1 
ATOM   4930  N  N   . ALA C  1 56  ? -63.835  2.996   60.109  1.00 30.52  ? 55  ALA E N   1 
ATOM   4931  C  CA  . ALA C  1 56  ? -63.058  3.733   61.112  1.00 34.07  ? 55  ALA E CA  1 
ATOM   4932  C  C   . ALA C  1 56  ? -63.797  5.021   61.481  1.00 34.66  ? 55  ALA E C   1 
ATOM   4933  O  O   . ALA C  1 56  ? -63.178  6.062   61.579  1.00 39.92  ? 55  ALA E O   1 
ATOM   4934  C  CB  . ALA C  1 56  ? -61.674  4.042   60.573  1.00 34.34  ? 55  ALA E CB  1 
ATOM   4935  N  N   . GLY C  1 57  ? -65.124  4.957   61.620  1.00 31.48  ? 56  GLY E N   1 
ATOM   4936  C  CA  . GLY C  1 57  ? -65.908  6.158   61.831  1.00 30.71  ? 56  GLY E CA  1 
ATOM   4937  C  C   . GLY C  1 57  ? -65.885  7.048   60.597  1.00 30.82  ? 56  GLY E C   1 
ATOM   4938  O  O   . GLY C  1 57  ? -65.770  6.560   59.455  1.00 28.08  ? 56  GLY E O   1 
ATOM   4939  N  N   . CYS C  1 58  ? -65.997  8.363   60.813  1.00 28.48  ? 57  CYS E N   1 
ATOM   4940  C  CA  . CYS C  1 58  ? -66.209  9.281   59.707  1.00 28.26  ? 57  CYS E CA  1 
ATOM   4941  C  C   . CYS C  1 58  ? -64.937  9.443   58.875  1.00 28.11  ? 57  CYS E C   1 
ATOM   4942  O  O   . CYS C  1 58  ? -65.033  9.841   57.699  1.00 29.72  ? 57  CYS E O   1 
ATOM   4943  C  CB  . CYS C  1 58  ? -66.724  10.627  60.204  1.00 31.91  ? 57  CYS E CB  1 
ATOM   4944  S  SG  . CYS C  1 58  ? -68.265  10.446  61.130  1.00 35.43  ? 57  CYS E SG  1 
ATOM   4945  N  N   . THR C  1 59  ? -63.778  9.089   59.439  1.00 26.81  ? 58  THR E N   1 
ATOM   4946  C  CA  . THR C  1 59  ? -62.461  9.194   58.736  1.00 30.36  ? 58  THR E CA  1 
ATOM   4947  C  C   . THR C  1 59  ? -62.438  8.367   57.452  1.00 27.71  ? 58  THR E C   1 
ATOM   4948  O  O   . THR C  1 59  ? -61.905  8.779   56.450  1.00 28.86  ? 58  THR E O   1 
ATOM   4949  C  CB  . THR C  1 59  ? -61.296  8.637   59.568  1.00 35.01  ? 58  THR E CB  1 
ATOM   4950  O  OG1 . THR C  1 59  ? -61.419  9.095   60.907  1.00 41.15  ? 58  THR E OG1 1 
ATOM   4951  C  CG2 . THR C  1 59  ? -59.944  9.032   59.020  1.00 39.46  ? 58  THR E CG2 1 
ATOM   4952  N  N   . SER C  1 60  ? -63.048  7.182   57.482  1.00 25.32  ? 59  SER E N   1 
ATOM   4953  C  CA  . SER C  1 60  ? -62.969  6.304   56.326  1.00 26.29  ? 59  SER E CA  1 
ATOM   4954  C  C   . SER C  1 60  ? -63.938  6.710   55.191  1.00 24.92  ? 59  SER E C   1 
ATOM   4955  O  O   . SER C  1 60  ? -63.976  6.060   54.154  1.00 25.48  ? 59  SER E O   1 
ATOM   4956  C  CB  . SER C  1 60  ? -63.138  4.864   56.765  1.00 28.17  ? 59  SER E CB  1 
ATOM   4957  O  OG  . SER C  1 60  ? -64.128  4.739   57.756  1.00 32.30  ? 59  SER E OG  1 
ATOM   4958  N  N   . ALA C  1 61  ? -64.702  7.795   55.355  1.00 23.26  ? 60  ALA E N   1 
ATOM   4959  C  CA  . ALA C  1 61  ? -65.613  8.305   54.292  1.00 23.95  ? 60  ALA E CA  1 
ATOM   4960  C  C   . ALA C  1 61  ? -64.836  8.928   53.123  1.00 24.86  ? 60  ALA E C   1 
ATOM   4961  O  O   . ALA C  1 61  ? -65.406  9.217   52.047  1.00 25.05  ? 60  ALA E O   1 
ATOM   4962  C  CB  . ALA C  1 61  ? -66.566  9.314   54.868  1.00 24.11  ? 60  ALA E CB  1 
ATOM   4963  N  N   . GLY C  1 62  ? -63.546  9.175   53.328  1.00 26.84  ? 61  GLY E N   1 
ATOM   4964  C  CA  . GLY C  1 62  ? -62.697  9.727   52.274  1.00 26.65  ? 61  GLY E CA  1 
ATOM   4965  C  C   . GLY C  1 62  ? -62.938  11.217  52.062  1.00 26.31  ? 61  GLY E C   1 
ATOM   4966  O  O   . GLY C  1 62  ? -63.489  11.897  52.927  1.00 26.75  ? 61  GLY E O   1 
ATOM   4967  N  N   . PRO C  1 63  ? -62.514  11.763  50.897  1.00 27.24  ? 62  PRO E N   1 
ATOM   4968  C  CA  . PRO C  1 63  ? -62.689  13.175  50.594  1.00 27.32  ? 62  PRO E CA  1 
ATOM   4969  C  C   . PRO C  1 63  ? -64.109  13.498  50.114  1.00 27.10  ? 62  PRO E C   1 
ATOM   4970  O  O   . PRO C  1 63  ? -64.974  12.611  50.042  1.00 24.05  ? 62  PRO E O   1 
ATOM   4971  C  CB  . PRO C  1 63  ? -61.653  13.401  49.488  1.00 28.97  ? 62  PRO E CB  1 
ATOM   4972  C  CG  . PRO C  1 63  ? -61.645  12.108  48.740  1.00 29.23  ? 62  PRO E CG  1 
ATOM   4973  C  CD  . PRO C  1 63  ? -61.819  11.046  49.817  1.00 28.73  ? 62  PRO E CD  1 
ATOM   4974  N  N   . HIS C  1 64  ? -64.325  14.766  49.786  1.00 25.82  ? 63  HIS E N   1 
ATOM   4975  C  CA  . HIS C  1 64  ? -65.619  15.229  49.269  1.00 28.53  ? 63  HIS E CA  1 
ATOM   4976  C  C   . HIS C  1 64  ? -65.919  14.466  47.982  1.00 27.38  ? 63  HIS E C   1 
ATOM   4977  O  O   . HIS C  1 64  ? -65.023  14.163  47.230  1.00 27.26  ? 63  HIS E O   1 
ATOM   4978  C  CB  . HIS C  1 64  ? -65.626  16.756  49.068  1.00 31.30  ? 63  HIS E CB  1 
ATOM   4979  C  CG  . HIS C  1 64  ? -65.594  17.515  50.350  1.00 33.81  ? 63  HIS E CG  1 
ATOM   4980  N  ND1 . HIS C  1 64  ? -65.706  18.887  50.407  1.00 33.14  ? 63  HIS E ND1 1 
ATOM   4981  C  CD2 . HIS C  1 64  ? -65.496  17.082  51.630  1.00 35.72  ? 63  HIS E CD2 1 
ATOM   4982  C  CE1 . HIS C  1 64  ? -65.648  19.273  51.670  1.00 33.92  ? 63  HIS E CE1 1 
ATOM   4983  N  NE2 . HIS C  1 64  ? -65.551  18.172  52.457  1.00 38.04  ? 63  HIS E NE2 1 
ATOM   4984  N  N   . PHE C  1 65  ? -67.190  14.113  47.773  1.00 27.21  ? 64  PHE E N   1 
ATOM   4985  C  CA  . PHE C  1 65  ? -67.616  13.481  46.534  1.00 26.10  ? 64  PHE E CA  1 
ATOM   4986  C  C   . PHE C  1 65  ? -67.447  14.492  45.388  1.00 25.76  ? 64  PHE E C   1 
ATOM   4987  O  O   . PHE C  1 65  ? -68.091  15.548  45.398  1.00 26.77  ? 64  PHE E O   1 
ATOM   4988  C  CB  . PHE C  1 65  ? -69.070  13.035  46.647  1.00 25.39  ? 64  PHE E CB  1 
ATOM   4989  C  CG  . PHE C  1 65  ? -69.624  12.382  45.410  1.00 26.12  ? 64  PHE E CG  1 
ATOM   4990  C  CD1 . PHE C  1 65  ? -70.904  12.668  44.976  1.00 26.73  ? 64  PHE E CD1 1 
ATOM   4991  C  CD2 . PHE C  1 65  ? -68.872  11.470  44.696  1.00 26.96  ? 64  PHE E CD2 1 
ATOM   4992  C  CE1 . PHE C  1 65  ? -71.419  12.046  43.854  1.00 27.56  ? 64  PHE E CE1 1 
ATOM   4993  C  CE2 . PHE C  1 65  ? -69.382  10.862  43.563  1.00 27.45  ? 64  PHE E CE2 1 
ATOM   4994  C  CZ  . PHE C  1 65  ? -70.656  11.150  43.150  1.00 27.55  ? 64  PHE E CZ  1 
ATOM   4995  N  N   . ASN C  1 66  ? -66.594  14.145  44.415  1.00 27.77  ? 65  ASN E N   1 
ATOM   4996  C  CA  . ASN C  1 66  ? -66.066  15.097  43.437  1.00 30.92  ? 65  ASN E CA  1 
ATOM   4997  C  C   . ASN C  1 66  ? -65.822  14.387  42.107  1.00 32.87  ? 65  ASN E C   1 
ATOM   4998  O  O   . ASN C  1 66  ? -64.682  14.312  41.647  1.00 36.77  ? 65  ASN E O   1 
ATOM   4999  C  CB  . ASN C  1 66  ? -64.793  15.760  43.979  1.00 32.74  ? 65  ASN E CB  1 
ATOM   5000  C  CG  . ASN C  1 66  ? -64.237  16.862  43.091  1.00 36.57  ? 65  ASN E CG  1 
ATOM   5001  O  OD1 . ASN C  1 66  ? -64.974  17.512  42.342  1.00 32.95  ? 65  ASN E OD1 1 
ATOM   5002  N  ND2 . ASN C  1 66  ? -62.934  17.096  43.201  1.00 34.58  ? 65  ASN E ND2 1 
ATOM   5003  N  N   . PRO C  1 67  ? -66.870  13.852  41.438  1.00 31.95  ? 66  PRO E N   1 
ATOM   5004  C  CA  . PRO C  1 67  ? -66.672  13.114  40.187  1.00 35.76  ? 66  PRO E CA  1 
ATOM   5005  C  C   . PRO C  1 67  ? -66.181  14.015  39.036  1.00 36.68  ? 66  PRO E C   1 
ATOM   5006  O  O   . PRO C  1 67  ? -65.546  13.521  38.130  1.00 38.04  ? 66  PRO E O   1 
ATOM   5007  C  CB  . PRO C  1 67  ? -68.053  12.511  39.884  1.00 34.51  ? 66  PRO E CB  1 
ATOM   5008  C  CG  . PRO C  1 67  ? -69.034  13.428  40.606  1.00 32.20  ? 66  PRO E CG  1 
ATOM   5009  C  CD  . PRO C  1 67  ? -68.287  13.949  41.821  1.00 32.49  ? 66  PRO E CD  1 
ATOM   5010  N  N   . LEU C  1 68  ? -66.431  15.329  39.098  1.00 38.06  ? 67  LEU E N   1 
ATOM   5011  C  CA  . LEU C  1 68  ? -65.954  16.259  38.032  1.00 41.40  ? 67  LEU E CA  1 
ATOM   5012  C  C   . LEU C  1 68  ? -64.546  16.823  38.304  1.00 43.30  ? 67  LEU E C   1 
ATOM   5013  O  O   . LEU C  1 68  ? -64.100  17.691  37.551  1.00 48.34  ? 67  LEU E O   1 
ATOM   5014  C  CB  . LEU C  1 68  ? -66.968  17.398  37.885  1.00 41.33  ? 67  LEU E CB  1 
ATOM   5015  C  CG  . LEU C  1 68  ? -68.376  16.953  37.495  1.00 42.91  ? 67  LEU E CG  1 
ATOM   5016  C  CD1 . LEU C  1 68  ? -69.295  18.150  37.313  1.00 45.95  ? 67  LEU E CD1 1 
ATOM   5017  C  CD2 . LEU C  1 68  ? -68.340  16.104  36.235  1.00 45.51  ? 67  LEU E CD2 1 
ATOM   5018  N  N   . SER C  1 69  ? -63.855  16.351  39.350  1.00 44.20  ? 68  SER E N   1 
ATOM   5019  C  CA  . SER C  1 69  ? -62.481  16.802  39.718  1.00 48.30  ? 68  SER E CA  1 
ATOM   5020  C  C   . SER C  1 69  ? -62.375  18.336  39.724  1.00 47.64  ? 68  SER E C   1 
ATOM   5021  O  O   . SER C  1 69  ? -61.476  18.895  39.106  1.00 48.75  ? 68  SER E O   1 
ATOM   5022  C  CB  . SER C  1 69  ? -61.433  16.209  38.797  1.00 49.38  ? 68  SER E CB  1 
ATOM   5023  O  OG  . SER C  1 69  ? -61.667  14.829  38.582  1.00 54.51  ? 68  SER E OG  1 
ATOM   5024  N  N   . ARG C  1 70  ? -63.304  19.002  40.415  1.00 44.66  ? 69  ARG E N   1 
ATOM   5025  C  CA  . ARG C  1 70  ? -63.308  20.454  40.574  1.00 44.58  ? 69  ARG E CA  1 
ATOM   5026  C  C   . ARG C  1 70  ? -62.796  20.806  41.976  1.00 45.96  ? 69  ARG E C   1 
ATOM   5027  O  O   . ARG C  1 70  ? -62.531  19.916  42.796  1.00 42.56  ? 69  ARG E O   1 
ATOM   5028  C  CB  . ARG C  1 70  ? -64.712  21.015  40.321  1.00 48.03  ? 69  ARG E CB  1 
ATOM   5029  C  CG  . ARG C  1 70  ? -65.183  20.837  38.882  1.00 53.00  ? 69  ARG E CG  1 
ATOM   5030  C  CD  . ARG C  1 70  ? -66.399  21.685  38.559  1.00 58.56  ? 69  ARG E CD  1 
ATOM   5031  N  NE  . ARG C  1 70  ? -66.923  21.425  37.223  1.00 61.74  ? 69  ARG E NE  1 
ATOM   5032  C  CZ  . ARG C  1 70  ? -68.134  21.777  36.796  1.00 64.34  ? 69  ARG E CZ  1 
ATOM   5033  N  NH1 . ARG C  1 70  ? -68.547  21.371  35.608  1.00 66.47  ? 69  ARG E NH1 1 
ATOM   5034  N  NH2 . ARG C  1 70  ? -68.934  22.515  37.551  1.00 58.89  ? 69  ARG E NH2 1 
ATOM   5035  N  N   . LYS C  1 71  ? -62.632  22.112  42.212  1.00 45.00  ? 70  LYS E N   1 
ATOM   5036  C  CA  . LYS C  1 71  ? -62.252  22.658  43.493  1.00 46.79  ? 70  LYS E CA  1 
ATOM   5037  C  C   . LYS C  1 71  ? -63.510  22.866  44.353  1.00 44.67  ? 70  LYS E C   1 
ATOM   5038  O  O   . LYS C  1 71  ? -64.625  23.103  43.837  1.00 40.63  ? 70  LYS E O   1 
ATOM   5039  C  CB  . LYS C  1 71  ? -61.488  23.974  43.307  1.00 51.51  ? 70  LYS E CB  1 
ATOM   5040  C  CG  . LYS C  1 71  ? -60.083  23.819  42.730  1.00 59.28  ? 70  LYS E CG  1 
ATOM   5041  C  CD  . LYS C  1 71  ? -59.227  25.050  42.909  1.00 67.13  ? 70  LYS E CD  1 
ATOM   5042  C  CE  . LYS C  1 71  ? -59.812  26.284  42.251  1.00 75.88  ? 70  LYS E CE  1 
ATOM   5043  N  NZ  . LYS C  1 71  ? -58.923  27.460  42.419  1.00 82.86  ? 70  LYS E NZ  1 
ATOM   5044  N  N   . HIS C  1 72  ? -63.302  22.800  45.673  1.00 40.27  ? 71  HIS E N   1 
ATOM   5045  C  CA  . HIS C  1 72  ? -64.366  22.943  46.630  1.00 39.50  ? 71  HIS E CA  1 
ATOM   5046  C  C   . HIS C  1 72  ? -64.991  24.323  46.457  1.00 39.79  ? 71  HIS E C   1 
ATOM   5047  O  O   . HIS C  1 72  ? -64.296  25.307  46.184  1.00 37.68  ? 71  HIS E O   1 
ATOM   5048  C  CB  . HIS C  1 72  ? -63.840  22.739  48.056  1.00 39.77  ? 71  HIS E CB  1 
ATOM   5049  C  CG  . HIS C  1 72  ? -64.853  23.006  49.107  1.00 41.32  ? 71  HIS E CG  1 
ATOM   5050  N  ND1 . HIS C  1 72  ? -65.896  22.136  49.373  1.00 38.19  ? 71  HIS E ND1 1 
ATOM   5051  C  CD2 . HIS C  1 72  ? -64.978  24.042  49.965  1.00 41.18  ? 71  HIS E CD2 1 
ATOM   5052  C  CE1 . HIS C  1 72  ? -66.630  22.637  50.343  1.00 41.54  ? 71  HIS E CE1 1 
ATOM   5053  N  NE2 . HIS C  1 72  ? -66.083  23.803  50.728  1.00 43.88  ? 71  HIS E NE2 1 
ATOM   5054  N  N   . GLY C  1 73  ? -66.310  24.390  46.636  1.00 38.85  ? 72  GLY E N   1 
ATOM   5055  C  CA  . GLY C  1 73  ? -66.982  25.662  46.697  1.00 36.28  ? 72  GLY E CA  1 
ATOM   5056  C  C   . GLY C  1 73  ? -68.228  25.586  47.543  1.00 36.83  ? 72  GLY E C   1 
ATOM   5057  O  O   . GLY C  1 73  ? -68.431  24.620  48.266  1.00 37.69  ? 72  GLY E O   1 
ATOM   5058  N  N   . GLY C  1 74  ? -69.036  26.645  47.452  1.00 36.30  ? 73  GLY E N   1 
ATOM   5059  C  CA  . GLY C  1 74  ? -70.371  26.672  47.998  1.00 39.87  ? 73  GLY E CA  1 
ATOM   5060  C  C   . GLY C  1 74  ? -71.358  26.041  47.024  1.00 39.50  ? 73  GLY E C   1 
ATOM   5061  O  O   . GLY C  1 74  ? -71.092  25.976  45.823  1.00 38.95  ? 73  GLY E O   1 
ATOM   5062  N  N   . PRO C  1 75  ? -72.531  25.583  47.512  1.00 41.29  ? 74  PRO E N   1 
ATOM   5063  C  CA  . PRO C  1 75  ? -73.515  24.904  46.669  1.00 42.05  ? 74  PRO E CA  1 
ATOM   5064  C  C   . PRO C  1 75  ? -73.950  25.700  45.426  1.00 45.29  ? 74  PRO E C   1 
ATOM   5065  O  O   . PRO C  1 75  ? -74.266  25.091  44.400  1.00 43.65  ? 74  PRO E O   1 
ATOM   5066  C  CB  . PRO C  1 75  ? -74.726  24.701  47.587  1.00 41.21  ? 74  PRO E CB  1 
ATOM   5067  C  CG  . PRO C  1 75  ? -74.485  25.634  48.757  1.00 42.77  ? 74  PRO E CG  1 
ATOM   5068  C  CD  . PRO C  1 75  ? -72.984  25.715  48.902  1.00 41.95  ? 74  PRO E CD  1 
ATOM   5069  N  N   . LYS C  1 76  ? -73.931  27.037  45.520  1.00 46.39  ? 75  LYS E N   1 
ATOM   5070  C  CA  . LYS C  1 76  ? -74.408  27.915  44.441  1.00 51.68  ? 75  LYS E CA  1 
ATOM   5071  C  C   . LYS C  1 76  ? -73.287  28.306  43.452  1.00 49.22  ? 75  LYS E C   1 
ATOM   5072  O  O   . LYS C  1 76  ? -73.529  29.077  42.512  1.00 46.19  ? 75  LYS E O   1 
ATOM   5073  C  CB  . LYS C  1 76  ? -75.032  29.154  45.080  1.00 57.08  ? 75  LYS E CB  1 
ATOM   5074  C  CG  . LYS C  1 76  ? -74.048  30.267  45.410  1.00 63.87  ? 75  LYS E CG  1 
ATOM   5075  C  CD  . LYS C  1 76  ? -74.535  31.181  46.508  1.00 71.97  ? 75  LYS E CD  1 
ATOM   5076  C  CE  . LYS C  1 76  ? -75.997  31.554  46.380  1.00 77.39  ? 75  LYS E CE  1 
ATOM   5077  N  NZ  . LYS C  1 76  ? -76.350  32.080  45.036  1.00 77.43  ? 75  LYS E NZ  1 
ATOM   5078  N  N   . ASP C  1 77  ? -72.066  27.794  43.651  1.00 44.91  ? 76  ASP E N   1 
ATOM   5079  C  CA  . ASP C  1 77  ? -70.954  28.032  42.748  1.00 46.20  ? 76  ASP E CA  1 
ATOM   5080  C  C   . ASP C  1 77  ? -70.941  26.941  41.672  1.00 49.56  ? 76  ASP E C   1 
ATOM   5081  O  O   . ASP C  1 77  ? -71.254  25.783  41.969  1.00 48.19  ? 76  ASP E O   1 
ATOM   5082  C  CB  . ASP C  1 77  ? -69.622  28.039  43.507  1.00 47.64  ? 76  ASP E CB  1 
ATOM   5083  C  CG  . ASP C  1 77  ? -69.516  29.098  44.600  1.00 51.86  ? 76  ASP E CG  1 
ATOM   5084  O  OD1 . ASP C  1 77  ? -69.021  28.761  45.698  1.00 51.84  ? 76  ASP E OD1 1 
ATOM   5085  O  OD2 . ASP C  1 77  ? -69.895  30.263  44.338  1.00 51.64  ? 76  ASP E OD2 1 
ATOM   5086  N  N   . GLU C  1 78  ? -70.542  27.294  40.442  1.00 48.21  ? 77  GLU E N   1 
ATOM   5087  C  CA  . GLU C  1 78  ? -70.315  26.284  39.402  1.00 50.64  ? 77  GLU E CA  1 
ATOM   5088  C  C   . GLU C  1 78  ? -69.064  25.485  39.770  1.00 44.01  ? 77  GLU E C   1 
ATOM   5089  O  O   . GLU C  1 78  ? -69.044  24.266  39.600  1.00 45.87  ? 77  GLU E O   1 
ATOM   5090  C  CB  . GLU C  1 78  ? -70.113  26.856  37.995  1.00 60.50  ? 77  GLU E CB  1 
ATOM   5091  C  CG  . GLU C  1 78  ? -70.122  25.774  36.905  1.00 70.05  ? 77  GLU E CG  1 
ATOM   5092  C  CD  . GLU C  1 78  ? -69.297  26.046  35.651  1.00 81.98  ? 77  GLU E CD  1 
ATOM   5093  O  OE1 . GLU C  1 78  ? -69.548  27.072  34.985  1.00 87.62  ? 77  GLU E OE1 1 
ATOM   5094  O  OE2 . GLU C  1 78  ? -68.398  25.227  35.333  1.00 87.45  ? 77  GLU E OE2 1 
ATOM   5095  N  N   . GLU C  1 79  ? -68.021  26.179  40.243  1.00 42.60  ? 78  GLU E N   1 
ATOM   5096  C  CA  . GLU C  1 79  ? -66.819  25.501  40.721  1.00 42.88  ? 78  GLU E CA  1 
ATOM   5097  C  C   . GLU C  1 79  ? -67.104  25.026  42.153  1.00 39.95  ? 78  GLU E C   1 
ATOM   5098  O  O   . GLU C  1 79  ? -66.961  25.765  43.132  1.00 38.55  ? 78  GLU E O   1 
ATOM   5099  C  CB  . GLU C  1 79  ? -65.566  26.379  40.640  1.00 44.37  ? 78  GLU E CB  1 
ATOM   5100  C  CG  . GLU C  1 79  ? -64.275  25.615  40.913  1.00 45.26  ? 78  GLU E CG  1 
ATOM   5101  C  CD  . GLU C  1 79  ? -63.806  24.689  39.801  1.00 51.59  ? 78  GLU E CD  1 
ATOM   5102  O  OE1 . GLU C  1 79  ? -62.793  23.984  39.999  1.00 53.81  ? 78  GLU E OE1 1 
ATOM   5103  O  OE2 . GLU C  1 79  ? -64.447  24.667  38.736  1.00 56.75  ? 78  GLU E OE2 1 
ATOM   5104  N  N   . ARG C  1 80  ? -67.531  23.768  42.247  1.00 36.72  ? 79  ARG E N   1 
ATOM   5105  C  CA  . ARG C  1 80  ? -67.802  23.117  43.529  1.00 36.55  ? 79  ARG E CA  1 
ATOM   5106  C  C   . ARG C  1 80  ? -67.626  21.615  43.336  1.00 33.67  ? 79  ARG E C   1 
ATOM   5107  O  O   . ARG C  1 80  ? -67.622  21.138  42.198  1.00 33.26  ? 79  ARG E O   1 
ATOM   5108  C  CB  . ARG C  1 80  ? -69.237  23.399  43.975  1.00 35.39  ? 79  ARG E CB  1 
ATOM   5109  C  CG  . ARG C  1 80  ? -70.280  22.864  43.002  1.00 35.56  ? 79  ARG E CG  1 
ATOM   5110  C  CD  . ARG C  1 80  ? -71.668  22.966  43.600  1.00 36.28  ? 79  ARG E CD  1 
ATOM   5111  N  NE  . ARG C  1 80  ? -72.067  21.767  44.326  1.00 34.20  ? 79  ARG E NE  1 
ATOM   5112  C  CZ  . ARG C  1 80  ? -73.323  21.528  44.704  1.00 35.87  ? 79  ARG E CZ  1 
ATOM   5113  N  NH1 . ARG C  1 80  ? -73.661  20.342  45.194  1.00 29.15  ? 79  ARG E NH1 1 
ATOM   5114  N  NH2 . ARG C  1 80  ? -74.241  22.476  44.546  1.00 30.97  ? 79  ARG E NH2 1 
ATOM   5115  N  N   . HIS C  1 81  ? -67.495  20.893  44.449  1.00 32.60  ? 80  HIS E N   1 
ATOM   5116  C  CA  . HIS C  1 81  ? -67.631  19.456  44.430  1.00 31.74  ? 80  HIS E CA  1 
ATOM   5117  C  C   . HIS C  1 81  ? -69.121  19.142  44.328  1.00 29.59  ? 80  HIS E C   1 
ATOM   5118  O  O   . HIS C  1 81  ? -69.962  19.907  44.834  1.00 29.28  ? 80  HIS E O   1 
ATOM   5119  C  CB  . HIS C  1 81  ? -67.013  18.803  45.677  1.00 33.53  ? 80  HIS E CB  1 
ATOM   5120  C  CG  . HIS C  1 81  ? -65.577  19.137  45.909  1.00 35.59  ? 80  HIS E CG  1 
ATOM   5121  N  ND1 . HIS C  1 81  ? -65.024  19.280  47.178  1.00 36.36  ? 80  HIS E ND1 1 
ATOM   5122  C  CD2 . HIS C  1 81  ? -64.580  19.360  45.032  1.00 39.50  ? 80  HIS E CD2 1 
ATOM   5123  C  CE1 . HIS C  1 81  ? -63.742  19.540  47.050  1.00 38.83  ? 80  HIS E CE1 1 
ATOM   5124  N  NE2 . HIS C  1 81  ? -63.444  19.590  45.744  1.00 37.35  ? 80  HIS E NE2 1 
ATOM   5125  N  N   . VAL C  1 82  ? -69.447  17.988  43.734  1.00 27.66  ? 81  VAL E N   1 
ATOM   5126  C  CA  . VAL C  1 82  ? -70.819  17.545  43.751  1.00 27.73  ? 81  VAL E CA  1 
ATOM   5127  C  C   . VAL C  1 82  ? -71.282  17.494  45.216  1.00 25.87  ? 81  VAL E C   1 
ATOM   5128  O  O   . VAL C  1 82  ? -72.412  17.856  45.524  1.00 27.50  ? 81  VAL E O   1 
ATOM   5129  C  CB  . VAL C  1 82  ? -71.002  16.213  43.000  1.00 27.68  ? 81  VAL E CB  1 
ATOM   5130  C  CG1 . VAL C  1 82  ? -72.350  15.558  43.268  1.00 27.99  ? 81  VAL E CG1 1 
ATOM   5131  C  CG2 . VAL C  1 82  ? -70.807  16.426  41.504  1.00 31.45  ? 81  VAL E CG2 1 
ATOM   5132  N  N   . GLY C  1 83  ? -70.380  17.107  46.126  1.00 27.14  ? 82  GLY E N   1 
ATOM   5133  C  CA  . GLY C  1 83  ? -70.760  16.891  47.540  1.00 28.23  ? 82  GLY E CA  1 
ATOM   5134  C  C   . GLY C  1 83  ? -70.856  18.143  48.404  1.00 30.74  ? 82  GLY E C   1 
ATOM   5135  O  O   . GLY C  1 83  ? -71.197  18.029  49.580  1.00 30.18  ? 82  GLY E O   1 
ATOM   5136  N  N   A SER C  1 84  ? -70.554  19.334  47.867  0.60 33.17  ? 83  SER E N   1 
ATOM   5137  C  CA  A SER C  1 84  ? -70.437  20.535  48.708  0.60 33.96  ? 83  SER E CA  1 
ATOM   5138  C  C   A SER C  1 84  ? -71.812  21.199  48.873  0.60 31.91  ? 83  SER E C   1 
ATOM   5139  O  O   A SER C  1 84  ? -72.247  21.964  48.013  0.60 35.29  ? 83  SER E O   1 
ATOM   5140  C  CB  A SER C  1 84  ? -69.362  21.462  48.154  0.60 38.08  ? 83  SER E CB  1 
ATOM   5141  O  OG  A SER C  1 84  ? -68.046  20.904  48.340  0.60 43.00  ? 83  SER E OG  1 
ATOM   5142  N  N   B ASP C  1 84  ? -70.602  19.320  47.807  0.40 28.33  ? 83  ASP E N   1 
ATOM   5143  C  CA  B ASP C  1 84  ? -70.575  20.583  48.528  0.40 27.35  ? 83  ASP E CA  1 
ATOM   5144  C  C   B ASP C  1 84  ? -72.001  21.070  48.771  0.40 27.42  ? 83  ASP E C   1 
ATOM   5145  O  O   B ASP C  1 84  ? -72.651  21.590  47.862  0.40 28.77  ? 83  ASP E O   1 
ATOM   5146  C  CB  B ASP C  1 84  ? -69.791  21.639  47.749  0.40 26.54  ? 83  ASP E CB  1 
ATOM   5147  C  CG  B ASP C  1 84  ? -68.334  21.251  47.652  0.40 26.30  ? 83  ASP E CG  1 
ATOM   5148  O  OD1 B ASP C  1 84  ? -67.948  20.318  48.404  0.40 30.27  ? 83  ASP E OD1 1 
ATOM   5149  O  OD2 B ASP C  1 84  ? -67.615  21.841  46.842  0.40 22.92  ? 83  ASP E OD2 1 
ATOM   5150  N  N   . LEU C  1 85  ? -72.482  20.908  50.003  1.00 26.97  ? 84  LEU E N   1 
ATOM   5151  C  CA  . LEU C  1 85  ? -73.833  21.385  50.324  1.00 26.55  ? 84  LEU E CA  1 
ATOM   5152  C  C   . LEU C  1 85  ? -73.805  22.575  51.297  1.00 26.76  ? 84  LEU E C   1 
ATOM   5153  O  O   . LEU C  1 85  ? -74.820  22.935  51.836  1.00 28.91  ? 84  LEU E O   1 
ATOM   5154  C  CB  . LEU C  1 85  ? -74.651  20.223  50.892  1.00 28.33  ? 84  LEU E CB  1 
ATOM   5155  C  CG  . LEU C  1 85  ? -74.885  19.055  49.929  1.00 29.09  ? 84  LEU E CG  1 
ATOM   5156  C  CD1 . LEU C  1 85  ? -75.692  17.973  50.612  1.00 31.32  ? 84  LEU E CD1 1 
ATOM   5157  C  CD2 . LEU C  1 85  ? -75.594  19.516  48.670  1.00 31.16  ? 84  LEU E CD2 1 
ATOM   5158  N  N   . GLY C  1 86  ? -72.651  23.206  51.475  1.00 26.34  ? 85  GLY E N   1 
ATOM   5159  C  CA  . GLY C  1 86  ? -72.565  24.456  52.232  1.00 29.30  ? 85  GLY E CA  1 
ATOM   5160  C  C   . GLY C  1 86  ? -72.569  24.228  53.741  1.00 26.67  ? 85  GLY E C   1 
ATOM   5161  O  O   . GLY C  1 86  ? -71.871  23.349  54.265  1.00 27.58  ? 85  GLY E O   1 
ATOM   5162  N  N   . ASN C  1 87  ? -73.338  25.062  54.434  1.00 27.15  ? 86  ASN E N   1 
ATOM   5163  C  CA  . ASN C  1 87  ? -73.351  25.149  55.896  1.00 27.01  ? 86  ASN E CA  1 
ATOM   5164  C  C   . ASN C  1 87  ? -74.759  24.911  56.395  1.00 27.56  ? 86  ASN E C   1 
ATOM   5165  O  O   . ASN C  1 87  ? -75.697  25.332  55.751  1.00 27.70  ? 86  ASN E O   1 
ATOM   5166  C  CB  . ASN C  1 87  ? -72.941  26.542  56.382  1.00 28.64  ? 86  ASN E CB  1 
ATOM   5167  C  CG  . ASN C  1 87  ? -71.452  26.748  56.271  1.00 30.86  ? 86  ASN E CG  1 
ATOM   5168  O  OD1 . ASN C  1 87  ? -70.678  26.056  56.934  1.00 31.14  ? 86  ASN E OD1 1 
ATOM   5169  N  ND2 . ASN C  1 87  ? -71.051  27.636  55.378  1.00 32.40  ? 86  ASN E ND2 1 
ATOM   5170  N  N   . VAL C  1 88  ? -74.876  24.255  57.549  1.00 26.24  ? 87  VAL E N   1 
ATOM   5171  C  CA  . VAL C  1 88  ? -76.094  24.226  58.301  1.00 26.33  ? 87  VAL E CA  1 
ATOM   5172  C  C   . VAL C  1 88  ? -75.857  25.094  59.543  1.00 26.34  ? 87  VAL E C   1 
ATOM   5173  O  O   . VAL C  1 88  ? -74.721  25.289  59.943  1.00 26.73  ? 87  VAL E O   1 
ATOM   5174  C  CB  . VAL C  1 88  ? -76.531  22.782  58.642  1.00 27.21  ? 87  VAL E CB  1 
ATOM   5175  C  CG1 . VAL C  1 88  ? -76.720  21.948  57.376  1.00 28.51  ? 87  VAL E CG1 1 
ATOM   5176  C  CG2 . VAL C  1 88  ? -75.583  22.094  59.620  1.00 26.85  ? 87  VAL E CG2 1 
ATOM   5177  N  N   . THR C  1 89  ? -76.941  25.601  60.125  1.00 26.71  ? 88  THR E N   1 
ATOM   5178  C  CA  . THR C  1 89  ? -76.858  26.557  61.205  1.00 29.97  ? 88  THR E CA  1 
ATOM   5179  C  C   . THR C  1 89  ? -77.511  25.957  62.440  1.00 27.21  ? 88  THR E C   1 
ATOM   5180  O  O   . THR C  1 89  ? -78.678  25.642  62.407  1.00 27.05  ? 88  THR E O   1 
ATOM   5181  C  CB  . THR C  1 89  ? -77.552  27.889  60.878  1.00 31.60  ? 88  THR E CB  1 
ATOM   5182  O  OG1 . THR C  1 89  ? -76.998  28.349  59.654  1.00 36.12  ? 88  THR E OG1 1 
ATOM   5183  C  CG2 . THR C  1 89  ? -77.338  28.930  61.959  1.00 34.72  ? 88  THR E CG2 1 
ATOM   5184  N  N   . ALA C  1 90  ? -76.738  25.822  63.517  1.00 26.63  ? 89  ALA E N   1 
ATOM   5185  C  CA  . ALA C  1 90  ? -77.308  25.383  64.769  1.00 27.76  ? 89  ALA E CA  1 
ATOM   5186  C  C   . ALA C  1 90  ? -77.685  26.621  65.598  1.00 28.77  ? 89  ALA E C   1 
ATOM   5187  O  O   . ALA C  1 90  ? -76.914  27.578  65.675  1.00 29.09  ? 89  ALA E O   1 
ATOM   5188  C  CB  . ALA C  1 90  ? -76.342  24.481  65.493  1.00 27.33  ? 89  ALA E CB  1 
ATOM   5189  N  N   . ASP C  1 91  ? -78.870  26.555  66.204  1.00 30.45  ? 90  ASP E N   1 
ATOM   5190  C  CA  . ASP C  1 91  ? -79.402  27.552  67.120  1.00 36.37  ? 90  ASP E CA  1 
ATOM   5191  C  C   . ASP C  1 91  ? -78.712  27.397  68.485  1.00 37.89  ? 90  ASP E C   1 
ATOM   5192  O  O   . ASP C  1 91  ? -77.776  26.612  68.642  1.00 32.77  ? 90  ASP E O   1 
ATOM   5193  C  CB  . ASP C  1 91  ? -80.933  27.426  67.193  1.00 35.34  ? 90  ASP E CB  1 
ATOM   5194  C  CG  . ASP C  1 91  ? -81.440  26.164  67.877  1.00 37.16  ? 90  ASP E CG  1 
ATOM   5195  O  OD1 . ASP C  1 91  ? -82.629  25.866  67.716  1.00 40.30  ? 90  ASP E OD1 1 
ATOM   5196  O  OD2 . ASP C  1 91  ? -80.648  25.488  68.572  1.00 33.94  ? 90  ASP E OD2 1 
ATOM   5197  N  N   . LYS C  1 92  ? -79.205  28.122  69.492  1.00 36.57  ? 91  LYS E N   1 
ATOM   5198  C  CA  . LYS C  1 92  ? -78.524  28.188  70.780  1.00 41.06  ? 91  LYS E CA  1 
ATOM   5199  C  C   . LYS C  1 92  ? -78.735  26.890  71.569  1.00 36.37  ? 91  LYS E C   1 
ATOM   5200  O  O   . LYS C  1 92  ? -77.978  26.635  72.469  1.00 38.47  ? 91  LYS E O   1 
ATOM   5201  C  CB  . LYS C  1 92  ? -78.910  29.459  71.558  1.00 45.92  ? 91  LYS E CB  1 
ATOM   5202  C  CG  . LYS C  1 92  ? -80.380  29.674  71.908  1.00 56.74  ? 91  LYS E CG  1 
ATOM   5203  C  CD  . LYS C  1 92  ? -80.989  28.660  72.872  1.00 71.37  ? 91  LYS E CD  1 
ATOM   5204  C  CE  . LYS C  1 92  ? -80.284  28.533  74.214  1.00 80.89  ? 91  LYS E CE  1 
ATOM   5205  N  NZ  . LYS C  1 92  ? -80.031  29.840  74.870  1.00 87.36  ? 91  LYS E NZ  1 
ATOM   5206  N  N   . ASP C  1 93  ? -79.735  26.075  71.212  1.00 34.96  ? 92  ASP E N   1 
ATOM   5207  C  CA  . ASP C  1 93  ? -79.926  24.749  71.810  1.00 36.92  ? 92  ASP E CA  1 
ATOM   5208  C  C   . ASP C  1 93  ? -79.156  23.651  71.047  1.00 35.49  ? 92  ASP E C   1 
ATOM   5209  O  O   . ASP C  1 93  ? -79.301  22.473  71.346  1.00 34.02  ? 92  ASP E O   1 
ATOM   5210  C  CB  . ASP C  1 93  ? -81.411  24.401  71.859  1.00 39.99  ? 92  ASP E CB  1 
ATOM   5211  C  CG  . ASP C  1 93  ? -82.176  25.288  72.822  1.00 48.15  ? 92  ASP E CG  1 
ATOM   5212  O  OD1 . ASP C  1 93  ? -83.287  25.694  72.462  1.00 50.47  ? 92  ASP E OD1 1 
ATOM   5213  O  OD2 . ASP C  1 93  ? -81.637  25.573  73.920  1.00 49.94  ? 92  ASP E OD2 1 
ATOM   5214  N  N   . GLY C  1 94  ? -78.355  24.040  70.057  1.00 33.51  ? 93  GLY E N   1 
ATOM   5215  C  CA  . GLY C  1 94  ? -77.494  23.112  69.323  1.00 33.87  ? 93  GLY E CA  1 
ATOM   5216  C  C   . GLY C  1 94  ? -78.239  22.333  68.245  1.00 30.99  ? 93  GLY E C   1 
ATOM   5217  O  O   . GLY C  1 94  ? -77.735  21.305  67.797  1.00 30.49  ? 93  GLY E O   1 
ATOM   5218  N  N   . VAL C  1 95  ? -79.419  22.826  67.834  1.00 29.67  ? 94  VAL E N   1 
ATOM   5219  C  CA  . VAL C  1 95  ? -80.271  22.170  66.829  1.00 29.48  ? 94  VAL E CA  1 
ATOM   5220  C  C   . VAL C  1 95  ? -80.149  22.945  65.514  1.00 32.09  ? 94  VAL E C   1 
ATOM   5221  O  O   . VAL C  1 95  ? -80.332  24.169  65.486  1.00 28.00  ? 94  VAL E O   1 
ATOM   5222  C  CB  . VAL C  1 95  ? -81.746  22.080  67.250  1.00 30.29  ? 94  VAL E CB  1 
ATOM   5223  C  CG1 . VAL C  1 95  ? -82.594  21.436  66.159  1.00 30.45  ? 94  VAL E CG1 1 
ATOM   5224  C  CG2 . VAL C  1 95  ? -81.934  21.358  68.564  1.00 29.43  ? 94  VAL E CG2 1 
ATOM   5225  N  N   . ALA C  1 96  ? -79.812  22.226  64.440  1.00 29.80  ? 95  ALA E N   1 
ATOM   5226  C  CA  . ALA C  1 96  ? -79.834  22.762  63.088  1.00 28.69  ? 95  ALA E CA  1 
ATOM   5227  C  C   . ALA C  1 96  ? -81.019  22.167  62.331  1.00 30.15  ? 95  ALA E C   1 
ATOM   5228  O  O   . ALA C  1 96  ? -81.107  20.946  62.199  1.00 28.50  ? 95  ALA E O   1 
ATOM   5229  C  CB  . ALA C  1 96  ? -78.539  22.443  62.397  1.00 28.51  ? 95  ALA E CB  1 
ATOM   5230  N  N   . ASP C  1 97  ? -81.894  23.038  61.812  1.00 27.58  ? 96  ASP E N   1 
ATOM   5231  C  CA  . ASP C  1 97  ? -82.972  22.649  60.928  1.00 31.58  ? 96  ASP E CA  1 
ATOM   5232  C  C   . ASP C  1 97  ? -82.461  22.789  59.498  1.00 30.66  ? 96  ASP E C   1 
ATOM   5233  O  O   . ASP C  1 97  ? -82.029  23.865  59.081  1.00 34.30  ? 96  ASP E O   1 
ATOM   5234  C  CB  . ASP C  1 97  ? -84.238  23.493  61.112  1.00 37.56  ? 96  ASP E CB  1 
ATOM   5235  C  CG  . ASP C  1 97  ? -84.995  23.196  62.397  1.00 44.29  ? 96  ASP E CG  1 
ATOM   5236  O  OD1 . ASP C  1 97  ? -85.677  24.126  62.900  1.00 56.75  ? 96  ASP E OD1 1 
ATOM   5237  O  OD2 . ASP C  1 97  ? -84.897  22.038  62.899  1.00 52.28  ? 96  ASP E OD2 1 
ATOM   5238  N  N   . VAL C  1 98  ? -82.523  21.697  58.750  1.00 26.69  ? 97  VAL E N   1 
ATOM   5239  C  CA  . VAL C  1 98  ? -81.939  21.650  57.420  1.00 28.43  ? 97  VAL E CA  1 
ATOM   5240  C  C   . VAL C  1 98  ? -83.086  21.645  56.410  1.00 27.84  ? 97  VAL E C   1 
ATOM   5241  O  O   . VAL C  1 98  ? -84.056  20.847  56.535  1.00 24.02  ? 97  VAL E O   1 
ATOM   5242  C  CB  . VAL C  1 98  ? -81.024  20.419  57.253  1.00 29.99  ? 97  VAL E CB  1 
ATOM   5243  C  CG1 . VAL C  1 98  ? -80.417  20.320  55.864  1.00 29.61  ? 97  VAL E CG1 1 
ATOM   5244  C  CG2 . VAL C  1 98  ? -79.934  20.373  58.313  1.00 29.57  ? 97  VAL E CG2 1 
ATOM   5245  N  N   . SER C  1 99  ? -82.963  22.533  55.420  1.00 30.69  ? 98  SER E N   1 
ATOM   5246  C  CA  . SER C  1 99  ? -83.871  22.582  54.290  1.00 34.95  ? 98  SER E CA  1 
ATOM   5247  C  C   . SER C  1 99  ? -83.163  23.202  53.087  1.00 37.77  ? 98  SER E C   1 
ATOM   5248  O  O   . SER C  1 99  ? -82.944  24.407  53.017  1.00 36.40  ? 98  SER E O   1 
ATOM   5249  C  CB  . SER C  1 99  ? -85.124  23.329  54.616  1.00 40.90  ? 98  SER E CB  1 
ATOM   5250  O  OG  . SER C  1 99  ? -86.103  23.084  53.610  1.00 46.06  ? 98  SER E OG  1 
ATOM   5251  N  N   . ILE C  1 100 ? -82.816  22.344  52.141  1.00 30.27  ? 99  ILE E N   1 
ATOM   5252  C  CA  . ILE C  1 100 ? -81.932  22.651  51.033  1.00 33.62  ? 99  ILE E CA  1 
ATOM   5253  C  C   . ILE C  1 100 ? -82.605  22.068  49.790  1.00 32.78  ? 99  ILE E C   1 
ATOM   5254  O  O   . ILE C  1 100 ? -83.261  21.008  49.875  1.00 27.09  ? 99  ILE E O   1 
ATOM   5255  C  CB  . ILE C  1 100 ? -80.551  21.991  51.270  1.00 36.01  ? 99  ILE E CB  1 
ATOM   5256  C  CG1 . ILE C  1 100 ? -79.795  22.645  52.424  1.00 43.57  ? 99  ILE E CG1 1 
ATOM   5257  C  CG2 . ILE C  1 100 ? -79.714  21.956  49.997  1.00 38.38  ? 99  ILE E CG2 1 
ATOM   5258  C  CD1 . ILE C  1 100 ? -78.497  21.945  52.767  1.00 46.10  ? 99  ILE E CD1 1 
ATOM   5259  N  N   . GLU C  1 101 ? -82.436  22.744  48.658  1.00 30.47  ? 100 GLU E N   1 
ATOM   5260  C  CA  . GLU C  1 101 ? -82.697  22.143  47.365  1.00 32.52  ? 100 GLU E CA  1 
ATOM   5261  C  C   . GLU C  1 101 ? -81.388  22.205  46.592  1.00 30.40  ? 100 GLU E C   1 
ATOM   5262  O  O   . GLU C  1 101 ? -80.731  23.227  46.613  1.00 31.93  ? 100 GLU E O   1 
ATOM   5263  C  CB  . GLU C  1 101 ? -83.820  22.847  46.607  1.00 38.05  ? 100 GLU E CB  1 
ATOM   5264  C  CG  . GLU C  1 101 ? -84.146  22.145  45.305  1.00 43.93  ? 100 GLU E CG  1 
ATOM   5265  C  CD  . GLU C  1 101 ? -85.314  22.713  44.518  1.00 52.36  ? 100 GLU E CD  1 
ATOM   5266  O  OE1 . GLU C  1 101 ? -86.431  22.122  44.600  1.00 59.00  ? 100 GLU E OE1 1 
ATOM   5267  O  OE2 . GLU C  1 101 ? -85.098  23.720  43.813  1.00 52.42  ? 100 GLU E OE2 1 
ATOM   5268  N  N   . ASP C  1 102 ? -81.008  21.110  45.929  1.00 27.87  ? 101 ASP E N   1 
ATOM   5269  C  CA  . ASP C  1 102 ? -79.764  21.099  45.192  1.00 27.26  ? 101 ASP E CA  1 
ATOM   5270  C  C   . ASP C  1 102 ? -79.970  20.426  43.833  1.00 27.32  ? 101 ASP E C   1 
ATOM   5271  O  O   . ASP C  1 102 ? -80.611  19.399  43.755  1.00 25.91  ? 101 ASP E O   1 
ATOM   5272  C  CB  . ASP C  1 102 ? -78.654  20.436  46.010  1.00 27.91  ? 101 ASP E CB  1 
ATOM   5273  C  CG  . ASP C  1 102 ? -77.276  20.663  45.410  1.00 31.48  ? 101 ASP E CG  1 
ATOM   5274  O  OD1 . ASP C  1 102 ? -76.805  19.788  44.636  1.00 26.17  ? 101 ASP E OD1 1 
ATOM   5275  O  OD2 . ASP C  1 102 ? -76.709  21.747  45.668  1.00 33.95  ? 101 ASP E OD2 1 
ATOM   5276  N  N   . SER C  1 103 ? -79.367  21.006  42.783  1.00 25.21  ? 102 SER E N   1 
ATOM   5277  C  CA  . SER C  1 103 ? -79.510  20.545  41.398  1.00 28.39  ? 102 SER E CA  1 
ATOM   5278  C  C   . SER C  1 103 ? -78.269  19.814  40.881  1.00 24.62  ? 102 SER E C   1 
ATOM   5279  O  O   . SER C  1 103 ? -78.255  19.406  39.736  1.00 28.26  ? 102 SER E O   1 
ATOM   5280  C  CB  . SER C  1 103 ? -79.853  21.718  40.481  1.00 29.34  ? 102 SER E CB  1 
ATOM   5281  O  OG  . SER C  1 103 ? -81.207  22.064  40.674  1.00 38.48  ? 102 SER E OG  1 
ATOM   5282  N  N   . VAL C  1 104 ? -77.231  19.669  41.699  1.00 25.15  ? 103 VAL E N   1 
ATOM   5283  C  CA  . VAL C  1 104 ? -76.001  19.009  41.294  1.00 24.42  ? 103 VAL E CA  1 
ATOM   5284  C  C   . VAL C  1 104 ? -75.952  17.566  41.820  1.00 24.50  ? 103 VAL E C   1 
ATOM   5285  O  O   . VAL C  1 104 ? -75.582  16.660  41.081  1.00 24.76  ? 103 VAL E O   1 
ATOM   5286  C  CB  . VAL C  1 104 ? -74.774  19.821  41.733  1.00 25.74  ? 103 VAL E CB  1 
ATOM   5287  C  CG1 . VAL C  1 104 ? -73.480  19.124  41.351  1.00 25.13  ? 103 VAL E CG1 1 
ATOM   5288  C  CG2 . VAL C  1 104 ? -74.804  21.227  41.138  1.00 27.46  ? 103 VAL E CG2 1 
ATOM   5289  N  N   . ILE C  1 105 ? -76.273  17.359  43.095  1.00 23.34  ? 104 ILE E N   1 
ATOM   5290  C  CA  . ILE C  1 105 ? -76.436  15.993  43.611  1.00 21.56  ? 104 ILE E CA  1 
ATOM   5291  C  C   . ILE C  1 105 ? -77.628  15.340  42.903  1.00 21.61  ? 104 ILE E C   1 
ATOM   5292  O  O   . ILE C  1 105 ? -78.503  16.021  42.392  1.00 22.15  ? 104 ILE E O   1 
ATOM   5293  C  CB  . ILE C  1 105 ? -76.609  15.952  45.136  1.00 21.15  ? 104 ILE E CB  1 
ATOM   5294  C  CG1 . ILE C  1 105 ? -77.844  16.728  45.606  1.00 21.20  ? 104 ILE E CG1 1 
ATOM   5295  C  CG2 . ILE C  1 105 ? -75.335  16.423  45.818  1.00 23.13  ? 104 ILE E CG2 1 
ATOM   5296  C  CD1 . ILE C  1 105 ? -78.204  16.477  47.055  1.00 21.71  ? 104 ILE E CD1 1 
ATOM   5297  N  N   . SER C  1 106 ? -77.641  14.000  42.908  1.00 21.07  ? 105 SER E N   1 
ATOM   5298  C  CA  . SER C  1 106 ? -78.745  13.204  42.417  1.00 20.41  ? 105 SER E CA  1 
ATOM   5299  C  C   . SER C  1 106 ? -78.892  11.979  43.318  1.00 20.25  ? 105 SER E C   1 
ATOM   5300  O  O   . SER C  1 106 ? -77.965  11.662  44.065  1.00 20.04  ? 105 SER E O   1 
ATOM   5301  C  CB  . SER C  1 106 ? -78.531  12.790  40.960  1.00 20.67  ? 105 SER E CB  1 
ATOM   5302  O  OG  . SER C  1 106 ? -79.726  12.242  40.415  1.00 20.84  ? 105 SER E OG  1 
ATOM   5303  N  N   . LEU C  1 107 ? -80.043  11.307  43.229  1.00 20.21  ? 106 LEU E N   1 
ATOM   5304  C  CA  . LEU C  1 107 ? -80.289  10.033  43.913  1.00 20.91  ? 106 LEU E CA  1 
ATOM   5305  C  C   . LEU C  1 107 ? -80.200  8.843   42.938  1.00 23.21  ? 106 LEU E C   1 
ATOM   5306  O  O   . LEU C  1 107 ? -80.531  7.716   43.303  1.00 22.38  ? 106 LEU E O   1 
ATOM   5307  C  CB  . LEU C  1 107 ? -81.668  10.084  44.564  1.00 20.86  ? 106 LEU E CB  1 
ATOM   5308  C  CG  . LEU C  1 107 ? -81.843  11.170  45.628  1.00 21.25  ? 106 LEU E CG  1 
ATOM   5309  C  CD1 . LEU C  1 107 ? -83.162  11.041  46.351  1.00 22.24  ? 106 LEU E CD1 1 
ATOM   5310  C  CD2 . LEU C  1 107 ? -80.710  11.173  46.609  1.00 20.44  ? 106 LEU E CD2 1 
ATOM   5311  N  N   . SER C  1 108 ? -79.711  9.099   41.726  1.00 23.63  ? 107 SER E N   1 
ATOM   5312  C  CA  . SER C  1 108 ? -79.519  8.098   40.677  1.00 24.56  ? 107 SER E CA  1 
ATOM   5313  C  C   . SER C  1 108 ? -78.480  8.621   39.693  1.00 22.65  ? 107 SER E C   1 
ATOM   5314  O  O   . SER C  1 108 ? -78.221  9.821   39.666  1.00 22.21  ? 107 SER E O   1 
ATOM   5315  C  CB  . SER C  1 108 ? -80.826  7.768   39.973  1.00 26.62  ? 107 SER E CB  1 
ATOM   5316  O  OG  . SER C  1 108 ? -81.313  8.878   39.221  1.00 26.56  ? 107 SER E OG  1 
ATOM   5317  N  N   . GLY C  1 109 ? -77.875  7.697   38.933  1.00 22.16  ? 108 GLY E N   1 
ATOM   5318  C  CA  . GLY C  1 109 ? -76.917  7.972   37.891  1.00 23.90  ? 108 GLY E CA  1 
ATOM   5319  C  C   . GLY C  1 109 ? -75.580  8.496   38.387  1.00 26.68  ? 108 GLY E C   1 
ATOM   5320  O  O   . GLY C  1 109 ? -75.146  8.256   39.508  1.00 24.48  ? 108 GLY E O   1 
ATOM   5321  N  N   . ASP C  1 110 ? -74.926  9.265   37.513  1.00 26.94  ? 109 ASP E N   1 
ATOM   5322  C  CA  . ASP C  1 110 ? -73.538  9.702   37.677  1.00 27.76  ? 109 ASP E CA  1 
ATOM   5323  C  C   . ASP C  1 110 ? -73.292  10.400  39.026  1.00 25.46  ? 109 ASP E C   1 
ATOM   5324  O  O   . ASP C  1 110 ? -72.286  10.186  39.675  1.00 25.97  ? 109 ASP E O   1 
ATOM   5325  C  CB  . ASP C  1 110 ? -73.163  10.693  36.582  1.00 30.74  ? 109 ASP E CB  1 
ATOM   5326  C  CG  . ASP C  1 110 ? -73.542  10.240  35.181  1.00 38.11  ? 109 ASP E CG  1 
ATOM   5327  O  OD1 . ASP C  1 110 ? -74.810  10.070  34.901  1.00 33.07  ? 109 ASP E OD1 1 
ATOM   5328  O  OD2 . ASP C  1 110 ? -72.577  10.037  34.381  1.00 38.97  ? 109 ASP E OD2 1 
ATOM   5329  N  N   . HIS C  1 111 ? -74.189  11.308  39.393  1.00 24.42  ? 110 HIS E N   1 
ATOM   5330  C  CA  . HIS C  1 111 ? -74.021  12.131  40.590  1.00 24.72  ? 110 HIS E CA  1 
ATOM   5331  C  C   . HIS C  1 111 ? -74.790  11.551  41.785  1.00 21.79  ? 110 HIS E C   1 
ATOM   5332  O  O   . HIS C  1 111 ? -75.009  12.280  42.780  1.00 21.51  ? 110 HIS E O   1 
ATOM   5333  C  CB  . HIS C  1 111 ? -74.457  13.565  40.295  1.00 24.27  ? 110 HIS E CB  1 
ATOM   5334  C  CG  . HIS C  1 111 ? -73.492  14.287  39.425  1.00 28.40  ? 110 HIS E CG  1 
ATOM   5335  N  ND1 . HIS C  1 111 ? -73.621  15.639  39.149  1.00 30.73  ? 110 HIS E ND1 1 
ATOM   5336  C  CD2 . HIS C  1 111 ? -72.374  13.870  38.800  1.00 29.56  ? 110 HIS E CD2 1 
ATOM   5337  C  CE1 . HIS C  1 111 ? -72.619  16.012  38.377  1.00 31.69  ? 110 HIS E CE1 1 
ATOM   5338  N  NE2 . HIS C  1 111 ? -71.848  14.944  38.132  1.00 29.59  ? 110 HIS E NE2 1 
ATOM   5339  N  N   . SER C  1 112 ? -75.194  10.271  41.697  1.00 22.23  ? 111 SER E N   1 
ATOM   5340  C  CA  . SER C  1 112 ? -75.926  9.601   42.782  1.00 21.04  ? 111 SER E CA  1 
ATOM   5341  C  C   . SER C  1 112 ? -75.092  9.651   44.065  1.00 20.36  ? 111 SER E C   1 
ATOM   5342  O  O   . SER C  1 112 ? -73.911  9.295   44.075  1.00 19.84  ? 111 SER E O   1 
ATOM   5343  C  CB  . SER C  1 112 ? -76.242  8.155   42.484  1.00 22.30  ? 111 SER E CB  1 
ATOM   5344  O  OG  . SER C  1 112 ? -76.888  7.559   43.613  1.00 21.25  ? 111 SER E OG  1 
ATOM   5345  N  N   . ILE C  1 113 ? -75.743  10.042  45.151  1.00 20.36  ? 112 ILE E N   1 
ATOM   5346  C  CA  . ILE C  1 113 ? -75.105  10.045  46.458  1.00 21.44  ? 112 ILE E CA  1 
ATOM   5347  C  C   . ILE C  1 113 ? -75.529  8.801   47.263  1.00 20.64  ? 112 ILE E C   1 
ATOM   5348  O  O   . ILE C  1 113 ? -75.155  8.689   48.403  1.00 20.12  ? 112 ILE E O   1 
ATOM   5349  C  CB  . ILE C  1 113 ? -75.421  11.355  47.201  1.00 20.99  ? 112 ILE E CB  1 
ATOM   5350  C  CG1 . ILE C  1 113 ? -76.918  11.532  47.448  1.00 21.46  ? 112 ILE E CG1 1 
ATOM   5351  C  CG2 . ILE C  1 113 ? -74.811  12.547  46.476  1.00 23.00  ? 112 ILE E CG2 1 
ATOM   5352  C  CD1 . ILE C  1 113 ? -77.283  12.735  48.275  1.00 21.54  ? 112 ILE E CD1 1 
ATOM   5353  N  N   . ILE C  1 114 ? -76.332  7.901   46.679  1.00 20.21  ? 113 ILE E N   1 
ATOM   5354  C  CA  . ILE C  1 114 ? -76.751  6.688   47.373  1.00 19.92  ? 113 ILE E CA  1 
ATOM   5355  C  C   . ILE C  1 114 ? -75.497  5.859   47.661  1.00 19.32  ? 113 ILE E C   1 
ATOM   5356  O  O   . ILE C  1 114 ? -74.671  5.680   46.812  1.00 17.82  ? 113 ILE E O   1 
ATOM   5357  C  CB  . ILE C  1 114 ? -77.775  5.884   46.546  1.00 21.67  ? 113 ILE E CB  1 
ATOM   5358  C  CG1 . ILE C  1 114 ? -79.009  6.702   46.164  1.00 24.60  ? 113 ILE E CG1 1 
ATOM   5359  C  CG2 . ILE C  1 114 ? -78.166  4.600   47.258  1.00 20.06  ? 113 ILE E CG2 1 
ATOM   5360  C  CD1 . ILE C  1 114 ? -79.860  7.135   47.326  1.00 23.75  ? 113 ILE E CD1 1 
ATOM   5361  N  N   . GLY C  1 115 ? -75.337  5.407   48.904  1.00 19.41  ? 114 GLY E N   1 
ATOM   5362  C  CA  . GLY C  1 115 ? -74.175  4.615   49.279  1.00 19.51  ? 114 GLY E CA  1 
ATOM   5363  C  C   . GLY C  1 115 ? -72.958  5.440   49.638  1.00 19.21  ? 114 GLY E C   1 
ATOM   5364  O  O   . GLY C  1 115 ? -71.931  4.860   49.931  1.00 18.84  ? 114 GLY E O   1 
ATOM   5365  N  N   . ARG C  1 116 ? -73.064  6.783   49.603  1.00 18.56  ? 115 ARG E N   1 
ATOM   5366  C  CA  . ARG C  1 116 ? -71.983  7.644   50.006  1.00 19.23  ? 115 ARG E CA  1 
ATOM   5367  C  C   . ARG C  1 116 ? -72.265  8.099   51.445  1.00 20.54  ? 115 ARG E C   1 
ATOM   5368  O  O   . ARG C  1 116 ? -73.216  7.619   52.044  1.00 21.43  ? 115 ARG E O   1 
ATOM   5369  C  CB  . ARG C  1 116 ? -71.840  8.766   48.985  1.00 19.27  ? 115 ARG E CB  1 
ATOM   5370  C  CG  . ARG C  1 116 ? -71.737  8.207   47.570  1.00 21.39  ? 115 ARG E CG  1 
ATOM   5371  C  CD  . ARG C  1 116 ? -71.037  9.105   46.595  1.00 21.46  ? 115 ARG E CD  1 
ATOM   5372  N  NE  . ARG C  1 116 ? -71.059  8.512   45.260  1.00 21.50  ? 115 ARG E NE  1 
ATOM   5373  C  CZ  . ARG C  1 116 ? -70.071  7.826   44.703  1.00 23.00  ? 115 ARG E CZ  1 
ATOM   5374  N  NH1 . ARG C  1 116 ? -70.185  7.444   43.430  1.00 22.24  ? 115 ARG E NH1 1 
ATOM   5375  N  NH2 . ARG C  1 116 ? -68.963  7.589   45.380  1.00 20.37  ? 115 ARG E NH2 1 
ATOM   5376  N  N   . THR C  1 117 ? -71.406  8.953   52.007  1.00 22.01  ? 116 THR E N   1 
ATOM   5377  C  CA  . THR C  1 117 ? -71.537  9.372   53.416  1.00 21.59  ? 116 THR E CA  1 
ATOM   5378  C  C   . THR C  1 117 ? -71.860  10.858  53.481  1.00 21.82  ? 116 THR E C   1 
ATOM   5379  O  O   . THR C  1 117 ? -71.175  11.672  52.858  1.00 22.35  ? 116 THR E O   1 
ATOM   5380  C  CB  . THR C  1 117 ? -70.264  9.086   54.223  1.00 22.83  ? 116 THR E CB  1 
ATOM   5381  O  OG1 . THR C  1 117 ? -70.076  7.678   54.289  1.00 22.07  ? 116 THR E OG1 1 
ATOM   5382  C  CG2 . THR C  1 117 ? -70.309  9.580   55.655  1.00 23.30  ? 116 THR E CG2 1 
ATOM   5383  N  N   . LEU C  1 118 ? -72.897  11.202  54.244  1.00 20.61  ? 117 LEU E N   1 
ATOM   5384  C  CA  . LEU C  1 118 ? -73.168  12.579  54.609  1.00 21.19  ? 117 LEU E CA  1 
ATOM   5385  C  C   . LEU C  1 118 ? -72.390  12.887  55.892  1.00 21.47  ? 117 LEU E C   1 
ATOM   5386  O  O   . LEU C  1 118 ? -72.442  12.102  56.815  1.00 20.79  ? 117 LEU E O   1 
ATOM   5387  C  CB  . LEU C  1 118 ? -74.670  12.729  54.820  1.00 22.17  ? 117 LEU E CB  1 
ATOM   5388  C  CG  . LEU C  1 118 ? -75.172  14.146  55.035  1.00 23.51  ? 117 LEU E CG  1 
ATOM   5389  C  CD1 . LEU C  1 118 ? -74.887  15.045  53.828  1.00 24.26  ? 117 LEU E CD1 1 
ATOM   5390  C  CD2 . LEU C  1 118 ? -76.659  14.121  55.350  1.00 24.84  ? 117 LEU E CD2 1 
ATOM   5391  N  N   . VAL C  1 119 ? -71.701  14.031  55.938  1.00 20.54  ? 118 VAL E N   1 
ATOM   5392  C  CA  . VAL C  1 119 ? -70.854  14.423  57.071  1.00 23.33  ? 118 VAL E CA  1 
ATOM   5393  C  C   . VAL C  1 119 ? -71.246  15.831  57.536  1.00 22.51  ? 118 VAL E C   1 
ATOM   5394  O  O   . VAL C  1 119 ? -71.453  16.741  56.707  1.00 22.69  ? 118 VAL E O   1 
ATOM   5395  C  CB  . VAL C  1 119 ? -69.368  14.415  56.671  1.00 25.32  ? 118 VAL E CB  1 
ATOM   5396  C  CG1 . VAL C  1 119 ? -68.467  14.910  57.800  1.00 25.71  ? 118 VAL E CG1 1 
ATOM   5397  C  CG2 . VAL C  1 119 ? -68.931  13.052  56.176  1.00 25.09  ? 118 VAL E CG2 1 
ATOM   5398  N  N   . VAL C  1 120 ? -71.323  16.015  58.855  1.00 21.41  ? 119 VAL E N   1 
ATOM   5399  C  CA  . VAL C  1 120 ? -71.418  17.341  59.426  1.00 22.37  ? 119 VAL E CA  1 
ATOM   5400  C  C   . VAL C  1 120 ? -70.133  17.626  60.218  1.00 23.45  ? 119 VAL E C   1 
ATOM   5401  O  O   . VAL C  1 120 ? -69.645  16.791  60.997  1.00 22.82  ? 119 VAL E O   1 
ATOM   5402  C  CB  . VAL C  1 120 ? -72.706  17.535  60.247  1.00 23.15  ? 119 VAL E CB  1 
ATOM   5403  C  CG1 . VAL C  1 120 ? -72.800  16.596  61.429  1.00 23.64  ? 119 VAL E CG1 1 
ATOM   5404  C  CG2 . VAL C  1 120 ? -72.855  18.986  60.695  1.00 23.22  ? 119 VAL E CG2 1 
ATOM   5405  N  N   . HIS C  1 121 ? -69.594  18.830  60.009  1.00 24.15  ? 120 HIS E N   1 
ATOM   5406  C  CA  . HIS C  1 121 ? -68.243  19.189  60.396  1.00 24.42  ? 120 HIS E CA  1 
ATOM   5407  C  C   . HIS C  1 121 ? -68.238  20.086  61.641  1.00 26.56  ? 120 HIS E C   1 
ATOM   5408  O  O   . HIS C  1 121 ? -69.229  20.689  62.010  1.00 28.92  ? 120 HIS E O   1 
ATOM   5409  C  CB  . HIS C  1 121 ? -67.533  19.882  59.252  1.00 23.95  ? 120 HIS E CB  1 
ATOM   5410  C  CG  . HIS C  1 121 ? -67.005  18.959  58.221  1.00 24.78  ? 120 HIS E CG  1 
ATOM   5411  N  ND1 . HIS C  1 121 ? -65.770  18.381  58.340  1.00 25.06  ? 120 HIS E ND1 1 
ATOM   5412  C  CD2 . HIS C  1 121 ? -67.530  18.506  57.061  1.00 26.09  ? 120 HIS E CD2 1 
ATOM   5413  C  CE1 . HIS C  1 121 ? -65.529  17.634  57.282  1.00 24.54  ? 120 HIS E CE1 1 
ATOM   5414  N  NE2 . HIS C  1 121 ? -66.584  17.704  56.470  1.00 25.96  ? 120 HIS E NE2 1 
ATOM   5415  N  N   . GLU C  1 122 ? -67.056  20.165  62.248  1.00 29.33  ? 121 GLU E N   1 
ATOM   5416  C  CA  . GLU C  1 122 ? -66.802  20.917  63.476  1.00 31.25  ? 121 GLU E CA  1 
ATOM   5417  C  C   . GLU C  1 122 ? -67.008  22.415  63.226  1.00 31.42  ? 121 GLU E C   1 
ATOM   5418  O  O   . GLU C  1 122 ? -67.653  23.062  64.026  1.00 34.30  ? 121 GLU E O   1 
ATOM   5419  C  CB  . GLU C  1 122 ? -65.391  20.554  63.935  1.00 38.31  ? 121 GLU E CB  1 
ATOM   5420  C  CG  . GLU C  1 122 ? -64.813  21.416  65.041  1.00 43.21  ? 121 GLU E CG  1 
ATOM   5421  C  CD  . GLU C  1 122 ? -63.297  21.295  65.172  1.00 48.58  ? 121 GLU E CD  1 
ATOM   5422  O  OE1 . GLU C  1 122 ? -62.802  21.533  66.290  1.00 56.43  ? 121 GLU E OE1 1 
ATOM   5423  O  OE2 . GLU C  1 122 ? -62.601  20.996  64.144  1.00 45.42  ? 121 GLU E OE2 1 
ATOM   5424  N  N   . LYS C  1 123 ? -66.517  22.928  62.092  1.00 31.13  ? 122 LYS E N   1 
ATOM   5425  C  CA  . LYS C  1 123 ? -66.460  24.372  61.833  1.00 37.37  ? 122 LYS E CA  1 
ATOM   5426  C  C   . LYS C  1 123 ? -67.236  24.737  60.562  1.00 36.00  ? 122 LYS E C   1 
ATOM   5427  O  O   . LYS C  1 123 ? -67.690  23.876  59.805  1.00 29.12  ? 122 LYS E O   1 
ATOM   5428  C  CB  . LYS C  1 123 ? -65.020  24.846  61.587  1.00 40.49  ? 122 LYS E CB  1 
ATOM   5429  C  CG  . LYS C  1 123 ? -63.974  24.528  62.648  1.00 47.89  ? 122 LYS E CG  1 
ATOM   5430  C  CD  . LYS C  1 123 ? -62.558  24.675  62.092  1.00 54.53  ? 122 LYS E CD  1 
ATOM   5431  C  CE  . LYS C  1 123 ? -61.550  25.202  63.090  1.00 63.77  ? 122 LYS E CE  1 
ATOM   5432  N  NZ  . LYS C  1 123 ? -61.252  24.201  64.143  1.00 68.89  ? 122 LYS E NZ  1 
ATOM   5433  N  N   . ALA C  1 124 ? -67.327  26.049  60.321  1.00 35.15  ? 123 ALA E N   1 
ATOM   5434  C  CA  . ALA C  1 124 ? -67.975  26.580  59.163  1.00 35.79  ? 123 ALA E CA  1 
ATOM   5435  C  C   . ALA C  1 124 ? -67.168  26.179  57.927  1.00 35.02  ? 123 ALA E C   1 
ATOM   5436  O  O   . ALA C  1 124 ? -65.954  26.038  57.971  1.00 34.31  ? 123 ALA E O   1 
ATOM   5437  C  CB  . ALA C  1 124 ? -68.122  28.083  59.275  1.00 36.90  ? 123 ALA E CB  1 
ATOM   5438  N  N   . ASP C  1 125 ? -67.897  25.932  56.839  1.00 33.83  ? 124 ASP E N   1 
ATOM   5439  C  CA  . ASP C  1 125 ? -67.344  25.814  55.521  1.00 33.96  ? 124 ASP E CA  1 
ATOM   5440  C  C   . ASP C  1 125 ? -67.224  27.243  54.963  1.00 32.71  ? 124 ASP E C   1 
ATOM   5441  O  O   . ASP C  1 125 ? -68.224  27.962  54.918  1.00 33.79  ? 124 ASP E O   1 
ATOM   5442  C  CB  . ASP C  1 125 ? -68.269  24.925  54.696  1.00 33.86  ? 124 ASP E CB  1 
ATOM   5443  C  CG  . ASP C  1 125 ? -67.814  24.664  53.280  1.00 37.81  ? 124 ASP E CG  1 
ATOM   5444  O  OD1 . ASP C  1 125 ? -66.921  25.406  52.795  1.00 38.54  ? 124 ASP E OD1 1 
ATOM   5445  O  OD2 . ASP C  1 125 ? -68.351  23.708  52.673  1.00 37.76  ? 124 ASP E OD2 1 
ATOM   5446  N  N   . ASP C  1 126 ? -66.014  27.630  54.558  1.00 33.48  ? 125 ASP E N   1 
ATOM   5447  C  CA  . ASP C  1 126 ? -65.734  28.982  54.028  1.00 39.43  ? 125 ASP E CA  1 
ATOM   5448  C  C   . ASP C  1 126 ? -66.067  29.066  52.529  1.00 40.25  ? 125 ASP E C   1 
ATOM   5449  O  O   . ASP C  1 126 ? -65.765  30.079  51.888  1.00 40.11  ? 125 ASP E O   1 
ATOM   5450  C  CB  . ASP C  1 126 ? -64.287  29.398  54.316  1.00 39.87  ? 125 ASP E CB  1 
ATOM   5451  C  CG  . ASP C  1 126 ? -63.221  28.605  53.576  1.00 41.49  ? 125 ASP E CG  1 
ATOM   5452  O  OD1 . ASP C  1 126 ? -62.078  28.549  54.089  1.00 45.02  ? 125 ASP E OD1 1 
ATOM   5453  O  OD2 . ASP C  1 126 ? -63.533  28.027  52.512  1.00 41.17  ? 125 ASP E OD2 1 
ATOM   5454  N  N   . LEU C  1 127 ? -66.666  27.997  51.983  1.00 36.77  ? 126 LEU E N   1 
ATOM   5455  C  CA  . LEU C  1 127 ? -67.237  27.941  50.655  1.00 36.18  ? 126 LEU E CA  1 
ATOM   5456  C  C   . LEU C  1 127 ? -66.140  28.100  49.591  1.00 39.25  ? 126 LEU E C   1 
ATOM   5457  O  O   . LEU C  1 127 ? -66.415  28.531  48.464  1.00 38.75  ? 126 LEU E O   1 
ATOM   5458  C  CB  . LEU C  1 127 ? -68.329  29.008  50.516  1.00 36.74  ? 126 LEU E CB  1 
ATOM   5459  C  CG  . LEU C  1 127 ? -69.390  29.010  51.613  1.00 36.99  ? 126 LEU E CG  1 
ATOM   5460  C  CD1 . LEU C  1 127 ? -70.431  30.092  51.367  1.00 37.69  ? 126 LEU E CD1 1 
ATOM   5461  C  CD2 . LEU C  1 127 ? -70.064  27.648  51.730  1.00 39.01  ? 126 LEU E CD2 1 
ATOM   5462  N  N   . GLY C  1 128 ? -64.917  27.678  49.929  1.00 39.89  ? 127 GLY E N   1 
ATOM   5463  C  CA  . GLY C  1 128 ? -63.800  27.661  48.990  1.00 43.68  ? 127 GLY E CA  1 
ATOM   5464  C  C   . GLY C  1 128 ? -63.160  29.038  48.806  1.00 51.94  ? 127 GLY E C   1 
ATOM   5465  O  O   . GLY C  1 128 ? -62.288  29.177  47.951  1.00 52.50  ? 127 GLY E O   1 
ATOM   5466  N  N   . LYS C  1 129 ? -63.565  30.021  49.634  1.00 52.04  ? 128 LYS E N   1 
ATOM   5467  C  CA  . LYS C  1 129 ? -63.225  31.461  49.506  1.00 57.82  ? 128 LYS E CA  1 
ATOM   5468  C  C   . LYS C  1 129 ? -62.299  31.886  50.663  1.00 60.51  ? 128 LYS E C   1 
ATOM   5469  O  O   . LYS C  1 129 ? -62.280  33.057  51.044  1.00 57.81  ? 128 LYS E O   1 
ATOM   5470  C  CB  . LYS C  1 129 ? -64.506  32.314  49.527  1.00 60.83  ? 128 LYS E CB  1 
ATOM   5471  C  CG  . LYS C  1 129 ? -65.166  32.636  48.187  1.00 63.83  ? 128 LYS E CG  1 
ATOM   5472  C  CD  . LYS C  1 129 ? -65.365  31.450  47.259  1.00 67.11  ? 128 LYS E CD  1 
ATOM   5473  C  CE  . LYS C  1 129 ? -66.689  31.464  46.514  1.00 70.11  ? 128 LYS E CE  1 
ATOM   5474  N  NZ  . LYS C  1 129 ? -67.739  30.707  47.245  1.00 65.38  ? 128 LYS E NZ  1 
ATOM   5475  N  N   . GLY C  1 130 ? -61.546  30.928  51.226  1.00 62.67  ? 129 GLY E N   1 
ATOM   5476  C  CA  . GLY C  1 130 ? -60.669  31.150  52.386  1.00 66.35  ? 129 GLY E CA  1 
ATOM   5477  C  C   . GLY C  1 130 ? -59.273  31.604  51.982  1.00 70.17  ? 129 GLY E C   1 
ATOM   5478  O  O   . GLY C  1 130 ? -58.543  32.153  52.796  1.00 71.81  ? 129 GLY E O   1 
ATOM   5479  N  N   . GLY C  1 131 ? -58.896  31.331  50.729  1.00 72.64  ? 130 GLY E N   1 
ATOM   5480  C  CA  . GLY C  1 131 ? -57.650  31.810  50.138  1.00 75.88  ? 130 GLY E CA  1 
ATOM   5481  C  C   . GLY C  1 131 ? -56.426  31.035  50.606  1.00 75.39  ? 130 GLY E C   1 
ATOM   5482  O  O   . GLY C  1 131 ? -55.332  31.583  50.651  1.00 79.31  ? 130 GLY E O   1 
ATOM   5483  N  N   . ASN C  1 132 ? -56.613  29.759  50.956  1.00 76.04  ? 131 ASN E N   1 
ATOM   5484  C  CA  . ASN C  1 132 ? -55.509  28.816  51.180  1.00 72.02  ? 131 ASN E CA  1 
ATOM   5485  C  C   . ASN C  1 132 ? -55.868  27.487  50.498  1.00 73.95  ? 131 ASN E C   1 
ATOM   5486  O  O   . ASN C  1 132 ? -57.009  27.288  50.052  1.00 72.64  ? 131 ASN E O   1 
ATOM   5487  C  CB  . ASN C  1 132 ? -55.186  28.660  52.670  1.00 70.66  ? 131 ASN E CB  1 
ATOM   5488  C  CG  . ASN C  1 132 ? -56.403  28.346  53.515  1.00 70.52  ? 131 ASN E CG  1 
ATOM   5489  O  OD1 . ASN C  1 132 ? -57.033  27.309  53.340  1.00 63.49  ? 131 ASN E OD1 1 
ATOM   5490  N  ND2 . ASN C  1 132 ? -56.750  29.241  54.426  1.00 71.12  ? 131 ASN E ND2 1 
ATOM   5491  N  N   . GLU C  1 133 ? -54.889  26.583  50.419  1.00 69.15  ? 132 GLU E N   1 
ATOM   5492  C  CA  . GLU C  1 133 ? -55.045  25.311  49.731  1.00 68.40  ? 132 GLU E CA  1 
ATOM   5493  C  C   . GLU C  1 133 ? -56.164  24.477  50.376  1.00 67.67  ? 132 GLU E C   1 
ATOM   5494  O  O   . GLU C  1 133 ? -56.959  23.838  49.671  1.00 60.95  ? 132 GLU E O   1 
ATOM   5495  C  CB  . GLU C  1 133 ? -53.724  24.549  49.752  1.00 75.06  ? 132 GLU E CB  1 
ATOM   5496  C  CG  . GLU C  1 133 ? -53.825  23.161  49.152  1.00 79.32  ? 132 GLU E CG  1 
ATOM   5497  C  CD  . GLU C  1 133 ? -52.573  22.727  48.417  1.00 85.00  ? 132 GLU E CD  1 
ATOM   5498  O  OE1 . GLU C  1 133 ? -52.444  23.078  47.231  1.00 90.66  ? 132 GLU E OE1 1 
ATOM   5499  O  OE2 . GLU C  1 133 ? -51.727  22.060  49.039  1.00 91.44  ? 132 GLU E OE2 1 
ATOM   5500  N  N   . GLU C  1 134 ? -56.215  24.472  51.714  1.00 64.39  ? 133 GLU E N   1 
ATOM   5501  C  CA  . GLU C  1 134 ? -57.229  23.715  52.466  1.00 60.70  ? 133 GLU E CA  1 
ATOM   5502  C  C   . GLU C  1 134 ? -58.650  24.168  52.083  1.00 53.63  ? 133 GLU E C   1 
ATOM   5503  O  O   . GLU C  1 134 ? -59.548  23.322  51.949  1.00 46.18  ? 133 GLU E O   1 
ATOM   5504  C  CB  . GLU C  1 134 ? -57.040  23.876  53.977  1.00 60.00  ? 133 GLU E CB  1 
ATOM   5505  C  CG  . GLU C  1 134 ? -57.838  22.868  54.782  1.00 59.33  ? 133 GLU E CG  1 
ATOM   5506  C  CD  . GLU C  1 134 ? -57.632  21.431  54.326  1.00 64.64  ? 133 GLU E CD  1 
ATOM   5507  O  OE1 . GLU C  1 134 ? -56.459  21.010  54.191  1.00 66.45  ? 133 GLU E OE1 1 
ATOM   5508  O  OE2 . GLU C  1 134 ? -58.641  20.745  54.069  1.00 64.57  ? 133 GLU E OE2 1 
ATOM   5509  N  N   . SER C  1 135 ? -58.852  25.487  51.923  1.00 47.00  ? 134 SER E N   1 
ATOM   5510  C  CA  . SER C  1 135 ? -60.165  26.053  51.556  1.00 48.92  ? 134 SER E CA  1 
ATOM   5511  C  C   . SER C  1 135 ? -60.705  25.400  50.275  1.00 50.80  ? 134 SER E C   1 
ATOM   5512  O  O   . SER C  1 135 ? -61.911  25.143  50.189  1.00 43.64  ? 134 SER E O   1 
ATOM   5513  C  CB  . SER C  1 135 ? -60.119  27.548  51.390  1.00 49.28  ? 134 SER E CB  1 
ATOM   5514  O  OG  . SER C  1 135 ? -61.403  28.051  51.036  1.00 46.36  ? 134 SER E OG  1 
ATOM   5515  N  N   . THR C  1 136 ? -59.810  25.151  49.303  1.00 48.22  ? 135 THR E N   1 
ATOM   5516  C  CA  . THR C  1 136 ? -60.172  24.646  47.977  1.00 54.41  ? 135 THR E CA  1 
ATOM   5517  C  C   . THR C  1 136 ? -60.411  23.126  48.029  1.00 54.58  ? 135 THR E C   1 
ATOM   5518  O  O   . THR C  1 136 ? -60.814  22.544  47.015  1.00 50.34  ? 135 THR E O   1 
ATOM   5519  C  CB  . THR C  1 136 ? -59.108  24.968  46.910  1.00 55.44  ? 135 THR E CB  1 
ATOM   5520  O  OG1 . THR C  1 136 ? -57.948  24.172  47.164  1.00 57.57  ? 135 THR E OG1 1 
ATOM   5521  C  CG2 . THR C  1 136 ? -58.719  26.429  46.853  1.00 53.42  ? 135 THR E CG2 1 
ATOM   5522  N  N   . LYS C  1 137 ? -60.158  22.491  49.190  1.00 55.68  ? 136 LYS E N   1 
ATOM   5523  C  CA  . LYS C  1 137 ? -60.368  21.044  49.357  1.00 56.46  ? 136 LYS E CA  1 
ATOM   5524  C  C   . LYS C  1 137 ? -61.525  20.744  50.330  1.00 49.19  ? 136 LYS E C   1 
ATOM   5525  O  O   . LYS C  1 137 ? -62.345  19.876  50.028  1.00 43.71  ? 136 LYS E O   1 
ATOM   5526  C  CB  . LYS C  1 137 ? -59.051  20.366  49.750  1.00 63.68  ? 136 LYS E CB  1 
ATOM   5527  C  CG  . LYS C  1 137 ? -58.250  19.854  48.557  1.00 72.89  ? 136 LYS E CG  1 
ATOM   5528  C  CD  . LYS C  1 137 ? -56.905  19.247  48.900  1.00 78.55  ? 136 LYS E CD  1 
ATOM   5529  C  CE  . LYS C  1 137 ? -55.813  20.281  49.079  1.00 85.14  ? 136 LYS E CE  1 
ATOM   5530  N  NZ  . LYS C  1 137 ? -54.482  19.724  48.738  1.00 88.78  ? 136 LYS E NZ  1 
ATOM   5531  N  N   . THR C  1 138 ? -61.570  21.422  51.490  1.00 46.43  ? 137 THR E N   1 
ATOM   5532  C  CA  . THR C  1 138 ? -62.531  21.096  52.565  1.00 42.18  ? 137 THR E CA  1 
ATOM   5533  C  C   . THR C  1 138 ? -63.300  22.319  53.069  1.00 42.40  ? 137 THR E C   1 
ATOM   5534  O  O   . THR C  1 138 ? -64.163  22.175  53.929  1.00 42.52  ? 137 THR E O   1 
ATOM   5535  C  CB  . THR C  1 138 ? -61.832  20.492  53.786  1.00 44.47  ? 137 THR E CB  1 
ATOM   5536  O  OG1 . THR C  1 138 ? -61.018  21.530  54.339  1.00 45.16  ? 137 THR E OG1 1 
ATOM   5537  C  CG2 . THR C  1 138 ? -61.039  19.246  53.445  1.00 44.37  ? 137 THR E CG2 1 
ATOM   5538  N  N   . GLY C  1 139 ? -62.976  23.516  52.563  1.00 41.67  ? 138 GLY E N   1 
ATOM   5539  C  CA  . GLY C  1 139 ? -63.610  24.739  53.033  1.00 40.14  ? 138 GLY E CA  1 
ATOM   5540  C  C   . GLY C  1 139 ? -63.201  25.102  54.461  1.00 42.35  ? 138 GLY E C   1 
ATOM   5541  O  O   . GLY C  1 139 ? -63.854  25.946  55.079  1.00 41.37  ? 138 GLY E O   1 
ATOM   5542  N  N   . ASN C  1 140 ? -62.136  24.462  54.975  1.00 39.72  ? 139 ASN E N   1 
ATOM   5543  C  CA  . ASN C  1 140 ? -61.621  24.648  56.354  1.00 41.40  ? 139 ASN E CA  1 
ATOM   5544  C  C   . ASN C  1 140 ? -62.686  24.251  57.392  1.00 38.28  ? 139 ASN E C   1 
ATOM   5545  O  O   . ASN C  1 140 ? -62.772  24.853  58.467  1.00 39.49  ? 139 ASN E O   1 
ATOM   5546  C  CB  . ASN C  1 140 ? -61.070  26.072  56.549  1.00 42.35  ? 139 ASN E CB  1 
ATOM   5547  C  CG  . ASN C  1 140 ? -59.759  26.278  55.814  1.00 46.12  ? 139 ASN E CG  1 
ATOM   5548  O  OD1 . ASN C  1 140 ? -58.770  25.624  56.134  1.00 47.32  ? 139 ASN E OD1 1 
ATOM   5549  N  ND2 . ASN C  1 140 ? -59.748  27.116  54.783  1.00 45.02  ? 139 ASN E ND2 1 
ATOM   5550  N  N   . ALA C  1 141 ? -63.462  23.191  57.103  1.00 38.18  ? 140 ALA E N   1 
ATOM   5551  C  CA  . ALA C  1 141 ? -64.638  22.835  57.920  1.00 33.35  ? 140 ALA E CA  1 
ATOM   5552  C  C   . ALA C  1 141 ? -64.220  21.998  59.138  1.00 32.14  ? 140 ALA E C   1 
ATOM   5553  O  O   . ALA C  1 141 ? -65.030  21.771  60.051  1.00 29.90  ? 140 ALA E O   1 
ATOM   5554  C  CB  . ALA C  1 141 ? -65.659  22.117  57.072  1.00 33.91  ? 140 ALA E CB  1 
ATOM   5555  N  N   . GLY C  1 142 ? -62.967  21.532  59.138  1.00 33.45  ? 141 GLY E N   1 
ATOM   5556  C  CA  . GLY C  1 142 ? -62.381  20.855  60.310  1.00 35.91  ? 141 GLY E CA  1 
ATOM   5557  C  C   . GLY C  1 142 ? -62.886  19.423  60.446  1.00 36.86  ? 141 GLY E C   1 
ATOM   5558  O  O   . GLY C  1 142 ? -63.227  18.780  59.455  1.00 32.40  ? 141 GLY E O   1 
ATOM   5559  N  N   . SER C  1 143 ? -62.934  18.916  61.686  1.00 34.52  ? 142 SER E N   1 
ATOM   5560  C  CA  . SER C  1 143 ? -63.142  17.505  61.909  1.00 34.78  ? 142 SER E CA  1 
ATOM   5561  C  C   . SER C  1 143 ? -64.619  17.122  61.671  1.00 29.91  ? 142 SER E C   1 
ATOM   5562  O  O   . SER C  1 143 ? -65.527  17.943  61.591  1.00 28.18  ? 142 SER E O   1 
ATOM   5563  C  CB  . SER C  1 143 ? -62.621  17.079  63.261  1.00 37.39  ? 142 SER E CB  1 
ATOM   5564  O  OG  . SER C  1 143 ? -63.373  17.649  64.300  1.00 41.58  ? 142 SER E OG  1 
ATOM   5565  N  N   . ARG C  1 144 ? -64.816  15.828  61.519  1.00 28.06  ? 143 ARG E N   1 
ATOM   5566  C  CA  . ARG C  1 144 ? -66.079  15.244  61.160  1.00 28.82  ? 143 ARG E CA  1 
ATOM   5567  C  C   . ARG C  1 144 ? -66.769  14.858  62.467  1.00 28.99  ? 143 ARG E C   1 
ATOM   5568  O  O   . ARG C  1 144 ? -66.332  13.932  63.100  1.00 30.95  ? 143 ARG E O   1 
ATOM   5569  C  CB  . ARG C  1 144 ? -65.807  14.047  60.250  1.00 26.47  ? 143 ARG E CB  1 
ATOM   5570  C  CG  . ARG C  1 144 ? -64.905  14.390  59.069  1.00 28.05  ? 143 ARG E CG  1 
ATOM   5571  C  CD  . ARG C  1 144 ? -64.429  13.200  58.258  1.00 29.42  ? 143 ARG E CD  1 
ATOM   5572  N  NE  . ARG C  1 144 ? -63.680  13.679  57.109  1.00 29.36  ? 143 ARG E NE  1 
ATOM   5573  C  CZ  . ARG C  1 144 ? -63.340  12.965  56.050  1.00 27.74  ? 143 ARG E CZ  1 
ATOM   5574  N  NH1 . ARG C  1 144 ? -62.537  13.513  55.158  1.00 26.64  ? 143 ARG E NH1 1 
ATOM   5575  N  NH2 . ARG C  1 144 ? -63.799  11.733  55.875  1.00 25.18  ? 143 ARG E NH2 1 
ATOM   5576  N  N   . LEU C  1 145 ? -67.831  15.574  62.831  1.00 25.59  ? 144 LEU E N   1 
ATOM   5577  C  CA  . LEU C  1 145 ? -68.531  15.390  64.109  1.00 27.45  ? 144 LEU E CA  1 
ATOM   5578  C  C   . LEU C  1 145 ? -69.448  14.168  64.064  1.00 26.67  ? 144 LEU E C   1 
ATOM   5579  O  O   . LEU C  1 145 ? -69.597  13.465  65.052  1.00 22.83  ? 144 LEU E O   1 
ATOM   5580  C  CB  . LEU C  1 145 ? -69.371  16.629  64.391  1.00 31.28  ? 144 LEU E CB  1 
ATOM   5581  C  CG  . LEU C  1 145 ? -68.758  17.688  65.304  1.00 37.46  ? 144 LEU E CG  1 
ATOM   5582  C  CD1 . LEU C  1 145 ? -67.245  17.690  65.258  1.00 36.11  ? 144 LEU E CD1 1 
ATOM   5583  C  CD2 . LEU C  1 145 ? -69.335  19.046  64.979  1.00 35.84  ? 144 LEU E CD2 1 
ATOM   5584  N  N   . ALA C  1 146 ? -70.132  13.989  62.935  1.00 22.84  ? 145 ALA E N   1 
ATOM   5585  C  CA  . ALA C  1 146 ? -71.028  12.862  62.739  1.00 22.13  ? 145 ALA E CA  1 
ATOM   5586  C  C   . ALA C  1 146 ? -71.184  12.608  61.237  1.00 21.40  ? 145 ALA E C   1 
ATOM   5587  O  O   . ALA C  1 146 ? -70.928  13.489  60.399  1.00 19.98  ? 145 ALA E O   1 
ATOM   5588  C  CB  . ALA C  1 146 ? -72.369  13.121  63.376  1.00 21.80  ? 145 ALA E CB  1 
ATOM   5589  N  N   . CYS C  1 147 ? -71.617  11.393  60.924  1.00 22.25  ? 146 CYS E N   1 
ATOM   5590  C  CA  . CYS C  1 147 ? -71.798  10.966  59.554  1.00 22.40  ? 146 CYS E CA  1 
ATOM   5591  C  C   . CYS C  1 147 ? -72.719  9.748   59.513  1.00 21.56  ? 146 CYS E C   1 
ATOM   5592  O  O   . CYS C  1 147 ? -73.038  9.144   60.538  1.00 20.66  ? 146 CYS E O   1 
ATOM   5593  C  CB  . CYS C  1 147 ? -70.453  10.625  58.926  1.00 25.46  ? 146 CYS E CB  1 
ATOM   5594  S  SG  . CYS C  1 147 ? -69.583  9.291   59.787  1.00 29.05  ? 146 CYS E SG  1 
ATOM   5595  N  N   . GLY C  1 148 ? -73.145  9.401   58.303  1.00 20.35  ? 147 GLY E N   1 
ATOM   5596  C  CA  . GLY C  1 148 ? -73.936  8.219   58.073  1.00 20.19  ? 147 GLY E CA  1 
ATOM   5597  C  C   . GLY C  1 148 ? -73.931  7.901   56.605  1.00 19.98  ? 147 GLY E C   1 
ATOM   5598  O  O   . GLY C  1 148 ? -73.657  8.800   55.797  1.00 18.49  ? 147 GLY E O   1 
ATOM   5599  N  N   . VAL C  1 149 ? -74.236  6.640   56.277  1.00 19.91  ? 148 VAL E N   1 
ATOM   5600  C  CA  . VAL C  1 149 ? -74.349  6.218   54.911  1.00 19.91  ? 148 VAL E CA  1 
ATOM   5601  C  C   . VAL C  1 149 ? -75.750  6.615   54.396  1.00 20.19  ? 148 VAL E C   1 
ATOM   5602  O  O   . VAL C  1 149 ? -76.776  6.418   55.075  1.00 19.19  ? 148 VAL E O   1 
ATOM   5603  C  CB  . VAL C  1 149 ? -74.088  4.713   54.769  1.00 21.43  ? 148 VAL E CB  1 
ATOM   5604  C  CG1 . VAL C  1 149 ? -74.150  4.290   53.314  1.00 20.82  ? 148 VAL E CG1 1 
ATOM   5605  C  CG2 . VAL C  1 149 ? -72.763  4.279   55.408  1.00 21.98  ? 148 VAL E CG2 1 
ATOM   5606  N  N   . ILE C  1 150 ? -75.794  7.113   53.154  1.00 19.38  ? 149 ILE E N   1 
ATOM   5607  C  CA  . ILE C  1 150 ? -77.028  7.579   52.567  1.00 20.52  ? 149 ILE E CA  1 
ATOM   5608  C  C   . ILE C  1 150 ? -77.705  6.364   51.931  1.00 19.95  ? 149 ILE E C   1 
ATOM   5609  O  O   . ILE C  1 150 ? -77.157  5.743   51.034  1.00 21.03  ? 149 ILE E O   1 
ATOM   5610  C  CB  . ILE C  1 150 ? -76.763  8.712   51.565  1.00 21.38  ? 149 ILE E CB  1 
ATOM   5611  C  CG1 . ILE C  1 150 ? -76.094  9.896   52.263  1.00 22.57  ? 149 ILE E CG1 1 
ATOM   5612  C  CG2 . ILE C  1 150 ? -78.054  9.093   50.862  1.00 20.55  ? 149 ILE E CG2 1 
ATOM   5613  C  CD1 . ILE C  1 150 ? -75.583  10.929  51.323  1.00 23.95  ? 149 ILE E CD1 1 
ATOM   5614  N  N   . GLY C  1 151 ? -78.878  6.018   52.453  1.00 19.12  ? 150 GLY E N   1 
ATOM   5615  C  CA  . GLY C  1 151 ? -79.549  4.797   52.120  1.00 19.97  ? 150 GLY E CA  1 
ATOM   5616  C  C   . GLY C  1 151 ? -80.857  5.052   51.404  1.00 21.50  ? 150 GLY E C   1 
ATOM   5617  O  O   . GLY C  1 151 ? -81.479  6.119   51.549  1.00 19.34  ? 150 GLY E O   1 
ATOM   5618  N  N   . ILE C  1 152 ? -81.289  4.042   50.660  1.00 21.62  ? 151 ILE E N   1 
ATOM   5619  C  CA  . ILE C  1 152 ? -82.558  4.085   49.950  1.00 23.26  ? 151 ILE E CA  1 
ATOM   5620  C  C   . ILE C  1 152 ? -83.698  4.037   50.956  1.00 23.32  ? 151 ILE E C   1 
ATOM   5621  O  O   . ILE C  1 152 ? -83.697  3.189   51.855  1.00 21.25  ? 151 ILE E O   1 
ATOM   5622  C  CB  . ILE C  1 152 ? -82.644  2.937   48.937  1.00 22.54  ? 151 ILE E CB  1 
ATOM   5623  C  CG1 . ILE C  1 152 ? -81.565  3.108   47.872  1.00 23.09  ? 151 ILE E CG1 1 
ATOM   5624  C  CG2 . ILE C  1 152 ? -84.049  2.860   48.343  1.00 25.71  ? 151 ILE E CG2 1 
ATOM   5625  C  CD1 . ILE C  1 152 ? -81.316  1.884   47.017  1.00 23.83  ? 151 ILE E CD1 1 
ATOM   5626  N  N   . ALA C  1 153 ? -84.667  4.953   50.806  1.00 23.26  ? 152 ALA E N   1 
ATOM   5627  C  CA  . ALA C  1 153 ? -85.805  5.026   51.733  1.00 26.25  ? 152 ALA E CA  1 
ATOM   5628  C  C   . ALA C  1 153 ? -87.078  4.614   50.997  1.00 29.25  ? 152 ALA E C   1 
ATOM   5629  O  O   . ALA C  1 153 ? -87.121  4.645   49.763  1.00 34.13  ? 152 ALA E O   1 
ATOM   5630  C  CB  . ALA C  1 153 ? -85.946  6.411   52.298  1.00 26.67  ? 152 ALA E CB  1 
ATOM   5631  N  N   . GLN C  1 154 ? -88.119  4.309   51.760  1.00 39.18  ? 153 GLN E N   1 
ATOM   5632  C  CA  . GLN C  1 154 ? -89.368  3.839   51.151  1.00 50.59  ? 153 GLN E CA  1 
ATOM   5633  C  C   . GLN C  1 154 ? -89.941  4.931   50.233  1.00 60.90  ? 153 GLN E C   1 
ATOM   5634  O  O   . GLN C  1 154 ? -90.290  6.024   50.688  1.00 60.03  ? 153 GLN E O   1 
ATOM   5635  C  CB  . GLN C  1 154 ? -90.379  3.375   52.190  1.00 49.48  ? 153 GLN E CB  1 
ATOM   5636  C  CG  . GLN C  1 154 ? -91.634  2.811   51.534  1.00 54.55  ? 153 GLN E CG  1 
ATOM   5637  C  CD  . GLN C  1 154 ? -92.275  1.691   52.317  1.00 56.99  ? 153 GLN E CD  1 
ATOM   5638  O  OE1 . GLN C  1 154 ? -92.142  1.604   53.535  1.00 64.35  ? 153 GLN E OE1 1 
ATOM   5639  N  NE2 . GLN C  1 154 ? -92.977  0.814   51.616  1.00 57.79  ? 153 GLN E NE2 1 
ATOM   5640  N  N   . GLY C  1 155 ? -90.058  4.547   48.954  1.00 69.50  ? 154 GLY E N   1 
ATOM   5641  C  CA  . GLY C  1 155 ? -90.083  5.371   47.733  1.00 75.61  ? 154 GLY E CA  1 
ATOM   5642  C  C   . GLY C  1 155 ? -89.812  4.481   46.513  1.00 83.12  ? 154 GLY E C   1 
ATOM   5643  O  O   . GLY C  1 155 ? -89.574  3.265   46.663  1.00 73.79  ? 154 GLY E O   1 
ATOM   5644  N  N   . ALA C  1 156 ? -89.842  5.058   45.304  1.00 82.22  ? 155 ALA E N   1 
ATOM   5645  C  CA  . ALA C  1 156 ? -89.820  4.275   44.051  1.00 84.87  ? 155 ALA E CA  1 
ATOM   5646  C  C   . ALA C  1 156 ? -88.385  4.157   43.508  1.00 83.24  ? 155 ALA E C   1 
ATOM   5647  O  O   . ALA C  1 156 ? -87.445  4.671   44.104  1.00 78.38  ? 155 ALA E O   1 
ATOM   5648  C  CB  . ALA C  1 156 ? -90.754  4.913   43.047  1.00 88.03  ? 155 ALA E CB  1 
ATOM   5649  N  N   . ALA C  1 157 ? -88.233  3.446   42.382  1.00 83.91  ? 156 ALA E N   1 
ATOM   5650  C  CA  . ALA C  1 157 ? -86.984  3.410   41.614  1.00 85.00  ? 156 ALA E CA  1 
ATOM   5651  C  C   . ALA C  1 157 ? -86.929  4.637   40.696  1.00 80.50  ? 156 ALA E C   1 
ATOM   5652  O  O   . ALA C  1 157 ? -85.858  5.079   40.286  1.00 75.42  ? 156 ALA E O   1 
ATOM   5653  C  CB  . ALA C  1 157 ? -86.890  2.124   40.825  1.00 85.94  ? 156 ALA E CB  1 
ATOM   5654  N  N   . GLY C  1 167 ? -82.972  1.232   42.188  1.00 60.65  ? 166 GLY E N   1 
ATOM   5655  C  CA  . GLY C  1 167 ? -81.741  1.311   43.033  1.00 59.28  ? 166 GLY E CA  1 
ATOM   5656  C  C   . GLY C  1 167 ? -81.325  2.754   43.283  1.00 61.22  ? 166 GLY E C   1 
ATOM   5657  O  O   . GLY C  1 167 ? -82.075  3.587   43.804  1.00 49.69  ? 166 GLY E O   1 
ATOM   5658  N  N   . GLY C  1 168 ? -80.100  3.068   42.885  1.00 54.55  ? 167 GLY E N   1 
ATOM   5659  C  CA  . GLY C  1 168 ? -79.570  4.317   43.215  1.00 44.95  ? 167 GLY E CA  1 
ATOM   5660  C  C   . GLY C  1 168 ? -78.066  4.353   43.078  1.00 40.35  ? 167 GLY E C   1 
ATOM   5661  O  O   . GLY C  1 168 ? -77.577  5.406   42.687  1.00 32.29  ? 167 GLY E O   1 
ATOM   5662  N  N   . GLY C  1 169 ? -77.364  3.246   43.423  1.00 37.36  ? 168 GLY E N   1 
ATOM   5663  C  CA  . GLY C  1 169 ? -75.922  3.252   43.550  1.00 36.38  ? 168 GLY E CA  1 
ATOM   5664  C  C   . GLY C  1 169 ? -75.170  2.155   42.810  1.00 41.66  ? 168 GLY E C   1 
ATOM   5665  O  O   . GLY C  1 169 ? -75.700  1.041   42.557  1.00 35.11  ? 168 GLY E O   1 
ATOM   5666  N  N   . SER C  1 170 ? -73.877  2.457   42.560  1.00 43.19  ? 169 SER E N   1 
ATOM   5667  C  CA  . SER C  1 170 ? -72.978  1.648   41.730  1.00 49.07  ? 169 SER E CA  1 
ATOM   5668  C  C   . SER C  1 170 ? -71.550  1.614   42.320  1.00 46.25  ? 169 SER E C   1 
ATOM   5669  O  O   . SER C  1 170 ? -71.100  2.670   42.758  1.00 48.35  ? 169 SER E O   1 
ATOM   5670  C  CB  . SER C  1 170 ? -72.989  2.215   40.323  1.00 54.01  ? 169 SER E CB  1 
ATOM   5671  O  OG  . SER C  1 170 ? -71.854  1.784   39.592  1.00 60.18  ? 169 SER E OG  1 
ATOM   5672  N  N   . ALA C  1 171 ? -70.852  0.441   42.284  1.00 37.06  ? 170 ALA E N   1 
ATOM   5673  C  CA  . ALA C  1 171 ? -69.430  0.290   42.761  1.00 34.85  ? 170 ALA E CA  1 
ATOM   5674  C  C   . ALA C  1 171 ? -68.812  -1.093  42.455  1.00 31.61  ? 170 ALA E C   1 
ATOM   5675  O  O   . ALA C  1 171 ? -69.492  -2.031  42.148  1.00 36.47  ? 170 ALA E O   1 
ATOM   5676  C  CB  . ALA C  1 171 ? -69.385  0.555   44.249  1.00 35.12  ? 170 ALA E CB  1 
ATOM   5677  N  N   . THR C  1 172 ? -67.486  -1.195  42.567  1.00 29.17  ? 171 THR E N   1 
ATOM   5678  C  CA  . THR C  1 172 ? -66.743  -2.478  42.514  1.00 30.94  ? 171 THR E CA  1 
ATOM   5679  C  C   . THR C  1 172 ? -66.471  -3.021  43.924  1.00 26.99  ? 171 THR E C   1 
ATOM   5680  O  O   . THR C  1 172 ? -66.166  -4.215  44.063  1.00 24.90  ? 171 THR E O   1 
ATOM   5681  C  CB  . THR C  1 172 ? -65.399  -2.334  41.788  1.00 33.00  ? 171 THR E CB  1 
ATOM   5682  O  OG1 . THR C  1 172 ? -64.656  -1.249  42.360  1.00 31.88  ? 171 THR E OG1 1 
ATOM   5683  C  CG2 . THR C  1 172 ? -65.611  -2.059  40.307  1.00 33.92  ? 171 THR E CG2 1 
ATOM   5684  N  N   . LYS C  1 173 ? -66.501  -2.146  44.939  1.00 25.22  ? 172 LYS E N   1 
ATOM   5685  C  CA  . LYS C  1 173 ? -66.344  -2.584  46.343  1.00 28.34  ? 172 LYS E CA  1 
ATOM   5686  C  C   . LYS C  1 173 ? -67.380  -1.878  47.214  1.00 23.25  ? 172 LYS E C   1 
ATOM   5687  O  O   . LYS C  1 173 ? -67.686  -0.711  47.007  1.00 22.92  ? 172 LYS E O   1 
ATOM   5688  C  CB  . LYS C  1 173 ? -64.971  -2.273  46.953  1.00 34.23  ? 172 LYS E CB  1 
ATOM   5689  C  CG  . LYS C  1 173 ? -63.751  -2.811  46.213  1.00 44.54  ? 172 LYS E CG  1 
ATOM   5690  C  CD  . LYS C  1 173 ? -62.823  -3.737  47.022  1.00 54.93  ? 172 LYS E CD  1 
ATOM   5691  C  CE  . LYS C  1 173 ? -62.580  -3.364  48.478  1.00 60.84  ? 172 LYS E CE  1 
ATOM   5692  N  NZ  . LYS C  1 173 ? -63.363  -4.216  49.415  1.00 62.60  ? 172 LYS E NZ  1 
ATOM   5693  N  N   . ALA C  1 174 ? -67.856  -2.591  48.231  1.00 20.48  ? 173 ALA E N   1 
ATOM   5694  C  CA  . ALA C  1 174 ? -68.773  -2.024  49.188  1.00 20.12  ? 173 ALA E CA  1 
ATOM   5695  C  C   . ALA C  1 174 ? -68.427  -2.579  50.572  1.00 21.11  ? 173 ALA E C   1 
ATOM   5696  O  O   . ALA C  1 174 ? -67.662  -3.555  50.695  1.00 20.52  ? 173 ALA E O   1 
ATOM   5697  C  CB  . ALA C  1 174 ? -70.189  -2.349  48.787  1.00 20.69  ? 173 ALA E CB  1 
ATOM   5698  N  N   . VAL C  1 175 ? -69.017  -1.967  51.603  1.00 19.07  ? 174 VAL E N   1 
ATOM   5699  C  CA  . VAL C  1 175 ? -68.740  -2.322  52.968  1.00 19.68  ? 174 VAL E CA  1 
ATOM   5700  C  C   . VAL C  1 175 ? -69.956  -1.963  53.809  1.00 19.74  ? 174 VAL E C   1 
ATOM   5701  O  O   . VAL C  1 175 ? -70.725  -1.068  53.447  1.00 20.54  ? 174 VAL E O   1 
ATOM   5702  C  CB  . VAL C  1 175 ? -67.450  -1.639  53.467  1.00 19.62  ? 174 VAL E CB  1 
ATOM   5703  C  CG1 . VAL C  1 175 ? -67.615  -0.146  53.645  1.00 21.27  ? 174 VAL E CG1 1 
ATOM   5704  C  CG2 . VAL C  1 175 ? -66.939  -2.285  54.733  1.00 23.32  ? 174 VAL E CG2 1 
ATOM   5705  N  N   . CYS C  1 176 ? -70.132  -2.713  54.895  1.00 19.17  ? 175 CYS E N   1 
ATOM   5706  C  CA  . CYS C  1 176 ? -71.227  -2.543  55.776  1.00 19.45  ? 175 CYS E CA  1 
ATOM   5707  C  C   . CYS C  1 176 ? -70.753  -2.797  57.211  1.00 19.54  ? 175 CYS E C   1 
ATOM   5708  O  O   . CYS C  1 176 ? -70.102  -3.808  57.483  1.00 18.52  ? 175 CYS E O   1 
ATOM   5709  C  CB  . CYS C  1 176 ? -72.340  -3.508  55.395  1.00 20.41  ? 175 CYS E CB  1 
ATOM   5710  S  SG  . CYS C  1 176 ? -73.773  -3.368  56.488  1.00 24.33  ? 175 CYS E SG  1 
ATOM   5711  N  N   . VAL C  1 177 ? -71.021  -1.834  58.091  1.00 18.32  ? 176 VAL E N   1 
ATOM   5712  C  CA  . VAL C  1 177 ? -70.792  -1.970  59.517  1.00 19.92  ? 176 VAL E CA  1 
ATOM   5713  C  C   . VAL C  1 177 ? -72.124  -2.370  60.158  1.00 19.78  ? 176 VAL E C   1 
ATOM   5714  O  O   . VAL C  1 177 ? -73.076  -1.592  60.128  1.00 18.46  ? 176 VAL E O   1 
ATOM   5715  C  CB  . VAL C  1 177 ? -70.236  -0.659  60.111  1.00 22.65  ? 176 VAL E CB  1 
ATOM   5716  C  CG1 . VAL C  1 177 ? -70.030  -0.761  61.628  1.00 23.21  ? 176 VAL E CG1 1 
ATOM   5717  C  CG2 . VAL C  1 177 ? -68.938  -0.239  59.423  1.00 22.82  ? 176 VAL E CG2 1 
ATOM   5718  N  N   . LEU C  1 178 ? -72.178  -3.580  60.724  1.00 19.13  ? 177 LEU E N   1 
ATOM   5719  C  CA  . LEU C  1 178 ? -73.341  -4.108  61.379  1.00 21.60  ? 177 LEU E CA  1 
ATOM   5720  C  C   . LEU C  1 178 ? -73.285  -3.733  62.868  1.00 21.04  ? 177 LEU E C   1 
ATOM   5721  O  O   . LEU C  1 178 ? -72.318  -4.016  63.527  1.00 19.43  ? 177 LEU E O   1 
ATOM   5722  C  CB  . LEU C  1 178 ? -73.382  -5.637  61.320  1.00 24.59  ? 177 LEU E CB  1 
ATOM   5723  C  CG  . LEU C  1 178 ? -73.584  -6.334  59.978  1.00 27.94  ? 177 LEU E CG  1 
ATOM   5724  C  CD1 A LEU C  1 178 ? -74.899  -5.957  59.362  0.60 28.41  ? 177 LEU E CD1 1 
ATOM   5725  C  CD1 B LEU C  1 178 ? -74.906  -5.958  59.360  0.40 28.20  ? 177 LEU E CD1 1 
ATOM   5726  C  CD2 A LEU C  1 178 ? -72.445  -6.035  59.034  0.60 30.07  ? 177 LEU E CD2 1 
ATOM   5727  C  CD2 B LEU C  1 178 ? -72.445  -6.035  59.028  0.40 28.83  ? 177 LEU E CD2 1 
ATOM   5728  N  N   . LYS C  1 179 ? -74.357  -3.131  63.368  1.00 22.16  ? 178 LYS E N   1 
ATOM   5729  C  CA  . LYS C  1 179 ? -74.490  -2.785  64.771  1.00 26.55  ? 178 LYS E CA  1 
ATOM   5730  C  C   . LYS C  1 179 ? -75.915  -3.098  65.177  1.00 23.84  ? 178 LYS E C   1 
ATOM   5731  O  O   . LYS C  1 179 ? -76.785  -3.104  64.333  1.00 19.52  ? 178 LYS E O   1 
ATOM   5732  C  CB  . LYS C  1 179 ? -74.287  -1.294  65.019  1.00 30.35  ? 178 LYS E CB  1 
ATOM   5733  C  CG  . LYS C  1 179 ? -72.939  -0.730  64.596  1.00 40.75  ? 178 LYS E CG  1 
ATOM   5734  C  CD  . LYS C  1 179 ? -71.746  -1.358  65.298  1.00 50.83  ? 178 LYS E CD  1 
ATOM   5735  C  CE  . LYS C  1 179 ? -70.741  -0.355  65.847  1.00 60.16  ? 178 LYS E CE  1 
ATOM   5736  N  NZ  . LYS C  1 179 ? -70.632  0.879   65.033  1.00 60.56  ? 178 LYS E NZ  1 
ATOM   5737  N  N   . GLY C  1 180 ? -76.125  -3.298  66.475  1.00 24.63  ? 179 GLY E N   1 
ATOM   5738  C  CA  . GLY C  1 180 ? -77.471  -3.397  67.031  1.00 27.91  ? 179 GLY E CA  1 
ATOM   5739  C  C   . GLY C  1 180 ? -77.479  -3.029  68.511  1.00 27.72  ? 179 GLY E C   1 
ATOM   5740  O  O   . GLY C  1 180 ? -76.509  -2.469  69.015  1.00 29.30  ? 179 GLY E O   1 
ATOM   5741  N  N   . ASP C  1 181 ? -78.562  -3.377  69.195  1.00 29.93  ? 180 ASP E N   1 
ATOM   5742  C  CA  . ASP C  1 181 ? -78.778  -2.951  70.589  1.00 34.54  ? 180 ASP E CA  1 
ATOM   5743  C  C   . ASP C  1 181 ? -78.159  -3.962  71.555  1.00 33.69  ? 180 ASP E C   1 
ATOM   5744  O  O   . ASP C  1 181 ? -78.010  -3.675  72.729  1.00 38.26  ? 180 ASP E O   1 
ATOM   5745  C  CB  . ASP C  1 181 ? -80.265  -2.772  70.880  1.00 37.07  ? 180 ASP E CB  1 
ATOM   5746  C  CG  . ASP C  1 181 ? -80.847  -1.535  70.215  1.00 41.00  ? 180 ASP E CG  1 
ATOM   5747  O  OD1 . ASP C  1 181 ? -80.123  -0.509  70.125  1.00 43.66  ? 180 ASP E OD1 1 
ATOM   5748  O  OD2 . ASP C  1 181 ? -82.012  -1.612  69.777  1.00 52.20  ? 180 ASP E OD2 1 
ATOM   5749  N  N   . GLY C  1 182 ? -77.767  -5.122  71.029  1.00 29.64  ? 181 GLY E N   1 
ATOM   5750  C  CA  . GLY C  1 182 ? -77.194  -6.207  71.798  1.00 28.03  ? 181 GLY E CA  1 
ATOM   5751  C  C   . GLY C  1 182 ? -75.712  -6.360  71.516  1.00 26.67  ? 181 GLY E C   1 
ATOM   5752  O  O   . GLY C  1 182 ? -75.043  -5.410  71.114  1.00 24.65  ? 181 GLY E O   1 
ATOM   5753  N  N   . PRO C  1 183 ? -75.133  -7.561  71.723  1.00 24.26  ? 182 PRO E N   1 
ATOM   5754  C  CA  . PRO C  1 183 ? -73.698  -7.731  71.530  1.00 24.00  ? 182 PRO E CA  1 
ATOM   5755  C  C   . PRO C  1 183 ? -73.260  -7.948  70.078  1.00 22.61  ? 182 PRO E C   1 
ATOM   5756  O  O   . PRO C  1 183 ? -72.076  -8.073  69.824  1.00 22.53  ? 182 PRO E O   1 
ATOM   5757  C  CB  . PRO C  1 183 ? -73.410  -9.000  72.341  1.00 24.46  ? 182 PRO E CB  1 
ATOM   5758  C  CG  . PRO C  1 183 ? -74.664  -9.796  72.216  1.00 23.76  ? 182 PRO E CG  1 
ATOM   5759  C  CD  . PRO C  1 183 ? -75.792  -8.778  72.204  1.00 24.58  ? 182 PRO E CD  1 
ATOM   5760  N  N   . VAL C  1 184 ? -74.189  -8.002  69.121  1.00 22.75  ? 183 VAL E N   1 
ATOM   5761  C  CA  . VAL C  1 184 ? -73.802  -8.420  67.778  1.00 23.28  ? 183 VAL E CA  1 
ATOM   5762  C  C   . VAL C  1 184 ? -73.187  -7.223  67.054  1.00 23.73  ? 183 VAL E C   1 
ATOM   5763  O  O   . VAL C  1 184 ? -73.786  -6.148  66.974  1.00 22.02  ? 183 VAL E O   1 
ATOM   5764  C  CB  . VAL C  1 184 ? -74.978  -9.022  66.995  1.00 22.66  ? 183 VAL E CB  1 
ATOM   5765  C  CG1 . VAL C  1 184 ? -74.580  -9.379  65.568  1.00 23.07  ? 183 VAL E CG1 1 
ATOM   5766  C  CG2 . VAL C  1 184 ? -75.543  -10.242 67.711  1.00 22.26  ? 183 VAL E CG2 1 
ATOM   5767  N  N   . GLN C  1 185 ? -72.017  -7.438  66.469  1.00 23.25  ? 184 GLN E N   1 
ATOM   5768  C  CA  . GLN C  1 185 ? -71.320  -6.345  65.811  1.00 26.94  ? 184 GLN E CA  1 
ATOM   5769  C  C   . GLN C  1 185 ? -70.401  -6.948  64.754  1.00 23.66  ? 184 GLN E C   1 
ATOM   5770  O  O   . GLN C  1 185 ? -69.798  -7.972  64.994  1.00 21.50  ? 184 GLN E O   1 
ATOM   5771  C  CB  . GLN C  1 185 ? -70.571  -5.576  66.897  1.00 32.87  ? 184 GLN E CB  1 
ATOM   5772  C  CG  . GLN C  1 185 ? -69.728  -4.431  66.398  1.00 47.76  ? 184 GLN E CG  1 
ATOM   5773  C  CD  . GLN C  1 185 ? -69.242  -3.606  67.567  1.00 57.23  ? 184 GLN E CD  1 
ATOM   5774  O  OE1 . GLN C  1 185 ? -68.481  -4.084  68.413  1.00 57.81  ? 184 GLN E OE1 1 
ATOM   5775  N  NE2 . GLN C  1 185 ? -69.721  -2.371  67.639  1.00 59.43  ? 184 GLN E NE2 1 
ATOM   5776  N  N   . GLY C  1 186 ? -70.257  -6.289  63.604  1.00 21.92  ? 185 GLY E N   1 
ATOM   5777  C  CA  . GLY C  1 186 ? -69.309  -6.792  62.629  1.00 22.20  ? 185 GLY E CA  1 
ATOM   5778  C  C   . GLY C  1 186 ? -69.109  -5.880  61.437  1.00 20.84  ? 185 GLY E C   1 
ATOM   5779  O  O   . GLY C  1 186 ? -69.694  -4.815  61.349  1.00 20.08  ? 185 GLY E O   1 
ATOM   5780  N  N   . ILE C  1 187 ? -68.206  -6.312  60.560  1.00 20.37  ? 186 ILE E N   1 
ATOM   5781  C  CA  . ILE C  1 187 ? -67.884  -5.604  59.355  1.00 21.39  ? 186 ILE E CA  1 
ATOM   5782  C  C   . ILE C  1 187 ? -67.916  -6.590  58.196  1.00 21.30  ? 186 ILE E C   1 
ATOM   5783  O  O   . ILE C  1 187 ? -67.256  -7.625  58.249  1.00 20.76  ? 186 ILE E O   1 
ATOM   5784  C  CB  . ILE C  1 187 ? -66.534  -4.876  59.433  1.00 22.66  ? 186 ILE E CB  1 
ATOM   5785  C  CG1 . ILE C  1 187 ? -66.565  -3.788  60.502  1.00 25.90  ? 186 ILE E CG1 1 
ATOM   5786  C  CG2 . ILE C  1 187 ? -66.178  -4.296  58.067  1.00 23.08  ? 186 ILE E CG2 1 
ATOM   5787  C  CD1 . ILE C  1 187 ? -65.224  -3.145  60.741  1.00 27.79  ? 186 ILE E CD1 1 
ATOM   5788  N  N   . ILE C  1 188 ? -68.703  -6.250  57.174  1.00 19.89  ? 187 ILE E N   1 
ATOM   5789  C  CA  . ILE C  1 188 ? -68.854  -7.115  56.020  1.00 20.34  ? 187 ILE E CA  1 
ATOM   5790  C  C   . ILE C  1 188 ? -68.416  -6.337  54.770  1.00 20.59  ? 187 ILE E C   1 
ATOM   5791  O  O   . ILE C  1 188 ? -68.857  -5.211  54.521  1.00 19.14  ? 187 ILE E O   1 
ATOM   5792  C  CB  . ILE C  1 188 ? -70.283  -7.690  55.889  1.00 18.93  ? 187 ILE E CB  1 
ATOM   5793  C  CG1 . ILE C  1 188 ? -70.679  -8.600  57.054  1.00 19.19  ? 187 ILE E CG1 1 
ATOM   5794  C  CG2 . ILE C  1 188 ? -70.436  -8.417  54.561  1.00 20.02  ? 187 ILE E CG2 1 
ATOM   5795  C  CD1 . ILE C  1 188 ? -69.844  -9.887  57.154  1.00 21.36  ? 187 ILE E CD1 1 
ATOM   5796  N  N   . ASN C  1 189 ? -67.547  -6.984  53.987  1.00 20.85  ? 188 ASN E N   1 
ATOM   5797  C  CA  . ASN C  1 189 ? -66.963  -6.450  52.748  1.00 22.76  ? 188 ASN E CA  1 
ATOM   5798  C  C   . ASN C  1 189 ? -67.657  -7.115  51.559  1.00 21.45  ? 188 ASN E C   1 
ATOM   5799  O  O   . ASN C  1 189 ? -68.037  -8.289  51.624  1.00 20.37  ? 188 ASN E O   1 
ATOM   5800  C  CB  . ASN C  1 189 ? -65.446  -6.689  52.668  1.00 23.10  ? 188 ASN E CB  1 
ATOM   5801  C  CG  . ASN C  1 189 ? -64.711  -6.138  53.865  1.00 25.81  ? 188 ASN E CG  1 
ATOM   5802  O  OD1 . ASN C  1 189 ? -64.575  -4.919  53.994  1.00 24.86  ? 188 ASN E OD1 1 
ATOM   5803  N  ND2 . ASN C  1 189 ? -64.339  -7.020  54.788  1.00 26.03  ? 188 ASN E ND2 1 
ATOM   5804  N  N   . PHE C  1 190 ? -67.754  -6.371  50.452  1.00 20.70  ? 189 PHE E N   1 
ATOM   5805  C  CA  . PHE C  1 190 ? -68.307  -6.894  49.208  1.00 21.59  ? 189 PHE E CA  1 
ATOM   5806  C  C   . PHE C  1 190 ? -67.355  -6.496  48.083  1.00 22.71  ? 189 PHE E C   1 
ATOM   5807  O  O   . PHE C  1 190 ? -66.884  -5.366  48.069  1.00 21.24  ? 189 PHE E O   1 
ATOM   5808  C  CB  . PHE C  1 190 ? -69.682  -6.311  48.881  1.00 21.11  ? 189 PHE E CB  1 
ATOM   5809  C  CG  . PHE C  1 190 ? -70.743  -6.474  49.929  1.00 22.11  ? 189 PHE E CG  1 
ATOM   5810  C  CD1 . PHE C  1 190 ? -71.745  -7.425  49.781  1.00 22.34  ? 189 PHE E CD1 1 
ATOM   5811  C  CD2 . PHE C  1 190 ? -70.762  -5.651  51.053  1.00 20.38  ? 189 PHE E CD2 1 
ATOM   5812  C  CE1 . PHE C  1 190 ? -72.737  -7.560  50.746  1.00 22.69  ? 189 PHE E CE1 1 
ATOM   5813  C  CE2 . PHE C  1 190 ? -71.761  -5.780  52.004  1.00 19.78  ? 189 PHE E CE2 1 
ATOM   5814  C  CZ  . PHE C  1 190 ? -72.732  -6.746  51.859  1.00 20.58  ? 189 PHE E CZ  1 
ATOM   5815  N  N   . GLU C  1 191 ? -67.123  -7.401  47.133  1.00 23.13  ? 190 GLU E N   1 
ATOM   5816  C  CA  . GLU C  1 191 ? -66.277  -7.075  45.999  1.00 25.17  ? 190 GLU E CA  1 
ATOM   5817  C  C   . GLU C  1 191 ? -66.892  -7.697  44.757  1.00 24.16  ? 190 GLU E C   1 
ATOM   5818  O  O   . GLU C  1 191 ? -67.268  -8.850  44.763  1.00 23.61  ? 190 GLU E O   1 
ATOM   5819  C  CB  . GLU C  1 191 ? -64.841  -7.574  46.195  1.00 29.48  ? 190 GLU E CB  1 
ATOM   5820  C  CG  . GLU C  1 191 ? -63.908  -7.185  45.061  1.00 38.40  ? 190 GLU E CG  1 
ATOM   5821  C  CD  . GLU C  1 191 ? -62.633  -8.015  45.035  1.00 46.08  ? 190 GLU E CD  1 
ATOM   5822  O  OE1 . GLU C  1 191 ? -61.749  -7.718  45.847  1.00 45.58  ? 190 GLU E OE1 1 
ATOM   5823  O  OE2 . GLU C  1 191 ? -62.575  -9.015  44.255  1.00 57.85  ? 190 GLU E OE2 1 
ATOM   5824  N  N   . GLN C  1 192 ? -66.929  -6.907  43.686  1.00 23.36  ? 191 GLN E N   1 
ATOM   5825  C  CA  . GLN C  1 192 ? -67.454  -7.363  42.420  1.00 26.15  ? 191 GLN E CA  1 
ATOM   5826  C  C   . GLN C  1 192 ? -66.561  -6.769  41.323  1.00 29.99  ? 191 GLN E C   1 
ATOM   5827  O  O   . GLN C  1 192 ? -66.757  -5.633  40.906  1.00 28.97  ? 191 GLN E O   1 
ATOM   5828  C  CB  . GLN C  1 192 ? -68.922  -6.964  42.276  1.00 24.24  ? 191 GLN E CB  1 
ATOM   5829  C  CG  . GLN C  1 192 ? -69.576  -7.601  41.052  1.00 24.84  ? 191 GLN E CG  1 
ATOM   5830  C  CD  . GLN C  1 192 ? -70.952  -7.066  40.769  1.00 25.66  ? 191 GLN E CD  1 
ATOM   5831  O  OE1 . GLN C  1 192 ? -71.258  -5.917  41.115  1.00 26.06  ? 191 GLN E OE1 1 
ATOM   5832  N  NE2 . GLN C  1 192 ? -71.791  -7.899  40.170  1.00 22.27  ? 191 GLN E NE2 1 
ATOM   5833  N  N   . LYS C  1 193 ? -65.547  -7.534  40.931  1.00 34.29  ? 192 LYS E N   1 
ATOM   5834  C  CA  . LYS C  1 193 ? -64.536  -7.112  39.933  1.00 44.24  ? 192 LYS E CA  1 
ATOM   5835  C  C   . LYS C  1 193 ? -65.174  -6.801  38.573  1.00 41.84  ? 192 LYS E C   1 
ATOM   5836  O  O   . LYS C  1 193 ? -64.817  -5.817  37.938  1.00 44.74  ? 192 LYS E O   1 
ATOM   5837  C  CB  . LYS C  1 193 ? -63.490  -8.209  39.739  1.00 51.36  ? 192 LYS E CB  1 
ATOM   5838  C  CG  . LYS C  1 193 ? -62.534  -8.387  40.912  1.00 62.58  ? 192 LYS E CG  1 
ATOM   5839  C  CD  . LYS C  1 193 ? -61.678  -9.644  40.825  1.00 73.77  ? 192 LYS E CD  1 
ATOM   5840  C  CE  . LYS C  1 193 ? -62.458  -10.880 40.417  1.00 78.11  ? 192 LYS E CE  1 
ATOM   5841  N  NZ  . LYS C  1 193 ? -61.759  -12.127 40.810  1.00 82.55  ? 192 LYS E NZ  1 
ATOM   5842  N  N   . GLU C  1 194 ? -66.093  -7.650  38.119  1.00 41.21  ? 193 GLU E N   1 
ATOM   5843  C  CA  . GLU C  1 194 ? -66.764  -7.424  36.844  1.00 46.21  ? 193 GLU E CA  1 
ATOM   5844  C  C   . GLU C  1 194 ? -68.269  -7.309  37.100  1.00 41.25  ? 193 GLU E C   1 
ATOM   5845  O  O   . GLU C  1 194 ? -68.831  -8.055  37.891  1.00 38.79  ? 193 GLU E O   1 
ATOM   5846  C  CB  . GLU C  1 194 ? -66.380  -8.509  35.828  1.00 53.31  ? 193 GLU E CB  1 
ATOM   5847  C  CG  . GLU C  1 194 ? -66.281  -9.919  36.395  1.00 65.02  ? 193 GLU E CG  1 
ATOM   5848  C  CD  . GLU C  1 194 ? -66.197  -11.053 35.371  1.00 77.08  ? 193 GLU E CD  1 
ATOM   5849  O  OE1 . GLU C  1 194 ? -67.067  -11.973 35.396  1.00 75.13  ? 193 GLU E OE1 1 
ATOM   5850  O  OE2 . GLU C  1 194 ? -65.255  -11.033 34.549  1.00 88.49  ? 193 GLU E OE2 1 
ATOM   5851  N  N   . SER C  1 195 ? -68.920  -6.372  36.410  1.00 42.39  ? 194 SER E N   1 
ATOM   5852  C  CA  . SER C  1 195 ? -70.348  -6.060  36.636  1.00 43.13  ? 194 SER E CA  1 
ATOM   5853  C  C   . SER C  1 195 ? -71.259  -7.251  36.297  1.00 43.26  ? 194 SER E C   1 
ATOM   5854  O  O   . SER C  1 195 ? -72.363  -7.361  36.815  1.00 46.29  ? 194 SER E O   1 
ATOM   5855  C  CB  . SER C  1 195 ? -70.748  -4.838  35.863  1.00 49.04  ? 194 SER E CB  1 
ATOM   5856  O  OG  . SER C  1 195 ? -70.832  -5.125  34.473  1.00 51.23  ? 194 SER E OG  1 
ATOM   5857  N  N   . ASN C  1 196 ? -70.790  -8.163  35.446  1.00 42.49  ? 195 ASN E N   1 
ATOM   5858  C  CA  . ASN C  1 196 ? -71.589  -9.328  35.068  1.00 48.72  ? 195 ASN E CA  1 
ATOM   5859  C  C   . ASN C  1 196 ? -71.217  -10.515 35.963  1.00 49.10  ? 195 ASN E C   1 
ATOM   5860  O  O   . ASN C  1 196 ? -71.608  -11.651 35.698  1.00 53.07  ? 195 ASN E O   1 
ATOM   5861  C  CB  . ASN C  1 196 ? -71.380  -9.706  33.597  1.00 53.21  ? 195 ASN E CB  1 
ATOM   5862  C  CG  . ASN C  1 196 ? -69.962  -10.153 33.303  1.00 58.14  ? 195 ASN E CG  1 
ATOM   5863  O  OD1 . ASN C  1 196 ? -69.008  -9.447  33.632  1.00 58.84  ? 195 ASN E OD1 1 
ATOM   5864  N  ND2 . ASN C  1 196 ? -69.810  -11.317 32.688  1.00 57.76  ? 195 ASN E ND2 1 
ATOM   5865  N  N   . GLY C  1 197 ? -70.433  -10.244 37.008  1.00 39.70  ? 196 GLY E N   1 
ATOM   5866  C  CA  . GLY C  1 197 ? -69.802  -11.277 37.753  1.00 38.95  ? 196 GLY E CA  1 
ATOM   5867  C  C   . GLY C  1 197 ? -70.397  -11.440 39.150  1.00 33.12  ? 196 GLY E C   1 
ATOM   5868  O  O   . GLY C  1 197 ? -71.227  -10.656 39.602  1.00 29.69  ? 196 GLY E O   1 
ATOM   5869  N  N   . PRO C  1 198 ? -69.964  -12.493 39.857  1.00 31.00  ? 197 PRO E N   1 
ATOM   5870  C  CA  . PRO C  1 198 ? -70.380  -12.731 41.232  1.00 29.17  ? 197 PRO E CA  1 
ATOM   5871  C  C   . PRO C  1 198 ? -69.854  -11.655 42.191  1.00 26.03  ? 197 PRO E C   1 
ATOM   5872  O  O   . PRO C  1 198 ? -68.846  -10.968 41.927  1.00 24.73  ? 197 PRO E O   1 
ATOM   5873  C  CB  . PRO C  1 198 ? -69.791  -14.114 41.541  1.00 31.09  ? 197 PRO E CB  1 
ATOM   5874  C  CG  . PRO C  1 198 ? -68.629  -14.261 40.600  1.00 34.28  ? 197 PRO E CG  1 
ATOM   5875  C  CD  . PRO C  1 198 ? -69.046  -13.523 39.353  1.00 34.93  ? 197 PRO E CD  1 
ATOM   5876  N  N   . VAL C  1 199 ? -70.568  -11.501 43.309  1.00 25.41  ? 198 VAL E N   1 
ATOM   5877  C  CA  . VAL C  1 199 ? -70.127  -10.628 44.388  1.00 23.53  ? 198 VAL E CA  1 
ATOM   5878  C  C   . VAL C  1 199 ? -69.538  -11.516 45.480  1.00 23.44  ? 198 VAL E C   1 
ATOM   5879  O  O   . VAL C  1 199 ? -70.212  -12.424 45.960  1.00 22.60  ? 198 VAL E O   1 
ATOM   5880  C  CB  . VAL C  1 199 ? -71.284  -9.785  44.949  1.00 22.51  ? 198 VAL E CB  1 
ATOM   5881  C  CG1 . VAL C  1 199 ? -70.794  -8.835  46.035  1.00 20.44  ? 198 VAL E CG1 1 
ATOM   5882  C  CG2 . VAL C  1 199 ? -72.027  -9.023  43.863  1.00 23.84  ? 198 VAL E CG2 1 
ATOM   5883  N  N   . LYS C  1 200 ? -68.309  -11.225 45.880  1.00 23.67  ? 199 LYS E N   1 
ATOM   5884  C  CA  . LYS C  1 200 ? -67.699  -11.890 47.007  1.00 26.37  ? 199 LYS E CA  1 
ATOM   5885  C  C   . LYS C  1 200 ? -68.079  -11.113 48.269  1.00 24.60  ? 199 LYS E C   1 
ATOM   5886  O  O   . LYS C  1 200 ? -68.010  -9.877  48.278  1.00 23.68  ? 199 LYS E O   1 
ATOM   5887  C  CB  . LYS C  1 200 ? -66.179  -11.994 46.821  1.00 32.93  ? 199 LYS E CB  1 
ATOM   5888  C  CG  . LYS C  1 200 ? -65.751  -12.982 45.745  1.00 43.15  ? 199 LYS E CG  1 
ATOM   5889  C  CD  . LYS C  1 200 ? -64.446  -12.625 45.034  1.00 58.04  ? 199 LYS E CD  1 
ATOM   5890  C  CE  . LYS C  1 200 ? -64.581  -11.543 43.971  1.00 67.31  ? 199 LYS E CE  1 
ATOM   5891  N  NZ  . LYS C  1 200 ? -65.519  -11.899 42.867  1.00 68.48  ? 199 LYS E NZ  1 
ATOM   5892  N  N   . VAL C  1 201 ? -68.462  -11.849 49.313  1.00 22.72  ? 200 VAL E N   1 
ATOM   5893  C  CA  . VAL C  1 201 ? -68.964  -11.277 50.562  1.00 21.45  ? 200 VAL E CA  1 
ATOM   5894  C  C   . VAL C  1 201 ? -68.163  -11.897 51.704  1.00 21.08  ? 200 VAL E C   1 
ATOM   5895  O  O   . VAL C  1 201 ? -68.213  -13.097 51.890  1.00 23.67  ? 200 VAL E O   1 
ATOM   5896  C  CB  . VAL C  1 201 ? -70.472  -11.549 50.750  1.00 20.17  ? 200 VAL E CB  1 
ATOM   5897  C  CG1 . VAL C  1 201 ? -71.015  -10.891 52.002  1.00 19.85  ? 200 VAL E CG1 1 
ATOM   5898  C  CG2 . VAL C  1 201 ? -71.297  -11.131 49.561  1.00 21.45  ? 200 VAL E CG2 1 
ATOM   5899  N  N   . TRP C  1 202 ? -67.427  -11.085 52.464  1.00 20.70  ? 201 TRP E N   1 
ATOM   5900  C  CA  . TRP C  1 202 ? -66.667  -11.648 53.530  1.00 22.73  ? 201 TRP E CA  1 
ATOM   5901  C  C   . TRP C  1 202 ? -66.481  -10.646 54.663  1.00 22.01  ? 201 TRP E C   1 
ATOM   5902  O  O   . TRP C  1 202 ? -66.538  -9.426  54.467  1.00 21.82  ? 201 TRP E O   1 
ATOM   5903  C  CB  . TRP C  1 202 ? -65.310  -12.170 53.035  1.00 22.97  ? 201 TRP E CB  1 
ATOM   5904  C  CG  . TRP C  1 202 ? -64.310  -11.090 52.784  1.00 23.82  ? 201 TRP E CG  1 
ATOM   5905  C  CD1 . TRP C  1 202 ? -63.269  -10.750 53.592  1.00 26.29  ? 201 TRP E CD1 1 
ATOM   5906  C  CD2 . TRP C  1 202 ? -64.248  -10.200 51.659  1.00 24.79  ? 201 TRP E CD2 1 
ATOM   5907  N  NE1 . TRP C  1 202 ? -62.588  -9.691  53.065  1.00 26.78  ? 201 TRP E NE1 1 
ATOM   5908  C  CE2 . TRP C  1 202 ? -63.139  -9.352  51.864  1.00 26.30  ? 201 TRP E CE2 1 
ATOM   5909  C  CE3 . TRP C  1 202 ? -65.010  -10.032 50.502  1.00 26.09  ? 201 TRP E CE3 1 
ATOM   5910  C  CZ2 . TRP C  1 202 ? -62.769  -8.356  50.958  1.00 28.43  ? 201 TRP E CZ2 1 
ATOM   5911  C  CZ3 . TRP C  1 202 ? -64.660  -9.041  49.612  1.00 28.91  ? 201 TRP E CZ3 1 
ATOM   5912  C  CH2 . TRP C  1 202 ? -63.549  -8.216  49.832  1.00 30.09  ? 201 TRP E CH2 1 
ATOM   5913  N  N   . GLY C  1 203 ? -66.180  -11.198 55.835  1.00 20.68  ? 202 GLY E N   1 
ATOM   5914  C  CA  . GLY C  1 203 ? -65.834  -10.379 57.008  1.00 20.74  ? 202 GLY E CA  1 
ATOM   5915  C  C   . GLY C  1 203 ? -66.151  -11.145 58.259  1.00 22.22  ? 202 GLY E C   1 
ATOM   5916  O  O   . GLY C  1 203 ? -66.248  -12.348 58.191  1.00 23.37  ? 202 GLY E O   1 
ATOM   5917  N  N   . SER C  1 204 ? -66.300  -10.441 59.386  1.00 22.32  ? 203 SER E N   1 
ATOM   5918  C  CA  . SER C  1 204 ? -66.452  -11.051 60.699  1.00 25.53  ? 203 SER E CA  1 
ATOM   5919  C  C   . SER C  1 204 ? -67.585  -10.365 61.441  1.00 23.17  ? 203 SER E C   1 
ATOM   5920  O  O   . SER C  1 204 ? -67.655  -9.130  61.447  1.00 23.91  ? 203 SER E O   1 
ATOM   5921  C  CB  . SER C  1 204 ? -65.192  -10.935 61.536  1.00 27.51  ? 203 SER E CB  1 
ATOM   5922  O  OG  . SER C  1 204 ? -64.274  -11.924 61.151  1.00 40.95  ? 203 SER E OG  1 
ATOM   5923  N  N   . ILE C  1 205 ? -68.411  -11.181 62.090  1.00 21.82  ? 204 ILE E N   1 
ATOM   5924  C  CA  . ILE C  1 205 ? -69.459  -10.721 62.980  1.00 22.57  ? 204 ILE E CA  1 
ATOM   5925  C  C   . ILE C  1 205 ? -69.261  -11.439 64.318  1.00 23.78  ? 204 ILE E C   1 
ATOM   5926  O  O   . ILE C  1 205 ? -69.153  -12.675 64.329  1.00 24.79  ? 204 ILE E O   1 
ATOM   5927  C  CB  . ILE C  1 205 ? -70.851  -11.026 62.411  1.00 22.37  ? 204 ILE E CB  1 
ATOM   5928  C  CG1 . ILE C  1 205 ? -71.001  -10.562 60.961  1.00 21.70  ? 204 ILE E CG1 1 
ATOM   5929  C  CG2 . ILE C  1 205 ? -71.924  -10.436 63.309  1.00 21.20  ? 204 ILE E CG2 1 
ATOM   5930  C  CD1 . ILE C  1 205 ? -72.275  -11.003 60.329  1.00 22.50  ? 204 ILE E CD1 1 
ATOM   5931  N  N   . LYS C  1 206 ? -69.222  -10.679 65.418  1.00 21.56  ? 205 LYS E N   1 
ATOM   5932  C  CA  . LYS C  1 206 ? -69.077  -11.277 66.762  1.00 23.10  ? 205 LYS E CA  1 
ATOM   5933  C  C   . LYS C  1 206 ? -70.405  -11.125 67.512  1.00 22.57  ? 205 LYS E C   1 
ATOM   5934  O  O   . LYS C  1 206 ? -71.317  -10.395 67.054  1.00 20.76  ? 205 LYS E O   1 
ATOM   5935  C  CB  . LYS C  1 206 ? -67.898  -10.650 67.520  1.00 26.98  ? 205 LYS E CB  1 
ATOM   5936  C  CG  . LYS C  1 206 ? -67.982  -9.147  67.757  1.00 33.06  ? 205 LYS E CG  1 
ATOM   5937  C  CD  . LYS C  1 206 ? -67.872  -8.689  69.213  1.00 44.79  ? 205 LYS E CD  1 
ATOM   5938  C  CE  . LYS C  1 206 ? -69.173  -8.868  69.981  1.00 49.80  ? 205 LYS E CE  1 
ATOM   5939  N  NZ  . LYS C  1 206 ? -69.400  -7.848  71.045  1.00 45.79  ? 205 LYS E NZ  1 
ATOM   5940  N  N   . GLY C  1 207 ? -70.518  -11.837 68.649  1.00 19.79  ? 206 GLY E N   1 
ATOM   5941  C  CA  . GLY C  1 207 ? -71.620  -11.701 69.585  1.00 19.55  ? 206 GLY E CA  1 
ATOM   5942  C  C   . GLY C  1 207 ? -72.817  -12.572 69.242  1.00 21.14  ? 206 GLY E C   1 
ATOM   5943  O  O   . GLY C  1 207 ? -73.878  -12.368 69.795  1.00 22.91  ? 206 GLY E O   1 
ATOM   5944  N  N   . LEU C  1 208 ? -72.649  -13.535 68.319  1.00 20.89  ? 207 LEU E N   1 
ATOM   5945  C  CA  . LEU C  1 208 ? -73.736  -14.373 67.820  1.00 19.93  ? 207 LEU E CA  1 
ATOM   5946  C  C   . LEU C  1 208 ? -73.742  -15.698 68.581  1.00 19.99  ? 207 LEU E C   1 
ATOM   5947  O  O   . LEU C  1 208 ? -72.698  -16.273 68.790  1.00 21.06  ? 207 LEU E O   1 
ATOM   5948  C  CB  . LEU C  1 208 ? -73.520  -14.666 66.327  1.00 20.39  ? 207 LEU E CB  1 
ATOM   5949  C  CG  . LEU C  1 208 ? -73.775  -13.506 65.361  1.00 20.65  ? 207 LEU E CG  1 
ATOM   5950  C  CD1 . LEU C  1 208 ? -73.213  -13.823 63.981  1.00 21.03  ? 207 LEU E CD1 1 
ATOM   5951  C  CD2 . LEU C  1 208 ? -75.250  -13.171 65.273  1.00 19.42  ? 207 LEU E CD2 1 
ATOM   5952  N  N   . THR C  1 209 ? -74.926  -16.226 68.867  1.00 20.05  ? 208 THR E N   1 
ATOM   5953  C  CA  . THR C  1 209 ? -75.032  -17.568 69.414  1.00 22.08  ? 208 THR E CA  1 
ATOM   5954  C  C   . THR C  1 209 ? -74.484  -18.573 68.393  1.00 22.24  ? 208 THR E C   1 
ATOM   5955  O  O   . THR C  1 209 ? -74.679  -18.460 67.166  1.00 19.75  ? 208 THR E O   1 
ATOM   5956  C  CB  . THR C  1 209 ? -76.472  -17.891 69.822  1.00 23.78  ? 208 THR E CB  1 
ATOM   5957  O  OG1 . THR C  1 209 ? -77.317  -17.782 68.680  1.00 28.61  ? 208 THR E OG1 1 
ATOM   5958  C  CG2 . THR C  1 209 ? -76.995  -16.960 70.890  1.00 24.37  ? 208 THR E CG2 1 
ATOM   5959  N  N   . GLU C  1 210 ? -73.759  -19.556 68.899  1.00 20.55  ? 209 GLU E N   1 
ATOM   5960  C  CA  . GLU C  1 210 ? -73.173  -20.597 68.064  1.00 22.41  ? 209 GLU E CA  1 
ATOM   5961  C  C   . GLU C  1 210 ? -74.225  -21.198 67.125  1.00 21.68  ? 209 GLU E C   1 
ATOM   5962  O  O   . GLU C  1 210 ? -75.326  -21.503 67.522  1.00 22.52  ? 209 GLU E O   1 
ATOM   5963  C  CB  . GLU C  1 210 ? -72.604  -21.686 68.986  1.00 26.45  ? 209 GLU E CB  1 
ATOM   5964  C  CG  . GLU C  1 210 ? -71.919  -22.808 68.228  1.00 32.06  ? 209 GLU E CG  1 
ATOM   5965  C  CD  . GLU C  1 210 ? -71.306  -23.879 69.132  1.00 39.30  ? 209 GLU E CD  1 
ATOM   5966  O  OE1 . GLU C  1 210 ? -71.658  -23.930 70.338  1.00 39.69  ? 209 GLU E OE1 1 
ATOM   5967  O  OE2 . GLU C  1 210 ? -70.478  -24.649 68.626  1.00 46.30  ? 209 GLU E OE2 1 
ATOM   5968  N  N   . GLY C  1 211 ? -73.871  -21.396 65.856  1.00 21.85  ? 210 GLY E N   1 
ATOM   5969  C  CA  . GLY C  1 211 ? -74.788  -22.031 64.901  1.00 20.73  ? 210 GLY E CA  1 
ATOM   5970  C  C   . GLY C  1 211 ? -75.207  -21.064 63.791  1.00 19.81  ? 210 GLY E C   1 
ATOM   5971  O  O   . GLY C  1 211 ? -74.551  -20.035 63.587  1.00 17.83  ? 210 GLY E O   1 
ATOM   5972  N  N   . LEU C  1 212 ? -76.359  -21.340 63.164  1.00 19.42  ? 211 LEU E N   1 
ATOM   5973  C  CA  . LEU C  1 212 ? -76.775  -20.686 61.922  1.00 22.41  ? 211 LEU E CA  1 
ATOM   5974  C  C   . LEU C  1 212 ? -77.606  -19.433 62.220  1.00 19.76  ? 211 LEU E C   1 
ATOM   5975  O  O   . LEU C  1 212 ? -78.465  -19.459 63.051  1.00 20.56  ? 211 LEU E O   1 
ATOM   5976  C  CB  . LEU C  1 212 ? -77.606  -21.643 61.064  1.00 24.12  ? 211 LEU E CB  1 
ATOM   5977  C  CG  . LEU C  1 212 ? -76.873  -22.870 60.511  1.00 27.46  ? 211 LEU E CG  1 
ATOM   5978  C  CD1 . LEU C  1 212 ? -77.876  -23.941 60.102  1.00 30.17  ? 211 LEU E CD1 1 
ATOM   5979  C  CD2 . LEU C  1 212 ? -76.032  -22.499 59.326  1.00 27.15  ? 211 LEU E CD2 1 
ATOM   5980  N  N   . HIS C  1 213 ? -77.399  -18.397 61.405  1.00 18.52  ? 212 HIS E N   1 
ATOM   5981  C  CA  . HIS C  1 213 ? -78.129  -17.128 61.487  1.00 18.19  ? 212 HIS E CA  1 
ATOM   5982  C  C   . HIS C  1 213 ? -78.463  -16.639 60.079  1.00 17.09  ? 212 HIS E C   1 
ATOM   5983  O  O   . HIS C  1 213 ? -77.566  -16.486 59.291  1.00 17.06  ? 212 HIS E O   1 
ATOM   5984  C  CB  . HIS C  1 213 ? -77.272  -16.073 62.187  1.00 18.34  ? 212 HIS E CB  1 
ATOM   5985  C  CG  . HIS C  1 213 ? -77.014  -16.380 63.615  1.00 18.81  ? 212 HIS E CG  1 
ATOM   5986  N  ND1 . HIS C  1 213 ? -77.854  -15.937 64.597  1.00 20.29  ? 212 HIS E ND1 1 
ATOM   5987  C  CD2 . HIS C  1 213 ? -76.064  -17.129 64.225  1.00 19.68  ? 212 HIS E CD2 1 
ATOM   5988  C  CE1 . HIS C  1 213 ? -77.417  -16.377 65.773  1.00 20.89  ? 212 HIS E CE1 1 
ATOM   5989  N  NE2 . HIS C  1 213 ? -76.340  -17.138 65.575  1.00 17.94  ? 212 HIS E NE2 1 
ATOM   5990  N  N   . GLY C  1 214 ? -79.737  -16.287 59.856  1.00 17.77  ? 213 GLY E N   1 
ATOM   5991  C  CA  . GLY C  1 214 ? -80.175  -15.684 58.624  1.00 18.74  ? 213 GLY E CA  1 
ATOM   5992  C  C   . GLY C  1 214 ? -79.380  -14.428 58.344  1.00 17.97  ? 213 GLY E C   1 
ATOM   5993  O  O   . GLY C  1 214 ? -79.031  -13.683 59.268  1.00 16.74  ? 213 GLY E O   1 
ATOM   5994  N  N   . PHE C  1 215 ? -79.112  -14.191 57.058  1.00 17.76  ? 214 PHE E N   1 
ATOM   5995  C  CA  . PHE C  1 215 ? -78.231  -13.172 56.602  1.00 18.35  ? 214 PHE E CA  1 
ATOM   5996  C  C   . PHE C  1 215 ? -78.764  -12.672 55.258  1.00 19.90  ? 214 PHE E C   1 
ATOM   5997  O  O   . PHE C  1 215 ? -78.729  -13.428 54.255  1.00 18.30  ? 214 PHE E O   1 
ATOM   5998  C  CB  . PHE C  1 215 ? -76.843  -13.788 56.482  1.00 17.23  ? 214 PHE E CB  1 
ATOM   5999  C  CG  . PHE C  1 215 ? -75.714  -12.849 56.172  1.00 18.62  ? 214 PHE E CG  1 
ATOM   6000  C  CD1 . PHE C  1 215 ? -75.272  -11.936 57.117  1.00 19.25  ? 214 PHE E CD1 1 
ATOM   6001  C  CD2 . PHE C  1 215 ? -75.051  -12.915 54.954  1.00 18.39  ? 214 PHE E CD2 1 
ATOM   6002  C  CE1 . PHE C  1 215 ? -74.187  -11.117 56.837  1.00 19.69  ? 214 PHE E CE1 1 
ATOM   6003  C  CE2 . PHE C  1 215 ? -73.987  -12.076 54.672  1.00 19.12  ? 214 PHE E CE2 1 
ATOM   6004  C  CZ  . PHE C  1 215 ? -73.543  -11.196 55.620  1.00 20.21  ? 214 PHE E CZ  1 
ATOM   6005  N  N   . HIS C  1 216 ? -79.314  -11.451 55.241  1.00 18.30  ? 215 HIS E N   1 
ATOM   6006  C  CA  . HIS C  1 216 ? -80.024  -11.006 54.055  1.00 19.31  ? 215 HIS E CA  1 
ATOM   6007  C  C   . HIS C  1 216 ? -79.837  -9.517  53.791  1.00 18.90  ? 215 HIS E C   1 
ATOM   6008  O  O   . HIS C  1 216 ? -79.589  -8.727  54.737  1.00 19.39  ? 215 HIS E O   1 
ATOM   6009  C  CB  . HIS C  1 216 ? -81.528  -11.179 54.219  1.00 20.10  ? 215 HIS E CB  1 
ATOM   6010  C  CG  . HIS C  1 216 ? -81.972  -12.438 54.864  1.00 20.37  ? 215 HIS E CG  1 
ATOM   6011  N  ND1 . HIS C  1 216 ? -82.691  -12.411 56.023  1.00 21.88  ? 215 HIS E ND1 1 
ATOM   6012  C  CD2 . HIS C  1 216 ? -81.937  -13.719 54.449  1.00 21.36  ? 215 HIS E CD2 1 
ATOM   6013  C  CE1 . HIS C  1 216 ? -82.992  -13.651 56.360  1.00 23.69  ? 215 HIS E CE1 1 
ATOM   6014  N  NE2 . HIS C  1 216 ? -82.544  -14.480 55.406  1.00 21.07  ? 215 HIS E NE2 1 
ATOM   6015  N  N   . VAL C  1 217 ? -80.068  -9.140  52.517  1.00 18.36  ? 216 VAL E N   1 
ATOM   6016  C  CA  . VAL C  1 217 ? -80.175  -7.759  52.150  1.00 18.21  ? 216 VAL E CA  1 
ATOM   6017  C  C   . VAL C  1 217 ? -81.650  -7.379  52.186  1.00 19.03  ? 216 VAL E C   1 
ATOM   6018  O  O   . VAL C  1 217 ? -82.486  -8.012  51.539  1.00 19.54  ? 216 VAL E O   1 
ATOM   6019  C  CB  . VAL C  1 217 ? -79.530  -7.471  50.784  1.00 19.39  ? 216 VAL E CB  1 
ATOM   6020  C  CG1 . VAL C  1 217 ? -79.676  -6.010  50.406  1.00 19.41  ? 216 VAL E CG1 1 
ATOM   6021  C  CG2 . VAL C  1 217 ? -78.058  -7.859  50.779  1.00 19.71  ? 216 VAL E CG2 1 
ATOM   6022  N  N   . HIS C  1 218 ? -81.959  -6.358  52.982  1.00 16.80  ? 217 HIS E N   1 
ATOM   6023  C  CA  . HIS C  1 218 ? -83.313  -5.838  53.109  1.00 18.94  ? 217 HIS E CA  1 
ATOM   6024  C  C   . HIS C  1 218 ? -83.444  -4.613  52.191  1.00 19.88  ? 217 HIS E C   1 
ATOM   6025  O  O   . HIS C  1 218 ? -82.468  -4.030  51.775  1.00 20.88  ? 217 HIS E O   1 
ATOM   6026  C  CB  . HIS C  1 218 ? -83.673  -5.576  54.591  1.00 17.92  ? 217 HIS E CB  1 
ATOM   6027  C  CG  . HIS C  1 218 ? -83.914  -6.811  55.406  1.00 19.31  ? 217 HIS E CG  1 
ATOM   6028  N  ND1 . HIS C  1 218 ? -85.124  -7.026  56.050  1.00 18.89  ? 217 HIS E ND1 1 
ATOM   6029  C  CD2 . HIS C  1 218 ? -83.162  -7.914  55.655  1.00 18.59  ? 217 HIS E CD2 1 
ATOM   6030  C  CE1 . HIS C  1 218 ? -85.097  -8.202  56.667  1.00 20.41  ? 217 HIS E CE1 1 
ATOM   6031  N  NE2 . HIS C  1 218 ? -83.935  -8.789  56.414  1.00 20.32  ? 217 HIS E NE2 1 
ATOM   6032  N  N   . GLU C  1 219 ? -84.676  -4.234  51.872  1.00 21.84  ? 218 GLU E N   1 
ATOM   6033  C  CA  . GLU C  1 219 ? -84.936  -3.348  50.742  1.00 22.18  ? 218 GLU E CA  1 
ATOM   6034  C  C   . GLU C  1 219 ? -84.407  -1.925  51.007  1.00 21.58  ? 218 GLU E C   1 
ATOM   6035  O  O   . GLU C  1 219 ? -83.840  -1.304  50.106  1.00 22.86  ? 218 GLU E O   1 
ATOM   6036  C  CB  . GLU C  1 219 ? -86.444  -3.311  50.496  1.00 26.57  ? 218 GLU E CB  1 
ATOM   6037  C  CG  . GLU C  1 219 ? -86.805  -2.405  49.341  1.00 30.70  ? 218 GLU E CG  1 
ATOM   6038  C  CD  . GLU C  1 219 ? -88.263  -2.478  48.909  1.00 34.15  ? 218 GLU E CD  1 
ATOM   6039  O  OE1 . GLU C  1 219 ? -88.600  -1.790  47.929  1.00 35.83  ? 218 GLU E OE1 1 
ATOM   6040  O  OE2 . GLU C  1 219 ? -89.052  -3.172  49.581  1.00 33.13  ? 218 GLU E OE2 1 
ATOM   6041  N  N   . PHE C  1 220 ? -84.614  -1.394  52.217  1.00 20.16  ? 219 PHE E N   1 
ATOM   6042  C  CA  . PHE C  1 220 ? -84.322  0.022   52.492  1.00 21.00  ? 219 PHE E CA  1 
ATOM   6043  C  C   . PHE C  1 220 ? -83.065  0.163   53.339  1.00 21.54  ? 219 PHE E C   1 
ATOM   6044  O  O   . PHE C  1 220 ? -82.865  -0.571  54.316  1.00 24.08  ? 219 PHE E O   1 
ATOM   6045  C  CB  . PHE C  1 220 ? -85.499  0.710   53.178  1.00 21.60  ? 219 PHE E CB  1 
ATOM   6046  C  CG  . PHE C  1 220 ? -86.799  0.480   52.453  1.00 23.15  ? 219 PHE E CG  1 
ATOM   6047  C  CD1 . PHE C  1 220 ? -86.969  0.941   51.166  1.00 23.88  ? 219 PHE E CD1 1 
ATOM   6048  C  CD2 . PHE C  1 220 ? -87.825  -0.238  53.038  1.00 26.27  ? 219 PHE E CD2 1 
ATOM   6049  C  CE1 . PHE C  1 220 ? -88.149  0.704   50.482  1.00 27.36  ? 219 PHE E CE1 1 
ATOM   6050  C  CE2 . PHE C  1 220 ? -89.004  -0.482  52.346  1.00 26.26  ? 219 PHE E CE2 1 
ATOM   6051  C  CZ  . PHE C  1 220 ? -89.164  -0.003  51.074  1.00 25.77  ? 219 PHE E CZ  1 
ATOM   6052  N  N   . GLY C  1 221 ? -82.261  1.167   52.987  1.00 21.56  ? 220 GLY E N   1 
ATOM   6053  C  CA  . GLY C  1 221 ? -81.113  1.609   53.776  1.00 21.52  ? 220 GLY E CA  1 
ATOM   6054  C  C   . GLY C  1 221 ? -81.532  2.660   54.785  1.00 22.19  ? 220 GLY E C   1 
ATOM   6055  O  O   . GLY C  1 221 ? -80.942  3.762   54.875  1.00 20.89  ? 220 GLY E O   1 
ATOM   6056  N  N   . ASP C  1 222 ? -82.592  2.327   55.516  1.00 22.11  ? 221 ASP E N   1 
ATOM   6057  C  CA  . ASP C  1 222 ? -83.247  3.234   56.452  1.00 22.97  ? 221 ASP E CA  1 
ATOM   6058  C  C   . ASP C  1 222 ? -83.121  2.651   57.860  1.00 22.86  ? 221 ASP E C   1 
ATOM   6059  O  O   . ASP C  1 222 ? -83.766  1.672   58.155  1.00 23.53  ? 221 ASP E O   1 
ATOM   6060  C  CB  . ASP C  1 222 ? -84.712  3.401   56.074  1.00 21.89  ? 221 ASP E CB  1 
ATOM   6061  C  CG  . ASP C  1 222 ? -85.512  4.370   56.933  1.00 24.26  ? 221 ASP E CG  1 
ATOM   6062  O  OD1 . ASP C  1 222 ? -86.520  4.839   56.426  1.00 25.96  ? 221 ASP E OD1 1 
ATOM   6063  O  OD2 . ASP C  1 222 ? -85.119  4.655   58.092  1.00 25.42  ? 221 ASP E OD2 1 
ATOM   6064  N  N   . ASN C  1 223 ? -82.263  3.242   58.681  1.00 23.73  ? 222 ASN E N   1 
ATOM   6065  C  CA  . ASN C  1 223 ? -82.055  2.744   60.044  1.00 27.54  ? 222 ASN E CA  1 
ATOM   6066  C  C   . ASN C  1 223 ? -82.581  3.820   61.023  1.00 25.39  ? 222 ASN E C   1 
ATOM   6067  O  O   . ASN C  1 223 ? -82.139  3.874   62.141  1.00 25.29  ? 222 ASN E O   1 
ATOM   6068  C  CB  . ASN C  1 223 ? -80.643  2.112   60.277  1.00 29.47  ? 222 ASN E CB  1 
ATOM   6069  C  CG  A ASN C  1 223 ? -80.219  1.111   59.205  0.60 27.76  ? 222 ASN E CG  1 
ATOM   6070  C  CG  B ASN C  1 223 ? -80.059  2.472   61.625  0.40 32.84  ? 222 ASN E CG  1 
ATOM   6071  O  OD1 A ASN C  1 223 ? -81.020  0.431   58.564  0.60 24.74  ? 222 ASN E OD1 1 
ATOM   6072  O  OD1 B ASN C  1 223 ? -79.926  1.589   62.472  0.40 37.01  ? 222 ASN E OD1 1 
ATOM   6073  N  ND2 A ASN C  1 223 ? -78.925  0.842   59.185  0.60 25.55  ? 222 ASN E ND2 1 
ATOM   6074  N  ND2 B ASN C  1 223 ? -79.601  3.698   61.810  0.40 39.00  ? 222 ASN E ND2 1 
ATOM   6075  N  N   . THR C  1 224 ? -83.579  4.621   60.607  1.00 23.66  ? 223 THR E N   1 
ATOM   6076  C  CA  . THR C  1 224 ? -84.159  5.672   61.469  1.00 25.91  ? 223 THR E CA  1 
ATOM   6077  C  C   . THR C  1 224 ? -84.804  5.052   62.714  1.00 27.79  ? 223 THR E C   1 
ATOM   6078  O  O   . THR C  1 224 ? -84.728  5.638   63.753  1.00 29.44  ? 223 THR E O   1 
ATOM   6079  C  CB  . THR C  1 224 ? -85.183  6.546   60.736  1.00 24.94  ? 223 THR E CB  1 
ATOM   6080  O  OG1 . THR C  1 224 ? -86.213  5.723   60.182  1.00 25.70  ? 223 THR E OG1 1 
ATOM   6081  C  CG2 . THR C  1 224 ? -84.549  7.369   59.635  1.00 25.44  ? 223 THR E CG2 1 
ATOM   6082  N  N   . ALA C  1 225 ? -85.400  3.852   62.603  1.00 31.25  ? 224 ALA E N   1 
ATOM   6083  C  CA  . ALA C  1 225 ? -85.928  3.116   63.767  1.00 29.88  ? 224 ALA E CA  1 
ATOM   6084  C  C   . ALA C  1 225 ? -85.169  1.798   63.925  1.00 31.53  ? 224 ALA E C   1 
ATOM   6085  O  O   . ALA C  1 225 ? -85.756  0.744   64.072  1.00 37.32  ? 224 ALA E O   1 
ATOM   6086  C  CB  . ALA C  1 225 ? -87.412  2.876   63.599  1.00 31.10  ? 224 ALA E CB  1 
ATOM   6087  N  N   . GLY C  1 226 ? -83.846  1.861   63.838  1.00 29.53  ? 225 GLY E N   1 
ATOM   6088  C  CA  . GLY C  1 226 ? -83.025  0.674   63.919  1.00 30.19  ? 225 GLY E CA  1 
ATOM   6089  C  C   . GLY C  1 226 ? -83.292  -0.247  62.731  1.00 30.29  ? 225 GLY E C   1 
ATOM   6090  O  O   . GLY C  1 226 ? -83.703  0.202   61.654  1.00 28.45  ? 225 GLY E O   1 
ATOM   6091  N  N   . CYS C  1 227 ? -83.091  -1.545  62.943  1.00 26.86  ? 226 CYS E N   1 
ATOM   6092  C  CA  . CYS C  1 227 ? -83.171  -2.529  61.862  1.00 26.74  ? 226 CYS E CA  1 
ATOM   6093  C  C   . CYS C  1 227 ? -84.613  -2.674  61.342  1.00 25.75  ? 226 CYS E C   1 
ATOM   6094  O  O   . CYS C  1 227 ? -84.816  -3.098  60.199  1.00 23.26  ? 226 CYS E O   1 
ATOM   6095  C  CB  . CYS C  1 227 ? -82.586  -3.854  62.339  1.00 27.99  ? 226 CYS E CB  1 
ATOM   6096  S  SG  . CYS C  1 227 ? -80.853  -3.690  62.842  1.00 31.82  ? 226 CYS E SG  1 
ATOM   6097  N  N   . THR C  1 228 ? -85.616  -2.299  62.148  1.00 24.03  ? 227 THR E N   1 
ATOM   6098  C  CA  . THR C  1 228 ? -87.006  -2.468  61.737  1.00 27.75  ? 227 THR E CA  1 
ATOM   6099  C  C   . THR C  1 228 ? -87.340  -1.633  60.496  1.00 25.30  ? 227 THR E C   1 
ATOM   6100  O  O   . THR C  1 228 ? -88.106  -2.093  59.644  1.00 26.89  ? 227 THR E O   1 
ATOM   6101  C  CB  . THR C  1 228 ? -88.014  -2.086  62.825  1.00 32.59  ? 227 THR E CB  1 
ATOM   6102  O  OG1 . THR C  1 228 ? -87.577  -2.642  64.054  1.00 41.64  ? 227 THR E OG1 1 
ATOM   6103  C  CG2 . THR C  1 228 ? -89.393  -2.620  62.515  1.00 34.83  ? 227 THR E CG2 1 
ATOM   6104  N  N   . SER C  1 229 ? -86.732  -0.450  60.357  1.00 22.38  ? 228 SER E N   1 
ATOM   6105  C  CA  . SER C  1 229 ? -87.098  0.433   59.248  1.00 24.80  ? 228 SER E CA  1 
ATOM   6106  C  C   . SER C  1 229 ? -86.446  -0.005  57.927  1.00 23.29  ? 228 SER E C   1 
ATOM   6107  O  O   . SER C  1 229 ? -86.727  0.579   56.901  1.00 23.71  ? 228 SER E O   1 
ATOM   6108  C  CB  . SER C  1 229 ? -86.839  1.877   59.577  1.00 25.22  ? 228 SER E CB  1 
ATOM   6109  O  OG  . SER C  1 229 ? -85.616  2.027   60.225  1.00 26.55  ? 228 SER E OG  1 
ATOM   6110  N  N   . ALA C  1 230 ? -85.660  -1.096  57.933  1.00 22.49  ? 229 ALA E N   1 
ATOM   6111  C  CA  . ALA C  1 230 ? -85.024  -1.588  56.696  1.00 22.32  ? 229 ALA E CA  1 
ATOM   6112  C  C   . ALA C  1 230 ? -86.042  -2.270  55.775  1.00 21.63  ? 229 ALA E C   1 
ATOM   6113  O  O   . ALA C  1 230 ? -85.747  -2.561  54.628  1.00 22.73  ? 229 ALA E O   1 
ATOM   6114  C  CB  . ALA C  1 230 ? -83.892  -2.528  57.015  1.00 22.21  ? 229 ALA E CB  1 
ATOM   6115  N  N   . GLY C  1 231 ? -87.232  -2.565  56.304  1.00 21.75  ? 230 GLY E N   1 
ATOM   6116  C  CA  . GLY C  1 231 ? -88.307  -3.160  55.544  1.00 22.18  ? 230 GLY E CA  1 
ATOM   6117  C  C   . GLY C  1 231 ? -88.057  -4.647  55.296  1.00 21.56  ? 230 GLY E C   1 
ATOM   6118  O  O   . GLY C  1 231 ? -87.274  -5.272  56.019  1.00 20.87  ? 230 GLY E O   1 
ATOM   6119  N  N   . PRO C  1 232 ? -88.735  -5.232  54.289  1.00 25.06  ? 231 PRO E N   1 
ATOM   6120  C  CA  . PRO C  1 232 ? -88.626  -6.662  54.002  1.00 23.72  ? 231 PRO E CA  1 
ATOM   6121  C  C   . PRO C  1 232 ? -87.372  -6.962  53.182  1.00 22.67  ? 231 PRO E C   1 
ATOM   6122  O  O   . PRO C  1 232 ? -86.570  -6.091  52.886  1.00 22.01  ? 231 PRO E O   1 
ATOM   6123  C  CB  . PRO C  1 232 ? -89.915  -6.957  53.224  1.00 25.44  ? 231 PRO E CB  1 
ATOM   6124  C  CG  . PRO C  1 232 ? -90.159  -5.664  52.451  1.00 25.68  ? 231 PRO E CG  1 
ATOM   6125  C  CD  . PRO C  1 232 ? -89.664  -4.559  53.369  1.00 24.57  ? 231 PRO E CD  1 
ATOM   6126  N  N   . HIS C  1 233 ? -87.197  -8.233  52.835  1.00 22.26  ? 232 HIS E N   1 
ATOM   6127  C  CA  . HIS C  1 233 ? -86.068  -8.628  52.007  1.00 21.20  ? 232 HIS E CA  1 
ATOM   6128  C  C   . HIS C  1 233 ? -86.119  -7.866  50.682  1.00 21.25  ? 232 HIS E C   1 
ATOM   6129  O  O   . HIS C  1 233 ? -87.181  -7.594  50.169  1.00 22.86  ? 232 HIS E O   1 
ATOM   6130  C  CB  . HIS C  1 233 ? -86.087  -10.151 51.799  1.00 22.37  ? 232 HIS E CB  1 
ATOM   6131  C  CG  . HIS C  1 233 ? -85.840  -10.909 53.054  1.00 23.66  ? 232 HIS E CG  1 
ATOM   6132  N  ND1 . HIS C  1 233 ? -85.720  -12.279 53.095  1.00 23.67  ? 232 HIS E ND1 1 
ATOM   6133  C  CD2 . HIS C  1 233 ? -85.640  -10.470 54.318  1.00 25.02  ? 232 HIS E CD2 1 
ATOM   6134  C  CE1 . HIS C  1 233 ? -85.497  -12.649 54.339  1.00 24.31  ? 232 HIS E CE1 1 
ATOM   6135  N  NE2 . HIS C  1 233 ? -85.387  -11.549 55.107  1.00 25.96  ? 232 HIS E NE2 1 
ATOM   6136  N  N   . PHE C  1 234 ? -84.946  -7.549  50.133  1.00 19.82  ? 233 PHE E N   1 
ATOM   6137  C  CA  . PHE C  1 234 ? -84.828  -6.932  48.854  1.00 20.34  ? 233 PHE E CA  1 
ATOM   6138  C  C   . PHE C  1 234 ? -85.288  -7.945  47.807  1.00 20.88  ? 233 PHE E C   1 
ATOM   6139  O  O   . PHE C  1 234 ? -84.698  -9.033  47.699  1.00 20.66  ? 233 PHE E O   1 
ATOM   6140  C  CB  . PHE C  1 234 ? -83.388  -6.461  48.629  1.00 20.41  ? 233 PHE E CB  1 
ATOM   6141  C  CG  . PHE C  1 234 ? -83.122  -5.863  47.272  1.00 21.77  ? 233 PHE E CG  1 
ATOM   6142  C  CD1 . PHE C  1 234 ? -81.984  -6.209  46.565  1.00 23.16  ? 233 PHE E CD1 1 
ATOM   6143  C  CD2 . PHE C  1 234 ? -84.011  -4.956  46.703  1.00 23.90  ? 233 PHE E CD2 1 
ATOM   6144  C  CE1 . PHE C  1 234 ? -81.729  -5.666  45.313  1.00 23.87  ? 233 PHE E CE1 1 
ATOM   6145  C  CE2 . PHE C  1 234 ? -83.770  -4.429  45.445  1.00 23.05  ? 233 PHE E CE2 1 
ATOM   6146  C  CZ  . PHE C  1 234 ? -82.624  -4.769  44.763  1.00 23.26  ? 233 PHE E CZ  1 
ATOM   6147  N  N   . ASN C  1 235 ? -86.377  -7.621  47.092  1.00 21.11  ? 234 ASN E N   1 
ATOM   6148  C  CA  . ASN C  1 235 ? -87.115  -8.614  46.293  1.00 23.08  ? 234 ASN E CA  1 
ATOM   6149  C  C   . ASN C  1 235 ? -87.681  -7.953  45.038  1.00 26.77  ? 234 ASN E C   1 
ATOM   6150  O  O   . ASN C  1 235 ? -88.886  -7.894  44.829  1.00 26.06  ? 234 ASN E O   1 
ATOM   6151  C  CB  . ASN C  1 235 ? -88.206  -9.277  47.130  1.00 23.67  ? 234 ASN E CB  1 
ATOM   6152  C  CG  . ASN C  1 235 ? -88.956  -10.391 46.422  1.00 24.84  ? 234 ASN E CG  1 
ATOM   6153  O  OD1 . ASN C  1 235 ? -88.439  -11.031 45.513  1.00 24.83  ? 234 ASN E OD1 1 
ATOM   6154  N  ND2 . ASN C  1 235 ? -90.168  -10.654 46.880  1.00 24.99  ? 234 ASN E ND2 1 
ATOM   6155  N  N   . PRO C  1 236 ? -86.827  -7.428  44.148  1.00 28.16  ? 235 PRO E N   1 
ATOM   6156  C  CA  . PRO C  1 236 ? -87.333  -6.719  42.978  1.00 30.32  ? 235 PRO E CA  1 
ATOM   6157  C  C   . PRO C  1 236 ? -88.066  -7.602  41.953  1.00 33.56  ? 235 PRO E C   1 
ATOM   6158  O  O   . PRO C  1 236 ? -88.775  -7.068  41.133  1.00 35.36  ? 235 PRO E O   1 
ATOM   6159  C  CB  . PRO C  1 236 ? -86.064  -6.084  42.405  1.00 27.74  ? 235 PRO E CB  1 
ATOM   6160  C  CG  . PRO C  1 236 ? -84.959  -7.032  42.830  1.00 26.57  ? 235 PRO E CG  1 
ATOM   6161  C  CD  . PRO C  1 236 ? -85.365  -7.469  44.221  1.00 25.96  ? 235 PRO E CD  1 
ATOM   6162  N  N   . LEU C  1 237 ? -87.929  -8.927  42.024  1.00 34.88  ? 236 LEU E N   1 
ATOM   6163  C  CA  . LEU C  1 237 ? -88.624  -9.825  41.082  1.00 32.82  ? 236 LEU E CA  1 
ATOM   6164  C  C   . LEU C  1 237 ? -89.890  -10.407 41.712  1.00 34.38  ? 236 LEU E C   1 
ATOM   6165  O  O   . LEU C  1 237 ? -90.524  -11.258 41.110  1.00 34.39  ? 236 LEU E O   1 
ATOM   6166  C  CB  . LEU C  1 237 ? -87.656  -10.933 40.660  1.00 35.81  ? 236 LEU E CB  1 
ATOM   6167  C  CG  . LEU C  1 237 ? -86.425  -10.473 39.881  1.00 40.61  ? 236 LEU E CG  1 
ATOM   6168  C  CD1 . LEU C  1 237 ? -85.480  -11.635 39.604  1.00 43.61  ? 236 LEU E CD1 1 
ATOM   6169  C  CD2 . LEU C  1 237 ? -86.827  -9.814  38.576  1.00 45.03  ? 236 LEU E CD2 1 
ATOM   6170  N  N   . SER C  1 238 ? -90.241  -9.968  42.933  1.00 33.75  ? 237 SER E N   1 
ATOM   6171  C  CA  . SER C  1 238 ? -91.454  -10.378 43.620  1.00 35.52  ? 237 SER E CA  1 
ATOM   6172  C  C   . SER C  1 238 ? -91.558  -11.908 43.663  1.00 36.79  ? 237 SER E C   1 
ATOM   6173  O  O   . SER C  1 238 ? -92.576  -12.466 43.282  1.00 36.63  ? 237 SER E O   1 
ATOM   6174  C  CB  . SER C  1 238 ? -92.688  -9.770  42.964  1.00 40.87  ? 237 SER E CB  1 
ATOM   6175  O  OG  . SER C  1 238 ? -92.766  -8.373  43.219  1.00 41.59  ? 237 SER E OG  1 
ATOM   6176  N  N   . ARG C  1 239 ? -90.496  -12.568 44.131  1.00 33.24  ? 238 ARG E N   1 
ATOM   6177  C  CA  . ARG C  1 239 ? -90.444  -13.994 44.292  1.00 31.00  ? 238 ARG E CA  1 
ATOM   6178  C  C   . ARG C  1 239 ? -90.632  -14.337 45.772  1.00 29.80  ? 238 ARG E C   1 
ATOM   6179  O  O   . ARG C  1 239 ? -90.678  -13.452 46.627  1.00 26.15  ? 238 ARG E O   1 
ATOM   6180  C  CB  . ARG C  1 239 ? -89.138  -14.507 43.687  1.00 35.75  ? 238 ARG E CB  1 
ATOM   6181  C  CG  . ARG C  1 239 ? -89.141  -14.436 42.164  1.00 40.10  ? 238 ARG E CG  1 
ATOM   6182  C  CD  . ARG C  1 239 ? -88.000  -15.179 41.513  1.00 44.56  ? 238 ARG E CD  1 
ATOM   6183  N  NE  . ARG C  1 239 ? -87.978  -14.942 40.075  1.00 47.83  ? 238 ARG E NE  1 
ATOM   6184  C  CZ  . ARG C  1 239 ? -87.011  -15.353 39.253  1.00 51.64  ? 238 ARG E CZ  1 
ATOM   6185  N  NH1 . ARG C  1 239 ? -87.009  -14.975 37.987  1.00 53.12  ? 238 ARG E NH1 1 
ATOM   6186  N  NH2 . ARG C  1 239 ? -86.051  -16.144 39.691  1.00 51.48  ? 238 ARG E NH2 1 
ATOM   6187  N  N   . LYS C  1 240 ? -90.819  -15.632 46.043  1.00 27.54  ? 239 LYS E N   1 
ATOM   6188  C  CA  . LYS C  1 240 ? -90.873  -16.145 47.390  1.00 29.68  ? 239 LYS E CA  1 
ATOM   6189  C  C   . LYS C  1 240 ? -89.436  -16.246 47.918  1.00 27.19  ? 239 LYS E C   1 
ATOM   6190  O  O   . LYS C  1 240 ? -88.497  -16.377 47.150  1.00 23.35  ? 239 LYS E O   1 
ATOM   6191  C  CB  . LYS C  1 240 ? -91.528  -17.539 47.433  1.00 34.90  ? 239 LYS E CB  1 
ATOM   6192  C  CG  . LYS C  1 240 ? -93.011  -17.644 47.080  1.00 43.32  ? 239 LYS E CG  1 
ATOM   6193  C  CD  . LYS C  1 240 ? -93.859  -16.383 47.299  1.00 51.49  ? 239 LYS E CD  1 
ATOM   6194  C  CE  . LYS C  1 240 ? -94.205  -15.659 46.000  1.00 60.34  ? 239 LYS E CE  1 
ATOM   6195  N  NZ  . LYS C  1 240 ? -94.775  -14.299 46.208  1.00 62.18  ? 239 LYS E NZ  1 
ATOM   6196  N  N   . HIS C  1 241 ? -89.295  -16.238 49.244  1.00 25.08  ? 240 HIS E N   1 
ATOM   6197  C  CA  . HIS C  1 241 ? -88.006  -16.441 49.908  1.00 23.33  ? 240 HIS E CA  1 
ATOM   6198  C  C   . HIS C  1 241 ? -87.442  -17.834 49.582  1.00 25.61  ? 240 HIS E C   1 
ATOM   6199  O  O   . HIS C  1 241 ? -88.166  -18.815 49.547  1.00 24.86  ? 240 HIS E O   1 
ATOM   6200  C  CB  . HIS C  1 241 ? -88.176  -16.273 51.427  1.00 22.75  ? 240 HIS E CB  1 
ATOM   6201  C  CG  . HIS C  1 241 ? -86.913  -16.460 52.204  1.00 22.90  ? 240 HIS E CG  1 
ATOM   6202  N  ND1 . HIS C  1 241 ? -85.869  -15.547 52.182  1.00 23.78  ? 240 HIS E ND1 1 
ATOM   6203  C  CD2 . HIS C  1 241 ? -86.495  -17.495 52.956  1.00 21.37  ? 240 HIS E CD2 1 
ATOM   6204  C  CE1 . HIS C  1 241 ? -84.898  -15.999 52.940  1.00 25.22  ? 240 HIS E CE1 1 
ATOM   6205  N  NE2 . HIS C  1 241 ? -85.252  -17.190 53.420  1.00 22.04  ? 240 HIS E NE2 1 
ATOM   6206  N  N   . GLY C  1 242 ? -86.125  -17.918 49.448  1.00 21.85  ? 241 GLY E N   1 
ATOM   6207  C  CA  . GLY C  1 242 ? -85.471  -19.174 49.269  1.00 23.29  ? 241 GLY E CA  1 
ATOM   6208  C  C   . GLY C  1 242 ? -84.053  -19.094 49.746  1.00 23.20  ? 241 GLY E C   1 
ATOM   6209  O  O   . GLY C  1 242 ? -83.647  -18.081 50.278  1.00 25.18  ? 241 GLY E O   1 
ATOM   6210  N  N   . GLY C  1 243 ? -83.297  -20.175 49.547  1.00 22.37  ? 242 GLY E N   1 
ATOM   6211  C  CA  . GLY C  1 243 ? -81.888  -20.150 49.785  1.00 23.57  ? 242 GLY E CA  1 
ATOM   6212  C  C   . GLY C  1 243 ? -81.172  -19.570 48.573  1.00 23.46  ? 242 GLY E C   1 
ATOM   6213  O  O   . GLY C  1 243 ? -81.739  -19.508 47.474  1.00 24.75  ? 242 GLY E O   1 
ATOM   6214  N  N   . PRO C  1 244 ? -79.913  -19.128 48.738  1.00 23.98  ? 243 PRO E N   1 
ATOM   6215  C  CA  . PRO C  1 244 ? -79.188  -18.475 47.656  1.00 26.78  ? 243 PRO E CA  1 
ATOM   6216  C  C   . PRO C  1 244 ? -79.022  -19.342 46.392  1.00 28.52  ? 243 PRO E C   1 
ATOM   6217  O  O   . PRO C  1 244 ? -78.909  -18.794 45.298  1.00 24.41  ? 243 PRO E O   1 
ATOM   6218  C  CB  . PRO C  1 244 ? -77.819  -18.119 48.266  1.00 25.49  ? 243 PRO E CB  1 
ATOM   6219  C  CG  . PRO C  1 244 ? -77.719  -18.923 49.540  1.00 24.42  ? 243 PRO E CG  1 
ATOM   6220  C  CD  . PRO C  1 244 ? -79.138  -19.200 49.977  1.00 24.80  ? 243 PRO E CD  1 
ATOM   6221  N  N   . LYS C  1 245 ? -79.012  -20.668 46.551  1.00 29.83  ? 244 LYS E N   1 
ATOM   6222  C  CA  . LYS C  1 245 ? -78.835  -21.595 45.432  1.00 34.60  ? 244 LYS E CA  1 
ATOM   6223  C  C   . LYS C  1 245 ? -80.152  -21.906 44.707  1.00 33.62  ? 244 LYS E C   1 
ATOM   6224  O  O   . LYS C  1 245 ? -80.117  -22.558 43.685  1.00 37.49  ? 244 LYS E O   1 
ATOM   6225  C  CB  . LYS C  1 245 ? -78.160  -22.868 45.947  1.00 40.98  ? 244 LYS E CB  1 
ATOM   6226  C  CG  . LYS C  1 245 ? -76.696  -22.668 46.308  1.00 46.70  ? 244 LYS E CG  1 
ATOM   6227  C  CD  . LYS C  1 245 ? -76.097  -23.792 47.131  1.00 60.33  ? 244 LYS E CD  1 
ATOM   6228  C  CE  . LYS C  1 245 ? -75.817  -25.051 46.328  1.00 69.61  ? 244 LYS E CE  1 
ATOM   6229  N  NZ  . LYS C  1 245 ? -76.930  -26.028 46.423  1.00 72.19  ? 244 LYS E NZ  1 
ATOM   6230  N  N   . ASP C  1 246 ? -81.295  -21.435 45.215  1.00 30.90  ? 245 ASP E N   1 
ATOM   6231  C  CA  . ASP C  1 246 ? -82.607  -21.638 44.591  1.00 33.19  ? 245 ASP E CA  1 
ATOM   6232  C  C   . ASP C  1 246 ? -82.858  -20.613 43.481  1.00 36.30  ? 245 ASP E C   1 
ATOM   6233  O  O   . ASP C  1 246 ? -82.392  -19.467 43.552  1.00 32.21  ? 245 ASP E O   1 
ATOM   6234  C  CB  . ASP C  1 246 ? -83.728  -21.546 45.633  1.00 35.00  ? 245 ASP E CB  1 
ATOM   6235  C  CG  . ASP C  1 246 ? -83.644  -22.613 46.717  1.00 39.01  ? 245 ASP E CG  1 
ATOM   6236  O  OD1 . ASP C  1 246 ? -84.055  -22.343 47.875  1.00 38.38  ? 245 ASP E OD1 1 
ATOM   6237  O  OD2 . ASP C  1 246 ? -83.149  -23.704 46.404  1.00 40.88  ? 245 ASP E OD2 1 
ATOM   6238  N  N   . GLU C  1 247 ? -83.669  -20.997 42.489  1.00 36.35  ? 246 GLU E N   1 
ATOM   6239  C  CA  . GLU C  1 247 ? -84.127  -20.047 41.458  1.00 39.47  ? 246 GLU E CA  1 
ATOM   6240  C  C   . GLU C  1 247 ? -85.215  -19.146 42.065  1.00 33.71  ? 246 GLU E C   1 
ATOM   6241  O  O   . GLU C  1 247 ? -85.226  -17.914 41.865  1.00 36.45  ? 246 GLU E O   1 
ATOM   6242  C  CB  . GLU C  1 247 ? -84.630  -20.789 40.212  1.00 49.01  ? 246 GLU E CB  1 
ATOM   6243  C  CG  . GLU C  1 247 ? -83.945  -20.353 38.919  1.00 64.74  ? 246 GLU E CG  1 
ATOM   6244  C  CD  . GLU C  1 247 ? -84.579  -19.185 38.170  1.00 77.13  ? 246 GLU E CD  1 
ATOM   6245  O  OE1 . GLU C  1 247 ? -85.789  -19.276 37.850  1.00 89.04  ? 246 GLU E OE1 1 
ATOM   6246  O  OE2 . GLU C  1 247 ? -83.858  -18.192 37.882  1.00 82.85  ? 246 GLU E OE2 1 
ATOM   6247  N  N   . GLU C  1 248 ? -86.121  -19.763 42.829  1.00 29.34  ? 247 GLU E N   1 
ATOM   6248  C  CA  . GLU C  1 248 ? -87.109  -19.046 43.608  1.00 31.52  ? 247 GLU E CA  1 
ATOM   6249  C  C   . GLU C  1 248 ? -86.440  -18.539 44.908  1.00 27.60  ? 247 GLU E C   1 
ATOM   6250  O  O   . GLU C  1 248 ? -86.321  -19.258 45.890  1.00 28.42  ? 247 GLU E O   1 
ATOM   6251  C  CB  . GLU C  1 248 ? -88.330  -19.941 43.849  1.00 33.05  ? 247 GLU E CB  1 
ATOM   6252  C  CG  . GLU C  1 248 ? -89.546  -19.191 44.388  1.00 36.32  ? 247 GLU E CG  1 
ATOM   6253  C  CD  . GLU C  1 248 ? -90.280  -18.306 43.391  1.00 38.30  ? 247 GLU E CD  1 
ATOM   6254  O  OE1 . GLU C  1 248 ? -91.138  -17.508 43.816  1.00 35.34  ? 247 GLU E OE1 1 
ATOM   6255  O  OE2 . GLU C  1 248 ? -89.975  -18.390 42.201  1.00 46.90  ? 247 GLU E OE2 1 
ATOM   6256  N  N   . ARG C  1 249 ? -85.961  -17.293 44.872  1.00 27.08  ? 248 ARG E N   1 
ATOM   6257  C  CA  . ARG C  1 249 ? -85.374  -16.579 46.029  1.00 24.41  ? 248 ARG E CA  1 
ATOM   6258  C  C   . ARG C  1 249 ? -85.587  -15.084 45.809  1.00 26.06  ? 248 ARG E C   1 
ATOM   6259  O  O   . ARG C  1 249 ? -85.822  -14.637 44.703  1.00 25.91  ? 248 ARG E O   1 
ATOM   6260  C  CB  . ARG C  1 249 ? -83.883  -16.869 46.172  1.00 23.77  ? 248 ARG E CB  1 
ATOM   6261  C  CG  . ARG C  1 249 ? -83.088  -16.547 44.913  1.00 24.96  ? 248 ARG E CG  1 
ATOM   6262  C  CD  . ARG C  1 249 ? -81.595  -16.614 45.075  1.00 24.59  ? 248 ARG E CD  1 
ATOM   6263  N  NE  . ARG C  1 249 ? -81.060  -15.446 45.765  1.00 25.32  ? 248 ARG E NE  1 
ATOM   6264  C  CZ  . ARG C  1 249 ? -79.768  -15.143 45.849  1.00 24.00  ? 248 ARG E CZ  1 
ATOM   6265  N  NH1 . ARG C  1 249 ? -79.398  -13.938 46.264  1.00 21.35  ? 248 ARG E NH1 1 
ATOM   6266  N  NH2 . ARG C  1 249 ? -78.849  -16.038 45.517  1.00 23.96  ? 248 ARG E NH2 1 
ATOM   6267  N  N   . HIS C  1 250 ? -85.549  -14.334 46.901  1.00 22.59  ? 249 HIS E N   1 
ATOM   6268  C  CA  . HIS C  1 250 ? -85.361  -12.904 46.859  1.00 23.11  ? 249 HIS E CA  1 
ATOM   6269  C  C   . HIS C  1 250 ? -83.931  -12.598 46.411  1.00 22.75  ? 249 HIS E C   1 
ATOM   6270  O  O   . HIS C  1 250 ? -83.005  -13.326 46.735  1.00 22.96  ? 249 HIS E O   1 
ATOM   6271  C  CB  . HIS C  1 250 ? -85.617  -12.308 48.245  1.00 22.39  ? 249 HIS E CB  1 
ATOM   6272  C  CG  . HIS C  1 250 ? -86.956  -12.634 48.810  1.00 22.48  ? 249 HIS E CG  1 
ATOM   6273  N  ND1 . HIS C  1 250 ? -87.192  -12.766 50.174  1.00 21.25  ? 249 HIS E ND1 1 
ATOM   6274  C  CD2 . HIS C  1 250 ? -88.145  -12.801 48.202  1.00 22.45  ? 249 HIS E CD2 1 
ATOM   6275  C  CE1 . HIS C  1 250 ? -88.479  -12.964 50.372  1.00 22.30  ? 249 HIS E CE1 1 
ATOM   6276  N  NE2 . HIS C  1 250 ? -89.082  -13.014 49.176  1.00 24.64  ? 249 HIS E NE2 1 
ATOM   6277  N  N   . VAL C  1 251 ? -83.731  -11.465 45.733  1.00 21.69  ? 250 VAL E N   1 
ATOM   6278  C  CA  . VAL C  1 251 ? -82.383  -11.013 45.464  1.00 21.46  ? 250 VAL E CA  1 
ATOM   6279  C  C   . VAL C  1 251 ? -81.580  -10.940 46.769  1.00 20.76  ? 250 VAL E C   1 
ATOM   6280  O  O   . VAL C  1 251 ? -80.395  -11.303 46.794  1.00 22.29  ? 250 VAL E O   1 
ATOM   6281  C  CB  . VAL C  1 251 ? -82.346  -9.697  44.674  1.00 22.41  ? 250 VAL E CB  1 
ATOM   6282  C  CG1 . VAL C  1 251 ? -80.954  -9.089  44.674  1.00 24.04  ? 250 VAL E CG1 1 
ATOM   6283  C  CG2 . VAL C  1 251 ? -82.821  -9.930  43.245  1.00 23.90  ? 250 VAL E CG2 1 
ATOM   6284  N  N   . GLY C  1 252 ? -82.215  -10.506 47.861  1.00 20.76  ? 251 GLY E N   1 
ATOM   6285  C  CA  . GLY C  1 252 ? -81.475  -10.337 49.130  1.00 21.95  ? 251 GLY E CA  1 
ATOM   6286  C  C   . GLY C  1 252 ? -81.271  -11.607 49.958  1.00 22.49  ? 251 GLY E C   1 
ATOM   6287  O  O   . GLY C  1 252 ? -80.721  -11.515 51.071  1.00 22.35  ? 251 GLY E O   1 
ATOM   6288  N  N   A SER C  1 253 ? -81.742  -12.771 49.492  0.40 22.46  ? 252 SER E N   1 
ATOM   6289  C  CA  A SER C  1 253 ? -81.719  -14.009 50.311  0.40 23.43  ? 252 SER E CA  1 
ATOM   6290  C  C   A SER C  1 253 ? -80.350  -14.704 50.219  0.40 22.14  ? 252 SER E C   1 
ATOM   6291  O  O   A SER C  1 253 ? -80.194  -15.630 49.419  0.40 22.11  ? 252 SER E O   1 
ATOM   6292  C  CB  A SER C  1 253 ? -82.890  -14.922 49.926  0.40 24.89  ? 252 SER E CB  1 
ATOM   6293  O  OG  A SER C  1 253 ? -84.137  -14.478 50.503  0.40 29.97  ? 252 SER E OG  1 
ATOM   6294  N  N   B ASP C  1 253 ? -81.667  -12.765 49.405  0.60 19.64  ? 252 ASP E N   1 
ATOM   6295  C  CA  B ASP C  1 253 ? -81.570  -14.041 50.104  0.60 19.63  ? 252 ASP E CA  1 
ATOM   6296  C  C   B ASP C  1 253 ? -80.152  -14.585 50.047  0.60 19.91  ? 252 ASP E C   1 
ATOM   6297  O  O   B ASP C  1 253 ? -79.753  -15.288 49.120  0.60 20.95  ? 252 ASP E O   1 
ATOM   6298  C  CB  B ASP C  1 253 ? -82.551  -15.064 49.545  0.60 18.82  ? 252 ASP E CB  1 
ATOM   6299  C  CG  B ASP C  1 253 ? -83.951  -14.656 49.901  0.60 19.83  ? 252 ASP E CG  1 
ATOM   6300  O  OD1 B ASP C  1 253 ? -84.062  -13.745 50.812  0.60 23.65  ? 252 ASP E OD1 1 
ATOM   6301  O  OD2 B ASP C  1 253 ? -84.883  -15.223 49.338  0.60 16.44  ? 252 ASP E OD2 1 
ATOM   6302  N  N   . LEU C  1 254 ? -79.397  -14.300 51.095  1.00 20.19  ? 253 LEU E N   1 
ATOM   6303  C  CA  . LEU C  1 254 ? -78.024  -14.784 51.121  1.00 21.54  ? 253 LEU E CA  1 
ATOM   6304  C  C   . LEU C  1 254 ? -77.841  -15.978 52.071  1.00 20.95  ? 253 LEU E C   1 
ATOM   6305  O  O   . LEU C  1 254 ? -76.724  -16.339 52.297  1.00 21.99  ? 253 LEU E O   1 
ATOM   6306  C  CB  . LEU C  1 254 ? -77.083  -13.640 51.504  1.00 21.04  ? 253 LEU E CB  1 
ATOM   6307  C  CG  . LEU C  1 254 ? -76.948  -12.535 50.461  1.00 25.14  ? 253 LEU E CG  1 
ATOM   6308  C  CD1 . LEU C  1 254 ? -76.089  -11.403 50.982  1.00 24.65  ? 253 LEU E CD1 1 
ATOM   6309  C  CD2 . LEU C  1 254 ? -76.390  -13.076 49.151  1.00 26.39  ? 253 LEU E CD2 1 
ATOM   6310  N  N   . GLY C  1 255 ? -78.923  -16.556 52.609  1.00 21.42  ? 254 GLY E N   1 
ATOM   6311  C  CA  . GLY C  1 255 ? -78.870  -17.826 53.351  1.00 19.41  ? 254 GLY E CA  1 
ATOM   6312  C  C   . GLY C  1 255 ? -78.449  -17.589 54.799  1.00 20.66  ? 254 GLY E C   1 
ATOM   6313  O  O   . GLY C  1 255 ? -78.884  -16.622 55.409  1.00 19.15  ? 254 GLY E O   1 
ATOM   6314  N  N   . ASN C  1 256 ? -77.571  -18.452 55.298  1.00 17.79  ? 255 ASN E N   1 
ATOM   6315  C  CA  . ASN C  1 256 ? -77.124  -18.462 56.667  1.00 19.97  ? 255 ASN E CA  1 
ATOM   6316  C  C   . ASN C  1 256 ? -75.641  -18.102 56.739  1.00 19.92  ? 255 ASN E C   1 
ATOM   6317  O  O   . ASN C  1 256 ? -74.857  -18.322 55.783  1.00 19.59  ? 255 ASN E O   1 
ATOM   6318  C  CB  . ASN C  1 256 ? -77.361  -19.830 57.310  1.00 19.96  ? 255 ASN E CB  1 
ATOM   6319  C  CG  . ASN C  1 256 ? -78.822  -20.075 57.602  1.00 20.74  ? 255 ASN E CG  1 
ATOM   6320  O  OD1 . ASN C  1 256 ? -79.401  -19.381 58.433  1.00 21.79  ? 255 ASN E OD1 1 
ATOM   6321  N  ND2 . ASN C  1 256 ? -79.429  -21.039 56.919  1.00 18.86  ? 255 ASN E ND2 1 
ATOM   6322  N  N   . VAL C  1 257 ? -75.265  -17.541 57.895  1.00 18.30  ? 256 VAL E N   1 
ATOM   6323  C  CA  . VAL C  1 257 ? -73.892  -17.488 58.333  1.00 18.61  ? 256 VAL E CA  1 
ATOM   6324  C  C   . VAL C  1 257 ? -73.828  -18.277 59.642  1.00 18.29  ? 256 VAL E C   1 
ATOM   6325  O  O   . VAL C  1 257 ? -74.833  -18.403 60.340  1.00 20.76  ? 256 VAL E O   1 
ATOM   6326  C  CB  . VAL C  1 257 ? -73.347  -16.047 58.480  1.00 18.01  ? 256 VAL E CB  1 
ATOM   6327  C  CG1 . VAL C  1 257 ? -73.345  -15.327 57.141  1.00 18.96  ? 256 VAL E CG1 1 
ATOM   6328  C  CG2 . VAL C  1 257 ? -74.097  -15.234 59.518  1.00 17.95  ? 256 VAL E CG2 1 
ATOM   6329  N  N   . THR C  1 258 ? -72.647  -18.817 59.929  1.00 19.14  ? 257 THR E N   1 
ATOM   6330  C  CA  . THR C  1 258 ? -72.404  -19.711 61.051  1.00 19.93  ? 257 THR E CA  1 
ATOM   6331  C  C   . THR C  1 258 ? -71.432  -19.072 62.028  1.00 18.59  ? 257 THR E C   1 
ATOM   6332  O  O   . THR C  1 258 ? -70.334  -18.681 61.661  1.00 20.71  ? 257 THR E O   1 
ATOM   6333  C  CB  . THR C  1 258 ? -71.831  -21.057 60.578  1.00 23.08  ? 257 THR E CB  1 
ATOM   6334  O  OG1 . THR C  1 258 ? -72.795  -21.639 59.699  1.00 22.19  ? 257 THR E OG1 1 
ATOM   6335  C  CG2 . THR C  1 258 ? -71.563  -21.995 61.735  1.00 24.16  ? 257 THR E CG2 1 
ATOM   6336  N  N   . ALA C  1 259 ? -71.864  -18.967 63.283  1.00 19.49  ? 258 ALA E N   1 
ATOM   6337  C  CA  . ALA C  1 259 ? -71.019  -18.530 64.357  1.00 21.79  ? 258 ALA E CA  1 
ATOM   6338  C  C   . ALA C  1 259 ? -70.402  -19.771 65.015  1.00 21.26  ? 258 ALA E C   1 
ATOM   6339  O  O   . ALA C  1 259 ? -71.083  -20.754 65.232  1.00 21.76  ? 258 ALA E O   1 
ATOM   6340  C  CB  . ALA C  1 259 ? -71.841  -17.754 65.351  1.00 22.76  ? 258 ALA E CB  1 
ATOM   6341  N  N   . ASP C  1 260 ? -69.130  -19.671 65.368  1.00 24.09  ? 259 ASP E N   1 
ATOM   6342  C  CA  . ASP C  1 260 ? -68.397  -20.729 66.072  1.00 25.91  ? 259 ASP E CA  1 
ATOM   6343  C  C   . ASP C  1 260 ? -68.736  -20.641 67.567  1.00 28.39  ? 259 ASP E C   1 
ATOM   6344  O  O   . ASP C  1 260 ? -69.565  -19.805 67.984  1.00 24.51  ? 259 ASP E O   1 
ATOM   6345  C  CB  . ASP C  1 260 ? -66.901  -20.597 65.771  1.00 27.13  ? 259 ASP E CB  1 
ATOM   6346  C  CG  . ASP C  1 260 ? -66.259  -19.324 66.298  1.00 28.71  ? 259 ASP E CG  1 
ATOM   6347  O  OD1 . ASP C  1 260 ? -65.181  -18.980 65.803  1.00 30.92  ? 259 ASP E OD1 1 
ATOM   6348  O  OD2 . ASP C  1 260 ? -66.832  -18.686 67.211  1.00 28.64  ? 259 ASP E OD2 1 
ATOM   6349  N  N   . LYS C  1 261 ? -68.077  -21.474 68.388  1.00 29.26  ? 260 LYS E N   1 
ATOM   6350  C  CA  . LYS C  1 261 ? -68.387  -21.553 69.822  1.00 32.74  ? 260 LYS E CA  1 
ATOM   6351  C  C   . LYS C  1 261 ? -68.013  -20.263 70.578  1.00 30.19  ? 260 LYS E C   1 
ATOM   6352  O  O   . LYS C  1 261 ? -68.477  -20.083 71.686  1.00 35.23  ? 260 LYS E O   1 
ATOM   6353  C  CB  . LYS C  1 261 ? -67.684  -22.746 70.484  1.00 38.73  ? 260 LYS E CB  1 
ATOM   6354  C  CG  . LYS C  1 261 ? -66.160  -22.749 70.376  1.00 47.63  ? 260 LYS E CG  1 
ATOM   6355  C  CD  . LYS C  1 261 ? -65.469  -23.678 71.368  1.00 58.41  ? 260 LYS E CD  1 
ATOM   6356  C  CE  . LYS C  1 261 ? -65.376  -23.109 72.776  1.00 68.32  ? 260 LYS E CE  1 
ATOM   6357  N  NZ  . LYS C  1 261 ? -64.469  -21.931 72.857  1.00 72.40  ? 260 LYS E NZ  1 
ATOM   6358  N  N   . ASP C  1 262 ? -67.169  -19.395 70.011  1.00 28.37  ? 261 ASP E N   1 
ATOM   6359  C  CA  . ASP C  1 262 ? -66.854  -18.090 70.613  1.00 28.63  ? 261 ASP E CA  1 
ATOM   6360  C  C   . ASP C  1 262 ? -67.847  -17.001 70.178  1.00 27.43  ? 261 ASP E C   1 
ATOM   6361  O  O   . ASP C  1 262 ? -67.677  -15.831 70.543  1.00 27.16  ? 261 ASP E O   1 
ATOM   6362  C  CB  . ASP C  1 262 ? -65.448  -17.640 70.229  1.00 30.99  ? 261 ASP E CB  1 
ATOM   6363  C  CG  . ASP C  1 262 ? -64.367  -18.563 70.773  1.00 37.48  ? 261 ASP E CG  1 
ATOM   6364  O  OD1 . ASP C  1 262 ? -64.555  -19.087 71.889  1.00 40.33  ? 261 ASP E OD1 1 
ATOM   6365  O  OD2 . ASP C  1 262 ? -63.384  -18.784 70.056  1.00 42.18  ? 261 ASP E OD2 1 
ATOM   6366  N  N   . GLY C  1 263 ? -68.829  -17.364 69.340  1.00 25.88  ? 262 GLY E N   1 
ATOM   6367  C  CA  . GLY C  1 263 ? -69.843  -16.414 68.868  1.00 24.46  ? 262 GLY E CA  1 
ATOM   6368  C  C   . GLY C  1 263 ? -69.390  -15.612 67.655  1.00 22.66  ? 262 GLY E C   1 
ATOM   6369  O  O   . GLY C  1 263 ? -70.024  -14.621 67.327  1.00 23.03  ? 262 GLY E O   1 
ATOM   6370  N  N   . VAL C  1 264 ? -68.341  -16.071 66.958  1.00 22.03  ? 263 VAL E N   1 
ATOM   6371  C  CA  . VAL C  1 264 ? -67.779  -15.365 65.814  1.00 23.09  ? 263 VAL E CA  1 
ATOM   6372  C  C   . VAL C  1 264 ? -68.188  -16.081 64.520  1.00 24.11  ? 263 VAL E C   1 
ATOM   6373  O  O   . VAL C  1 264 ? -67.984  -17.295 64.363  1.00 24.31  ? 263 VAL E O   1 
ATOM   6374  C  CB  . VAL C  1 264 ? -66.245  -15.221 65.909  1.00 24.88  ? 263 VAL E CB  1 
ATOM   6375  C  CG1 . VAL C  1 264 ? -65.681  -14.535 64.675  1.00 25.64  ? 263 VAL E CG1 1 
ATOM   6376  C  CG2 . VAL C  1 264 ? -65.803  -14.486 67.170  1.00 25.55  ? 263 VAL E CG2 1 
ATOM   6377  N  N   . ALA C  1 265 ? -68.753  -15.305 63.587  1.00 23.41  ? 264 ALA E N   1 
ATOM   6378  C  CA  . ALA C  1 265 ? -69.057  -15.762 62.232  1.00 23.61  ? 264 ALA E CA  1 
ATOM   6379  C  C   . ALA C  1 265 ? -68.030  -15.149 61.278  1.00 24.73  ? 264 ALA E C   1 
ATOM   6380  O  O   . ALA C  1 265 ? -68.011  -13.919 61.102  1.00 22.36  ? 264 ALA E O   1 
ATOM   6381  C  CB  . ALA C  1 265 ? -70.461  -15.395 61.832  1.00 24.49  ? 264 ALA E CB  1 
ATOM   6382  N  N   . ASP C  1 266 ? -67.146  -16.006 60.733  1.00 22.80  ? 265 ASP E N   1 
ATOM   6383  C  CA  . ASP C  1 266 ? -66.200  -15.623 59.705  1.00 23.87  ? 265 ASP E CA  1 
ATOM   6384  C  C   . ASP C  1 266 ? -66.861  -15.849 58.348  1.00 23.66  ? 265 ASP E C   1 
ATOM   6385  O  O   . ASP C  1 266 ? -66.759  -16.926 57.736  1.00 25.28  ? 265 ASP E O   1 
ATOM   6386  C  CB  . ASP C  1 266 ? -64.869  -16.363 59.856  1.00 28.73  ? 265 ASP E CB  1 
ATOM   6387  C  CG  . ASP C  1 266 ? -64.087  -15.914 61.087  1.00 32.73  ? 265 ASP E CG  1 
ATOM   6388  O  OD1 . ASP C  1 266 ? -63.939  -14.667 61.305  1.00 33.19  ? 265 ASP E OD1 1 
ATOM   6389  O  OD2 . ASP C  1 266 ? -63.699  -16.802 61.862  1.00 41.33  ? 265 ASP E OD2 1 
ATOM   6390  N  N   . VAL C  1 267 ? -67.537  -14.807 57.873  1.00 21.42  ? 266 VAL E N   1 
ATOM   6391  C  CA  . VAL C  1 267 ? -68.426  -14.904 56.724  1.00 20.80  ? 266 VAL E CA  1 
ATOM   6392  C  C   . VAL C  1 267 ? -67.594  -15.041 55.446  1.00 20.92  ? 266 VAL E C   1 
ATOM   6393  O  O   . VAL C  1 267 ? -66.612  -14.329 55.258  1.00 20.28  ? 266 VAL E O   1 
ATOM   6394  C  CB  . VAL C  1 267 ? -69.334  -13.670 56.642  1.00 21.38  ? 266 VAL E CB  1 
ATOM   6395  C  CG1 . VAL C  1 267 ? -70.177  -13.696 55.381  1.00 23.36  ? 266 VAL E CG1 1 
ATOM   6396  C  CG2 . VAL C  1 267 ? -70.205  -13.568 57.896  1.00 23.67  ? 266 VAL E CG2 1 
ATOM   6397  N  N   . SER C  1 268 ? -68.030  -15.929 54.556  1.00 23.17  ? 267 SER E N   1 
ATOM   6398  C  CA  . SER C  1 268 ? -67.404  -16.085 53.256  1.00 27.00  ? 267 SER E CA  1 
ATOM   6399  C  C   . SER C  1 268 ? -68.432  -16.683 52.302  1.00 26.88  ? 267 SER E C   1 
ATOM   6400  O  O   . SER C  1 268 ? -68.763  -17.860 52.364  1.00 27.35  ? 267 SER E O   1 
ATOM   6401  C  CB  . SER C  1 268 ? -66.157  -16.935 53.343  1.00 34.09  ? 267 SER E CB  1 
ATOM   6402  O  OG  . SER C  1 268 ? -65.454  -16.882 52.118  1.00 36.85  ? 267 SER E OG  1 
ATOM   6403  N  N   . ILE C  1 269 ? -68.962  -15.828 51.436  1.00 26.72  ? 268 ILE E N   1 
ATOM   6404  C  CA  . ILE C  1 269 ? -70.070  -16.165 50.562  1.00 26.57  ? 268 ILE E CA  1 
ATOM   6405  C  C   . ILE C  1 269 ? -69.694  -15.621 49.182  1.00 25.71  ? 268 ILE E C   1 
ATOM   6406  O  O   . ILE C  1 269 ? -69.013  -14.594 49.068  1.00 24.88  ? 268 ILE E O   1 
ATOM   6407  C  CB  . ILE C  1 269 ? -71.379  -15.548 51.117  1.00 29.38  ? 268 ILE E CB  1 
ATOM   6408  C  CG1 . ILE C  1 269 ? -71.909  -16.306 52.335  1.00 29.11  ? 268 ILE E CG1 1 
ATOM   6409  C  CG2 . ILE C  1 269 ? -72.474  -15.423 50.065  1.00 30.56  ? 268 ILE E CG2 1 
ATOM   6410  C  CD1 . ILE C  1 269 ? -73.052  -15.574 53.040  1.00 28.80  ? 268 ILE E CD1 1 
ATOM   6411  N  N   . GLU C  1 270 ? -70.122  -16.324 48.143  1.00 25.47  ? 269 GLU E N   1 
ATOM   6412  C  CA  . GLU C  1 270 ? -70.040  -15.801 46.783  1.00 28.51  ? 269 GLU E CA  1 
ATOM   6413  C  C   . GLU C  1 270 ? -71.437  -15.943 46.186  1.00 26.65  ? 269 GLU E C   1 
ATOM   6414  O  O   . GLU C  1 270 ? -72.061  -16.992 46.292  1.00 26.14  ? 269 GLU E O   1 
ATOM   6415  C  CB  . GLU C  1 270 ? -68.938  -16.535 46.020  1.00 32.58  ? 269 GLU E CB  1 
ATOM   6416  C  CG  . GLU C  1 270 ? -68.772  -16.064 44.594  1.00 42.21  ? 269 GLU E CG  1 
ATOM   6417  C  CD  . GLU C  1 270 ? -67.623  -16.704 43.813  1.00 48.38  ? 269 GLU E CD  1 
ATOM   6418  O  OE1 . GLU C  1 270 ? -67.189  -16.088 42.823  1.00 58.58  ? 269 GLU E OE1 1 
ATOM   6419  O  OE2 . GLU C  1 270 ? -67.159  -17.812 44.192  1.00 59.48  ? 269 GLU E OE2 1 
ATOM   6420  N  N   . ASP C  1 271 ? -71.975  -14.852 45.642  1.00 25.46  ? 270 ASP E N   1 
ATOM   6421  C  CA  . ASP C  1 271 ? -73.356  -14.876 45.162  1.00 25.52  ? 270 ASP E CA  1 
ATOM   6422  C  C   . ASP C  1 271 ? -73.416  -14.152 43.817  1.00 26.62  ? 270 ASP E C   1 
ATOM   6423  O  O   . ASP C  1 271 ? -72.781  -13.097 43.660  1.00 25.38  ? 270 ASP E O   1 
ATOM   6424  C  CB  . ASP C  1 271 ? -74.307  -14.227 46.166  1.00 25.76  ? 270 ASP E CB  1 
ATOM   6425  C  CG  . ASP C  1 271 ? -75.766  -14.449 45.818  1.00 28.89  ? 270 ASP E CG  1 
ATOM   6426  O  OD1 . ASP C  1 271 ? -76.411  -13.520 45.236  1.00 25.88  ? 270 ASP E OD1 1 
ATOM   6427  O  OD2 . ASP C  1 271 ? -76.250  -15.556 46.091  1.00 31.78  ? 270 ASP E OD2 1 
ATOM   6428  N  N   . SER C  1 272 ? -74.216  -14.666 42.876  1.00 26.78  ? 271 SER E N   1 
ATOM   6429  C  CA  . SER C  1 272 ? -74.305  -13.965 41.589  1.00 30.36  ? 271 SER E CA  1 
ATOM   6430  C  C   . SER C  1 272 ? -75.733  -13.512 41.282  1.00 27.76  ? 271 SER E C   1 
ATOM   6431  O  O   . SER C  1 272 ? -76.038  -13.157 40.151  1.00 29.94  ? 271 SER E O   1 
ATOM   6432  C  CB  . SER C  1 272 ? -73.695  -14.770 40.459  1.00 35.65  ? 271 SER E CB  1 
ATOM   6433  O  OG  . SER C  1 272 ? -74.057  -16.120 40.592  1.00 38.46  ? 271 SER E OG  1 
ATOM   6434  N  N   . VAL C  1 273 ? -76.579  -13.413 42.301  1.00 23.41  ? 272 VAL E N   1 
ATOM   6435  C  CA  . VAL C  1 273 ? -77.835  -12.767 42.123  1.00 24.28  ? 272 VAL E CA  1 
ATOM   6436  C  C   . VAL C  1 273 ? -77.757  -11.310 42.629  1.00 24.50  ? 272 VAL E C   1 
ATOM   6437  O  O   . VAL C  1 273 ? -78.278  -10.402 41.970  1.00 23.06  ? 272 VAL E O   1 
ATOM   6438  C  CB  . VAL C  1 273 ? -78.963  -13.579 42.771  1.00 23.92  ? 272 VAL E CB  1 
ATOM   6439  C  CG1 . VAL C  1 273 ? -80.273  -12.804 42.787  1.00 23.79  ? 272 VAL E CG1 1 
ATOM   6440  C  CG2 . VAL C  1 273 ? -79.133  -14.912 42.048  1.00 25.37  ? 272 VAL E CG2 1 
ATOM   6441  N  N   . ILE C  1 274 ? -77.131  -11.077 43.787  1.00 22.07  ? 273 ILE E N   1 
ATOM   6442  C  CA  . ILE C  1 274 ? -76.881  -9.711  44.204  1.00 22.29  ? 273 ILE E CA  1 
ATOM   6443  C  C   . ILE C  1 274 ? -75.875  -9.094  43.225  1.00 23.12  ? 273 ILE E C   1 
ATOM   6444  O  O   . ILE C  1 274 ? -75.103  -9.795  42.578  1.00 22.52  ? 273 ILE E O   1 
ATOM   6445  C  CB  . ILE C  1 274 ? -76.377  -9.594  45.653  1.00 21.45  ? 273 ILE E CB  1 
ATOM   6446  C  CG1 . ILE C  1 274 ? -75.114  -10.421 45.900  1.00 22.15  ? 273 ILE E CG1 1 
ATOM   6447  C  CG2 . ILE C  1 274 ? -77.485  -9.924  46.619  1.00 21.90  ? 273 ILE E CG2 1 
ATOM   6448  C  CD1 . ILE C  1 274 ? -74.334  -9.998  47.119  1.00 22.38  ? 273 ILE E CD1 1 
ATOM   6449  N  N   . SER C  1 275 ? -75.854  -7.764  43.198  1.00 21.63  ? 274 SER E N   1 
ATOM   6450  C  CA  . SER C  1 275 ? -74.899  -7.011  42.438  1.00 21.34  ? 274 SER E CA  1 
ATOM   6451  C  C   . SER C  1 275 ? -74.572  -5.720  43.191  1.00 19.73  ? 274 SER E C   1 
ATOM   6452  O  O   . SER C  1 275 ? -75.288  -5.331  44.108  1.00 21.26  ? 274 SER E O   1 
ATOM   6453  C  CB  . SER C  1 275 ? -75.441  -6.735  41.049  1.00 22.36  ? 274 SER E CB  1 
ATOM   6454  O  OG  . SER C  1 275 ? -74.429  -6.188  40.234  1.00 22.79  ? 274 SER E OG  1 
ATOM   6455  N  N   . LEU C  1 276 ? -73.472  -5.085  42.815  1.00 21.58  ? 275 LEU E N   1 
ATOM   6456  C  CA  . LEU C  1 276 ? -73.123  -3.746  43.307  1.00 22.84  ? 275 LEU E CA  1 
ATOM   6457  C  C   . LEU C  1 276 ? -73.469  -2.668  42.273  1.00 24.89  ? 275 LEU E C   1 
ATOM   6458  O  O   . LEU C  1 276 ? -73.146  -1.511  42.467  1.00 24.28  ? 275 LEU E O   1 
ATOM   6459  C  CB  . LEU C  1 276 ? -71.640  -3.697  43.679  1.00 21.62  ? 275 LEU E CB  1 
ATOM   6460  C  CG  . LEU C  1 276 ? -71.200  -4.781  44.660  1.00 22.55  ? 275 LEU E CG  1 
ATOM   6461  C  CD1 . LEU C  1 276 ? -69.749  -4.565  45.086  1.00 23.00  ? 275 LEU E CD1 1 
ATOM   6462  C  CD2 . LEU C  1 276 ? -72.120  -4.817  45.879  1.00 22.49  ? 275 LEU E CD2 1 
ATOM   6463  N  N   . SER C  1 277 ? -74.149  -3.041  41.193  1.00 26.63  ? 276 SER E N   1 
ATOM   6464  C  CA  . SER C  1 277 ? -74.684  -2.048  40.280  1.00 30.13  ? 276 SER E CA  1 
ATOM   6465  C  C   . SER C  1 277 ? -75.907  -2.620  39.576  1.00 28.33  ? 276 SER E C   1 
ATOM   6466  O  O   . SER C  1 277 ? -76.206  -3.815  39.695  1.00 28.84  ? 276 SER E O   1 
ATOM   6467  C  CB  . SER C  1 277 ? -73.652  -1.582  39.283  1.00 32.42  ? 276 SER E CB  1 
ATOM   6468  O  OG  . SER C  1 277 ? -73.193  -2.674  38.510  1.00 34.01  ? 276 SER E OG  1 
ATOM   6469  N  N   . GLY C  1 278 ? -76.628  -1.713  38.916  1.00 28.78  ? 277 GLY E N   1 
ATOM   6470  C  CA  . GLY C  1 278 ? -77.821  -2.018  38.160  1.00 29.26  ? 277 GLY E CA  1 
ATOM   6471  C  C   . GLY C  1 278 ? -79.021  -2.306  39.044  1.00 27.28  ? 277 GLY E C   1 
ATOM   6472  O  O   . GLY C  1 278 ? -79.093  -1.910  40.216  1.00 26.03  ? 277 GLY E O   1 
ATOM   6473  N  N   . ASP C  1 279 ? -79.960  -3.043  38.461  1.00 24.98  ? 278 ASP E N   1 
ATOM   6474  C  CA  . ASP C  1 279 ? -81.268  -3.333  39.052  1.00 27.61  ? 278 ASP E CA  1 
ATOM   6475  C  C   . ASP C  1 279 ? -81.145  -4.127  40.367  1.00 24.55  ? 278 ASP E C   1 
ATOM   6476  O  O   . ASP C  1 279 ? -81.968  -3.988  41.245  1.00 26.74  ? 278 ASP E O   1 
ATOM   6477  C  CB  . ASP C  1 279 ? -82.099  -4.167  38.075  1.00 29.68  ? 278 ASP E CB  1 
ATOM   6478  C  CG  . ASP C  1 279 ? -82.757  -3.339  36.979  1.00 37.78  ? 278 ASP E CG  1 
ATOM   6479  O  OD1 . ASP C  1 279 ? -83.405  -3.944  36.124  1.00 38.01  ? 278 ASP E OD1 1 
ATOM   6480  O  OD2 . ASP C  1 279 ? -82.666  -2.091  37.039  1.00 41.32  ? 278 ASP E OD2 1 
ATOM   6481  N  N   . HIS C  1 280 ? -80.148  -5.007  40.459  1.00 22.50  ? 279 HIS E N   1 
ATOM   6482  C  CA  . HIS C  1 280 ? -79.999  -5.872  41.627  1.00 23.66  ? 279 HIS E CA  1 
ATOM   6483  C  C   . HIS C  1 280 ? -78.979  -5.280  42.605  1.00 20.73  ? 279 HIS E C   1 
ATOM   6484  O  O   . HIS C  1 280 ? -78.511  -5.973  43.508  1.00 22.23  ? 279 HIS E O   1 
ATOM   6485  C  CB  . HIS C  1 280 ? -79.622  -7.292  41.178  1.00 24.41  ? 279 HIS E CB  1 
ATOM   6486  C  CG  . HIS C  1 280 ? -80.743  -8.032  40.531  1.00 27.08  ? 279 HIS E CG  1 
ATOM   6487  N  ND1 . HIS C  1 280 ? -80.641  -9.373  40.190  1.00 31.49  ? 279 HIS E ND1 1 
ATOM   6488  C  CD2 . HIS C  1 280 ? -81.990  -7.648  40.199  1.00 30.12  ? 279 HIS E CD2 1 
ATOM   6489  C  CE1 . HIS C  1 280 ? -81.774  -9.757  39.631  1.00 33.14  ? 279 HIS E CE1 1 
ATOM   6490  N  NE2 . HIS C  1 280 ? -82.604  -8.716  39.600  1.00 32.31  ? 279 HIS E NE2 1 
ATOM   6491  N  N   . SER C  1 281 ? -78.622  -4.009  42.417  1.00 20.47  ? 280 SER E N   1 
ATOM   6492  C  CA  . SER C  1 281 ? -77.665  -3.345  43.280  1.00 20.65  ? 280 SER E CA  1 
ATOM   6493  C  C   . SER C  1 281 ? -78.189  -3.360  44.730  1.00 19.29  ? 280 SER E C   1 
ATOM   6494  O  O   . SER C  1 281 ? -79.330  -3.001  45.004  1.00 19.96  ? 280 SER E O   1 
ATOM   6495  C  CB  . SER C  1 281 ? -77.392  -1.927  42.874  1.00 22.46  ? 280 SER E CB  1 
ATOM   6496  O  OG  . SER C  1 281 ? -76.386  -1.385  43.731  1.00 22.70  ? 280 SER E OG  1 
ATOM   6497  N  N   . ILE C  1 282 ? -77.301  -3.703  45.646  1.00 19.25  ? 281 ILE E N   1 
ATOM   6498  C  CA  . ILE C  1 282 ? -77.559  -3.658  47.082  1.00 19.56  ? 281 ILE E CA  1 
ATOM   6499  C  C   . ILE C  1 282 ? -76.924  -2.400  47.708  1.00 18.73  ? 281 ILE E C   1 
ATOM   6500  O  O   . ILE C  1 282 ? -77.033  -2.209  48.922  1.00 18.54  ? 281 ILE E O   1 
ATOM   6501  C  CB  . ILE C  1 282 ? -77.059  -4.969  47.723  1.00 20.08  ? 281 ILE E CB  1 
ATOM   6502  C  CG1 . ILE C  1 282 ? -75.543  -5.120  47.642  1.00 21.38  ? 281 ILE E CG1 1 
ATOM   6503  C  CG2 . ILE C  1 282 ? -77.775  -6.152  47.100  1.00 22.11  ? 281 ILE E CG2 1 
ATOM   6504  C  CD1 . ILE C  1 282 ? -75.005  -6.334  48.351  1.00 23.83  ? 281 ILE E CD1 1 
ATOM   6505  N  N   . ILE C  1 283 ? -76.280  -1.543  46.902  1.00 18.99  ? 282 ILE E N   1 
ATOM   6506  C  CA  . ILE C  1 283 ? -75.683  -0.292  47.394  1.00 19.48  ? 282 ILE E CA  1 
ATOM   6507  C  C   . ILE C  1 283 ? -76.810  0.580   47.947  1.00 19.51  ? 282 ILE E C   1 
ATOM   6508  O  O   . ILE C  1 283 ? -77.807  0.799   47.267  1.00 19.36  ? 282 ILE E O   1 
ATOM   6509  C  CB  . ILE C  1 283 ? -74.910  0.469   46.305  1.00 21.45  ? 282 ILE E CB  1 
ATOM   6510  C  CG1 . ILE C  1 283 ? -73.786  -0.378  45.712  1.00 23.34  ? 282 ILE E CG1 1 
ATOM   6511  C  CG2 . ILE C  1 283 ? -74.390  1.811   46.832  1.00 21.74  ? 282 ILE E CG2 1 
ATOM   6512  C  CD1 . ILE C  1 283 ? -72.746  -0.791  46.685  1.00 24.30  ? 282 ILE E CD1 1 
ATOM   6513  N  N   . GLY C  1 284 ? -76.673  1.023   49.200  1.00 18.74  ? 283 GLY E N   1 
ATOM   6514  C  CA  . GLY C  1 284 ? -77.694  1.873   49.835  1.00 19.12  ? 283 GLY E CA  1 
ATOM   6515  C  C   . GLY C  1 284 ? -78.847  1.086   50.455  1.00 19.40  ? 283 GLY E C   1 
ATOM   6516  O  O   . GLY C  1 284 ? -79.857  1.681   50.871  1.00 20.00  ? 283 GLY E O   1 
ATOM   6517  N  N   . ARG C  1 285 ? -78.735  -0.244  50.486  1.00 16.61  ? 284 ARG E N   1 
ATOM   6518  C  CA  . ARG C  1 285 ? -79.723  -1.072  51.145  1.00 18.07  ? 284 ARG E CA  1 
ATOM   6519  C  C   . ARG C  1 285 ? -79.129  -1.535  52.480  1.00 18.02  ? 284 ARG E C   1 
ATOM   6520  O  O   . ARG C  1 285 ? -78.070  -1.079  52.860  1.00 21.80  ? 284 ARG E O   1 
ATOM   6521  C  CB  . ARG C  1 285 ? -80.181  -2.204  50.234  1.00 18.90  ? 284 ARG E CB  1 
ATOM   6522  C  CG  . ARG C  1 285 ? -80.671  -1.688  48.885  1.00 19.60  ? 284 ARG E CG  1 
ATOM   6523  C  CD  . ARG C  1 285 ? -81.451  -2.672  48.054  1.00 20.87  ? 284 ARG E CD  1 
ATOM   6524  N  NE  . ARG C  1 285 ? -81.727  -2.138  46.718  1.00 21.83  ? 284 ARG E NE  1 
ATOM   6525  C  CZ  . ARG C  1 285 ? -82.807  -1.439  46.360  1.00 21.16  ? 284 ARG E CZ  1 
ATOM   6526  N  NH1 . ARG C  1 285 ? -82.948  -1.086  45.078  1.00 19.81  ? 284 ARG E NH1 1 
ATOM   6527  N  NH2 . ARG C  1 285 ? -83.750  -1.180  47.252  1.00 18.64  ? 284 ARG E NH2 1 
ATOM   6528  N  N   . THR C  1 286 ? -79.854  -2.363  53.230  1.00 17.48  ? 285 THR E N   1 
ATOM   6529  C  CA  . THR C  1 286 ? -79.439  -2.716  54.583  1.00 17.92  ? 285 THR E CA  1 
ATOM   6530  C  C   . THR C  1 286 ? -79.103  -4.210  54.611  1.00 18.08  ? 285 THR E C   1 
ATOM   6531  O  O   . THR C  1 286 ? -79.891  -5.023  54.146  1.00 17.97  ? 285 THR E O   1 
ATOM   6532  C  CB  . THR C  1 286 ? -80.509  -2.344  55.615  1.00 18.49  ? 285 THR E CB  1 
ATOM   6533  O  OG1 . THR C  1 286 ? -80.596  -0.915  55.701  1.00 21.45  ? 285 THR E OG1 1 
ATOM   6534  C  CG2 . THR C  1 286 ? -80.208  -2.891  57.000  1.00 19.05  ? 285 THR E CG2 1 
ATOM   6535  N  N   . LEU C  1 287 ? -77.946  -4.544  55.167  1.00 17.75  ? 286 LEU E N   1 
ATOM   6536  C  CA  . LEU C  1 287 ? -77.604  -5.933  55.476  1.00 17.24  ? 286 LEU E CA  1 
ATOM   6537  C  C   . LEU C  1 287 ? -78.058  -6.224  56.916  1.00 17.62  ? 286 LEU E C   1 
ATOM   6538  O  O   . LEU C  1 287 ? -77.771  -5.423  57.799  1.00 17.17  ? 286 LEU E O   1 
ATOM   6539  C  CB  . LEU C  1 287 ? -76.101  -6.087  55.302  1.00 17.51  ? 286 LEU E CB  1 
ATOM   6540  C  CG  . LEU C  1 287 ? -75.544  -7.493  55.532  1.00 18.98  ? 286 LEU E CG  1 
ATOM   6541  C  CD1 . LEU C  1 287 ? -76.063  -8.472  54.496  1.00 19.90  ? 286 LEU E CD1 1 
ATOM   6542  C  CD2 . LEU C  1 287 ? -74.033  -7.455  55.522  1.00 19.96  ? 286 LEU E CD2 1 
ATOM   6543  N  N   . VAL C  1 288 ? -78.753  -7.352  57.127  1.00 17.61  ? 287 VAL E N   1 
ATOM   6544  C  CA  . VAL C  1 288 ? -79.279  -7.767  58.422  1.00 18.03  ? 287 VAL E CA  1 
ATOM   6545  C  C   . VAL C  1 288 ? -78.756  -9.167  58.764  1.00 18.65  ? 287 VAL E C   1 
ATOM   6546  O  O   . VAL C  1 288 ? -78.746  -10.077 57.920  1.00 17.85  ? 287 VAL E O   1 
ATOM   6547  C  CB  . VAL C  1 288 ? -80.821  -7.753  58.429  1.00 19.78  ? 287 VAL E CB  1 
ATOM   6548  C  CG1 . VAL C  1 288 ? -81.389  -8.163  59.778  1.00 19.55  ? 287 VAL E CG1 1 
ATOM   6549  C  CG2 . VAL C  1 288 ? -81.367  -6.390  58.021  1.00 20.06  ? 287 VAL E CG2 1 
ATOM   6550  N  N   . VAL C  1 289 ? -78.353  -9.350  60.025  1.00 18.07  ? 288 VAL E N   1 
ATOM   6551  C  CA  . VAL C  1 289 ? -78.132  -10.681 60.548  1.00 18.82  ? 288 VAL E CA  1 
ATOM   6552  C  C   . VAL C  1 289 ? -79.185  -10.963 61.625  1.00 18.70  ? 288 VAL E C   1 
ATOM   6553  O  O   . VAL C  1 289 ? -79.502  -10.112 62.457  1.00 17.92  ? 288 VAL E O   1 
ATOM   6554  C  CB  . VAL C  1 289 ? -76.685  -10.861 61.028  1.00 20.13  ? 288 VAL E CB  1 
ATOM   6555  C  CG1 . VAL C  1 289 ? -76.304  -9.881  62.126  1.00 21.10  ? 288 VAL E CG1 1 
ATOM   6556  C  CG2 . VAL C  1 289 ? -76.420  -12.302 61.443  1.00 19.98  ? 288 VAL E CG2 1 
ATOM   6557  N  N   . HIS C  1 290 ? -79.708  -12.186 61.600  1.00 17.64  ? 289 HIS E N   1 
ATOM   6558  C  CA  . HIS C  1 290 ? -80.920  -12.554 62.318  1.00 18.51  ? 289 HIS E CA  1 
ATOM   6559  C  C   . HIS C  1 290 ? -80.610  -13.437 63.527  1.00 19.17  ? 289 HIS E C   1 
ATOM   6560  O  O   . HIS C  1 290 ? -79.532  -14.012 63.675  1.00 19.37  ? 289 HIS E O   1 
ATOM   6561  C  CB  . HIS C  1 290 ? -81.898  -13.254 61.378  1.00 18.67  ? 289 HIS E CB  1 
ATOM   6562  C  CG  . HIS C  1 290 ? -82.603  -12.339 60.447  1.00 20.10  ? 289 HIS E CG  1 
ATOM   6563  N  ND1 . HIS C  1 290 ? -83.803  -11.756 60.784  1.00 20.62  ? 289 HIS E ND1 1 
ATOM   6564  C  CD2 . HIS C  1 290 ? -82.307  -11.922 59.190  1.00 20.63  ? 289 HIS E CD2 1 
ATOM   6565  C  CE1 . HIS C  1 290 ? -84.224  -11.011 59.779  1.00 22.69  ? 289 HIS E CE1 1 
ATOM   6566  N  NE2 . HIS C  1 290 ? -83.339  -11.114 58.775  1.00 21.57  ? 289 HIS E NE2 1 
ATOM   6567  N  N   . GLU C  1 291 ? -81.619  -13.524 64.382  1.00 20.46  ? 290 GLU E N   1 
ATOM   6568  C  CA  . GLU C  1 291 ? -81.617  -14.256 65.627  1.00 22.58  ? 290 GLU E CA  1 
ATOM   6569  C  C   . GLU C  1 291 ? -81.507  -15.767 65.371  1.00 21.72  ? 290 GLU E C   1 
ATOM   6570  O  O   . GLU C  1 291 ? -80.819  -16.457 66.100  1.00 20.74  ? 290 GLU E O   1 
ATOM   6571  C  CB  . GLU C  1 291 ? -82.923  -13.875 66.318  1.00 26.69  ? 290 GLU E CB  1 
ATOM   6572  C  CG  . GLU C  1 291 ? -83.239  -14.605 67.604  1.00 33.74  ? 290 GLU E CG  1 
ATOM   6573  C  CD  . GLU C  1 291 ? -84.717  -14.522 68.002  1.00 41.51  ? 290 GLU E CD  1 
ATOM   6574  O  OE1 . GLU C  1 291 ? -85.612  -14.189 67.133  1.00 39.09  ? 290 GLU E OE1 1 
ATOM   6575  O  OE2 . GLU C  1 291 ? -84.993  -14.790 69.179  1.00 50.56  ? 290 GLU E OE2 1 
ATOM   6576  N  N   . LYS C  1 292 ? -82.216  -16.273 64.359  1.00 21.86  ? 291 LYS E N   1 
ATOM   6577  C  CA  . LYS C  1 292 ? -82.333  -17.702 64.132  1.00 24.44  ? 291 LYS E CA  1 
ATOM   6578  C  C   . LYS C  1 292 ? -81.825  -18.073 62.740  1.00 23.21  ? 291 LYS E C   1 
ATOM   6579  O  O   . LYS C  1 292 ? -81.605  -17.210 61.896  1.00 20.98  ? 291 LYS E O   1 
ATOM   6580  C  CB  . LYS C  1 292 ? -83.805  -18.128 64.185  1.00 27.21  ? 291 LYS E CB  1 
ATOM   6581  C  CG  . LYS C  1 292 ? -84.545  -17.811 65.466  1.00 32.07  ? 291 LYS E CG  1 
ATOM   6582  C  CD  . LYS C  1 292 ? -85.994  -18.164 65.312  1.00 40.27  ? 291 LYS E CD  1 
ATOM   6583  C  CE  . LYS C  1 292 ? -86.878  -17.628 66.412  1.00 49.31  ? 291 LYS E CE  1 
ATOM   6584  N  NZ  . LYS C  1 292 ? -88.274  -17.529 65.923  1.00 57.86  ? 291 LYS E NZ  1 
ATOM   6585  N  N   . ALA C  1 293 ? -81.745  -19.389 62.505  1.00 20.92  ? 292 ALA E N   1 
ATOM   6586  C  CA  . ALA C  1 293 ? -81.457  -19.961 61.202  1.00 22.87  ? 292 ALA E CA  1 
ATOM   6587  C  C   . ALA C  1 293 ? -82.562  -19.592 60.200  1.00 21.33  ? 292 ALA E C   1 
ATOM   6588  O  O   . ALA C  1 293 ? -83.725  -19.552 60.521  1.00 21.73  ? 292 ALA E O   1 
ATOM   6589  C  CB  . ALA C  1 293 ? -81.312  -21.458 61.334  1.00 24.30  ? 292 ALA E CB  1 
ATOM   6590  N  N   . ASP C  1 294 ? -82.134  -19.256 58.986  1.00 20.08  ? 293 ASP E N   1 
ATOM   6591  C  CA  . ASP C  1 294 ? -82.953  -19.178 57.823  1.00 21.23  ? 293 ASP E CA  1 
ATOM   6592  C  C   . ASP C  1 294 ? -83.230  -20.613 57.333  1.00 20.33  ? 293 ASP E C   1 
ATOM   6593  O  O   . ASP C  1 294 ? -82.309  -21.349 56.998  1.00 20.14  ? 293 ASP E O   1 
ATOM   6594  C  CB  . ASP C  1 294 ? -82.232  -18.330 56.777  1.00 21.22  ? 293 ASP E CB  1 
ATOM   6595  C  CG  . ASP C  1 294 ? -83.041  -17.986 55.539  1.00 23.15  ? 293 ASP E CG  1 
ATOM   6596  O  OD1 . ASP C  1 294 ? -84.061  -18.665 55.280  1.00 22.27  ? 293 ASP E OD1 1 
ATOM   6597  O  OD2 . ASP C  1 294 ? -82.641  -17.021 54.844  1.00 24.09  ? 293 ASP E OD2 1 
ATOM   6598  N  N   . ASP C  1 295 ? -84.505  -20.985 57.237  1.00 19.71  ? 294 ASP E N   1 
ATOM   6599  C  CA  . ASP C  1 295 ? -84.902  -22.357 56.769  1.00 20.77  ? 294 ASP E CA  1 
ATOM   6600  C  C   . ASP C  1 295 ? -84.883  -22.452 55.235  1.00 21.02  ? 294 ASP E C   1 
ATOM   6601  O  O   . ASP C  1 295 ? -85.324  -23.468 54.682  1.00 19.84  ? 294 ASP E O   1 
ATOM   6602  C  CB  . ASP C  1 295 ? -86.267  -22.769 57.324  1.00 20.53  ? 294 ASP E CB  1 
ATOM   6603  C  CG  . ASP C  1 295 ? -87.473  -21.934 56.900  1.00 21.51  ? 294 ASP E CG  1 
ATOM   6604  O  OD1 . ASP C  1 295 ? -88.488  -21.987 57.634  1.00 22.57  ? 294 ASP E OD1 1 
ATOM   6605  O  OD2 . ASP C  1 295 ? -87.417  -21.261 55.834  1.00 21.98  ? 294 ASP E OD2 1 
ATOM   6606  N  N   . LEU C  1 296 ? -84.441  -21.384 54.555  1.00 20.10  ? 295 LEU E N   1 
ATOM   6607  C  CA  . LEU C  1 296 ? -84.208  -21.345 53.099  1.00 20.94  ? 295 LEU E CA  1 
ATOM   6608  C  C   . LEU C  1 296 ? -85.524  -21.579 52.351  1.00 21.99  ? 295 LEU E C   1 
ATOM   6609  O  O   . LEU C  1 296 ? -85.541  -22.059 51.218  1.00 22.79  ? 295 LEU E O   1 
ATOM   6610  C  CB  . LEU C  1 296 ? -83.126  -22.359 52.701  1.00 22.45  ? 295 LEU E CB  1 
ATOM   6611  C  CG  . LEU C  1 296 ? -81.822  -22.294 53.503  1.00 23.89  ? 295 LEU E CG  1 
ATOM   6612  C  CD1 . LEU C  1 296 ? -80.797  -23.307 52.989  1.00 24.73  ? 295 LEU E CD1 1 
ATOM   6613  C  CD2 . LEU C  1 296 ? -81.228  -20.891 53.499  1.00 23.57  ? 295 LEU E CD2 1 
ATOM   6614  N  N   . GLY C  1 297 ? -86.632  -21.180 52.977  1.00 20.92  ? 296 GLY E N   1 
ATOM   6615  C  CA  . GLY C  1 297 ? -87.935  -21.271 52.347  1.00 21.69  ? 296 GLY E CA  1 
ATOM   6616  C  C   . GLY C  1 297 ? -88.507  -22.676 52.376  1.00 21.68  ? 296 GLY E C   1 
ATOM   6617  O  O   . GLY C  1 297 ? -89.490  -22.925 51.708  1.00 21.63  ? 296 GLY E O   1 
ATOM   6618  N  N   . LYS C  1 298 ? -87.943  -23.571 53.203  1.00 21.60  ? 297 LYS E N   1 
ATOM   6619  C  CA  . LYS C  1 298 ? -88.371  -24.992 53.244  1.00 24.06  ? 297 LYS E CA  1 
ATOM   6620  C  C   . LYS C  1 298 ? -89.115  -25.310 54.543  1.00 22.91  ? 297 LYS E C   1 
ATOM   6621  O  O   . LYS C  1 298 ? -89.211  -26.466 54.935  1.00 22.20  ? 297 LYS E O   1 
ATOM   6622  C  CB  . LYS C  1 298 ? -87.145  -25.888 53.046  1.00 26.50  ? 297 LYS E CB  1 
ATOM   6623  C  CG  . LYS C  1 298 ? -86.494  -25.705 51.684  1.00 30.24  ? 297 LYS E CG  1 
ATOM   6624  C  CD  . LYS C  1 298 ? -85.087  -26.253 51.592  1.00 39.38  ? 297 LYS E CD  1 
ATOM   6625  C  CE  . LYS C  1 298 ? -85.006  -27.752 51.764  1.00 45.38  ? 297 LYS E CE  1 
ATOM   6626  N  NZ  . LYS C  1 298 ? -83.768  -28.290 51.140  1.00 53.74  ? 297 LYS E NZ  1 
ATOM   6627  N  N   . GLY C  1 299 ? -89.630  -24.271 55.209  1.00 19.54  ? 298 GLY E N   1 
ATOM   6628  C  CA  . GLY C  1 299 ? -90.235  -24.412 56.505  1.00 19.89  ? 298 GLY E CA  1 
ATOM   6629  C  C   . GLY C  1 299 ? -91.711  -24.812 56.471  1.00 19.38  ? 298 GLY E C   1 
ATOM   6630  O  O   . GLY C  1 299 ? -92.275  -25.165 57.521  1.00 19.55  ? 298 GLY E O   1 
ATOM   6631  N  N   . GLY C  1 300 ? -92.370  -24.637 55.320  1.00 20.10  ? 299 GLY E N   1 
ATOM   6632  C  CA  . GLY C  1 300 ? -93.774  -25.110 55.090  1.00 20.36  ? 299 GLY E CA  1 
ATOM   6633  C  C   . GLY C  1 300 ? -94.864  -24.217 55.683  1.00 22.34  ? 299 GLY E C   1 
ATOM   6634  O  O   . GLY C  1 300 ? -96.051  -24.553 55.604  1.00 22.42  ? 299 GLY E O   1 
ATOM   6635  N  N   . ASN C  1 301 ? -94.490  -23.104 56.323  1.00 23.66  ? 300 ASN E N   1 
ATOM   6636  C  CA  . ASN C  1 301 ? -95.465  -22.157 56.835  1.00 23.54  ? 300 ASN E CA  1 
ATOM   6637  C  C   . ASN C  1 301 ? -95.372  -20.862 56.019  1.00 25.00  ? 300 ASN E C   1 
ATOM   6638  O  O   . ASN C  1 301 ? -94.472  -20.679 55.201  1.00 24.55  ? 300 ASN E O   1 
ATOM   6639  C  CB  . ASN C  1 301 ? -95.322  -21.933 58.345  1.00 23.80  ? 300 ASN E CB  1 
ATOM   6640  C  CG  . ASN C  1 301 ? -94.043  -21.245 58.768  1.00 22.55  ? 300 ASN E CG  1 
ATOM   6641  O  OD1 . ASN C  1 301 ? -93.091  -21.164 58.004  1.00 23.07  ? 300 ASN E OD1 1 
ATOM   6642  N  ND2 . ASN C  1 301 ? -94.013  -20.766 60.000  1.00 22.40  ? 300 ASN E ND2 1 
ATOM   6643  N  N   . GLU C  1 302 ? -96.296  -19.940 56.277  1.00 25.99  ? 301 GLU E N   1 
ATOM   6644  C  CA  . GLU C  1 302 ? -96.349  -18.695 55.504  1.00 28.58  ? 301 GLU E CA  1 
ATOM   6645  C  C   . GLU C  1 302 ? -95.042  -17.932 55.682  1.00 24.45  ? 301 GLU E C   1 
ATOM   6646  O  O   . GLU C  1 302 ? -94.495  -17.367 54.747  1.00 25.94  ? 301 GLU E O   1 
ATOM   6647  C  CB  . GLU C  1 302 ? -97.506  -17.798 55.967  1.00 33.15  ? 301 GLU E CB  1 
ATOM   6648  C  CG  . GLU C  1 302 ? -98.861  -18.469 55.828  1.00 41.89  ? 301 GLU E CG  1 
ATOM   6649  C  CD  . GLU C  1 302 ? -100.065 -17.709 56.374  1.00 50.07  ? 301 GLU E CD  1 
ATOM   6650  O  OE1 . GLU C  1 302 ? -101.205 -18.095 56.026  1.00 53.86  ? 301 GLU E OE1 1 
ATOM   6651  O  OE2 . GLU C  1 302 ? -99.864  -16.756 57.163  1.00 55.94  ? 301 GLU E OE2 1 
ATOM   6652  N  N   . GLU C  1 303 ? -94.577  -17.903 56.922  1.00 24.94  ? 302 GLU E N   1 
ATOM   6653  C  CA  . GLU C  1 303 ? -93.408  -17.108 57.305  1.00 27.82  ? 302 GLU E CA  1 
ATOM   6654  C  C   . GLU C  1 303 ? -92.154  -17.559 56.520  1.00 25.61  ? 302 GLU E C   1 
ATOM   6655  O  O   . GLU C  1 303 ? -91.315  -16.746 56.156  1.00 23.49  ? 302 GLU E O   1 
ATOM   6656  C  CB  . GLU C  1 303 ? -93.229  -17.218 58.818  1.00 27.05  ? 302 GLU E CB  1 
ATOM   6657  C  CG  . GLU C  1 303 ? -92.288  -16.192 59.377  1.00 31.49  ? 302 GLU E CG  1 
ATOM   6658  C  CD  . GLU C  1 303 ? -92.744  -14.775 59.049  1.00 36.90  ? 302 GLU E CD  1 
ATOM   6659  O  OE1 . GLU C  1 303 ? -93.832  -14.398 59.505  1.00 39.60  ? 302 GLU E OE1 1 
ATOM   6660  O  OE2 . GLU C  1 303 ? -92.027  -14.078 58.307  1.00 35.30  ? 302 GLU E OE2 1 
ATOM   6661  N  N   . SER C  1 304 ? -92.025  -18.864 56.267  1.00 23.29  ? 303 SER E N   1 
ATOM   6662  C  CA  . SER C  1 304 ? -90.865  -19.416 55.573  1.00 22.59  ? 303 SER E CA  1 
ATOM   6663  C  C   . SER C  1 304 ? -90.674  -18.735 54.215  1.00 24.47  ? 303 SER E C   1 
ATOM   6664  O  O   . SER C  1 304 ? -89.553  -18.464 53.820  1.00 24.32  ? 303 SER E O   1 
ATOM   6665  C  CB  . SER C  1 304 ? -90.986  -20.932 55.408  1.00 22.49  ? 303 SER E CB  1 
ATOM   6666  O  OG  . SER C  1 304 ? -89.851  -21.467 54.761  1.00 20.71  ? 303 SER E OG  1 
ATOM   6667  N  N   . THR C  1 305 ? -91.783  -18.494 53.512  1.00 25.57  ? 304 THR E N   1 
ATOM   6668  C  CA  . THR C  1 305 ? -91.796  -17.928 52.157  1.00 27.89  ? 304 THR E CA  1 
ATOM   6669  C  C   . THR C  1 305 ? -91.523  -16.413 52.183  1.00 27.95  ? 304 THR E C   1 
ATOM   6670  O  O   . THR C  1 305 ? -91.348  -15.793 51.124  1.00 28.84  ? 304 THR E O   1 
ATOM   6671  C  CB  . THR C  1 305 ? -93.173  -18.139 51.502  1.00 30.43  ? 304 THR E CB  1 
ATOM   6672  O  OG1 . THR C  1 305 ? -94.134  -17.315 52.180  1.00 34.94  ? 304 THR E OG1 1 
ATOM   6673  C  CG2 . THR C  1 305 ? -93.648  -19.567 51.579  1.00 32.08  ? 304 THR E CG2 1 
ATOM   6674  N  N   . LYS C  1 306 ? -91.476  -15.820 53.379  1.00 27.01  ? 305 LYS E N   1 
ATOM   6675  C  CA  . LYS C  1 306 ? -91.172  -14.382 53.530  1.00 29.98  ? 305 LYS E CA  1 
ATOM   6676  C  C   . LYS C  1 306 ? -89.772  -14.146 54.109  1.00 25.96  ? 305 LYS E C   1 
ATOM   6677  O  O   . LYS C  1 306 ? -88.995  -13.336 53.547  1.00 23.27  ? 305 LYS E O   1 
ATOM   6678  C  CB  . LYS C  1 306 ? -92.261  -13.721 54.378  1.00 34.98  ? 305 LYS E CB  1 
ATOM   6679  C  CG  . LYS C  1 306 ? -93.651  -13.854 53.772  1.00 42.62  ? 305 LYS E CG  1 
ATOM   6680  C  CD  . LYS C  1 306 ? -94.629  -12.800 54.223  1.00 54.09  ? 305 LYS E CD  1 
ATOM   6681  C  CE  . LYS C  1 306 ? -94.996  -12.908 55.690  1.00 64.98  ? 305 LYS E CE  1 
ATOM   6682  N  NZ  . LYS C  1 306 ? -96.222  -13.716 55.895  1.00 70.54  ? 305 LYS E NZ  1 
ATOM   6683  N  N   . THR C  1 307 ? -89.480  -14.772 55.259  1.00 23.39  ? 306 THR E N   1 
ATOM   6684  C  CA  . THR C  1 307 ? -88.282  -14.455 56.041  1.00 25.98  ? 306 THR E CA  1 
ATOM   6685  C  C   . THR C  1 307 ? -87.428  -15.692 56.346  1.00 24.46  ? 306 THR E C   1 
ATOM   6686  O  O   . THR C  1 307 ? -86.384  -15.576 56.973  1.00 23.54  ? 306 THR E O   1 
ATOM   6687  C  CB  . THR C  1 307 ? -88.679  -13.801 57.370  1.00 26.95  ? 306 THR E CB  1 
ATOM   6688  O  OG1 . THR C  1 307 ? -89.420  -14.760 58.126  1.00 26.15  ? 306 THR E OG1 1 
ATOM   6689  C  CG2 . THR C  1 307 ? -89.525  -12.558 57.179  1.00 28.48  ? 306 THR E CG2 1 
ATOM   6690  N  N   . GLY C  1 308 ? -87.913  -16.880 55.977  1.00 20.87  ? 307 GLY E N   1 
ATOM   6691  C  CA  . GLY C  1 308 ? -87.230  -18.113 56.313  1.00 20.65  ? 307 GLY E CA  1 
ATOM   6692  C  C   . GLY C  1 308 ? -87.283  -18.427 57.791  1.00 18.93  ? 307 GLY E C   1 
ATOM   6693  O  O   . GLY C  1 308 ? -86.516  -19.281 58.265  1.00 18.84  ? 307 GLY E O   1 
ATOM   6694  N  N   . ASN C  1 309 ? -88.198  -17.767 58.511  1.00 19.39  ? 308 ASN E N   1 
ATOM   6695  C  CA  . ASN C  1 309 ? -88.398  -17.942 59.965  1.00 20.35  ? 308 ASN E CA  1 
ATOM   6696  C  C   . ASN C  1 309 ? -87.134  -17.556 60.737  1.00 19.92  ? 308 ASN E C   1 
ATOM   6697  O  O   . ASN C  1 309 ? -86.861  -18.137 61.781  1.00 20.94  ? 308 ASN E O   1 
ATOM   6698  C  CB  . ASN C  1 309 ? -88.802  -19.378 60.335  1.00 20.66  ? 308 ASN E CB  1 
ATOM   6699  C  CG  . ASN C  1 309 ? -90.220  -19.713 59.918  1.00 22.55  ? 308 ASN E CG  1 
ATOM   6700  O  OD1 . ASN C  1 309 ? -91.163  -19.225 60.522  1.00 22.35  ? 308 ASN E OD1 1 
ATOM   6701  N  ND2 . ASN C  1 309 ? -90.389  -20.514 58.875  1.00 20.85  ? 308 ASN E ND2 1 
ATOM   6702  N  N   . ALA C  1 310 ? -86.367  -16.596 60.210  1.00 20.88  ? 309 ALA E N   1 
ATOM   6703  C  CA  . ALA C  1 310 ? -85.053  -16.242 60.772  1.00 20.98  ? 309 ALA E CA  1 
ATOM   6704  C  C   . ALA C  1 310 ? -85.200  -15.361 62.028  1.00 20.47  ? 309 ALA E C   1 
ATOM   6705  O  O   . ALA C  1 310 ? -84.221  -15.080 62.719  1.00 19.57  ? 309 ALA E O   1 
ATOM   6706  C  CB  . ALA C  1 310 ? -84.242  -15.546 59.719  1.00 22.20  ? 309 ALA E CB  1 
ATOM   6707  N  N   . GLY C  1 311 ? -86.415  -14.872 62.274  1.00 21.77  ? 310 GLY E N   1 
ATOM   6708  C  CA  . GLY C  1 311 ? -86.748  -14.148 63.482  1.00 23.68  ? 310 GLY E CA  1 
ATOM   6709  C  C   . GLY C  1 311 ? -86.137  -12.754 63.523  1.00 22.49  ? 310 GLY E C   1 
ATOM   6710  O  O   . GLY C  1 311 ? -85.962  -12.085 62.490  1.00 19.98  ? 310 GLY E O   1 
ATOM   6711  N  N   . SER C  1 312 ? -85.849  -12.305 64.750  1.00 22.11  ? 311 SER E N   1 
ATOM   6712  C  CA  . SER C  1 312 ? -85.475  -10.923 65.063  1.00 24.50  ? 311 SER E CA  1 
ATOM   6713  C  C   . SER C  1 312 ? -84.199  -10.499 64.333  1.00 22.97  ? 311 SER E C   1 
ATOM   6714  O  O   . SER C  1 312 ? -83.272  -11.291 64.123  1.00 21.84  ? 311 SER E O   1 
ATOM   6715  C  CB  . SER C  1 312 ? -85.268  -10.734 66.553  1.00 27.21  ? 311 SER E CB  1 
ATOM   6716  O  OG  . SER C  1 312 ? -86.470  -11.049 67.219  1.00 36.92  ? 311 SER E OG  1 
ATOM   6717  N  N   . ARG C  1 313 ? -84.116  -9.191  64.094  1.00 20.93  ? 312 ARG E N   1 
ATOM   6718  C  CA  . ARG C  1 313 ? -82.953  -8.547  63.497  1.00 22.61  ? 312 ARG E CA  1 
ATOM   6719  C  C   . ARG C  1 313 ? -81.962  -8.164  64.602  1.00 22.18  ? 312 ARG E C   1 
ATOM   6720  O  O   . ARG C  1 313 ? -82.233  -7.269  65.356  1.00 23.63  ? 312 ARG E O   1 
ATOM   6721  C  CB  . ARG C  1 313 ? -83.451  -7.340  62.709  1.00 22.34  ? 312 ARG E CB  1 
ATOM   6722  C  CG  . ARG C  1 313 ? -84.535  -7.717  61.710  1.00 22.58  ? 312 ARG E CG  1 
ATOM   6723  C  CD  . ARG C  1 313 ? -85.131  -6.553  60.962  1.00 22.19  ? 312 ARG E CD  1 
ATOM   6724  N  NE  . ARG C  1 313 ? -86.259  -6.989  60.161  1.00 20.94  ? 312 ARG E NE  1 
ATOM   6725  C  CZ  . ARG C  1 313 ? -86.772  -6.347  59.119  1.00 22.83  ? 312 ARG E CZ  1 
ATOM   6726  N  NH1 . ARG C  1 313 ? -87.759  -6.920  58.434  1.00 19.80  ? 312 ARG E NH1 1 
ATOM   6727  N  NH2 . ARG C  1 313 ? -86.300  -5.155  58.770  1.00 21.16  ? 312 ARG E NH2 1 
ATOM   6728  N  N   . LEU C  1 314 ? -80.805  -8.830  64.685  1.00 20.39  ? 313 LEU E N   1 
ATOM   6729  C  CA  . LEU C  1 314 ? -79.892  -8.622  65.795  1.00 20.62  ? 313 LEU E CA  1 
ATOM   6730  C  C   . LEU C  1 314 ? -78.963  -7.443  65.529  1.00 20.54  ? 313 LEU E C   1 
ATOM   6731  O  O   . LEU C  1 314 ? -78.541  -6.769  66.481  1.00 20.75  ? 313 LEU E O   1 
ATOM   6732  C  CB  . LEU C  1 314 ? -79.089  -9.893  66.034  1.00 22.14  ? 313 LEU E CB  1 
ATOM   6733  C  CG  . LEU C  1 314 ? -79.915  -11.078 66.539  1.00 25.33  ? 313 LEU E CG  1 
ATOM   6734  C  CD1 . LEU C  1 314 ? -78.998  -12.218 66.911  1.00 26.16  ? 313 LEU E CD1 1 
ATOM   6735  C  CD2 . LEU C  1 314 ? -80.784  -10.670 67.733  1.00 26.92  ? 313 LEU E CD2 1 
ATOM   6736  N  N   . ALA C  1 315 ? -78.587  -7.252  64.260  1.00 17.76  ? 314 ALA E N   1 
ATOM   6737  C  CA  . ALA C  1 315 ? -77.692  -6.173  63.871  1.00 18.10  ? 314 ALA E CA  1 
ATOM   6738  C  C   . ALA C  1 315 ? -77.874  -5.907  62.374  1.00 18.68  ? 314 ALA E C   1 
ATOM   6739  O  O   . ALA C  1 315 ? -78.306  -6.797  61.602  1.00 17.96  ? 314 ALA E O   1 
ATOM   6740  C  CB  . ALA C  1 315 ? -76.252  -6.514  64.198  1.00 18.09  ? 314 ALA E CB  1 
ATOM   6741  N  N   . CYS C  1 316 ? -77.584  -4.669  61.979  1.00 18.41  ? 315 CYS E N   1 
ATOM   6742  C  CA  . CYS C  1 316 ? -77.739  -4.282  60.595  1.00 18.75  ? 315 CYS E CA  1 
ATOM   6743  C  C   . CYS C  1 316 ? -76.902  -3.045  60.318  1.00 18.98  ? 315 CYS E C   1 
ATOM   6744  O  O   . CYS C  1 316 ? -76.400  -2.385  61.245  1.00 17.27  ? 315 CYS E O   1 
ATOM   6745  C  CB  . CYS C  1 316 ? -79.194  -3.980  60.268  1.00 22.10  ? 315 CYS E CB  1 
ATOM   6746  S  SG  . CYS C  1 316 ? -79.889  -2.592  61.210  1.00 25.58  ? 315 CYS E SG  1 
ATOM   6747  N  N   . GLY C  1 317 ? -76.758  -2.739  59.024  1.00 18.50  ? 316 GLY E N   1 
ATOM   6748  C  CA  . GLY C  1 317 ? -76.193  -1.496  58.619  1.00 19.55  ? 316 GLY E CA  1 
ATOM   6749  C  C   . GLY C  1 317 ? -76.442  -1.249  57.155  1.00 19.16  ? 316 GLY E C   1 
ATOM   6750  O  O   . GLY C  1 317 ? -76.843  -2.148  56.426  1.00 18.76  ? 316 GLY E O   1 
ATOM   6751  N  N   . VAL C  1 318 ? -76.209  -0.012  56.751  1.00 18.44  ? 317 VAL E N   1 
ATOM   6752  C  CA  . VAL C  1 318 ? -76.382  0.372   55.387  1.00 18.94  ? 317 VAL E CA  1 
ATOM   6753  C  C   . VAL C  1 318 ? -75.129  0.030   54.569  1.00 19.30  ? 317 VAL E C   1 
ATOM   6754  O  O   . VAL C  1 318 ? -73.991  0.224   55.006  1.00 20.22  ? 317 VAL E O   1 
ATOM   6755  C  CB  . VAL C  1 318 ? -76.748  1.861   55.274  1.00 19.81  ? 317 VAL E CB  1 
ATOM   6756  C  CG1 . VAL C  1 318 ? -77.040  2.216   53.832  1.00 19.20  ? 317 VAL E CG1 1 
ATOM   6757  C  CG2 . VAL C  1 318 ? -77.906  2.231   56.181  1.00 19.39  ? 317 VAL E CG2 1 
ATOM   6758  N  N   . ILE C  1 319 ? -75.358  -0.525  53.368  1.00 19.45  ? 318 ILE E N   1 
ATOM   6759  C  CA  . ILE C  1 319 ? -74.277  -0.977  52.519  1.00 19.10  ? 318 ILE E CA  1 
ATOM   6760  C  C   . ILE C  1 319 ? -73.752  0.231   51.752  1.00 20.55  ? 318 ILE E C   1 
ATOM   6761  O  O   . ILE C  1 319 ? -74.466  0.775   50.959  1.00 20.77  ? 318 ILE E O   1 
ATOM   6762  C  CB  . ILE C  1 319 ? -74.742  -2.102  51.590  1.00 18.71  ? 318 ILE E CB  1 
ATOM   6763  C  CG1 . ILE C  1 319 ? -75.234  -3.306  52.386  1.00 19.44  ? 318 ILE E CG1 1 
ATOM   6764  C  CG2 . ILE C  1 319 ? -73.633  -2.486  50.635  1.00 19.67  ? 318 ILE E CG2 1 
ATOM   6765  C  CD1 . ILE C  1 319 ? -76.094  -4.266  51.614  1.00 20.69  ? 318 ILE E CD1 1 
ATOM   6766  N  N   . GLY C  1 320 ? -72.489  0.596   51.984  1.00 20.84  ? 319 GLY E N   1 
ATOM   6767  C  CA  . GLY C  1 320 ? -71.890  1.781   51.404  1.00 22.47  ? 319 GLY E CA  1 
ATOM   6768  C  C   . GLY C  1 320 ? -70.823  1.457   50.374  1.00 23.22  ? 319 GLY E C   1 
ATOM   6769  O  O   . GLY C  1 320 ? -70.194  0.415   50.423  1.00 21.00  ? 319 GLY E O   1 
ATOM   6770  N  N   . ILE C  1 321 ? -70.585  2.411   49.469  1.00 23.57  ? 320 ILE E N   1 
ATOM   6771  C  CA  . ILE C  1 321 ? -69.474  2.330   48.501  1.00 24.55  ? 320 ILE E CA  1 
ATOM   6772  C  C   . ILE C  1 321 ? -68.139  2.408   49.243  1.00 24.35  ? 320 ILE E C   1 
ATOM   6773  O  O   . ILE C  1 321 ? -67.920  3.297   50.075  1.00 23.89  ? 320 ILE E O   1 
ATOM   6774  C  CB  . ILE C  1 321 ? -69.589  3.429   47.425  1.00 23.20  ? 320 ILE E CB  1 
ATOM   6775  C  CG1 . ILE C  1 321 ? -70.917  3.294   46.675  1.00 22.82  ? 320 ILE E CG1 1 
ATOM   6776  C  CG2 . ILE C  1 321 ? -68.380  3.413   46.490  1.00 24.12  ? 320 ILE E CG2 1 
ATOM   6777  C  CD1 . ILE C  1 321 ? -71.260  4.494   45.798  1.00 24.08  ? 320 ILE E CD1 1 
ATOM   6778  N  N   . ALA C  1 322 ? -67.255  1.442   48.962  1.00 24.41  ? 321 ALA E N   1 
ATOM   6779  C  CA  . ALA C  1 322 ? -65.936  1.410   49.588  1.00 29.02  ? 321 ALA E CA  1 
ATOM   6780  C  C   . ALA C  1 322 ? -64.874  1.766   48.540  1.00 30.65  ? 321 ALA E C   1 
ATOM   6781  O  O   . ALA C  1 322 ? -65.119  1.616   47.351  1.00 35.55  ? 321 ALA E O   1 
ATOM   6782  C  CB  . ALA C  1 322 ? -65.700  0.046   50.196  1.00 26.05  ? 321 ALA E CB  1 
ATOM   6783  N  N   . GLN C  1 323 ? -63.674  2.126   48.982  1.00 43.55  ? 322 GLN E N   1 
ATOM   6784  C  CA  . GLN C  1 323 ? -62.619  2.570   48.043  1.00 53.46  ? 322 GLN E CA  1 
ATOM   6785  C  C   . GLN C  1 323 ? -62.107  1.371   47.246  1.00 61.77  ? 322 GLN E C   1 
ATOM   6786  O  O   . GLN C  1 323 ? -61.688  0.448   47.937  1.00 66.44  ? 322 GLN E O   1 
ATOM   6787  C  CB  . GLN C  1 323 ? -61.462  3.248   48.769  1.00 53.37  ? 322 GLN E CB  1 
ATOM   6788  C  CG  . GLN C  1 323 ? -60.475  3.918   47.819  1.00 61.69  ? 322 GLN E CG  1 
ATOM   6789  C  CD  . GLN C  1 323 ? -59.453  4.757   48.548  1.00 64.32  ? 322 GLN E CD  1 
ATOM   6790  O  OE1 . GLN C  1 323 ? -58.744  4.276   49.430  1.00 70.01  ? 322 GLN E OE1 1 
ATOM   6791  N  NE2 . GLN C  1 323 ? -59.364  6.023   48.174  1.00 69.08  ? 322 GLN E NE2 1 
ATOM   6792  O  OXT . GLN C  1 323 ? -62.130  1.311   45.987  1.00 63.66  ? 322 GLN E OXT 1 
ATOM   6793  N  N   . ALA D  1 2   ? -61.838  -51.777 41.993  1.00 34.05  ? 1   ALA G N   1 
ATOM   6794  C  CA  . ALA D  1 2   ? -62.547  -52.997 42.479  1.00 31.17  ? 1   ALA G CA  1 
ATOM   6795  C  C   . ALA D  1 2   ? -64.057  -52.851 42.263  1.00 30.61  ? 1   ALA G C   1 
ATOM   6796  O  O   . ALA D  1 2   ? -64.554  -51.771 42.037  1.00 34.91  ? 1   ALA G O   1 
ATOM   6797  C  CB  . ALA D  1 2   ? -62.235  -53.218 43.940  1.00 34.26  ? 1   ALA G CB  1 
ATOM   6798  N  N   . THR D  1 3   ? -64.757  -53.964 42.448  1.00 26.94  ? 2   THR G N   1 
ATOM   6799  C  CA  . THR D  1 3   ? -66.201  -54.108 42.390  1.00 29.48  ? 2   THR G CA  1 
ATOM   6800  C  C   . THR D  1 3   ? -66.815  -53.982 43.797  1.00 26.98  ? 2   THR G C   1 
ATOM   6801  O  O   . THR D  1 3   ? -67.997  -53.598 43.973  1.00 24.64  ? 2   THR G O   1 
ATOM   6802  C  CB  . THR D  1 3   ? -66.447  -55.461 41.710  1.00 32.16  ? 2   THR G CB  1 
ATOM   6803  O  OG1 . THR D  1 3   ? -66.919  -55.136 40.406  1.00 44.01  ? 2   THR G OG1 1 
ATOM   6804  C  CG2 . THR D  1 3   ? -67.362  -56.399 42.443  1.00 36.30  ? 2   THR G CG2 1 
ATOM   6805  N  N   . LYS D  1 4   ? -66.020  -54.337 44.806  1.00 25.50  ? 3   LYS G N   1 
ATOM   6806  C  CA  . LYS D  1 4   ? -66.448  -54.358 46.191  1.00 27.15  ? 3   LYS G CA  1 
ATOM   6807  C  C   . LYS D  1 4   ? -65.324  -53.803 47.065  1.00 25.39  ? 3   LYS G C   1 
ATOM   6808  O  O   . LYS D  1 4   ? -64.136  -54.151 46.869  1.00 24.96  ? 3   LYS G O   1 
ATOM   6809  C  CB  . LYS D  1 4   ? -66.763  -55.806 46.587  1.00 34.36  ? 3   LYS G CB  1 
ATOM   6810  C  CG  . LYS D  1 4   ? -67.982  -55.995 47.471  1.00 45.24  ? 3   LYS G CG  1 
ATOM   6811  C  CD  . LYS D  1 4   ? -68.366  -57.453 47.737  1.00 53.01  ? 3   LYS G CD  1 
ATOM   6812  C  CE  . LYS D  1 4   ? -68.526  -58.301 46.491  1.00 57.94  ? 3   LYS G CE  1 
ATOM   6813  N  NZ  . LYS D  1 4   ? -69.519  -57.725 45.554  1.00 67.29  ? 3   LYS G NZ  1 
ATOM   6814  N  N   . ALA D  1 5   ? -65.689  -53.003 48.073  1.00 22.38  ? 4   ALA G N   1 
ATOM   6815  C  CA  . ALA D  1 5   ? -64.714  -52.456 48.987  1.00 22.41  ? 4   ALA G CA  1 
ATOM   6816  C  C   . ALA D  1 5   ? -65.295  -52.454 50.405  1.00 22.42  ? 4   ALA G C   1 
ATOM   6817  O  O   . ALA D  1 5   ? -66.499  -52.668 50.622  1.00 23.16  ? 4   ALA G O   1 
ATOM   6818  C  CB  . ALA D  1 5   ? -64.274  -51.081 48.537  1.00 20.91  ? 4   ALA G CB  1 
ATOM   6819  N  N   . VAL D  1 6   ? -64.409  -52.232 51.372  1.00 21.37  ? 5   VAL G N   1 
ATOM   6820  C  CA  . VAL D  1 6   ? -64.799  -52.274 52.741  1.00 22.42  ? 5   VAL G CA  1 
ATOM   6821  C  C   . VAL D  1 6   ? -63.882  -51.352 53.540  1.00 21.38  ? 5   VAL G C   1 
ATOM   6822  O  O   . VAL D  1 6   ? -62.745  -51.105 53.169  1.00 22.30  ? 5   VAL G O   1 
ATOM   6823  C  CB  . VAL D  1 6   ? -64.805  -53.710 53.284  1.00 23.26  ? 5   VAL G CB  1 
ATOM   6824  C  CG1 . VAL D  1 6   ? -63.400  -54.264 53.425  1.00 24.04  ? 5   VAL G CG1 1 
ATOM   6825  C  CG2 . VAL D  1 6   ? -65.552  -53.800 54.607  1.00 22.90  ? 5   VAL G CG2 1 
ATOM   6826  N  N   . CYS D  1 7   ? -64.419  -50.834 54.644  1.00 20.42  ? 6   CYS G N   1 
ATOM   6827  C  CA  . CYS D  1 7   ? -63.688  -49.931 55.498  1.00 21.02  ? 6   CYS G CA  1 
ATOM   6828  C  C   . CYS D  1 7   ? -64.046  -50.233 56.943  1.00 21.56  ? 6   CYS G C   1 
ATOM   6829  O  O   . CYS D  1 7   ? -65.236  -50.302 57.282  1.00 21.17  ? 6   CYS G O   1 
ATOM   6830  C  CB  . CYS D  1 7   ? -64.039  -48.484 55.163  1.00 22.78  ? 6   CYS G CB  1 
ATOM   6831  S  SG  . CYS D  1 7   ? -63.111  -47.289 56.149  1.00 24.96  ? 6   CYS G SG  1 
ATOM   6832  N  N   . VAL D  1 8   ? -63.022  -50.374 57.789  1.00 21.59  ? 7   VAL G N   1 
ATOM   6833  C  CA  . VAL D  1 8   ? -63.215  -50.565 59.211  1.00 20.94  ? 7   VAL G CA  1 
ATOM   6834  C  C   . VAL D  1 8   ? -62.882  -49.238 59.872  1.00 22.20  ? 7   VAL G C   1 
ATOM   6835  O  O   . VAL D  1 8   ? -61.772  -48.766 59.748  1.00 22.46  ? 7   VAL G O   1 
ATOM   6836  C  CB  . VAL D  1 8   ? -62.346  -51.713 59.749  1.00 21.90  ? 7   VAL G CB  1 
ATOM   6837  C  CG1 . VAL D  1 8   ? -62.463  -51.843 61.250  1.00 22.95  ? 7   VAL G CG1 1 
ATOM   6838  C  CG2 . VAL D  1 8   ? -62.696  -53.014 59.065  1.00 23.17  ? 7   VAL G CG2 1 
ATOM   6839  N  N   . LEU D  1 9   ? -63.881  -48.611 60.505  1.00 22.96  ? 8   LEU G N   1 
ATOM   6840  C  CA  . LEU D  1 9   ? -63.694  -47.324 61.129  1.00 23.06  ? 8   LEU G CA  1 
ATOM   6841  C  C   . LEU D  1 9   ? -63.295  -47.543 62.591  1.00 21.82  ? 8   LEU G C   1 
ATOM   6842  O  O   . LEU D  1 9   ? -64.008  -48.242 63.302  1.00 21.26  ? 8   LEU G O   1 
ATOM   6843  C  CB  . LEU D  1 9   ? -65.013  -46.539 61.059  1.00 27.94  ? 8   LEU G CB  1 
ATOM   6844  C  CG  . LEU D  1 9   ? -65.540  -46.177 59.665  1.00 31.23  ? 8   LEU G CG  1 
ATOM   6845  C  CD1 A LEU D  1 9   ? -66.984  -45.722 59.745  0.60 35.48  ? 8   LEU G CD1 1 
ATOM   6846  C  CD1 B LEU D  1 9   ? -66.988  -45.728 59.742  0.40 33.89  ? 8   LEU G CD1 1 
ATOM   6847  C  CD2 A LEU D  1 9   ? -64.719  -45.067 59.056  0.60 33.50  ? 8   LEU G CD2 1 
ATOM   6848  C  CD2 B LEU D  1 9   ? -64.710  -45.072 59.050  0.40 32.52  ? 8   LEU G CD2 1 
ATOM   6849  N  N   . LYS D  1 10  ? -62.224  -46.882 63.030  1.00 21.86  ? 9   LYS G N   1 
ATOM   6850  C  CA  . LYS D  1 10  ? -61.843  -46.843 64.416  1.00 26.30  ? 9   LYS G CA  1 
ATOM   6851  C  C   . LYS D  1 10  ? -61.302  -45.456 64.709  1.00 23.89  ? 9   LYS G C   1 
ATOM   6852  O  O   . LYS D  1 10  ? -60.865  -44.759 63.799  1.00 24.73  ? 9   LYS G O   1 
ATOM   6853  C  CB  . LYS D  1 10  ? -60.688  -47.796 64.755  1.00 31.63  ? 9   LYS G CB  1 
ATOM   6854  C  CG  . LYS D  1 10  ? -60.818  -49.234 64.279  1.00 38.91  ? 9   LYS G CG  1 
ATOM   6855  C  CD  . LYS D  1 10  ? -62.117  -49.940 64.651  1.00 49.27  ? 9   LYS G CD  1 
ATOM   6856  C  CE  . LYS D  1 10  ? -62.585  -49.764 66.087  1.00 62.98  ? 9   LYS G CE  1 
ATOM   6857  N  NZ  . LYS D  1 10  ? -61.587  -50.172 67.107  1.00 69.73  ? 9   LYS G NZ  1 
ATOM   6858  N  N   . GLY D  1 11  ? -61.256  -45.119 65.996  1.00 24.97  ? 10  GLY G N   1 
ATOM   6859  C  CA  . GLY D  1 11  ? -60.736  -43.837 66.469  1.00 28.71  ? 10  GLY G CA  1 
ATOM   6860  C  C   . GLY D  1 11  ? -60.194  -43.928 67.892  1.00 28.77  ? 10  GLY G C   1 
ATOM   6861  O  O   . GLY D  1 11  ? -60.052  -45.019 68.447  1.00 25.42  ? 10  GLY G O   1 
ATOM   6862  N  N   . ASP D  1 12  ? -59.919  -42.765 68.471  1.00 32.13  ? 11  ASP G N   1 
ATOM   6863  C  CA  . ASP D  1 12  ? -59.421  -42.647 69.841  1.00 38.75  ? 11  ASP G CA  1 
ATOM   6864  C  C   . ASP D  1 12  ? -60.531  -42.887 70.861  1.00 37.27  ? 11  ASP G C   1 
ATOM   6865  O  O   . ASP D  1 12  ? -60.245  -43.143 72.016  1.00 44.07  ? 11  ASP G O   1 
ATOM   6866  C  CB  . ASP D  1 12  ? -58.838  -41.264 70.120  1.00 45.89  ? 11  ASP G CB  1 
ATOM   6867  C  CG  . ASP D  1 12  ? -57.539  -41.030 69.380  1.00 56.03  ? 11  ASP G CG  1 
ATOM   6868  O  OD1 . ASP D  1 12  ? -56.785  -42.009 69.214  1.00 59.36  ? 11  ASP G OD1 1 
ATOM   6869  O  OD2 . ASP D  1 12  ? -57.312  -39.882 68.951  1.00 66.94  ? 11  ASP G OD2 1 
ATOM   6870  N  N   . GLY D  1 13  ? -61.788  -42.797 70.433  1.00 31.05  ? 12  GLY G N   1 
ATOM   6871  C  CA  . GLY D  1 13  ? -62.902  -42.952 71.308  1.00 27.79  ? 12  GLY G CA  1 
ATOM   6872  C  C   . GLY D  1 13  ? -63.644  -44.247 71.027  1.00 27.20  ? 12  GLY G C   1 
ATOM   6873  O  O   . GLY D  1 13  ? -63.074  -45.203 70.502  1.00 27.84  ? 12  GLY G O   1 
ATOM   6874  N  N   . PRO D  1 14  ? -64.946  -44.306 71.377  1.00 25.65  ? 13  PRO G N   1 
ATOM   6875  C  CA  . PRO D  1 14  ? -65.725  -45.525 71.200  1.00 26.36  ? 13  PRO G CA  1 
ATOM   6876  C  C   . PRO D  1 14  ? -66.326  -45.730 69.807  1.00 24.65  ? 13  PRO G C   1 
ATOM   6877  O  O   . PRO D  1 14  ? -66.999  -46.712 69.605  1.00 26.39  ? 13  PRO G O   1 
ATOM   6878  C  CB  . PRO D  1 14  ? -66.858  -45.316 72.207  1.00 27.76  ? 13  PRO G CB  1 
ATOM   6879  C  CG  . PRO D  1 14  ? -67.083  -43.816 72.221  1.00 26.07  ? 13  PRO G CG  1 
ATOM   6880  C  CD  . PRO D  1 14  ? -65.715  -43.212 71.998  1.00 27.35  ? 13  PRO G CD  1 
ATOM   6881  N  N   . VAL D  1 15  ? -66.145  -44.778 68.889  1.00 23.43  ? 14  VAL G N   1 
ATOM   6882  C  CA  . VAL D  1 15  ? -66.825  -44.889 67.612  1.00 23.50  ? 14  VAL G CA  1 
ATOM   6883  C  C   . VAL D  1 15  ? -66.134  -45.978 66.791  1.00 24.51  ? 14  VAL G C   1 
ATOM   6884  O  O   . VAL D  1 15  ? -64.929  -45.907 66.571  1.00 26.08  ? 14  VAL G O   1 
ATOM   6885  C  CB  . VAL D  1 15  ? -66.837  -43.559 66.849  1.00 22.85  ? 14  VAL G CB  1 
ATOM   6886  C  CG1 . VAL D  1 15  ? -67.436  -43.745 65.466  1.00 24.20  ? 14  VAL G CG1 1 
ATOM   6887  C  CG2 . VAL D  1 15  ? -67.577  -42.483 67.618  1.00 24.13  ? 14  VAL G CG2 1 
ATOM   6888  N  N   . GLN D  1 16  ? -66.914  -46.939 66.304  1.00 24.42  ? 15  GLN G N   1 
ATOM   6889  C  CA  . GLN D  1 16  ? -66.383  -47.978 65.465  1.00 27.47  ? 15  GLN G CA  1 
ATOM   6890  C  C   . GLN D  1 16  ? -67.462  -48.523 64.531  1.00 26.29  ? 15  GLN G C   1 
ATOM   6891  O  O   . GLN D  1 16  ? -68.645  -48.519 64.837  1.00 26.59  ? 15  GLN G O   1 
ATOM   6892  C  CB  . GLN D  1 16  ? -65.775  -49.112 66.304  1.00 29.98  ? 15  GLN G CB  1 
ATOM   6893  C  CG  . GLN D  1 16  ? -66.718  -49.827 67.254  1.00 33.33  ? 15  GLN G CG  1 
ATOM   6894  C  CD  . GLN D  1 16  ? -65.979  -50.879 68.061  1.00 37.58  ? 15  GLN G CD  1 
ATOM   6895  O  OE1 . GLN D  1 16  ? -66.061  -50.941 69.289  1.00 39.83  ? 15  GLN G OE1 1 
ATOM   6896  N  NE2 . GLN D  1 16  ? -65.225  -51.714 67.373  1.00 37.14  ? 15  GLN G NE2 1 
ATOM   6897  N  N   . GLY D  1 17  ? -67.026  -49.050 63.391  1.00 25.42  ? 16  GLY G N   1 
ATOM   6898  C  CA  . GLY D  1 17  ? -67.956  -49.639 62.470  1.00 25.00  ? 16  GLY G CA  1 
ATOM   6899  C  C   . GLY D  1 17  ? -67.303  -50.231 61.244  1.00 21.93  ? 16  GLY G C   1 
ATOM   6900  O  O   . GLY D  1 17  ? -66.090  -50.191 61.057  1.00 21.82  ? 16  GLY G O   1 
ATOM   6901  N  N   . ILE D  1 18  ? -68.163  -50.793 60.410  1.00 22.27  ? 17  ILE G N   1 
ATOM   6902  C  CA  . ILE D  1 18  ? -67.785  -51.400 59.162  1.00 22.53  ? 17  ILE G CA  1 
ATOM   6903  C  C   . ILE D  1 18  ? -68.709  -50.844 58.083  1.00 21.85  ? 17  ILE G C   1 
ATOM   6904  O  O   . ILE D  1 18  ? -69.920  -50.938 58.194  1.00 22.80  ? 17  ILE G O   1 
ATOM   6905  C  CB  . ILE D  1 18  ? -67.897  -52.934 59.256  1.00 23.69  ? 17  ILE G CB  1 
ATOM   6906  C  CG1 . ILE D  1 18  ? -66.878  -53.516 60.245  1.00 26.49  ? 17  ILE G CG1 1 
ATOM   6907  C  CG2 . ILE D  1 18  ? -67.787  -53.551 57.868  1.00 23.26  ? 17  ILE G CG2 1 
ATOM   6908  C  CD1 . ILE D  1 18  ? -67.065  -54.998 60.504  1.00 28.17  ? 17  ILE G CD1 1 
ATOM   6909  N  N   . ILE D  1 19  ? -68.113  -50.321 57.023  1.00 20.72  ? 18  ILE G N   1 
ATOM   6910  C  CA  . ILE D  1 19  ? -68.859  -49.821 55.903  1.00 21.64  ? 18  ILE G CA  1 
ATOM   6911  C  C   . ILE D  1 19  ? -68.398  -50.577 54.651  1.00 21.66  ? 18  ILE G C   1 
ATOM   6912  O  O   . ILE D  1 19  ? -67.192  -50.672 54.406  1.00 20.79  ? 18  ILE G O   1 
ATOM   6913  C  CB  . ILE D  1 19  ? -68.657  -48.300 55.754  1.00 20.41  ? 18  ILE G CB  1 
ATOM   6914  C  CG1 . ILE D  1 19  ? -69.163  -47.499 56.962  1.00 21.94  ? 18  ILE G CG1 1 
ATOM   6915  C  CG2 . ILE D  1 19  ? -69.279  -47.824 54.453  1.00 21.03  ? 18  ILE G CG2 1 
ATOM   6916  C  CD1 . ILE D  1 19  ? -70.672  -47.555 57.165  1.00 21.38  ? 18  ILE G CD1 1 
ATOM   6917  N  N   . ASN D  1 20  ? -69.389  -51.065 53.892  1.00 20.37  ? 19  ASN G N   1 
ATOM   6918  C  CA  . ASN D  1 20  ? -69.278  -51.770 52.628  1.00 21.75  ? 19  ASN G CA  1 
ATOM   6919  C  C   . ASN D  1 20  ? -69.605  -50.823 51.471  1.00 21.06  ? 19  ASN G C   1 
ATOM   6920  O  O   . ASN D  1 20  ? -70.442  -49.927 51.608  1.00 21.68  ? 19  ASN G O   1 
ATOM   6921  C  CB  . ASN D  1 20  ? -70.237  -52.963 52.565  1.00 23.75  ? 19  ASN G CB  1 
ATOM   6922  C  CG  . ASN D  1 20  ? -70.109  -53.857 53.781  1.00 26.53  ? 19  ASN G CG  1 
ATOM   6923  O  OD1 . ASN D  1 20  ? -69.121  -54.564 53.902  1.00 27.39  ? 19  ASN G OD1 1 
ATOM   6924  N  ND2 . ASN D  1 20  ? -71.046  -53.770 54.720  1.00 26.59  ? 19  ASN G ND2 1 
ATOM   6925  N  N   . PHE D  1 21  ? -68.911  -51.045 50.350  1.00 20.53  ? 20  PHE G N   1 
ATOM   6926  C  CA  . PHE D  1 21  ? -69.084  -50.378 49.113  1.00 21.46  ? 20  PHE G CA  1 
ATOM   6927  C  C   . PHE D  1 21  ? -69.260  -51.432 48.025  1.00 24.15  ? 20  PHE G C   1 
ATOM   6928  O  O   . PHE D  1 21  ? -68.526  -52.414 47.998  1.00 24.23  ? 20  PHE G O   1 
ATOM   6929  C  CB  . PHE D  1 21  ? -67.887  -49.494 48.753  1.00 21.43  ? 20  PHE G CB  1 
ATOM   6930  C  CG  . PHE D  1 21  ? -67.522  -48.442 49.772  1.00 21.96  ? 20  PHE G CG  1 
ATOM   6931  C  CD1 . PHE D  1 21  ? -67.912  -47.128 49.605  1.00 20.47  ? 20  PHE G CD1 1 
ATOM   6932  C  CD2 . PHE D  1 21  ? -66.790  -48.778 50.911  1.00 22.04  ? 20  PHE G CD2 1 
ATOM   6933  C  CE1 . PHE D  1 21  ? -67.580  -46.162 50.545  1.00 21.06  ? 20  PHE G CE1 1 
ATOM   6934  C  CE2 . PHE D  1 21  ? -66.447  -47.813 51.843  1.00 20.82  ? 20  PHE G CE2 1 
ATOM   6935  C  CZ  . PHE D  1 21  ? -66.838  -46.506 51.653  1.00 21.72  ? 20  PHE G CZ  1 
ATOM   6936  N  N   . GLU D  1 22  ? -70.215  -51.208 47.119  1.00 22.69  ? 21  GLU G N   1 
ATOM   6937  C  CA  . GLU D  1 22  ? -70.412  -52.109 45.992  1.00 25.09  ? 21  GLU G CA  1 
ATOM   6938  C  C   . GLU D  1 22  ? -70.710  -51.298 44.736  1.00 25.40  ? 21  GLU G C   1 
ATOM   6939  O  O   . GLU D  1 22  ? -71.561  -50.402 44.751  1.00 25.37  ? 21  GLU G O   1 
ATOM   6940  C  CB  . GLU D  1 22  ? -71.548  -53.081 46.292  1.00 27.70  ? 21  GLU G CB  1 
ATOM   6941  C  CG  . GLU D  1 22  ? -71.796  -54.096 45.202  1.00 36.92  ? 21  GLU G CG  1 
ATOM   6942  C  CD  . GLU D  1 22  ? -72.771  -55.168 45.667  1.00 44.39  ? 21  GLU G CD  1 
ATOM   6943  O  OE1 . GLU D  1 22  ? -73.977  -55.009 45.414  1.00 53.04  ? 21  GLU G OE1 1 
ATOM   6944  O  OE2 . GLU D  1 22  ? -72.326  -56.113 46.348  1.00 51.47  ? 21  GLU G OE2 1 
ATOM   6945  N  N   . GLN D  1 23  ? -70.031  -51.649 43.654  1.00 24.71  ? 22  GLN G N   1 
ATOM   6946  C  CA  . GLN D  1 23  ? -70.205  -51.016 42.366  1.00 25.61  ? 22  GLN G CA  1 
ATOM   6947  C  C   . GLN D  1 23  ? -70.079  -52.096 41.282  1.00 30.06  ? 22  GLN G C   1 
ATOM   6948  O  O   . GLN D  1 23  ? -68.977  -52.408 40.818  1.00 31.48  ? 22  GLN G O   1 
ATOM   6949  C  CB  . GLN D  1 23  ? -69.156  -49.929 42.169  1.00 24.82  ? 22  GLN G CB  1 
ATOM   6950  C  CG  . GLN D  1 23  ? -69.406  -49.078 40.937  1.00 24.80  ? 22  GLN G CG  1 
ATOM   6951  C  CD  . GLN D  1 23  ? -68.265  -48.127 40.695  1.00 27.61  ? 22  GLN G CD  1 
ATOM   6952  O  OE1 . GLN D  1 23  ? -67.140  -48.418 41.083  1.00 27.12  ? 22  GLN G OE1 1 
ATOM   6953  N  NE2 . GLN D  1 23  ? -68.550  -46.981 40.077  1.00 25.83  ? 22  GLN G NE2 1 
ATOM   6954  N  N   . LYS D  1 24  ? -71.225  -52.603 40.848  1.00 33.39  ? 23  LYS G N   1 
ATOM   6955  C  CA  . LYS D  1 24  ? -71.267  -53.778 39.986  1.00 41.64  ? 23  LYS G CA  1 
ATOM   6956  C  C   . LYS D  1 24  ? -70.951  -53.344 38.551  1.00 41.12  ? 23  LYS G C   1 
ATOM   6957  O  O   . LYS D  1 24  ? -70.433  -54.132 37.803  1.00 44.97  ? 23  LYS G O   1 
ATOM   6958  C  CB  . LYS D  1 24  ? -72.569  -54.569 40.174  1.00 49.29  ? 23  LYS G CB  1 
ATOM   6959  C  CG  . LYS D  1 24  ? -73.886  -53.865 39.839  1.00 59.96  ? 23  LYS G CG  1 
ATOM   6960  C  CD  . LYS D  1 24  ? -74.312  -52.672 40.709  1.00 67.76  ? 23  LYS G CD  1 
ATOM   6961  C  CE  . LYS D  1 24  ? -74.003  -52.752 42.200  1.00 63.50  ? 23  LYS G CE  1 
ATOM   6962  N  NZ  . LYS D  1 24  ? -73.947  -51.397 42.807  1.00 59.97  ? 23  LYS G NZ  1 
ATOM   6963  N  N   . GLU D  1 25  ? -71.168  -52.066 38.215  1.00 38.80  ? 24  GLU G N   1 
ATOM   6964  C  CA  . GLU D  1 25  ? -70.787  -51.505 36.918  1.00 40.93  ? 24  GLU G CA  1 
ATOM   6965  C  C   . GLU D  1 25  ? -69.885  -50.281 37.128  1.00 37.95  ? 24  GLU G C   1 
ATOM   6966  O  O   . GLU D  1 25  ? -70.205  -49.424 37.950  1.00 33.85  ? 24  GLU G O   1 
ATOM   6967  C  CB  . GLU D  1 25  ? -72.053  -51.087 36.161  1.00 49.17  ? 24  GLU G CB  1 
ATOM   6968  C  CG  . GLU D  1 25  ? -73.010  -52.227 35.861  1.00 56.37  ? 24  GLU G CG  1 
ATOM   6969  C  CD  . GLU D  1 25  ? -72.449  -53.300 34.939  1.00 66.50  ? 24  GLU G CD  1 
ATOM   6970  O  OE1 . GLU D  1 25  ? -71.406  -53.045 34.285  1.00 77.58  ? 24  GLU G OE1 1 
ATOM   6971  O  OE2 . GLU D  1 25  ? -73.051  -54.394 34.880  1.00 78.95  ? 24  GLU G OE2 1 
ATOM   6972  N  N   . SER D  1 26  ? -68.808  -50.148 36.344  1.00 35.16  ? 25  SER G N   1 
ATOM   6973  C  CA  . SER D  1 26  ? -67.843  -49.056 36.576  1.00 38.27  ? 25  SER G CA  1 
ATOM   6974  C  C   . SER D  1 26  ? -68.428  -47.702 36.153  1.00 37.62  ? 25  SER G C   1 
ATOM   6975  O  O   . SER D  1 26  ? -67.941  -46.644 36.575  1.00 37.78  ? 25  SER G O   1 
ATOM   6976  C  CB  . SER D  1 26  ? -66.537  -49.320 35.882  1.00 42.10  ? 25  SER G CB  1 
ATOM   6977  O  OG  . SER D  1 26  ? -66.685  -49.198 34.477  1.00 42.54  ? 25  SER G OG  1 
ATOM   6978  N  N   . ASN D  1 27  ? -69.481  -47.735 35.336  1.00 33.91  ? 26  ASN G N   1 
ATOM   6979  C  CA  . ASN D  1 27  ? -70.171  -46.510 34.907  1.00 40.18  ? 26  ASN G CA  1 
ATOM   6980  C  C   . ASN D  1 27  ? -71.415  -46.278 35.776  1.00 39.12  ? 26  ASN G C   1 
ATOM   6981  O  O   . ASN D  1 27  ? -72.292  -45.469 35.421  1.00 42.70  ? 26  ASN G O   1 
ATOM   6982  C  CB  . ASN D  1 27  ? -70.543  -46.559 33.418  1.00 42.31  ? 26  ASN G CB  1 
ATOM   6983  C  CG  . ASN D  1 27  ? -71.703  -47.493 33.120  1.00 46.45  ? 26  ASN G CG  1 
ATOM   6984  O  OD1 . ASN D  1 27  ? -71.935  -48.462 33.841  1.00 48.98  ? 26  ASN G OD1 1 
ATOM   6985  N  ND2 . ASN D  1 27  ? -72.445  -47.213 32.060  1.00 47.86  ? 26  ASN G ND2 1 
ATOM   6986  N  N   . GLY D  1 28  ? -71.515  -47.013 36.892  1.00 36.11  ? 27  GLY G N   1 
ATOM   6987  C  CA  . GLY D  1 28  ? -72.725  -47.026 37.680  1.00 33.22  ? 27  GLY G CA  1 
ATOM   6988  C  C   . GLY D  1 28  ? -72.488  -46.458 39.071  1.00 30.21  ? 27  GLY G C   1 
ATOM   6989  O  O   . GLY D  1 28  ? -71.361  -46.176 39.454  1.00 27.65  ? 27  GLY G O   1 
ATOM   6990  N  N   . PRO D  1 29  ? -73.564  -46.303 39.859  1.00 29.05  ? 28  PRO G N   1 
ATOM   6991  C  CA  . PRO D  1 29  ? -73.472  -45.765 41.212  1.00 27.79  ? 28  PRO G CA  1 
ATOM   6992  C  C   . PRO D  1 29  ? -72.758  -46.735 42.156  1.00 25.46  ? 28  PRO G C   1 
ATOM   6993  O  O   . PRO D  1 29  ? -72.718  -47.964 41.895  1.00 23.35  ? 28  PRO G O   1 
ATOM   6994  C  CB  . PRO D  1 29  ? -74.940  -45.650 41.674  1.00 28.96  ? 28  PRO G CB  1 
ATOM   6995  C  CG  . PRO D  1 29  ? -75.756  -45.775 40.403  1.00 32.95  ? 28  PRO G CG  1 
ATOM   6996  C  CD  . PRO D  1 29  ? -74.940  -46.664 39.493  1.00 30.67  ? 28  PRO G CD  1 
ATOM   6997  N  N   . VAL D  1 30  ? -72.272  -46.200 43.275  1.00 24.13  ? 29  VAL G N   1 
ATOM   6998  C  CA  . VAL D  1 30  ? -71.718  -47.026 44.345  1.00 23.20  ? 29  VAL G CA  1 
ATOM   6999  C  C   . VAL D  1 30  ? -72.747  -47.110 45.477  1.00 26.20  ? 29  VAL G C   1 
ATOM   7000  O  O   . VAL D  1 30  ? -73.198  -46.066 46.008  1.00 27.82  ? 29  VAL G O   1 
ATOM   7001  C  CB  . VAL D  1 30  ? -70.396  -46.415 44.850  1.00 24.42  ? 29  VAL G CB  1 
ATOM   7002  C  CG1 . VAL D  1 30  ? -69.778  -47.249 45.951  1.00 23.35  ? 29  VAL G CG1 1 
ATOM   7003  C  CG2 . VAL D  1 30  ? -69.404  -46.168 43.724  1.00 25.17  ? 29  VAL G CG2 1 
ATOM   7004  N  N   . LYS D  1 31  ? -73.093  -48.328 45.885  1.00 24.88  ? 30  LYS G N   1 
ATOM   7005  C  CA  . LYS D  1 31  ? -73.882  -48.530 47.071  1.00 28.83  ? 30  LYS G CA  1 
ATOM   7006  C  C   . LYS D  1 31  ? -72.959  -48.528 48.291  1.00 26.73  ? 30  LYS G C   1 
ATOM   7007  O  O   . LYS D  1 31  ? -71.905  -49.198 48.295  1.00 22.40  ? 30  LYS G O   1 
ATOM   7008  C  CB  . LYS D  1 31  ? -74.621  -49.868 47.028  1.00 36.20  ? 30  LYS G CB  1 
ATOM   7009  C  CG  . LYS D  1 31  ? -75.818  -49.947 46.090  1.00 48.43  ? 30  LYS G CG  1 
ATOM   7010  C  CD  . LYS D  1 31  ? -76.582  -51.277 46.225  1.00 61.38  ? 30  LYS G CD  1 
ATOM   7011  C  CE  . LYS D  1 31  ? -77.274  -51.450 47.572  1.00 70.02  ? 30  LYS G CE  1 
ATOM   7012  N  NZ  . LYS D  1 31  ? -77.047  -52.789 48.180  1.00 72.08  ? 30  LYS G NZ  1 
ATOM   7013  N  N   . VAL D  1 32  ? -73.377  -47.811 49.338  1.00 21.79  ? 31  VAL G N   1 
ATOM   7014  C  CA  . VAL D  1 32  ? -72.610  -47.671 50.576  1.00 22.36  ? 31  VAL G CA  1 
ATOM   7015  C  C   . VAL D  1 32  ? -73.518  -48.059 51.737  1.00 24.33  ? 31  VAL G C   1 
ATOM   7016  O  O   . VAL D  1 32  ? -74.583  -47.444 51.928  1.00 24.77  ? 31  VAL G O   1 
ATOM   7017  C  CB  . VAL D  1 32  ? -72.063  -46.242 50.755  1.00 22.21  ? 31  VAL G CB  1 
ATOM   7018  C  CG1 . VAL D  1 32  ? -71.157  -46.108 51.975  1.00 22.95  ? 31  VAL G CG1 1 
ATOM   7019  C  CG2 . VAL D  1 32  ? -71.363  -45.737 49.505  1.00 21.83  ? 31  VAL G CG2 1 
ATOM   7020  N  N   . TRP D  1 33  ? -73.112  -49.061 52.526  1.00 23.10  ? 32  TRP G N   1 
ATOM   7021  C  CA  . TRP D  1 33  ? -73.964  -49.521 53.628  1.00 22.33  ? 32  TRP G CA  1 
ATOM   7022  C  C   . TRP D  1 33  ? -73.147  -50.193 54.720  1.00 23.16  ? 32  TRP G C   1 
ATOM   7023  O  O   . TRP D  1 33  ? -72.070  -50.688 54.468  1.00 24.62  ? 32  TRP G O   1 
ATOM   7024  C  CB  . TRP D  1 33  ? -75.072  -50.452 53.116  1.00 24.24  ? 32  TRP G CB  1 
ATOM   7025  C  CG  . TRP D  1 33  ? -74.648  -51.868 52.889  1.00 25.43  ? 32  TRP G CG  1 
ATOM   7026  C  CD1 . TRP D  1 33  ? -74.805  -52.921 53.740  1.00 26.51  ? 32  TRP G CD1 1 
ATOM   7027  C  CD2 . TRP D  1 33  ? -73.921  -52.370 51.753  1.00 27.25  ? 32  TRP G CD2 1 
ATOM   7028  N  NE1 . TRP D  1 33  ? -74.261  -54.048 53.189  1.00 27.75  ? 32  TRP G NE1 1 
ATOM   7029  C  CE2 . TRP D  1 33  ? -73.724  -53.748 51.965  1.00 28.23  ? 32  TRP G CE2 1 
ATOM   7030  C  CE3 . TRP D  1 33  ? -73.433  -51.798 50.575  1.00 29.17  ? 32  TRP G CE3 1 
ATOM   7031  C  CZ2 . TRP D  1 33  ? -73.055  -54.557 51.043  1.00 29.53  ? 32  TRP G CZ2 1 
ATOM   7032  C  CZ3 . TRP D  1 33  ? -72.774  -52.591 49.662  1.00 30.67  ? 32  TRP G CZ3 1 
ATOM   7033  C  CH2 . TRP D  1 33  ? -72.587  -53.959 49.896  1.00 31.49  ? 32  TRP G CH2 1 
ATOM   7034  N  N   . GLY D  1 34  ? -73.697  -50.175 55.930  1.00 23.38  ? 33  GLY G N   1 
ATOM   7035  C  CA  . GLY D  1 34  ? -73.126  -50.854 57.070  1.00 23.35  ? 33  GLY G CA  1 
ATOM   7036  C  C   . GLY D  1 34  ? -73.585  -50.198 58.350  1.00 24.96  ? 33  GLY G C   1 
ATOM   7037  O  O   . GLY D  1 34  ? -74.612  -49.579 58.370  1.00 25.50  ? 33  GLY G O   1 
ATOM   7038  N  N   . SER D  1 35  ? -72.802  -50.344 59.409  1.00 25.92  ? 34  SER G N   1 
ATOM   7039  C  CA  . SER D  1 35  ? -73.185  -49.935 60.740  1.00 26.49  ? 34  SER G CA  1 
ATOM   7040  C  C   . SER D  1 35  ? -72.003  -49.236 61.394  1.00 26.88  ? 34  SER G C   1 
ATOM   7041  O  O   . SER D  1 35  ? -70.900  -49.759 61.345  1.00 24.93  ? 34  SER G O   1 
ATOM   7042  C  CB  . SER D  1 35  ? -73.604  -51.111 61.593  1.00 30.03  ? 34  SER G CB  1 
ATOM   7043  O  OG  . SER D  1 35  ? -74.978  -51.378 61.404  1.00 44.37  ? 34  SER G OG  1 
ATOM   7044  N  N   . ILE D  1 36  ? -72.273  -48.100 62.042  1.00 23.68  ? 35  ILE G N   1 
ATOM   7045  C  CA  . ILE D  1 36  ? -71.322  -47.434 62.899  1.00 23.90  ? 35  ILE G CA  1 
ATOM   7046  C  C   . ILE D  1 36  ? -71.992  -47.307 64.261  1.00 25.51  ? 35  ILE G C   1 
ATOM   7047  O  O   . ILE D  1 36  ? -73.179  -46.961 64.313  1.00 27.00  ? 35  ILE G O   1 
ATOM   7048  C  CB  . ILE D  1 36  ? -70.936  -46.058 62.350  1.00 24.66  ? 35  ILE G CB  1 
ATOM   7049  C  CG1 . ILE D  1 36  ? -70.535  -46.099 60.876  1.00 23.87  ? 35  ILE G CG1 1 
ATOM   7050  C  CG2 . ILE D  1 36  ? -69.866  -45.436 63.222  1.00 23.53  ? 35  ILE G CG2 1 
ATOM   7051  C  CD1 . ILE D  1 36  ? -70.436  -44.720 60.245  1.00 25.40  ? 35  ILE G CD1 1 
ATOM   7052  N  N   . LYS D  1 37  ? -71.259  -47.611 65.334  1.00 23.85  ? 36  LYS G N   1 
ATOM   7053  C  CA  . LYS D  1 37  ? -71.804  -47.547 66.676  1.00 26.25  ? 36  LYS G CA  1 
ATOM   7054  C  C   . LYS D  1 37  ? -70.902  -46.676 67.544  1.00 24.94  ? 36  LYS G C   1 
ATOM   7055  O  O   . LYS D  1 37  ? -69.835  -46.242 67.109  1.00 25.14  ? 36  LYS G O   1 
ATOM   7056  C  CB  . LYS D  1 37  ? -71.999  -48.956 67.238  1.00 29.19  ? 36  LYS G CB  1 
ATOM   7057  C  CG  . LYS D  1 37  ? -70.719  -49.734 67.489  1.00 35.07  ? 36  LYS G CG  1 
ATOM   7058  C  CD  . LYS D  1 37  ? -70.996  -51.204 67.798  1.00 39.54  ? 36  LYS G CD  1 
ATOM   7059  C  CE  . LYS D  1 37  ? -69.731  -52.030 67.904  1.00 43.57  ? 36  LYS G CE  1 
ATOM   7060  N  NZ  . LYS D  1 37  ? -70.045  -53.478 67.934  1.00 44.83  ? 36  LYS G NZ  1 
ATOM   7061  N  N   . GLY D  1 38  ? -71.369  -46.393 68.765  1.00 23.67  ? 37  GLY G N   1 
ATOM   7062  C  CA  . GLY D  1 38  ? -70.659  -45.533 69.687  1.00 23.70  ? 37  GLY G CA  1 
ATOM   7063  C  C   . GLY D  1 38  ? -70.806  -44.049 69.366  1.00 23.34  ? 37  GLY G C   1 
ATOM   7064  O  O   . GLY D  1 38  ? -70.028  -43.238 69.852  1.00 23.83  ? 37  GLY G O   1 
ATOM   7065  N  N   . LEU D  1 39  ? -71.800  -43.692 68.549  1.00 23.54  ? 38  LEU G N   1 
ATOM   7066  C  CA  . LEU D  1 39  ? -72.063  -42.284 68.167  1.00 23.35  ? 38  LEU G CA  1 
ATOM   7067  C  C   . LEU D  1 39  ? -73.144  -41.684 69.061  1.00 24.47  ? 38  LEU G C   1 
ATOM   7068  O  O   . LEU D  1 39  ? -74.055  -42.376 69.456  1.00 29.44  ? 38  LEU G O   1 
ATOM   7069  C  CB  . LEU D  1 39  ? -72.561  -42.230 66.721  1.00 22.27  ? 38  LEU G CB  1 
ATOM   7070  C  CG  . LEU D  1 39  ? -71.546  -42.546 65.632  1.00 23.29  ? 38  LEU G CG  1 
ATOM   7071  C  CD1 . LEU D  1 39  ? -72.249  -42.798 64.310  1.00 25.19  ? 38  LEU G CD1 1 
ATOM   7072  C  CD2 . LEU D  1 39  ? -70.526  -41.418 65.506  1.00 23.53  ? 38  LEU G CD2 1 
ATOM   7073  N  N   . THR D  1 40  ? -73.079  -40.371 69.278  1.00 26.22  ? 39  THR G N   1 
ATOM   7074  C  CA  . THR D  1 40  ? -74.185  -39.631 69.873  1.00 27.41  ? 39  THR G CA  1 
ATOM   7075  C  C   . THR D  1 40  ? -75.358  -39.560 68.888  1.00 28.21  ? 39  THR G C   1 
ATOM   7076  O  O   . THR D  1 40  ? -75.172  -39.497 67.677  1.00 26.05  ? 39  THR G O   1 
ATOM   7077  C  CB  . THR D  1 40  ? -73.729  -38.234 70.283  1.00 28.59  ? 39  THR G CB  1 
ATOM   7078  O  OG1 . THR D  1 40  ? -73.232  -37.602 69.111  1.00 30.54  ? 39  THR G OG1 1 
ATOM   7079  C  CG2 . THR D  1 40  ? -72.643  -38.259 71.332  1.00 31.24  ? 39  THR G CG2 1 
ATOM   7080  N  N   . GLU D  1 41  ? -76.583  -39.594 69.417  1.00 29.80  ? 40  GLU G N   1 
ATOM   7081  C  CA  . GLU D  1 41  ? -77.797  -39.546 68.589  1.00 31.31  ? 40  GLU G CA  1 
ATOM   7082  C  C   . GLU D  1 41  ? -77.767  -38.287 67.715  1.00 28.69  ? 40  GLU G C   1 
ATOM   7083  O  O   . GLU D  1 41  ? -77.349  -37.247 68.175  1.00 29.25  ? 40  GLU G O   1 
ATOM   7084  C  CB  . GLU D  1 41  ? -79.047  -39.546 69.474  1.00 35.67  ? 40  GLU G CB  1 
ATOM   7085  C  CG  . GLU D  1 41  ? -80.351  -39.600 68.696  1.00 38.79  ? 40  GLU G CG  1 
ATOM   7086  C  CD  . GLU D  1 41  ? -81.589  -39.602 69.583  1.00 46.06  ? 40  GLU G CD  1 
ATOM   7087  O  OE1 . GLU D  1 41  ? -82.699  -39.625 69.029  1.00 49.09  ? 40  GLU G OE1 1 
ATOM   7088  O  OE2 . GLU D  1 41  ? -81.436  -39.601 70.829  1.00 43.24  ? 40  GLU G OE2 1 
ATOM   7089  N  N   . GLY D  1 42  ? -78.160  -38.427 66.443  1.00 26.59  ? 41  GLY G N   1 
ATOM   7090  C  CA  . GLY D  1 42  ? -78.263  -37.297 65.504  1.00 27.51  ? 41  GLY G CA  1 
ATOM   7091  C  C   . GLY D  1 42  ? -77.291  -37.417 64.326  1.00 26.74  ? 41  GLY G C   1 
ATOM   7092  O  O   . GLY D  1 42  ? -76.771  -38.499 64.042  1.00 23.96  ? 41  GLY G O   1 
ATOM   7093  N  N   . LEU D  1 43  ? -77.023  -36.284 63.671  1.00 23.90  ? 42  LEU G N   1 
ATOM   7094  C  CA  . LEU D  1 43  ? -76.338  -36.232 62.387  1.00 26.50  ? 42  LEU G CA  1 
ATOM   7095  C  C   . LEU D  1 43  ? -74.821  -36.130 62.584  1.00 25.11  ? 42  LEU G C   1 
ATOM   7096  O  O   . LEU D  1 43  ? -74.350  -35.420 63.434  1.00 24.21  ? 42  LEU G O   1 
ATOM   7097  C  CB  . LEU D  1 43  ? -76.831  -35.032 61.577  1.00 27.19  ? 42  LEU G CB  1 
ATOM   7098  C  CG  . LEU D  1 43  ? -78.258  -35.112 61.045  1.00 31.47  ? 42  LEU G CG  1 
ATOM   7099  C  CD1 . LEU D  1 43  ? -78.730  -33.729 60.622  1.00 36.63  ? 42  LEU G CD1 1 
ATOM   7100  C  CD2 . LEU D  1 43  ? -78.357  -36.055 59.864  1.00 33.26  ? 42  LEU G CD2 1 
ATOM   7101  N  N   . HIS D  1 44  ? -74.082  -36.838 61.727  1.00 22.20  ? 43  HIS G N   1 
ATOM   7102  C  CA  . HIS D  1 44  ? -72.613  -36.863 61.702  1.00 21.85  ? 43  HIS G CA  1 
ATOM   7103  C  C   . HIS D  1 44  ? -72.147  -36.813 60.247  1.00 19.77  ? 43  HIS G C   1 
ATOM   7104  O  O   . HIS D  1 44  ? -72.592  -37.617 59.434  1.00 19.17  ? 43  HIS G O   1 
ATOM   7105  C  CB  . HIS D  1 44  ? -72.089  -38.126 62.398  1.00 21.88  ? 43  HIS G CB  1 
ATOM   7106  C  CG  . HIS D  1 44  ? -72.446  -38.200 63.836  1.00 23.85  ? 43  HIS G CG  1 
ATOM   7107  N  ND1 . HIS D  1 44  ? -71.647  -37.648 64.824  1.00 25.91  ? 43  HIS G ND1 1 
ATOM   7108  C  CD2 . HIS D  1 44  ? -73.521  -38.727 64.460  1.00 26.27  ? 43  HIS G CD2 1 
ATOM   7109  C  CE1 . HIS D  1 44  ? -72.202  -37.876 66.002  1.00 27.38  ? 43  HIS G CE1 1 
ATOM   7110  N  NE2 . HIS D  1 44  ? -73.354  -38.530 65.804  1.00 25.92  ? 43  HIS G NE2 1 
ATOM   7111  N  N   . GLY D  1 45  ? -71.245  -35.876 59.965  1.00 18.52  ? 44  GLY G N   1 
ATOM   7112  C  CA  . GLY D  1 45  ? -70.597  -35.749 58.699  1.00 20.47  ? 44  GLY G CA  1 
ATOM   7113  C  C   . GLY D  1 45  ? -69.868  -37.035 58.332  1.00 19.29  ? 44  GLY G C   1 
ATOM   7114  O  O   . GLY D  1 45  ? -69.339  -37.735 59.210  1.00 18.44  ? 44  GLY G O   1 
ATOM   7115  N  N   . PHE D  1 46  ? -69.854  -37.333 57.034  1.00 18.50  ? 45  PHE G N   1 
ATOM   7116  C  CA  . PHE D  1 46  ? -69.426  -38.618 56.526  1.00 18.86  ? 45  PHE G CA  1 
ATOM   7117  C  C   . PHE D  1 46  ? -68.804  -38.390 55.160  1.00 19.63  ? 45  PHE G C   1 
ATOM   7118  O  O   . PHE D  1 46  ? -69.508  -38.104 54.208  1.00 20.31  ? 45  PHE G O   1 
ATOM   7119  C  CB  . PHE D  1 46  ? -70.631  -39.549 56.504  1.00 19.68  ? 45  PHE G CB  1 
ATOM   7120  C  CG  . PHE D  1 46  ? -70.388  -40.989 56.156  1.00 19.12  ? 45  PHE G CG  1 
ATOM   7121  C  CD1 . PHE D  1 46  ? -69.722  -41.831 57.025  1.00 19.92  ? 45  PHE G CD1 1 
ATOM   7122  C  CD2 . PHE D  1 46  ? -70.871  -41.506 54.966  1.00 21.44  ? 45  PHE G CD2 1 
ATOM   7123  C  CE1 . PHE D  1 46  ? -69.573  -43.180 56.727  1.00 20.96  ? 45  PHE G CE1 1 
ATOM   7124  C  CE2 . PHE D  1 46  ? -70.708  -42.846 54.662  1.00 20.73  ? 45  PHE G CE2 1 
ATOM   7125  C  CZ  . PHE D  1 46  ? -70.048  -43.672 55.536  1.00 21.13  ? 45  PHE G CZ  1 
ATOM   7126  N  N   . HIS D  1 47  ? -67.471  -38.489 55.091  1.00 19.24  ? 46  HIS G N   1 
ATOM   7127  C  CA  . HIS D  1 47  ? -66.721  -38.078 53.908  1.00 19.34  ? 46  HIS G CA  1 
ATOM   7128  C  C   . HIS D  1 47  ? -65.549  -39.013 53.600  1.00 19.45  ? 46  HIS G C   1 
ATOM   7129  O  O   . HIS D  1 47  ? -64.956  -39.627 54.505  1.00 18.96  ? 46  HIS G O   1 
ATOM   7130  C  CB  . HIS D  1 47  ? -66.119  -36.689 54.088  1.00 21.67  ? 46  HIS G CB  1 
ATOM   7131  C  CG  . HIS D  1 47  ? -66.987  -35.709 54.780  1.00 22.18  ? 46  HIS G CG  1 
ATOM   7132  N  ND1 . HIS D  1 47  ? -66.593  -35.113 55.954  1.00 24.78  ? 46  HIS G ND1 1 
ATOM   7133  C  CD2 . HIS D  1 47  ? -68.207  -35.208 54.458  1.00 23.40  ? 46  HIS G CD2 1 
ATOM   7134  C  CE1 . HIS D  1 47  ? -67.541  -34.275 56.341  1.00 25.23  ? 46  HIS G CE1 1 
ATOM   7135  N  NE2 . HIS D  1 47  ? -68.560  -34.327 55.441  1.00 24.53  ? 46  HIS G NE2 1 
ATOM   7136  N  N   . VAL D  1 48  ? -65.182  -39.030 52.321  1.00 18.67  ? 47  VAL G N   1 
ATOM   7137  C  CA  . VAL D  1 48  ? -63.945  -39.585 51.879  1.00 20.40  ? 47  VAL G CA  1 
ATOM   7138  C  C   . VAL D  1 48  ? -62.906  -38.465 51.820  1.00 21.51  ? 47  VAL G C   1 
ATOM   7139  O  O   . VAL D  1 48  ? -63.065  -37.483 51.111  1.00 23.40  ? 47  VAL G O   1 
ATOM   7140  C  CB  . VAL D  1 48  ? -64.074  -40.323 50.537  1.00 20.68  ? 47  VAL G CB  1 
ATOM   7141  C  CG1 . VAL D  1 48  ? -62.740  -40.940 50.117  1.00 21.63  ? 47  VAL G CG1 1 
ATOM   7142  C  CG2 . VAL D  1 48  ? -65.140  -41.392 50.603  1.00 21.03  ? 47  VAL G CG2 1 
ATOM   7143  N  N   . HIS D  1 49  ? -61.835  -38.652 52.589  1.00 19.57  ? 48  HIS G N   1 
ATOM   7144  C  CA  . HIS D  1 49  ? -60.701  -37.763 52.655  1.00 20.59  ? 48  HIS G CA  1 
ATOM   7145  C  C   . HIS D  1 49  ? -59.619  -38.290 51.712  1.00 21.79  ? 48  HIS G C   1 
ATOM   7146  O  O   . HIS D  1 49  ? -59.647  -39.454 51.326  1.00 22.32  ? 48  HIS G O   1 
ATOM   7147  C  CB  . HIS D  1 49  ? -60.247  -37.633 54.111  1.00 21.39  ? 48  HIS G CB  1 
ATOM   7148  C  CG  . HIS D  1 49  ? -61.168  -36.814 54.956  1.00 21.48  ? 48  HIS G CG  1 
ATOM   7149  N  ND1 . HIS D  1 49  ? -60.733  -35.668 55.590  1.00 21.29  ? 48  HIS G ND1 1 
ATOM   7150  C  CD2 . HIS D  1 49  ? -62.473  -36.947 55.280  1.00 21.94  ? 48  HIS G CD2 1 
ATOM   7151  C  CE1 . HIS D  1 49  ? -61.729  -35.136 56.270  1.00 22.27  ? 48  HIS G CE1 1 
ATOM   7152  N  NE2 . HIS D  1 49  ? -62.807  -35.875 56.085  1.00 22.72  ? 48  HIS G NE2 1 
ATOM   7153  N  N   . GLU D  1 50  ? -58.680  -37.422 51.346  1.00 20.78  ? 49  GLU G N   1 
ATOM   7154  C  CA  . GLU D  1 50  ? -57.848  -37.634 50.188  1.00 23.90  ? 49  GLU G CA  1 
ATOM   7155  C  C   . GLU D  1 50  ? -56.844  -38.791 50.382  1.00 23.01  ? 49  GLU G C   1 
ATOM   7156  O  O   . GLU D  1 50  ? -56.601  -39.558 49.453  1.00 23.65  ? 49  GLU G O   1 
ATOM   7157  C  CB  . GLU D  1 50  ? -57.080  -36.357 49.876  1.00 26.37  ? 49  GLU G CB  1 
ATOM   7158  C  CG  . GLU D  1 50  ? -56.329  -36.461 48.578  1.00 29.07  ? 49  GLU G CG  1 
ATOM   7159  C  CD  . GLU D  1 50  ? -55.609  -35.194 48.168  1.00 32.24  ? 49  GLU G CD  1 
ATOM   7160  O  OE1 . GLU D  1 50  ? -54.954  -35.244 47.133  1.00 39.91  ? 49  GLU G OE1 1 
ATOM   7161  O  OE2 . GLU D  1 50  ? -55.716  -34.178 48.885  1.00 33.87  ? 49  GLU G OE2 1 
ATOM   7162  N  N   . PHE D  1 51  ? -56.252  -38.895 51.570  1.00 23.01  ? 50  PHE G N   1 
ATOM   7163  C  CA  . PHE D  1 51  ? -55.146  -39.834 51.788  1.00 23.24  ? 50  PHE G CA  1 
ATOM   7164  C  C   . PHE D  1 51  ? -55.590  -40.973 52.691  1.00 24.18  ? 50  PHE G C   1 
ATOM   7165  O  O   . PHE D  1 51  ? -56.243  -40.757 53.714  1.00 23.68  ? 50  PHE G O   1 
ATOM   7166  C  CB  . PHE D  1 51  ? -53.945  -39.115 52.406  1.00 23.70  ? 50  PHE G CB  1 
ATOM   7167  C  CG  . PHE D  1 51  ? -53.512  -37.906 51.632  1.00 25.83  ? 50  PHE G CG  1 
ATOM   7168  C  CD1 . PHE D  1 51  ? -53.145  -38.015 50.302  1.00 29.45  ? 50  PHE G CD1 1 
ATOM   7169  C  CD2 . PHE D  1 51  ? -53.506  -36.655 52.221  1.00 31.77  ? 50  PHE G CD2 1 
ATOM   7170  C  CE1 . PHE D  1 51  ? -52.782  -36.893 49.575  1.00 31.56  ? 50  PHE G CE1 1 
ATOM   7171  C  CE2 . PHE D  1 51  ? -53.125  -35.536 51.494  1.00 32.53  ? 50  PHE G CE2 1 
ATOM   7172  C  CZ  . PHE D  1 51  ? -52.762  -35.657 50.178  1.00 30.05  ? 50  PHE G CZ  1 
ATOM   7173  N  N   . GLY D  1 52  ? -55.147  -42.183 52.339  1.00 24.70  ? 51  GLY G N   1 
ATOM   7174  C  CA  . GLY D  1 52  ? -55.305  -43.351 53.161  1.00 25.25  ? 51  GLY G CA  1 
ATOM   7175  C  C   . GLY D  1 52  ? -54.152  -43.493 54.140  1.00 27.79  ? 51  GLY G C   1 
ATOM   7176  O  O   . GLY D  1 52  ? -53.498  -44.555 54.224  1.00 24.38  ? 51  GLY G O   1 
ATOM   7177  N  N   . ASP D  1 53  ? -53.913  -42.408 54.882  1.00 26.11  ? 52  ASP G N   1 
ATOM   7178  C  CA  . ASP D  1 53  ? -52.753  -42.241 55.730  1.00 26.51  ? 52  ASP G CA  1 
ATOM   7179  C  C   . ASP D  1 53  ? -53.298  -42.026 57.133  1.00 27.00  ? 52  ASP G C   1 
ATOM   7180  O  O   . ASP D  1 53  ? -53.917  -40.983 57.393  1.00 27.45  ? 52  ASP G O   1 
ATOM   7181  C  CB  . ASP D  1 53  ? -51.884  -41.072 55.256  1.00 25.83  ? 52  ASP G CB  1 
ATOM   7182  C  CG  . ASP D  1 53  ? -50.648  -40.791 56.097  1.00 26.86  ? 52  ASP G CG  1 
ATOM   7183  O  OD1 . ASP D  1 53  ? -49.740  -40.176 55.555  1.00 28.38  ? 52  ASP G OD1 1 
ATOM   7184  O  OD2 . ASP D  1 53  ? -50.596  -41.204 57.275  1.00 28.44  ? 52  ASP G OD2 1 
ATOM   7185  N  N   . ASN D  1 54  ? -53.139  -43.042 57.982  1.00 25.56  ? 53  ASN G N   1 
ATOM   7186  C  CA  . ASN D  1 54  ? -53.624  -43.004 59.345  1.00 27.77  ? 53  ASN G CA  1 
ATOM   7187  C  C   . ASN D  1 54  ? -52.392  -42.995 60.288  1.00 28.26  ? 53  ASN G C   1 
ATOM   7188  O  O   . ASN D  1 54  ? -52.517  -43.287 61.463  1.00 26.31  ? 53  ASN G O   1 
ATOM   7189  C  CB  . ASN D  1 54  ? -54.748  -44.053 59.596  1.00 31.58  ? 53  ASN G CB  1 
ATOM   7190  C  CG  A ASN D  1 54  ? -55.851  -43.646 58.616  0.60 31.18  ? 53  ASN G CG  1 
ATOM   7191  C  CG  B ASN D  1 54  ? -54.139  -44.830 60.742  0.40 33.57  ? 53  ASN G CG  1 
ATOM   7192  O  OD1 A ASN D  1 54  ? -55.921  -42.552 58.048  0.60 30.14  ? 53  ASN G OD1 1 
ATOM   7193  O  OD1 B ASN D  1 54  ? -53.209  -45.607 60.559  0.40 40.49  ? 53  ASN G OD1 1 
ATOM   7194  N  ND2 A ASN D  1 54  ? -56.835  -44.519 58.509  0.60 29.23  ? 53  ASN G ND2 1 
ATOM   7195  N  ND2 B ASN D  1 54  ? -54.757  -44.730 61.907  0.40 32.93  ? 53  ASN G ND2 1 
ATOM   7196  N  N   . THR D  1 55  ? -51.232  -42.503 59.817  1.00 27.80  ? 54  THR G N   1 
ATOM   7197  C  CA  . THR D  1 55  ? -49.982  -42.529 60.643  1.00 31.10  ? 54  THR G CA  1 
ATOM   7198  C  C   . THR D  1 55  ? -50.101  -41.650 61.897  1.00 34.73  ? 54  THR G C   1 
ATOM   7199  O  O   . THR D  1 55  ? -49.553  -41.988 62.910  1.00 33.99  ? 54  THR G O   1 
ATOM   7200  C  CB  . THR D  1 55  ? -48.730  -42.100 59.871  1.00 28.38  ? 54  THR G CB  1 
ATOM   7201  O  OG1 . THR D  1 55  ? -48.940  -40.795 59.341  1.00 29.61  ? 54  THR G OG1 1 
ATOM   7202  C  CG2 . THR D  1 55  ? -48.375  -43.060 58.754  1.00 28.10  ? 54  THR G CG2 1 
ATOM   7203  N  N   . ALA D  1 56  ? -50.815  -40.523 61.826  1.00 30.58  ? 55  ALA G N   1 
ATOM   7204  C  CA  . ALA D  1 56  ? -51.051  -39.734 63.002  1.00 33.61  ? 55  ALA G CA  1 
ATOM   7205  C  C   . ALA D  1 56  ? -52.547  -39.746 63.321  1.00 35.29  ? 55  ALA G C   1 
ATOM   7206  O  O   . ALA D  1 56  ? -53.099  -38.723 63.624  1.00 39.95  ? 55  ALA G O   1 
ATOM   7207  C  CB  . ALA D  1 56  ? -50.529  -38.328 62.796  1.00 36.27  ? 55  ALA G CB  1 
ATOM   7208  N  N   . GLY D  1 57  ? -53.185  -40.922 63.228  1.00 31.23  ? 56  GLY G N   1 
ATOM   7209  C  CA  . GLY D  1 57  ? -54.621  -41.036 63.356  1.00 30.20  ? 56  GLY G CA  1 
ATOM   7210  C  C   . GLY D  1 57  ? -55.358  -40.402 62.178  1.00 30.59  ? 56  GLY G C   1 
ATOM   7211  O  O   . GLY D  1 57  ? -54.795  -40.213 61.081  1.00 29.31  ? 56  GLY G O   1 
ATOM   7212  N  N   . CYS D  1 58  ? -56.613  -40.017 62.428  1.00 29.01  ? 57  CYS G N   1 
ATOM   7213  C  CA  . CYS D  1 58  ? -57.533  -39.493 61.392  1.00 28.71  ? 57  CYS G CA  1 
ATOM   7214  C  C   . CYS D  1 58  ? -57.044  -38.165 60.789  1.00 28.54  ? 57  CYS G C   1 
ATOM   7215  O  O   . CYS D  1 58  ? -57.330  -37.881 59.618  1.00 26.55  ? 57  CYS G O   1 
ATOM   7216  C  CB  . CYS D  1 58  ? -58.944  -39.387 61.957  1.00 29.09  ? 57  CYS G CB  1 
ATOM   7217  S  SG  . CYS D  1 58  ? -59.634  -41.000 62.422  1.00 33.05  ? 57  CYS G SG  1 
ATOM   7218  N  N   . THR D  1 59  ? -56.249  -37.392 61.534  1.00 27.06  ? 58  THR G N   1 
ATOM   7219  C  CA  . THR D  1 59  ? -55.681  -36.126 61.045  1.00 29.23  ? 58  THR G CA  1 
ATOM   7220  C  C   . THR D  1 59  ? -54.852  -36.292 59.769  1.00 30.50  ? 58  THR G C   1 
ATOM   7221  O  O   . THR D  1 59  ? -54.859  -35.397 58.894  1.00 27.44  ? 58  THR G O   1 
ATOM   7222  C  CB  . THR D  1 59  ? -54.717  -35.480 62.048  1.00 35.01  ? 58  THR G CB  1 
ATOM   7223  O  OG1 . THR D  1 59  ? -55.361  -35.472 63.310  1.00 42.65  ? 58  THR G OG1 1 
ATOM   7224  C  CG2 . THR D  1 59  ? -54.313  -34.072 61.668  1.00 36.27  ? 58  THR G CG2 1 
ATOM   7225  N  N   . SER D  1 60  ? -54.110  -37.398 59.637  1.00 25.93  ? 59  SER G N   1 
ATOM   7226  C  CA  . SER D  1 60  ? -53.221  -37.503 58.474  1.00 27.20  ? 59  SER G CA  1 
ATOM   7227  C  C   . SER D  1 60  ? -53.973  -37.853 57.182  1.00 25.21  ? 59  SER G C   1 
ATOM   7228  O  O   . SER D  1 60  ? -53.353  -37.900 56.085  1.00 24.60  ? 59  SER G O   1 
ATOM   7229  C  CB  . SER D  1 60  ? -52.078  -38.460 58.711  1.00 29.71  ? 59  SER G CB  1 
ATOM   7230  O  OG  . SER D  1 60  ? -52.364  -39.360 59.738  1.00 33.42  ? 59  SER G OG  1 
ATOM   7231  N  N   . ALA D  1 61  ? -55.283  -38.094 57.271  1.00 23.44  ? 60  ALA G N   1 
ATOM   7232  C  CA  . ALA D  1 61  ? -56.075  -38.379 56.065  1.00 24.43  ? 60  ALA G CA  1 
ATOM   7233  C  C   . ALA D  1 61  ? -56.203  -37.150 55.147  1.00 24.30  ? 60  ALA G C   1 
ATOM   7234  O  O   . ALA D  1 61  ? -56.640  -37.277 54.011  1.00 24.64  ? 60  ALA G O   1 
ATOM   7235  C  CB  . ALA D  1 61  ? -57.420  -38.901 56.448  1.00 25.56  ? 60  ALA G CB  1 
ATOM   7236  N  N   . GLY D  1 62  ? -55.808  -35.977 55.640  1.00 23.77  ? 61  GLY G N   1 
ATOM   7237  C  CA  . GLY D  1 62  ? -55.853  -34.737 54.894  1.00 25.40  ? 61  GLY G CA  1 
ATOM   7238  C  C   . GLY D  1 62  ? -57.284  -34.228 54.685  1.00 24.57  ? 61  GLY G C   1 
ATOM   7239  O  O   . GLY D  1 62  ? -58.208  -34.625 55.389  1.00 27.21  ? 61  GLY G O   1 
ATOM   7240  N  N   . PRO D  1 63  ? -57.509  -33.337 53.699  1.00 25.79  ? 62  PRO G N   1 
ATOM   7241  C  CA  . PRO D  1 63  ? -58.833  -32.746 53.472  1.00 25.03  ? 62  PRO G CA  1 
ATOM   7242  C  C   . PRO D  1 63  ? -59.709  -33.728 52.689  1.00 24.16  ? 62  PRO G C   1 
ATOM   7243  O  O   . PRO D  1 63  ? -59.271  -34.850 52.345  1.00 22.32  ? 62  PRO G O   1 
ATOM   7244  C  CB  . PRO D  1 63  ? -58.483  -31.490 52.651  1.00 25.96  ? 62  PRO G CB  1 
ATOM   7245  C  CG  . PRO D  1 63  ? -57.312  -31.962 51.805  1.00 26.44  ? 62  PRO G CG  1 
ATOM   7246  C  CD  . PRO D  1 63  ? -56.508  -32.836 52.750  1.00 24.82  ? 62  PRO G CD  1 
ATOM   7247  N  N   . HIS D  1 64  ? -60.907  -33.278 52.346  1.00 21.82  ? 63  HIS G N   1 
ATOM   7248  C  CA  . HIS D  1 64  ? -61.829  -34.075 51.566  1.00 21.96  ? 63  HIS G CA  1 
ATOM   7249  C  C   . HIS D  1 64  ? -61.201  -34.385 50.211  1.00 21.76  ? 63  HIS G C   1 
ATOM   7250  O  O   . HIS D  1 64  ? -60.481  -33.574 49.655  1.00 21.85  ? 63  HIS G O   1 
ATOM   7251  C  CB  . HIS D  1 64  ? -63.183  -33.367 51.427  1.00 22.29  ? 63  HIS G CB  1 
ATOM   7252  C  CG  . HIS D  1 64  ? -63.888  -33.223 52.729  1.00 24.50  ? 63  HIS G CG  1 
ATOM   7253  N  ND1 . HIS D  1 64  ? -65.091  -32.593 52.859  1.00 24.96  ? 63  HIS G ND1 1 
ATOM   7254  C  CD2 . HIS D  1 64  ? -63.530  -33.622 53.970  1.00 26.32  ? 63  HIS G CD2 1 
ATOM   7255  C  CE1 . HIS D  1 64  ? -65.453  -32.594 54.122  1.00 26.49  ? 63  HIS G CE1 1 
ATOM   7256  N  NE2 . HIS D  1 64  ? -64.531  -33.277 54.832  1.00 27.49  ? 63  HIS G NE2 1 
ATOM   7257  N  N   . PHE D  1 65  ? -61.477  -35.583 49.701  1.00 21.24  ? 64  PHE G N   1 
ATOM   7258  C  CA  . PHE D  1 65  ? -61.048  -35.968 48.372  1.00 21.72  ? 64  PHE G CA  1 
ATOM   7259  C  C   . PHE D  1 65  ? -61.777  -35.072 47.352  1.00 22.02  ? 64  PHE G C   1 
ATOM   7260  O  O   . PHE D  1 65  ? -62.979  -35.129 47.277  1.00 22.00  ? 64  PHE G O   1 
ATOM   7261  C  CB  . PHE D  1 65  ? -61.329  -37.461 48.164  1.00 20.55  ? 64  PHE G CB  1 
ATOM   7262  C  CG  . PHE D  1 65  ? -60.985  -37.987 46.792  1.00 21.68  ? 64  PHE G CG  1 
ATOM   7263  C  CD1 . PHE D  1 65  ? -61.843  -38.854 46.137  1.00 23.09  ? 64  PHE G CD1 1 
ATOM   7264  C  CD2 . PHE D  1 65  ? -59.789  -37.648 46.171  1.00 24.22  ? 64  PHE G CD2 1 
ATOM   7265  C  CE1 . PHE D  1 65  ? -61.518  -39.360 44.887  1.00 24.33  ? 64  PHE G CE1 1 
ATOM   7266  C  CE2 . PHE D  1 65  ? -59.477  -38.138 44.910  1.00 23.53  ? 64  PHE G CE2 1 
ATOM   7267  C  CZ  . PHE D  1 65  ? -60.344  -38.994 44.274  1.00 23.90  ? 64  PHE G CZ  1 
ATOM   7268  N  N   . ASN D  1 66  ? -61.015  -34.294 46.575  1.00 21.64  ? 65  ASN G N   1 
ATOM   7269  C  CA  . ASN D  1 66  ? -61.518  -33.148 45.817  1.00 24.91  ? 65  ASN G CA  1 
ATOM   7270  C  C   . ASN D  1 66  ? -60.720  -32.978 44.529  1.00 26.79  ? 65  ASN G C   1 
ATOM   7271  O  O   . ASN D  1 66  ? -60.150  -31.919 44.290  1.00 27.23  ? 65  ASN G O   1 
ATOM   7272  C  CB  . ASN D  1 66  ? -61.457  -31.862 46.652  1.00 22.85  ? 65  ASN G CB  1 
ATOM   7273  C  CG  . ASN D  1 66  ? -62.117  -30.653 46.019  1.00 24.52  ? 65  ASN G CG  1 
ATOM   7274  O  OD1 . ASN D  1 66  ? -62.950  -30.776 45.127  1.00 25.23  ? 65  ASN G OD1 1 
ATOM   7275  N  ND2 . ASN D  1 66  ? -61.766  -29.472 46.506  1.00 23.72  ? 65  ASN G ND2 1 
ATOM   7276  N  N   . PRO D  1 67  ? -60.679  -33.983 43.629  1.00 27.29  ? 66  PRO G N   1 
ATOM   7277  C  CA  . PRO D  1 67  ? -59.866  -33.866 42.421  1.00 29.55  ? 66  PRO G CA  1 
ATOM   7278  C  C   . PRO D  1 67  ? -60.379  -32.781 41.460  1.00 32.42  ? 66  PRO G C   1 
ATOM   7279  O  O   . PRO D  1 67  ? -59.611  -32.297 40.675  1.00 32.79  ? 66  PRO G O   1 
ATOM   7280  C  CB  . PRO D  1 67  ? -59.981  -35.240 41.744  1.00 28.61  ? 66  PRO G CB  1 
ATOM   7281  C  CG  . PRO D  1 67  ? -61.258  -35.835 42.297  1.00 27.89  ? 66  PRO G CG  1 
ATOM   7282  C  CD  . PRO D  1 67  ? -61.430  -35.242 43.685  1.00 27.45  ? 66  PRO G CD  1 
ATOM   7283  N  N   . LEU D  1 68  ? -61.659  -32.395 41.540  1.00 32.78  ? 67  LEU G N   1 
ATOM   7284  C  CA  . LEU D  1 68  ? -62.175  -31.344 40.665  1.00 31.83  ? 67  LEU G CA  1 
ATOM   7285  C  C   . LEU D  1 68  ? -61.993  -29.945 41.258  1.00 32.51  ? 67  LEU G C   1 
ATOM   7286  O  O   . LEU D  1 68  ? -62.370  -28.994 40.608  1.00 31.99  ? 67  LEU G O   1 
ATOM   7287  C  CB  . LEU D  1 68  ? -63.640  -31.625 40.350  1.00 34.61  ? 67  LEU G CB  1 
ATOM   7288  C  CG  . LEU D  1 68  ? -63.889  -32.919 39.586  1.00 36.57  ? 67  LEU G CG  1 
ATOM   7289  C  CD1 . LEU D  1 68  ? -65.369  -33.155 39.364  1.00 40.96  ? 67  LEU G CD1 1 
ATOM   7290  C  CD2 . LEU D  1 68  ? -63.170  -32.913 38.260  1.00 43.04  ? 67  LEU G CD2 1 
ATOM   7291  N  N   . SER D  1 69  ? -61.380  -29.817 42.446  1.00 31.64  ? 68  SER G N   1 
ATOM   7292  C  CA  . SER D  1 69  ? -61.131  -28.539 43.099  1.00 34.90  ? 68  SER G CA  1 
ATOM   7293  C  C   . SER D  1 69  ? -62.426  -27.716 43.219  1.00 34.95  ? 68  SER G C   1 
ATOM   7294  O  O   . SER D  1 69  ? -62.466  -26.564 42.827  1.00 32.71  ? 68  SER G O   1 
ATOM   7295  C  CB  . SER D  1 69  ? -60.079  -27.740 42.364  1.00 37.61  ? 68  SER G CB  1 
ATOM   7296  O  OG  . SER D  1 69  ? -58.806  -28.306 42.571  1.00 43.60  ? 68  SER G OG  1 
ATOM   7297  N  N   . ARG D  1 70  ? -63.474  -28.317 43.770  1.00 31.44  ? 69  ARG G N   1 
ATOM   7298  C  CA  . ARG D  1 70  ? -64.709  -27.633 44.006  1.00 30.79  ? 69  ARG G CA  1 
ATOM   7299  C  C   . ARG D  1 70  ? -64.811  -27.275 45.491  1.00 30.21  ? 69  ARG G C   1 
ATOM   7300  O  O   . ARG D  1 70  ? -63.975  -27.660 46.300  1.00 28.59  ? 69  ARG G O   1 
ATOM   7301  C  CB  . ARG D  1 70  ? -65.842  -28.498 43.459  1.00 30.94  ? 69  ARG G CB  1 
ATOM   7302  C  CG  . ARG D  1 70  ? -65.926  -28.421 41.939  1.00 34.53  ? 69  ARG G CG  1 
ATOM   7303  C  CD  . ARG D  1 70  ? -66.877  -29.420 41.339  1.00 39.72  ? 69  ARG G CD  1 
ATOM   7304  N  NE  . ARG D  1 70  ? -66.692  -29.491 39.896  1.00 41.66  ? 69  ARG G NE  1 
ATOM   7305  C  CZ  . ARG D  1 70  ? -67.612  -29.898 39.036  1.00 43.72  ? 69  ARG G CZ  1 
ATOM   7306  N  NH1 . ARG D  1 70  ? -67.320  -29.920 37.748  1.00 44.05  ? 69  ARG G NH1 1 
ATOM   7307  N  NH2 . ARG D  1 70  ? -68.798  -30.308 39.465  1.00 43.15  ? 69  ARG G NH2 1 
ATOM   7308  N  N   . LYS D  1 71  ? -65.815  -26.467 45.813  1.00 28.34  ? 70  LYS G N   1 
ATOM   7309  C  CA  . LYS D  1 71  ? -66.210  -26.212 47.197  1.00 30.16  ? 70  LYS G CA  1 
ATOM   7310  C  C   . LYS D  1 71  ? -67.030  -27.401 47.722  1.00 25.48  ? 70  LYS G C   1 
ATOM   7311  O  O   . LYS D  1 71  ? -67.672  -28.136 46.968  1.00 23.82  ? 70  LYS G O   1 
ATOM   7312  C  CB  . LYS D  1 71  ? -66.985  -24.892 47.284  1.00 33.50  ? 70  LYS G CB  1 
ATOM   7313  C  CG  . LYS D  1 71  ? -66.144  -23.646 47.021  1.00 39.27  ? 70  LYS G CG  1 
ATOM   7314  C  CD  . LYS D  1 71  ? -66.942  -22.353 47.015  1.00 48.35  ? 70  LYS G CD  1 
ATOM   7315  C  CE  . LYS D  1 71  ? -67.749  -22.164 45.745  1.00 60.31  ? 70  LYS G CE  1 
ATOM   7316  N  NZ  . LYS D  1 71  ? -68.194  -20.757 45.580  1.00 68.52  ? 70  LYS G NZ  1 
ATOM   7317  N  N   . HIS D  1 72  ? -67.032  -27.548 49.044  1.00 23.85  ? 71  HIS G N   1 
ATOM   7318  C  CA  . HIS D  1 72  ? -67.784  -28.570 49.722  1.00 23.40  ? 71  HIS G CA  1 
ATOM   7319  C  C   . HIS D  1 72  ? -69.285  -28.357 49.481  1.00 24.08  ? 71  HIS G C   1 
ATOM   7320  O  O   . HIS D  1 72  ? -69.777  -27.239 49.442  1.00 24.86  ? 71  HIS G O   1 
ATOM   7321  C  CB  . HIS D  1 72  ? -67.431  -28.524 51.213  1.00 22.85  ? 71  HIS G CB  1 
ATOM   7322  C  CG  . HIS D  1 72  ? -68.199  -29.492 52.049  1.00 23.65  ? 71  HIS G CG  1 
ATOM   7323  N  ND1 . HIS D  1 72  ? -67.926  -30.849 52.078  1.00 24.82  ? 71  HIS G ND1 1 
ATOM   7324  C  CD2 . HIS D  1 72  ? -69.221  -29.303 52.911  1.00 23.50  ? 71  HIS G CD2 1 
ATOM   7325  C  CE1 . HIS D  1 72  ? -68.767  -31.441 52.902  1.00 25.86  ? 71  HIS G CE1 1 
ATOM   7326  N  NE2 . HIS D  1 72  ? -69.552  -30.530 53.430  1.00 24.14  ? 71  HIS G NE2 1 
ATOM   7327  N  N   . GLY D  1 73  ? -70.009  -29.454 49.350  1.00 21.15  ? 72  GLY G N   1 
ATOM   7328  C  CA  . GLY D  1 73  ? -71.416  -29.456 49.258  1.00 22.10  ? 72  GLY G CA  1 
ATOM   7329  C  C   . GLY D  1 73  ? -71.980  -30.748 49.785  1.00 22.97  ? 72  GLY G C   1 
ATOM   7330  O  O   . GLY D  1 73  ? -71.285  -31.569 50.394  1.00 24.43  ? 72  GLY G O   1 
ATOM   7331  N  N   . GLY D  1 74  ? -73.275  -30.911 49.580  1.00 23.12  ? 73  GLY G N   1 
ATOM   7332  C  CA  . GLY D  1 74  ? -73.911  -32.130 49.907  1.00 23.47  ? 73  GLY G CA  1 
ATOM   7333  C  C   . GLY D  1 74  ? -73.829  -33.050 48.699  1.00 24.15  ? 73  GLY G C   1 
ATOM   7334  O  O   . GLY D  1 74  ? -73.550  -32.572 47.598  1.00 23.85  ? 73  GLY G O   1 
ATOM   7335  N  N   . PRO D  1 75  ? -74.079  -34.361 48.876  1.00 24.83  ? 74  PRO G N   1 
ATOM   7336  C  CA  . PRO D  1 75  ? -73.951  -35.320 47.784  1.00 27.17  ? 74  PRO G CA  1 
ATOM   7337  C  C   . PRO D  1 75  ? -74.833  -34.994 46.567  1.00 29.64  ? 74  PRO G C   1 
ATOM   7338  O  O   . PRO D  1 75  ? -74.456  -35.343 45.443  1.00 26.29  ? 74  PRO G O   1 
ATOM   7339  C  CB  . PRO D  1 75  ? -74.357  -36.667 48.387  1.00 26.78  ? 74  PRO G CB  1 
ATOM   7340  C  CG  . PRO D  1 75  ? -74.969  -36.368 49.745  1.00 27.51  ? 74  PRO G CG  1 
ATOM   7341  C  CD  . PRO D  1 75  ? -74.486  -34.990 50.137  1.00 26.94  ? 74  PRO G CD  1 
ATOM   7342  N  N   . LYS D  1 76  ? -75.969  -34.321 46.796  1.00 30.44  ? 75  LYS G N   1 
ATOM   7343  C  CA  . LYS D  1 76  ? -76.892  -34.014 45.706  1.00 35.04  ? 75  LYS G CA  1 
ATOM   7344  C  C   . LYS D  1 76  ? -76.498  -32.724 44.991  1.00 32.43  ? 75  LYS G C   1 
ATOM   7345  O  O   . LYS D  1 76  ? -77.017  -32.471 43.947  1.00 39.21  ? 75  LYS G O   1 
ATOM   7346  C  CB  . LYS D  1 76  ? -78.331  -33.982 46.216  1.00 40.46  ? 75  LYS G CB  1 
ATOM   7347  C  CG  . LYS D  1 76  ? -78.942  -35.365 46.400  1.00 49.65  ? 75  LYS G CG  1 
ATOM   7348  C  CD  . LYS D  1 76  ? -79.990  -35.430 47.495  1.00 65.25  ? 75  LYS G CD  1 
ATOM   7349  C  CE  . LYS D  1 76  ? -81.422  -35.235 47.024  1.00 75.75  ? 75  LYS G CE  1 
ATOM   7350  N  NZ  . LYS D  1 76  ? -82.403  -35.768 48.011  1.00 79.15  ? 75  LYS G NZ  1 
ATOM   7351  N  N   . ASP D  1 77  ? -75.525  -31.965 45.499  1.00 32.32  ? 76  ASP G N   1 
ATOM   7352  C  CA  . ASP D  1 77  ? -75.075  -30.742 44.844  1.00 33.94  ? 76  ASP G CA  1 
ATOM   7353  C  C   . ASP D  1 77  ? -74.124  -31.044 43.679  1.00 35.69  ? 76  ASP G C   1 
ATOM   7354  O  O   . ASP D  1 77  ? -73.384  -32.005 43.702  1.00 35.79  ? 76  ASP G O   1 
ATOM   7355  C  CB  . ASP D  1 77  ? -74.430  -29.789 45.856  1.00 37.34  ? 76  ASP G CB  1 
ATOM   7356  C  CG  . ASP D  1 77  ? -75.391  -29.370 46.948  1.00 41.25  ? 76  ASP G CG  1 
ATOM   7357  O  OD1 . ASP D  1 77  ? -74.945  -29.116 48.091  1.00 46.00  ? 76  ASP G OD1 1 
ATOM   7358  O  OD2 . ASP D  1 77  ? -76.593  -29.351 46.662  1.00 42.67  ? 76  ASP G OD2 1 
ATOM   7359  N  N   . GLU D  1 78  ? -74.123  -30.163 42.668  1.00 36.37  ? 77  GLU G N   1 
ATOM   7360  C  CA  . GLU D  1 78  ? -73.147  -30.193 41.577  1.00 40.45  ? 77  GLU G CA  1 
ATOM   7361  C  C   . GLU D  1 78  ? -71.801  -29.686 42.094  1.00 36.56  ? 77  GLU G C   1 
ATOM   7362  O  O   . GLU D  1 78  ? -70.719  -30.249 41.781  1.00 34.94  ? 77  GLU G O   1 
ATOM   7363  C  CB  . GLU D  1 78  ? -73.619  -29.334 40.401  1.00 49.15  ? 77  GLU G CB  1 
ATOM   7364  C  CG  . GLU D  1 78  ? -72.845  -29.585 39.118  1.00 59.31  ? 77  GLU G CG  1 
ATOM   7365  C  CD  . GLU D  1 78  ? -73.366  -28.850 37.885  1.00 71.82  ? 77  GLU G CD  1 
ATOM   7366  O  OE1 . GLU D  1 78  ? -74.517  -28.331 37.924  1.00 73.58  ? 77  GLU G OE1 1 
ATOM   7367  O  OE2 . GLU D  1 78  ? -72.615  -28.786 36.882  1.00 81.70  ? 77  GLU G OE2 1 
ATOM   7368  N  N   . GLU D  1 79  ? -71.874  -28.618 42.890  1.00 31.75  ? 78  GLU G N   1 
ATOM   7369  C  CA  . GLU D  1 79  ? -70.707  -28.088 43.579  1.00 31.45  ? 78  GLU G CA  1 
ATOM   7370  C  C   . GLU D  1 79  ? -70.534  -28.885 44.883  1.00 29.36  ? 78  GLU G C   1 
ATOM   7371  O  O   . GLU D  1 79  ? -71.203  -28.627 45.887  1.00 27.82  ? 78  GLU G O   1 
ATOM   7372  C  CB  . GLU D  1 79  ? -70.870  -26.591 43.810  1.00 33.16  ? 78  GLU G CB  1 
ATOM   7373  C  CG  . GLU D  1 79  ? -69.605  -25.897 44.293  1.00 36.04  ? 78  GLU G CG  1 
ATOM   7374  C  CD  . GLU D  1 79  ? -68.490  -25.701 43.279  1.00 37.04  ? 78  GLU G CD  1 
ATOM   7375  O  OE1 . GLU D  1 79  ? -67.382  -25.274 43.677  1.00 37.31  ? 78  GLU G OE1 1 
ATOM   7376  O  OE2 . GLU D  1 79  ? -68.713  -25.982 42.102  1.00 43.35  ? 78  GLU G OE2 1 
ATOM   7377  N  N   . ARG D  1 80  ? -69.651  -29.893 44.824  1.00 25.91  ? 79  ARG G N   1 
ATOM   7378  C  CA  . ARG D  1 80  ? -69.298  -30.752 45.954  1.00 24.46  ? 79  ARG G CA  1 
ATOM   7379  C  C   . ARG D  1 80  ? -67.912  -31.330 45.693  1.00 24.57  ? 79  ARG G C   1 
ATOM   7380  O  O   . ARG D  1 80  ? -67.429  -31.334 44.551  1.00 26.08  ? 79  ARG G O   1 
ATOM   7381  C  CB  . ARG D  1 80  ? -70.289  -31.911 46.106  1.00 23.09  ? 79  ARG G CB  1 
ATOM   7382  C  CG  . ARG D  1 80  ? -70.389  -32.812 44.882  1.00 23.75  ? 79  ARG G CG  1 
ATOM   7383  C  CD  . ARG D  1 80  ? -71.252  -34.014 45.157  1.00 24.09  ? 79  ARG G CD  1 
ATOM   7384  N  NE  . ARG D  1 80  ? -70.449  -35.097 45.723  1.00 24.25  ? 79  ARG G NE  1 
ATOM   7385  C  CZ  . ARG D  1 80  ? -70.835  -36.361 45.806  1.00 22.14  ? 79  ARG G CZ  1 
ATOM   7386  N  NH1 . ARG D  1 80  ? -69.973  -37.267 46.248  1.00 22.22  ? 79  ARG G NH1 1 
ATOM   7387  N  NH2 . ARG D  1 80  ? -72.066  -36.723 45.474  1.00 20.80  ? 79  ARG G NH2 1 
ATOM   7388  N  N   . HIS D  1 81  ? -67.281  -31.780 46.767  1.00 23.66  ? 80  HIS G N   1 
ATOM   7389  C  CA  . HIS D  1 81  ? -66.108  -32.641 46.685  1.00 22.34  ? 80  HIS G CA  1 
ATOM   7390  C  C   . HIS D  1 81  ? -66.573  -34.031 46.253  1.00 21.59  ? 80  HIS G C   1 
ATOM   7391  O  O   . HIS D  1 81  ? -67.640  -34.492 46.636  1.00 21.47  ? 80  HIS G O   1 
ATOM   7392  C  CB  . HIS D  1 81  ? -65.363  -32.671 48.030  1.00 22.26  ? 80  HIS G CB  1 
ATOM   7393  C  CG  . HIS D  1 81  ? -64.989  -31.331 48.582  1.00 22.70  ? 80  HIS G CG  1 
ATOM   7394  N  ND1 . HIS D  1 81  ? -65.011  -31.029 49.945  1.00 21.38  ? 80  HIS G ND1 1 
ATOM   7395  C  CD2 . HIS D  1 81  ? -64.569  -30.212 47.952  1.00 22.78  ? 80  HIS G CD2 1 
ATOM   7396  C  CE1 . HIS D  1 81  ? -64.562  -29.798 50.112  1.00 23.25  ? 80  HIS G CE1 1 
ATOM   7397  N  NE2 . HIS D  1 81  ? -64.303  -29.275 48.896  1.00 21.59  ? 80  HIS G NE2 1 
ATOM   7398  N  N   . VAL D  1 82  ? -65.727  -34.749 45.506  1.00 22.08  ? 81  VAL G N   1 
ATOM   7399  C  CA  . VAL D  1 82  ? -65.989  -36.144 45.259  1.00 21.29  ? 81  VAL G CA  1 
ATOM   7400  C  C   . VAL D  1 82  ? -66.289  -36.886 46.571  1.00 19.13  ? 81  VAL G C   1 
ATOM   7401  O  O   . VAL D  1 82  ? -67.192  -37.676 46.641  1.00 20.73  ? 81  VAL G O   1 
ATOM   7402  C  CB  . VAL D  1 82  ? -64.850  -36.809 44.465  1.00 23.02  ? 81  VAL G CB  1 
ATOM   7403  C  CG1 . VAL D  1 82  ? -65.058  -38.322 44.423  1.00 22.84  ? 81  VAL G CG1 1 
ATOM   7404  C  CG2 . VAL D  1 82  ? -64.808  -36.211 43.057  1.00 23.93  ? 81  VAL G CG2 1 
ATOM   7405  N  N   . GLY D  1 83  ? -65.567  -36.568 47.630  1.00 21.89  ? 82  GLY G N   1 
ATOM   7406  C  CA  . GLY D  1 83  ? -65.724  -37.287 48.894  1.00 22.36  ? 82  GLY G CA  1 
ATOM   7407  C  C   . GLY D  1 83  ? -66.894  -36.829 49.763  1.00 23.28  ? 82  GLY G C   1 
ATOM   7408  O  O   . GLY D  1 83  ? -67.051  -37.371 50.866  1.00 23.10  ? 82  GLY G O   1 
ATOM   7409  N  N   A SER D  1 84  ? -67.720  -35.871 49.291  0.55 23.67  ? 83  SER G N   1 
ATOM   7410  C  CA  A SER D  1 84  ? -68.826  -35.279 50.095  0.55 23.95  ? 83  SER G CA  1 
ATOM   7411  C  C   A SER D  1 84  ? -70.050  -36.201 50.128  0.55 23.62  ? 83  SER G C   1 
ATOM   7412  O  O   A SER D  1 84  ? -70.983  -35.971 49.356  0.55 24.81  ? 83  SER G O   1 
ATOM   7413  C  CB  A SER D  1 84  ? -69.254  -33.916 49.568  0.55 23.98  ? 83  SER G CB  1 
ATOM   7414  O  OG  A SER D  1 84  ? -68.224  -32.937 49.586  0.55 25.44  ? 83  SER G OG  1 
ATOM   7415  N  N   B ASP D  1 84  ? -67.718  -35.894 49.266  0.45 21.57  ? 83  ASP G N   1 
ATOM   7416  C  CA  B ASP D  1 84  ? -68.825  -35.379 50.053  0.45 21.03  ? 83  ASP G CA  1 
ATOM   7417  C  C   B ASP D  1 84  ? -69.988  -36.365 50.022  0.45 21.77  ? 83  ASP G C   1 
ATOM   7418  O  O   B ASP D  1 84  ? -70.770  -36.406 49.078  0.45 24.77  ? 83  ASP G O   1 
ATOM   7419  C  CB  B ASP D  1 84  ? -69.263  -34.002 49.573  0.45 19.38  ? 83  ASP G CB  1 
ATOM   7420  C  CG  B ASP D  1 84  ? -68.206  -32.975 49.891  0.45 18.95  ? 83  ASP G CG  1 
ATOM   7421  O  OD1 B ASP D  1 84  ? -67.375  -33.290 50.785  0.45 19.30  ? 83  ASP G OD1 1 
ATOM   7422  O  OD2 B ASP D  1 84  ? -68.189  -31.921 49.219  0.45 15.15  ? 83  ASP G OD2 1 
ATOM   7423  N  N   . LEU D  1 85  ? -70.121  -37.129 51.098  1.00 20.84  ? 84  LEU G N   1 
ATOM   7424  C  CA  . LEU D  1 85  ? -71.211  -38.077 51.185  1.00 22.36  ? 84  LEU G CA  1 
ATOM   7425  C  C   . LEU D  1 85  ? -72.250  -37.639 52.214  1.00 21.16  ? 84  LEU G C   1 
ATOM   7426  O  O   . LEU D  1 85  ? -73.070  -38.454 52.573  1.00 24.62  ? 84  LEU G O   1 
ATOM   7427  C  CB  . LEU D  1 85  ? -70.684  -39.475 51.529  1.00 22.07  ? 84  LEU G CB  1 
ATOM   7428  C  CG  . LEU D  1 85  ? -69.740  -40.076 50.492  1.00 24.76  ? 84  LEU G CG  1 
ATOM   7429  C  CD1 . LEU D  1 85  ? -69.317  -41.473 50.911  1.00 25.17  ? 84  LEU G CD1 1 
ATOM   7430  C  CD2 . LEU D  1 85  ? -70.388  -40.109 49.123  1.00 27.16  ? 84  LEU G CD2 1 
ATOM   7431  N  N   . GLY D  1 86  ? -72.202  -36.386 52.677  1.00 20.81  ? 85  GLY G N   1 
ATOM   7432  C  CA  . GLY D  1 86  ? -73.279  -35.831 53.502  1.00 21.00  ? 85  GLY G CA  1 
ATOM   7433  C  C   . GLY D  1 86  ? -73.198  -36.272 54.954  1.00 21.32  ? 85  GLY G C   1 
ATOM   7434  O  O   . GLY D  1 86  ? -72.117  -36.342 55.570  1.00 19.34  ? 85  GLY G O   1 
ATOM   7435  N  N   . ASN D  1 87  ? -74.358  -36.579 55.501  1.00 20.56  ? 86  ASN G N   1 
ATOM   7436  C  CA  . ASN D  1 87  ? -74.512  -36.981 56.875  1.00 21.28  ? 86  ASN G CA  1 
ATOM   7437  C  C   . ASN D  1 87  ? -74.943  -38.450 56.966  1.00 21.16  ? 86  ASN G C   1 
ATOM   7438  O  O   . ASN D  1 87  ? -75.628  -38.975 56.090  1.00 21.16  ? 86  ASN G O   1 
ATOM   7439  C  CB  . ASN D  1 87  ? -75.568  -36.120 57.576  1.00 20.27  ? 86  ASN G CB  1 
ATOM   7440  C  CG  . ASN D  1 87  ? -75.055  -34.728 57.828  1.00 22.48  ? 86  ASN G CG  1 
ATOM   7441  O  OD1 . ASN D  1 87  ? -74.175  -34.541 58.665  1.00 23.61  ? 86  ASN G OD1 1 
ATOM   7442  N  ND2 . ASN D  1 87  ? -75.600  -33.752 57.127  1.00 18.33  ? 86  ASN G ND2 1 
ATOM   7443  N  N   . VAL D  1 88  ? -74.618  -39.046 58.107  1.00 19.52  ? 87  VAL G N   1 
ATOM   7444  C  CA  . VAL D  1 88  ? -75.231  -40.259 58.565  1.00 21.16  ? 87  VAL G CA  1 
ATOM   7445  C  C   . VAL D  1 88  ? -75.875  -39.951 59.919  1.00 21.41  ? 87  VAL G C   1 
ATOM   7446  O  O   . VAL D  1 88  ? -75.431  -39.056 60.631  1.00 23.30  ? 87  VAL G O   1 
ATOM   7447  C  CB  . VAL D  1 88  ? -74.237  -41.441 58.624  1.00 20.16  ? 87  VAL G CB  1 
ATOM   7448  C  CG1 . VAL D  1 88  ? -73.726  -41.773 57.237  1.00 19.57  ? 87  VAL G CG1 1 
ATOM   7449  C  CG2 . VAL D  1 88  ? -73.084  -41.210 59.577  1.00 20.69  ? 87  VAL G CG2 1 
ATOM   7450  N  N   . THR D  1 89  ? -76.939  -40.690 60.224  1.00 21.57  ? 88  THR G N   1 
ATOM   7451  C  CA  . THR D  1 89  ? -77.766  -40.442 61.385  1.00 23.49  ? 88  THR G CA  1 
ATOM   7452  C  C   . THR D  1 89  ? -77.668  -41.624 62.350  1.00 22.03  ? 88  THR G C   1 
ATOM   7453  O  O   . THR D  1 89  ? -77.933  -42.744 61.980  1.00 23.63  ? 88  THR G O   1 
ATOM   7454  C  CB  . THR D  1 89  ? -79.223  -40.200 60.971  1.00 24.46  ? 88  THR G CB  1 
ATOM   7455  O  OG1 . THR D  1 89  ? -79.253  -39.076 60.093  1.00 22.84  ? 88  THR G OG1 1 
ATOM   7456  C  CG2 . THR D  1 89  ? -80.134  -39.956 62.158  1.00 26.72  ? 88  THR G CG2 1 
ATOM   7457  N  N   . ALA D  1 90  ? -77.275  -41.328 63.584  1.00 22.93  ? 89  ALA G N   1 
ATOM   7458  C  CA  . ALA D  1 90  ? -77.255  -42.297 64.651  1.00 25.28  ? 89  ALA G CA  1 
ATOM   7459  C  C   . ALA D  1 90  ? -78.593  -42.245 65.403  1.00 24.77  ? 89  ALA G C   1 
ATOM   7460  O  O   . ALA D  1 90  ? -79.074  -41.173 65.730  1.00 24.86  ? 89  ALA G O   1 
ATOM   7461  C  CB  . ALA D  1 90  ? -76.098  -42.030 65.583  1.00 24.68  ? 89  ALA G CB  1 
ATOM   7462  N  N   . ASP D  1 91  ? -79.136  -43.426 65.694  1.00 25.04  ? 90  ASP G N   1 
ATOM   7463  C  CA  . ASP D  1 91  ? -80.335  -43.591 66.512  1.00 27.37  ? 90  ASP G CA  1 
ATOM   7464  C  C   . ASP D  1 91  ? -79.995  -43.436 68.008  1.00 30.24  ? 90  ASP G C   1 
ATOM   7465  O  O   . ASP D  1 91  ? -78.864  -43.103 68.400  1.00 29.80  ? 90  ASP G O   1 
ATOM   7466  C  CB  . ASP D  1 91  ? -81.002  -44.918 66.159  1.00 26.72  ? 90  ASP G CB  1 
ATOM   7467  C  CG  . ASP D  1 91  ? -80.245  -46.170 66.580  1.00 28.16  ? 90  ASP G CG  1 
ATOM   7468  O  OD1 . ASP D  1 91  ? -80.543  -47.216 65.998  1.00 29.98  ? 90  ASP G OD1 1 
ATOM   7469  O  OD2 . ASP D  1 91  ? -79.357  -46.090 67.461  1.00 27.36  ? 90  ASP G OD2 1 
ATOM   7470  N  N   . LYS D  1 92  ? -80.992  -43.687 68.864  1.00 33.78  ? 91  LYS G N   1 
ATOM   7471  C  CA  . LYS D  1 92  ? -80.903  -43.480 70.328  1.00 35.56  ? 91  LYS G CA  1 
ATOM   7472  C  C   . LYS D  1 92  ? -79.981  -44.539 70.964  1.00 32.99  ? 91  LYS G C   1 
ATOM   7473  O  O   . LYS D  1 92  ? -79.549  -44.380 72.079  1.00 35.56  ? 91  LYS G O   1 
ATOM   7474  C  CB  . LYS D  1 92  ? -82.312  -43.534 70.939  1.00 40.98  ? 91  LYS G CB  1 
ATOM   7475  C  CG  . LYS D  1 92  ? -82.998  -44.900 70.828  1.00 48.95  ? 91  LYS G CG  1 
ATOM   7476  C  CD  . LYS D  1 92  ? -84.382  -44.915 70.135  1.00 57.60  ? 91  LYS G CD  1 
ATOM   7477  C  CE  . LYS D  1 92  ? -84.349  -45.142 68.622  1.00 55.99  ? 91  LYS G CE  1 
ATOM   7478  N  NZ  . LYS D  1 92  ? -84.008  -43.906 67.860  1.00 44.93  ? 91  LYS G NZ  1 
ATOM   7479  N  N   . ASP D  1 93  ? -79.708  -45.639 70.249  1.00 35.15  ? 92  ASP G N   1 
ATOM   7480  C  CA  . ASP D  1 93  ? -78.727  -46.661 70.658  1.00 36.11  ? 92  ASP G CA  1 
ATOM   7481  C  C   . ASP D  1 93  ? -77.294  -46.333 70.203  1.00 35.05  ? 92  ASP G C   1 
ATOM   7482  O  O   . ASP D  1 93  ? -76.372  -47.113 70.429  1.00 32.42  ? 92  ASP G O   1 
ATOM   7483  C  CB  . ASP D  1 93  ? -79.159  -48.020 70.123  1.00 39.19  ? 92  ASP G CB  1 
ATOM   7484  C  CG  . ASP D  1 93  ? -80.385  -48.524 70.859  1.00 45.24  ? 92  ASP G CG  1 
ATOM   7485  O  OD1 . ASP D  1 93  ? -80.437  -48.329 72.087  1.00 48.88  ? 92  ASP G OD1 1 
ATOM   7486  O  OD2 . ASP D  1 93  ? -81.274  -49.076 70.202  1.00 53.37  ? 92  ASP G OD2 1 
ATOM   7487  N  N   . GLY D  1 94  ? -77.107  -45.183 69.564  1.00 31.72  ? 93  GLY G N   1 
ATOM   7488  C  CA  . GLY D  1 94  ? -75.811  -44.724 69.085  1.00 28.78  ? 93  GLY G CA  1 
ATOM   7489  C  C   . GLY D  1 94  ? -75.371  -45.399 67.793  1.00 26.33  ? 93  GLY G C   1 
ATOM   7490  O  O   . GLY D  1 94  ? -74.210  -45.334 67.447  1.00 25.70  ? 93  GLY G O   1 
ATOM   7491  N  N   . VAL D  1 95  ? -76.312  -45.991 67.056  1.00 24.76  ? 94  VAL G N   1 
ATOM   7492  C  CA  . VAL D  1 95  ? -76.014  -46.742 65.869  1.00 25.00  ? 94  VAL G CA  1 
ATOM   7493  C  C   . VAL D  1 95  ? -76.497  -45.961 64.646  1.00 25.93  ? 94  VAL G C   1 
ATOM   7494  O  O   . VAL D  1 95  ? -77.691  -45.555 64.565  1.00 24.25  ? 94  VAL G O   1 
ATOM   7495  C  CB  . VAL D  1 95  ? -76.676  -48.134 65.922  1.00 26.03  ? 94  VAL G CB  1 
ATOM   7496  C  CG1 . VAL D  1 95  ? -76.514  -48.913 64.630  1.00 27.44  ? 94  VAL G CG1 1 
ATOM   7497  C  CG2 . VAL D  1 95  ? -76.165  -48.960 67.091  1.00 29.62  ? 94  VAL G CG2 1 
ATOM   7498  N  N   . ALA D  1 96  ? -75.599  -45.820 63.670  1.00 22.64  ? 95  ALA G N   1 
ATOM   7499  C  CA  . ALA D  1 96  ? -75.939  -45.354 62.327  1.00 22.91  ? 95  ALA G CA  1 
ATOM   7500  C  C   . ALA D  1 96  ? -75.970  -46.547 61.375  1.00 24.63  ? 95  ALA G C   1 
ATOM   7501  O  O   . ALA D  1 96  ? -74.911  -47.141 61.085  1.00 24.38  ? 95  ALA G O   1 
ATOM   7502  C  CB  . ALA D  1 96  ? -74.953  -44.312 61.858  1.00 23.31  ? 95  ALA G CB  1 
ATOM   7503  N  N   . ASP D  1 97  ? -77.179  -46.903 60.923  1.00 25.60  ? 96  ASP G N   1 
ATOM   7504  C  CA  . ASP D  1 97  ? -77.391  -47.917 59.907  1.00 27.40  ? 96  ASP G CA  1 
ATOM   7505  C  C   . ASP D  1 97  ? -77.290  -47.244 58.541  1.00 25.68  ? 96  ASP G C   1 
ATOM   7506  O  O   . ASP D  1 97  ? -78.286  -46.862 57.935  1.00 27.14  ? 96  ASP G O   1 
ATOM   7507  C  CB  . ASP D  1 97  ? -78.715  -48.654 60.112  1.00 30.27  ? 96  ASP G CB  1 
ATOM   7508  C  CG  . ASP D  1 97  ? -78.640  -49.636 61.273  1.00 36.14  ? 96  ASP G CG  1 
ATOM   7509  O  OD1 . ASP D  1 97  ? -77.618  -50.414 61.343  1.00 36.19  ? 96  ASP G OD1 1 
ATOM   7510  O  OD2 . ASP D  1 97  ? -79.557  -49.585 62.131  1.00 37.01  ? 96  ASP G OD2 1 
ATOM   7511  N  N   . VAL D  1 98  ? -76.065  -47.158 58.040  1.00 22.94  ? 97  VAL G N   1 
ATOM   7512  C  CA  . VAL D  1 98  ? -75.766  -46.375 56.876  1.00 23.01  ? 97  VAL G CA  1 
ATOM   7513  C  C   . VAL D  1 98  ? -76.335  -47.041 55.619  1.00 24.51  ? 97  VAL G C   1 
ATOM   7514  O  O   . VAL D  1 98  ? -76.150  -48.241 55.396  1.00 23.05  ? 97  VAL G O   1 
ATOM   7515  C  CB  . VAL D  1 98  ? -74.260  -46.151 56.742  1.00 22.92  ? 97  VAL G CB  1 
ATOM   7516  C  CG1 . VAL D  1 98  ? -73.963  -45.402 55.462  1.00 24.68  ? 97  VAL G CG1 1 
ATOM   7517  C  CG2 . VAL D  1 98  ? -73.698  -45.443 57.966  1.00 23.50  ? 97  VAL G CG2 1 
ATOM   7518  N  N   . SER D  1 99  ? -76.959  -46.217 54.765  1.00 23.68  ? 98  SER G N   1 
ATOM   7519  C  CA  . SER D  1 99  ? -77.510  -46.637 53.478  1.00 25.91  ? 98  SER G CA  1 
ATOM   7520  C  C   . SER D  1 99  ? -77.526  -45.438 52.533  1.00 26.88  ? 98  SER G C   1 
ATOM   7521  O  O   . SER D  1 99  ? -78.376  -44.569 52.649  1.00 28.61  ? 98  SER G O   1 
ATOM   7522  C  CB  . SER D  1 99  ? -78.906  -47.213 53.645  1.00 30.65  ? 98  SER G CB  1 
ATOM   7523  O  OG  . SER D  1 99  ? -79.306  -47.892 52.471  1.00 35.09  ? 98  SER G OG  1 
ATOM   7524  N  N   . ILE D  1 100 ? -76.559  -45.404 51.625  1.00 24.04  ? 99  ILE G N   1 
ATOM   7525  C  CA  . ILE D  1 100 ? -76.303  -44.309 50.725  1.00 26.06  ? 99  ILE G CA  1 
ATOM   7526  C  C   . ILE D  1 100 ? -76.037  -44.919 49.349  1.00 29.17  ? 99  ILE G C   1 
ATOM   7527  O  O   . ILE D  1 100 ? -75.441  -46.008 49.229  1.00 24.99  ? 99  ILE G O   1 
ATOM   7528  C  CB  . ILE D  1 100 ? -75.110  -43.477 51.252  1.00 27.10  ? 99  ILE G CB  1 
ATOM   7529  C  CG1 . ILE D  1 100 ? -75.523  -42.615 52.446  1.00 28.30  ? 99  ILE G CG1 1 
ATOM   7530  C  CG2 . ILE D  1 100 ? -74.450  -42.613 50.191  1.00 28.81  ? 99  ILE G CG2 1 
ATOM   7531  C  CD1 . ILE D  1 100 ? -74.349  -42.021 53.175  1.00 28.07  ? 99  ILE G CD1 1 
ATOM   7532  N  N   . GLU D  1 101 ? -76.492  -44.227 48.310  1.00 27.27  ? 100 GLU G N   1 
ATOM   7533  C  CA  . GLU D  1 101 ? -76.111  -44.544 46.960  1.00 28.66  ? 100 GLU G CA  1 
ATOM   7534  C  C   . GLU D  1 101 ? -75.557  -43.271 46.326  1.00 28.10  ? 100 GLU G C   1 
ATOM   7535  O  O   . GLU D  1 101 ? -76.167  -42.195 46.389  1.00 26.51  ? 100 GLU G O   1 
ATOM   7536  C  CB  . GLU D  1 101 ? -77.318  -45.115 46.220  1.00 32.31  ? 100 GLU G CB  1 
ATOM   7537  C  CG  . GLU D  1 101 ? -76.976  -45.634 44.851  1.00 40.11  ? 100 GLU G CG  1 
ATOM   7538  C  CD  . GLU D  1 101 ? -78.157  -46.263 44.129  1.00 46.18  ? 100 GLU G CD  1 
ATOM   7539  O  OE1 . GLU D  1 101 ? -78.513  -45.745 43.059  1.00 46.81  ? 100 GLU G OE1 1 
ATOM   7540  O  OE2 . GLU D  1 101 ? -78.725  -47.249 44.659  1.00 54.38  ? 100 GLU G OE2 1 
ATOM   7541  N  N   . ASP D  1 102 ? -74.368  -43.362 45.737  1.00 25.29  ? 101 ASP G N   1 
ATOM   7542  C  CA  . ASP D  1 102 ? -73.747  -42.164 45.229  1.00 24.52  ? 101 ASP G CA  1 
ATOM   7543  C  C   . ASP D  1 102 ? -73.122  -42.466 43.877  1.00 26.72  ? 101 ASP G C   1 
ATOM   7544  O  O   . ASP D  1 102 ? -72.448  -43.487 43.717  1.00 25.46  ? 101 ASP G O   1 
ATOM   7545  C  CB  . ASP D  1 102 ? -72.660  -41.632 46.164  1.00 24.64  ? 101 ASP G CB  1 
ATOM   7546  C  CG  . ASP D  1 102 ? -72.181  -40.248 45.759  1.00 28.11  ? 101 ASP G CG  1 
ATOM   7547  O  OD1 . ASP D  1 102 ? -71.047  -40.111 45.188  1.00 27.96  ? 101 ASP G OD1 1 
ATOM   7548  O  OD2 . ASP D  1 102 ? -72.944  -39.295 46.004  1.00 29.28  ? 101 ASP G OD2 1 
ATOM   7549  N  N   . SER D  1 103 ? -73.227  -41.521 42.948  1.00 27.72  ? 102 SER G N   1 
ATOM   7550  C  CA  . SER D  1 103 ? -72.706  -41.770 41.621  1.00 29.24  ? 102 SER G CA  1 
ATOM   7551  C  C   . SER D  1 103 ? -71.550  -40.835 41.271  1.00 27.75  ? 102 SER G C   1 
ATOM   7552  O  O   . SER D  1 103 ? -71.125  -40.814 40.131  1.00 29.27  ? 102 SER G O   1 
ATOM   7553  C  CB  . SER D  1 103 ? -73.840  -41.735 40.620  1.00 34.55  ? 102 SER G CB  1 
ATOM   7554  O  OG  A SER D  1 103 ? -74.488  -40.478 40.670  0.60 39.32  ? 102 SER G OG  1 
ATOM   7555  O  OG  B SER D  1 103 ? -74.505  -40.485 40.678  0.40 37.15  ? 102 SER G OG  1 
ATOM   7556  N  N   . VAL D  1 104 ? -70.980  -40.140 42.261  1.00 22.12  ? 103 VAL G N   1 
ATOM   7557  C  CA  . VAL D  1 104 ? -69.822  -39.314 42.025  1.00 24.21  ? 103 VAL G CA  1 
ATOM   7558  C  C   . VAL D  1 104 ? -68.557  -40.055 42.481  1.00 23.73  ? 103 VAL G C   1 
ATOM   7559  O  O   . VAL D  1 104 ? -67.543  -40.013 41.793  1.00 26.80  ? 103 VAL G O   1 
ATOM   7560  C  CB  . VAL D  1 104 ? -69.950  -37.939 42.703  1.00 23.60  ? 103 VAL G CB  1 
ATOM   7561  C  CG1 . VAL D  1 104 ? -68.640  -37.177 42.658  1.00 23.84  ? 103 VAL G CG1 1 
ATOM   7562  C  CG2 . VAL D  1 104 ? -71.065  -37.117 42.058  1.00 27.19  ? 103 VAL G CG2 1 
ATOM   7563  N  N   . ILE D  1 105 ? -68.596  -40.673 43.663  1.00 22.91  ? 104 ILE G N   1 
ATOM   7564  C  CA  . ILE D  1 105 ? -67.514  -41.574 44.052  1.00 22.80  ? 104 ILE G CA  1 
ATOM   7565  C  C   . ILE D  1 105 ? -67.526  -42.753 43.078  1.00 21.74  ? 104 ILE G C   1 
ATOM   7566  O  O   . ILE D  1 105 ? -68.545  -43.083 42.481  1.00 21.33  ? 104 ILE G O   1 
ATOM   7567  C  CB  . ILE D  1 105 ? -67.615  -42.072 45.508  1.00 21.75  ? 104 ILE G CB  1 
ATOM   7568  C  CG1 . ILE D  1 105 ? -68.932  -42.794 45.788  1.00 20.88  ? 104 ILE G CG1 1 
ATOM   7569  C  CG2 . ILE D  1 105 ? -67.366  -40.929 46.471  1.00 22.50  ? 104 ILE G CG2 1 
ATOM   7570  C  CD1 . ILE D  1 105 ? -68.910  -43.634 47.043  1.00 20.99  ? 104 ILE G CD1 1 
ATOM   7571  N  N   . SER D  1 106 ? -66.395  -43.440 43.023  1.00 21.93  ? 105 SER G N   1 
ATOM   7572  C  CA  . SER D  1 106 ? -66.241  -44.643 42.276  1.00 22.50  ? 105 SER G CA  1 
ATOM   7573  C  C   . SER D  1 106 ? -65.292  -45.577 43.024  1.00 22.56  ? 105 SER G C   1 
ATOM   7574  O  O   . SER D  1 106 ? -64.556  -45.145 43.922  1.00 22.06  ? 105 SER G O   1 
ATOM   7575  C  CB  . SER D  1 106 ? -65.713  -44.362 40.878  1.00 24.11  ? 105 SER G CB  1 
ATOM   7576  O  OG  . SER D  1 106 ? -65.897  -45.518 40.057  1.00 25.88  ? 105 SER G OG  1 
ATOM   7577  N  N   . LEU D  1 107 ? -65.313  -46.848 42.632  1.00 23.00  ? 106 LEU G N   1 
ATOM   7578  C  CA  . LEU D  1 107 ? -64.301  -47.812 43.117  1.00 23.53  ? 106 LEU G CA  1 
ATOM   7579  C  C   . LEU D  1 107 ? -63.243  -48.096 42.035  1.00 24.71  ? 106 LEU G C   1 
ATOM   7580  O  O   . LEU D  1 107 ? -62.431  -49.040 42.192  1.00 25.02  ? 106 LEU G O   1 
ATOM   7581  C  CB  . LEU D  1 107 ? -64.988  -49.101 43.564  1.00 21.31  ? 106 LEU G CB  1 
ATOM   7582  C  CG  . LEU D  1 107 ? -66.058  -48.967 44.637  1.00 22.84  ? 106 LEU G CG  1 
ATOM   7583  C  CD1 . LEU D  1 107 ? -66.562  -50.336 45.080  1.00 21.92  ? 106 LEU G CD1 1 
ATOM   7584  C  CD2 . LEU D  1 107 ? -65.540  -48.188 45.823  1.00 22.75  ? 106 LEU G CD2 1 
ATOM   7585  N  N   . SER D  1 108 ? -63.230  -47.302 40.959  1.00 23.58  ? 107 SER G N   1 
ATOM   7586  C  CA  . SER D  1 108 ? -62.146  -47.332 39.968  1.00 26.98  ? 107 SER G CA  1 
ATOM   7587  C  C   . SER D  1 108 ? -62.070  -45.989 39.263  1.00 27.37  ? 107 SER G C   1 
ATOM   7588  O  O   . SER D  1 108 ? -62.982  -45.185 39.368  1.00 27.14  ? 107 SER G O   1 
ATOM   7589  C  CB  . SER D  1 108 ? -62.286  -48.448 38.956  1.00 29.80  ? 107 SER G CB  1 
ATOM   7590  O  OG  . SER D  1 108 ? -63.558  -48.425 38.322  1.00 34.13  ? 107 SER G OG  1 
ATOM   7591  N  N   . GLY D  1 109 ? -60.956  -45.791 38.560  1.00 27.29  ? 108 GLY G N   1 
ATOM   7592  C  CA  . GLY D  1 109 ? -60.712  -44.617 37.726  1.00 28.83  ? 108 GLY G CA  1 
ATOM   7593  C  C   . GLY D  1 109 ? -60.346  -43.401 38.559  1.00 28.09  ? 108 GLY G C   1 
ATOM   7594  O  O   . GLY D  1 109 ? -59.938  -43.527 39.710  1.00 26.81  ? 108 GLY G O   1 
ATOM   7595  N  N   . ASP D  1 110 ? -60.556  -42.226 37.960  1.00 27.86  ? 109 ASP G N   1 
ATOM   7596  C  CA  . ASP D  1 110 ? -60.149  -40.932 38.483  1.00 29.57  ? 109 ASP G CA  1 
ATOM   7597  C  C   . ASP D  1 110 ? -60.776  -40.668 39.861  1.00 26.33  ? 109 ASP G C   1 
ATOM   7598  O  O   . ASP D  1 110 ? -60.153  -40.046 40.680  1.00 24.68  ? 109 ASP G O   1 
ATOM   7599  C  CB  . ASP D  1 110 ? -60.634  -39.795 37.577  1.00 33.72  ? 109 ASP G CB  1 
ATOM   7600  C  CG  . ASP D  1 110 ? -59.936  -39.650 36.233  1.00 36.79  ? 109 ASP G CG  1 
ATOM   7601  O  OD1 . ASP D  1 110 ? -60.204  -38.643 35.561  1.00 41.74  ? 109 ASP G OD1 1 
ATOM   7602  O  OD2 . ASP D  1 110 ? -59.143  -40.528 35.865  1.00 41.12  ? 109 ASP G OD2 1 
ATOM   7603  N  N   . HIS D  1 111 ? -62.033  -41.085 40.047  1.00 23.02  ? 110 HIS G N   1 
ATOM   7604  C  CA  . HIS D  1 111 ? -62.777  -40.813 41.253  1.00 24.74  ? 110 HIS G CA  1 
ATOM   7605  C  C   . HIS D  1 111 ? -62.686  -41.993 42.231  1.00 23.74  ? 110 HIS G C   1 
ATOM   7606  O  O   . HIS D  1 111 ? -63.466  -42.035 43.202  1.00 22.81  ? 110 HIS G O   1 
ATOM   7607  C  CB  . HIS D  1 111 ? -64.235  -40.460 40.909  1.00 26.05  ? 110 HIS G CB  1 
ATOM   7608  C  CG  . HIS D  1 111 ? -64.363  -39.108 40.282  1.00 28.69  ? 110 HIS G CG  1 
ATOM   7609  N  ND1 . HIS D  1 111 ? -65.590  -38.506 40.078  1.00 31.75  ? 110 HIS G ND1 1 
ATOM   7610  C  CD2 . HIS D  1 111 ? -63.428  -38.221 39.879  1.00 30.40  ? 110 HIS G CD2 1 
ATOM   7611  C  CE1 . HIS D  1 111 ? -65.396  -37.323 39.531  1.00 33.23  ? 110 HIS G CE1 1 
ATOM   7612  N  NE2 . HIS D  1 111 ? -64.083  -37.131 39.380  1.00 31.55  ? 110 HIS G NE2 1 
ATOM   7613  N  N   . SER D  1 112 ? -61.726  -42.916 42.024  1.00 21.21  ? 111 SER G N   1 
ATOM   7614  C  CA  . SER D  1 112 ? -61.651  -44.090 42.876  1.00 19.97  ? 111 SER G CA  1 
ATOM   7615  C  C   . SER D  1 112 ? -61.380  -43.638 44.315  1.00 17.72  ? 111 SER G C   1 
ATOM   7616  O  O   . SER D  1 112 ? -60.535  -42.808 44.531  1.00 19.16  ? 111 SER G O   1 
ATOM   7617  C  CB  . SER D  1 112 ? -60.578  -45.068 42.450  1.00 20.15  ? 111 SER G CB  1 
ATOM   7618  O  OG  . SER D  1 112 ? -60.620  -46.170 43.330  1.00 21.12  ? 111 SER G OG  1 
ATOM   7619  N  N   . ILE D  1 113 ? -62.082  -44.225 45.277  1.00 18.24  ? 112 ILE G N   1 
ATOM   7620  C  CA  . ILE D  1 113 ? -61.842  -43.972 46.689  1.00 19.75  ? 112 ILE G CA  1 
ATOM   7621  C  C   . ILE D  1 113 ? -61.047  -45.127 47.322  1.00 20.57  ? 112 ILE G C   1 
ATOM   7622  O  O   . ILE D  1 113 ? -60.804  -45.088 48.530  1.00 18.26  ? 112 ILE G O   1 
ATOM   7623  C  CB  . ILE D  1 113 ? -63.180  -43.725 47.419  1.00 20.59  ? 112 ILE G CB  1 
ATOM   7624  C  CG1 . ILE D  1 113 ? -64.064  -44.972 47.394  1.00 21.21  ? 112 ILE G CG1 1 
ATOM   7625  C  CG2 . ILE D  1 113 ? -63.873  -42.505 46.814  1.00 23.05  ? 112 ILE G CG2 1 
ATOM   7626  C  CD1 . ILE D  1 113 ? -65.384  -44.855 48.132  1.00 22.64  ? 112 ILE G CD1 1 
ATOM   7627  N  N   . ILE D  1 114 ? -60.668  -46.150 46.527  1.00 20.89  ? 113 ILE G N   1 
ATOM   7628  C  CA  . ILE D  1 114 ? -59.808  -47.240 47.015  1.00 21.78  ? 113 ILE G CA  1 
ATOM   7629  C  C   . ILE D  1 114 ? -58.473  -46.663 47.489  1.00 19.82  ? 113 ILE G C   1 
ATOM   7630  O  O   . ILE D  1 114 ? -57.787  -45.926 46.781  1.00 18.54  ? 113 ILE G O   1 
ATOM   7631  C  CB  . ILE D  1 114 ? -59.554  -48.330 45.955  1.00 22.51  ? 113 ILE G CB  1 
ATOM   7632  C  CG1 . ILE D  1 114 ? -60.848  -48.926 45.402  1.00 24.77  ? 113 ILE G CG1 1 
ATOM   7633  C  CG2 . ILE D  1 114 ? -58.642  -49.420 46.516  1.00 23.69  ? 113 ILE G CG2 1 
ATOM   7634  C  CD1 . ILE D  1 114 ? -61.710  -49.571 46.397  1.00 24.59  ? 113 ILE G CD1 1 
ATOM   7635  N  N   . GLY D  1 115 ? -58.113  -46.988 48.726  1.00 19.97  ? 114 GLY G N   1 
ATOM   7636  C  CA  . GLY D  1 115 ? -56.865  -46.504 49.301  1.00 20.28  ? 114 GLY G CA  1 
ATOM   7637  C  C   . GLY D  1 115 ? -56.956  -45.108 49.910  1.00 20.44  ? 114 GLY G C   1 
ATOM   7638  O  O   . GLY D  1 115 ? -55.927  -44.539 50.278  1.00 18.78  ? 114 GLY G O   1 
ATOM   7639  N  N   . ARG D  1 116 ? -58.171  -44.547 50.009  1.00 20.57  ? 115 ARG G N   1 
ATOM   7640  C  CA  . ARG D  1 116 ? -58.396  -43.243 50.660  1.00 21.94  ? 115 ARG G CA  1 
ATOM   7641  C  C   . ARG D  1 116 ? -59.054  -43.561 52.005  1.00 22.79  ? 115 ARG G C   1 
ATOM   7642  O  O   . ARG D  1 116 ? -59.214  -44.730 52.335  1.00 22.60  ? 115 ARG G O   1 
ATOM   7643  C  CB  . ARG D  1 116 ? -59.188  -42.327 49.708  1.00 22.75  ? 115 ARG G CB  1 
ATOM   7644  C  CG  . ARG D  1 116 ? -58.560  -42.226 48.320  1.00 22.82  ? 115 ARG G CG  1 
ATOM   7645  C  CD  . ARG D  1 116 ? -59.094  -41.108 47.468  1.00 23.11  ? 115 ARG G CD  1 
ATOM   7646  N  NE  . ARG D  1 116 ? -58.473  -41.068 46.150  1.00 22.96  ? 115 ARG G NE  1 
ATOM   7647  C  CZ  . ARG D  1 116 ? -57.363  -40.404 45.815  1.00 21.79  ? 115 ARG G CZ  1 
ATOM   7648  N  NH1 . ARG D  1 116 ? -56.973  -40.433 44.550  1.00 22.21  ? 115 ARG G NH1 1 
ATOM   7649  N  NH2 . ARG D  1 116 ? -56.670  -39.708 46.701  1.00 20.13  ? 115 ARG G NH2 1 
ATOM   7650  N  N   . THR D  1 117 ? -59.392  -42.534 52.786  1.00 19.98  ? 116 THR G N   1 
ATOM   7651  C  CA  . THR D  1 117 ? -59.890  -42.697 54.128  1.00 20.69  ? 116 THR G CA  1 
ATOM   7652  C  C   . THR D  1 117 ? -61.344  -42.226 54.215  1.00 20.12  ? 116 THR G C   1 
ATOM   7653  O  O   . THR D  1 117 ? -61.681  -41.129 53.745  1.00 22.50  ? 116 THR G O   1 
ATOM   7654  C  CB  . THR D  1 117 ? -59.028  -41.903 55.110  1.00 21.72  ? 116 THR G CB  1 
ATOM   7655  O  OG1 . THR D  1 117 ? -57.695  -42.416 55.030  1.00 21.91  ? 116 THR G OG1 1 
ATOM   7656  C  CG2 . THR D  1 117 ? -59.536  -41.958 56.534  1.00 21.79  ? 116 THR G CG2 1 
ATOM   7657  N  N   . LEU D  1 118 ? -62.200  -43.079 54.777  1.00 18.85  ? 117 LEU G N   1 
ATOM   7658  C  CA  . LEU D  1 118 ? -63.541  -42.720 55.167  1.00 18.93  ? 117 LEU G CA  1 
ATOM   7659  C  C   . LEU D  1 118 ? -63.482  -42.198 56.603  1.00 20.11  ? 117 LEU G C   1 
ATOM   7660  O  O   . LEU D  1 118 ? -62.851  -42.826 57.482  1.00 19.03  ? 117 LEU G O   1 
ATOM   7661  C  CB  . LEU D  1 118 ? -64.435  -43.954 55.026  1.00 20.08  ? 117 LEU G CB  1 
ATOM   7662  C  CG  . LEU D  1 118 ? -65.920  -43.732 55.300  1.00 22.24  ? 117 LEU G CG  1 
ATOM   7663  C  CD1 . LEU D  1 118 ? -66.553  -42.833 54.248  1.00 22.24  ? 117 LEU G CD1 1 
ATOM   7664  C  CD2 . LEU D  1 118 ? -66.648  -45.056 55.369  1.00 23.12  ? 117 LEU G CD2 1 
ATOM   7665  N  N   . VAL D  1 119 ? -64.140  -41.063 56.840  1.00 19.79  ? 118 VAL G N   1 
ATOM   7666  C  CA  . VAL D  1 119 ? -64.147  -40.393 58.135  1.00 21.16  ? 118 VAL G CA  1 
ATOM   7667  C  C   . VAL D  1 119 ? -65.599  -40.166 58.561  1.00 21.71  ? 118 VAL G C   1 
ATOM   7668  O  O   . VAL D  1 119 ? -66.421  -39.731 57.745  1.00 20.69  ? 118 VAL G O   1 
ATOM   7669  C  CB  . VAL D  1 119 ? -63.385  -39.056 58.078  1.00 22.49  ? 118 VAL G CB  1 
ATOM   7670  C  CG1 . VAL D  1 119 ? -63.456  -38.317 59.412  1.00 23.84  ? 118 VAL G CG1 1 
ATOM   7671  C  CG2 . VAL D  1 119 ? -61.939  -39.237 57.649  1.00 22.31  ? 118 VAL G CG2 1 
ATOM   7672  N  N   . VAL D  1 120 ? -65.907  -40.458 59.832  1.00 20.33  ? 119 VAL G N   1 
ATOM   7673  C  CA  . VAL D  1 120 ? -67.162  -40.029 60.449  1.00 20.32  ? 119 VAL G CA  1 
ATOM   7674  C  C   . VAL D  1 120 ? -66.847  -38.971 61.520  1.00 21.29  ? 119 VAL G C   1 
ATOM   7675  O  O   . VAL D  1 120 ? -65.899  -39.115 62.321  1.00 20.92  ? 119 VAL G O   1 
ATOM   7676  C  CB  . VAL D  1 120 ? -67.978  -41.207 61.005  1.00 21.22  ? 119 VAL G CB  1 
ATOM   7677  C  CG1 . VAL D  1 120 ? -67.236  -41.938 62.114  1.00 22.93  ? 119 VAL G CG1 1 
ATOM   7678  C  CG2 . VAL D  1 120 ? -69.345  -40.725 61.475  1.00 21.45  ? 119 VAL G CG2 1 
ATOM   7679  N  N   . HIS D  1 121 ? -67.609  -37.872 61.485  1.00 19.73  ? 120 HIS G N   1 
ATOM   7680  C  CA  . HIS D  1 121 ? -67.276  -36.649 62.196  1.00 20.06  ? 120 HIS G CA  1 
ATOM   7681  C  C   . HIS D  1 121 ? -68.157  -36.464 63.437  1.00 20.59  ? 120 HIS G C   1 
ATOM   7682  O  O   . HIS D  1 121 ? -69.194  -37.105 63.633  1.00 21.51  ? 120 HIS G O   1 
ATOM   7683  C  CB  . HIS D  1 121 ? -67.429  -35.441 61.274  1.00 18.93  ? 120 HIS G CB  1 
ATOM   7684  C  CG  . HIS D  1 121 ? -66.341  -35.283 60.287  1.00 19.91  ? 120 HIS G CG  1 
ATOM   7685  N  ND1 . HIS D  1 121 ? -65.302  -34.424 60.497  1.00 20.17  ? 120 HIS G ND1 1 
ATOM   7686  C  CD2 . HIS D  1 121 ? -66.176  -35.780 59.035  1.00 20.87  ? 120 HIS G CD2 1 
ATOM   7687  C  CE1 . HIS D  1 121 ? -64.508  -34.439 59.447  1.00 21.29  ? 120 HIS G CE1 1 
ATOM   7688  N  NE2 . HIS D  1 121 ? -65.035  -35.227 58.529  1.00 21.54  ? 120 HIS G NE2 1 
ATOM   7689  N  N   . GLU D  1 122 ? -67.714  -35.528 64.261  1.00 23.11  ? 121 GLU G N   1 
ATOM   7690  C  CA  . GLU D  1 122 ? -68.311  -35.207 65.558  1.00 25.31  ? 121 GLU G CA  1 
ATOM   7691  C  C   . GLU D  1 122 ? -69.695  -34.548 65.412  1.00 23.44  ? 121 GLU G C   1 
ATOM   7692  O  O   . GLU D  1 122 ? -70.611  -34.861 66.173  1.00 22.22  ? 121 GLU G O   1 
ATOM   7693  C  CB  . GLU D  1 122 ? -67.320  -34.285 66.258  1.00 29.21  ? 121 GLU G CB  1 
ATOM   7694  C  CG  . GLU D  1 122 ? -67.850  -33.569 67.473  1.00 36.34  ? 121 GLU G CG  1 
ATOM   7695  C  CD  . GLU D  1 122 ? -66.857  -32.518 67.957  1.00 41.87  ? 121 GLU G CD  1 
ATOM   7696  O  OE1 . GLU D  1 122 ? -66.639  -32.500 69.167  1.00 51.76  ? 121 GLU G OE1 1 
ATOM   7697  O  OE2 . GLU D  1 122 ? -66.269  -31.747 67.108  1.00 39.59  ? 121 GLU G OE2 1 
ATOM   7698  N  N   . LYS D  1 123 ? -69.849  -33.687 64.412  1.00 24.15  ? 122 LYS G N   1 
ATOM   7699  C  CA  . LYS D  1 123 ? -71.043  -32.840 64.252  1.00 27.67  ? 122 LYS G CA  1 
ATOM   7700  C  C   . LYS D  1 123 ? -71.685  -33.070 62.882  1.00 24.52  ? 122 LYS G C   1 
ATOM   7701  O  O   . LYS D  1 123 ? -71.104  -33.742 62.012  1.00 21.79  ? 122 LYS G O   1 
ATOM   7702  C  CB  . LYS D  1 123 ? -70.650  -31.356 64.337  1.00 31.60  ? 122 LYS G CB  1 
ATOM   7703  C  CG  . LYS D  1 123 ? -70.021  -30.929 65.652  1.00 37.15  ? 122 LYS G CG  1 
ATOM   7704  C  CD  . LYS D  1 123 ? -69.885  -29.432 65.770  1.00 41.18  ? 122 LYS G CD  1 
ATOM   7705  C  CE  . LYS D  1 123 ? -68.699  -28.908 65.002  1.00 46.25  ? 122 LYS G CE  1 
ATOM   7706  N  NZ  . LYS D  1 123 ? -68.727  -27.428 64.893  1.00 53.65  ? 122 LYS G NZ  1 
ATOM   7707  N  N   . ALA D  1 124 ? -72.851  -32.438 62.677  1.00 23.43  ? 123 ALA G N   1 
ATOM   7708  C  CA  . ALA D  1 124 ? -73.551  -32.458 61.402  1.00 22.97  ? 123 ALA G CA  1 
ATOM   7709  C  C   . ALA D  1 124 ? -72.744  -31.699 60.349  1.00 22.10  ? 123 ALA G C   1 
ATOM   7710  O  O   . ALA D  1 124 ? -72.071  -30.720 60.630  1.00 21.91  ? 123 ALA G O   1 
ATOM   7711  C  CB  . ALA D  1 124 ? -74.928  -31.871 61.565  1.00 25.97  ? 123 ALA G CB  1 
ATOM   7712  N  N   . ASP D  1 125 ? -72.802  -32.193 59.119  1.00 21.28  ? 124 ASP G N   1 
ATOM   7713  C  CA  . ASP D  1 125 ? -72.320  -31.497 57.957  1.00 22.25  ? 124 ASP G CA  1 
ATOM   7714  C  C   . ASP D  1 125 ? -73.421  -30.536 57.476  1.00 21.61  ? 124 ASP G C   1 
ATOM   7715  O  O   . ASP D  1 125 ? -74.541  -30.979 57.205  1.00 21.07  ? 124 ASP G O   1 
ATOM   7716  C  CB  . ASP D  1 125 ? -71.951  -32.548 56.903  1.00 22.05  ? 124 ASP G CB  1 
ATOM   7717  C  CG  . ASP D  1 125 ? -71.320  -32.059 55.618  1.00 25.06  ? 124 ASP G CG  1 
ATOM   7718  O  OD1 . ASP D  1 125 ? -71.453  -30.846 55.311  1.00 23.89  ? 124 ASP G OD1 1 
ATOM   7719  O  OD2 . ASP D  1 125 ? -70.736  -32.931 54.891  1.00 25.16  ? 124 ASP G OD2 1 
ATOM   7720  N  N   . ASP D  1 126 ? -73.081  -29.254 57.316  1.00 21.60  ? 125 ASP G N   1 
ATOM   7721  C  CA  . ASP D  1 126 ? -74.037  -28.211 56.893  1.00 23.77  ? 125 ASP G CA  1 
ATOM   7722  C  C   . ASP D  1 126 ? -74.195  -28.202 55.360  1.00 22.98  ? 125 ASP G C   1 
ATOM   7723  O  O   . ASP D  1 126 ? -74.915  -27.352 54.790  1.00 21.13  ? 125 ASP G O   1 
ATOM   7724  C  CB  . ASP D  1 126 ? -73.659  -26.848 57.491  1.00 24.33  ? 125 ASP G CB  1 
ATOM   7725  C  CG  . ASP D  1 126 ? -72.423  -26.169 56.941  1.00 23.30  ? 125 ASP G CG  1 
ATOM   7726  O  OD1 . ASP D  1 126 ? -71.934  -25.242 57.618  1.00 24.83  ? 125 ASP G OD1 1 
ATOM   7727  O  OD2 . ASP D  1 126 ? -71.950  -26.552 55.845  1.00 22.81  ? 125 ASP G OD2 1 
ATOM   7728  N  N   . LEU D  1 127 ? -73.517  -29.132 54.676  1.00 21.08  ? 126 LEU G N   1 
ATOM   7729  C  CA  . LEU D  1 127 ? -73.662  -29.377 53.255  1.00 20.80  ? 126 LEU G CA  1 
ATOM   7730  C  C   . LEU D  1 127 ? -73.212  -28.150 52.461  1.00 21.87  ? 126 LEU G C   1 
ATOM   7731  O  O   . LEU D  1 127 ? -73.639  -27.949 51.353  1.00 21.28  ? 126 LEU G O   1 
ATOM   7732  C  CB  . LEU D  1 127 ? -75.099  -29.784 52.903  1.00 23.59  ? 126 LEU G CB  1 
ATOM   7733  C  CG  . LEU D  1 127 ? -75.680  -30.967 53.676  1.00 24.73  ? 126 LEU G CG  1 
ATOM   7734  C  CD1 . LEU D  1 127 ? -77.058  -31.324 53.171  1.00 26.26  ? 126 LEU G CD1 1 
ATOM   7735  C  CD2 . LEU D  1 127 ? -74.776  -32.192 53.623  1.00 24.41  ? 126 LEU G CD2 1 
ATOM   7736  N  N   . GLY D  1 128 ? -72.251  -27.407 53.013  1.00 21.60  ? 127 GLY G N   1 
ATOM   7737  C  CA  . GLY D  1 128 ? -71.645  -26.269 52.361  1.00 21.32  ? 127 GLY G CA  1 
ATOM   7738  C  C   . GLY D  1 128 ? -72.537  -25.024 52.355  1.00 22.18  ? 127 GLY G C   1 
ATOM   7739  O  O   . GLY D  1 128 ? -72.215  -24.080 51.659  1.00 22.32  ? 127 GLY G O   1 
ATOM   7740  N  N   . LYS D  1 129 ? -73.588  -25.019 53.182  1.00 21.27  ? 128 LYS G N   1 
ATOM   7741  C  CA  . LYS D  1 129 ? -74.619  -23.962 53.234  1.00 24.07  ? 128 LYS G CA  1 
ATOM   7742  C  C   . LYS D  1 129 ? -74.481  -23.098 54.498  1.00 23.90  ? 128 LYS G C   1 
ATOM   7743  O  O   . LYS D  1 129 ? -75.390  -22.373 54.824  1.00 23.56  ? 128 LYS G O   1 
ATOM   7744  C  CB  . LYS D  1 129 ? -76.005  -24.616 53.130  1.00 26.05  ? 128 LYS G CB  1 
ATOM   7745  C  CG  . LYS D  1 129 ? -76.248  -25.271 51.766  1.00 30.11  ? 128 LYS G CG  1 
ATOM   7746  C  CD  . LYS D  1 129 ? -77.628  -25.838 51.529  1.00 35.82  ? 128 LYS G CD  1 
ATOM   7747  C  CE  . LYS D  1 129 ? -77.766  -26.438 50.130  1.00 42.22  ? 128 LYS G CE  1 
ATOM   7748  N  NZ  . LYS D  1 129 ? -76.862  -27.605 49.913  1.00 47.54  ? 128 LYS G NZ  1 
ATOM   7749  N  N   . GLY D  1 130 ? -73.309  -23.126 55.141  1.00 23.26  ? 129 GLY G N   1 
ATOM   7750  C  CA  . GLY D  1 130 ? -73.083  -22.494 56.424  1.00 23.74  ? 129 GLY G CA  1 
ATOM   7751  C  C   . GLY D  1 130 ? -72.676  -21.026 56.357  1.00 23.68  ? 129 GLY G C   1 
ATOM   7752  O  O   . GLY D  1 130 ? -72.732  -20.344 57.393  1.00 23.90  ? 129 GLY G O   1 
ATOM   7753  N  N   . GLY D  1 131 ? -72.175  -20.577 55.200  1.00 20.96  ? 130 GLY G N   1 
ATOM   7754  C  CA  . GLY D  1 131 ? -71.857  -19.177 54.933  1.00 22.95  ? 130 GLY G CA  1 
ATOM   7755  C  C   . GLY D  1 131 ? -70.567  -18.691 55.564  1.00 25.98  ? 130 GLY G C   1 
ATOM   7756  O  O   . GLY D  1 131 ? -70.291  -17.499 55.517  1.00 22.55  ? 130 GLY G O   1 
ATOM   7757  N  N   . ASN D  1 132 ? -69.800  -19.596 56.200  1.00 26.09  ? 131 ASN G N   1 
ATOM   7758  C  CA  . ASN D  1 132 ? -68.465  -19.302 56.716  1.00 28.73  ? 131 ASN G CA  1 
ATOM   7759  C  C   . ASN D  1 132 ? -67.461  -20.075 55.862  1.00 28.53  ? 131 ASN G C   1 
ATOM   7760  O  O   . ASN D  1 132 ? -67.830  -20.980 55.068  1.00 27.05  ? 131 ASN G O   1 
ATOM   7761  C  CB  . ASN D  1 132 ? -68.337  -19.558 58.237  1.00 29.11  ? 131 ASN G CB  1 
ATOM   7762  C  CG  . ASN D  1 132 ? -68.440  -21.020 58.636  1.00 30.58  ? 131 ASN G CG  1 
ATOM   7763  O  OD1 . ASN D  1 132 ? -68.768  -21.869 57.809  1.00 28.71  ? 131 ASN G OD1 1 
ATOM   7764  N  ND2 . ASN D  1 132 ? -68.179  -21.325 59.901  1.00 28.62  ? 131 ASN G ND2 1 
ATOM   7765  N  N   . GLU D  1 133 ? -66.184  -19.705 55.977  1.00 31.47  ? 132 GLU G N   1 
ATOM   7766  C  CA  . GLU D  1 133 ? -65.142  -20.345 55.139  1.00 32.38  ? 132 GLU G CA  1 
ATOM   7767  C  C   . GLU D  1 133 ? -65.106  -21.851 55.426  1.00 28.97  ? 132 GLU G C   1 
ATOM   7768  O  O   . GLU D  1 133 ? -64.921  -22.622 54.519  1.00 30.10  ? 132 GLU G O   1 
ATOM   7769  C  CB  . GLU D  1 133 ? -63.690  -19.839 55.293  1.00 38.87  ? 132 GLU G CB  1 
ATOM   7770  C  CG  A GLU D  1 133 ? -63.330  -20.011 53.814  0.60 43.58  ? 132 GLU G CG  1 
ATOM   7771  C  CG  B GLU D  1 133 ? -63.688  -19.607 56.794  0.40 39.01  ? 132 GLU G CG  1 
ATOM   7772  C  CD  A GLU D  1 133 ? -61.867  -19.769 53.482  0.60 50.02  ? 132 GLU G CD  1 
ATOM   7773  C  CD  B GLU D  1 133 ? -63.609  -18.146 57.182  0.40 41.63  ? 132 GLU G CD  1 
ATOM   7774  O  OE1 A GLU D  1 133 ? -61.493  -19.957 52.303  0.60 52.94  ? 132 GLU G OE1 1 
ATOM   7775  O  OE1 B GLU D  1 133 ? -62.612  -17.767 57.857  0.40 42.00  ? 132 GLU G OE1 1 
ATOM   7776  O  OE2 A GLU D  1 133 ? -61.102  -19.399 54.399  0.60 53.70  ? 132 GLU G OE2 1 
ATOM   7777  O  OE2 B GLU D  1 133 ? -64.520  -17.393 56.786  0.40 40.75  ? 132 GLU G OE2 1 
ATOM   7778  N  N   . GLU D  1 134 ? -65.298  -22.242 56.688  1.00 29.74  ? 133 GLU G N   1 
ATOM   7779  C  CA  . GLU D  1 134 ? -65.175  -23.651 57.089  1.00 30.87  ? 133 GLU G CA  1 
ATOM   7780  C  C   . GLU D  1 134 ? -66.246  -24.491 56.361  1.00 29.92  ? 133 GLU G C   1 
ATOM   7781  O  O   . GLU D  1 134 ? -66.028  -25.664 56.047  1.00 26.74  ? 133 GLU G O   1 
ATOM   7782  C  CB  . GLU D  1 134 ? -65.326  -23.728 58.610  1.00 32.60  ? 133 GLU G CB  1 
ATOM   7783  C  CG  . GLU D  1 134 ? -64.941  -25.067 59.206  1.00 36.87  ? 133 GLU G CG  1 
ATOM   7784  C  CD  . GLU D  1 134 ? -63.500  -25.435 58.877  1.00 38.66  ? 133 GLU G CD  1 
ATOM   7785  O  OE1 . GLU D  1 134 ? -62.626  -24.590 59.070  1.00 46.27  ? 133 GLU G OE1 1 
ATOM   7786  O  OE2 . GLU D  1 134 ? -63.275  -26.519 58.335  1.00 42.16  ? 133 GLU G OE2 1 
ATOM   7787  N  N   . SER D  1 135 ? -67.435  -23.904 56.131  1.00 25.39  ? 134 SER G N   1 
ATOM   7788  C  CA  . SER D  1 135 ? -68.557  -24.623 55.500  1.00 25.25  ? 134 SER G CA  1 
ATOM   7789  C  C   . SER D  1 135 ? -68.099  -25.142 54.136  1.00 24.26  ? 134 SER G C   1 
ATOM   7790  O  O   . SER D  1 135 ? -68.426  -26.250 53.760  1.00 23.42  ? 134 SER G O   1 
ATOM   7791  C  CB  . SER D  1 135 ? -69.789  -23.753 55.344  1.00 25.81  ? 134 SER G CB  1 
ATOM   7792  O  OG  . SER D  1 135 ? -70.877  -24.475 54.775  1.00 23.45  ? 134 SER G OG  1 
ATOM   7793  N  N   . THR D  1 136 ? -67.354  -24.302 53.414  1.00 24.21  ? 135 THR G N   1 
ATOM   7794  C  CA  . THR D  1 136 ? -66.929  -24.546 52.060  1.00 28.26  ? 135 THR G CA  1 
ATOM   7795  C  C   . THR D  1 136 ? -65.782  -25.573 52.016  1.00 28.02  ? 135 THR G C   1 
ATOM   7796  O  O   . THR D  1 136 ? -65.380  -26.001 50.935  1.00 28.55  ? 135 THR G O   1 
ATOM   7797  C  CB  . THR D  1 136 ? -66.464  -23.240 51.387  1.00 30.12  ? 135 THR G CB  1 
ATOM   7798  O  OG1 . THR D  1 136 ? -65.249  -22.809 51.997  1.00 33.15  ? 135 THR G OG1 1 
ATOM   7799  C  CG2 . THR D  1 136 ? -67.474  -22.122 51.494  1.00 33.14  ? 135 THR G CG2 1 
ATOM   7800  N  N   . LYS D  1 137 ? -65.240  -25.939 53.179  1.00 28.01  ? 136 LYS G N   1 
ATOM   7801  C  CA  . LYS D  1 137 ? -64.107  -26.899 53.259  1.00 31.19  ? 136 LYS G CA  1 
ATOM   7802  C  C   . LYS D  1 137 ? -64.557  -28.228 53.869  1.00 27.42  ? 136 LYS G C   1 
ATOM   7803  O  O   . LYS D  1 137 ? -64.300  -29.255 53.277  1.00 26.38  ? 136 LYS G O   1 
ATOM   7804  C  CB  . LYS D  1 137 ? -62.938  -26.260 54.016  1.00 33.69  ? 136 LYS G CB  1 
ATOM   7805  C  CG  . LYS D  1 137 ? -62.280  -25.136 53.226  1.00 39.12  ? 136 LYS G CG  1 
ATOM   7806  C  CD  . LYS D  1 137 ? -61.029  -24.563 53.847  1.00 49.91  ? 136 LYS G CD  1 
ATOM   7807  C  CE  . LYS D  1 137 ? -61.242  -24.008 55.240  1.00 56.27  ? 136 LYS G CE  1 
ATOM   7808  N  NZ  . LYS D  1 137 ? -60.351  -22.852 55.519  1.00 62.38  ? 136 LYS G NZ  1 
ATOM   7809  N  N   . THR D  1 138 ? -65.250  -28.178 55.014  1.00 25.79  ? 137 THR G N   1 
ATOM   7810  C  CA  . THR D  1 138 ? -65.575  -29.346 55.819  1.00 26.86  ? 137 THR G CA  1 
ATOM   7811  C  C   . THR D  1 138 ? -67.064  -29.450 56.152  1.00 25.21  ? 137 THR G C   1 
ATOM   7812  O  O   . THR D  1 138 ? -67.487  -30.426 56.783  1.00 25.25  ? 137 THR G O   1 
ATOM   7813  C  CB  . THR D  1 138 ? -64.790  -29.321 57.138  1.00 27.50  ? 137 THR G CB  1 
ATOM   7814  O  OG1 . THR D  1 138 ? -65.254  -28.218 57.922  1.00 26.83  ? 137 THR G OG1 1 
ATOM   7815  C  CG2 . THR D  1 138 ? -63.295  -29.207 56.921  1.00 29.84  ? 137 THR G CG2 1 
ATOM   7816  N  N   . GLY D  1 139 ? -67.860  -28.428 55.816  1.00 24.77  ? 138 GLY G N   1 
ATOM   7817  C  CA  . GLY D  1 139 ? -69.281  -28.388 56.246  1.00 22.08  ? 138 GLY G CA  1 
ATOM   7818  C  C   . GLY D  1 139 ? -69.468  -28.176 57.747  1.00 21.23  ? 138 GLY G C   1 
ATOM   7819  O  O   . GLY D  1 139 ? -70.535  -28.432 58.266  1.00 21.44  ? 138 GLY G O   1 
ATOM   7820  N  N   . ASN D  1 140 ? -68.446  -27.664 58.438  1.00 21.49  ? 139 ASN G N   1 
ATOM   7821  C  CA  . ASN D  1 140 ? -68.459  -27.421 59.873  1.00 22.56  ? 139 ASN G CA  1 
ATOM   7822  C  C   . ASN D  1 140 ? -68.709  -28.735 60.629  1.00 21.79  ? 139 ASN G C   1 
ATOM   7823  O  O   . ASN D  1 140 ? -69.297  -28.715 61.718  1.00 22.54  ? 139 ASN G O   1 
ATOM   7824  C  CB  . ASN D  1 140 ? -69.482  -26.328 60.255  1.00 23.37  ? 139 ASN G CB  1 
ATOM   7825  C  CG  . ASN D  1 140 ? -69.023  -24.952 59.821  1.00 24.27  ? 139 ASN G CG  1 
ATOM   7826  O  OD1 . ASN D  1 140 ? -68.120  -24.399 60.426  1.00 26.04  ? 139 ASN G OD1 1 
ATOM   7827  N  ND2 . ASN D  1 140 ? -69.621  -24.387 58.779  1.00 24.23  ? 139 ASN G ND2 1 
ATOM   7828  N  N   . ALA D  1 141 ? -68.256  -29.876 60.080  1.00 20.54  ? 140 ALA G N   1 
ATOM   7829  C  CA  . ALA D  1 141 ? -68.545  -31.207 60.676  1.00 21.25  ? 140 ALA G CA  1 
ATOM   7830  C  C   . ALA D  1 141 ? -67.692  -31.487 61.925  1.00 20.65  ? 140 ALA G C   1 
ATOM   7831  O  O   . ALA D  1 141 ? -67.918  -32.456 62.608  1.00 21.31  ? 140 ALA G O   1 
ATOM   7832  C  CB  . ALA D  1 141 ? -68.318  -32.299 59.662  1.00 20.89  ? 140 ALA G CB  1 
ATOM   7833  N  N   . GLY D  1 142 ? -66.657  -30.691 62.157  1.00 23.11  ? 141 GLY G N   1 
ATOM   7834  C  CA  . GLY D  1 142 ? -65.902  -30.771 63.390  1.00 25.22  ? 141 GLY G CA  1 
ATOM   7835  C  C   . GLY D  1 142 ? -64.943  -31.949 63.360  1.00 25.53  ? 141 GLY G C   1 
ATOM   7836  O  O   . GLY D  1 142 ? -64.510  -32.402 62.292  1.00 22.47  ? 141 GLY G O   1 
ATOM   7837  N  N   . SER D  1 143 ? -64.604  -32.445 64.546  1.00 24.19  ? 142 SER G N   1 
ATOM   7838  C  CA  . SER D  1 143 ? -63.459  -33.339 64.699  1.00 26.00  ? 142 SER G CA  1 
ATOM   7839  C  C   . SER D  1 143 ? -63.786  -34.721 64.107  1.00 22.30  ? 142 SER G C   1 
ATOM   7840  O  O   . SER D  1 143 ? -64.944  -35.095 63.872  1.00 20.84  ? 142 SER G O   1 
ATOM   7841  C  CB  . SER D  1 143 ? -63.041  -33.387 66.153  1.00 29.88  ? 142 SER G CB  1 
ATOM   7842  O  OG  . SER D  1 143 ? -63.948  -34.179 66.868  1.00 37.74  ? 142 SER G OG  1 
ATOM   7843  N  N   . ARG D  1 144 ? -62.732  -35.465 63.796  1.00 23.38  ? 143 ARG G N   1 
ATOM   7844  C  CA  . ARG D  1 144 ? -62.824  -36.762 63.182  1.00 22.77  ? 143 ARG G CA  1 
ATOM   7845  C  C   . ARG D  1 144 ? -62.927  -37.801 64.296  1.00 23.12  ? 143 ARG G C   1 
ATOM   7846  O  O   . ARG D  1 144 ? -61.965  -38.012 65.004  1.00 26.42  ? 143 ARG G O   1 
ATOM   7847  C  CB  . ARG D  1 144 ? -61.601  -36.950 62.279  1.00 22.80  ? 143 ARG G CB  1 
ATOM   7848  C  CG  . ARG D  1 144 ? -61.396  -35.805 61.290  1.00 24.27  ? 143 ARG G CG  1 
ATOM   7849  C  CD  . ARG D  1 144 ? -60.100  -35.859 60.524  1.00 23.61  ? 143 ARG G CD  1 
ATOM   7850  N  NE  . ARG D  1 144 ? -59.946  -34.657 59.726  1.00 25.38  ? 143 ARG G NE  1 
ATOM   7851  C  CZ  . ARG D  1 144 ? -59.221  -34.554 58.615  1.00 25.85  ? 143 ARG G CZ  1 
ATOM   7852  N  NH1 . ARG D  1 144 ? -59.273  -33.428 57.915  1.00 22.68  ? 143 ARG G NH1 1 
ATOM   7853  N  NH2 . ARG D  1 144 ? -58.488  -35.576 58.197  1.00 22.00  ? 143 ARG G NH2 1 
ATOM   7854  N  N   . LEU D  1 145 ? -64.078  -38.458 64.441  1.00 22.59  ? 144 LEU G N   1 
ATOM   7855  C  CA  . LEU D  1 145 ? -64.290  -39.398 65.555  1.00 22.37  ? 144 LEU G CA  1 
ATOM   7856  C  C   . LEU D  1 145 ? -63.654  -40.762 65.250  1.00 23.95  ? 144 LEU G C   1 
ATOM   7857  O  O   . LEU D  1 145 ? -63.213  -41.461 66.161  1.00 21.52  ? 144 LEU G O   1 
ATOM   7858  C  CB  . LEU D  1 145 ? -65.782  -39.574 65.841  1.00 25.10  ? 144 LEU G CB  1 
ATOM   7859  C  CG  . LEU D  1 145 ? -66.540  -38.314 66.279  1.00 25.87  ? 144 LEU G CG  1 
ATOM   7860  C  CD1 . LEU D  1 145 ? -67.968  -38.666 66.658  1.00 28.68  ? 144 LEU G CD1 1 
ATOM   7861  C  CD2 . LEU D  1 145 ? -65.844  -37.623 67.434  1.00 27.91  ? 144 LEU G CD2 1 
ATOM   7862  N  N   . ALA D  1 146 ? -63.719  -41.182 63.982  1.00 22.33  ? 145 ALA G N   1 
ATOM   7863  C  CA  . ALA D  1 146 ? -63.230  -42.477 63.557  1.00 23.20  ? 145 ALA G CA  1 
ATOM   7864  C  C   . ALA D  1 146 ? -62.981  -42.435 62.048  1.00 23.64  ? 145 ALA G C   1 
ATOM   7865  O  O   . ALA D  1 146 ? -63.561  -41.600 61.334  1.00 22.04  ? 145 ALA G O   1 
ATOM   7866  C  CB  . ALA D  1 146 ? -64.202  -43.580 63.930  1.00 23.33  ? 145 ALA G CB  1 
ATOM   7867  N  N   . CYS D  1 147 ? -62.086  -43.311 61.590  1.00 21.23  ? 146 CYS G N   1 
ATOM   7868  C  CA  . CYS D  1 147 ? -61.717  -43.375 60.219  1.00 23.21  ? 146 CYS G CA  1 
ATOM   7869  C  C   . CYS D  1 147 ? -61.103  -44.750 59.910  1.00 23.45  ? 146 CYS G C   1 
ATOM   7870  O  O   . CYS D  1 147 ? -60.761  -45.533 60.803  1.00 19.76  ? 146 CYS G O   1 
ATOM   7871  C  CB  . CYS D  1 147 ? -60.751  -42.258 59.853  1.00 25.34  ? 146 CYS G CB  1 
ATOM   7872  S  SG  . CYS D  1 147 ? -59.172  -42.314 60.744  1.00 29.39  ? 146 CYS G SG  1 
ATOM   7873  N  N   . GLY D  1 148 ? -60.975  -45.024 58.620  1.00 21.87  ? 147 GLY G N   1 
ATOM   7874  C  CA  . GLY D  1 148 ? -60.274  -46.212 58.163  1.00 23.56  ? 147 GLY G CA  1 
ATOM   7875  C  C   . GLY D  1 148 ? -59.949  -46.071 56.699  1.00 23.24  ? 147 GLY G C   1 
ATOM   7876  O  O   . GLY D  1 148 ? -60.551  -45.229 56.010  1.00 21.97  ? 147 GLY G O   1 
ATOM   7877  N  N   . VAL D  1 149 ? -59.005  -46.887 56.235  1.00 20.95  ? 148 VAL G N   1 
ATOM   7878  C  CA  . VAL D  1 149 ? -58.632  -46.898 54.838  1.00 21.20  ? 148 VAL G CA  1 
ATOM   7879  C  C   . VAL D  1 149 ? -59.595  -47.818 54.095  1.00 20.75  ? 148 VAL G C   1 
ATOM   7880  O  O   . VAL D  1 149 ? -59.941  -48.909 54.562  1.00 23.31  ? 148 VAL G O   1 
ATOM   7881  C  CB  . VAL D  1 149 ? -57.158  -47.319 54.653  1.00 22.84  ? 148 VAL G CB  1 
ATOM   7882  C  CG1 . VAL D  1 149 ? -56.726  -47.238 53.203  1.00 21.80  ? 148 VAL G CG1 1 
ATOM   7883  C  CG2 . VAL D  1 149 ? -56.234  -46.488 55.513  1.00 23.51  ? 148 VAL G CG2 1 
ATOM   7884  N  N   . ILE D  1 150 ? -60.025  -47.366 52.919  1.00 19.53  ? 149 ILE G N   1 
ATOM   7885  C  CA  . ILE D  1 150 ? -60.971  -48.094 52.137  1.00 21.20  ? 149 ILE G CA  1 
ATOM   7886  C  C   . ILE D  1 150 ? -60.196  -49.144 51.330  1.00 22.33  ? 149 ILE G C   1 
ATOM   7887  O  O   . ILE D  1 150 ? -59.343  -48.802 50.508  1.00 21.07  ? 149 ILE G O   1 
ATOM   7888  C  CB  . ILE D  1 150 ? -61.781  -47.138 51.243  1.00 22.18  ? 149 ILE G CB  1 
ATOM   7889  C  CG1 . ILE D  1 150 ? -62.540  -46.103 52.085  1.00 22.40  ? 149 ILE G CG1 1 
ATOM   7890  C  CG2 . ILE D  1 150 ? -62.715  -47.908 50.330  1.00 23.78  ? 149 ILE G CG2 1 
ATOM   7891  C  CD1 . ILE D  1 150 ? -63.077  -44.940 51.272  1.00 24.23  ? 149 ILE G CD1 1 
ATOM   7892  N  N   . GLY D  1 151 ? -60.522  -50.412 51.571  1.00 21.58  ? 150 GLY G N   1 
ATOM   7893  C  CA  . GLY D  1 151 ? -59.789  -51.523 51.013  1.00 23.31  ? 150 GLY G CA  1 
ATOM   7894  C  C   . GLY D  1 151 ? -60.610  -52.354 50.049  1.00 22.67  ? 150 GLY G C   1 
ATOM   7895  O  O   . GLY D  1 151 ? -61.827  -52.397 50.120  1.00 22.73  ? 150 GLY G O   1 
ATOM   7896  N  N   . ILE D  1 152 ? -59.911  -53.080 49.171  1.00 22.61  ? 151 ILE G N   1 
ATOM   7897  C  CA  . ILE D  1 152 ? -60.553  -54.002 48.231  1.00 23.32  ? 151 ILE G CA  1 
ATOM   7898  C  C   . ILE D  1 152 ? -61.129  -55.173 49.019  1.00 25.02  ? 151 ILE G C   1 
ATOM   7899  O  O   . ILE D  1 152 ? -60.427  -55.735 49.837  1.00 25.74  ? 151 ILE G O   1 
ATOM   7900  C  CB  . ILE D  1 152 ? -59.559  -54.467 47.153  1.00 23.27  ? 151 ILE G CB  1 
ATOM   7901  C  CG1 . ILE D  1 152 ? -59.060  -53.273 46.350  1.00 23.76  ? 151 ILE G CG1 1 
ATOM   7902  C  CG2 . ILE D  1 152 ? -60.155  -55.583 46.292  1.00 24.37  ? 151 ILE G CG2 1 
ATOM   7903  C  CD1 . ILE D  1 152 ? -57.834  -53.526 45.529  1.00 25.16  ? 151 ILE G CD1 1 
ATOM   7904  N  N   . ALA D  1 153 ? -62.406  -55.510 48.776  1.00 25.52  ? 152 ALA G N   1 
ATOM   7905  C  CA  . ALA D  1 153 ? -63.084  -56.612 49.465  1.00 30.00  ? 152 ALA G CA  1 
ATOM   7906  C  C   . ALA D  1 153 ? -63.287  -57.777 48.480  1.00 32.38  ? 152 ALA G C   1 
ATOM   7907  O  O   . ALA D  1 153 ? -63.226  -57.583 47.268  1.00 36.91  ? 152 ALA G O   1 
ATOM   7908  C  CB  . ALA D  1 153 ? -64.400  -56.133 50.023  1.00 28.28  ? 152 ALA G CB  1 
ATOM   7909  N  N   . GLN D  1 154 ? -63.631  -58.957 48.987  1.00 44.07  ? 153 GLN G N   1 
ATOM   7910  C  CA  . GLN D  1 154 ? -63.802  -60.126 48.087  1.00 54.72  ? 153 GLN G CA  1 
ATOM   7911  C  C   . GLN D  1 154 ? -64.942  -59.893 47.082  1.00 64.10  ? 153 GLN G C   1 
ATOM   7912  O  O   . GLN D  1 154 ? -66.103  -59.780 47.462  1.00 67.98  ? 153 GLN G O   1 
ATOM   7913  C  CB  . GLN D  1 154 ? -64.023  -61.418 48.856  1.00 58.05  ? 153 GLN G CB  1 
ATOM   7914  C  CG  . GLN D  1 154 ? -63.837  -62.641 47.969  1.00 61.43  ? 153 GLN G CG  1 
ATOM   7915  C  CD  . GLN D  1 154 ? -63.341  -63.820 48.765  1.00 63.67  ? 153 GLN G CD  1 
ATOM   7916  O  OE1 . GLN D  1 154 ? -62.458  -64.554 48.333  1.00 67.43  ? 153 GLN G OE1 1 
ATOM   7917  N  NE2 . GLN D  1 154 ? -63.894  -63.987 49.955  1.00 61.09  ? 153 GLN G NE2 1 
ATOM   7918  N  N   . GLY D  1 155 ? -64.561  -59.924 45.797  1.00 68.87  ? 154 GLY G N   1 
ATOM   7919  C  CA  . GLY D  1 155 ? -65.175  -59.226 44.661  1.00 72.96  ? 154 GLY G CA  1 
ATOM   7920  C  C   . GLY D  1 155 ? -64.143  -59.091 43.543  1.00 77.56  ? 154 GLY G C   1 
ATOM   7921  O  O   . GLY D  1 155 ? -62.985  -59.473 43.732  1.00 75.60  ? 154 GLY G O   1 
ATOM   7922  N  N   . ALA D  1 156 ? -64.541  -58.540 42.388  1.00 75.71  ? 155 ALA G N   1 
ATOM   7923  C  CA  . ALA D  1 156 ? -63.758  -58.642 41.138  1.00 74.88  ? 155 ALA G CA  1 
ATOM   7924  C  C   . ALA D  1 156 ? -63.161  -57.288 40.708  1.00 76.64  ? 155 ALA G C   1 
ATOM   7925  O  O   . ALA D  1 156 ? -63.151  -56.323 41.474  1.00 70.15  ? 155 ALA G O   1 
ATOM   7926  C  CB  . ALA D  1 156 ? -64.654  -59.210 40.060  1.00 74.67  ? 155 ALA G CB  1 
ATOM   7927  N  N   . ALA D  1 157 ? -62.585  -57.285 39.493  1.00 76.02  ? 156 ALA G N   1 
ATOM   7928  C  CA  . ALA D  1 157 ? -62.427  -56.120 38.578  1.00 72.49  ? 156 ALA G CA  1 
ATOM   7929  C  C   . ALA D  1 157 ? -62.167  -54.817 39.341  1.00 71.20  ? 156 ALA G C   1 
ATOM   7930  O  O   . ALA D  1 157 ? -62.305  -53.732 38.766  1.00 68.16  ? 156 ALA G O   1 
ATOM   7931  C  CB  . ALA D  1 157 ? -63.651  -55.999 37.695  1.00 64.03  ? 156 ALA G CB  1 
ATOM   7932  N  N   . GLY D  1 167 ? -57.917  -54.165 40.398  1.00 60.59  ? 166 GLY G N   1 
ATOM   7933  C  CA  . GLY D  1 167 ? -57.526  -53.416 41.630  1.00 56.47  ? 166 GLY G CA  1 
ATOM   7934  C  C   . GLY D  1 167 ? -58.569  -52.368 41.991  1.00 59.42  ? 166 GLY G C   1 
ATOM   7935  O  O   . GLY D  1 167 ? -59.701  -52.675 42.399  1.00 46.90  ? 166 GLY G O   1 
ATOM   7936  N  N   . GLY D  1 168 ? -58.200  -51.104 41.804  1.00 50.72  ? 167 GLY G N   1 
ATOM   7937  C  CA  . GLY D  1 168 ? -59.009  -50.045 42.261  1.00 44.60  ? 167 GLY G CA  1 
ATOM   7938  C  C   . GLY D  1 168 ? -58.233  -48.758 42.422  1.00 38.00  ? 167 GLY G C   1 
ATOM   7939  O  O   . GLY D  1 168 ? -58.791  -47.711 42.155  1.00 34.97  ? 167 GLY G O   1 
ATOM   7940  N  N   . GLY D  1 169 ? -56.961  -48.845 42.843  1.00 36.68  ? 168 GLY G N   1 
ATOM   7941  C  CA  . GLY D  1 169 ? -56.209  -47.701 43.286  1.00 34.60  ? 168 GLY G CA  1 
ATOM   7942  C  C   . GLY D  1 169 ? -54.888  -47.481 42.573  1.00 37.19  ? 168 GLY G C   1 
ATOM   7943  O  O   . GLY D  1 169 ? -54.217  -48.446 42.126  1.00 30.97  ? 168 GLY G O   1 
ATOM   7944  N  N   . SER D  1 170 ? -54.490  -46.195 42.552  1.00 42.80  ? 169 SER G N   1 
ATOM   7945  C  CA  . SER D  1 170 ? -53.289  -45.682 41.890  1.00 53.06  ? 169 SER G CA  1 
ATOM   7946  C  C   . SER D  1 170 ? -52.659  -44.561 42.731  1.00 49.90  ? 169 SER G C   1 
ATOM   7947  O  O   . SER D  1 170 ? -53.433  -43.775 43.293  1.00 46.92  ? 169 SER G O   1 
ATOM   7948  C  CB  . SER D  1 170 ? -53.642  -45.171 40.510  1.00 66.17  ? 169 SER G CB  1 
ATOM   7949  O  OG  . SER D  1 170 ? -54.712  -44.229 40.576  1.00 79.91  ? 169 SER G OG  1 
ATOM   7950  N  N   . ALA D  1 171 ? -51.303  -44.466 42.746  1.00 40.62  ? 170 ALA G N   1 
ATOM   7951  C  CA  . ALA D  1 171 ? -50.504  -43.415 43.494  1.00 40.05  ? 170 ALA G CA  1 
ATOM   7952  C  C   . ALA D  1 171 ? -48.976  -43.486 43.234  1.00 39.78  ? 170 ALA G C   1 
ATOM   7953  O  O   . ALA D  1 171 ? -48.455  -44.473 42.749  1.00 43.54  ? 170 ALA G O   1 
ATOM   7954  C  CB  . ALA D  1 171 ? -50.755  -43.577 44.970  1.00 40.28  ? 170 ALA G CB  1 
ATOM   7955  N  N   . THR D  1 172 ? -48.256  -42.440 43.665  1.00 36.61  ? 171 THR G N   1 
ATOM   7956  C  CA  . THR D  1 172 ? -46.785  -42.310 43.608  1.00 37.05  ? 171 THR G CA  1 
ATOM   7957  C  C   . THR D  1 172 ? -46.158  -42.641 44.974  1.00 32.62  ? 171 THR G C   1 
ATOM   7958  O  O   . THR D  1 172 ? -44.978  -43.061 45.060  1.00 29.91  ? 171 THR G O   1 
ATOM   7959  C  CB  . THR D  1 172 ? -46.408  -40.895 43.142  1.00 42.33  ? 171 THR G CB  1 
ATOM   7960  O  OG1 . THR D  1 172 ? -46.420  -40.961 41.714  1.00 54.56  ? 171 THR G OG1 1 
ATOM   7961  C  CG2 . THR D  1 172 ? -45.064  -40.400 43.627  1.00 46.27  ? 171 THR G CG2 1 
ATOM   7962  N  N   . LYS D  1 173 ? -46.929  -42.403 46.035  1.00 28.61  ? 172 LYS G N   1 
ATOM   7963  C  CA  . LYS D  1 173 ? -46.555  -42.698 47.403  1.00 31.13  ? 172 LYS G CA  1 
ATOM   7964  C  C   . LYS D  1 173 ? -47.738  -43.366 48.096  1.00 28.80  ? 172 LYS G C   1 
ATOM   7965  O  O   . LYS D  1 173 ? -48.894  -42.983 47.875  1.00 25.44  ? 172 LYS G O   1 
ATOM   7966  C  CB  . LYS D  1 173 ? -46.194  -41.439 48.191  1.00 36.08  ? 172 LYS G CB  1 
ATOM   7967  C  CG  . LYS D  1 173 ? -44.883  -40.780 47.809  1.00 45.53  ? 172 LYS G CG  1 
ATOM   7968  C  CD  . LYS D  1 173 ? -44.165  -40.187 48.990  1.00 52.56  ? 172 LYS G CD  1 
ATOM   7969  C  CE  . LYS D  1 173 ? -43.523  -41.245 49.863  1.00 61.31  ? 172 LYS G CE  1 
ATOM   7970  N  NZ  . LYS D  1 173 ? -43.279  -40.734 51.231  1.00 66.84  ? 172 LYS G NZ  1 
ATOM   7971  N  N   . ALA D  1 174 ? -47.423  -44.352 48.932  1.00 23.32  ? 173 ALA G N   1 
ATOM   7972  C  CA  . ALA D  1 174 ? -48.394  -45.048 49.733  1.00 22.45  ? 173 ALA G CA  1 
ATOM   7973  C  C   . ALA D  1 174 ? -47.796  -45.264 51.124  1.00 21.78  ? 173 ALA G C   1 
ATOM   7974  O  O   . ALA D  1 174 ? -46.594  -45.079 51.345  1.00 21.66  ? 173 ALA G O   1 
ATOM   7975  C  CB  . ALA D  1 174 ? -48.810  -46.343 49.091  1.00 21.55  ? 173 ALA G CB  1 
ATOM   7976  N  N   . VAL D  1 175 ? -48.668  -45.601 52.063  1.00 23.40  ? 174 VAL G N   1 
ATOM   7977  C  CA  . VAL D  1 175 ? -48.312  -45.788 53.439  1.00 22.81  ? 174 VAL G CA  1 
ATOM   7978  C  C   . VAL D  1 175 ? -49.271  -46.814 54.028  1.00 23.45  ? 174 VAL G C   1 
ATOM   7979  O  O   . VAL D  1 175 ? -50.440  -46.965 53.606  1.00 24.43  ? 174 VAL G O   1 
ATOM   7980  C  CB  . VAL D  1 175 ? -48.327  -44.468 54.225  1.00 23.59  ? 174 VAL G CB  1 
ATOM   7981  C  CG1 . VAL D  1 175 ? -49.733  -43.922 54.400  1.00 24.51  ? 174 VAL G CG1 1 
ATOM   7982  C  CG2 . VAL D  1 175 ? -47.655  -44.619 55.572  1.00 25.39  ? 174 VAL G CG2 1 
ATOM   7983  N  N   . CYS D  1 176 ? -48.759  -47.525 55.020  1.00 23.33  ? 175 CYS G N   1 
ATOM   7984  C  CA  . CYS D  1 176 ? -49.483  -48.558 55.666  1.00 23.91  ? 175 CYS G CA  1 
ATOM   7985  C  C   . CYS D  1 176 ? -49.118  -48.514 57.153  1.00 23.66  ? 175 CYS G C   1 
ATOM   7986  O  O   . CYS D  1 176 ? -47.929  -48.517 57.500  1.00 23.59  ? 175 CYS G O   1 
ATOM   7987  C  CB  . CYS D  1 176 ? -49.160  -49.913 55.042  1.00 22.40  ? 175 CYS G CB  1 
ATOM   7988  S  SG  . CYS D  1 176 ? -50.047  -51.281 55.831  1.00 27.05  ? 175 CYS G SG  1 
ATOM   7989  N  N   . VAL D  1 177 ? -50.138  -48.418 58.009  1.00 22.35  ? 176 VAL G N   1 
ATOM   7990  C  CA  . VAL D  1 177 ? -49.998  -48.556 59.455  1.00 22.36  ? 176 VAL G CA  1 
ATOM   7991  C  C   . VAL D  1 177 ? -50.346  -50.004 59.833  1.00 23.16  ? 176 VAL G C   1 
ATOM   7992  O  O   . VAL D  1 177 ? -51.473  -50.439 59.678  1.00 23.17  ? 176 VAL G O   1 
ATOM   7993  C  CB  . VAL D  1 177 ? -50.886  -47.543 60.204  1.00 23.33  ? 176 VAL G CB  1 
ATOM   7994  C  CG1 . VAL D  1 177 ? -50.779  -47.688 61.713  1.00 24.58  ? 176 VAL G CG1 1 
ATOM   7995  C  CG2 . VAL D  1 177 ? -50.563  -46.129 59.790  1.00 23.54  ? 176 VAL G CG2 1 
ATOM   7996  N  N   . LEU D  1 178 ? -49.376  -50.719 60.400  1.00 23.34  ? 177 LEU G N   1 
ATOM   7997  C  CA  . LEU D  1 178 ? -49.530  -52.113 60.838  1.00 25.89  ? 177 LEU G CA  1 
ATOM   7998  C  C   . LEU D  1 178 ? -49.915  -52.152 62.321  1.00 25.20  ? 177 LEU G C   1 
ATOM   7999  O  O   . LEU D  1 178 ? -49.258  -51.547 63.152  1.00 24.97  ? 177 LEU G O   1 
ATOM   8000  C  CB  . LEU D  1 178 ? -48.208  -52.863 60.630  1.00 29.15  ? 177 LEU G CB  1 
ATOM   8001  C  CG  . LEU D  1 178 ? -47.700  -52.969 59.192  1.00 32.64  ? 177 LEU G CG  1 
ATOM   8002  C  CD1 . LEU D  1 178 ? -46.239  -53.396 59.170  1.00 37.71  ? 177 LEU G CD1 1 
ATOM   8003  C  CD2 . LEU D  1 178 ? -48.518  -53.967 58.423  1.00 33.12  ? 177 LEU G CD2 1 
ATOM   8004  N  N   . LYS D  1 179 ? -50.987  -52.876 62.618  1.00 25.63  ? 178 LYS G N   1 
ATOM   8005  C  CA  . LYS D  1 179 ? -51.465  -53.094 63.955  1.00 29.94  ? 178 LYS G CA  1 
ATOM   8006  C  C   . LYS D  1 179 ? -51.997  -54.520 64.010  1.00 26.95  ? 178 LYS G C   1 
ATOM   8007  O  O   . LYS D  1 179 ? -52.374  -55.077 62.982  1.00 23.20  ? 178 LYS G O   1 
ATOM   8008  C  CB  . LYS D  1 179 ? -52.618  -52.142 64.310  1.00 32.85  ? 178 LYS G CB  1 
ATOM   8009  C  CG  . LYS D  1 179 ? -52.232  -50.676 64.397  1.00 39.73  ? 178 LYS G CG  1 
ATOM   8010  C  CD  . LYS D  1 179 ? -51.276  -50.389 65.542  1.00 49.01  ? 178 LYS G CD  1 
ATOM   8011  C  CE  . LYS D  1 179 ? -50.725  -48.977 65.550  1.00 56.77  ? 178 LYS G CE  1 
ATOM   8012  N  NZ  . LYS D  1 179 ? -51.804  -47.972 65.738  1.00 62.93  ? 178 LYS G NZ  1 
ATOM   8013  N  N   . GLY D  1 180 ? -52.095  -55.055 65.226  1.00 27.41  ? 179 GLY G N   1 
ATOM   8014  C  CA  . GLY D  1 180 ? -52.666  -56.380 65.456  1.00 29.83  ? 179 GLY G CA  1 
ATOM   8015  C  C   . GLY D  1 180 ? -53.141  -56.513 66.892  1.00 32.39  ? 179 GLY G C   1 
ATOM   8016  O  O   . GLY D  1 180 ? -53.221  -55.524 67.615  1.00 30.66  ? 179 GLY G O   1 
ATOM   8017  N  N   . ASP D  1 181 ? -53.422  -57.749 67.303  1.00 37.21  ? 180 ASP G N   1 
ATOM   8018  C  CA  . ASP D  1 181 ? -53.931  -58.041 68.634  1.00 40.43  ? 180 ASP G CA  1 
ATOM   8019  C  C   . ASP D  1 181 ? -52.813  -57.946 69.673  1.00 43.00  ? 180 ASP G C   1 
ATOM   8020  O  O   . ASP D  1 181 ? -53.096  -57.762 70.846  1.00 47.13  ? 180 ASP G O   1 
ATOM   8021  C  CB  . ASP D  1 181 ? -54.547  -59.437 68.699  1.00 47.33  ? 180 ASP G CB  1 
ATOM   8022  C  CG  . ASP D  1 181 ? -55.937  -59.516 68.096  1.00 56.16  ? 180 ASP G CG  1 
ATOM   8023  O  OD1 . ASP D  1 181 ? -56.557  -58.439 67.859  1.00 56.42  ? 180 ASP G OD1 1 
ATOM   8024  O  OD2 . ASP D  1 181 ? -56.397  -60.657 67.874  1.00 70.22  ? 180 ASP G OD2 1 
ATOM   8025  N  N   . GLY D  1 182 ? -51.559  -58.091 69.233  1.00 38.78  ? 181 GLY G N   1 
ATOM   8026  C  CA  . GLY D  1 182 ? -50.412  -58.080 70.108  1.00 34.63  ? 181 GLY G CA  1 
ATOM   8027  C  C   . GLY D  1 182 ? -49.685  -56.749 70.078  1.00 31.51  ? 181 GLY G C   1 
ATOM   8028  O  O   . GLY D  1 182 ? -50.264  -55.720 69.742  1.00 31.30  ? 181 GLY G O   1 
ATOM   8029  N  N   . PRO D  1 183 ? -48.381  -56.738 70.436  1.00 29.83  ? 182 PRO G N   1 
ATOM   8030  C  CA  . PRO D  1 183 ? -47.592  -55.508 70.470  1.00 29.70  ? 182 PRO G CA  1 
ATOM   8031  C  C   . PRO D  1 183 ? -46.937  -55.069 69.165  1.00 28.07  ? 182 PRO G C   1 
ATOM   8032  O  O   . PRO D  1 183 ? -46.264  -54.049 69.150  1.00 28.53  ? 182 PRO G O   1 
ATOM   8033  C  CB  . PRO D  1 183 ? -46.483  -55.889 71.471  1.00 31.67  ? 182 PRO G CB  1 
ATOM   8034  C  CG  . PRO D  1 183 ? -46.234  -57.357 71.177  1.00 31.39  ? 182 PRO G CG  1 
ATOM   8035  C  CD  . PRO D  1 183 ? -47.609  -57.920 70.862  1.00 32.00  ? 182 PRO G CD  1 
ATOM   8036  N  N   . VAL D  1 184 ? -47.126  -55.827 68.076  1.00 28.19  ? 183 VAL G N   1 
ATOM   8037  C  CA  . VAL D  1 184 ? -46.464  -55.494 66.823  1.00 29.69  ? 183 VAL G CA  1 
ATOM   8038  C  C   . VAL D  1 184 ? -47.138  -54.247 66.228  1.00 29.26  ? 183 VAL G C   1 
ATOM   8039  O  O   . VAL D  1 184 ? -48.333  -54.216 66.056  1.00 29.43  ? 183 VAL G O   1 
ATOM   8040  C  CB  . VAL D  1 184 ? -46.471  -56.669 65.827  1.00 31.55  ? 183 VAL G CB  1 
ATOM   8041  C  CG1 . VAL D  1 184 ? -45.886  -56.261 64.491  1.00 32.60  ? 183 VAL G CG1 1 
ATOM   8042  C  CG2 . VAL D  1 184 ? -45.713  -57.872 66.361  1.00 34.70  ? 183 VAL G CG2 1 
ATOM   8043  N  N   . GLN D  1 185 ? -46.349  -53.224 65.909  1.00 29.35  ? 184 GLN G N   1 
ATOM   8044  C  CA  . GLN D  1 185 ? -46.886  -52.087 65.220  1.00 33.52  ? 184 GLN G CA  1 
ATOM   8045  C  C   . GLN D  1 185 ? -45.798  -51.430 64.382  1.00 30.32  ? 184 GLN G C   1 
ATOM   8046  O  O   . GLN D  1 185 ? -44.618  -51.500 64.678  1.00 31.14  ? 184 GLN G O   1 
ATOM   8047  C  CB  . GLN D  1 185 ? -47.555  -51.114 66.197  1.00 35.35  ? 184 GLN G CB  1 
ATOM   8048  C  CG  . GLN D  1 185 ? -46.658  -50.526 67.270  1.00 40.90  ? 184 GLN G CG  1 
ATOM   8049  C  CD  . GLN D  1 185 ? -47.414  -49.559 68.158  1.00 44.71  ? 184 GLN G CD  1 
ATOM   8050  O  OE1 . GLN D  1 185 ? -47.385  -49.654 69.384  1.00 46.63  ? 184 GLN G OE1 1 
ATOM   8051  N  NE2 . GLN D  1 185 ? -48.106  -48.610 67.548  1.00 46.85  ? 184 GLN G NE2 1 
ATOM   8052  N  N   . GLY D  1 186 ? -46.224  -50.756 63.324  1.00 29.32  ? 185 GLY G N   1 
ATOM   8053  C  CA  . GLY D  1 186 ? -45.282  -50.029 62.526  1.00 29.16  ? 185 GLY G CA  1 
ATOM   8054  C  C   . GLY D  1 186 ? -45.924  -49.196 61.439  1.00 27.95  ? 185 GLY G C   1 
ATOM   8055  O  O   . GLY D  1 186 ? -47.161  -49.194 61.256  1.00 27.45  ? 185 GLY G O   1 
ATOM   8056  N  N   . ILE D  1 187 ? -45.052  -48.470 60.741  1.00 26.03  ? 186 ILE G N   1 
ATOM   8057  C  CA  . ILE D  1 187 ? -45.399  -47.680 59.582  1.00 25.91  ? 186 ILE G CA  1 
ATOM   8058  C  C   . ILE D  1 187 ? -44.464  -48.078 58.446  1.00 25.26  ? 186 ILE G C   1 
ATOM   8059  O  O   . ILE D  1 187 ? -43.248  -48.021 58.598  1.00 23.62  ? 186 ILE G O   1 
ATOM   8060  C  CB  . ILE D  1 187 ? -45.301  -46.181 59.907  1.00 25.20  ? 186 ILE G CB  1 
ATOM   8061  C  CG1 . ILE D  1 187 ? -46.283  -45.789 61.015  1.00 27.90  ? 186 ILE G CG1 1 
ATOM   8062  C  CG2 . ILE D  1 187 ? -45.494  -45.345 58.645  1.00 24.96  ? 186 ILE G CG2 1 
ATOM   8063  C  CD1 . ILE D  1 187 ? -46.014  -44.423 61.621  1.00 27.83  ? 186 ILE G CD1 1 
ATOM   8064  N  N   . ILE D  1 188 ? -45.052  -48.490 57.327  1.00 24.02  ? 187 ILE G N   1 
ATOM   8065  C  CA  . ILE D  1 188 ? -44.323  -48.779 56.107  1.00 24.69  ? 187 ILE G CA  1 
ATOM   8066  C  C   . ILE D  1 188 ? -44.753  -47.797 54.996  1.00 24.47  ? 187 ILE G C   1 
ATOM   8067  O  O   . ILE D  1 188 ? -45.945  -47.600 54.748  1.00 23.89  ? 187 ILE G O   1 
ATOM   8068  C  CB  . ILE D  1 188 ? -44.546  -50.249 55.722  1.00 23.80  ? 187 ILE G CB  1 
ATOM   8069  C  CG1 . ILE D  1 188 ? -44.059  -51.209 56.814  1.00 24.22  ? 187 ILE G CG1 1 
ATOM   8070  C  CG2 . ILE D  1 188 ? -43.904  -50.558 54.392  1.00 23.44  ? 187 ILE G CG2 1 
ATOM   8071  C  CD1 . ILE D  1 188 ? -42.552  -51.158 57.041  1.00 25.98  ? 187 ILE G CD1 1 
ATOM   8072  N  N   . ASN D  1 189 ? -43.747  -47.180 54.377  1.00 20.70  ? 188 ASN G N   1 
ATOM   8073  C  CA  . ASN D  1 189 ? -43.822  -46.255 53.287  1.00 24.32  ? 188 ASN G CA  1 
ATOM   8074  C  C   . ASN D  1 189 ? -43.519  -46.999 51.991  1.00 26.13  ? 188 ASN G C   1 
ATOM   8075  O  O   . ASN D  1 189 ? -42.731  -47.966 51.966  1.00 24.42  ? 188 ASN G O   1 
ATOM   8076  C  CB  . ASN D  1 189 ? -42.855  -45.096 53.486  1.00 24.77  ? 188 ASN G CB  1 
ATOM   8077  C  CG  . ASN D  1 189 ? -43.117  -44.395 54.798  1.00 32.33  ? 188 ASN G CG  1 
ATOM   8078  O  OD1 . ASN D  1 189 ? -44.135  -43.724 54.945  1.00 29.44  ? 188 ASN G OD1 1 
ATOM   8079  N  ND2 . ASN D  1 189 ? -42.209  -44.550 55.752  1.00 32.98  ? 188 ASN G ND2 1 
ATOM   8080  N  N   . PHE D  1 190 ? -44.176  -46.559 50.919  1.00 24.10  ? 189 PHE G N   1 
ATOM   8081  C  CA  . PHE D  1 190 ? -43.920  -47.050 49.573  1.00 24.46  ? 189 PHE G CA  1 
ATOM   8082  C  C   . PHE D  1 190 ? -43.758  -45.845 48.656  1.00 24.15  ? 189 PHE G C   1 
ATOM   8083  O  O   . PHE D  1 190 ? -44.508  -44.852 48.770  1.00 25.24  ? 189 PHE G O   1 
ATOM   8084  C  CB  . PHE D  1 190 ? -45.069  -47.896 49.023  1.00 24.47  ? 189 PHE G CB  1 
ATOM   8085  C  CG  . PHE D  1 190 ? -45.511  -49.060 49.861  1.00 23.83  ? 189 PHE G CG  1 
ATOM   8086  C  CD1 . PHE D  1 190 ? -45.165  -50.360 49.501  1.00 26.35  ? 189 PHE G CD1 1 
ATOM   8087  C  CD2 . PHE D  1 190 ? -46.280  -48.869 50.996  1.00 24.52  ? 189 PHE G CD2 1 
ATOM   8088  C  CE1 . PHE D  1 190 ? -45.582  -51.444 50.263  1.00 26.82  ? 189 PHE G CE1 1 
ATOM   8089  C  CE2 . PHE D  1 190 ? -46.680  -49.954 51.761  1.00 25.34  ? 189 PHE G CE2 1 
ATOM   8090  C  CZ  . PHE D  1 190 ? -46.362  -51.236 51.377  1.00 25.90  ? 189 PHE G CZ  1 
ATOM   8091  N  N   . GLU D  1 191 ? -42.824  -45.938 47.720  1.00 24.38  ? 190 GLU G N   1 
ATOM   8092  C  CA  . GLU D  1 191 ? -42.636  -44.881 46.752  1.00 26.29  ? 190 GLU G CA  1 
ATOM   8093  C  C   . GLU D  1 191 ? -42.307  -45.497 45.399  1.00 26.72  ? 190 GLU G C   1 
ATOM   8094  O  O   . GLU D  1 191 ? -41.471  -46.395 45.299  1.00 25.06  ? 190 GLU G O   1 
ATOM   8095  C  CB  . GLU D  1 191 ? -41.550  -43.930 47.242  1.00 30.82  ? 190 GLU G CB  1 
ATOM   8096  C  CG  . GLU D  1 191 ? -41.276  -42.771 46.306  1.00 39.22  ? 190 GLU G CG  1 
ATOM   8097  C  CD  . GLU D  1 191 ? -40.283  -41.770 46.886  1.00 45.57  ? 190 GLU G CD  1 
ATOM   8098  O  OE1 . GLU D  1 191 ? -39.120  -41.804 46.463  1.00 54.50  ? 190 GLU G OE1 1 
ATOM   8099  O  OE2 . GLU D  1 191 ? -40.666  -40.997 47.794  1.00 51.95  ? 190 GLU G OE2 1 
ATOM   8100  N  N   . GLN D  1 192 ? -42.986  -45.002 44.362  1.00 24.19  ? 191 GLN G N   1 
ATOM   8101  C  CA  . GLN D  1 192 ? -42.782  -45.443 43.008  1.00 26.02  ? 191 GLN G CA  1 
ATOM   8102  C  C   . GLN D  1 192 ? -42.717  -44.181 42.143  1.00 32.09  ? 191 GLN G C   1 
ATOM   8103  O  O   . GLN D  1 192 ? -43.748  -43.571 41.868  1.00 32.68  ? 191 GLN G O   1 
ATOM   8104  C  CB  . GLN D  1 192 ? -43.902  -46.385 42.588  1.00 23.80  ? 191 GLN G CB  1 
ATOM   8105  C  CG  . GLN D  1 192 ? -43.643  -47.031 41.248  1.00 22.68  ? 191 GLN G CG  1 
ATOM   8106  C  CD  . GLN D  1 192 ? -44.755  -47.939 40.799  1.00 22.62  ? 191 GLN G CD  1 
ATOM   8107  O  OE1 . GLN D  1 192 ? -44.581  -48.855 39.976  1.00 26.50  ? 191 GLN G OE1 1 
ATOM   8108  N  NE2 . GLN D  1 192 ? -45.927  -47.697 41.341  1.00 20.44  ? 191 GLN G NE2 1 
ATOM   8109  N  N   . LYS D  1 193 ? -41.504  -43.795 41.753  1.00 34.00  ? 192 LYS G N   1 
ATOM   8110  C  CA  . LYS D  1 193 ? -41.280  -42.525 41.088  1.00 42.06  ? 192 LYS G CA  1 
ATOM   8111  C  C   . LYS D  1 193 ? -41.785  -42.597 39.643  1.00 37.30  ? 192 LYS G C   1 
ATOM   8112  O  O   . LYS D  1 193 ? -42.272  -41.625 39.127  1.00 39.00  ? 192 LYS G O   1 
ATOM   8113  C  CB  . LYS D  1 193 ? -39.805  -42.135 41.191  1.00 49.81  ? 192 LYS G CB  1 
ATOM   8114  C  CG  . LYS D  1 193 ? -39.475  -41.317 42.435  1.00 61.82  ? 192 LYS G CG  1 
ATOM   8115  C  CD  . LYS D  1 193 ? -37.989  -41.130 42.686  1.00 73.22  ? 192 LYS G CD  1 
ATOM   8116  C  CE  . LYS D  1 193 ? -37.201  -42.424 42.592  1.00 83.64  ? 192 LYS G CE  1 
ATOM   8117  N  NZ  . LYS D  1 193 ? -35.925  -42.364 43.347  1.00 89.88  ? 192 LYS G NZ  1 
ATOM   8118  N  N   . GLU D  1 194 ? -41.711  -43.764 39.002  1.00 33.62  ? 193 GLU G N   1 
ATOM   8119  C  CA  . GLU D  1 194 ? -42.381  -43.900 37.720  1.00 34.49  ? 193 GLU G CA  1 
ATOM   8120  C  C   . GLU D  1 194 ? -43.217  -45.171 37.718  1.00 30.90  ? 193 GLU G C   1 
ATOM   8121  O  O   . GLU D  1 194 ? -42.840  -46.183 38.304  1.00 31.03  ? 193 GLU G O   1 
ATOM   8122  C  CB  . GLU D  1 194 ? -41.422  -43.878 36.532  1.00 40.85  ? 193 GLU G CB  1 
ATOM   8123  C  CG  . GLU D  1 194 ? -40.139  -44.630 36.754  1.00 48.10  ? 193 GLU G CG  1 
ATOM   8124  C  CD  . GLU D  1 194 ? -38.963  -43.728 37.087  1.00 56.36  ? 193 GLU G CD  1 
ATOM   8125  O  OE1 . GLU D  1 194 ? -39.180  -42.511 37.288  1.00 55.09  ? 193 GLU G OE1 1 
ATOM   8126  O  OE2 . GLU D  1 194 ? -37.830  -44.247 37.116  1.00 72.45  ? 193 GLU G OE2 1 
ATOM   8127  N  N   . SER D  1 195 ? -44.357  -45.094 37.033  1.00 26.90  ? 194 SER G N   1 
ATOM   8128  C  CA  . SER D  1 195 ? -45.384  -46.130 37.106  1.00 28.48  ? 194 SER G CA  1 
ATOM   8129  C  C   . SER D  1 195 ? -44.853  -47.487 36.618  1.00 26.96  ? 194 SER G C   1 
ATOM   8130  O  O   . SER D  1 195 ? -45.451  -48.512 36.872  1.00 27.98  ? 194 SER G O   1 
ATOM   8131  C  CB  . SER D  1 195 ? -46.586  -45.695 36.318  1.00 29.06  ? 194 SER G CB  1 
ATOM   8132  O  OG  . SER D  1 195 ? -46.263  -45.585 34.937  1.00 30.05  ? 194 SER G OG  1 
ATOM   8133  N  N   . ASN D  1 196 ? -43.793  -47.471 35.799  1.00 27.50  ? 195 ASN G N   1 
ATOM   8134  C  CA  . ASN D  1 196 ? -43.240  -48.709 35.248  1.00 29.29  ? 195 ASN G CA  1 
ATOM   8135  C  C   . ASN D  1 196 ? -41.932  -49.053 35.965  1.00 31.42  ? 195 ASN G C   1 
ATOM   8136  O  O   . ASN D  1 196 ? -41.250  -49.967 35.579  1.00 33.95  ? 195 ASN G O   1 
ATOM   8137  C  CB  . ASN D  1 196 ? -43.052  -48.668 33.724  1.00 28.18  ? 195 ASN G CB  1 
ATOM   8138  C  CG  . ASN D  1 196 ? -42.029  -47.647 33.271  1.00 27.92  ? 195 ASN G CG  1 
ATOM   8139  O  OD1 . ASN D  1 196 ? -41.947  -46.557 33.830  1.00 29.72  ? 195 ASN G OD1 1 
ATOM   8140  N  ND2 . ASN D  1 196 ? -41.259  -47.989 32.253  1.00 26.73  ? 195 ASN G ND2 1 
ATOM   8141  N  N   . GLY D  1 197 ? -41.613  -48.311 37.019  1.00 30.42  ? 196 GLY G N   1 
ATOM   8142  C  CA  . GLY D  1 197 ? -40.388  -48.526 37.746  1.00 33.54  ? 196 GLY G CA  1 
ATOM   8143  C  C   . GLY D  1 197 ? -40.621  -49.334 39.022  1.00 30.34  ? 196 GLY G C   1 
ATOM   8144  O  O   . GLY D  1 197 ? -41.750  -49.679 39.365  1.00 26.64  ? 196 GLY G O   1 
ATOM   8145  N  N   . PRO D  1 198 ? -39.533  -49.639 39.758  1.00 31.59  ? 197 PRO G N   1 
ATOM   8146  C  CA  . PRO D  1 198 ? -39.623  -50.421 40.985  1.00 32.11  ? 197 PRO G CA  1 
ATOM   8147  C  C   . PRO D  1 198 ? -40.289  -49.603 42.102  1.00 27.85  ? 197 PRO G C   1 
ATOM   8148  O  O   . PRO D  1 198 ? -40.297  -48.367 42.048  1.00 28.20  ? 197 PRO G O   1 
ATOM   8149  C  CB  . PRO D  1 198 ? -38.145  -50.702 41.325  1.00 32.78  ? 197 PRO G CB  1 
ATOM   8150  C  CG  . PRO D  1 198 ? -37.401  -49.532 40.727  1.00 34.93  ? 197 PRO G CG  1 
ATOM   8151  C  CD  . PRO D  1 198 ? -38.148  -49.229 39.448  1.00 33.74  ? 197 PRO G CD  1 
ATOM   8152  N  N   . VAL D  1 199 ? -40.816  -50.299 43.105  1.00 25.05  ? 198 VAL G N   1 
ATOM   8153  C  CA  . VAL D  1 199 ? -41.339  -49.659 44.311  1.00 26.69  ? 198 VAL G CA  1 
ATOM   8154  C  C   . VAL D  1 199 ? -40.327  -49.799 45.457  1.00 27.77  ? 198 VAL G C   1 
ATOM   8155  O  O   . VAL D  1 199 ? -39.909  -50.917 45.762  1.00 27.52  ? 198 VAL G O   1 
ATOM   8156  C  CB  . VAL D  1 199 ? -42.674  -50.306 44.705  1.00 24.82  ? 198 VAL G CB  1 
ATOM   8157  C  CG1 . VAL D  1 199 ? -43.256  -49.655 45.951  1.00 24.25  ? 198 VAL G CG1 1 
ATOM   8158  C  CG2 . VAL D  1 199 ? -43.661  -50.315 43.548  1.00 25.44  ? 198 VAL G CG2 1 
ATOM   8159  N  N   . LYS D  1 200 ? -39.964  -48.679 46.084  1.00 25.22  ? 199 LYS G N   1 
ATOM   8160  C  CA  . LYS D  1 200 ? -39.185  -48.691 47.310  1.00 29.36  ? 199 LYS G CA  1 
ATOM   8161  C  C   . LYS D  1 200 ? -40.138  -48.809 48.496  1.00 28.85  ? 199 LYS G C   1 
ATOM   8162  O  O   . LYS D  1 200 ? -41.147  -48.087 48.545  1.00 26.07  ? 199 LYS G O   1 
ATOM   8163  C  CB  . LYS D  1 200 ? -38.336  -47.434 47.452  1.00 33.40  ? 199 LYS G CB  1 
ATOM   8164  C  CG  . LYS D  1 200 ? -37.377  -47.205 46.299  1.00 46.68  ? 199 LYS G CG  1 
ATOM   8165  C  CD  . LYS D  1 200 ? -36.378  -46.095 46.540  1.00 55.81  ? 199 LYS G CD  1 
ATOM   8166  C  CE  . LYS D  1 200 ? -35.397  -45.960 45.391  1.00 62.29  ? 199 LYS G CE  1 
ATOM   8167  N  NZ  . LYS D  1 200 ? -34.602  -44.713 45.502  1.00 67.80  ? 199 LYS G NZ  1 
ATOM   8168  N  N   . VAL D  1 201 ? -39.795  -49.706 49.428  1.00 23.42  ? 200 VAL G N   1 
ATOM   8169  C  CA  . VAL D  1 201 ? -40.573  -50.020 50.596  1.00 24.57  ? 200 VAL G CA  1 
ATOM   8170  C  C   . VAL D  1 201 ? -39.664  -49.829 51.808  1.00 27.53  ? 200 VAL G C   1 
ATOM   8171  O  O   . VAL D  1 201 ? -38.590  -50.440 51.893  1.00 27.56  ? 200 VAL G O   1 
ATOM   8172  C  CB  . VAL D  1 201 ? -41.103  -51.458 50.532  1.00 23.95  ? 200 VAL G CB  1 
ATOM   8173  C  CG1 . VAL D  1 201 ? -41.931  -51.822 51.747  1.00 24.87  ? 200 VAL G CG1 1 
ATOM   8174  C  CG2 . VAL D  1 201 ? -41.842  -51.753 49.240  1.00 25.12  ? 200 VAL G CG2 1 
ATOM   8175  N  N   . TRP D  1 202 ? -40.064  -48.980 52.747  1.00 27.40  ? 201 TRP G N   1 
ATOM   8176  C  CA  . TRP D  1 202 ? -39.216  -48.737 53.905  1.00 27.27  ? 201 TRP G CA  1 
ATOM   8177  C  C   . TRP D  1 202 ? -40.038  -48.236 55.084  1.00 28.99  ? 201 TRP G C   1 
ATOM   8178  O  O   . TRP D  1 202 ? -41.083  -47.627 54.911  1.00 27.24  ? 201 TRP G O   1 
ATOM   8179  C  CB  . TRP D  1 202 ? -38.103  -47.742 53.576  1.00 28.26  ? 201 TRP G CB  1 
ATOM   8180  C  CG  . TRP D  1 202 ? -38.537  -46.311 53.605  1.00 29.32  ? 201 TRP G CG  1 
ATOM   8181  C  CD1 . TRP D  1 202 ? -38.404  -45.420 54.629  1.00 31.38  ? 201 TRP G CD1 1 
ATOM   8182  C  CD2 . TRP D  1 202 ? -39.199  -45.608 52.541  1.00 29.83  ? 201 TRP G CD2 1 
ATOM   8183  N  NE1 . TRP D  1 202 ? -38.938  -44.211 54.269  1.00 31.54  ? 201 TRP G NE1 1 
ATOM   8184  C  CE2 . TRP D  1 202 ? -39.421  -44.293 52.990  1.00 29.93  ? 201 TRP G CE2 1 
ATOM   8185  C  CE3 . TRP D  1 202 ? -39.617  -45.966 51.256  1.00 30.99  ? 201 TRP G CE3 1 
ATOM   8186  C  CZ2 . TRP D  1 202 ? -40.048  -43.333 52.195  1.00 35.12  ? 201 TRP G CZ2 1 
ATOM   8187  C  CZ3 . TRP D  1 202 ? -40.249  -45.025 50.473  1.00 34.95  ? 201 TRP G CZ3 1 
ATOM   8188  C  CH2 . TRP D  1 202 ? -40.445  -43.720 50.932  1.00 35.81  ? 201 TRP G CH2 1 
ATOM   8189  N  N   . GLY D  1 203 ? -39.478  -48.432 56.275  1.00 28.25  ? 202 GLY G N   1 
ATOM   8190  C  CA  . GLY D  1 203 ? -40.038  -47.943 57.518  1.00 28.34  ? 202 GLY G CA  1 
ATOM   8191  C  C   . GLY D  1 203 ? -39.581  -48.822 58.660  1.00 28.73  ? 202 GLY G C   1 
ATOM   8192  O  O   . GLY D  1 203 ? -38.556  -49.484 58.577  1.00 30.74  ? 202 GLY G O   1 
ATOM   8193  N  N   . SER D  1 204 ? -40.381  -48.861 59.710  1.00 29.69  ? 203 SER G N   1 
ATOM   8194  C  CA  . SER D  1 204 ? -39.987  -49.466 60.944  1.00 32.93  ? 203 SER G CA  1 
ATOM   8195  C  C   . SER D  1 204 ? -41.177  -50.225 61.527  1.00 31.42  ? 203 SER G C   1 
ATOM   8196  O  O   . SER D  1 204 ? -42.306  -49.711 61.567  1.00 30.67  ? 203 SER G O   1 
ATOM   8197  C  CB  . SER D  1 204 ? -39.448  -48.412 61.876  1.00 35.14  ? 203 SER G CB  1 
ATOM   8198  O  OG  . SER D  1 204 ? -39.270  -48.964 63.161  1.00 51.71  ? 203 SER G OG  1 
ATOM   8199  N  N   . ILE D  1 205 ? -40.933  -51.470 61.916  1.00 26.45  ? 204 ILE G N   1 
ATOM   8200  C  CA  . ILE D  1 205 ? -41.903  -52.278 62.615  1.00 28.04  ? 204 ILE G CA  1 
ATOM   8201  C  C   . ILE D  1 205 ? -41.270  -52.651 63.962  1.00 31.39  ? 204 ILE G C   1 
ATOM   8202  O  O   . ILE D  1 205 ? -40.124  -53.102 63.986  1.00 32.28  ? 204 ILE G O   1 
ATOM   8203  C  CB  . ILE D  1 205 ? -42.270  -53.520 61.802  1.00 27.90  ? 204 ILE G CB  1 
ATOM   8204  C  CG1 . ILE D  1 205 ? -42.729  -53.198 60.380  1.00 27.71  ? 204 ILE G CG1 1 
ATOM   8205  C  CG2 . ILE D  1 205 ? -43.284  -54.374 62.544  1.00 28.91  ? 204 ILE G CG2 1 
ATOM   8206  C  CD1 . ILE D  1 205 ? -42.951  -54.445 59.555  1.00 30.29  ? 204 ILE G CD1 1 
ATOM   8207  N  N   . LYS D  1 206 ? -41.992  -52.408 65.060  1.00 30.65  ? 205 LYS G N   1 
ATOM   8208  C  CA  . LYS D  1 206 ? -41.513  -52.673 66.417  1.00 32.43  ? 205 LYS G CA  1 
ATOM   8209  C  C   . LYS D  1 206 ? -42.435  -53.711 67.074  1.00 30.10  ? 205 LYS G C   1 
ATOM   8210  O  O   . LYS D  1 206 ? -43.469  -54.088 66.513  1.00 27.46  ? 205 LYS G O   1 
ATOM   8211  C  CB  . LYS D  1 206 ? -41.333  -51.341 67.154  1.00 34.49  ? 205 LYS G CB  1 
ATOM   8212  C  CG  . LYS D  1 206 ? -42.606  -50.666 67.647  1.00 41.22  ? 205 LYS G CG  1 
ATOM   8213  C  CD  . LYS D  1 206 ? -42.359  -49.264 68.204  1.00 43.92  ? 205 LYS G CD  1 
ATOM   8214  C  CE  . LYS D  1 206 ? -43.625  -48.524 68.588  1.00 45.70  ? 205 LYS G CE  1 
ATOM   8215  N  NZ  . LYS D  1 206 ? -43.333  -47.111 68.944  1.00 47.31  ? 205 LYS G NZ  1 
ATOM   8216  N  N   . GLY D  1 207 ? -41.997  -54.248 68.225  1.00 28.77  ? 206 GLY G N   1 
ATOM   8217  C  CA  . GLY D  1 207 ? -42.715  -55.291 68.960  1.00 26.84  ? 206 GLY G CA  1 
ATOM   8218  C  C   . GLY D  1 207 ? -42.567  -56.694 68.383  1.00 27.05  ? 206 GLY G C   1 
ATOM   8219  O  O   . GLY D  1 207 ? -43.372  -57.587 68.691  1.00 29.67  ? 206 GLY G O   1 
ATOM   8220  N  N   . LEU D  1 208 ? -41.543  -56.921 67.553  1.00 27.59  ? 207 LEU G N   1 
ATOM   8221  C  CA  . LEU D  1 208 ? -41.310  -58.236 66.977  1.00 30.19  ? 207 LEU G CA  1 
ATOM   8222  C  C   . LEU D  1 208 ? -40.237  -58.989 67.783  1.00 32.73  ? 207 LEU G C   1 
ATOM   8223  O  O   . LEU D  1 208 ? -39.344  -58.380 68.331  1.00 35.09  ? 207 LEU G O   1 
ATOM   8224  C  CB  . LEU D  1 208 ? -40.813  -58.070 65.539  1.00 32.58  ? 207 LEU G CB  1 
ATOM   8225  C  CG  . LEU D  1 208 ? -41.825  -57.549 64.523  1.00 29.58  ? 207 LEU G CG  1 
ATOM   8226  C  CD1 . LEU D  1 208 ? -41.106  -56.993 63.319  1.00 29.97  ? 207 LEU G CD1 1 
ATOM   8227  C  CD2 . LEU D  1 208 ? -42.780  -58.658 64.118  1.00 28.88  ? 207 LEU G CD2 1 
ATOM   8228  N  N   . THR D  1 209 ? -40.308  -60.321 67.746  1.00 36.39  ? 208 THR G N   1 
ATOM   8229  C  CA  . THR D  1 209 ? -39.200  -61.185 68.143  1.00 38.46  ? 208 THR G CA  1 
ATOM   8230  C  C   . THR D  1 209 ? -38.040  -61.014 67.154  1.00 41.23  ? 208 THR G C   1 
ATOM   8231  O  O   . THR D  1 209 ? -38.241  -60.866 65.940  1.00 37.02  ? 208 THR G O   1 
ATOM   8232  C  CB  . THR D  1 209 ? -39.637  -62.649 68.217  1.00 38.75  ? 208 THR G CB  1 
ATOM   8233  O  OG1 . THR D  1 209 ? -40.090  -63.059 66.926  1.00 41.01  ? 208 THR G OG1 1 
ATOM   8234  C  CG2 . THR D  1 209 ? -40.743  -62.874 69.227  1.00 40.96  ? 208 THR G CG2 1 
ATOM   8235  N  N   . GLU D  1 210 ? -36.822  -61.054 67.690  1.00 40.50  ? 209 GLU G N   1 
ATOM   8236  C  CA  . GLU D  1 210 ? -35.602  -61.019 66.905  1.00 41.87  ? 209 GLU G CA  1 
ATOM   8237  C  C   . GLU D  1 210 ? -35.639  -62.143 65.867  1.00 37.57  ? 209 GLU G C   1 
ATOM   8238  O  O   . GLU D  1 210 ? -36.102  -63.258 66.140  1.00 39.26  ? 209 GLU G O   1 
ATOM   8239  C  CB  . GLU D  1 210 ? -34.382  -61.161 67.818  1.00 47.21  ? 209 GLU G CB  1 
ATOM   8240  C  CG  . GLU D  1 210 ? -33.072  -60.998 67.078  1.00 51.41  ? 209 GLU G CG  1 
ATOM   8241  C  CD  . GLU D  1 210 ? -31.839  -61.286 67.913  1.00 60.82  ? 209 GLU G CD  1 
ATOM   8242  O  OE1 . GLU D  1 210 ? -30.755  -61.407 67.311  1.00 63.56  ? 209 GLU G OE1 1 
ATOM   8243  O  OE2 . GLU D  1 210 ? -31.967  -61.382 69.158  1.00 64.08  ? 209 GLU G OE2 1 
ATOM   8244  N  N   . GLY D  1 211 ? -35.191  -61.820 64.651  1.00 36.32  ? 210 GLY G N   1 
ATOM   8245  C  CA  . GLY D  1 211 ? -35.135  -62.796 63.568  1.00 35.90  ? 210 GLY G CA  1 
ATOM   8246  C  C   . GLY D  1 211 ? -36.003  -62.410 62.379  1.00 33.60  ? 210 GLY G C   1 
ATOM   8247  O  O   . GLY D  1 211 ? -36.451  -61.266 62.264  1.00 32.59  ? 210 GLY G O   1 
ATOM   8248  N  N   . LEU D  1 212 ? -36.252  -63.399 61.520  1.00 34.12  ? 211 LEU G N   1 
ATOM   8249  C  CA  . LEU D  1 212 ? -36.936  -63.220 60.240  1.00 36.27  ? 211 LEU G CA  1 
ATOM   8250  C  C   . LEU D  1 212 ? -38.455  -63.335 60.422  1.00 35.87  ? 211 LEU G C   1 
ATOM   8251  O  O   . LEU D  1 212 ? -38.962  -64.201 61.128  1.00 31.51  ? 211 LEU G O   1 
ATOM   8252  C  CB  . LEU D  1 212 ? -36.470  -64.287 59.253  1.00 37.58  ? 211 LEU G CB  1 
ATOM   8253  C  CG  . LEU D  1 212 ? -34.996  -64.249 58.862  1.00 43.54  ? 211 LEU G CG  1 
ATOM   8254  C  CD1 . LEU D  1 212 ? -34.617  -65.541 58.156  1.00 48.71  ? 211 LEU G CD1 1 
ATOM   8255  C  CD2 . LEU D  1 212 ? -34.700  -63.063 57.979  1.00 42.42  ? 211 LEU G CD2 1 
ATOM   8256  N  N   . HIS D  1 213 ? -39.185  -62.480 59.700  1.00 29.53  ? 212 HIS G N   1 
ATOM   8257  C  CA  . HIS D  1 213 ? -40.639  -62.511 59.676  1.00 29.37  ? 212 HIS G CA  1 
ATOM   8258  C  C   . HIS D  1 213 ? -41.115  -62.333 58.230  1.00 27.30  ? 212 HIS G C   1 
ATOM   8259  O  O   . HIS D  1 213 ? -40.660  -61.412 57.518  1.00 26.64  ? 212 HIS G O   1 
ATOM   8260  C  CB  . HIS D  1 213 ? -41.191  -61.396 60.566  1.00 29.84  ? 212 HIS G CB  1 
ATOM   8261  C  CG  . HIS D  1 213 ? -40.869  -61.552 62.012  1.00 30.88  ? 212 HIS G CG  1 
ATOM   8262  N  ND1 . HIS D  1 213 ? -41.701  -62.251 62.873  1.00 29.73  ? 212 HIS G ND1 1 
ATOM   8263  C  CD2 . HIS D  1 213 ? -39.847  -61.083 62.764  1.00 31.08  ? 212 HIS G CD2 1 
ATOM   8264  C  CE1 . HIS D  1 213 ? -41.207  -62.189 64.100  1.00 30.25  ? 212 HIS G CE1 1 
ATOM   8265  N  NE2 . HIS D  1 213 ? -40.079  -61.487 64.061  1.00 30.64  ? 212 HIS G NE2 1 
ATOM   8266  N  N   . GLY D  1 214 ? -42.001  -63.223 57.796  1.00 26.03  ? 213 GLY G N   1 
ATOM   8267  C  CA  . GLY D  1 214 ? -42.612  -63.089 56.484  1.00 27.56  ? 213 GLY G CA  1 
ATOM   8268  C  C   . GLY D  1 214 ? -43.334  -61.757 56.376  1.00 25.01  ? 213 GLY G C   1 
ATOM   8269  O  O   . GLY D  1 214 ? -43.859  -61.222 57.387  1.00 24.47  ? 213 GLY G O   1 
ATOM   8270  N  N   . PHE D  1 215 ? -43.340  -61.220 55.158  1.00 26.01  ? 214 PHE G N   1 
ATOM   8271  C  CA  . PHE D  1 215 ? -43.783  -59.862 54.855  1.00 25.43  ? 214 PHE G CA  1 
ATOM   8272  C  C   . PHE D  1 215 ? -44.408  -59.872 53.463  1.00 25.38  ? 214 PHE G C   1 
ATOM   8273  O  O   . PHE D  1 215 ? -43.700  -60.056 52.473  1.00 24.01  ? 214 PHE G O   1 
ATOM   8274  C  CB  . PHE D  1 215 ? -42.578  -58.936 54.943  1.00 26.97  ? 214 PHE G CB  1 
ATOM   8275  C  CG  . PHE D  1 215 ? -42.807  -57.457 54.820  1.00 26.21  ? 214 PHE G CG  1 
ATOM   8276  C  CD1 . PHE D  1 215 ? -43.448  -56.749 55.824  1.00 28.39  ? 214 PHE G CD1 1 
ATOM   8277  C  CD2 . PHE D  1 215 ? -42.295  -56.761 53.739  1.00 27.14  ? 214 PHE G CD2 1 
ATOM   8278  C  CE1 . PHE D  1 215 ? -43.591  -55.372 55.738  1.00 26.59  ? 214 PHE G CE1 1 
ATOM   8279  C  CE2 . PHE D  1 215 ? -42.441  -55.384 53.655  1.00 27.45  ? 214 PHE G CE2 1 
ATOM   8280  C  CZ  . PHE D  1 215 ? -43.076  -54.693 54.661  1.00 27.88  ? 214 PHE G CZ  1 
ATOM   8281  N  N   . HIS D  1 216 ? -45.743  -59.804 53.422  1.00 23.24  ? 215 HIS G N   1 
ATOM   8282  C  CA  . HIS D  1 216 ? -46.470  -60.042 52.189  1.00 25.70  ? 215 HIS G CA  1 
ATOM   8283  C  C   . HIS D  1 216 ? -47.608  -59.029 52.015  1.00 23.67  ? 215 HIS G C   1 
ATOM   8284  O  O   . HIS D  1 216 ? -48.178  -58.514 53.005  1.00 22.95  ? 215 HIS G O   1 
ATOM   8285  C  CB  . HIS D  1 216 ? -47.085  -61.439 52.138  1.00 27.05  ? 215 HIS G CB  1 
ATOM   8286  C  CG  . HIS D  1 216 ? -46.196  -62.533 52.607  1.00 30.38  ? 215 HIS G CG  1 
ATOM   8287  N  ND1 . HIS D  1 216 ? -46.636  -63.490 53.499  1.00 31.65  ? 215 HIS G ND1 1 
ATOM   8288  C  CD2 . HIS D  1 216 ? -44.911  -62.832 52.311  1.00 31.23  ? 215 HIS G CD2 1 
ATOM   8289  C  CE1 . HIS D  1 216 ? -45.649  -64.337 53.732  1.00 33.50  ? 215 HIS G CE1 1 
ATOM   8290  N  NE2 . HIS D  1 216 ? -44.580  -63.950 53.022  1.00 32.25  ? 215 HIS G NE2 1 
ATOM   8291  N  N   . VAL D  1 217 ? -47.971  -58.830 50.748  1.00 21.36  ? 216 VAL G N   1 
ATOM   8292  C  CA  . VAL D  1 217 ? -49.221  -58.159 50.399  1.00 23.64  ? 216 VAL G CA  1 
ATOM   8293  C  C   . VAL D  1 217 ? -50.258  -59.247 50.131  1.00 23.60  ? 216 VAL G C   1 
ATOM   8294  O  O   . VAL D  1 217 ? -50.087  -60.092 49.254  1.00 25.85  ? 216 VAL G O   1 
ATOM   8295  C  CB  . VAL D  1 217 ? -49.061  -57.229 49.186  1.00 23.18  ? 216 VAL G CB  1 
ATOM   8296  C  CG1 . VAL D  1 217 ? -50.403  -56.573 48.830  1.00 23.60  ? 216 VAL G CG1 1 
ATOM   8297  C  CG2 . VAL D  1 217 ? -47.977  -56.197 49.420  1.00 23.52  ? 216 VAL G CG2 1 
ATOM   8298  N  N   . HIS D  1 218 ? -51.309  -59.228 50.931  1.00 22.35  ? 217 HIS G N   1 
ATOM   8299  C  CA  . HIS D  1 218 ? -52.443  -60.111 50.814  1.00 23.71  ? 217 HIS G CA  1 
ATOM   8300  C  C   . HIS D  1 218 ? -53.502  -59.422 49.935  1.00 24.58  ? 217 HIS G C   1 
ATOM   8301  O  O   . HIS D  1 218 ? -53.481  -58.214 49.778  1.00 26.22  ? 217 HIS G O   1 
ATOM   8302  C  CB  . HIS D  1 218 ? -52.900  -60.516 52.225  1.00 24.18  ? 217 HIS G CB  1 
ATOM   8303  C  CG  . HIS D  1 218 ? -52.005  -61.510 52.917  1.00 27.30  ? 217 HIS G CG  1 
ATOM   8304  N  ND1 . HIS D  1 218 ? -52.448  -62.778 53.245  1.00 27.31  ? 217 HIS G ND1 1 
ATOM   8305  C  CD2 . HIS D  1 218 ? -50.720  -61.439 53.351  1.00 26.84  ? 217 HIS G CD2 1 
ATOM   8306  C  CE1 . HIS D  1 218 ? -51.489  -63.435 53.874  1.00 30.19  ? 217 HIS G CE1 1 
ATOM   8307  N  NE2 . HIS D  1 218 ? -50.389  -62.663 53.908  1.00 30.48  ? 217 HIS G NE2 1 
ATOM   8308  N  N   . GLU D  1 219 ? -54.428  -60.202 49.377  1.00 24.14  ? 218 GLU G N   1 
ATOM   8309  C  CA  . GLU D  1 219 ? -55.263  -59.785 48.283  1.00 25.32  ? 218 GLU G CA  1 
ATOM   8310  C  C   . GLU D  1 219 ? -56.266  -58.678 48.680  1.00 25.58  ? 218 GLU G C   1 
ATOM   8311  O  O   . GLU D  1 219 ? -56.487  -57.756 47.910  1.00 26.65  ? 218 GLU G O   1 
ATOM   8312  C  CB  . GLU D  1 219 ? -56.018  -60.999 47.767  1.00 28.55  ? 218 GLU G CB  1 
ATOM   8313  C  CG  . GLU D  1 219 ? -56.886  -60.670 46.580  1.00 31.49  ? 218 GLU G CG  1 
ATOM   8314  C  CD  . GLU D  1 219 ? -57.475  -61.872 45.861  1.00 35.64  ? 218 GLU G CD  1 
ATOM   8315  O  OE1 . GLU D  1 219 ? -58.068  -61.648 44.799  1.00 40.28  ? 218 GLU G OE1 1 
ATOM   8316  O  OE2 . GLU D  1 219 ? -57.361  -63.014 46.386  1.00 35.99  ? 218 GLU G OE2 1 
ATOM   8317  N  N   . PHE D  1 220 ? -56.892  -58.804 49.853  1.00 25.84  ? 219 PHE G N   1 
ATOM   8318  C  CA  . PHE D  1 220 ? -58.018  -57.953 50.234  1.00 25.52  ? 219 PHE G CA  1 
ATOM   8319  C  C   . PHE D  1 220 ? -57.573  -56.965 51.302  1.00 26.03  ? 219 PHE G C   1 
ATOM   8320  O  O   . PHE D  1 220 ? -56.848  -57.311 52.250  1.00 25.35  ? 219 PHE G O   1 
ATOM   8321  C  CB  . PHE D  1 220 ? -59.197  -58.808 50.690  1.00 27.03  ? 219 PHE G CB  1 
ATOM   8322  C  CG  . PHE D  1 220 ? -59.618  -59.810 49.654  1.00 27.26  ? 219 PHE G CG  1 
ATOM   8323  C  CD1 . PHE D  1 220 ? -60.023  -59.394 48.403  1.00 29.19  ? 219 PHE G CD1 1 
ATOM   8324  C  CD2 . PHE D  1 220 ? -59.561  -61.167 49.918  1.00 32.03  ? 219 PHE G CD2 1 
ATOM   8325  C  CE1 . PHE D  1 220 ? -60.383  -60.312 47.432  1.00 31.64  ? 219 PHE G CE1 1 
ATOM   8326  C  CE2 . PHE D  1 220 ? -59.940  -62.088 48.954  1.00 31.90  ? 219 PHE G CE2 1 
ATOM   8327  C  CZ  . PHE D  1 220 ? -60.339  -61.660 47.713  1.00 32.48  ? 219 PHE G CZ  1 
ATOM   8328  N  N   . GLY D  1 221 ? -57.978  -55.710 51.119  1.00 23.78  ? 220 GLY G N   1 
ATOM   8329  C  CA  . GLY D  1 221 ? -57.843  -54.693 52.154  1.00 24.60  ? 220 GLY G CA  1 
ATOM   8330  C  C   . GLY D  1 221 ? -59.015  -54.747 53.114  1.00 25.51  ? 220 GLY G C   1 
ATOM   8331  O  O   . GLY D  1 221 ? -59.668  -53.747 53.379  1.00 26.31  ? 220 GLY G O   1 
ATOM   8332  N  N   . ASP D  1 222 ? -59.284  -55.954 53.620  1.00 26.91  ? 221 ASP G N   1 
ATOM   8333  C  CA  . ASP D  1 222 ? -60.438  -56.256 54.434  1.00 26.59  ? 221 ASP G CA  1 
ATOM   8334  C  C   . ASP D  1 222 ? -59.911  -56.688 55.795  1.00 28.35  ? 221 ASP G C   1 
ATOM   8335  O  O   . ASP D  1 222 ? -59.330  -57.783 55.885  1.00 26.98  ? 221 ASP G O   1 
ATOM   8336  C  CB  . ASP D  1 222 ? -61.278  -57.353 53.784  1.00 26.90  ? 221 ASP G CB  1 
ATOM   8337  C  CG  . ASP D  1 222 ? -62.537  -57.741 54.541  1.00 27.80  ? 221 ASP G CG  1 
ATOM   8338  O  OD1 . ASP D  1 222 ? -63.446  -58.263 53.881  1.00 32.55  ? 221 ASP G OD1 1 
ATOM   8339  O  OD2 . ASP D  1 222 ? -62.602  -57.524 55.773  1.00 28.79  ? 221 ASP G OD2 1 
ATOM   8340  N  N   . ASN D  1 223 ? -60.054  -55.815 56.797  1.00 26.04  ? 222 ASN G N   1 
ATOM   8341  C  CA  . ASN D  1 223 ? -59.624  -56.104 58.164  1.00 29.30  ? 222 ASN G CA  1 
ATOM   8342  C  C   . ASN D  1 223 ? -60.852  -56.291 59.077  1.00 28.31  ? 222 ASN G C   1 
ATOM   8343  O  O   . ASN D  1 223 ? -60.772  -56.097 60.307  1.00 27.71  ? 222 ASN G O   1 
ATOM   8344  C  CB  . ASN D  1 223 ? -58.638  -55.031 58.656  1.00 33.20  ? 222 ASN G CB  1 
ATOM   8345  C  CG  . ASN D  1 223 ? -57.313  -55.013 57.899  1.00 41.64  ? 222 ASN G CG  1 
ATOM   8346  O  OD1 . ASN D  1 223 ? -57.035  -55.873 57.046  1.00 45.92  ? 222 ASN G OD1 1 
ATOM   8347  N  ND2 . ASN D  1 223 ? -56.471  -54.036 58.215  1.00 42.45  ? 222 ASN G ND2 1 
ATOM   8348  N  N   . THR D  1 224 ? -61.995  -56.710 58.511  1.00 28.64  ? 223 THR G N   1 
ATOM   8349  C  CA  . THR D  1 224 ? -63.238  -56.751 59.296  1.00 30.55  ? 223 THR G CA  1 
ATOM   8350  C  C   . THR D  1 224 ? -63.158  -57.811 60.403  1.00 33.71  ? 223 THR G C   1 
ATOM   8351  O  O   . THR D  1 224 ? -63.759  -57.630 61.431  1.00 30.90  ? 223 THR G O   1 
ATOM   8352  C  CB  . THR D  1 224 ? -64.485  -57.024 58.452  1.00 30.33  ? 223 THR G CB  1 
ATOM   8353  O  OG1 . THR D  1 224 ? -64.249  -58.213 57.708  1.00 29.17  ? 223 THR G OG1 1 
ATOM   8354  C  CG2 . THR D  1 224 ? -64.840  -55.875 57.529  1.00 32.08  ? 223 THR G CG2 1 
ATOM   8355  N  N   . ALA D  1 225 ? -62.399  -58.890 60.192  1.00 33.36  ? 224 ALA G N   1 
ATOM   8356  C  CA  . ALA D  1 225 ? -62.140  -59.870 61.250  1.00 37.30  ? 224 ALA G CA  1 
ATOM   8357  C  C   . ALA D  1 225 ? -60.643  -59.908 61.587  1.00 41.28  ? 224 ALA G C   1 
ATOM   8358  O  O   . ALA D  1 225 ? -60.071  -60.962 61.795  1.00 45.86  ? 224 ALA G O   1 
ATOM   8359  C  CB  . ALA D  1 225 ? -62.646  -61.224 60.810  1.00 40.20  ? 224 ALA G CB  1 
ATOM   8360  N  N   . GLY D  1 226 ? -60.019  -58.733 61.653  1.00 37.18  ? 225 GLY G N   1 
ATOM   8361  C  CA  . GLY D  1 226 ? -58.592  -58.610 61.803  1.00 33.80  ? 225 GLY G CA  1 
ATOM   8362  C  C   . GLY D  1 226 ? -57.857  -59.031 60.538  1.00 31.82  ? 225 GLY G C   1 
ATOM   8363  O  O   . GLY D  1 226 ? -58.416  -59.028 59.438  1.00 31.21  ? 225 GLY G O   1 
ATOM   8364  N  N   . CYS D  1 227 ? -56.611  -59.472 60.712  1.00 30.66  ? 226 CYS G N   1 
ATOM   8365  C  CA  . CYS D  1 227 ? -55.710  -59.800 59.600  1.00 31.83  ? 226 CYS G CA  1 
ATOM   8366  C  C   . CYS D  1 227 ? -56.194  -61.013 58.787  1.00 28.93  ? 226 CYS G C   1 
ATOM   8367  O  O   . CYS D  1 227 ? -55.898  -61.110 57.605  1.00 29.33  ? 226 CYS G O   1 
ATOM   8368  C  CB  . CYS D  1 227 ? -54.298  -59.990 60.140  1.00 33.74  ? 226 CYS G CB  1 
ATOM   8369  S  SG  . CYS D  1 227 ? -53.671  -58.494 60.947  1.00 38.58  ? 226 CYS G SG  1 
ATOM   8370  N  N   . THR D  1 228 ? -56.975  -61.903 59.403  1.00 29.67  ? 227 THR G N   1 
ATOM   8371  C  CA  . THR D  1 228 ? -57.529  -63.113 58.769  1.00 31.88  ? 227 THR G CA  1 
ATOM   8372  C  C   . THR D  1 228 ? -58.333  -62.771 57.518  1.00 31.09  ? 227 THR G C   1 
ATOM   8373  O  O   . THR D  1 228 ? -58.294  -63.485 56.527  1.00 30.34  ? 227 THR G O   1 
ATOM   8374  C  CB  . THR D  1 228 ? -58.516  -63.830 59.702  1.00 39.34  ? 227 THR G CB  1 
ATOM   8375  O  OG1 . THR D  1 228 ? -57.849  -64.108 60.925  1.00 47.96  ? 227 THR G OG1 1 
ATOM   8376  C  CG2 . THR D  1 228 ? -59.060  -65.120 59.125  1.00 46.06  ? 227 THR G CG2 1 
ATOM   8377  N  N   . SER D  1 229 ? -59.077  -61.656 57.568  1.00 27.69  ? 228 SER G N   1 
ATOM   8378  C  CA  . SER D  1 229 ? -60.017  -61.340 56.491  1.00 28.65  ? 228 SER G CA  1 
ATOM   8379  C  C   . SER D  1 229 ? -59.309  -60.798 55.239  1.00 27.90  ? 228 SER G C   1 
ATOM   8380  O  O   . SER D  1 229 ? -59.914  -60.681 54.177  1.00 29.61  ? 228 SER G O   1 
ATOM   8381  C  CB  . SER D  1 229 ? -61.135  -60.448 57.019  1.00 30.63  ? 228 SER G CB  1 
ATOM   8382  O  OG  . SER D  1 229 ? -60.642  -59.445 57.871  1.00 35.86  ? 228 SER G OG  1 
ATOM   8383  N  N   . ALA D  1 230 ? -58.000  -60.543 55.355  1.00 27.51  ? 229 ALA G N   1 
ATOM   8384  C  CA  . ALA D  1 230 ? -57.160  -60.084 54.246  1.00 27.96  ? 229 ALA G CA  1 
ATOM   8385  C  C   . ALA D  1 230 ? -56.991  -61.153 53.150  1.00 28.04  ? 229 ALA G C   1 
ATOM   8386  O  O   . ALA D  1 230 ? -56.558  -60.849 52.038  1.00 28.07  ? 229 ALA G O   1 
ATOM   8387  C  CB  . ALA D  1 230 ? -55.828  -59.657 54.794  1.00 28.10  ? 229 ALA G CB  1 
ATOM   8388  N  N   . GLY D  1 231 ? -57.371  -62.394 53.443  1.00 27.29  ? 230 GLY G N   1 
ATOM   8389  C  CA  . GLY D  1 231 ? -57.330  -63.458 52.457  1.00 28.01  ? 230 GLY G CA  1 
ATOM   8390  C  C   . GLY D  1 231 ? -55.897  -63.919 52.158  1.00 26.56  ? 230 GLY G C   1 
ATOM   8391  O  O   . GLY D  1 231 ? -54.988  -63.683 52.946  1.00 26.58  ? 230 GLY G O   1 
ATOM   8392  N  N   . PRO D  1 232 ? -55.666  -64.601 51.016  1.00 27.64  ? 231 PRO G N   1 
ATOM   8393  C  CA  . PRO D  1 232 ? -54.350  -65.147 50.677  1.00 30.25  ? 231 PRO G CA  1 
ATOM   8394  C  C   . PRO D  1 232 ? -53.458  -64.073 50.055  1.00 30.11  ? 231 PRO G C   1 
ATOM   8395  O  O   . PRO D  1 232 ? -53.850  -62.883 49.959  1.00 26.45  ? 231 PRO G O   1 
ATOM   8396  C  CB  . PRO D  1 232 ? -54.708  -66.239 49.659  1.00 30.20  ? 231 PRO G CB  1 
ATOM   8397  C  CG  . PRO D  1 232 ? -55.888  -65.647 48.916  1.00 30.41  ? 231 PRO G CG  1 
ATOM   8398  C  CD  . PRO D  1 232 ? -56.669  -64.912 49.987  1.00 28.40  ? 231 PRO G CD  1 
ATOM   8399  N  N   . HIS D  1 233 ? -52.258  -64.482 49.665  1.00 27.65  ? 232 HIS G N   1 
ATOM   8400  C  CA  . HIS D  1 233 ? -51.310  -63.578 49.049  1.00 27.80  ? 232 HIS G CA  1 
ATOM   8401  C  C   . HIS D  1 233 ? -51.928  -63.025 47.765  1.00 26.89  ? 232 HIS G C   1 
ATOM   8402  O  O   . HIS D  1 233 ? -52.656  -63.723 47.074  1.00 24.83  ? 232 HIS G O   1 
ATOM   8403  C  CB  . HIS D  1 233 ? -49.949  -64.251 48.806  1.00 30.15  ? 232 HIS G CB  1 
ATOM   8404  C  CG  . HIS D  1 233 ? -49.238  -64.613 50.067  1.00 31.85  ? 232 HIS G CG  1 
ATOM   8405  N  ND1 . HIS D  1 233 ? -48.018  -65.246 50.078  1.00 31.27  ? 232 HIS G ND1 1 
ATOM   8406  C  CD2 . HIS D  1 233 ? -49.595  -64.458 51.361  1.00 34.28  ? 232 HIS G CD2 1 
ATOM   8407  C  CE1 . HIS D  1 233 ? -47.629  -65.420 51.330  1.00 34.31  ? 232 HIS G CE1 1 
ATOM   8408  N  NE2 . HIS D  1 233 ? -48.573  -64.920 52.155  1.00 35.62  ? 232 HIS G NE2 1 
ATOM   8409  N  N   . PHE D  1 234 ? -51.614  -61.762 47.464  1.00 24.08  ? 233 PHE G N   1 
ATOM   8410  C  CA  . PHE D  1 234 ? -52.014  -61.155 46.226  1.00 25.72  ? 233 PHE G CA  1 
ATOM   8411  C  C   . PHE D  1 234 ? -51.261  -61.852 45.090  1.00 26.45  ? 233 PHE G C   1 
ATOM   8412  O  O   . PHE D  1 234 ? -50.028  -61.830 45.048  1.00 27.99  ? 233 PHE G O   1 
ATOM   8413  C  CB  . PHE D  1 234 ? -51.732  -59.651 46.239  1.00 25.09  ? 233 PHE G CB  1 
ATOM   8414  C  CG  . PHE D  1 234 ? -52.036  -58.917 44.954  1.00 24.00  ? 233 PHE G CG  1 
ATOM   8415  C  CD1 . PHE D  1 234 ? -51.153  -57.976 44.459  1.00 25.54  ? 233 PHE G CD1 1 
ATOM   8416  C  CD2 . PHE D  1 234 ? -53.234  -59.102 44.294  1.00 28.04  ? 233 PHE G CD2 1 
ATOM   8417  C  CE1 . PHE D  1 234 ? -51.430  -57.271 43.301  1.00 24.62  ? 233 PHE G CE1 1 
ATOM   8418  C  CE2 . PHE D  1 234 ? -53.518  -58.397 43.142  1.00 25.37  ? 233 PHE G CE2 1 
ATOM   8419  C  CZ  . PHE D  1 234 ? -52.609  -57.495 42.641  1.00 26.36  ? 233 PHE G CZ  1 
ATOM   8420  N  N   . ASN D  1 235 ? -52.031  -62.426 44.164  1.00 29.00  ? 234 ASN G N   1 
ATOM   8421  C  CA  . ASN D  1 235 ? -51.511  -63.389 43.200  1.00 31.76  ? 234 ASN G CA  1 
ATOM   8422  C  C   . ASN D  1 235 ? -52.295  -63.298 41.895  1.00 31.31  ? 234 ASN G C   1 
ATOM   8423  O  O   . ASN D  1 235 ? -52.927  -64.263 41.470  1.00 32.63  ? 234 ASN G O   1 
ATOM   8424  C  CB  . ASN D  1 235 ? -51.576  -64.797 43.801  1.00 30.59  ? 234 ASN G CB  1 
ATOM   8425  C  CG  . ASN D  1 235 ? -50.887  -65.867 42.974  1.00 33.63  ? 234 ASN G CG  1 
ATOM   8426  O  OD1 . ASN D  1 235 ? -49.980  -65.589 42.180  1.00 30.99  ? 234 ASN G OD1 1 
ATOM   8427  N  ND2 . ASN D  1 235 ? -51.298  -67.104 43.203  1.00 29.38  ? 234 ASN G ND2 1 
ATOM   8428  N  N   . PRO D  1 236 ? -52.279  -62.155 41.184  1.00 31.64  ? 235 PRO G N   1 
ATOM   8429  C  CA  . PRO D  1 236 ? -53.104  -62.024 39.989  1.00 33.82  ? 235 PRO G CA  1 
ATOM   8430  C  C   . PRO D  1 236 ? -52.634  -62.982 38.872  1.00 38.31  ? 235 PRO G C   1 
ATOM   8431  O  O   . PRO D  1 236 ? -53.398  -63.252 37.969  1.00 38.63  ? 235 PRO G O   1 
ATOM   8432  C  CB  . PRO D  1 236 ? -52.916  -60.558 39.576  1.00 33.64  ? 235 PRO G CB  1 
ATOM   8433  C  CG  . PRO D  1 236 ? -51.574  -60.164 40.161  1.00 31.44  ? 235 PRO G CG  1 
ATOM   8434  C  CD  . PRO D  1 236 ? -51.448  -60.967 41.438  1.00 31.46  ? 235 PRO G CD  1 
ATOM   8435  N  N   . LEU D  1 237 ? -51.396  -63.502 38.944  1.00 39.58  ? 236 LEU G N   1 
ATOM   8436  C  CA  . LEU D  1 237 ? -50.872  -64.389 37.894  1.00 39.04  ? 236 LEU G CA  1 
ATOM   8437  C  C   . LEU D  1 237 ? -51.026  -65.880 38.239  1.00 39.44  ? 236 LEU G C   1 
ATOM   8438  O  O   . LEU D  1 237 ? -50.559  -66.722 37.466  1.00 40.87  ? 236 LEU G O   1 
ATOM   8439  C  CB  . LEU D  1 237 ? -49.410  -64.031 37.637  1.00 39.69  ? 236 LEU G CB  1 
ATOM   8440  C  CG  . LEU D  1 237 ? -49.213  -62.680 36.964  1.00 41.43  ? 236 LEU G CG  1 
ATOM   8441  C  CD1 . LEU D  1 237 ? -47.776  -62.228 37.090  1.00 42.55  ? 236 LEU G CD1 1 
ATOM   8442  C  CD2 . LEU D  1 237 ? -49.634  -62.751 35.505  1.00 47.77  ? 236 LEU G CD2 1 
ATOM   8443  N  N   . SER D  1 238 ? -51.698  -66.211 39.347  1.00 38.37  ? 237 SER G N   1 
ATOM   8444  C  CA  . SER D  1 238 ? -51.957  -67.604 39.774  1.00 43.28  ? 237 SER G CA  1 
ATOM   8445  C  C   . SER D  1 238 ? -50.672  -68.448 39.725  1.00 44.91  ? 237 SER G C   1 
ATOM   8446  O  O   . SER D  1 238 ? -50.652  -69.535 39.141  1.00 42.96  ? 237 SER G O   1 
ATOM   8447  C  CB  . SER D  1 238 ? -53.042  -68.242 38.939  1.00 45.02  ? 237 SER G CB  1 
ATOM   8448  O  OG  . SER D  1 238 ? -54.191  -67.413 38.890  1.00 49.62  ? 237 SER G OG  1 
ATOM   8449  N  N   . ARG D  1 239 ? -49.604  -67.939 40.344  1.00 42.03  ? 238 ARG G N   1 
ATOM   8450  C  CA  . ARG D  1 239 ? -48.361  -68.670 40.509  1.00 42.37  ? 238 ARG G CA  1 
ATOM   8451  C  C   . ARG D  1 239 ? -48.283  -69.213 41.941  1.00 42.99  ? 238 ARG G C   1 
ATOM   8452  O  O   . ARG D  1 239 ? -49.165  -68.960 42.765  1.00 39.43  ? 238 ARG G O   1 
ATOM   8453  C  CB  . ARG D  1 239 ? -47.187  -67.758 40.147  1.00 43.39  ? 238 ARG G CB  1 
ATOM   8454  C  CG  . ARG D  1 239 ? -47.105  -67.468 38.655  1.00 44.46  ? 238 ARG G CG  1 
ATOM   8455  C  CD  . ARG D  1 239 ? -45.980  -66.525 38.316  1.00 46.89  ? 238 ARG G CD  1 
ATOM   8456  N  NE  . ARG D  1 239 ? -45.977  -66.210 36.900  1.00 49.68  ? 238 ARG G NE  1 
ATOM   8457  C  CZ  . ARG D  1 239 ? -45.049  -65.471 36.301  1.00 56.54  ? 238 ARG G CZ  1 
ATOM   8458  N  NH1 . ARG D  1 239 ? -45.207  -65.119 35.038  1.00 57.43  ? 238 ARG G NH1 1 
ATOM   8459  N  NH2 . ARG D  1 239 ? -43.969  -65.083 36.963  1.00 55.17  ? 238 ARG G NH2 1 
ATOM   8460  N  N   . LYS D  1 240 ? -47.225  -69.987 42.210  1.00 41.14  ? 239 LYS G N   1 
ATOM   8461  C  CA  . LYS D  1 240 ? -46.918  -70.490 43.524  1.00 39.52  ? 239 LYS G CA  1 
ATOM   8462  C  C   . LYS D  1 240 ? -46.087  -69.434 44.253  1.00 35.06  ? 239 LYS G C   1 
ATOM   8463  O  O   . LYS D  1 240 ? -45.419  -68.614 43.611  1.00 34.19  ? 239 LYS G O   1 
ATOM   8464  C  CB  . LYS D  1 240 ? -46.168  -71.822 43.414  1.00 44.73  ? 239 LYS G CB  1 
ATOM   8465  C  CG  . LYS D  1 240 ? -46.939  -72.931 42.706  1.00 53.08  ? 239 LYS G CG  1 
ATOM   8466  C  CD  . LYS D  1 240 ? -46.487  -74.345 43.063  1.00 60.41  ? 239 LYS G CD  1 
ATOM   8467  C  CE  . LYS D  1 240 ? -44.991  -74.581 42.936  1.00 68.91  ? 239 LYS G CE  1 
ATOM   8468  N  NZ  . LYS D  1 240 ? -44.539  -74.637 41.522  1.00 72.62  ? 239 LYS G NZ  1 
ATOM   8469  N  N   . HIS D  1 241 ? -46.153  -69.478 45.588  1.00 33.42  ? 240 HIS G N   1 
ATOM   8470  C  CA  . HIS D  1 241 ? -45.373  -68.629 46.470  1.00 32.70  ? 240 HIS G CA  1 
ATOM   8471  C  C   . HIS D  1 241 ? -43.882  -68.890 46.224  1.00 37.86  ? 240 HIS G C   1 
ATOM   8472  O  O   . HIS D  1 241 ? -43.465  -70.020 45.973  1.00 37.51  ? 240 HIS G O   1 
ATOM   8473  C  CB  . HIS D  1 241 ? -45.749  -68.899 47.934  1.00 33.89  ? 240 HIS G CB  1 
ATOM   8474  C  CG  . HIS D  1 241 ? -44.963  -68.096 48.911  1.00 35.83  ? 240 HIS G CG  1 
ATOM   8475  N  ND1 . HIS D  1 241 ? -45.171  -66.746 49.083  1.00 35.82  ? 240 HIS G ND1 1 
ATOM   8476  C  CD2 . HIS D  1 241 ? -43.952  -68.437 49.741  1.00 34.28  ? 240 HIS G CD2 1 
ATOM   8477  C  CE1 . HIS D  1 241 ? -44.333  -66.294 49.992  1.00 39.63  ? 240 HIS G CE1 1 
ATOM   8478  N  NE2 . HIS D  1 241 ? -43.591  -67.312 50.419  1.00 36.84  ? 240 HIS G NE2 1 
ATOM   8479  N  N   . GLY D  1 242 ? -43.091  -67.821 46.267  1.00 33.10  ? 241 GLY G N   1 
ATOM   8480  C  CA  . GLY D  1 242 ? -41.660  -67.911 46.234  1.00 32.27  ? 241 GLY G CA  1 
ATOM   8481  C  C   . GLY D  1 242 ? -41.059  -66.719 46.932  1.00 33.30  ? 241 GLY G C   1 
ATOM   8482  O  O   . GLY D  1 242 ? -41.764  -65.953 47.628  1.00 34.33  ? 241 GLY G O   1 
ATOM   8483  N  N   . GLY D  1 243 ? -39.757  -66.538 46.729  1.00 32.06  ? 242 GLY G N   1 
ATOM   8484  C  CA  . GLY D  1 243 ? -39.075  -65.385 47.237  1.00 32.45  ? 242 GLY G CA  1 
ATOM   8485  C  C   . GLY D  1 243 ? -39.210  -64.258 46.226  1.00 31.90  ? 242 GLY G C   1 
ATOM   8486  O  O   . GLY D  1 243 ? -39.488  -64.528 45.064  1.00 31.83  ? 242 GLY G O   1 
ATOM   8487  N  N   . PRO D  1 244 ? -39.013  -62.989 46.635  1.00 31.88  ? 243 PRO G N   1 
ATOM   8488  C  CA  . PRO D  1 244 ? -39.171  -61.860 45.720  1.00 33.55  ? 243 PRO G CA  1 
ATOM   8489  C  C   . PRO D  1 244 ? -38.280  -61.963 44.469  1.00 37.67  ? 243 PRO G C   1 
ATOM   8490  O  O   . PRO D  1 244 ? -38.649  -61.465 43.415  1.00 33.23  ? 243 PRO G O   1 
ATOM   8491  C  CB  . PRO D  1 244 ? -38.837  -60.621 46.573  1.00 33.47  ? 243 PRO G CB  1 
ATOM   8492  C  CG  . PRO D  1 244 ? -38.197  -61.140 47.844  1.00 33.00  ? 243 PRO G CG  1 
ATOM   8493  C  CD  . PRO D  1 244 ? -38.637  -62.581 47.994  1.00 32.31  ? 243 PRO G CD  1 
ATOM   8494  N  N   . LYS D  1 245 ? -37.131  -62.638 44.571  1.00 39.11  ? 244 LYS G N   1 
ATOM   8495  C  CA  . LYS D  1 245 ? -36.210  -62.699 43.448  1.00 43.59  ? 244 LYS G CA  1 
ATOM   8496  C  C   . LYS D  1 245 ? -36.558  -63.857 42.497  1.00 41.87  ? 244 LYS G C   1 
ATOM   8497  O  O   . LYS D  1 245 ? -36.021  -63.915 41.419  1.00 43.82  ? 244 LYS G O   1 
ATOM   8498  C  CB  . LYS D  1 245 ? -34.779  -62.721 43.994  1.00 51.70  ? 244 LYS G CB  1 
ATOM   8499  C  CG  . LYS D  1 245 ? -34.379  -61.432 44.701  1.00 54.29  ? 244 LYS G CG  1 
ATOM   8500  C  CD  . LYS D  1 245 ? -33.439  -61.627 45.864  1.00 66.59  ? 244 LYS G CD  1 
ATOM   8501  C  CE  . LYS D  1 245 ? -32.095  -62.205 45.463  1.00 75.29  ? 244 LYS G CE  1 
ATOM   8502  N  NZ  . LYS D  1 245 ? -31.049  -61.903 46.471  1.00 78.63  ? 244 LYS G NZ  1 
ATOM   8503  N  N   . ASP D  1 246 ? -37.492  -64.741 42.860  1.00 41.15  ? 245 ASP G N   1 
ATOM   8504  C  CA  . ASP D  1 246 ? -37.894  -65.839 41.977  1.00 43.27  ? 245 ASP G CA  1 
ATOM   8505  C  C   . ASP D  1 246 ? -38.877  -65.352 40.907  1.00 47.55  ? 245 ASP G C   1 
ATOM   8506  O  O   . ASP D  1 246 ? -39.647  -64.418 41.139  1.00 41.16  ? 245 ASP G O   1 
ATOM   8507  C  CB  . ASP D  1 246 ? -38.586  -66.965 42.749  1.00 45.81  ? 245 ASP G CB  1 
ATOM   8508  C  CG  . ASP D  1 246 ? -37.721  -67.557 43.839  1.00 46.49  ? 245 ASP G CG  1 
ATOM   8509  O  OD1 . ASP D  1 246 ? -38.289  -67.973 44.870  1.00 43.92  ? 245 ASP G OD1 1 
ATOM   8510  O  OD2 . ASP D  1 246 ? -36.486  -67.584 43.647  1.00 50.84  ? 245 ASP G OD2 1 
ATOM   8511  N  N   . GLU D  1 247 ? -38.895  -66.057 39.770  1.00 46.38  ? 246 GLU G N   1 
ATOM   8512  C  CA  . GLU D  1 247 ? -39.883  -65.835 38.713  1.00 49.51  ? 246 GLU G CA  1 
ATOM   8513  C  C   . GLU D  1 247 ? -41.215  -66.456 39.170  1.00 45.57  ? 246 GLU G C   1 
ATOM   8514  O  O   . GLU D  1 247 ? -42.296  -65.850 38.998  1.00 42.35  ? 246 GLU G O   1 
ATOM   8515  C  CB  . GLU D  1 247 ? -39.348  -66.357 37.371  1.00 57.95  ? 246 GLU G CB  1 
ATOM   8516  C  CG  . GLU D  1 247 ? -40.426  -66.784 36.379  1.00 68.70  ? 246 GLU G CG  1 
ATOM   8517  C  CD  . GLU D  1 247 ? -41.044  -65.707 35.492  1.00 79.85  ? 246 GLU G CD  1 
ATOM   8518  O  OE1 . GLU D  1 247 ? -41.522  -66.068 34.387  1.00 87.34  ? 246 GLU G OE1 1 
ATOM   8519  O  OE2 . GLU D  1 247 ? -41.065  -64.515 35.897  1.00 81.48  ? 246 GLU G OE2 1 
ATOM   8520  N  N   . GLU D  1 248 ? -41.141  -67.638 39.793  1.00 36.56  ? 247 GLU G N   1 
ATOM   8521  C  CA  . GLU D  1 248 ? -42.316  -68.246 40.405  1.00 38.43  ? 247 GLU G CA  1 
ATOM   8522  C  C   . GLU D  1 248 ? -42.514  -67.625 41.798  1.00 36.79  ? 247 GLU G C   1 
ATOM   8523  O  O   . GLU D  1 248 ? -41.871  -68.007 42.785  1.00 37.32  ? 247 GLU G O   1 
ATOM   8524  C  CB  . GLU D  1 248 ? -42.214  -69.771 40.469  1.00 39.60  ? 247 GLU G CB  1 
ATOM   8525  C  CG  . GLU D  1 248 ? -43.549  -70.454 40.731  1.00 42.08  ? 247 GLU G CG  1 
ATOM   8526  C  CD  . GLU D  1 248 ? -44.560  -70.472 39.585  1.00 45.22  ? 247 GLU G CD  1 
ATOM   8527  O  OE1 . GLU D  1 248 ? -45.711  -70.920 39.823  1.00 42.88  ? 247 GLU G OE1 1 
ATOM   8528  O  OE2 . GLU D  1 248 ? -44.215  -70.040 38.461  1.00 49.62  ? 247 GLU G OE2 1 
ATOM   8529  N  N   . ARG D  1 249 ? -43.384  -66.610 41.843  1.00 33.40  ? 248 ARG G N   1 
ATOM   8530  C  CA  . ARG D  1 249 ? -43.747  -65.921 43.061  1.00 31.98  ? 248 ARG G CA  1 
ATOM   8531  C  C   . ARG D  1 249 ? -45.148  -65.331 42.873  1.00 32.81  ? 248 ARG G C   1 
ATOM   8532  O  O   . ARG D  1 249 ? -45.625  -65.190 41.749  1.00 32.26  ? 248 ARG G O   1 
ATOM   8533  C  CB  . ARG D  1 249 ? -42.740  -64.818 43.399  1.00 31.01  ? 248 ARG G CB  1 
ATOM   8534  C  CG  . ARG D  1 249 ? -42.635  -63.720 42.351  1.00 31.56  ? 248 ARG G CG  1 
ATOM   8535  C  CD  . ARG D  1 249 ? -41.837  -62.520 42.824  1.00 32.20  ? 248 ARG G CD  1 
ATOM   8536  N  NE  . ARG D  1 249 ? -42.626  -61.572 43.602  1.00 30.73  ? 248 ARG G NE  1 
ATOM   8537  C  CZ  . ARG D  1 249 ? -42.228  -60.344 43.914  1.00 29.87  ? 248 ARG G CZ  1 
ATOM   8538  N  NH1 . ARG D  1 249 ? -43.094  -59.490 44.442  1.00 27.41  ? 248 ARG G NH1 1 
ATOM   8539  N  NH2 . ARG D  1 249 ? -40.973  -59.966 43.708  1.00 24.51  ? 248 ARG G NH2 1 
ATOM   8540  N  N   . HIS D  1 250 ? -45.797  -65.040 43.997  1.00 29.70  ? 249 HIS G N   1 
ATOM   8541  C  CA  . HIS D  1 250 ? -46.964  -64.190 44.036  1.00 29.76  ? 249 HIS G CA  1 
ATOM   8542  C  C   . HIS D  1 250 ? -46.492  -62.751 43.822  1.00 27.56  ? 249 HIS G C   1 
ATOM   8543  O  O   . HIS D  1 250 ? -45.390  -62.391 44.215  1.00 28.29  ? 249 HIS G O   1 
ATOM   8544  C  CB  . HIS D  1 250 ? -47.693  -64.349 45.375  1.00 29.44  ? 249 HIS G CB  1 
ATOM   8545  C  CG  . HIS D  1 250 ? -48.116  -65.745 45.670  1.00 31.02  ? 249 HIS G CG  1 
ATOM   8546  N  ND1 . HIS D  1 250 ? -48.211  -66.256 46.955  1.00 31.37  ? 249 HIS G ND1 1 
ATOM   8547  C  CD2 . HIS D  1 250 ? -48.486  -66.740 44.841  1.00 31.71  ? 249 HIS G CD2 1 
ATOM   8548  C  CE1 . HIS D  1 250 ? -48.691  -67.475 46.891  1.00 31.82  ? 249 HIS G CE1 1 
ATOM   8549  N  NE2 . HIS D  1 250 ? -48.843  -67.802 45.611  1.00 30.64  ? 249 HIS G NE2 1 
ATOM   8550  N  N   . VAL D  1 251 ? -47.372  -61.891 43.285  1.00 27.82  ? 250 VAL G N   1 
ATOM   8551  C  CA  . VAL D  1 251 ? -47.060  -60.481 43.275  1.00 24.31  ? 250 VAL G CA  1 
ATOM   8552  C  C   . VAL D  1 251 ? -46.750  -59.996 44.707  1.00 22.29  ? 250 VAL G C   1 
ATOM   8553  O  O   . VAL D  1 251 ? -45.827  -59.208 44.929  1.00 23.35  ? 250 VAL G O   1 
ATOM   8554  C  CB  . VAL D  1 251 ? -48.175  -59.679 42.577  1.00 27.42  ? 250 VAL G CB  1 
ATOM   8555  C  CG1 . VAL D  1 251 ? -48.023  -58.185 42.787  1.00 28.12  ? 250 VAL G CG1 1 
ATOM   8556  C  CG2 . VAL D  1 251 ? -48.203  -60.001 41.092  1.00 28.09  ? 250 VAL G CG2 1 
ATOM   8557  N  N   . GLY D  1 252 ? -47.504  -60.483 45.681  1.00 21.60  ? 251 GLY G N   1 
ATOM   8558  C  CA  . GLY D  1 252 ? -47.381  -60.051 47.083  1.00 26.21  ? 251 GLY G CA  1 
ATOM   8559  C  C   . GLY D  1 252 ? -46.227  -60.676 47.869  1.00 26.17  ? 251 GLY G C   1 
ATOM   8560  O  O   . GLY D  1 252 ? -46.079  -60.368 49.049  1.00 27.87  ? 251 GLY G O   1 
ATOM   8561  N  N   A SER D  1 253 ? -45.422  -61.559 47.248  0.45 27.53  ? 252 SER G N   1 
ATOM   8562  C  CA  A SER D  1 253 ? -44.291  -62.240 47.955  0.45 27.84  ? 252 SER G CA  1 
ATOM   8563  C  C   A SER D  1 253 ? -43.103  -61.297 48.107  0.45 27.05  ? 252 SER G C   1 
ATOM   8564  O  O   A SER D  1 253 ? -42.212  -61.305 47.261  0.45 29.04  ? 252 SER G O   1 
ATOM   8565  C  CB  A SER D  1 253 ? -43.828  -63.494 47.252  0.45 27.05  ? 252 SER G CB  1 
ATOM   8566  O  OG  A SER D  1 253 ? -44.903  -64.283 46.781  0.45 27.87  ? 252 SER G OG  1 
ATOM   8567  N  N   B ASP D  1 253 ? -45.379  -61.472 47.202  0.55 26.64  ? 252 ASP G N   1 
ATOM   8568  C  CA  B ASP D  1 253 ? -44.277  -62.132 47.886  0.55 27.15  ? 252 ASP G CA  1 
ATOM   8569  C  C   B ASP D  1 253 ? -43.112  -61.174 48.045  0.55 26.52  ? 252 ASP G C   1 
ATOM   8570  O  O   B ASP D  1 253 ? -42.288  -61.022 47.145  0.55 29.20  ? 252 ASP G O   1 
ATOM   8571  C  CB  B ASP D  1 253 ? -43.840  -63.393 47.158  0.55 26.37  ? 252 ASP G CB  1 
ATOM   8572  C  CG  B ASP D  1 253 ? -44.889  -64.448 47.367  0.55 27.23  ? 252 ASP G CG  1 
ATOM   8573  O  OD1 B ASP D  1 253 ? -45.676  -64.270 48.310  0.55 29.84  ? 252 ASP G OD1 1 
ATOM   8574  O  OD2 B ASP D  1 253 ? -44.945  -65.383 46.570  0.55 27.12  ? 252 ASP G OD2 1 
ATOM   8575  N  N   . LEU D  1 254 ? -43.051  -60.550 49.218  1.00 26.68  ? 253 LEU G N   1 
ATOM   8576  C  CA  . LEU D  1 254 ? -41.980  -59.618 49.466  1.00 27.32  ? 253 LEU G CA  1 
ATOM   8577  C  C   . LEU D  1 254 ? -40.927  -60.235 50.400  1.00 28.17  ? 253 LEU G C   1 
ATOM   8578  O  O   . LEU D  1 254 ? -40.091  -59.520 50.904  1.00 30.82  ? 253 LEU G O   1 
ATOM   8579  C  CB  . LEU D  1 254 ? -42.575  -58.334 50.051  1.00 27.71  ? 253 LEU G CB  1 
ATOM   8580  C  CG  . LEU D  1 254 ? -43.447  -57.526 49.084  1.00 28.59  ? 253 LEU G CG  1 
ATOM   8581  C  CD1 . LEU D  1 254 ? -43.929  -56.268 49.768  1.00 29.53  ? 253 LEU G CD1 1 
ATOM   8582  C  CD2 . LEU D  1 254 ? -42.694  -57.182 47.802  1.00 27.86  ? 253 LEU G CD2 1 
ATOM   8583  N  N   . GLY D  1 255 ? -40.980  -61.547 50.653  1.00 28.65  ? 254 GLY G N   1 
ATOM   8584  C  CA  . GLY D  1 255 ? -39.909  -62.205 51.404  1.00 27.93  ? 254 GLY G CA  1 
ATOM   8585  C  C   . GLY D  1 255 ? -40.017  -61.996 52.895  1.00 27.16  ? 254 GLY G C   1 
ATOM   8586  O  O   . GLY D  1 255 ? -41.102  -62.086 53.484  1.00 25.40  ? 254 GLY G O   1 
ATOM   8587  N  N   . ASN D  1 256 ? -38.866  -61.728 53.507  1.00 26.14  ? 255 ASN G N   1 
ATOM   8588  C  CA  . ASN D  1 256 ? -38.739  -61.577 54.929  1.00 25.92  ? 255 ASN G CA  1 
ATOM   8589  C  C   . ASN D  1 256 ? -38.276  -60.168 55.286  1.00 24.25  ? 255 ASN G C   1 
ATOM   8590  O  O   . ASN D  1 256 ? -37.613  -59.514 54.499  1.00 28.63  ? 255 ASN G O   1 
ATOM   8591  C  CB  . ASN D  1 256 ? -37.689  -62.539 55.488  1.00 27.82  ? 255 ASN G CB  1 
ATOM   8592  C  CG  . ASN D  1 256 ? -38.178  -63.964 55.471  1.00 28.92  ? 255 ASN G CG  1 
ATOM   8593  O  OD1 . ASN D  1 256 ? -39.075  -64.319 56.235  1.00 31.18  ? 255 ASN G OD1 1 
ATOM   8594  N  ND2 . ASN D  1 256 ? -37.618  -64.777 54.588  1.00 28.50  ? 255 ASN G ND2 1 
ATOM   8595  N  N   . VAL D  1 257 ? -38.602  -59.759 56.514  1.00 23.86  ? 256 VAL G N   1 
ATOM   8596  C  CA  . VAL D  1 257 ? -37.961  -58.656 57.166  1.00 25.16  ? 256 VAL G CA  1 
ATOM   8597  C  C   . VAL D  1 257 ? -37.318  -59.172 58.461  1.00 26.54  ? 256 VAL G C   1 
ATOM   8598  O  O   . VAL D  1 257 ? -37.799  -60.133 59.072  1.00 28.76  ? 256 VAL G O   1 
ATOM   8599  C  CB  . VAL D  1 257 ? -38.937  -57.488 57.426  1.00 24.26  ? 256 VAL G CB  1 
ATOM   8600  C  CG1 . VAL D  1 257 ? -39.501  -56.977 56.105  1.00 24.96  ? 256 VAL G CG1 1 
ATOM   8601  C  CG2 . VAL D  1 257 ? -40.034  -57.874 58.392  1.00 25.03  ? 256 VAL G CG2 1 
ATOM   8602  N  N   . THR D  1 258 ? -36.251  -58.493 58.873  1.00 28.02  ? 257 THR G N   1 
ATOM   8603  C  CA  . THR D  1 258 ? -35.438  -58.933 60.001  1.00 30.36  ? 257 THR G CA  1 
ATOM   8604  C  C   . THR D  1 258 ? -35.580  -57.937 61.153  1.00 28.82  ? 257 THR G C   1 
ATOM   8605  O  O   . THR D  1 258 ? -35.276  -56.762 60.998  1.00 30.41  ? 257 THR G O   1 
ATOM   8606  C  CB  . THR D  1 258 ? -33.966  -59.080 59.586  1.00 33.71  ? 257 THR G CB  1 
ATOM   8607  O  OG1 . THR D  1 258 ? -33.887  -60.041 58.533  1.00 30.06  ? 257 THR G OG1 1 
ATOM   8608  C  CG2 . THR D  1 258 ? -33.074  -59.487 60.742  1.00 37.09  ? 257 THR G CG2 1 
ATOM   8609  N  N   . ALA D  1 259 ? -36.023  -58.451 62.304  1.00 27.83  ? 258 ALA G N   1 
ATOM   8610  C  CA  . ALA D  1 259 ? -36.041  -57.687 63.542  1.00 32.98  ? 258 ALA G CA  1 
ATOM   8611  C  C   . ALA D  1 259 ? -34.722  -57.914 64.299  1.00 33.25  ? 258 ALA G C   1 
ATOM   8612  O  O   . ALA D  1 259 ? -34.233  -59.038 64.407  1.00 33.82  ? 258 ALA G O   1 
ATOM   8613  C  CB  . ALA D  1 259 ? -37.228  -58.080 64.386  1.00 31.84  ? 258 ALA G CB  1 
ATOM   8614  N  N   . ASP D  1 260 ? -34.163  -56.813 64.789  1.00 34.67  ? 259 ASP G N   1 
ATOM   8615  C  CA  . ASP D  1 260 ? -32.979  -56.797 65.604  1.00 37.24  ? 259 ASP G CA  1 
ATOM   8616  C  C   . ASP D  1 260 ? -33.391  -57.185 67.033  1.00 42.75  ? 259 ASP G C   1 
ATOM   8617  O  O   . ASP D  1 260 ? -34.534  -57.618 67.311  1.00 40.11  ? 259 ASP G O   1 
ATOM   8618  C  CB  . ASP D  1 260 ? -32.276  -55.444 65.477  1.00 35.01  ? 259 ASP G CB  1 
ATOM   8619  C  CG  . ASP D  1 260 ? -33.011  -54.281 66.122  1.00 34.56  ? 259 ASP G CG  1 
ATOM   8620  O  OD1 . ASP D  1 260 ? -32.678  -53.132 65.805  1.00 35.83  ? 259 ASP G OD1 1 
ATOM   8621  O  OD2 . ASP D  1 260 ? -33.904  -54.537 66.943  1.00 36.38  ? 259 ASP G OD2 1 
ATOM   8622  N  N   . LYS D  1 261 ? -32.448  -57.080 67.964  1.00 46.94  ? 260 LYS G N   1 
ATOM   8623  C  CA  . LYS D  1 261 ? -32.693  -57.676 69.266  1.00 48.88  ? 260 LYS G CA  1 
ATOM   8624  C  C   . LYS D  1 261 ? -33.437  -56.676 70.161  1.00 43.55  ? 260 LYS G C   1 
ATOM   8625  O  O   . LYS D  1 261 ? -33.824  -57.027 71.253  1.00 50.40  ? 260 LYS G O   1 
ATOM   8626  C  CB  . LYS D  1 261 ? -31.387  -58.227 69.848  1.00 57.02  ? 260 LYS G CB  1 
ATOM   8627  C  CG  . LYS D  1 261 ? -30.298  -57.207 70.141  1.00 60.81  ? 260 LYS G CG  1 
ATOM   8628  C  CD  . LYS D  1 261 ? -29.019  -57.887 70.615  1.00 72.50  ? 260 LYS G CD  1 
ATOM   8629  C  CE  . LYS D  1 261 ? -28.159  -57.009 71.501  1.00 76.45  ? 260 LYS G CE  1 
ATOM   8630  N  NZ  . LYS D  1 261 ? -27.807  -55.741 70.820  1.00 78.51  ? 260 LYS G NZ  1 
ATOM   8631  N  N   . ASP D  1 262 ? -33.652  -55.448 69.671  1.00 42.46  ? 261 ASP G N   1 
ATOM   8632  C  CA  . ASP D  1 262 ? -34.596  -54.483 70.260  1.00 44.63  ? 261 ASP G CA  1 
ATOM   8633  C  C   . ASP D  1 262 ? -36.027  -54.682 69.716  1.00 42.49  ? 261 ASP G C   1 
ATOM   8634  O  O   . ASP D  1 262 ? -36.899  -53.880 69.997  1.00 45.06  ? 261 ASP G O   1 
ATOM   8635  C  CB  . ASP D  1 262 ? -34.124  -53.052 69.990  1.00 47.09  ? 261 ASP G CB  1 
ATOM   8636  C  CG  . ASP D  1 262 ? -32.921  -52.644 70.819  1.00 55.20  ? 261 ASP G CG  1 
ATOM   8637  O  OD1 . ASP D  1 262 ? -32.269  -51.648 70.454  1.00 61.71  ? 261 ASP G OD1 1 
ATOM   8638  O  OD2 . ASP D  1 262 ? -32.652  -53.320 71.828  1.00 63.65  ? 261 ASP G OD2 1 
ATOM   8639  N  N   . GLY D  1 263 ? -36.253  -55.727 68.916  1.00 40.56  ? 262 GLY G N   1 
ATOM   8640  C  CA  . GLY D  1 263 ? -37.562  -56.059 68.320  1.00 41.18  ? 262 GLY G CA  1 
ATOM   8641  C  C   . GLY D  1 263 ? -37.979  -55.143 67.164  1.00 37.69  ? 262 GLY G C   1 
ATOM   8642  O  O   . GLY D  1 263 ? -39.154  -55.089 66.822  1.00 37.93  ? 262 GLY G O   1 
ATOM   8643  N  N   . VAL D  1 264 ? -37.018  -54.443 66.557  1.00 35.59  ? 263 VAL G N   1 
ATOM   8644  C  CA  . VAL D  1 264 ? -37.258  -53.492 65.506  1.00 34.81  ? 263 VAL G CA  1 
ATOM   8645  C  C   . VAL D  1 264 ? -36.740  -54.030 64.168  1.00 36.11  ? 263 VAL G C   1 
ATOM   8646  O  O   . VAL D  1 264 ? -35.557  -54.397 64.022  1.00 31.77  ? 263 VAL G O   1 
ATOM   8647  C  CB  . VAL D  1 264 ? -36.595  -52.147 65.817  1.00 36.65  ? 263 VAL G CB  1 
ATOM   8648  C  CG1 . VAL D  1 264 ? -36.872  -51.137 64.719  1.00 37.12  ? 263 VAL G CG1 1 
ATOM   8649  C  CG2 . VAL D  1 264 ? -37.011  -51.609 67.178  1.00 38.47  ? 263 VAL G CG2 1 
ATOM   8650  N  N   . ALA D  1 265 ? -37.633  -54.021 63.173  1.00 34.21  ? 264 ALA G N   1 
ATOM   8651  C  CA  . ALA D  1 265 ? -37.274  -54.274 61.770  1.00 30.50  ? 264 ALA G CA  1 
ATOM   8652  C  C   . ALA D  1 265 ? -37.241  -52.947 61.018  1.00 31.17  ? 264 ALA G C   1 
ATOM   8653  O  O   . ALA D  1 265 ? -38.275  -52.297 60.850  1.00 30.19  ? 264 ALA G O   1 
ATOM   8654  C  CB  . ALA D  1 265 ? -38.243  -55.244 61.151  1.00 28.10  ? 264 ALA G CB  1 
ATOM   8655  N  N   . ASP D  1 266 ? -36.042  -52.531 60.618  1.00 31.09  ? 265 ASP G N   1 
ATOM   8656  C  CA  . ASP D  1 266 ? -35.844  -51.371 59.821  1.00 32.04  ? 265 ASP G CA  1 
ATOM   8657  C  C   . ASP D  1 266 ? -35.918  -51.797 58.355  1.00 31.83  ? 265 ASP G C   1 
ATOM   8658  O  O   . ASP D  1 266 ? -34.884  -52.047 57.676  1.00 30.14  ? 265 ASP G O   1 
ATOM   8659  C  CB  . ASP D  1 266 ? -34.542  -50.643 60.157  1.00 37.14  ? 265 ASP G CB  1 
ATOM   8660  C  CG  . ASP D  1 266 ? -34.567  -49.949 61.510  1.00 44.67  ? 265 ASP G CG  1 
ATOM   8661  O  OD1 . ASP D  1 266 ? -35.582  -49.279 61.822  1.00 48.21  ? 265 ASP G OD1 1 
ATOM   8662  O  OD2 . ASP D  1 266 ? -33.574  -50.086 62.247  1.00 49.67  ? 265 ASP G OD2 1 
ATOM   8663  N  N   . VAL D  1 267 ? -37.152  -51.805 57.850  1.00 27.21  ? 266 VAL G N   1 
ATOM   8664  C  CA  . VAL D  1 267 ? -37.465  -52.396 56.565  1.00 26.87  ? 266 VAL G CA  1 
ATOM   8665  C  C   . VAL D  1 267 ? -36.834  -51.554 55.462  1.00 26.27  ? 266 VAL G C   1 
ATOM   8666  O  O   . VAL D  1 267 ? -36.898  -50.340 55.472  1.00 28.08  ? 266 VAL G O   1 
ATOM   8667  C  CB  . VAL D  1 267 ? -38.983  -52.553 56.367  1.00 28.56  ? 266 VAL G CB  1 
ATOM   8668  C  CG1 . VAL D  1 267 ? -39.304  -53.144 55.015  1.00 27.76  ? 266 VAL G CG1 1 
ATOM   8669  C  CG2 . VAL D  1 267 ? -39.612  -53.387 57.472  1.00 29.24  ? 266 VAL G CG2 1 
ATOM   8670  N  N   . SER D  1 268 ? -36.260  -52.234 54.473  1.00 28.08  ? 267 SER G N   1 
ATOM   8671  C  CA  . SER D  1 268 ? -35.712  -51.565 53.305  1.00 30.44  ? 267 SER G CA  1 
ATOM   8672  C  C   . SER D  1 268 ? -35.660  -52.565 52.156  1.00 33.37  ? 267 SER G C   1 
ATOM   8673  O  O   . SER D  1 268 ? -34.749  -53.382 52.093  1.00 32.61  ? 267 SER G O   1 
ATOM   8674  C  CB  . SER D  1 268 ? -34.339  -50.977 53.574  1.00 35.58  ? 267 SER G CB  1 
ATOM   8675  O  OG  . SER D  1 268 ? -33.888  -50.203 52.465  1.00 36.41  ? 267 SER G OG  1 
ATOM   8676  N  N   . ILE D  1 269 ? -36.657  -52.486 51.278  1.00 29.33  ? 268 ILE G N   1 
ATOM   8677  C  CA  . ILE D  1 269 ? -36.871  -53.410 50.196  1.00 29.37  ? 268 ILE G CA  1 
ATOM   8678  C  C   . ILE D  1 269 ? -37.119  -52.570 48.942  1.00 30.79  ? 268 ILE G C   1 
ATOM   8679  O  O   . ILE D  1 269 ? -37.687  -51.470 49.027  1.00 31.14  ? 268 ILE G O   1 
ATOM   8680  C  CB  . ILE D  1 269 ? -38.070  -54.322 50.535  1.00 31.56  ? 268 ILE G CB  1 
ATOM   8681  C  CG1 . ILE D  1 269 ? -37.696  -55.386 51.564  1.00 31.59  ? 268 ILE G CG1 1 
ATOM   8682  C  CG2 . ILE D  1 269 ? -38.692  -54.961 49.298  1.00 34.01  ? 268 ILE G CG2 1 
ATOM   8683  C  CD1 . ILE D  1 269 ? -38.898  -56.058 52.189  1.00 32.32  ? 268 ILE G CD1 1 
ATOM   8684  N  N   . GLU D  1 270 ? -36.690  -53.091 47.796  1.00 28.40  ? 269 GLU G N   1 
ATOM   8685  C  CA  . GLU D  1 270 ? -37.026  -52.546 46.507  1.00 32.87  ? 269 GLU G CA  1 
ATOM   8686  C  C   . GLU D  1 270 ? -37.554  -53.699 45.657  1.00 31.90  ? 269 GLU G C   1 
ATOM   8687  O  O   . GLU D  1 270 ? -36.930  -54.765 45.606  1.00 31.45  ? 269 GLU G O   1 
ATOM   8688  C  CB  . GLU D  1 270 ? -35.821  -51.853 45.880  1.00 36.09  ? 269 GLU G CB  1 
ATOM   8689  C  CG  . GLU D  1 270 ? -36.130  -51.290 44.507  1.00 44.00  ? 269 GLU G CG  1 
ATOM   8690  C  CD  . GLU D  1 270 ? -34.955  -50.666 43.762  1.00 50.29  ? 269 GLU G CD  1 
ATOM   8691  O  OE1 . GLU D  1 270 ? -34.366  -49.704 44.298  1.00 56.09  ? 269 GLU G OE1 1 
ATOM   8692  O  OE2 . GLU D  1 270 ? -34.652  -51.134 42.632  1.00 56.12  ? 269 GLU G OE2 1 
ATOM   8693  N  N   . ASP D  1 271 ? -38.751  -53.526 45.079  1.00 28.68  ? 270 ASP G N   1 
ATOM   8694  C  CA  . ASP D  1 271 ? -39.387  -54.619 44.341  1.00 28.88  ? 270 ASP G CA  1 
ATOM   8695  C  C   . ASP D  1 271 ? -39.914  -54.106 43.003  1.00 28.95  ? 270 ASP G C   1 
ATOM   8696  O  O   . ASP D  1 271 ? -40.438  -53.010 42.942  1.00 28.54  ? 270 ASP G O   1 
ATOM   8697  C  CB  . ASP D  1 271 ? -40.516  -55.270 45.135  1.00 28.55  ? 270 ASP G CB  1 
ATOM   8698  C  CG  . ASP D  1 271 ? -40.968  -56.586 44.520  1.00 33.08  ? 270 ASP G CG  1 
ATOM   8699  O  OD1 . ASP D  1 271 ? -42.048  -56.616 43.857  1.00 29.42  ? 270 ASP G OD1 1 
ATOM   8700  O  OD2 . ASP D  1 271 ? -40.251  -57.589 44.709  1.00 34.60  ? 270 ASP G OD2 1 
ATOM   8701  N  N   . SER D  1 272 ? -39.803  -54.943 41.966  1.00 27.06  ? 271 SER G N   1 
ATOM   8702  C  CA  . SER D  1 272 ? -40.092  -54.556 40.593  1.00 27.27  ? 271 SER G CA  1 
ATOM   8703  C  C   . SER D  1 272 ? -41.354  -55.304 40.103  1.00 26.80  ? 271 SER G C   1 
ATOM   8704  O  O   . SER D  1 272 ? -41.779  -55.186 38.961  1.00 29.56  ? 271 SER G O   1 
ATOM   8705  C  CB  . SER D  1 272 ? -38.812  -54.734 39.715  1.00 27.91  ? 271 SER G CB  1 
ATOM   8706  O  OG  A SER D  1 272 ? -38.954  -56.142 39.631  0.60 30.29  ? 271 SER G OG  1 
ATOM   8707  O  OG  B SER D  1 272 ? -38.481  -53.354 39.798  0.40 26.90  ? 271 SER G OG  1 
ATOM   8708  N  N   . VAL D  1 273 ? -42.021  -56.041 40.991  1.00 24.38  ? 272 VAL G N   1 
ATOM   8709  C  CA  . VAL D  1 273 ? -43.178  -56.793 40.581  1.00 25.57  ? 272 VAL G CA  1 
ATOM   8710  C  C   . VAL D  1 273 ? -44.457  -56.130 41.122  1.00 26.41  ? 272 VAL G C   1 
ATOM   8711  O  O   . VAL D  1 273 ? -45.479  -56.110 40.430  1.00 25.48  ? 272 VAL G O   1 
ATOM   8712  C  CB  . VAL D  1 273 ? -43.056  -58.267 41.008  1.00 25.51  ? 272 VAL G CB  1 
ATOM   8713  C  CG1 . VAL D  1 273 ? -44.340  -59.014 40.756  1.00 26.21  ? 272 VAL G CG1 1 
ATOM   8714  C  CG2 . VAL D  1 273 ? -41.892  -58.961 40.289  1.00 27.16  ? 272 VAL G CG2 1 
ATOM   8715  N  N   . ILE D  1 274 ? -44.429  -55.700 42.384  1.00 25.27  ? 273 ILE G N   1 
ATOM   8716  C  CA  . ILE D  1 274 ? -45.532  -54.901 42.936  1.00 24.97  ? 273 ILE G CA  1 
ATOM   8717  C  C   . ILE D  1 274 ? -45.507  -53.544 42.224  1.00 24.47  ? 273 ILE G C   1 
ATOM   8718  O  O   . ILE D  1 274 ? -44.450  -53.089 41.733  1.00 23.63  ? 273 ILE G O   1 
ATOM   8719  C  CB  . ILE D  1 274 ? -45.441  -54.716 44.464  1.00 23.77  ? 273 ILE G CB  1 
ATOM   8720  C  CG1 . ILE D  1 274 ? -44.115  -54.071 44.886  1.00 23.50  ? 273 ILE G CG1 1 
ATOM   8721  C  CG2 . ILE D  1 274 ? -45.701  -56.028 45.183  1.00 26.65  ? 273 ILE G CG2 1 
ATOM   8722  C  CD1 . ILE D  1 274 ? -44.119  -53.442 46.265  1.00 23.69  ? 273 ILE G CD1 1 
ATOM   8723  N  N   . SER D  1 275 ? -46.662  -52.873 42.249  1.00 24.22  ? 274 SER G N   1 
ATOM   8724  C  CA  . SER D  1 275 ? -46.815  -51.512 41.729  1.00 21.75  ? 274 SER G CA  1 
ATOM   8725  C  C   . SER D  1 275 ? -47.767  -50.741 42.638  1.00 22.19  ? 274 SER G C   1 
ATOM   8726  O  O   . SER D  1 275 ? -48.469  -51.328 43.433  1.00 22.62  ? 274 SER G O   1 
ATOM   8727  C  CB  . SER D  1 275 ? -47.332  -51.553 40.307  1.00 22.84  ? 274 SER G CB  1 
ATOM   8728  O  OG  . SER D  1 275 ? -47.161  -50.296 39.681  1.00 24.91  ? 274 SER G OG  1 
ATOM   8729  N  N   . LEU D  1 276 ? -47.775  -49.411 42.507  1.00 23.81  ? 275 LEU G N   1 
ATOM   8730  C  CA  . LEU D  1 276 ? -48.744  -48.583 43.198  1.00 22.30  ? 275 LEU G CA  1 
ATOM   8731  C  C   . LEU D  1 276 ? -49.823  -48.115 42.216  1.00 25.87  ? 275 LEU G C   1 
ATOM   8732  O  O   . LEU D  1 276 ? -50.636  -47.260 42.551  1.00 26.20  ? 275 LEU G O   1 
ATOM   8733  C  CB  . LEU D  1 276 ? -48.024  -47.394 43.832  1.00 22.15  ? 275 LEU G CB  1 
ATOM   8734  C  CG  . LEU D  1 276 ? -46.933  -47.737 44.838  1.00 23.06  ? 275 LEU G CG  1 
ATOM   8735  C  CD1 . LEU D  1 276 ? -46.419  -46.478 45.505  1.00 21.99  ? 275 LEU G CD1 1 
ATOM   8736  C  CD2 . LEU D  1 276 ? -47.413  -48.741 45.876  1.00 22.78  ? 275 LEU G CD2 1 
ATOM   8737  N  N   . SER D  1 277 ? -49.829  -48.683 41.012  1.00 24.35  ? 276 SER G N   1 
ATOM   8738  C  CA  . SER D  1 277 ? -50.857  -48.417 40.023  1.00 26.56  ? 276 SER G CA  1 
ATOM   8739  C  C   . SER D  1 277 ? -50.955  -49.613 39.082  1.00 26.65  ? 276 SER G C   1 
ATOM   8740  O  O   . SER D  1 277 ? -50.064  -50.482 39.054  1.00 24.94  ? 276 SER G O   1 
ATOM   8741  C  CB  . SER D  1 277 ? -50.601  -47.127 39.265  1.00 27.20  ? 276 SER G CB  1 
ATOM   8742  O  OG  . SER D  1 277 ? -49.360  -47.157 38.574  1.00 29.30  ? 276 SER G OG  1 
ATOM   8743  N  N   . GLY D  1 278 ? -52.070  -49.664 38.353  1.00 26.37  ? 277 GLY G N   1 
ATOM   8744  C  CA  . GLY D  1 278 ? -52.308  -50.636 37.321  1.00 27.17  ? 277 GLY G CA  1 
ATOM   8745  C  C   . GLY D  1 278 ? -52.546  -52.038 37.855  1.00 28.02  ? 277 GLY G C   1 
ATOM   8746  O  O   . GLY D  1 278 ? -52.999  -52.242 38.972  1.00 27.32  ? 277 GLY G O   1 
ATOM   8747  N  N   . ASP D  1 279 ? -52.206  -53.011 37.010  1.00 27.98  ? 278 ASP G N   1 
ATOM   8748  C  CA  . ASP D  1 279 ? -52.484  -54.422 37.184  1.00 31.35  ? 278 ASP G CA  1 
ATOM   8749  C  C   . ASP D  1 279 ? -52.020  -54.939 38.551  1.00 28.88  ? 278 ASP G C   1 
ATOM   8750  O  O   . ASP D  1 279 ? -52.748  -55.656 39.225  1.00 29.44  ? 278 ASP G O   1 
ATOM   8751  C  CB  . ASP D  1 279 ? -51.740  -55.218 36.110  1.00 36.46  ? 278 ASP G CB  1 
ATOM   8752  C  CG  . ASP D  1 279 ? -51.937  -54.649 34.706  1.00 39.37  ? 278 ASP G CG  1 
ATOM   8753  O  OD1 . ASP D  1 279 ? -51.431  -53.494 34.405  1.00 34.74  ? 278 ASP G OD1 1 
ATOM   8754  O  OD2 . ASP D  1 279 ? -52.653  -55.320 33.947  1.00 44.38  ? 278 ASP G OD2 1 
ATOM   8755  N  N   . HIS D  1 280 ? -50.797  -54.576 38.929  1.00 24.50  ? 279 HIS G N   1 
ATOM   8756  C  CA  . HIS D  1 280 ? -50.137  -55.149 40.117  1.00 26.88  ? 279 HIS G CA  1 
ATOM   8757  C  C   . HIS D  1 280 ? -50.222  -54.183 41.289  1.00 24.99  ? 279 HIS G C   1 
ATOM   8758  O  O   . HIS D  1 280 ? -49.500  -54.364 42.258  1.00 25.34  ? 279 HIS G O   1 
ATOM   8759  C  CB  . HIS D  1 280 ? -48.679  -55.518 39.809  1.00 26.01  ? 279 HIS G CB  1 
ATOM   8760  C  CG  . HIS D  1 280 ? -48.588  -56.745 38.969  1.00 29.71  ? 279 HIS G CG  1 
ATOM   8761  N  ND1 . HIS D  1 280 ? -47.376  -57.268 38.542  1.00 32.17  ? 279 HIS G ND1 1 
ATOM   8762  C  CD2 . HIS D  1 280 ? -49.555  -57.502 38.418  1.00 29.58  ? 279 HIS G CD2 1 
ATOM   8763  C  CE1 . HIS D  1 280 ? -47.616  -58.322 37.792  1.00 34.25  ? 279 HIS G CE1 1 
ATOM   8764  N  NE2 . HIS D  1 280 ? -48.942  -58.485 37.690  1.00 29.83  ? 279 HIS G NE2 1 
ATOM   8765  N  N   . SER D  1 281 ? -51.130  -53.195 41.184  1.00 23.80  ? 280 SER G N   1 
ATOM   8766  C  CA  . SER D  1 281 ? -51.345  -52.218 42.222  1.00 23.97  ? 280 SER G CA  1 
ATOM   8767  C  C   . SER D  1 281 ? -51.661  -52.917 43.541  1.00 20.38  ? 280 SER G C   1 
ATOM   8768  O  O   . SER D  1 281 ? -52.520  -53.760 43.580  1.00 23.20  ? 280 SER G O   1 
ATOM   8769  C  CB  . SER D  1 281 ? -52.463  -51.280 41.894  1.00 23.93  ? 280 SER G CB  1 
ATOM   8770  O  OG  . SER D  1 281 ? -52.611  -50.376 42.965  1.00 24.02  ? 280 SER G OG  1 
ATOM   8771  N  N   . ILE D  1 282 ? -51.008  -52.473 44.607  1.00 21.59  ? 281 ILE G N   1 
ATOM   8772  C  CA  . ILE D  1 282 ? -51.241  -52.972 45.949  1.00 21.83  ? 281 ILE G CA  1 
ATOM   8773  C  C   . ILE D  1 282 ? -52.047  -51.945 46.769  1.00 21.81  ? 281 ILE G C   1 
ATOM   8774  O  O   . ILE D  1 282 ? -52.329  -52.186 47.936  1.00 20.34  ? 281 ILE G O   1 
ATOM   8775  C  CB  . ILE D  1 282 ? -49.902  -53.329 46.633  1.00 23.90  ? 281 ILE G CB  1 
ATOM   8776  C  CG1 . ILE D  1 282 ? -49.014  -52.099 46.847  1.00 24.22  ? 281 ILE G CG1 1 
ATOM   8777  C  CG2 . ILE D  1 282 ? -49.198  -54.449 45.860  1.00 25.61  ? 281 ILE G CG2 1 
ATOM   8778  C  CD1 . ILE D  1 282 ? -47.734  -52.380 47.616  1.00 25.23  ? 281 ILE G CD1 1 
ATOM   8779  N  N   . ILE D  1 283 ? -52.429  -50.822 46.155  1.00 22.15  ? 282 ILE G N   1 
ATOM   8780  C  CA  . ILE D  1 283 ? -53.287  -49.809 46.823  1.00 22.91  ? 282 ILE G CA  1 
ATOM   8781  C  C   . ILE D  1 283 ? -54.612  -50.462 47.182  1.00 21.05  ? 282 ILE G C   1 
ATOM   8782  O  O   . ILE D  1 283 ? -55.260  -51.083 46.361  1.00 20.41  ? 282 ILE G O   1 
ATOM   8783  C  CB  . ILE D  1 283 ? -53.517  -48.557 45.965  1.00 24.98  ? 282 ILE G CB  1 
ATOM   8784  C  CG1 . ILE D  1 283 ? -52.206  -47.910 45.518  1.00 24.59  ? 282 ILE G CG1 1 
ATOM   8785  C  CG2 . ILE D  1 283 ? -54.435  -47.579 46.690  1.00 24.73  ? 282 ILE G CG2 1 
ATOM   8786  C  CD1 . ILE D  1 283 ? -51.366  -47.370 46.631  1.00 26.22  ? 282 ILE G CD1 1 
ATOM   8787  N  N   . GLY D  1 284 ? -54.971  -50.362 48.461  1.00 19.65  ? 283 GLY G N   1 
ATOM   8788  C  CA  . GLY D  1 284 ? -56.235  -50.908 48.943  1.00 19.63  ? 283 GLY G CA  1 
ATOM   8789  C  C   . GLY D  1 284 ? -56.143  -52.388 49.277  1.00 19.54  ? 283 GLY G C   1 
ATOM   8790  O  O   . GLY D  1 284 ? -57.139  -53.013 49.562  1.00 20.02  ? 283 GLY G O   1 
ATOM   8791  N  N   . ARG D  1 285 ? -54.933  -52.954 49.258  1.00 20.50  ? 284 ARG G N   1 
ATOM   8792  C  CA  . ARG D  1 285 ? -54.737  -54.334 49.701  1.00 21.97  ? 284 ARG G CA  1 
ATOM   8793  C  C   . ARG D  1 285 ? -54.087  -54.262 51.090  1.00 22.82  ? 284 ARG G C   1 
ATOM   8794  O  O   . ARG D  1 285 ? -53.944  -53.179 51.647  1.00 23.17  ? 284 ARG G O   1 
ATOM   8795  C  CB  . ARG D  1 285 ? -53.966  -55.125 48.635  1.00 22.85  ? 284 ARG G CB  1 
ATOM   8796  C  CG  . ARG D  1 285 ? -54.537  -54.968 47.229  1.00 23.27  ? 284 ARG G CG  1 
ATOM   8797  C  CD  . ARG D  1 285 ? -53.970  -55.918 46.203  1.00 23.75  ? 284 ARG G CD  1 
ATOM   8798  N  NE  . ARG D  1 285 ? -54.506  -55.706 44.861  1.00 22.81  ? 284 ARG G NE  1 
ATOM   8799  C  CZ  . ARG D  1 285 ? -55.615  -56.246 44.370  1.00 21.71  ? 284 ARG G CZ  1 
ATOM   8800  N  NH1 . ARG D  1 285 ? -55.933  -56.006 43.102  1.00 21.87  ? 284 ARG G NH1 1 
ATOM   8801  N  NH2 . ARG D  1 285 ? -56.364  -57.043 45.116  1.00 21.54  ? 284 ARG G NH2 1 
ATOM   8802  N  N   . THR D  1 286 ? -53.720  -55.408 51.654  1.00 22.97  ? 285 THR G N   1 
ATOM   8803  C  CA  . THR D  1 286 ? -53.296  -55.480 53.047  1.00 23.30  ? 285 THR G CA  1 
ATOM   8804  C  C   . THR D  1 286 ? -51.838  -55.935 53.095  1.00 25.48  ? 285 THR G C   1 
ATOM   8805  O  O   . THR D  1 286 ? -51.481  -56.928 52.488  1.00 24.90  ? 285 THR G O   1 
ATOM   8806  C  CB  . THR D  1 286 ? -54.168  -56.431 53.869  1.00 25.30  ? 285 THR G CB  1 
ATOM   8807  O  OG1 . THR D  1 286 ? -55.498  -55.925 53.970  1.00 26.30  ? 285 THR G OG1 1 
ATOM   8808  C  CG2 . THR D  1 286 ? -53.653  -56.667 55.272  1.00 25.82  ? 285 THR G CG2 1 
ATOM   8809  N  N   . LEU D  1 287 ? -51.021  -55.211 53.858  1.00 24.46  ? 286 LEU G N   1 
ATOM   8810  C  CA  . LEU D  1 287 ? -49.668  -55.604 54.153  1.00 24.57  ? 286 LEU G CA  1 
ATOM   8811  C  C   . LEU D  1 287 ? -49.715  -56.386 55.463  1.00 25.25  ? 286 LEU G C   1 
ATOM   8812  O  O   . LEU D  1 287 ? -50.378  -55.947 56.392  1.00 22.92  ? 286 LEU G O   1 
ATOM   8813  C  CB  . LEU D  1 287 ? -48.794  -54.360 54.293  1.00 25.17  ? 286 LEU G CB  1 
ATOM   8814  C  CG  . LEU D  1 287 ? -47.308  -54.639 54.487  1.00 25.74  ? 286 LEU G CG  1 
ATOM   8815  C  CD1 . LEU D  1 287 ? -46.706  -55.279 53.247  1.00 25.57  ? 286 LEU G CD1 1 
ATOM   8816  C  CD2 . LEU D  1 287 ? -46.568  -53.366 54.837  1.00 24.65  ? 286 LEU G CD2 1 
ATOM   8817  N  N   . VAL D  1 288 ? -49.035  -57.542 55.495  1.00 24.11  ? 287 VAL G N   1 
ATOM   8818  C  CA  . VAL D  1 288 ? -49.034  -58.440 56.654  1.00 25.82  ? 287 VAL G CA  1 
ATOM   8819  C  C   . VAL D  1 288 ? -47.583  -58.723 57.065  1.00 26.77  ? 287 VAL G C   1 
ATOM   8820  O  O   . VAL D  1 288 ? -46.717  -59.033 56.210  1.00 25.51  ? 287 VAL G O   1 
ATOM   8821  C  CB  . VAL D  1 288 ? -49.788  -59.755 56.387  1.00 27.54  ? 287 VAL G CB  1 
ATOM   8822  C  CG1 . VAL D  1 288 ? -49.710  -60.702 57.584  1.00 29.77  ? 287 VAL G CG1 1 
ATOM   8823  C  CG2 . VAL D  1 288 ? -51.255  -59.523 56.025  1.00 28.46  ? 287 VAL G CG2 1 
ATOM   8824  N  N   . VAL D  1 289 ? -47.327  -58.640 58.373  1.00 25.55  ? 288 VAL G N   1 
ATOM   8825  C  CA  . VAL D  1 289 ? -46.084  -59.162 58.940  1.00 26.72  ? 288 VAL G CA  1 
ATOM   8826  C  C   . VAL D  1 289 ? -46.424  -60.398 59.789  1.00 29.11  ? 288 VAL G C   1 
ATOM   8827  O  O   . VAL D  1 289 ? -47.376  -60.400 60.587  1.00 27.94  ? 288 VAL G O   1 
ATOM   8828  C  CB  . VAL D  1 289 ? -45.295  -58.087 59.714  1.00 28.39  ? 288 VAL G CB  1 
ATOM   8829  C  CG1 . VAL D  1 289 ? -46.074  -57.568 60.906  1.00 30.82  ? 288 VAL G CG1 1 
ATOM   8830  C  CG2 . VAL D  1 289 ? -43.921  -58.598 60.154  1.00 27.53  ? 288 VAL G CG2 1 
ATOM   8831  N  N   . HIS D  1 290 ? -45.629  -61.460 59.595  1.00 29.91  ? 289 HIS G N   1 
ATOM   8832  C  CA  . HIS D  1 290 ? -45.954  -62.775 60.063  1.00 27.95  ? 289 HIS G CA  1 
ATOM   8833  C  C   . HIS D  1 290 ? -45.101  -63.160 61.277  1.00 27.71  ? 289 HIS G C   1 
ATOM   8834  O  O   . HIS D  1 290 ? -44.092  -62.557 61.611  1.00 29.03  ? 289 HIS G O   1 
ATOM   8835  C  CB  . HIS D  1 290 ? -45.765  -63.795 58.939  1.00 28.46  ? 289 HIS G CB  1 
ATOM   8836  C  CG  . HIS D  1 290 ? -46.870  -63.861 57.932  1.00 26.97  ? 289 HIS G CG  1 
ATOM   8837  N  ND1 . HIS D  1 290 ? -47.969  -64.645 58.113  1.00 26.51  ? 289 HIS G ND1 1 
ATOM   8838  C  CD2 . HIS D  1 290 ? -46.998  -63.311 56.704  1.00 26.25  ? 289 HIS G CD2 1 
ATOM   8839  C  CE1 . HIS D  1 290 ? -48.755  -64.568 57.063  1.00 26.78  ? 289 HIS G CE1 1 
ATOM   8840  N  NE2 . HIS D  1 290 ? -48.185  -63.760 56.176  1.00 30.48  ? 289 HIS G NE2 1 
ATOM   8841  N  N   . GLU D  1 291 ? -45.567  -64.209 61.933  1.00 29.36  ? 290 GLU G N   1 
ATOM   8842  C  CA  . GLU D  1 291 ? -45.022  -64.751 63.169  1.00 34.50  ? 290 GLU G CA  1 
ATOM   8843  C  C   . GLU D  1 291 ? -43.624  -65.348 62.922  1.00 31.25  ? 290 GLU G C   1 
ATOM   8844  O  O   . GLU D  1 291 ? -42.714  -65.087 63.668  1.00 31.30  ? 290 GLU G O   1 
ATOM   8845  C  CB  . GLU D  1 291 ? -46.018  -65.815 63.633  1.00 38.64  ? 290 GLU G CB  1 
ATOM   8846  C  CG  . GLU D  1 291 ? -45.624  -66.575 64.878  1.00 46.67  ? 290 GLU G CG  1 
ATOM   8847  C  CD  . GLU D  1 291 ? -46.493  -67.809 65.068  1.00 53.71  ? 290 GLU G CD  1 
ATOM   8848  O  OE1 . GLU D  1 291 ? -46.617  -68.243 66.222  1.00 66.30  ? 290 GLU G OE1 1 
ATOM   8849  O  OE2 . GLU D  1 291 ? -47.050  -68.336 64.054  1.00 54.73  ? 290 GLU G OE2 1 
ATOM   8850  N  N   . LYS D  1 292 ? -43.481  -66.101 61.835  1.00 31.52  ? 291 LYS G N   1 
ATOM   8851  C  CA  . LYS D  1 292 ? -42.268  -66.873 61.544  1.00 37.69  ? 291 LYS G CA  1 
ATOM   8852  C  C   . LYS D  1 292 ? -41.645  -66.427 60.213  1.00 36.27  ? 291 LYS G C   1 
ATOM   8853  O  O   . LYS D  1 292 ? -42.219  -65.640 59.459  1.00 30.78  ? 291 LYS G O   1 
ATOM   8854  C  CB  . LYS D  1 292 ? -42.621  -68.359 61.464  1.00 38.09  ? 291 LYS G CB  1 
ATOM   8855  C  CG  . LYS D  1 292 ? -43.206  -68.927 62.749  1.00 45.49  ? 291 LYS G CG  1 
ATOM   8856  C  CD  . LYS D  1 292 ? -43.638  -70.367 62.647  1.00 49.99  ? 291 LYS G CD  1 
ATOM   8857  C  CE  . LYS D  1 292 ? -44.369  -70.669 61.360  1.00 57.29  ? 291 LYS G CE  1 
ATOM   8858  N  NZ  . LYS D  1 292 ? -45.190  -71.897 61.456  1.00 63.44  ? 291 LYS G NZ  1 
ATOM   8859  N  N   . ALA D  1 293 ? -40.472  -66.990 59.919  1.00 31.88  ? 292 ALA G N   1 
ATOM   8860  C  CA  . ALA D  1 293 ? -39.793  -66.784 58.661  1.00 34.16  ? 292 ALA G CA  1 
ATOM   8861  C  C   . ALA D  1 293 ? -40.616  -67.343 57.496  1.00 30.53  ? 292 ALA G C   1 
ATOM   8862  O  O   . ALA D  1 293 ? -41.365  -68.299 57.620  1.00 32.56  ? 292 ALA G O   1 
ATOM   8863  C  CB  . ALA D  1 293 ? -38.404  -67.382 58.711  1.00 35.73  ? 292 ALA G CB  1 
ATOM   8864  N  N   . ASP D  1 294 ? -40.494  -66.659 56.359  1.00 28.72  ? 293 ASP G N   1 
ATOM   8865  C  CA  . ASP D  1 294 ? -40.945  -67.125 55.071  1.00 29.69  ? 293 ASP G CA  1 
ATOM   8866  C  C   . ASP D  1 294 ? -39.830  -68.020 54.496  1.00 28.08  ? 293 ASP G C   1 
ATOM   8867  O  O   . ASP D  1 294 ? -38.733  -67.541 54.311  1.00 28.18  ? 293 ASP G O   1 
ATOM   8868  C  CB  . ASP D  1 294 ? -41.198  -65.914 54.168  1.00 29.66  ? 293 ASP G CB  1 
ATOM   8869  C  CG  . ASP D  1 294 ? -41.811  -66.215 52.815  1.00 35.92  ? 293 ASP G CG  1 
ATOM   8870  O  OD1 . ASP D  1 294 ? -41.712  -67.372 52.351  1.00 33.34  ? 293 ASP G OD1 1 
ATOM   8871  O  OD2 . ASP D  1 294 ? -42.403  -65.283 52.234  1.00 36.54  ? 293 ASP G OD2 1 
ATOM   8872  N  N   . ASP D  1 295 ? -40.159  -69.275 54.178  1.00 29.76  ? 294 ASP G N   1 
ATOM   8873  C  CA  . ASP D  1 295 ? -39.214  -70.276 53.623  1.00 33.02  ? 294 ASP G CA  1 
ATOM   8874  C  C   . ASP D  1 295 ? -39.063  -70.065 52.113  1.00 33.50  ? 294 ASP G C   1 
ATOM   8875  O  O   . ASP D  1 295 ? -38.349  -70.806 51.435  1.00 29.96  ? 294 ASP G O   1 
ATOM   8876  C  CB  . ASP D  1 295 ? -39.636  -71.709 53.988  1.00 31.18  ? 294 ASP G CB  1 
ATOM   8877  C  CG  . ASP D  1 295 ? -40.930  -72.213 53.357  1.00 33.36  ? 294 ASP G CG  1 
ATOM   8878  O  OD1 . ASP D  1 295 ? -41.560  -73.113 53.949  1.00 35.49  ? 294 ASP G OD1 1 
ATOM   8879  O  OD2 . ASP D  1 295 ? -41.310  -71.714 52.280  1.00 31.27  ? 294 ASP G OD2 1 
ATOM   8880  N  N   . LEU D  1 296 ? -39.763  -69.065 51.569  1.00 30.01  ? 295 LEU G N   1 
ATOM   8881  C  CA  . LEU D  1 296 ? -39.603  -68.639 50.181  1.00 28.60  ? 295 LEU G CA  1 
ATOM   8882  C  C   . LEU D  1 296 ? -39.966  -69.778 49.218  1.00 28.95  ? 295 LEU G C   1 
ATOM   8883  O  O   . LEU D  1 296 ? -39.441  -69.865 48.127  1.00 31.18  ? 295 LEU G O   1 
ATOM   8884  C  CB  . LEU D  1 296 ? -38.178  -68.129 49.921  1.00 30.43  ? 295 LEU G CB  1 
ATOM   8885  C  CG  . LEU D  1 296 ? -37.613  -67.073 50.869  1.00 34.19  ? 295 LEU G CG  1 
ATOM   8886  C  CD1 . LEU D  1 296 ? -36.172  -66.712 50.505  1.00 35.61  ? 295 LEU G CD1 1 
ATOM   8887  C  CD2 . LEU D  1 296 ? -38.461  -65.806 50.894  1.00 34.53  ? 295 LEU G CD2 1 
ATOM   8888  N  N   . GLY D  1 297 ? -40.912  -70.625 49.619  1.00 30.65  ? 296 GLY G N   1 
ATOM   8889  C  CA  . GLY D  1 297 ? -41.432  -71.686 48.780  1.00 32.23  ? 296 GLY G CA  1 
ATOM   8890  C  C   . GLY D  1 297 ? -40.531  -72.918 48.742  1.00 35.25  ? 296 GLY G C   1 
ATOM   8891  O  O   . GLY D  1 297 ? -40.759  -73.808 47.923  1.00 32.44  ? 296 GLY G O   1 
ATOM   8892  N  N   . LYS D  1 298 ? -39.552  -73.004 49.657  1.00 34.53  ? 297 LYS G N   1 
ATOM   8893  C  CA  . LYS D  1 298 ? -38.569  -74.121 49.659  1.00 36.84  ? 297 LYS G CA  1 
ATOM   8894  C  C   . LYS D  1 298 ? -38.706  -75.046 50.879  1.00 34.93  ? 297 LYS G C   1 
ATOM   8895  O  O   . LYS D  1 298 ? -37.747  -75.703 51.238  1.00 41.26  ? 297 LYS G O   1 
ATOM   8896  C  CB  . LYS D  1 298 ? -37.176  -73.503 49.604  1.00 36.96  ? 297 LYS G CB  1 
ATOM   8897  C  CG  . LYS D  1 298 ? -36.905  -72.798 48.287  1.00 39.82  ? 297 LYS G CG  1 
ATOM   8898  C  CD  . LYS D  1 298 ? -35.546  -72.178 48.234  1.00 44.58  ? 297 LYS G CD  1 
ATOM   8899  C  CE  . LYS D  1 298 ? -35.226  -71.668 46.849  1.00 50.98  ? 297 LYS G CE  1 
ATOM   8900  N  NZ  . LYS D  1 298 ? -33.959  -70.906 46.876  1.00 57.94  ? 297 LYS G NZ  1 
ATOM   8901  N  N   . GLY D  1 299 ? -39.893  -75.124 51.490  1.00 32.04  ? 298 GLY G N   1 
ATOM   8902  C  CA  . GLY D  1 299 ? -40.119  -75.885 52.722  1.00 34.23  ? 298 GLY G CA  1 
ATOM   8903  C  C   . GLY D  1 299 ? -40.652  -77.301 52.506  1.00 33.84  ? 298 GLY G C   1 
ATOM   8904  O  O   . GLY D  1 299 ? -40.856  -78.031 53.474  1.00 33.28  ? 298 GLY G O   1 
ATOM   8905  N  N   . GLY D  1 300 ? -40.925  -77.667 51.257  1.00 34.50  ? 299 GLY G N   1 
ATOM   8906  C  CA  . GLY D  1 300 ? -41.309  -79.033 50.880  1.00 39.44  ? 299 GLY G CA  1 
ATOM   8907  C  C   . GLY D  1 300 ? -42.745  -79.413 51.230  1.00 47.17  ? 299 GLY G C   1 
ATOM   8908  O  O   . GLY D  1 300 ? -43.072  -80.603 51.217  1.00 43.96  ? 299 GLY G O   1 
ATOM   8909  N  N   . ASN D  1 301 ? -43.621  -78.437 51.521  1.00 47.63  ? 300 ASN G N   1 
ATOM   8910  C  CA  . ASN D  1 301 ? -45.060  -78.743 51.765  1.00 47.10  ? 300 ASN G CA  1 
ATOM   8911  C  C   . ASN D  1 301 ? -45.964  -77.777 50.990  1.00 48.63  ? 300 ASN G C   1 
ATOM   8912  O  O   . ASN D  1 301 ? -45.511  -76.789 50.388  1.00 42.94  ? 300 ASN G O   1 
ATOM   8913  C  CB  . ASN D  1 301 ? -45.408  -78.810 53.254  1.00 45.28  ? 300 ASN G CB  1 
ATOM   8914  C  CG  . ASN D  1 301 ? -45.015  -77.586 54.045  1.00 50.89  ? 300 ASN G CG  1 
ATOM   8915  O  OD1 . ASN D  1 301 ? -44.962  -77.613 55.278  1.00 54.44  ? 300 ASN G OD1 1 
ATOM   8916  N  ND2 . ASN D  1 301 ? -44.752  -76.501 53.346  1.00 45.44  ? 300 ASN G ND2 1 
ATOM   8917  N  N   . GLU D  1 302 ? -47.262  -78.095 50.982  1.00 54.21  ? 301 GLU G N   1 
ATOM   8918  C  CA  . GLU D  1 302 ? -48.247  -77.279 50.265  1.00 57.32  ? 301 GLU G CA  1 
ATOM   8919  C  C   . GLU D  1 302 ? -48.287  -75.869 50.865  1.00 46.23  ? 301 GLU G C   1 
ATOM   8920  O  O   . GLU D  1 302 ? -48.378  -74.891 50.126  1.00 49.29  ? 301 GLU G O   1 
ATOM   8921  C  CB  . GLU D  1 302 ? -49.632  -77.924 50.269  1.00 63.60  ? 301 GLU G CB  1 
ATOM   8922  C  CG  . GLU D  1 302 ? -49.950  -78.625 48.961  1.00 72.41  ? 301 GLU G CG  1 
ATOM   8923  C  CD  . GLU D  1 302 ? -51.427  -78.910 48.756  1.00 86.07  ? 301 GLU G CD  1 
ATOM   8924  O  OE1 . GLU D  1 302 ? -51.747  -79.987 48.206  1.00 89.29  ? 301 GLU G OE1 1 
ATOM   8925  O  OE2 . GLU D  1 302 ? -52.254  -78.048 49.145  1.00 91.97  ? 301 GLU G OE2 1 
ATOM   8926  N  N   . GLU D  1 303 ? -48.173  -75.789 52.194  1.00 44.04  ? 302 GLU G N   1 
ATOM   8927  C  CA  . GLU D  1 303 ? -48.133  -74.517 52.930  1.00 43.90  ? 302 GLU G CA  1 
ATOM   8928  C  C   . GLU D  1 303 ? -46.970  -73.642 52.422  1.00 42.20  ? 302 GLU G C   1 
ATOM   8929  O  O   . GLU D  1 303 ? -47.107  -72.423 52.298  1.00 38.72  ? 302 GLU G O   1 
ATOM   8930  C  CB  . GLU D  1 303 ? -48.046  -74.790 54.433  1.00 46.82  ? 302 GLU G CB  1 
ATOM   8931  C  CG  . GLU D  1 303 ? -48.457  -73.618 55.298  1.00 54.95  ? 302 GLU G CG  1 
ATOM   8932  C  CD  . GLU D  1 303 ? -49.897  -73.171 55.077  1.00 63.26  ? 302 GLU G CD  1 
ATOM   8933  O  OE1 . GLU D  1 303 ? -50.820  -73.996 55.294  1.00 66.32  ? 302 GLU G OE1 1 
ATOM   8934  O  OE2 . GLU D  1 303 ? -50.093  -72.016 54.644  1.00 65.30  ? 302 GLU G OE2 1 
ATOM   8935  N  N   . SER D  1 304 ? -45.834  -74.262 52.082  1.00 34.62  ? 303 SER G N   1 
ATOM   8936  C  CA  . SER D  1 304 ? -44.662  -73.533 51.597  1.00 35.64  ? 303 SER G CA  1 
ATOM   8937  C  C   . SER D  1 304 ? -45.013  -72.764 50.315  1.00 34.08  ? 303 SER G C   1 
ATOM   8938  O  O   . SER D  1 304 ? -44.571  -71.644 50.117  1.00 32.67  ? 303 SER G O   1 
ATOM   8939  C  CB  . SER D  1 304 ? -43.482  -74.457 51.351  1.00 35.21  ? 303 SER G CB  1 
ATOM   8940  O  OG  . SER D  1 304 ? -42.315  -73.694 51.097  1.00 33.47  ? 303 SER G OG  1 
ATOM   8941  N  N   . THR D  1 305 ? -45.787  -73.399 49.434  1.00 34.10  ? 304 THR G N   1 
ATOM   8942  C  CA  . THR D  1 305 ? -46.071  -72.841 48.121  1.00 41.36  ? 304 THR G CA  1 
ATOM   8943  C  C   . THR D  1 305 ? -47.289  -71.895 48.177  1.00 40.29  ? 304 THR G C   1 
ATOM   8944  O  O   . THR D  1 305 ? -47.686  -71.378 47.141  1.00 38.02  ? 304 THR G O   1 
ATOM   8945  C  CB  . THR D  1 305 ? -46.287  -73.973 47.113  1.00 42.05  ? 304 THR G CB  1 
ATOM   8946  O  OG1 . THR D  1 305 ? -47.356  -74.735 47.668  1.00 49.73  ? 304 THR G OG1 1 
ATOM   8947  C  CG2 . THR D  1 305 ? -45.050  -74.812 46.897  1.00 46.19  ? 304 THR G CG2 1 
ATOM   8948  N  N   . LYS D  1 306 ? -47.861  -71.697 49.376  1.00 41.26  ? 305 LYS G N   1 
ATOM   8949  C  CA  . LYS D  1 306 ? -49.008  -70.812 49.625  1.00 44.38  ? 305 LYS G CA  1 
ATOM   8950  C  C   . LYS D  1 306 ? -48.575  -69.596 50.450  1.00 40.01  ? 305 LYS G C   1 
ATOM   8951  O  O   . LYS D  1 306 ? -48.826  -68.468 50.031  1.00 36.69  ? 305 LYS G O   1 
ATOM   8952  C  CB  . LYS D  1 306 ? -50.125  -71.534 50.384  1.00 48.82  ? 305 LYS G CB  1 
ATOM   8953  C  CG  . LYS D  1 306 ? -50.920  -72.540 49.566  1.00 56.04  ? 305 LYS G CG  1 
ATOM   8954  C  CD  . LYS D  1 306 ? -52.057  -73.185 50.347  1.00 63.73  ? 305 LYS G CD  1 
ATOM   8955  C  CE  . LYS D  1 306 ? -52.645  -74.402 49.661  1.00 67.79  ? 305 LYS G CE  1 
ATOM   8956  N  NZ  . LYS D  1 306 ? -53.068  -74.099 48.270  1.00 71.11  ? 305 LYS G NZ  1 
ATOM   8957  N  N   . THR D  1 307 ? -47.936  -69.845 51.601  1.00 33.79  ? 306 THR G N   1 
ATOM   8958  C  CA  . THR D  1 307 ? -47.620  -68.821 52.604  1.00 37.71  ? 306 THR G CA  1 
ATOM   8959  C  C   . THR D  1 307 ? -46.143  -68.798 53.014  1.00 36.17  ? 306 THR G C   1 
ATOM   8960  O  O   . THR D  1 307 ? -45.748  -67.972 53.836  1.00 37.51  ? 306 THR G O   1 
ATOM   8961  C  CB  . THR D  1 307 ? -48.423  -69.055 53.885  1.00 39.98  ? 306 THR G CB  1 
ATOM   8962  O  OG1 . THR D  1 307 ? -47.954  -70.282 54.454  1.00 39.02  ? 306 THR G OG1 1 
ATOM   8963  C  CG2 . THR D  1 307 ? -49.916  -69.110 53.642  1.00 39.13  ? 306 THR G CG2 1 
ATOM   8964  N  N   . GLY D  1 308 ? -45.330  -69.720 52.491  1.00 33.67  ? 307 GLY G N   1 
ATOM   8965  C  CA  . GLY D  1 308 ? -43.940  -69.839 52.927  1.00 32.78  ? 307 GLY G CA  1 
ATOM   8966  C  C   . GLY D  1 308 ? -43.808  -70.317 54.370  1.00 31.53  ? 307 GLY G C   1 
ATOM   8967  O  O   . GLY D  1 308 ? -42.757  -70.118 54.989  1.00 32.12  ? 307 GLY G O   1 
ATOM   8968  N  N   . ASN D  1 309 ? -44.860  -70.952 54.900  1.00 32.90  ? 308 ASN G N   1 
ATOM   8969  C  CA  . ASN D  1 309 ? -44.915  -71.386 56.298  1.00 33.89  ? 308 ASN G CA  1 
ATOM   8970  C  C   . ASN D  1 309 ? -44.631  -70.217 57.242  1.00 34.81  ? 308 ASN G C   1 
ATOM   8971  O  O   . ASN D  1 309 ? -44.018  -70.435 58.286  1.00 34.93  ? 308 ASN G O   1 
ATOM   8972  C  CB  . ASN D  1 309 ? -43.908  -72.511 56.596  1.00 36.51  ? 308 ASN G CB  1 
ATOM   8973  C  CG  . ASN D  1 309 ? -44.354  -73.821 56.001  1.00 37.16  ? 308 ASN G CG  1 
ATOM   8974  O  OD1 . ASN D  1 309 ? -45.350  -74.380 56.456  1.00 37.99  ? 308 ASN G OD1 1 
ATOM   8975  N  ND2 . ASN D  1 309 ? -43.694  -74.248 54.932  1.00 35.39  ? 308 ASN G ND2 1 
ATOM   8976  N  N   . ALA D  1 310 ? -45.089  -68.988 56.916  1.00 31.49  ? 309 ALA G N   1 
ATOM   8977  C  CA  . ALA D  1 310 ? -44.709  -67.860 57.747  1.00 30.39  ? 309 ALA G CA  1 
ATOM   8978  C  C   . ALA D  1 310 ? -45.600  -67.773 58.999  1.00 28.58  ? 309 ALA G C   1 
ATOM   8979  O  O   . ALA D  1 310 ? -45.340  -66.963 59.894  1.00 31.25  ? 309 ALA G O   1 
ATOM   8980  C  CB  . ALA D  1 310 ? -44.713  -66.577 56.947  1.00 32.73  ? 309 ALA G CB  1 
ATOM   8981  N  N   . GLY D  1 311 ? -46.629  -68.610 59.067  1.00 29.22  ? 310 GLY G N   1 
ATOM   8982  C  CA  . GLY D  1 311 ? -47.456  -68.722 60.251  1.00 33.36  ? 310 GLY G CA  1 
ATOM   8983  C  C   . GLY D  1 311 ? -48.407  -67.539 60.421  1.00 34.62  ? 310 GLY G C   1 
ATOM   8984  O  O   . GLY D  1 311 ? -48.842  -66.925 59.439  1.00 33.55  ? 310 GLY G O   1 
ATOM   8985  N  N   . SER D  1 312 ? -48.703  -67.233 61.690  1.00 33.76  ? 311 SER G N   1 
ATOM   8986  C  CA  . SER D  1 312 ? -49.745  -66.305 62.109  1.00 36.78  ? 311 SER G CA  1 
ATOM   8987  C  C   . SER D  1 312 ? -49.463  -64.900 61.584  1.00 33.41  ? 311 SER G C   1 
ATOM   8988  O  O   . SER D  1 312 ? -48.300  -64.523 61.388  1.00 31.71  ? 311 SER G O   1 
ATOM   8989  C  CB  . SER D  1 312 ? -49.843  -66.249 63.613  1.00 36.70  ? 311 SER G CB  1 
ATOM   8990  O  OG  . SER D  1 312 ? -50.474  -67.413 64.088  1.00 47.95  ? 311 SER G OG  1 
ATOM   8991  N  N   . ARG D  1 313 ? -50.551  -64.131 61.456  1.00 32.29  ? 312 ARG G N   1 
ATOM   8992  C  CA  . ARG D  1 313 ? -50.527  -62.737 61.048  1.00 29.26  ? 312 ARG G CA  1 
ATOM   8993  C  C   . ARG D  1 313 ? -50.454  -61.908 62.326  1.00 29.91  ? 312 ARG G C   1 
ATOM   8994  O  O   . ARG D  1 313 ? -51.414  -61.822 63.052  1.00 31.74  ? 312 ARG G O   1 
ATOM   8995  C  CB  . ARG D  1 313 ? -51.762  -62.438 60.191  1.00 29.21  ? 312 ARG G CB  1 
ATOM   8996  C  CG  . ARG D  1 313 ? -51.895  -63.376 59.004  1.00 29.39  ? 312 ARG G CG  1 
ATOM   8997  C  CD  . ARG D  1 313 ? -53.191  -63.257 58.242  1.00 30.53  ? 312 ARG G CD  1 
ATOM   8998  N  NE  . ARG D  1 313 ? -53.302  -64.308 57.238  1.00 28.25  ? 312 ARG G NE  1 
ATOM   8999  C  CZ  . ARG D  1 313 ? -53.993  -64.236 56.110  1.00 30.27  ? 312 ARG G CZ  1 
ATOM   9000  N  NH1 . ARG D  1 313 ? -53.929  -65.240 55.254  1.00 23.89  ? 312 ARG G NH1 1 
ATOM   9001  N  NH2 . ARG D  1 313 ? -54.751  -63.176 55.838  1.00 29.58  ? 312 ARG G NH2 1 
ATOM   9002  N  N   . LEU D  1 314 ? -49.283  -61.337 62.603  1.00 26.84  ? 313 LEU G N   1 
ATOM   9003  C  CA  . LEU D  1 314 ? -49.071  -60.591 63.831  1.00 29.91  ? 313 LEU G CA  1 
ATOM   9004  C  C   . LEU D  1 314 ? -49.672  -59.182 63.727  1.00 28.59  ? 313 LEU G C   1 
ATOM   9005  O  O   . LEU D  1 314 ? -50.105  -58.645 64.707  1.00 25.14  ? 313 LEU G O   1 
ATOM   9006  C  CB  . LEU D  1 314 ? -47.573  -60.482 64.094  1.00 31.22  ? 313 LEU G CB  1 
ATOM   9007  C  CG  . LEU D  1 314 ? -46.956  -61.532 65.019  1.00 37.01  ? 313 LEU G CG  1 
ATOM   9008  C  CD1 . LEU D  1 314 ? -47.625  -62.882 64.901  1.00 35.32  ? 313 LEU G CD1 1 
ATOM   9009  C  CD2 . LEU D  1 314 ? -45.468  -61.623 64.762  1.00 35.77  ? 313 LEU G CD2 1 
ATOM   9010  N  N   . ALA D  1 315 ? -49.530  -58.552 62.567  1.00 24.86  ? 314 ALA G N   1 
ATOM   9011  C  CA  . ALA D  1 315 ? -50.065  -57.230 62.358  1.00 25.65  ? 314 ALA G CA  1 
ATOM   9012  C  C   . ALA D  1 315 ? -50.279  -57.034 60.861  1.00 27.03  ? 314 ALA G C   1 
ATOM   9013  O  O   . ALA D  1 315 ? -49.713  -57.771 60.038  1.00 24.67  ? 314 ALA G O   1 
ATOM   9014  C  CB  . ALA D  1 315 ? -49.155  -56.181 62.918  1.00 24.88  ? 314 ALA G CB  1 
ATOM   9015  N  N   . CYS D  1 316 ? -51.162  -56.082 60.544  1.00 26.47  ? 315 CYS G N   1 
ATOM   9016  C  CA  . CYS D  1 316 ? -51.513  -55.784 59.189  1.00 25.52  ? 315 CYS G CA  1 
ATOM   9017  C  C   . CYS D  1 316 ? -52.133  -54.387 59.118  1.00 25.13  ? 315 CYS G C   1 
ATOM   9018  O  O   . CYS D  1 316 ? -52.482  -53.774 60.111  1.00 21.70  ? 315 CYS G O   1 
ATOM   9019  C  CB  . CYS D  1 316 ? -52.473  -56.824 58.628  1.00 28.95  ? 315 CYS G CB  1 
ATOM   9020  S  SG  . CYS D  1 316 ? -54.049  -56.922 59.505  1.00 32.33  ? 315 CYS G SG  1 
ATOM   9021  N  N   . GLY D  1 317 ? -52.271  -53.913 57.894  1.00 23.34  ? 316 GLY G N   1 
ATOM   9022  C  CA  . GLY D  1 317 ? -53.005  -52.722 57.648  1.00 25.34  ? 316 GLY G CA  1 
ATOM   9023  C  C   . GLY D  1 317 ? -53.292  -52.611 56.173  1.00 25.19  ? 316 GLY G C   1 
ATOM   9024  O  O   . GLY D  1 317 ? -52.647  -53.298 55.336  1.00 22.92  ? 316 GLY G O   1 
ATOM   9025  N  N   . VAL D  1 318 ? -54.234  -51.727 55.860  1.00 23.73  ? 317 VAL G N   1 
ATOM   9026  C  CA  . VAL D  1 318 ? -54.595  -51.455 54.483  1.00 22.26  ? 317 VAL G CA  1 
ATOM   9027  C  C   . VAL D  1 318 ? -53.594  -50.455 53.921  1.00 20.24  ? 317 VAL G C   1 
ATOM   9028  O  O   . VAL D  1 318 ? -53.280  -49.459 54.564  1.00 22.75  ? 317 VAL G O   1 
ATOM   9029  C  CB  . VAL D  1 318 ? -56.052  -50.959 54.390  1.00 22.36  ? 317 VAL G CB  1 
ATOM   9030  C  CG1 . VAL D  1 318 ? -56.437  -50.701 52.949  1.00 23.53  ? 317 VAL G CG1 1 
ATOM   9031  C  CG2 . VAL D  1 318 ? -57.008  -51.952 55.030  1.00 24.69  ? 317 VAL G CG2 1 
ATOM   9032  N  N   . ILE D  1 319 ? -53.128  -50.713 52.694  1.00 20.41  ? 318 ILE G N   1 
ATOM   9033  C  CA  . ILE D  1 319 ? -52.168  -49.868 52.015  1.00 22.09  ? 318 ILE G CA  1 
ATOM   9034  C  C   . ILE D  1 319 ? -52.912  -48.698 51.353  1.00 21.83  ? 318 ILE G C   1 
ATOM   9035  O  O   . ILE D  1 319 ? -53.742  -48.898 50.475  1.00 23.20  ? 318 ILE G O   1 
ATOM   9036  C  CB  . ILE D  1 319 ? -51.358  -50.674 50.987  1.00 22.83  ? 318 ILE G CB  1 
ATOM   9037  C  CG1 . ILE D  1 319 ? -50.546  -51.773 51.672  1.00 22.71  ? 318 ILE G CG1 1 
ATOM   9038  C  CG2 . ILE D  1 319 ? -50.454  -49.753 50.184  1.00 24.36  ? 318 ILE G CG2 1 
ATOM   9039  C  CD1 . ILE D  1 319 ? -50.060  -52.812 50.701  1.00 24.77  ? 318 ILE G CD1 1 
ATOM   9040  N  N   . GLY D  1 320 ? -52.579  -47.490 51.788  1.00 23.55  ? 319 GLY G N   1 
ATOM   9041  C  CA  . GLY D  1 320 ? -53.306  -46.300 51.428  1.00 25.31  ? 319 GLY G CA  1 
ATOM   9042  C  C   . GLY D  1 320 ? -52.465  -45.322 50.660  1.00 25.16  ? 319 GLY G C   1 
ATOM   9043  O  O   . GLY D  1 320 ? -51.216  -45.309 50.753  1.00 24.12  ? 319 GLY G O   1 
ATOM   9044  N  N   . ILE D  1 321 ? -53.170  -44.450 49.938  1.00 24.00  ? 320 ILE G N   1 
ATOM   9045  C  CA  . ILE D  1 321 ? -52.556  -43.413 49.173  1.00 25.48  ? 320 ILE G CA  1 
ATOM   9046  C  C   . ILE D  1 321 ? -52.005  -42.377 50.157  1.00 25.99  ? 320 ILE G C   1 
ATOM   9047  O  O   . ILE D  1 321 ? -52.698  -41.932 51.070  1.00 25.60  ? 320 ILE G O   1 
ATOM   9048  C  CB  . ILE D  1 321 ? -53.532  -42.782 48.191  1.00 25.75  ? 320 ILE G CB  1 
ATOM   9049  C  CG1 . ILE D  1 321 ? -54.184  -43.858 47.320  1.00 30.33  ? 320 ILE G CG1 1 
ATOM   9050  C  CG2 . ILE D  1 321 ? -52.802  -41.804 47.283  1.00 27.81  ? 320 ILE G CG2 1 
ATOM   9051  C  CD1 . ILE D  1 321 ? -55.228  -43.322 46.367  1.00 33.17  ? 320 ILE G CD1 1 
ATOM   9052  N  N   . ALA D  1 322 ? -50.730  -42.008 49.980  1.00 27.22  ? 321 ALA G N   1 
ATOM   9053  C  CA  . ALA D  1 322 ? -50.075  -40.994 50.796  1.00 29.75  ? 321 ALA G CA  1 
ATOM   9054  C  C   . ALA D  1 322 ? -49.801  -39.752 49.939  1.00 30.06  ? 321 ALA G C   1 
ATOM   9055  O  O   . ALA D  1 322 ? -49.717  -39.826 48.712  1.00 36.90  ? 321 ALA G O   1 
ATOM   9056  C  CB  . ALA D  1 322 ? -48.790  -41.534 51.375  1.00 30.07  ? 321 ALA G CB  1 
ATOM   9057  N  N   . GLN D  1 323 ? -49.559  -38.629 50.595  1.00 37.09  ? 322 GLN G N   1 
ATOM   9058  C  CA  . GLN D  1 323 ? -49.274  -37.369 49.877  1.00 44.91  ? 322 GLN G CA  1 
ATOM   9059  C  C   . GLN D  1 323 ? -47.999  -37.476 49.028  1.00 46.50  ? 322 GLN G C   1 
ATOM   9060  O  O   . GLN D  1 323 ? -46.913  -37.562 49.586  1.00 53.00  ? 322 GLN G O   1 
ATOM   9061  C  CB  . GLN D  1 323 ? -49.119  -36.218 50.859  1.00 45.99  ? 322 GLN G CB  1 
ATOM   9062  C  CG  . GLN D  1 323 ? -48.955  -34.876 50.147  1.00 54.21  ? 322 GLN G CG  1 
ATOM   9063  C  CD  . GLN D  1 323 ? -49.594  -33.740 50.909  1.00 56.78  ? 322 GLN G CD  1 
ATOM   9064  O  OE1 . GLN D  1 323 ? -49.638  -33.735 52.138  1.00 59.17  ? 322 GLN G OE1 1 
ATOM   9065  N  NE2 . GLN D  1 323 ? -50.111  -32.768 50.174  1.00 65.60  ? 322 GLN G NE2 1 
ATOM   9066  N  N   . ALA E  1 2   ? -51.711  -34.132 29.332  1.00 39.44  ? 1   ALA I N   1 
ATOM   9067  C  CA  . ALA E  1 2   ? -50.920  -32.942 28.929  1.00 37.17  ? 1   ALA I CA  1 
ATOM   9068  C  C   . ALA E  1 2   ? -51.769  -31.694 29.169  1.00 33.40  ? 1   ALA I C   1 
ATOM   9069  O  O   . ALA E  1 2   ? -52.941  -31.800 29.414  1.00 36.43  ? 1   ALA I O   1 
ATOM   9070  C  CB  . ALA E  1 2   ? -50.546  -33.069 27.475  1.00 39.46  ? 1   ALA I CB  1 
ATOM   9071  N  N   . THR E  1 3   ? -51.166  -30.529 28.997  1.00 29.81  ? 2   THR I N   1 
ATOM   9072  C  CA  . THR E  1 3   ? -51.808  -29.237 29.190  1.00 32.51  ? 2   THR I CA  1 
ATOM   9073  C  C   . THR E  1 3   ? -52.272  -28.692 27.820  1.00 28.21  ? 2   THR I C   1 
ATOM   9074  O  O   . THR E  1 3   ? -53.195  -27.885 27.736  1.00 27.32  ? 2   THR I O   1 
ATOM   9075  C  CB  . THR E  1 3   ? -50.788  -28.383 29.964  1.00 38.14  ? 2   THR I CB  1 
ATOM   9076  O  OG1 A THR E  1 3   ? -51.374  -27.963 31.194  0.60 49.88  ? 2   THR I OG1 1 
ATOM   9077  O  OG1 B THR E  1 3   ? -51.381  -27.964 31.192  0.40 45.94  ? 2   THR I OG1 1 
ATOM   9078  C  CG2 A THR E  1 3   ? -50.256  -27.192 29.205  0.60 38.92  ? 2   THR I CG2 1 
ATOM   9079  C  CG2 B THR E  1 3   ? -50.264  -27.187 29.204  0.40 38.46  ? 2   THR I CG2 1 
ATOM   9080  N  N   . LYS E  1 4   ? -51.556  -29.074 26.755  1.00 26.37  ? 3   LYS I N   1 
ATOM   9081  C  CA  . LYS E  1 4   ? -51.879  -28.708 25.375  1.00 27.81  ? 3   LYS I CA  1 
ATOM   9082  C  C   . LYS E  1 4   ? -51.796  -29.954 24.501  1.00 22.99  ? 3   LYS I C   1 
ATOM   9083  O  O   . LYS E  1 4   ? -50.943  -30.804 24.705  1.00 23.29  ? 3   LYS I O   1 
ATOM   9084  C  CB  . LYS E  1 4   ? -50.903  -27.676 24.807  1.00 30.55  ? 3   LYS I CB  1 
ATOM   9085  C  CG  . LYS E  1 4   ? -50.884  -26.336 25.523  1.00 39.13  ? 3   LYS I CG  1 
ATOM   9086  C  CD  . LYS E  1 4   ? -49.957  -25.297 24.897  1.00 47.20  ? 3   LYS I CD  1 
ATOM   9087  C  CE  . LYS E  1 4   ? -50.374  -24.923 23.487  1.00 53.50  ? 3   LYS I CE  1 
ATOM   9088  N  NZ  . LYS E  1 4   ? -49.624  -23.758 22.960  1.00 56.78  ? 3   LYS I NZ  1 
ATOM   9089  N  N   . ALA E  1 5   ? -52.662  -30.030 23.497  1.00 22.63  ? 4   ALA I N   1 
ATOM   9090  C  CA  . ALA E  1 5   ? -52.609  -31.109 22.524  1.00 23.07  ? 4   ALA I CA  1 
ATOM   9091  C  C   . ALA E  1 5   ? -52.898  -30.525 21.142  1.00 23.04  ? 4   ALA I C   1 
ATOM   9092  O  O   . ALA E  1 5   ? -53.401  -29.392 21.018  1.00 21.70  ? 4   ALA I O   1 
ATOM   9093  C  CB  . ALA E  1 5   ? -53.570  -32.220 22.901  1.00 22.62  ? 4   ALA I CB  1 
ATOM   9094  N  N   . VAL E  1 6   ? -52.604  -31.313 20.104  1.00 21.95  ? 5   VAL I N   1 
ATOM   9095  C  CA  . VAL E  1 6   ? -52.818  -30.859 18.759  1.00 23.11  ? 5   VAL I CA  1 
ATOM   9096  C  C   . VAL E  1 6   ? -53.138  -32.070 17.887  1.00 22.57  ? 5   VAL I C   1 
ATOM   9097  O  O   . VAL E  1 6   ? -52.739  -33.219 18.186  1.00 21.88  ? 5   VAL I O   1 
ATOM   9098  C  CB  . VAL E  1 6   ? -51.595  -30.065 18.254  1.00 24.92  ? 5   VAL I CB  1 
ATOM   9099  C  CG1 . VAL E  1 6   ? -50.361  -30.947 18.121  1.00 24.40  ? 5   VAL I CG1 1 
ATOM   9100  C  CG2 . VAL E  1 6   ? -51.881  -29.344 16.960  1.00 25.59  ? 5   VAL I CG2 1 
ATOM   9101  N  N   . CYS E  1 7   ? -53.888  -31.799 16.824  1.00 22.05  ? 6   CYS I N   1 
ATOM   9102  C  CA  . CYS E  1 7   ? -54.288  -32.811 15.897  1.00 22.44  ? 6   CYS I CA  1 
ATOM   9103  C  C   . CYS E  1 7   ? -54.211  -32.265 14.478  1.00 22.38  ? 6   CYS I C   1 
ATOM   9104  O  O   . CYS E  1 7   ? -54.816  -31.214 14.192  1.00 20.69  ? 6   CYS I O   1 
ATOM   9105  C  CB  . CYS E  1 7   ? -55.724  -33.225 16.182  1.00 25.14  ? 6   CYS I CB  1 
ATOM   9106  S  SG  . CYS E  1 7   ? -56.248  -34.615 15.173  1.00 27.34  ? 6   CYS I SG  1 
ATOM   9107  N  N   . VAL E  1 8   ? -53.511  -32.998 13.604  1.00 22.09  ? 7   VAL I N   1 
ATOM   9108  C  CA  . VAL E  1 8   ? -53.498  -32.708 12.154  1.00 23.52  ? 7   VAL I CA  1 
ATOM   9109  C  C   . VAL E  1 8   ? -54.520  -33.625 11.466  1.00 24.11  ? 7   VAL I C   1 
ATOM   9110  O  O   . VAL E  1 8   ? -54.386  -34.856 11.482  1.00 21.85  ? 7   VAL I O   1 
ATOM   9111  C  CB  . VAL E  1 8   ? -52.087  -32.852 11.560  1.00 25.16  ? 7   VAL I CB  1 
ATOM   9112  C  CG1 . VAL E  1 8   ? -52.093  -32.642 10.053  1.00 26.66  ? 7   VAL I CG1 1 
ATOM   9113  C  CG2 . VAL E  1 8   ? -51.109  -31.895 12.218  1.00 25.87  ? 7   VAL I CG2 1 
ATOM   9114  N  N   . LEU E  1 9   ? -55.573  -33.024 10.903  1.00 23.63  ? 8   LEU I N   1 
ATOM   9115  C  CA  . LEU E  1 9   ? -56.640  -33.784 10.247  1.00 26.31  ? 8   LEU I CA  1 
ATOM   9116  C  C   . LEU E  1 9   ? -56.276  -33.953 8.766   1.00 24.20  ? 8   LEU I C   1 
ATOM   9117  O  O   . LEU E  1 9   ? -56.002  -32.988 8.086   1.00 24.15  ? 8   LEU I O   1 
ATOM   9118  C  CB  . LEU E  1 9   ? -57.963  -33.033 10.388  1.00 28.01  ? 8   LEU I CB  1 
ATOM   9119  C  CG  . LEU E  1 9   ? -58.518  -32.910 11.803  1.00 31.13  ? 8   LEU I CG  1 
ATOM   9120  C  CD1 A LEU E  1 9   ? -59.687  -31.945 11.840  0.60 34.01  ? 8   LEU I CD1 1 
ATOM   9121  C  CD1 B LEU E  1 9   ? -59.681  -31.936 11.841  0.40 32.88  ? 8   LEU I CD1 1 
ATOM   9122  C  CD2 A LEU E  1 9   ? -58.968  -34.257 12.311  0.60 32.39  ? 8   LEU I CD2 1 
ATOM   9123  C  CD2 B LEU E  1 9   ? -58.969  -34.258 12.319  0.40 31.75  ? 8   LEU I CD2 1 
ATOM   9124  N  N   . LYS E  1 10  ? -56.302  -35.187 8.285   1.00 25.00  ? 9   LYS I N   1 
ATOM   9125  C  CA  . LYS E  1 10  ? -56.084  -35.479 6.883   1.00 29.16  ? 9   LYS I CA  1 
ATOM   9126  C  C   . LYS E  1 10  ? -57.053  -36.566 6.457   1.00 27.09  ? 9   LYS I C   1 
ATOM   9127  O  O   . LYS E  1 10  ? -57.467  -37.343 7.293   1.00 24.31  ? 9   LYS I O   1 
ATOM   9128  C  CB  . LYS E  1 10  ? -54.658  -35.982 6.653   1.00 32.57  ? 9   LYS I CB  1 
ATOM   9129  C  CG  . LYS E  1 10  ? -53.610  -34.877 6.663   1.00 39.77  ? 9   LYS I CG  1 
ATOM   9130  C  CD  . LYS E  1 10  ? -52.343  -35.241 5.910   1.00 51.30  ? 9   LYS I CD  1 
ATOM   9131  C  CE  . LYS E  1 10  ? -51.173  -35.561 6.812   1.00 56.82  ? 9   LYS I CE  1 
ATOM   9132  N  NZ  . LYS E  1 10  ? -50.446  -34.323 7.185   1.00 59.16  ? 9   LYS I NZ  1 
ATOM   9133  N  N   . GLY E  1 11  ? -57.336  -36.654 5.153   1.00 29.05  ? 10  GLY I N   1 
ATOM   9134  C  CA  . GLY E  1 11  ? -58.237  -37.697 4.646   1.00 33.05  ? 10  GLY I CA  1 
ATOM   9135  C  C   . GLY E  1 11  ? -58.000  -38.017 3.185   1.00 35.07  ? 10  GLY I C   1 
ATOM   9136  O  O   . GLY E  1 11  ? -57.099  -37.492 2.598   1.00 36.33  ? 10  GLY I O   1 
ATOM   9137  N  N   . ASP E  1 12  ? -58.854  -38.879 2.628   1.00 42.54  ? 11  ASP I N   1 
ATOM   9138  C  CA  . ASP E  1 12  ? -58.803  -39.259 1.199   1.00 49.38  ? 11  ASP I CA  1 
ATOM   9139  C  C   . ASP E  1 12  ? -58.992  -38.036 0.293   1.00 48.05  ? 11  ASP I C   1 
ATOM   9140  O  O   . ASP E  1 12  ? -58.387  -37.958 -0.769  1.00 57.51  ? 11  ASP I O   1 
ATOM   9141  C  CB  . ASP E  1 12  ? -59.889  -40.281 0.851   1.00 58.41  ? 11  ASP I CB  1 
ATOM   9142  C  CG  . ASP E  1 12  ? -59.407  -41.718 0.859   1.00 68.83  ? 11  ASP I CG  1 
ATOM   9143  O  OD1 . ASP E  1 12  ? -58.263  -41.952 1.309   1.00 69.13  ? 11  ASP I OD1 1 
ATOM   9144  O  OD2 . ASP E  1 12  ? -60.180  -42.591 0.405   1.00 83.79  ? 11  ASP I OD2 1 
ATOM   9145  N  N   . GLY E  1 13  ? -59.847  -37.100 0.719   1.00 40.59  ? 12  GLY I N   1 
ATOM   9146  C  CA  . GLY E  1 13  ? -60.298  -36.011 -0.093  1.00 35.72  ? 12  GLY I CA  1 
ATOM   9147  C  C   . GLY E  1 13  ? -59.578  -34.713 0.234   1.00 33.44  ? 12  GLY I C   1 
ATOM   9148  O  O   . GLY E  1 13  ? -58.441  -34.702 0.684   1.00 34.39  ? 12  GLY I O   1 
ATOM   9149  N  N   . PRO E  1 14  ? -60.219  -33.554 -0.012  1.00 31.78  ? 13  PRO I N   1 
ATOM   9150  C  CA  . PRO E  1 14  ? -59.567  -32.268 0.211   1.00 30.42  ? 13  PRO I CA  1 
ATOM   9151  C  C   . PRO E  1 14  ? -59.601  -31.752 1.659   1.00 27.36  ? 13  PRO I C   1 
ATOM   9152  O  O   . PRO E  1 14  ? -59.084  -30.694 1.945   1.00 28.54  ? 13  PRO I O   1 
ATOM   9153  C  CB  . PRO E  1 14  ? -60.400  -31.356 -0.700  1.00 31.86  ? 13  PRO I CB  1 
ATOM   9154  C  CG  . PRO E  1 14  ? -61.787  -31.945 -0.629  1.00 31.70  ? 13  PRO I CG  1 
ATOM   9155  C  CD  . PRO E  1 14  ? -61.579  -33.436 -0.557  1.00 32.05  ? 13  PRO I CD  1 
ATOM   9156  N  N   . VAL E  1 15  ? -60.249  -32.469 2.566   1.00 27.06  ? 14  VAL I N   1 
ATOM   9157  C  CA  . VAL E  1 15  ? -60.438  -31.927 3.897   1.00 27.95  ? 14  VAL I CA  1 
ATOM   9158  C  C   . VAL E  1 15  ? -59.116  -32.027 4.670   1.00 26.56  ? 14  VAL I C   1 
ATOM   9159  O  O   . VAL E  1 15  ? -58.567  -33.084 4.837   1.00 27.20  ? 14  VAL I O   1 
ATOM   9160  C  CB  . VAL E  1 15  ? -61.589  -32.631 4.628   1.00 26.74  ? 14  VAL I CB  1 
ATOM   9161  C  CG1 . VAL E  1 15  ? -61.708  -32.114 6.053   1.00 28.16  ? 14  VAL I CG1 1 
ATOM   9162  C  CG2 . VAL E  1 15  ? -62.903  -32.443 3.883   1.00 29.95  ? 14  VAL I CG2 1 
ATOM   9163  N  N   . GLN E  1 16  ? -58.656  -30.908 5.209   1.00 28.74  ? 15  GLN I N   1 
ATOM   9164  C  CA  . GLN E  1 16  ? -57.481  -30.929 6.057   1.00 30.36  ? 15  GLN I CA  1 
ATOM   9165  C  C   . GLN E  1 16  ? -57.564  -29.777 7.058   1.00 26.90  ? 15  GLN I C   1 
ATOM   9166  O  O   . GLN E  1 16  ? -58.187  -28.761 6.818   1.00 27.50  ? 15  GLN I O   1 
ATOM   9167  C  CB  . GLN E  1 16  ? -56.192  -30.863 5.235   1.00 33.52  ? 15  GLN I CB  1 
ATOM   9168  C  CG  . GLN E  1 16  ? -56.054  -29.607 4.401   1.00 39.88  ? 15  GLN I CG  1 
ATOM   9169  C  CD  . GLN E  1 16  ? -54.739  -29.607 3.654   1.00 48.73  ? 15  GLN I CD  1 
ATOM   9170  O  OE1 . GLN E  1 16  ? -53.684  -29.905 4.212   1.00 56.29  ? 15  GLN I OE1 1 
ATOM   9171  N  NE2 . GLN E  1 16  ? -54.795  -29.297 2.371   1.00 52.67  ? 15  GLN I NE2 1 
ATOM   9172  N  N   . GLY E  1 17  ? -56.915  -29.958 8.196   1.00 23.67  ? 16  GLY I N   1 
ATOM   9173  C  CA  . GLY E  1 17  ? -56.931  -28.907 9.187   1.00 26.27  ? 16  GLY I CA  1 
ATOM   9174  C  C   . GLY E  1 17  ? -56.057  -29.228 10.376  1.00 23.27  ? 16  GLY I C   1 
ATOM   9175  O  O   . GLY E  1 17  ? -55.456  -30.301 10.436  1.00 22.36  ? 16  GLY I O   1 
ATOM   9176  N  N   . ILE E  1 18  ? -55.969  -28.250 11.280  1.00 22.10  ? 17  ILE I N   1 
ATOM   9177  C  CA  . ILE E  1 18  ? -55.218  -28.360 12.482  1.00 22.86  ? 17  ILE I CA  1 
ATOM   9178  C  C   . ILE E  1 18  ? -56.121  -27.923 13.621  1.00 22.57  ? 17  ILE I C   1 
ATOM   9179  O  O   . ILE E  1 18  ? -56.647  -26.810 13.607  1.00 22.91  ? 17  ILE I O   1 
ATOM   9180  C  CB  . ILE E  1 18  ? -53.908  -27.537 12.438  1.00 23.74  ? 17  ILE I CB  1 
ATOM   9181  C  CG1 . ILE E  1 18  ? -52.942  -28.022 11.352  1.00 26.50  ? 17  ILE I CG1 1 
ATOM   9182  C  CG2 . ILE E  1 18  ? -53.256  -27.526 13.814  1.00 26.47  ? 17  ILE I CG2 1 
ATOM   9183  C  CD1 . ILE E  1 18  ? -51.739  -27.097 11.143  1.00 29.19  ? 17  ILE I CD1 1 
ATOM   9184  N  N   . ILE E  1 19  ? -56.237  -28.791 14.634  1.00 22.44  ? 18  ILE I N   1 
ATOM   9185  C  CA  . ILE E  1 19  ? -57.035  -28.477 15.805  1.00 21.28  ? 18  ILE I CA  1 
ATOM   9186  C  C   . ILE E  1 19  ? -56.130  -28.539 17.038  1.00 20.71  ? 18  ILE I C   1 
ATOM   9187  O  O   . ILE E  1 19  ? -55.383  -29.495 17.218  1.00 19.63  ? 18  ILE I O   1 
ATOM   9188  C  CB  . ILE E  1 19  ? -58.243  -29.425 15.917  1.00 21.11  ? 18  ILE I CB  1 
ATOM   9189  C  CG1 . ILE E  1 19  ? -59.177  -29.318 14.708  1.00 23.00  ? 18  ILE I CG1 1 
ATOM   9190  C  CG2 . ILE E  1 19  ? -58.969  -29.178 17.222  1.00 23.11  ? 18  ILE I CG2 1 
ATOM   9191  C  CD1 . ILE E  1 19  ? -59.937  -27.990 14.605  1.00 23.86  ? 18  ILE I CD1 1 
ATOM   9192  N  N   . ASN E  1 20  ? -56.217  -27.492 17.857  1.00 20.21  ? 19  ASN I N   1 
ATOM   9193  C  CA  . ASN E  1 20  ? -55.490  -27.319 19.105  1.00 21.93  ? 19  ASN I CA  1 
ATOM   9194  C  C   . ASN E  1 20  ? -56.438  -27.589 20.265  1.00 22.37  ? 19  ASN I C   1 
ATOM   9195  O  O   . ASN E  1 20  ? -57.638  -27.284 20.181  1.00 22.46  ? 19  ASN I O   1 
ATOM   9196  C  CB  . ASN E  1 20  ? -54.912  -25.901 19.244  1.00 24.49  ? 19  ASN I CB  1 
ATOM   9197  C  CG  . ASN E  1 20  ? -54.135  -25.485 18.012  1.00 26.91  ? 19  ASN I CG  1 
ATOM   9198  O  OD1 . ASN E  1 20  ? -54.629  -24.730 17.154  1.00 32.58  ? 19  ASN I OD1 1 
ATOM   9199  N  ND2 . ASN E  1 20  ? -52.970  -26.074 17.854  1.00 22.69  ? 19  ASN I ND2 1 
ATOM   9200  N  N   . PHE E  1 21  ? -55.880  -28.127 21.349  1.00 21.56  ? 20  PHE I N   1 
ATOM   9201  C  CA  . PHE E  1 21  ? -56.604  -28.308 22.588  1.00 22.26  ? 20  PHE I CA  1 
ATOM   9202  C  C   . PHE E  1 21  ? -55.760  -27.726 23.729  1.00 22.81  ? 20  PHE I C   1 
ATOM   9203  O  O   . PHE E  1 21  ? -54.540  -27.932 23.747  1.00 21.19  ? 20  PHE I O   1 
ATOM   9204  C  CB  . PHE E  1 21  ? -56.863  -29.791 22.868  1.00 22.60  ? 20  PHE I CB  1 
ATOM   9205  C  CG  . PHE E  1 21  ? -57.562  -30.581 21.791  1.00 20.31  ? 20  PHE I CG  1 
ATOM   9206  C  CD1 . PHE E  1 21  ? -58.878  -30.980 21.948  1.00 22.16  ? 20  PHE I CD1 1 
ATOM   9207  C  CD2 . PHE E  1 21  ? -56.883  -30.987 20.658  1.00 21.14  ? 20  PHE I CD2 1 
ATOM   9208  C  CE1 . PHE E  1 21  ? -59.512  -31.726 20.961  1.00 22.30  ? 20  PHE I CE1 1 
ATOM   9209  C  CE2 . PHE E  1 21  ? -57.506  -31.750 19.681  1.00 22.30  ? 20  PHE I CE2 1 
ATOM   9210  C  CZ  . PHE E  1 21  ? -58.826  -32.111 19.831  1.00 21.81  ? 20  PHE I CZ  1 
ATOM   9211  N  N   . GLU E  1 22  ? -56.405  -27.046 24.683  1.00 23.77  ? 21  GLU I N   1 
ATOM   9212  C  CA  . GLU E  1 22  ? -55.713  -26.480 25.872  1.00 27.49  ? 21  GLU I CA  1 
ATOM   9213  C  C   . GLU E  1 22  ? -56.581  -26.786 27.091  1.00 26.89  ? 21  GLU I C   1 
ATOM   9214  O  O   . GLU E  1 22  ? -57.800  -26.661 27.057  1.00 25.27  ? 21  GLU I O   1 
ATOM   9215  C  CB  . GLU E  1 22  ? -55.387  -24.967 25.796  1.00 32.07  ? 21  GLU I CB  1 
ATOM   9216  C  CG  A GLU E  1 22  ? -54.149  -24.896 26.690  0.60 38.61  ? 21  GLU I CG  1 
ATOM   9217  C  CG  B GLU E  1 22  ? -56.520  -24.438 24.966  0.40 34.28  ? 21  GLU I CG  1 
ATOM   9218  C  CD  A GLU E  1 22  ? -53.488  -23.514 26.612  0.60 44.36  ? 21  GLU I CD  1 
ATOM   9219  C  CD  B GLU E  1 22  ? -56.267  -22.963 24.648  0.40 39.44  ? 21  GLU I CD  1 
ATOM   9220  O  OE1 A GLU E  1 22  ? -52.279  -23.391 26.958  0.60 46.94  ? 21  GLU I OE1 1 
ATOM   9221  O  OE1 B GLU E  1 22  ? -55.071  -22.560 24.618  0.40 35.37  ? 21  GLU I OE1 1 
ATOM   9222  O  OE2 A GLU E  1 22  ? -54.182  -22.555 26.176  0.60 44.24  ? 21  GLU I OE2 1 
ATOM   9223  O  OE2 B GLU E  1 22  ? -57.250  -22.214 24.424  0.40 46.10  ? 21  GLU I OE2 1 
ATOM   9224  N  N   . GLN E  1 23  ? -55.925  -27.249 28.152  1.00 26.28  ? 22  GLN I N   1 
ATOM   9225  C  CA  . GLN E  1 23  ? -56.544  -27.511 29.419  1.00 29.68  ? 22  GLN I CA  1 
ATOM   9226  C  C   . GLN E  1 23  ? -55.547  -27.061 30.492  1.00 33.71  ? 22  GLN I C   1 
ATOM   9227  O  O   . GLN E  1 23  ? -54.629  -27.782 30.801  1.00 29.86  ? 22  GLN I O   1 
ATOM   9228  C  CB  . GLN E  1 23  ? -56.876  -28.996 29.588  1.00 25.90  ? 22  GLN I CB  1 
ATOM   9229  C  CG  . GLN E  1 23  ? -57.692  -29.296 30.841  1.00 26.39  ? 22  GLN I CG  1 
ATOM   9230  C  CD  . GLN E  1 23  ? -57.982  -30.768 30.966  1.00 26.21  ? 22  GLN I CD  1 
ATOM   9231  O  OE1 . GLN E  1 23  ? -57.161  -31.588 30.565  1.00 27.51  ? 22  GLN I OE1 1 
ATOM   9232  N  NE2 . GLN E  1 23  ? -59.171  -31.117 31.456  1.00 25.45  ? 22  GLN I NE2 1 
ATOM   9233  N  N   . LYS E  1 24  ? -55.739  -25.861 31.029  1.00 40.82  ? 23  LYS I N   1 
ATOM   9234  C  CA  . LYS E  1 24  ? -54.735  -25.276 31.928  1.00 54.82  ? 23  LYS I CA  1 
ATOM   9235  C  C   . LYS E  1 24  ? -54.801  -25.923 33.320  1.00 49.34  ? 23  LYS I C   1 
ATOM   9236  O  O   . LYS E  1 24  ? -53.798  -25.980 33.986  1.00 53.80  ? 23  LYS I O   1 
ATOM   9237  C  CB  . LYS E  1 24  ? -54.840  -23.747 31.939  1.00 61.78  ? 23  LYS I CB  1 
ATOM   9238  C  CG  . LYS E  1 24  ? -53.988  -23.081 30.861  1.00 74.20  ? 23  LYS I CG  1 
ATOM   9239  C  CD  . LYS E  1 24  ? -54.387  -21.653 30.516  1.00 84.26  ? 23  LYS I CD  1 
ATOM   9240  C  CE  . LYS E  1 24  ? -55.298  -21.542 29.308  1.00 92.35  ? 23  LYS I CE  1 
ATOM   9241  N  NZ  . LYS E  1 24  ? -55.147  -20.230 28.633  1.00 97.40  ? 23  LYS I NZ  1 
ATOM   9242  N  N   . GLU E  1 25  ? -55.931  -26.486 33.743  1.00 51.33  ? 24  GLU I N   1 
ATOM   9243  C  CA  . GLU E  1 25  ? -55.850  -27.338 34.940  1.00 59.51  ? 24  GLU I CA  1 
ATOM   9244  C  C   . GLU E  1 25  ? -56.582  -28.662 34.690  1.00 54.76  ? 24  GLU I C   1 
ATOM   9245  O  O   . GLU E  1 25  ? -57.618  -28.710 34.044  1.00 46.88  ? 24  GLU I O   1 
ATOM   9246  C  CB  . GLU E  1 25  ? -56.303  -26.573 36.191  1.00 72.13  ? 24  GLU I CB  1 
ATOM   9247  C  CG  . GLU E  1 25  ? -57.792  -26.625 36.485  1.00 81.57  ? 24  GLU I CG  1 
ATOM   9248  C  CD  . GLU E  1 25  ? -58.628  -25.609 35.729  1.00 93.08  ? 24  GLU I CD  1 
ATOM   9249  O  OE1 . GLU E  1 25  ? -58.181  -25.165 34.651  1.00 103.37 ? 24  GLU I OE1 1 
ATOM   9250  O  OE2 . GLU E  1 25  ? -59.727  -25.262 36.223  1.00 101.53 ? 24  GLU I OE2 1 
ATOM   9251  N  N   . SER E  1 26  ? -55.996  -29.755 35.187  1.00 55.61  ? 25  SER I N   1 
ATOM   9252  C  CA  . SER E  1 26  ? -56.592  -31.066 35.033  1.00 60.83  ? 25  SER I CA  1 
ATOM   9253  C  C   . SER E  1 26  ? -58.000  -30.948 35.592  1.00 60.88  ? 25  SER I C   1 
ATOM   9254  O  O   . SER E  1 26  ? -58.238  -30.068 36.406  1.00 62.55  ? 25  SER I O   1 
ATOM   9255  C  CB  . SER E  1 26  ? -55.802  -32.136 35.740  1.00 63.68  ? 25  SER I CB  1 
ATOM   9256  O  OG  . SER E  1 26  ? -55.953  -32.019 37.145  1.00 57.79  ? 25  SER I OG  1 
ATOM   9257  N  N   . ASN E  1 27  ? -58.930  -31.775 35.133  1.00 55.96  ? 26  ASN I N   1 
ATOM   9258  C  CA  . ASN E  1 27  ? -60.282  -31.603 35.608  1.00 66.40  ? 26  ASN I CA  1 
ATOM   9259  C  C   . ASN E  1 27  ? -60.985  -30.548 34.743  1.00 60.48  ? 26  ASN I C   1 
ATOM   9260  O  O   . ASN E  1 27  ? -62.056  -30.846 34.197  1.00 68.47  ? 26  ASN I O   1 
ATOM   9261  C  CB  . ASN E  1 27  ? -60.335  -31.210 37.100  1.00 72.26  ? 26  ASN I CB  1 
ATOM   9262  C  CG  . ASN E  1 27  ? -60.549  -29.728 37.383  1.00 75.26  ? 26  ASN I CG  1 
ATOM   9263  O  OD1 . ASN E  1 27  ? -59.694  -29.062 37.976  1.00 72.17  ? 26  ASN I OD1 1 
ATOM   9264  N  ND2 . ASN E  1 27  ? -61.701  -29.198 36.990  1.00 66.76  ? 26  ASN I ND2 1 
ATOM   9265  N  N   . GLY E  1 28  ? -60.383  -29.343 34.649  1.00 48.02  ? 27  GLY I N   1 
ATOM   9266  C  CA  . GLY E  1 28  ? -60.997  -28.121 34.085  1.00 44.35  ? 27  GLY I CA  1 
ATOM   9267  C  C   . GLY E  1 28  ? -61.458  -28.301 32.635  1.00 36.23  ? 27  GLY I C   1 
ATOM   9268  O  O   . GLY E  1 28  ? -61.171  -29.312 32.005  1.00 34.23  ? 27  GLY I O   1 
ATOM   9269  N  N   . PRO E  1 29  ? -62.195  -27.328 32.064  1.00 33.33  ? 28  PRO I N   1 
ATOM   9270  C  CA  . PRO E  1 29  ? -62.646  -27.413 30.677  1.00 32.46  ? 28  PRO I CA  1 
ATOM   9271  C  C   . PRO E  1 29  ? -61.492  -27.433 29.668  1.00 27.97  ? 28  PRO I C   1 
ATOM   9272  O  O   . PRO E  1 29  ? -60.422  -26.925 29.950  1.00 25.23  ? 28  PRO I O   1 
ATOM   9273  C  CB  . PRO E  1 29  ? -63.501  -26.154 30.463  1.00 35.12  ? 28  PRO I CB  1 
ATOM   9274  C  CG  . PRO E  1 29  ? -63.106  -25.228 31.590  1.00 38.04  ? 28  PRO I CG  1 
ATOM   9275  C  CD  . PRO E  1 29  ? -62.654  -26.108 32.733  1.00 36.43  ? 28  PRO I CD  1 
ATOM   9276  N  N   . VAL E  1 30  ? -61.740  -28.023 28.495  1.00 25.14  ? 29  VAL I N   1 
ATOM   9277  C  CA  . VAL E  1 30  ? -60.787  -28.062 27.396  1.00 25.19  ? 29  VAL I CA  1 
ATOM   9278  C  C   . VAL E  1 30  ? -61.244  -27.064 26.331  1.00 24.77  ? 29  VAL I C   1 
ATOM   9279  O  O   . VAL E  1 30  ? -62.386  -27.101 25.911  1.00 24.13  ? 29  VAL I O   1 
ATOM   9280  C  CB  . VAL E  1 30  ? -60.658  -29.480 26.808  1.00 24.95  ? 29  VAL I CB  1 
ATOM   9281  C  CG1 . VAL E  1 30  ? -59.638  -29.526 25.688  1.00 25.30  ? 29  VAL I CG1 1 
ATOM   9282  C  CG2 . VAL E  1 30  ? -60.321  -30.507 27.883  1.00 24.05  ? 29  VAL I CG2 1 
ATOM   9283  N  N   . LYS E  1 31  ? -60.354  -26.158 25.924  1.00 24.07  ? 30  LYS I N   1 
ATOM   9284  C  CA  . LYS E  1 31  ? -60.626  -25.292 24.804  1.00 27.28  ? 30  LYS I CA  1 
ATOM   9285  C  C   . LYS E  1 31  ? -60.118  -25.986 23.543  1.00 25.72  ? 30  LYS I C   1 
ATOM   9286  O  O   . LYS E  1 31  ? -59.001  -26.505 23.542  1.00 23.89  ? 30  LYS I O   1 
ATOM   9287  C  CB  . LYS E  1 31  ? -59.978  -23.919 24.990  1.00 32.84  ? 30  LYS I CB  1 
ATOM   9288  C  CG  . LYS E  1 31  ? -60.500  -23.110 26.166  1.00 42.34  ? 30  LYS I CG  1 
ATOM   9289  C  CD  . LYS E  1 31  ? -59.873  -21.715 26.258  1.00 52.43  ? 30  LYS I CD  1 
ATOM   9290  C  CE  . LYS E  1 31  ? -59.831  -21.164 27.672  1.00 59.93  ? 30  LYS I CE  1 
ATOM   9291  N  NZ  . LYS E  1 31  ? -61.141  -21.300 28.355  1.00 66.06  ? 30  LYS I NZ  1 
ATOM   9292  N  N   . VAL E  1 32  ? -60.948  -25.960 22.490  1.00 23.18  ? 31  VAL I N   1 
ATOM   9293  C  CA  . VAL E  1 32  ? -60.695  -26.624 21.235  1.00 22.35  ? 31  VAL I CA  1 
ATOM   9294  C  C   . VAL E  1 32  ? -60.803  -25.574 20.134  1.00 23.22  ? 31  VAL I C   1 
ATOM   9295  O  O   . VAL E  1 32  ? -61.858  -24.952 19.990  1.00 25.47  ? 31  VAL I O   1 
ATOM   9296  C  CB  . VAL E  1 32  ? -61.711  -27.756 21.002  1.00 22.63  ? 31  VAL I CB  1 
ATOM   9297  C  CG1 . VAL E  1 32  ? -61.440  -28.513 19.712  1.00 21.23  ? 31  VAL I CG1 1 
ATOM   9298  C  CG2 . VAL E  1 32  ? -61.783  -28.700 22.191  1.00 22.59  ? 31  VAL I CG2 1 
ATOM   9299  N  N   . TRP E  1 33  ? -59.733  -25.354 19.381  1.00 20.65  ? 32  TRP I N   1 
ATOM   9300  C  CA  . TRP E  1 33  ? -59.776  -24.298 18.378  1.00 23.86  ? 32  TRP I CA  1 
ATOM   9301  C  C   . TRP E  1 33  ? -58.808  -24.589 17.234  1.00 23.69  ? 32  TRP I C   1 
ATOM   9302  O  O   . TRP E  1 33  ? -57.804  -25.300 17.383  1.00 25.47  ? 32  TRP I O   1 
ATOM   9303  C  CB  . TRP E  1 33  ? -59.521  -22.939 19.018  1.00 25.75  ? 32  TRP I CB  1 
ATOM   9304  C  CG  . TRP E  1 33  ? -58.078  -22.567 19.026  1.00 30.85  ? 32  TRP I CG  1 
ATOM   9305  C  CD1 . TRP E  1 33  ? -57.371  -21.923 18.051  1.00 33.11  ? 32  TRP I CD1 1 
ATOM   9306  C  CD2 . TRP E  1 33  ? -57.139  -22.908 20.044  1.00 31.92  ? 32  TRP I CD2 1 
ATOM   9307  N  NE1 . TRP E  1 33  ? -56.056  -21.825 18.407  1.00 36.71  ? 32  TRP I NE1 1 
ATOM   9308  C  CE2 . TRP E  1 33  ? -55.889  -22.407 19.637  1.00 34.16  ? 32  TRP I CE2 1 
ATOM   9309  C  CE3 . TRP E  1 33  ? -57.247  -23.584 21.251  1.00 34.22  ? 32  TRP I CE3 1 
ATOM   9310  C  CZ2 . TRP E  1 33  ? -54.745  -22.550 20.406  1.00 35.03  ? 32  TRP I CZ2 1 
ATOM   9311  C  CZ3 . TRP E  1 33  ? -56.109  -23.736 22.006  1.00 41.09  ? 32  TRP I CZ3 1 
ATOM   9312  C  CH2 . TRP E  1 33  ? -54.878  -23.219 21.597  1.00 41.85  ? 32  TRP I CH2 1 
ATOM   9313  N  N   . GLY E  1 34  ? -59.150  -24.068 16.062  1.00 21.80  ? 33  GLY I N   1 
ATOM   9314  C  CA  . GLY E  1 34  ? -58.339  -24.261 14.897  1.00 21.87  ? 33  GLY I CA  1 
ATOM   9315  C  C   . GLY E  1 34  ? -59.149  -24.105 13.636  1.00 22.35  ? 33  GLY I C   1 
ATOM   9316  O  O   . GLY E  1 34  ? -60.223  -23.598 13.666  1.00 25.67  ? 33  GLY I O   1 
ATOM   9317  N  N   . SER E  1 35  ? -58.603  -24.581 12.529  1.00 24.45  ? 34  SER I N   1 
ATOM   9318  C  CA  . SER E  1 35  ? -59.147  -24.346 11.229  1.00 26.62  ? 34  SER I CA  1 
ATOM   9319  C  C   . SER E  1 35  ? -59.145  -25.656 10.460  1.00 25.55  ? 34  SER I C   1 
ATOM   9320  O  O   . SER E  1 35  ? -58.123  -26.377 10.493  1.00 28.38  ? 34  SER I O   1 
ATOM   9321  C  CB  . SER E  1 35  ? -58.316  -23.319 10.502  1.00 31.22  ? 34  SER I CB  1 
ATOM   9322  O  OG  . SER E  1 35  ? -59.161  -22.384 9.898   1.00 41.43  ? 34  SER I OG  1 
ATOM   9323  N  N   . ILE E  1 36  ? -60.279  -25.951 9.808   1.00 23.73  ? 35  ILE I N   1 
ATOM   9324  C  CA  . ILE E  1 36  ? -60.434  -27.057 8.887   1.00 24.27  ? 35  ILE I CA  1 
ATOM   9325  C  C   . ILE E  1 36  ? -60.890  -26.453 7.558   1.00 25.91  ? 35  ILE I C   1 
ATOM   9326  O  O   . ILE E  1 36  ? -61.847  -25.669 7.548   1.00 24.89  ? 35  ILE I O   1 
ATOM   9327  C  CB  . ILE E  1 36  ? -61.438  -28.113 9.396   1.00 23.67  ? 35  ILE I CB  1 
ATOM   9328  C  CG1 . ILE E  1 36  ? -61.186  -28.531 10.847  1.00 24.73  ? 35  ILE I CG1 1 
ATOM   9329  C  CG2 . ILE E  1 36  ? -61.436  -29.313 8.468   1.00 23.46  ? 35  ILE I CG2 1 
ATOM   9330  C  CD1 . ILE E  1 36  ? -62.285  -29.356 11.461  1.00 23.56  ? 35  ILE I CD1 1 
ATOM   9331  N  N   . LYS E  1 37  ? -60.224  -26.830 6.454   1.00 25.26  ? 36  LYS I N   1 
ATOM   9332  C  CA  . LYS E  1 37  ? -60.602  -26.328 5.125   1.00 26.93  ? 36  LYS I CA  1 
ATOM   9333  C  C   . LYS E  1 37  ? -61.017  -27.499 4.241   1.00 25.64  ? 36  LYS I C   1 
ATOM   9334  O  O   . LYS E  1 37  ? -60.840  -28.664 4.610   1.00 25.06  ? 36  LYS I O   1 
ATOM   9335  C  CB  . LYS E  1 37  ? -59.456  -25.506 4.528   1.00 31.77  ? 36  LYS I CB  1 
ATOM   9336  C  CG  . LYS E  1 37  ? -58.280  -26.312 4.003   1.00 38.82  ? 36  LYS I CG  1 
ATOM   9337  C  CD  . LYS E  1 37  ? -57.058  -25.451 3.717   1.00 47.53  ? 36  LYS I CD  1 
ATOM   9338  C  CE  . LYS E  1 37  ? -56.040  -26.147 2.837   1.00 52.10  ? 36  LYS I CE  1 
ATOM   9339  N  NZ  . LYS E  1 37  ? -56.227  -25.775 1.414   1.00 62.18  ? 36  LYS I NZ  1 
ATOM   9340  N  N   . GLY E  1 38  ? -61.604  -27.185 3.085   1.00 23.68  ? 37  GLY I N   1 
ATOM   9341  C  CA  . GLY E  1 38  ? -62.024  -28.193 2.129   1.00 23.44  ? 37  GLY I CA  1 
ATOM   9342  C  C   . GLY E  1 38  ? -63.382  -28.816 2.419   1.00 24.06  ? 37  GLY I C   1 
ATOM   9343  O  O   . GLY E  1 38  ? -63.743  -29.831 1.784   1.00 25.90  ? 37  GLY I O   1 
ATOM   9344  N  N   . LEU E  1 39  ? -64.157  -28.229 3.340   1.00 24.08  ? 38  LEU I N   1 
ATOM   9345  C  CA  . LEU E  1 39  ? -65.463  -28.779 3.734   1.00 23.98  ? 38  LEU I CA  1 
ATOM   9346  C  C   . LEU E  1 39  ? -66.573  -28.178 2.867   1.00 24.77  ? 38  LEU I C   1 
ATOM   9347  O  O   . LEU E  1 39  ? -66.444  -27.069 2.392   1.00 25.93  ? 38  LEU I O   1 
ATOM   9348  C  CB  . LEU E  1 39  ? -65.747  -28.438 5.199   1.00 23.78  ? 38  LEU I CB  1 
ATOM   9349  C  CG  . LEU E  1 39  ? -64.868  -29.154 6.225   1.00 23.35  ? 38  LEU I CG  1 
ATOM   9350  C  CD1 . LEU E  1 39  ? -64.958  -28.485 7.585   1.00 22.42  ? 38  LEU I CD1 1 
ATOM   9351  C  CD2 . LEU E  1 39  ? -65.244  -30.614 6.311   1.00 22.33  ? 38  LEU I CD2 1 
ATOM   9352  N  N   . THR E  1 40  ? -67.693  -28.899 2.738   1.00 24.50  ? 39  THR I N   1 
ATOM   9353  C  CA  . THR E  1 40  ? -68.913  -28.308 2.207   1.00 25.24  ? 39  THR I CA  1 
ATOM   9354  C  C   . THR E  1 40  ? -69.453  -27.314 3.237   1.00 26.15  ? 39  THR I C   1 
ATOM   9355  O  O   . THR E  1 40  ? -69.372  -27.532 4.465   1.00 24.64  ? 39  THR I O   1 
ATOM   9356  C  CB  . THR E  1 40  ? -69.939  -29.384 1.833   1.00 25.57  ? 39  THR I CB  1 
ATOM   9357  O  OG1 . THR E  1 40  ? -70.278  -30.114 3.011   1.00 26.50  ? 39  THR I OG1 1 
ATOM   9358  C  CG2 . THR E  1 40  ? -69.425  -30.318 0.762   1.00 26.28  ? 39  THR I CG2 1 
ATOM   9359  N  N   . GLU E  1 41  ? -69.983  -26.200 2.749   1.00 23.60  ? 40  GLU I N   1 
ATOM   9360  C  CA  . GLU E  1 41  ? -70.612  -25.213 3.612   1.00 26.46  ? 40  GLU I CA  1 
ATOM   9361  C  C   . GLU E  1 41  ? -71.667  -25.889 4.498   1.00 25.93  ? 40  GLU I C   1 
ATOM   9362  O  O   . GLU E  1 41  ? -72.419  -26.702 4.024   1.00 24.81  ? 40  GLU I O   1 
ATOM   9363  C  CB  . GLU E  1 41  ? -71.317  -24.137 2.783   1.00 26.83  ? 40  GLU I CB  1 
ATOM   9364  C  CG  . GLU E  1 41  ? -71.925  -23.046 3.633   1.00 29.47  ? 40  GLU I CG  1 
ATOM   9365  C  CD  . GLU E  1 41  ? -72.437  -21.857 2.829   1.00 37.20  ? 40  GLU I CD  1 
ATOM   9366  O  OE1 . GLU E  1 41  ? -72.777  -20.831 3.443   1.00 43.14  ? 40  GLU I OE1 1 
ATOM   9367  O  OE2 . GLU E  1 41  ? -72.443  -21.954 1.593   1.00 36.20  ? 40  GLU I OE2 1 
ATOM   9368  N  N   . GLY E  1 42  ? -71.716  -25.511 5.780   1.00 25.02  ? 41  GLY I N   1 
ATOM   9369  C  CA  . GLY E  1 42  ? -72.745  -26.000 6.708   1.00 25.86  ? 41  GLY I CA  1 
ATOM   9370  C  C   . GLY E  1 42  ? -72.156  -26.877 7.806   1.00 24.73  ? 41  GLY I C   1 
ATOM   9371  O  O   . GLY E  1 42  ? -70.973  -26.820 8.079   1.00 22.94  ? 41  GLY I O   1 
ATOM   9372  N  N   . LEU E  1 43  ? -73.011  -27.694 8.423   1.00 24.73  ? 42  LEU I N   1 
ATOM   9373  C  CA  . LEU E  1 43  ? -72.680  -28.414 9.669   1.00 25.50  ? 42  LEU I CA  1 
ATOM   9374  C  C   . LEU E  1 43  ? -71.990  -29.749 9.369   1.00 23.19  ? 42  LEU I C   1 
ATOM   9375  O  O   . LEU E  1 43  ? -72.387  -30.484 8.462   1.00 22.87  ? 42  LEU I O   1 
ATOM   9376  C  CB  . LEU E  1 43  ? -73.974  -28.659 10.448  1.00 27.28  ? 42  LEU I CB  1 
ATOM   9377  C  CG  . LEU E  1 43  ? -74.635  -27.438 11.074  1.00 30.89  ? 42  LEU I CG  1 
ATOM   9378  C  CD1 . LEU E  1 43  ? -76.075  -27.768 11.444  1.00 33.84  ? 42  LEU I CD1 1 
ATOM   9379  C  CD2 . LEU E  1 43  ? -73.900  -26.966 12.303  1.00 32.15  ? 42  LEU I CD2 1 
ATOM   9380  N  N   . HIS E  1 44  ? -70.977  -30.080 10.178  1.00 20.00  ? 43  HIS I N   1 
ATOM   9381  C  CA  . HIS E  1 44  ? -70.223  -31.350 10.090  1.00 19.56  ? 43  HIS I CA  1 
ATOM   9382  C  C   . HIS E  1 44  ? -70.000  -31.923 11.490  1.00 19.36  ? 43  HIS I C   1 
ATOM   9383  O  O   . HIS E  1 44  ? -69.470  -31.214 12.372  1.00 19.20  ? 43  HIS I O   1 
ATOM   9384  C  CB  . HIS E  1 44  ? -68.873  -31.119 9.403   1.00 19.86  ? 43  HIS I CB  1 
ATOM   9385  C  CG  . HIS E  1 44  ? -69.024  -30.674 7.989   1.00 21.95  ? 43  HIS I CG  1 
ATOM   9386  N  ND1 . HIS E  1 44  ? -69.111  -31.585 6.945   1.00 23.35  ? 43  HIS I ND1 1 
ATOM   9387  C  CD2 . HIS E  1 44  ? -69.120  -29.443 7.441   1.00 22.65  ? 43  HIS I CD2 1 
ATOM   9388  C  CE1 . HIS E  1 44  ? -69.262  -30.918 5.811   1.00 24.39  ? 43  HIS I CE1 1 
ATOM   9389  N  NE2 . HIS E  1 44  ? -69.272  -29.605 6.095   1.00 22.97  ? 43  HIS I NE2 1 
ATOM   9390  N  N   . GLY E  1 45  ? -70.372  -33.195 11.682  1.00 19.04  ? 44  GLY I N   1 
ATOM   9391  C  CA  . GLY E  1 45  ? -70.068  -33.941 12.902  1.00 19.78  ? 44  GLY I CA  1 
ATOM   9392  C  C   . GLY E  1 45  ? -68.580  -33.890 13.226  1.00 19.87  ? 44  GLY I C   1 
ATOM   9393  O  O   . GLY E  1 45  ? -67.739  -33.861 12.332  1.00 17.49  ? 44  GLY I O   1 
ATOM   9394  N  N   . PHE E  1 46  ? -68.275  -33.844 14.525  1.00 18.44  ? 45  PHE I N   1 
ATOM   9395  C  CA  . PHE E  1 46  ? -66.951  -33.582 15.039  1.00 19.09  ? 45  PHE I CA  1 
ATOM   9396  C  C   . PHE E  1 46  ? -66.797  -34.355 16.351  1.00 19.09  ? 45  PHE I C   1 
ATOM   9397  O  O   . PHE E  1 46  ? -67.432  -33.994 17.333  1.00 18.47  ? 45  PHE I O   1 
ATOM   9398  C  CB  . PHE E  1 46  ? -66.826  -32.079 15.298  1.00 20.61  ? 45  PHE I CB  1 
ATOM   9399  C  CG  . PHE E  1 46  ? -65.447  -31.554 15.572  1.00 20.08  ? 45  PHE I CG  1 
ATOM   9400  C  CD1 . PHE E  1 46  ? -64.448  -31.653 14.618  1.00 21.00  ? 45  PHE I CD1 1 
ATOM   9401  C  CD2 . PHE E  1 46  ? -65.154  -30.949 16.780  1.00 21.81  ? 45  PHE I CD2 1 
ATOM   9402  C  CE1 . PHE E  1 46  ? -63.195  -31.109 14.851  1.00 21.23  ? 45  PHE I CE1 1 
ATOM   9403  C  CE2 . PHE E  1 46  ? -63.890  -30.420 17.016  1.00 23.66  ? 45  PHE I CE2 1 
ATOM   9404  C  CZ  . PHE E  1 46  ? -62.927  -30.477 16.041  1.00 21.49  ? 45  PHE I CZ  1 
ATOM   9405  N  N   . HIS E  1 47  ? -66.010  -35.437 16.345  1.00 18.10  ? 46  HIS I N   1 
ATOM   9406  C  CA  . HIS E  1 47  ? -65.981  -36.319 17.521  1.00 20.22  ? 46  HIS I CA  1 
ATOM   9407  C  C   . HIS E  1 47  ? -64.588  -36.849 17.782  1.00 18.98  ? 46  HIS I C   1 
ATOM   9408  O  O   . HIS E  1 47  ? -63.794  -36.964 16.861  1.00 20.82  ? 46  HIS I O   1 
ATOM   9409  C  CB  . HIS E  1 47  ? -66.862  -37.571 17.344  1.00 21.69  ? 46  HIS I CB  1 
ATOM   9410  C  CG  . HIS E  1 47  ? -68.165  -37.290 16.692  1.00 22.00  ? 46  HIS I CG  1 
ATOM   9411  N  ND1 . HIS E  1 47  ? -68.502  -37.839 15.479  1.00 23.12  ? 46  HIS I ND1 1 
ATOM   9412  C  CD2 . HIS E  1 47  ? -69.214  -36.538 17.087  1.00 21.22  ? 46  HIS I CD2 1 
ATOM   9413  C  CE1 . HIS E  1 47  ? -69.704  -37.406 15.146  1.00 23.18  ? 46  HIS I CE1 1 
ATOM   9414  N  NE2 . HIS E  1 47  ? -70.162  -36.612 16.112  1.00 20.87  ? 46  HIS I NE2 1 
ATOM   9415  N  N   . VAL E  1 48  ? -64.372  -37.265 19.034  1.00 19.09  ? 47  VAL I N   1 
ATOM   9416  C  CA  . VAL E  1 48  ? -63.238  -38.064 19.376  1.00 19.41  ? 47  VAL I CA  1 
ATOM   9417  C  C   . VAL E  1 48  ? -63.668  -39.528 19.338  1.00 22.03  ? 47  VAL I C   1 
ATOM   9418  O  O   . VAL E  1 48  ? -64.632  -39.917 20.015  1.00 21.53  ? 47  VAL I O   1 
ATOM   9419  C  CB  . VAL E  1 48  ? -62.662  -37.684 20.747  1.00 20.26  ? 47  VAL I CB  1 
ATOM   9420  C  CG1 . VAL E  1 48  ? -61.452  -38.540 21.075  1.00 20.06  ? 47  VAL I CG1 1 
ATOM   9421  C  CG2 . VAL E  1 48  ? -62.284  -36.210 20.799  1.00 20.88  ? 47  VAL I CG2 1 
ATOM   9422  N  N   . HIS E  1 49  ? -62.946  -40.296 18.515  1.00 21.01  ? 48  HIS I N   1 
ATOM   9423  C  CA  . HIS E  1 49  ? -63.127  -41.718 18.335  1.00 21.00  ? 48  HIS I CA  1 
ATOM   9424  C  C   . HIS E  1 49  ? -62.147  -42.457 19.252  1.00 21.95  ? 48  HIS I C   1 
ATOM   9425  O  O   . HIS E  1 49  ? -61.143  -41.907 19.677  1.00 21.81  ? 48  HIS I O   1 
ATOM   9426  C  CB  . HIS E  1 49  ? -63.010  -42.058 16.841  1.00 19.99  ? 48  HIS I CB  1 
ATOM   9427  C  CG  . HIS E  1 49  ? -64.219  -41.648 16.056  1.00 21.85  ? 48  HIS I CG  1 
ATOM   9428  N  ND1 . HIS E  1 49  ? -65.016  -42.572 15.418  1.00 22.17  ? 48  HIS I ND1 1 
ATOM   9429  C  CD2 . HIS E  1 49  ? -64.791  -40.442 15.829  1.00 20.20  ? 48  HIS I CD2 1 
ATOM   9430  C  CE1 . HIS E  1 49  ? -66.030  -41.954 14.835  1.00 24.10  ? 48  HIS I CE1 1 
ATOM   9431  N  NE2 . HIS E  1 49  ? -65.938  -40.653 15.088  1.00 22.52  ? 48  HIS I NE2 1 
ATOM   9432  N  N   . GLU E  1 50  ? -62.428  -43.726 19.530  1.00 23.14  ? 49  GLU I N   1 
ATOM   9433  C  CA  . GLU E  1 50  ? -61.765  -44.420 20.641  1.00 22.75  ? 49  GLU I CA  1 
ATOM   9434  C  C   . GLU E  1 50  ? -60.282  -44.668 20.354  1.00 21.75  ? 49  GLU I C   1 
ATOM   9435  O  O   . GLU E  1 50  ? -59.478  -44.490 21.236  1.00 22.25  ? 49  GLU I O   1 
ATOM   9436  C  CB  . GLU E  1 50  ? -62.456  -45.745 20.912  1.00 25.81  ? 49  GLU I CB  1 
ATOM   9437  C  CG  . GLU E  1 50  ? -61.833  -46.511 22.060  1.00 29.42  ? 49  GLU I CG  1 
ATOM   9438  C  CD  . GLU E  1 50  ? -62.614  -47.732 22.527  1.00 33.03  ? 49  GLU I CD  1 
ATOM   9439  O  OE1 . GLU E  1 50  ? -62.183  -48.320 23.530  1.00 36.98  ? 49  GLU I OE1 1 
ATOM   9440  O  OE2 . GLU E  1 50  ? -63.621  -48.100 21.872  1.00 33.89  ? 49  GLU I OE2 1 
ATOM   9441  N  N   . PHE E  1 51  ? -59.926  -45.079 19.133  1.00 21.56  ? 50  PHE I N   1 
ATOM   9442  C  CA  . PHE E  1 51  ? -58.555  -45.528 18.881  1.00 22.77  ? 50  PHE I CA  1 
ATOM   9443  C  C   . PHE E  1 51  ? -57.788  -44.502 18.059  1.00 21.85  ? 50  PHE I C   1 
ATOM   9444  O  O   . PHE E  1 51  ? -58.323  -43.930 17.126  1.00 25.44  ? 50  PHE I O   1 
ATOM   9445  C  CB  . PHE E  1 51  ? -58.572  -46.879 18.170  1.00 23.64  ? 50  PHE I CB  1 
ATOM   9446  C  CG  . PHE E  1 51  ? -59.379  -47.907 18.902  1.00 24.63  ? 50  PHE I CG  1 
ATOM   9447  C  CD1 . PHE E  1 51  ? -59.039  -48.285 20.193  1.00 28.30  ? 50  PHE I CD1 1 
ATOM   9448  C  CD2 . PHE E  1 51  ? -60.497  -48.472 18.313  1.00 28.46  ? 50  PHE I CD2 1 
ATOM   9449  C  CE1 . PHE E  1 51  ? -59.796  -49.231 20.869  1.00 28.11  ? 50  PHE I CE1 1 
ATOM   9450  C  CE2 . PHE E  1 51  ? -61.259  -49.410 18.999  1.00 29.37  ? 50  PHE I CE2 1 
ATOM   9451  C  CZ  . PHE E  1 51  ? -60.909  -49.779 20.276  1.00 27.96  ? 50  PHE I CZ  1 
ATOM   9452  N  N   . GLY E  1 52  ? -56.522  -44.306 18.419  1.00 21.63  ? 51  GLY I N   1 
ATOM   9453  C  CA  . GLY E  1 52  ? -55.581  -43.506 17.654  1.00 23.05  ? 51  GLY I CA  1 
ATOM   9454  C  C   . GLY E  1 52  ? -54.869  -44.371 16.625  1.00 26.04  ? 51  GLY I C   1 
ATOM   9455  O  O   . GLY E  1 52  ? -53.644  -44.360 16.539  1.00 25.63  ? 51  GLY I O   1 
ATOM   9456  N  N   . ASP E  1 53  ? -55.675  -45.112 15.856  1.00 25.95  ? 52  ASP I N   1 
ATOM   9457  C  CA  . ASP E  1 53  ? -55.240  -46.139 14.930  1.00 26.24  ? 52  ASP I CA  1 
ATOM   9458  C  C   . ASP E  1 53  ? -55.678  -45.712 13.530  1.00 25.06  ? 52  ASP I C   1 
ATOM   9459  O  O   . ASP E  1 53  ? -56.858  -45.708 13.214  1.00 25.56  ? 52  ASP I O   1 
ATOM   9460  C  CB  . ASP E  1 53  ? -55.836  -47.483 15.313  1.00 26.88  ? 52  ASP I CB  1 
ATOM   9461  C  CG  . ASP E  1 53  ? -55.427  -48.645 14.424  1.00 28.92  ? 52  ASP I CG  1 
ATOM   9462  O  OD1 . ASP E  1 53  ? -55.585  -49.770 14.893  1.00 29.92  ? 52  ASP I OD1 1 
ATOM   9463  O  OD2 . ASP E  1 53  ? -54.964  -48.409 13.295  1.00 26.52  ? 52  ASP I OD2 1 
ATOM   9464  N  N   . ASN E  1 54  ? -54.721  -45.262 12.735  1.00 25.88  ? 53  ASN I N   1 
ATOM   9465  C  CA  . ASN E  1 54  ? -55.040  -44.807 11.421  1.00 31.43  ? 53  ASN I CA  1 
ATOM   9466  C  C   . ASN E  1 54  ? -54.398  -45.772 10.403  1.00 30.11  ? 53  ASN I C   1 
ATOM   9467  O  O   . ASN E  1 54  ? -54.159  -45.407 9.279   1.00 28.20  ? 53  ASN I O   1 
ATOM   9468  C  CB  . ASN E  1 54  ? -54.718  -43.313 11.281  1.00 37.11  ? 53  ASN I CB  1 
ATOM   9469  C  CG  . ASN E  1 54  ? -55.585  -42.423 12.176  1.00 44.42  ? 53  ASN I CG  1 
ATOM   9470  O  OD1 . ASN E  1 54  ? -56.535  -42.870 12.841  1.00 46.36  ? 53  ASN I OD1 1 
ATOM   9471  N  ND2 . ASN E  1 54  ? -55.290  -41.132 12.193  1.00 42.65  ? 53  ASN I ND2 1 
ATOM   9472  N  N   . THR E  1 55  ? -54.253  -47.046 10.775  1.00 29.72  ? 54  THR I N   1 
ATOM   9473  C  CA  . THR E  1 55  ? -53.626  -48.034 9.894   1.00 31.73  ? 54  THR I CA  1 
ATOM   9474  C  C   . THR E  1 55  ? -54.497  -48.321 8.659   1.00 34.31  ? 54  THR I C   1 
ATOM   9475  O  O   . THR E  1 55  ? -53.957  -48.676 7.628   1.00 35.46  ? 54  THR I O   1 
ATOM   9476  C  CB  . THR E  1 55  ? -53.287  -49.336 10.627  1.00 29.95  ? 54  THR I CB  1 
ATOM   9477  O  OG1 . THR E  1 55  ? -54.486  -49.844 11.199  1.00 29.47  ? 54  THR I OG1 1 
ATOM   9478  C  CG2 . THR E  1 55  ? -52.247  -49.142 11.705  1.00 30.55  ? 54  THR I CG2 1 
ATOM   9479  N  N   . ALA E  1 56  ? -55.817  -48.162 8.754   1.00 31.84  ? 55  ALA I N   1 
ATOM   9480  C  CA  . ALA E  1 56  ? -56.695  -48.281 7.582   1.00 34.14  ? 55  ALA I CA  1 
ATOM   9481  C  C   . ALA E  1 56  ? -57.454  -46.967 7.375   1.00 35.09  ? 55  ALA I C   1 
ATOM   9482  O  O   . ALA E  1 56  ? -58.661  -46.974 7.151   1.00 41.38  ? 55  ALA I O   1 
ATOM   9483  C  CB  . ALA E  1 56  ? -57.654  -49.440 7.770   1.00 36.45  ? 55  ALA I CB  1 
ATOM   9484  N  N   . GLY E  1 57  ? -56.735  -45.851 7.475   1.00 32.66  ? 56  GLY I N   1 
ATOM   9485  C  CA  . GLY E  1 57  ? -57.330  -44.518 7.446   1.00 33.98  ? 56  GLY I CA  1 
ATOM   9486  C  C   . GLY E  1 57  ? -58.228  -44.281 8.655   1.00 33.36  ? 56  GLY I C   1 
ATOM   9487  O  O   . GLY E  1 57  ? -58.017  -44.849 9.756   1.00 32.24  ? 56  GLY I O   1 
ATOM   9488  N  N   . CYS E  1 58  ? -59.271  -43.485 8.439   1.00 31.48  ? 57  CYS I N   1 
ATOM   9489  C  CA  . CYS E  1 58  ? -60.168  -43.060 9.514   1.00 31.73  ? 57  CYS I CA  1 
ATOM   9490  C  C   . CYS E  1 58  ? -61.040  -44.230 9.998   1.00 30.51  ? 57  CYS I C   1 
ATOM   9491  O  O   . CYS E  1 58  ? -61.484  -44.232 11.129  1.00 26.18  ? 57  CYS I O   1 
ATOM   9492  C  CB  . CYS E  1 58  ? -60.985  -41.862 9.051   1.00 33.12  ? 57  CYS I CB  1 
ATOM   9493  S  SG  . CYS E  1 58  ? -59.958  -40.423 8.636   1.00 35.01  ? 57  CYS I SG  1 
ATOM   9494  N  N   . THR E  1 59  ? -61.239  -45.257 9.165   1.00 30.44  ? 58  THR I N   1 
ATOM   9495  C  CA  . THR E  1 59  ? -62.071  -46.419 9.564   1.00 32.38  ? 58  THR I CA  1 
ATOM   9496  C  C   . THR E  1 59  ? -61.526  -47.114 10.818  1.00 28.28  ? 58  THR I C   1 
ATOM   9497  O  O   . THR E  1 59  ? -62.306  -47.570 11.672  1.00 30.40  ? 58  THR I O   1 
ATOM   9498  C  CB  . THR E  1 59  ? -62.136  -47.511 8.486   1.00 37.84  ? 58  THR I CB  1 
ATOM   9499  O  OG1 . THR E  1 59  ? -62.184  -46.877 7.215   1.00 46.67  ? 58  THR I OG1 1 
ATOM   9500  C  CG2 . THR E  1 59  ? -63.328  -48.420 8.675   1.00 40.13  ? 58  THR I CG2 1 
ATOM   9501  N  N   . SER E  1 60  ? -60.199  -47.182 10.956  1.00 25.31  ? 59  SER I N   1 
ATOM   9502  C  CA  . SER E  1 60  ? -59.612  -47.956 12.074  1.00 26.99  ? 59  SER I CA  1 
ATOM   9503  C  C   . SER E  1 60  ? -59.652  -47.204 13.411  1.00 25.36  ? 59  SER I C   1 
ATOM   9504  O  O   . SER E  1 60  ? -59.294  -47.770 14.418  1.00 24.45  ? 59  SER I O   1 
ATOM   9505  C  CB  . SER E  1 60  ? -58.226  -48.459 11.734  1.00 28.67  ? 59  SER I CB  1 
ATOM   9506  O  OG  A SER E  1 60  ? -57.487  -47.485 11.030  0.60 29.84  ? 59  SER I OG  1 
ATOM   9507  O  OG  B SER E  1 60  ? -57.486  -47.481 11.031  0.40 29.28  ? 59  SER I OG  1 
ATOM   9508  N  N   . ALA E  1 61  ? -60.165  -45.964 13.432  1.00 25.28  ? 60  ALA I N   1 
ATOM   9509  C  CA  . ALA E  1 61  ? -60.313  -45.180 14.673  1.00 23.17  ? 60  ALA I CA  1 
ATOM   9510  C  C   . ALA E  1 61  ? -61.395  -45.774 15.586  1.00 23.44  ? 60  ALA I C   1 
ATOM   9511  O  O   . ALA E  1 61  ? -61.505  -45.392 16.750  1.00 24.08  ? 60  ALA I O   1 
ATOM   9512  C  CB  . ALA E  1 61  ? -60.634  -43.752 14.330  1.00 23.32  ? 60  ALA I CB  1 
ATOM   9513  N  N   . GLY E  1 62  ? -62.230  -46.661 15.042  1.00 22.21  ? 61  GLY I N   1 
ATOM   9514  C  CA  . GLY E  1 62  ? -63.251  -47.307 15.799  1.00 23.80  ? 61  GLY I CA  1 
ATOM   9515  C  C   . GLY E  1 62  ? -64.429  -46.374 16.053  1.00 24.02  ? 61  GLY I C   1 
ATOM   9516  O  O   . GLY E  1 62  ? -64.585  -45.371 15.354  1.00 24.45  ? 61  GLY I O   1 
ATOM   9517  N  N   . PRO E  1 63  ? -65.287  -46.697 17.044  1.00 25.16  ? 62  PRO I N   1 
ATOM   9518  C  CA  . PRO E  1 63  ? -66.456  -45.886 17.362  1.00 24.70  ? 62  PRO I CA  1 
ATOM   9519  C  C   . PRO E  1 63  ? -66.092  -44.649 18.196  1.00 21.67  ? 62  PRO I C   1 
ATOM   9520  O  O   . PRO E  1 63  ? -64.927  -44.407 18.459  1.00 20.21  ? 62  PRO I O   1 
ATOM   9521  C  CB  . PRO E  1 63  ? -67.310  -46.868 18.171  1.00 26.82  ? 62  PRO I CB  1 
ATOM   9522  C  CG  . PRO E  1 63  ? -66.279  -47.674 18.929  1.00 26.03  ? 62  PRO I CG  1 
ATOM   9523  C  CD  . PRO E  1 63  ? -65.182  -47.883 17.913  1.00 26.77  ? 62  PRO I CD  1 
ATOM   9524  N  N   . HIS E  1 64  ? -67.113  -43.878 18.578  1.00 20.82  ? 63  HIS I N   1 
ATOM   9525  C  CA  . HIS E  1 64  ? -66.944  -42.728 19.425  1.00 22.23  ? 63  HIS I CA  1 
ATOM   9526  C  C   . HIS E  1 64  ? -66.321  -43.174 20.738  1.00 21.79  ? 63  HIS I C   1 
ATOM   9527  O  O   . HIS E  1 64  ? -66.615  -44.247 21.221  1.00 21.31  ? 63  HIS I O   1 
ATOM   9528  C  CB  . HIS E  1 64  ? -68.275  -42.000 19.673  1.00 22.54  ? 63  HIS I CB  1 
ATOM   9529  C  CG  . HIS E  1 64  ? -68.796  -41.389 18.424  1.00 23.51  ? 63  HIS I CG  1 
ATOM   9530  N  ND1 . HIS E  1 64  ? -69.932  -40.624 18.379  1.00 23.92  ? 63  HIS I ND1 1 
ATOM   9531  C  CD2 . HIS E  1 64  ? -68.303  -41.424 17.162  1.00 25.67  ? 63  HIS I CD2 1 
ATOM   9532  C  CE1 . HIS E  1 64  ? -70.140  -40.248 17.123  1.00 25.04  ? 63  HIS I CE1 1 
ATOM   9533  N  NE2 . HIS E  1 64  ? -69.112  -40.673 16.357  1.00 26.15  ? 63  HIS I NE2 1 
ATOM   9534  N  N   . PHE E  1 65  ? -65.447  -42.334 21.280  1.00 20.32  ? 64  PHE I N   1 
ATOM   9535  C  CA  . PHE E  1 65  ? -64.850  -42.584 22.572  1.00 21.63  ? 64  PHE I CA  1 
ATOM   9536  C  C   . PHE E  1 65  ? -65.960  -42.528 23.622  1.00 22.16  ? 64  PHE I C   1 
ATOM   9537  O  O   . PHE E  1 65  ? -66.619  -41.501 23.760  1.00 21.13  ? 64  PHE I O   1 
ATOM   9538  C  CB  . PHE E  1 65  ? -63.766  -41.545 22.847  1.00 20.99  ? 64  PHE I CB  1 
ATOM   9539  C  CG  . PHE E  1 65  ? -63.100  -41.687 24.188  1.00 22.12  ? 64  PHE I CG  1 
ATOM   9540  C  CD1 . PHE E  1 65  ? -62.788  -40.565 24.937  1.00 23.08  ? 64  PHE I CD1 1 
ATOM   9541  C  CD2 . PHE E  1 65  ? -62.788  -42.937 24.702  1.00 22.78  ? 64  PHE I CD2 1 
ATOM   9542  C  CE1 . PHE E  1 65  ? -62.158  -40.690 26.167  1.00 24.14  ? 64  PHE I CE1 1 
ATOM   9543  C  CE2 . PHE E  1 65  ? -62.187  -43.056 25.946  1.00 24.20  ? 64  PHE I CE2 1 
ATOM   9544  C  CZ  . PHE E  1 65  ? -61.860  -41.927 26.665  1.00 22.96  ? 64  PHE I CZ  1 
ATOM   9545  N  N   . ASN E  1 66  ? -66.191  -43.649 24.315  1.00 21.88  ? 65  ASN I N   1 
ATOM   9546  C  CA  . ASN E  1 66  ? -67.382  -43.821 25.110  1.00 22.98  ? 65  ASN I CA  1 
ATOM   9547  C  C   . ASN E  1 66  ? -67.091  -44.628 26.375  1.00 25.55  ? 65  ASN I C   1 
ATOM   9548  O  O   . ASN E  1 66  ? -67.688  -45.687 26.602  1.00 25.20  ? 65  ASN I O   1 
ATOM   9549  C  CB  . ASN E  1 66  ? -68.472  -44.475 24.273  1.00 23.64  ? 65  ASN I CB  1 
ATOM   9550  C  CG  . ASN E  1 66  ? -69.810  -44.556 24.978  1.00 24.55  ? 65  ASN I CG  1 
ATOM   9551  O  OD1 . ASN E  1 66  ? -70.089  -43.797 25.911  1.00 24.00  ? 65  ASN I OD1 1 
ATOM   9552  N  ND2 . ASN E  1 66  ? -70.650  -45.468 24.510  1.00 24.67  ? 65  ASN I ND2 1 
ATOM   9553  N  N   . PRO E  1 67  ? -66.188  -44.173 27.262  1.00 26.59  ? 66  PRO I N   1 
ATOM   9554  C  CA  . PRO E  1 67  ? -65.825  -44.987 28.425  1.00 29.99  ? 66  PRO I CA  1 
ATOM   9555  C  C   . PRO E  1 67  ? -66.966  -45.217 29.432  1.00 33.92  ? 66  PRO I C   1 
ATOM   9556  O  O   . PRO E  1 67  ? -66.891  -46.160 30.186  1.00 35.37  ? 66  PRO I O   1 
ATOM   9557  C  CB  . PRO E  1 67  ? -64.680  -44.207 29.067  1.00 28.25  ? 66  PRO I CB  1 
ATOM   9558  C  CG  . PRO E  1 67  ? -64.956  -42.780 28.647  1.00 27.43  ? 66  PRO I CG  1 
ATOM   9559  C  CD  . PRO E  1 67  ? -65.478  -42.889 27.231  1.00 26.06  ? 66  PRO I CD  1 
ATOM   9560  N  N   . LEU E  1 68  ? -68.026  -44.398 29.410  1.00 32.57  ? 67  LEU I N   1 
ATOM   9561  C  CA  . LEU E  1 68  ? -69.148  -44.581 30.346  1.00 33.81  ? 67  LEU I CA  1 
ATOM   9562  C  C   . LEU E  1 68  ? -70.332  -45.335 29.723  1.00 32.44  ? 67  LEU I C   1 
ATOM   9563  O  O   . LEU E  1 68  ? -71.390  -45.405 30.345  1.00 31.36  ? 67  LEU I O   1 
ATOM   9564  C  CB  . LEU E  1 68  ? -69.572  -43.199 30.836  1.00 34.69  ? 67  LEU I CB  1 
ATOM   9565  C  CG  . LEU E  1 68  ? -68.472  -42.500 31.619  1.00 38.80  ? 67  LEU I CG  1 
ATOM   9566  C  CD1 . LEU E  1 68  ? -68.858  -41.076 31.956  1.00 42.33  ? 67  LEU I CD1 1 
ATOM   9567  C  CD2 . LEU E  1 68  ? -68.125  -43.292 32.873  1.00 40.94  ? 67  LEU I CD2 1 
ATOM   9568  N  N   . SER E  1 69  ? -70.162  -45.870 28.502  1.00 31.71  ? 68  SER I N   1 
ATOM   9569  C  CA  . SER E  1 69  ? -71.142  -46.691 27.825  1.00 32.38  ? 68  SER I CA  1 
ATOM   9570  C  C   . SER E  1 69  ? -72.509  -46.008 27.771  1.00 32.34  ? 68  SER I C   1 
ATOM   9571  O  O   . SER E  1 69  ? -73.515  -46.607 28.122  1.00 32.68  ? 68  SER I O   1 
ATOM   9572  C  CB  . SER E  1 69  ? -71.246  -48.059 28.466  1.00 34.82  ? 68  SER I CB  1 
ATOM   9573  O  OG  . SER E  1 69  ? -69.982  -48.700 28.408  1.00 38.54  ? 68  SER I OG  1 
ATOM   9574  N  N   . ARG E  1 70  ? -72.536  -44.758 27.308  1.00 29.51  ? 69  ARG I N   1 
ATOM   9575  C  CA  . ARG E  1 70  ? -73.769  -44.037 27.116  1.00 28.70  ? 69  ARG I CA  1 
ATOM   9576  C  C   . ARG E  1 70  ? -74.142  -44.031 25.628  1.00 27.96  ? 69  ARG I C   1 
ATOM   9577  O  O   . ARG E  1 70  ? -73.379  -44.479 24.776  1.00 25.96  ? 69  ARG I O   1 
ATOM   9578  C  CB  . ARG E  1 70  ? -73.606  -42.598 27.587  1.00 32.68  ? 69  ARG I CB  1 
ATOM   9579  C  CG  . ARG E  1 70  ? -72.905  -42.442 28.926  1.00 38.36  ? 69  ARG I CG  1 
ATOM   9580  C  CD  . ARG E  1 70  ? -73.865  -42.423 30.080  1.00 42.93  ? 69  ARG I CD  1 
ATOM   9581  N  NE  . ARG E  1 70  ? -73.214  -42.060 31.335  1.00 49.00  ? 69  ARG I NE  1 
ATOM   9582  C  CZ  . ARG E  1 70  ? -73.447  -40.937 32.020  1.00 55.95  ? 69  ARG I CZ  1 
ATOM   9583  N  NH1 . ARG E  1 70  ? -72.994  -40.805 33.257  1.00 59.92  ? 69  ARG I NH1 1 
ATOM   9584  N  NH2 . ARG E  1 70  ? -74.135  -39.950 31.477  1.00 64.34  ? 69  ARG I NH2 1 
ATOM   9585  N  N   . LYS E  1 71  ? -75.328  -43.491 25.338  1.00 25.80  ? 70  LYS I N   1 
ATOM   9586  C  CA  . LYS E  1 71  ? -75.776  -43.240 23.992  1.00 27.49  ? 70  LYS I CA  1 
ATOM   9587  C  C   . LYS E  1 71  ? -75.215  -41.892 23.533  1.00 25.13  ? 70  LYS I C   1 
ATOM   9588  O  O   . LYS E  1 71  ? -74.867  -41.024 24.345  1.00 23.21  ? 70  LYS I O   1 
ATOM   9589  C  CB  . LYS E  1 71  ? -77.303  -43.235 23.901  1.00 32.74  ? 70  LYS I CB  1 
ATOM   9590  C  CG  . LYS E  1 71  ? -77.960  -44.581 24.197  1.00 40.43  ? 70  LYS I CG  1 
ATOM   9591  C  CD  . LYS E  1 71  ? -79.478  -44.535 24.247  1.00 49.95  ? 70  LYS I CD  1 
ATOM   9592  C  CE  . LYS E  1 71  ? -80.026  -43.757 25.431  1.00 60.53  ? 70  LYS I CE  1 
ATOM   9593  N  NZ  . LYS E  1 71  ? -81.495  -43.929 25.587  1.00 68.09  ? 70  LYS I NZ  1 
ATOM   9594  N  N   . HIS E  1 72  ? -75.138  -41.754 22.210  1.00 24.12  ? 71  HIS I N   1 
ATOM   9595  C  CA  . HIS E  1 72  ? -74.630  -40.562 21.561  1.00 23.24  ? 71  HIS I CA  1 
ATOM   9596  C  C   . HIS E  1 72  ? -75.548  -39.386 21.892  1.00 22.96  ? 71  HIS I C   1 
ATOM   9597  O  O   . HIS E  1 72  ? -76.775  -39.530 21.965  1.00 23.30  ? 71  HIS I O   1 
ATOM   9598  C  CB  . HIS E  1 72  ? -74.524  -40.816 20.052  1.00 23.15  ? 71  HIS I CB  1 
ATOM   9599  C  CG  . HIS E  1 72  ? -74.102  -39.608 19.284  1.00 23.07  ? 71  HIS I CG  1 
ATOM   9600  N  ND1 . HIS E  1 72  ? -72.792  -39.161 19.250  1.00 25.36  ? 71  HIS I ND1 1 
ATOM   9601  C  CD2 . HIS E  1 72  ? -74.817  -38.731 18.555  1.00 22.44  ? 71  HIS I CD2 1 
ATOM   9602  C  CE1 . HIS E  1 72  ? -72.731  -38.073 18.501  1.00 25.63  ? 71  HIS I CE1 1 
ATOM   9603  N  NE2 . HIS E  1 72  ? -73.948  -37.789 18.077  1.00 22.66  ? 71  HIS I NE2 1 
ATOM   9604  N  N   . GLY E  1 73  ? -74.946  -38.219 22.082  1.00 21.99  ? 72  GLY I N   1 
ATOM   9605  C  CA  . GLY E  1 73  ? -75.689  -37.008 22.278  1.00 22.47  ? 72  GLY I CA  1 
ATOM   9606  C  C   . GLY E  1 73  ? -74.914  -35.823 21.754  1.00 22.23  ? 72  GLY I C   1 
ATOM   9607  O  O   . GLY E  1 73  ? -73.912  -35.971 21.089  1.00 22.84  ? 72  GLY I O   1 
ATOM   9608  N  N   . GLY E  1 74  ? -75.434  -34.633 22.038  1.00 23.28  ? 73  GLY I N   1 
ATOM   9609  C  CA  . GLY E  1 74  ? -74.719  -33.411 21.777  1.00 23.71  ? 73  GLY I CA  1 
ATOM   9610  C  C   . GLY E  1 74  ? -73.862  -33.060 22.984  1.00 25.03  ? 73  GLY I C   1 
ATOM   9611  O  O   . GLY E  1 74  ? -74.100  -33.543 24.097  1.00 24.13  ? 73  GLY I O   1 
ATOM   9612  N  N   . PRO E  1 75  ? -72.839  -32.200 22.819  1.00 25.66  ? 74  PRO I N   1 
ATOM   9613  C  CA  . PRO E  1 75  ? -71.954  -31.885 23.934  1.00 24.72  ? 74  PRO I CA  1 
ATOM   9614  C  C   . PRO E  1 75  ? -72.663  -31.317 25.177  1.00 28.00  ? 74  PRO I C   1 
ATOM   9615  O  O   . PRO E  1 75  ? -72.171  -31.517 26.269  1.00 27.83  ? 74  PRO I O   1 
ATOM   9616  C  CB  . PRO E  1 75  ? -70.941  -30.901 23.334  1.00 23.63  ? 74  PRO I CB  1 
ATOM   9617  C  CG  . PRO E  1 75  ? -71.584  -30.380 22.075  1.00 25.21  ? 74  PRO I CG  1 
ATOM   9618  C  CD  . PRO E  1 75  ? -72.476  -31.504 21.576  1.00 24.39  ? 74  PRO I CD  1 
ATOM   9619  N  N   . LYS E  1 76  ? -73.819  -30.669 25.020  1.00 27.96  ? 75  LYS I N   1 
ATOM   9620  C  CA  . LYS E  1 76  ? -74.525  -30.095 26.148  1.00 32.96  ? 75  LYS I CA  1 
ATOM   9621  C  C   . LYS E  1 76  ? -75.422  -31.127 26.842  1.00 32.83  ? 75  LYS I C   1 
ATOM   9622  O  O   . LYS E  1 76  ? -76.006  -30.812 27.826  1.00 33.87  ? 75  LYS I O   1 
ATOM   9623  C  CB  . LYS E  1 76  ? -75.399  -28.921 25.703  1.00 38.17  ? 75  LYS I CB  1 
ATOM   9624  C  CG  . LYS E  1 76  ? -74.654  -27.707 25.178  1.00 43.07  ? 75  LYS I CG  1 
ATOM   9625  C  CD  . LYS E  1 76  ? -75.555  -26.787 24.374  1.00 54.27  ? 75  LYS I CD  1 
ATOM   9626  C  CE  . LYS E  1 76  ? -76.624  -26.098 25.211  1.00 60.84  ? 75  LYS I CE  1 
ATOM   9627  N  NZ  . LYS E  1 76  ? -77.749  -25.587 24.383  1.00 60.64  ? 75  LYS I NZ  1 
ATOM   9628  N  N   . ASP E  1 77  ? -75.547  -32.341 26.312  1.00 31.83  ? 76  ASP I N   1 
ATOM   9629  C  CA  . ASP E  1 77  ? -76.418  -33.351 26.891  1.00 33.02  ? 76  ASP I CA  1 
ATOM   9630  C  C   . ASP E  1 77  ? -75.706  -34.100 28.023  1.00 36.12  ? 76  ASP I C   1 
ATOM   9631  O  O   . ASP E  1 77  ? -74.487  -34.304 28.025  1.00 33.74  ? 76  ASP I O   1 
ATOM   9632  C  CB  . ASP E  1 77  ? -76.926  -34.321 25.828  1.00 32.36  ? 76  ASP I CB  1 
ATOM   9633  C  CG  . ASP E  1 77  ? -77.826  -33.635 24.827  1.00 38.92  ? 76  ASP I CG  1 
ATOM   9634  O  OD1 . ASP E  1 77  ? -77.713  -33.935 23.619  1.00 43.44  ? 76  ASP I OD1 1 
ATOM   9635  O  OD2 . ASP E  1 77  ? -78.587  -32.756 25.253  1.00 44.12  ? 76  ASP I OD2 1 
ATOM   9636  N  N   . GLU E  1 78  ? -76.522  -34.469 29.011  1.00 38.26  ? 77  GLU I N   1 
ATOM   9637  C  CA  . GLU E  1 78  ? -76.213  -35.405 30.066  1.00 40.79  ? 77  GLU I CA  1 
ATOM   9638  C  C   . GLU E  1 78  ? -75.833  -36.770 29.471  1.00 35.01  ? 77  GLU I C   1 
ATOM   9639  O  O   . GLU E  1 78  ? -74.801  -37.355 29.810  1.00 35.55  ? 77  GLU I O   1 
ATOM   9640  C  CB  . GLU E  1 78  ? -77.440  -35.495 30.984  1.00 50.65  ? 77  GLU I CB  1 
ATOM   9641  C  CG  . GLU E  1 78  ? -78.732  -35.978 30.289  1.00 58.52  ? 77  GLU I CG  1 
ATOM   9642  C  CD  . GLU E  1 78  ? -79.184  -35.299 28.988  1.00 62.10  ? 77  GLU I CD  1 
ATOM   9643  O  OE1 . GLU E  1 78  ? -79.301  -34.038 28.986  1.00 66.96  ? 77  GLU I OE1 1 
ATOM   9644  O  OE2 . GLU E  1 78  ? -79.434  -36.025 27.964  1.00 50.93  ? 77  GLU I OE2 1 
ATOM   9645  N  N   . GLU E  1 79  ? -76.669  -37.274 28.564  1.00 30.66  ? 78  GLU I N   1 
ATOM   9646  C  CA  . GLU E  1 79  ? -76.444  -38.544 27.901  1.00 30.08  ? 78  GLU I CA  1 
ATOM   9647  C  C   . GLU E  1 79  ? -75.679  -38.221 26.619  1.00 26.50  ? 78  GLU I C   1 
ATOM   9648  O  O   . GLU E  1 79  ? -76.247  -37.710 25.658  1.00 26.42  ? 78  GLU I O   1 
ATOM   9649  C  CB  . GLU E  1 79  ? -77.775  -39.245 27.628  1.00 31.26  ? 78  GLU I CB  1 
ATOM   9650  C  CG  . GLU E  1 79  ? -77.653  -40.639 27.045  1.00 35.44  ? 78  GLU I CG  1 
ATOM   9651  C  CD  . GLU E  1 79  ? -77.313  -41.752 28.031  1.00 38.96  ? 78  GLU I CD  1 
ATOM   9652  O  OE1 . GLU E  1 79  ? -77.108  -42.902 27.579  1.00 38.35  ? 78  GLU I OE1 1 
ATOM   9653  O  OE2 . GLU E  1 79  ? -77.225  -41.470 29.243  1.00 44.91  ? 78  GLU I OE2 1 
ATOM   9654  N  N   . ARG E  1 80  ? -74.377  -38.462 26.656  1.00 24.25  ? 79  ARG I N   1 
ATOM   9655  C  CA  . ARG E  1 80  ? -73.512  -38.300 25.481  1.00 24.80  ? 79  ARG I CA  1 
ATOM   9656  C  C   . ARG E  1 80  ? -72.305  -39.230 25.653  1.00 25.09  ? 79  ARG I C   1 
ATOM   9657  O  O   . ARG E  1 80  ? -72.022  -39.689 26.765  1.00 23.62  ? 79  ARG I O   1 
ATOM   9658  C  CB  . ARG E  1 80  ? -73.015  -36.857 25.365  1.00 21.90  ? 79  ARG I CB  1 
ATOM   9659  C  CG  . ARG E  1 80  ? -72.268  -36.401 26.608  1.00 22.73  ? 79  ARG I CG  1 
ATOM   9660  C  CD  . ARG E  1 80  ? -71.598  -35.056 26.490  1.00 20.72  ? 79  ARG I CD  1 
ATOM   9661  N  NE  . ARG E  1 80  ? -70.291  -35.184 25.842  1.00 23.21  ? 79  ARG I NE  1 
ATOM   9662  C  CZ  . ARG E  1 80  ? -69.420  -34.194 25.756  1.00 22.21  ? 79  ARG I CZ  1 
ATOM   9663  N  NH1 . ARG E  1 80  ? -68.207  -34.415 25.269  1.00 21.15  ? 79  ARG I NH1 1 
ATOM   9664  N  NH2 . ARG E  1 80  ? -69.765  -33.000 26.212  1.00 22.00  ? 79  ARG I NH2 1 
ATOM   9665  N  N   . HIS E  1 81  ? -71.612  -39.491 24.545  1.00 21.79  ? 80  HIS I N   1 
ATOM   9666  C  CA  . HIS E  1 81  ? -70.297  -40.082 24.576  1.00 22.76  ? 80  HIS I CA  1 
ATOM   9667  C  C   . HIS E  1 81  ? -69.322  -39.004 25.062  1.00 22.26  ? 80  HIS I C   1 
ATOM   9668  O  O   . HIS E  1 81  ? -69.530  -37.824 24.820  1.00 20.59  ? 80  HIS I O   1 
ATOM   9669  C  CB  . HIS E  1 81  ? -69.908  -40.601 23.181  1.00 22.65  ? 80  HIS I CB  1 
ATOM   9670  C  CG  . HIS E  1 81  ? -70.853  -41.584 22.606  1.00 21.68  ? 80  HIS I CG  1 
ATOM   9671  N  ND1 . HIS E  1 81  ? -71.068  -41.694 21.250  1.00 21.63  ? 80  HIS I ND1 1 
ATOM   9672  C  CD2 . HIS E  1 81  ? -71.588  -42.554 23.203  1.00 22.11  ? 80  HIS I CD2 1 
ATOM   9673  C  CE1 . HIS E  1 81  ? -71.890  -42.713 21.035  1.00 23.65  ? 80  HIS I CE1 1 
ATOM   9674  N  NE2 . HIS E  1 81  ? -72.222  -43.255 22.216  1.00 20.17  ? 80  HIS I NE2 1 
ATOM   9675  N  N   . VAL E  1 82  ? -68.249  -39.412 25.730  1.00 21.22  ? 81  VAL I N   1 
ATOM   9676  C  CA  . VAL E  1 82  ? -67.180  -38.447 26.052  1.00 22.79  ? 81  VAL I CA  1 
ATOM   9677  C  C   . VAL E  1 82  ? -66.722  -37.758 24.766  1.00 21.19  ? 81  VAL I C   1 
ATOM   9678  O  O   . VAL E  1 82  ? -66.512  -36.575 24.754  1.00 20.96  ? 81  VAL I O   1 
ATOM   9679  C  CB  . VAL E  1 82  ? -65.998  -39.098 26.789  1.00 22.15  ? 81  VAL I CB  1 
ATOM   9680  C  CG1 . VAL E  1 82  ? -64.793  -38.170 26.861  1.00 23.71  ? 81  VAL I CG1 1 
ATOM   9681  C  CG2 . VAL E  1 82  ? -66.432  -39.527 28.184  1.00 23.56  ? 81  VAL I CG2 1 
ATOM   9682  N  N   . GLY E  1 83  ? -66.624  -38.521 23.684  1.00 21.20  ? 82  GLY I N   1 
ATOM   9683  C  CA  . GLY E  1 83  ? -66.133  -37.988 22.416  1.00 22.55  ? 82  GLY I CA  1 
ATOM   9684  C  C   . GLY E  1 83  ? -67.105  -37.108 21.626  1.00 21.89  ? 82  GLY I C   1 
ATOM   9685  O  O   . GLY E  1 83  ? -66.733  -36.632 20.577  1.00 21.73  ? 82  GLY I O   1 
ATOM   9686  N  N   A SER E  1 84  ? -68.325  -36.858 22.115  0.55 23.87  ? 83  SER I N   1 
ATOM   9687  C  CA  A SER E  1 84  ? -69.370  -36.248 21.274  0.55 24.02  ? 83  SER I CA  1 
ATOM   9688  C  C   A SER E  1 84  ? -69.316  -34.713 21.382  0.55 23.16  ? 83  SER I C   1 
ATOM   9689  O  O   A SER E  1 84  ? -70.051  -34.118 22.163  0.55 22.38  ? 83  SER I O   1 
ATOM   9690  C  CB  A SER E  1 84  ? -70.724  -36.876 21.614  0.55 27.15  ? 83  SER I CB  1 
ATOM   9691  O  OG  A SER E  1 84  ? -70.898  -38.159 20.954  0.55 32.27  ? 83  SER I OG  1 
ATOM   9692  N  N   B ASP E  1 84  ? -68.291  -36.842 22.185  0.45 19.84  ? 83  ASP I N   1 
ATOM   9693  C  CA  B ASP E  1 84  ? -69.334  -36.121 21.479  0.45 18.29  ? 83  ASP I CA  1 
ATOM   9694  C  C   B ASP E  1 84  ? -69.074  -34.621 21.581  0.45 19.26  ? 83  ASP I C   1 
ATOM   9695  O  O   B ASP E  1 84  ? -69.386  -33.965 22.567  0.45 18.80  ? 83  ASP I O   1 
ATOM   9696  C  CB  B ASP E  1 84  ? -70.698  -36.509 22.025  0.45 16.93  ? 83  ASP I CB  1 
ATOM   9697  C  CG  B ASP E  1 84  ? -71.049  -37.911 21.582  0.45 16.81  ? 83  ASP I CG  1 
ATOM   9698  O  OD1 B ASP E  1 84  ? -70.300  -38.459 20.670  0.45 18.46  ? 83  ASP I OD1 1 
ATOM   9699  O  OD2 B ASP E  1 84  ? -72.012  -38.438 22.116  0.45 12.20  ? 83  ASP I OD2 1 
ATOM   9700  N  N   . LEU E  1 85  ? -68.490  -34.071 20.528  1.00 21.18  ? 84  LEU I N   1 
ATOM   9701  C  CA  . LEU E  1 85  ? -68.233  -32.647 20.521  1.00 20.49  ? 84  LEU I CA  1 
ATOM   9702  C  C   . LEU E  1 85  ? -69.165  -31.896 19.566  1.00 22.16  ? 84  LEU I C   1 
ATOM   9703  O  O   . LEU E  1 85  ? -68.937  -30.711 19.322  1.00 25.50  ? 84  LEU I O   1 
ATOM   9704  C  CB  . LEU E  1 85  ? -66.768  -32.415 20.164  1.00 21.21  ? 84  LEU I CB  1 
ATOM   9705  C  CG  . LEU E  1 85  ? -65.769  -32.964 21.183  1.00 21.94  ? 84  LEU I CG  1 
ATOM   9706  C  CD1 . LEU E  1 85  ? -64.365  -32.652 20.736  1.00 23.12  ? 84  LEU I CD1 1 
ATOM   9707  C  CD2 . LEU E  1 85  ? -66.007  -32.356 22.557  1.00 24.36  ? 84  LEU I CD2 1 
ATOM   9708  N  N   . GLY E  1 86  ? -70.189  -32.566 19.023  1.00 20.33  ? 85  GLY I N   1 
ATOM   9709  C  CA  . GLY E  1 86  ? -71.248  -31.862 18.302  1.00 20.54  ? 85  GLY I CA  1 
ATOM   9710  C  C   . GLY E  1 86  ? -70.860  -31.574 16.867  1.00 19.00  ? 85  GLY I C   1 
ATOM   9711  O  O   . GLY E  1 86  ? -70.263  -32.427 16.187  1.00 18.89  ? 85  GLY I O   1 
ATOM   9712  N  N   . ASN E  1 87  ? -71.258  -30.400 16.388  1.00 18.47  ? 86  ASN I N   1 
ATOM   9713  C  CA  . ASN E  1 87  ? -70.984  -29.999 15.013  1.00 19.96  ? 86  ASN I CA  1 
ATOM   9714  C  C   . ASN E  1 87  ? -69.949  -28.857 14.979  1.00 20.17  ? 86  ASN I C   1 
ATOM   9715  O  O   . ASN E  1 87  ? -69.808  -28.083 15.956  1.00 17.96  ? 86  ASN I O   1 
ATOM   9716  C  CB  . ASN E  1 87  ? -72.269  -29.530 14.325  1.00 20.68  ? 86  ASN I CB  1 
ATOM   9717  C  CG  . ASN E  1 87  ? -73.199  -30.667 14.000  1.00 21.13  ? 86  ASN I CG  1 
ATOM   9718  O  OD1 . ASN E  1 87  ? -72.840  -31.496 13.187  1.00 19.54  ? 86  ASN I OD1 1 
ATOM   9719  N  ND2 . ASN E  1 87  ? -74.371  -30.698 14.638  1.00 19.12  ? 86  ASN I ND2 1 
ATOM   9720  N  N   . VAL E  1 88  ? -69.246  -28.775 13.850  1.00 19.77  ? 87  VAL I N   1 
ATOM   9721  C  CA  . VAL E  1 88  ? -68.477  -27.615 13.444  1.00 20.66  ? 87  VAL I CA  1 
ATOM   9722  C  C   . VAL E  1 88  ? -69.093  -27.088 12.148  1.00 22.66  ? 87  VAL I C   1 
ATOM   9723  O  O   . VAL E  1 88  ? -69.671  -27.857 11.360  1.00 22.82  ? 87  VAL I O   1 
ATOM   9724  C  CB  . VAL E  1 88  ? -66.961  -27.901 13.325  1.00 20.42  ? 87  VAL I CB  1 
ATOM   9725  C  CG1 . VAL E  1 88  ? -66.370  -28.286 14.679  1.00 20.39  ? 87  VAL I CG1 1 
ATOM   9726  C  CG2 . VAL E  1 88  ? -66.581  -28.896 12.268  1.00 20.50  ? 87  VAL I CG2 1 
ATOM   9727  N  N   . THR E  1 89  ? -69.004  -25.774 11.942  1.00 21.69  ? 88  THR I N   1 
ATOM   9728  C  CA  . THR E  1 89  ? -69.660  -25.147 10.802  1.00 21.30  ? 88  THR I CA  1 
ATOM   9729  C  C   . THR E  1 89  ? -68.606  -24.602 9.847   1.00 22.42  ? 88  THR I C   1 
ATOM   9730  O  O   . THR E  1 89  ? -67.759  -23.818 10.257  1.00 21.06  ? 88  THR I O   1 
ATOM   9731  C  CB  . THR E  1 89  ? -70.583  -24.023 11.280  1.00 22.26  ? 88  THR I CB  1 
ATOM   9732  O  OG1 . THR E  1 89  ? -71.591  -24.601 12.112  1.00 22.01  ? 88  THR I OG1 1 
ATOM   9733  C  CG2 . THR E  1 89  ? -71.205  -23.235 10.146  1.00 22.31  ? 88  THR I CG2 1 
ATOM   9734  N  N   . ALA E  1 90  ? -68.687  -25.027 8.584   1.00 23.06  ? 89  ALA I N   1 
ATOM   9735  C  CA  . ALA E  1 90  ? -67.872  -24.500 7.498   1.00 23.96  ? 89  ALA I CA  1 
ATOM   9736  C  C   . ALA E  1 90  ? -68.622  -23.347 6.818   1.00 25.41  ? 89  ALA I C   1 
ATOM   9737  O  O   . ALA E  1 90  ? -69.812  -23.459 6.536   1.00 23.45  ? 89  ALA I O   1 
ATOM   9738  C  CB  . ALA E  1 90  ? -67.570  -25.587 6.497   1.00 23.41  ? 89  ALA I CB  1 
ATOM   9739  N  N   . ASP E  1 91  ? -67.892  -22.257 6.546   1.00 25.78  ? 90  ASP I N   1 
ATOM   9740  C  CA  . ASP E  1 91  ? -68.411  -21.085 5.846   1.00 26.99  ? 90  ASP I CA  1 
ATOM   9741  C  C   . ASP E  1 91  ? -68.484  -21.368 4.337   1.00 28.23  ? 90  ASP I C   1 
ATOM   9742  O  O   . ASP E  1 91  ? -68.296  -22.505 3.857   1.00 24.29  ? 90  ASP I O   1 
ATOM   9743  C  CB  . ASP E  1 91  ? -67.583  -19.843 6.217   1.00 27.71  ? 90  ASP I CB  1 
ATOM   9744  C  CG  . ASP E  1 91  ? -66.135  -19.861 5.743   1.00 28.45  ? 90  ASP I CG  1 
ATOM   9745  O  OD1 . ASP E  1 91  ? -65.327  -19.065 6.305   1.00 30.49  ? 90  ASP I OD1 1 
ATOM   9746  O  OD2 . ASP E  1 91  ? -65.812  -20.638 4.801   1.00 26.00  ? 90  ASP I OD2 1 
ATOM   9747  N  N   . LYS E  1 92  ? -68.793  -20.318 3.566   1.00 31.07  ? 91  LYS I N   1 
ATOM   9748  C  CA  . LYS E  1 92  ? -69.037  -20.432 2.121   1.00 36.43  ? 91  LYS I CA  1 
ATOM   9749  C  C   . LYS E  1 92  ? -67.751  -20.783 1.365   1.00 32.43  ? 91  LYS I C   1 
ATOM   9750  O  O   . LYS E  1 92  ? -67.823  -21.281 0.244   1.00 35.19  ? 91  LYS I O   1 
ATOM   9751  C  CB  . LYS E  1 92  ? -69.656  -19.141 1.566   1.00 41.71  ? 91  LYS I CB  1 
ATOM   9752  C  CG  . LYS E  1 92  ? -68.694  -17.978 1.357   1.00 50.56  ? 91  LYS I CG  1 
ATOM   9753  C  CD  . LYS E  1 92  ? -68.680  -16.935 2.467   1.00 61.10  ? 91  LYS I CD  1 
ATOM   9754  C  CE  . LYS E  1 92  ? -67.319  -16.742 3.115   1.00 68.38  ? 91  LYS I CE  1 
ATOM   9755  N  NZ  . LYS E  1 92  ? -67.414  -16.060 4.432   1.00 69.82  ? 91  LYS I NZ  1 
ATOM   9756  N  N   . ASP E  1 93  ? -66.584  -20.532 1.972   1.00 30.19  ? 92  ASP I N   1 
ATOM   9757  C  CA  . ASP E  1 93  ? -65.310  -20.916 1.371   1.00 30.34  ? 92  ASP I CA  1 
ATOM   9758  C  C   . ASP E  1 93  ? -64.866  -22.322 1.795   1.00 29.73  ? 92  ASP I C   1 
ATOM   9759  O  O   . ASP E  1 93  ? -63.747  -22.741 1.474   1.00 29.56  ? 92  ASP I O   1 
ATOM   9760  C  CB  . ASP E  1 93  ? -64.223  -19.914 1.740   1.00 32.97  ? 92  ASP I CB  1 
ATOM   9761  C  CG  . ASP E  1 93  ? -64.523  -18.516 1.209   1.00 39.55  ? 92  ASP I CG  1 
ATOM   9762  O  OD1 . ASP E  1 93  ? -64.997  -18.408 0.062   1.00 39.79  ? 92  ASP I OD1 1 
ATOM   9763  O  OD2 . ASP E  1 93  ? -64.295  -17.563 1.957   1.00 45.77  ? 92  ASP I OD2 1 
ATOM   9764  N  N   . GLY E  1 94  ? -65.682  -23.001 2.599   1.00 28.50  ? 93  GLY I N   1 
ATOM   9765  C  CA  . GLY E  1 94  ? -65.414  -24.359 3.011   1.00 26.48  ? 93  GLY I CA  1 
ATOM   9766  C  C   . GLY E  1 94  ? -64.507  -24.443 4.233   1.00 26.36  ? 93  GLY I C   1 
ATOM   9767  O  O   . GLY E  1 94  ? -63.950  -25.503 4.497   1.00 24.16  ? 93  GLY I O   1 
ATOM   9768  N  N   . VAL E  1 95  ? -64.438  -23.356 5.018   1.00 25.65  ? 94  VAL I N   1 
ATOM   9769  C  CA  . VAL E  1 95  ? -63.528  -23.251 6.147   1.00 24.68  ? 94  VAL I CA  1 
ATOM   9770  C  C   . VAL E  1 95  ? -64.327  -23.268 7.458   1.00 24.96  ? 94  VAL I C   1 
ATOM   9771  O  O   . VAL E  1 95  ? -65.225  -22.450 7.648   1.00 24.52  ? 94  VAL I O   1 
ATOM   9772  C  CB  . VAL E  1 95  ? -62.686  -21.973 6.069   1.00 26.58  ? 94  VAL I CB  1 
ATOM   9773  C  CG1 . VAL E  1 95  ? -61.877  -21.774 7.343   1.00 30.16  ? 94  VAL I CG1 1 
ATOM   9774  C  CG2 . VAL E  1 95  ? -61.781  -21.972 4.854   1.00 29.26  ? 94  VAL I CG2 1 
ATOM   9775  N  N   . ALA E  1 96  ? -63.985  -24.200 8.355   1.00 22.90  ? 95  ALA I N   1 
ATOM   9776  C  CA  . ALA E  1 96  ? -64.531  -24.216 9.695   1.00 22.80  ? 95  ALA I CA  1 
ATOM   9777  C  C   . ALA E  1 96  ? -63.499  -23.617 10.648  1.00 23.53  ? 95  ALA I C   1 
ATOM   9778  O  O   . ALA E  1 96  ? -62.455  -24.212 10.892  1.00 23.60  ? 95  ALA I O   1 
ATOM   9779  C  CB  . ALA E  1 96  ? -64.913  -25.620 10.100  1.00 24.35  ? 95  ALA I CB  1 
ATOM   9780  N  N   . ASP E  1 97  ? -63.799  -22.432 11.176  1.00 24.06  ? 96  ASP I N   1 
ATOM   9781  C  CA  . ASP E  1 97  ? -62.999  -21.816 12.230  1.00 25.46  ? 96  ASP I CA  1 
ATOM   9782  C  C   . ASP E  1 97  ? -63.502  -22.327 13.580  1.00 22.28  ? 96  ASP I C   1 
ATOM   9783  O  O   . ASP E  1 97  ? -64.323  -21.719 14.223  1.00 22.85  ? 96  ASP I O   1 
ATOM   9784  C  CB  . ASP E  1 97  ? -62.973  -20.286 12.089  1.00 27.58  ? 96  ASP I CB  1 
ATOM   9785  C  CG  . ASP E  1 97  ? -62.123  -19.852 10.891  1.00 32.73  ? 96  ASP I CG  1 
ATOM   9786  O  OD1 . ASP E  1 97  ? -62.608  -18.996 10.128  1.00 35.91  ? 96  ASP I OD1 1 
ATOM   9787  O  OD2 . ASP E  1 97  ? -61.012  -20.467 10.655  1.00 35.02  ? 96  ASP I OD2 1 
ATOM   9788  N  N   . VAL E  1 98  ? -62.947  -23.457 14.019  1.00 21.45  ? 97  VAL I N   1 
ATOM   9789  C  CA  . VAL E  1 98  ? -63.469  -24.163 15.167  1.00 22.06  ? 97  VAL I CA  1 
ATOM   9790  C  C   . VAL E  1 98  ? -63.201  -23.376 16.455  1.00 21.61  ? 97  VAL I C   1 
ATOM   9791  O  O   . VAL E  1 98  ? -62.089  -22.900 16.690  1.00 21.53  ? 97  VAL I O   1 
ATOM   9792  C  CB  . VAL E  1 98  ? -62.891  -25.589 15.251  1.00 20.98  ? 97  VAL I CB  1 
ATOM   9793  C  CG1 . VAL E  1 98  ? -63.382  -26.314 16.484  1.00 21.85  ? 97  VAL I CG1 1 
ATOM   9794  C  CG2 . VAL E  1 98  ? -63.231  -26.399 14.020  1.00 21.43  ? 97  VAL I CG2 1 
ATOM   9795  N  N   . SER E  1 99  ? -64.223  -23.289 17.304  1.00 22.00  ? 98  SER I N   1 
ATOM   9796  C  CA  . SER E  1 99  ? -64.078  -22.736 18.625  1.00 25.63  ? 98  SER I CA  1 
ATOM   9797  C  C   . SER E  1 99  ? -65.089  -23.378 19.579  1.00 25.01  ? 98  SER I C   1 
ATOM   9798  O  O   . SER E  1 99  ? -66.245  -23.019 19.609  1.00 26.76  ? 98  SER I O   1 
ATOM   9799  C  CB  . SER E  1 99  ? -64.212  -21.233 18.595  1.00 29.68  ? 98  SER I CB  1 
ATOM   9800  O  OG  . SER E  1 99  ? -64.031  -20.718 19.895  1.00 31.04  ? 98  SER I OG  1 
ATOM   9801  N  N   . ILE E  1 100 ? -64.611  -24.322 20.383  1.00 22.99  ? 99  ILE I N   1 
ATOM   9802  C  CA  . ILE E  1 100 ? -65.444  -25.115 21.270  1.00 26.63  ? 99  ILE I CA  1 
ATOM   9803  C  C   . ILE E  1 100 ? -64.803  -25.104 22.660  1.00 26.31  ? 99  ILE I C   1 
ATOM   9804  O  O   . ILE E  1 100 ? -63.585  -25.042 22.775  1.00 23.87  ? 99  ILE I O   1 
ATOM   9805  C  CB  . ILE E  1 100 ? -65.566  -26.541 20.706  1.00 28.00  ? 99  ILE I CB  1 
ATOM   9806  C  CG1 . ILE E  1 100 ? -66.530  -26.598 19.521  1.00 28.52  ? 99  ILE I CG1 1 
ATOM   9807  C  CG2 . ILE E  1 100 ? -65.947  -27.540 21.784  1.00 31.69  ? 99  ILE I CG2 1 
ATOM   9808  C  CD1 . ILE E  1 100 ? -66.389  -27.880 18.701  1.00 29.24  ? 99  ILE I CD1 1 
ATOM   9809  N  N   . GLU E  1 101 ? -65.642  -25.172 23.698  1.00 25.65  ? 100 GLU I N   1 
ATOM   9810  C  CA  . GLU E  1 101 ? -65.186  -25.401 25.045  1.00 28.75  ? 100 GLU I CA  1 
ATOM   9811  C  C   . GLU E  1 101 ? -65.986  -26.571 25.610  1.00 26.83  ? 100 GLU I C   1 
ATOM   9812  O  O   . GLU E  1 101 ? -67.187  -26.580 25.502  1.00 26.04  ? 100 GLU I O   1 
ATOM   9813  C  CB  . GLU E  1 101 ? -65.347  -24.148 25.902  1.00 34.35  ? 100 GLU I CB  1 
ATOM   9814  C  CG  . GLU E  1 101 ? -64.949  -24.392 27.340  1.00 40.74  ? 100 GLU I CG  1 
ATOM   9815  C  CD  . GLU E  1 101 ? -65.191  -23.223 28.282  1.00 48.94  ? 100 GLU I CD  1 
ATOM   9816  O  OE1 . GLU E  1 101 ? -64.649  -22.133 28.012  1.00 52.93  ? 100 GLU I OE1 1 
ATOM   9817  O  OE2 . GLU E  1 101 ? -65.913  -23.422 29.283  1.00 50.87  ? 100 GLU I OE2 1 
ATOM   9818  N  N   . ASP E  1 102 ? -65.301  -27.586 26.149  1.00 23.64  ? 101 ASP I N   1 
ATOM   9819  C  CA  . ASP E  1 102 ? -66.001  -28.774 26.621  1.00 25.63  ? 101 ASP I CA  1 
ATOM   9820  C  C   . ASP E  1 102 ? -65.388  -29.249 27.940  1.00 26.05  ? 101 ASP I C   1 
ATOM   9821  O  O   . ASP E  1 102 ? -64.154  -29.308 28.072  1.00 23.66  ? 101 ASP I O   1 
ATOM   9822  C  CB  . ASP E  1 102 ? -65.911  -29.909 25.608  1.00 25.66  ? 101 ASP I CB  1 
ATOM   9823  C  CG  . ASP E  1 102 ? -66.854  -31.057 25.927  1.00 28.30  ? 101 ASP I CG  1 
ATOM   9824  O  OD1 . ASP E  1 102 ? -66.365  -32.125 26.383  1.00 23.90  ? 101 ASP I OD1 1 
ATOM   9825  O  OD2 . ASP E  1 102 ? -68.080  -30.871 25.747  1.00 30.45  ? 101 ASP I OD2 1 
ATOM   9826  N  N   . SER E  1 103 ? -66.238  -29.672 28.869  1.00 25.11  ? 102 SER I N   1 
ATOM   9827  C  CA  . SER E  1 103 ? -65.751  -30.060 30.173  1.00 30.30  ? 102 SER I CA  1 
ATOM   9828  C  C   . SER E  1 103 ? -65.915  -31.563 30.409  1.00 28.14  ? 102 SER I C   1 
ATOM   9829  O  O   . SER E  1 103 ? -65.694  -32.025 31.514  1.00 29.78  ? 102 SER I O   1 
ATOM   9830  C  CB  . SER E  1 103 ? -66.445  -29.251 31.238  1.00 35.66  ? 102 SER I CB  1 
ATOM   9831  O  OG  . SER E  1 103 ? -67.841  -29.313 31.015  1.00 43.66  ? 102 SER I OG  1 
ATOM   9832  N  N   . VAL E  1 104 ? -66.252  -32.329 29.369  1.00 24.02  ? 103 VAL I N   1 
ATOM   9833  C  CA  . VAL E  1 104 ? -66.369  -33.774 29.521  1.00 24.72  ? 103 VAL I CA  1 
ATOM   9834  C  C   . VAL E  1 104 ? -65.089  -34.446 28.990  1.00 23.22  ? 103 VAL I C   1 
ATOM   9835  O  O   . VAL E  1 104 ? -64.574  -35.354 29.608  1.00 22.26  ? 103 VAL I O   1 
ATOM   9836  C  CB  . VAL E  1 104 ? -67.663  -34.313 28.872  1.00 23.80  ? 103 VAL I CB  1 
ATOM   9837  C  CG1 . VAL E  1 104 ? -67.683  -35.832 28.862  1.00 24.79  ? 103 VAL I CG1 1 
ATOM   9838  C  CG2 . VAL E  1 104 ? -68.901  -33.761 29.581  1.00 26.10  ? 103 VAL I CG2 1 
ATOM   9839  N  N   . ILE E  1 105 ? -64.601  -34.024 27.824  1.00 22.90  ? 104 ILE I N   1 
ATOM   9840  C  CA  . ILE E  1 105 ? -63.282  -34.470 27.377  1.00 22.27  ? 104 ILE I CA  1 
ATOM   9841  C  C   . ILE E  1 105 ? -62.244  -33.918 28.359  1.00 22.59  ? 104 ILE I C   1 
ATOM   9842  O  O   . ILE E  1 105 ? -62.462  -32.904 29.042  1.00 21.08  ? 104 ILE I O   1 
ATOM   9843  C  CB  . ILE E  1 105 ? -62.946  -34.027 25.946  1.00 20.98  ? 104 ILE I CB  1 
ATOM   9844  C  CG1 . ILE E  1 105 ? -62.911  -32.501 25.833  1.00 22.09  ? 104 ILE I CG1 1 
ATOM   9845  C  CG2 . ILE E  1 105 ? -63.885  -34.664 24.942  1.00 22.50  ? 104 ILE I CG2 1 
ATOM   9846  C  CD1 . ILE E  1 105 ? -62.246  -32.024 24.567  1.00 22.18  ? 104 ILE I CD1 1 
ATOM   9847  N  N   . SER E  1 106 ? -61.087  -34.570 28.378  1.00 19.86  ? 105 SER I N   1 
ATOM   9848  C  CA  . SER E  1 106 ? -59.965  -34.101 29.162  1.00 20.48  ? 105 SER I CA  1 
ATOM   9849  C  C   . SER E  1 106 ? -58.670  -34.413 28.405  1.00 21.98  ? 105 SER I C   1 
ATOM   9850  O  O   . SER E  1 106 ? -58.666  -35.199 27.449  1.00 22.38  ? 105 SER I O   1 
ATOM   9851  C  CB  . SER E  1 106 ? -59.974  -34.750 30.560  1.00 21.60  ? 105 SER I CB  1 
ATOM   9852  O  OG  . SER E  1 106 ? -58.970  -34.175 31.386  1.00 21.05  ? 105 SER I OG  1 
ATOM   9853  N  N   . LEU E  1 107 ? -57.573  -33.771 28.816  1.00 23.26  ? 106 LEU I N   1 
ATOM   9854  C  CA  . LEU E  1 107 ? -56.266  -34.110 28.312  1.00 22.31  ? 106 LEU I CA  1 
ATOM   9855  C  C   . LEU E  1 107 ? -55.481  -34.941 29.335  1.00 25.34  ? 106 LEU I C   1 
ATOM   9856  O  O   . LEU E  1 107 ? -54.290  -35.137 29.176  1.00 25.91  ? 106 LEU I O   1 
ATOM   9857  C  CB  . LEU E  1 107 ? -55.523  -32.831 27.969  1.00 21.51  ? 106 LEU I CB  1 
ATOM   9858  C  CG  . LEU E  1 107 ? -56.173  -31.955 26.905  1.00 22.55  ? 106 LEU I CG  1 
ATOM   9859  C  CD1 . LEU E  1 107 ? -55.250  -30.811 26.516  1.00 23.29  ? 106 LEU I CD1 1 
ATOM   9860  C  CD2 . LEU E  1 107 ? -56.562  -32.749 25.668  1.00 20.86  ? 106 LEU I CD2 1 
ATOM   9861  N  N   . SER E  1 108 ? -56.155  -35.438 30.370  1.00 25.56  ? 107 SER I N   1 
ATOM   9862  C  CA  . SER E  1 108 ? -55.546  -36.421 31.267  1.00 29.17  ? 107 SER I CA  1 
ATOM   9863  C  C   . SER E  1 108 ? -56.638  -37.226 31.970  1.00 26.82  ? 107 SER I C   1 
ATOM   9864  O  O   . SER E  1 108 ? -57.819  -36.875 31.911  1.00 26.83  ? 107 SER I O   1 
ATOM   9865  C  CB  . SER E  1 108 ? -54.615  -35.755 32.248  1.00 31.94  ? 107 SER I CB  1 
ATOM   9866  O  OG  . SER E  1 108 ? -55.351  -34.970 33.150  1.00 32.53  ? 107 SER I OG  1 
ATOM   9867  N  N   . GLY E  1 109 ? -56.229  -38.351 32.561  1.00 27.01  ? 108 GLY I N   1 
ATOM   9868  C  CA  . GLY E  1 109 ? -57.080  -39.236 33.324  1.00 26.47  ? 108 GLY I CA  1 
ATOM   9869  C  C   . GLY E  1 109 ? -57.991  -40.058 32.437  1.00 26.17  ? 108 GLY I C   1 
ATOM   9870  O  O   . GLY E  1 109 ? -57.725  -40.276 31.246  1.00 28.39  ? 108 GLY I O   1 
ATOM   9871  N  N   . ASP E  1 110 ? -59.095  -40.490 33.031  1.00 26.94  ? 109 ASP I N   1 
ATOM   9872  C  CA  . ASP E  1 110 ? -60.041  -41.436 32.443  1.00 30.92  ? 109 ASP I CA  1 
ATOM   9873  C  C   . ASP E  1 110 ? -60.601  -40.919 31.111  1.00 28.07  ? 109 ASP I C   1 
ATOM   9874  O  O   . ASP E  1 110 ? -60.852  -41.697 30.224  1.00 31.16  ? 109 ASP I O   1 
ATOM   9875  C  CB  . ASP E  1 110 ? -61.252  -41.648 33.359  1.00 33.44  ? 109 ASP I CB  1 
ATOM   9876  C  CG  . ASP E  1 110 ? -60.991  -42.625 34.494  1.00 40.81  ? 109 ASP I CG  1 
ATOM   9877  O  OD1 . ASP E  1 110 ? -61.813  -42.648 35.433  1.00 39.14  ? 109 ASP I OD1 1 
ATOM   9878  O  OD2 . ASP E  1 110 ? -59.975  -43.365 34.412  1.00 46.89  ? 109 ASP I OD2 1 
ATOM   9879  N  N   . HIS E  1 111 ? -60.847  -39.612 31.030  1.00 24.51  ? 110 HIS I N   1 
ATOM   9880  C  CA  . HIS E  1 111 ? -61.495  -39.009 29.865  1.00 25.63  ? 110 HIS I CA  1 
ATOM   9881  C  C   . HIS E  1 111 ? -60.474  -38.436 28.885  1.00 23.92  ? 110 HIS I C   1 
ATOM   9882  O  O   . HIS E  1 111 ? -60.843  -37.659 27.985  1.00 23.00  ? 110 HIS I O   1 
ATOM   9883  C  CB  . HIS E  1 111 ? -62.477  -37.951 30.346  1.00 26.29  ? 110 HIS I CB  1 
ATOM   9884  C  CG  . HIS E  1 111 ? -63.693  -38.557 30.959  1.00 30.21  ? 110 HIS I CG  1 
ATOM   9885  N  ND1 . HIS E  1 111 ? -64.831  -37.814 31.261  1.00 31.93  ? 110 HIS I ND1 1 
ATOM   9886  C  CD2 . HIS E  1 111 ? -63.967  -39.834 31.296  1.00 31.61  ? 110 HIS I CD2 1 
ATOM   9887  C  CE1 . HIS E  1 111 ? -65.736  -38.621 31.782  1.00 32.70  ? 110 HIS I CE1 1 
ATOM   9888  N  NE2 . HIS E  1 111 ? -65.228  -39.863 31.815  1.00 33.12  ? 110 HIS I NE2 1 
ATOM   9889  N  N   . SER E  1 112 ? -59.193  -38.778 29.079  1.00 22.21  ? 111 SER I N   1 
ATOM   9890  C  CA  . SER E  1 112 ? -58.133  -38.281 28.242  1.00 22.00  ? 111 SER I CA  1 
ATOM   9891  C  C   . SER E  1 112 ? -58.382  -38.696 26.785  1.00 21.31  ? 111 SER I C   1 
ATOM   9892  O  O   . SER E  1 112 ? -58.601  -39.868 26.478  1.00 20.80  ? 111 SER I O   1 
ATOM   9893  C  CB  . SER E  1 112 ? -56.770  -38.764 28.678  1.00 24.18  ? 111 SER I CB  1 
ATOM   9894  O  OG  . SER E  1 112 ? -55.780  -38.207 27.822  1.00 23.47  ? 111 SER I OG  1 
ATOM   9895  N  N   . ILE E  1 113 ? -58.260  -37.720 25.888  1.00 20.29  ? 112 ILE I N   1 
ATOM   9896  C  CA  . ILE E  1 113 ? -58.355  -37.936 24.458  1.00 21.26  ? 112 ILE I CA  1 
ATOM   9897  C  C   . ILE E  1 113 ? -56.955  -38.003 23.832  1.00 21.02  ? 112 ILE I C   1 
ATOM   9898  O  O   . ILE E  1 113 ? -56.840  -38.145 22.600  1.00 20.13  ? 112 ILE I O   1 
ATOM   9899  C  CB  . ILE E  1 113 ? -59.225  -36.836 23.814  1.00 21.51  ? 112 ILE I CB  1 
ATOM   9900  C  CG1 . ILE E  1 113 ? -58.564  -35.456 23.902  1.00 22.31  ? 112 ILE I CG1 1 
ATOM   9901  C  CG2 . ILE E  1 113 ? -60.604  -36.859 24.446  1.00 23.56  ? 112 ILE I CG2 1 
ATOM   9902  C  CD1 . ILE E  1 113 ? -59.411  -34.346 23.314  1.00 23.34  ? 112 ILE I CD1 1 
ATOM   9903  N  N   . ILE E  1 114 ? -55.896  -37.900 24.655  1.00 21.97  ? 113 ILE I N   1 
ATOM   9904  C  CA  . ILE E  1 114 ? -54.511  -38.009 24.146  1.00 22.97  ? 113 ILE I CA  1 
ATOM   9905  C  C   . ILE E  1 114 ? -54.326  -39.405 23.547  1.00 22.01  ? 113 ILE I C   1 
ATOM   9906  O  O   . ILE E  1 114 ? -54.668  -40.388 24.175  1.00 23.04  ? 113 ILE I O   1 
ATOM   9907  C  CB  . ILE E  1 114 ? -53.455  -37.729 25.228  1.00 23.52  ? 113 ILE I CB  1 
ATOM   9908  C  CG1 . ILE E  1 114 ? -53.592  -36.325 25.830  1.00 24.92  ? 113 ILE I CG1 1 
ATOM   9909  C  CG2 . ILE E  1 114 ? -52.058  -37.966 24.674  1.00 25.77  ? 113 ILE I CG2 1 
ATOM   9910  C  CD1 . ILE E  1 114 ? -53.431  -35.230 24.863  1.00 24.27  ? 113 ILE I CD1 1 
ATOM   9911  N  N   . GLY E  1 115 ? -53.861  -39.456 22.297  1.00 19.82  ? 114 GLY I N   1 
ATOM   9912  C  CA  . GLY E  1 115 ? -53.603  -40.722 21.597  1.00 21.25  ? 114 GLY I CA  1 
ATOM   9913  C  C   . GLY E  1 115 ? -54.860  -41.337 21.000  1.00 21.72  ? 114 GLY I C   1 
ATOM   9914  O  O   . GLY E  1 115 ? -54.856  -42.475 20.544  1.00 22.33  ? 114 GLY I O   1 
ATOM   9915  N  N   . ARG E  1 116 ? -55.957  -40.581 20.986  1.00 21.06  ? 115 ARG I N   1 
ATOM   9916  C  CA  . ARG E  1 116 ? -57.186  -41.039 20.329  1.00 21.72  ? 115 ARG I CA  1 
ATOM   9917  C  C   . ARG E  1 116 ? -57.319  -40.277 19.006  1.00 21.39  ? 115 ARG I C   1 
ATOM   9918  O  O   . ARG E  1 116 ? -56.418  -39.533 18.662  1.00 21.05  ? 115 ARG I O   1 
ATOM   9919  C  CB  . ARG E  1 116 ? -58.357  -40.873 21.294  1.00 21.50  ? 115 ARG I CB  1 
ATOM   9920  C  CG  . ARG E  1 116 ? -58.167  -41.673 22.583  1.00 21.51  ? 115 ARG I CG  1 
ATOM   9921  C  CD  . ARG E  1 116 ? -59.431  -41.799 23.407  1.00 22.43  ? 115 ARG I CD  1 
ATOM   9922  N  NE  . ARG E  1 116 ? -59.087  -42.348 24.714  1.00 24.75  ? 115 ARG I NE  1 
ATOM   9923  C  CZ  . ARG E  1 116 ? -59.041  -43.638 25.039  1.00 24.82  ? 115 ARG I CZ  1 
ATOM   9924  N  NH1 . ARG E  1 116 ? -58.759  -43.972 26.296  1.00 23.27  ? 115 ARG I NH1 1 
ATOM   9925  N  NH2 . ARG E  1 116 ? -59.317  -44.572 24.142  1.00 22.82  ? 115 ARG I NH2 1 
ATOM   9926  N  N   . THR E  1 117 ? -58.416  -40.465 18.266  1.00 20.73  ? 116 THR I N   1 
ATOM   9927  C  CA  . THR E  1 117 ? -58.523  -39.874 16.948  1.00 20.52  ? 116 THR I CA  1 
ATOM   9928  C  C   . THR E  1 117 ? -59.619  -38.809 16.949  1.00 20.91  ? 116 THR I C   1 
ATOM   9929  O  O   . THR E  1 117 ? -60.719  -39.087 17.408  1.00 23.24  ? 116 THR I O   1 
ATOM   9930  C  CB  . THR E  1 117 ? -58.796  -40.951 15.893  1.00 20.82  ? 116 THR I CB  1 
ATOM   9931  O  OG1 . THR E  1 117 ? -57.638  -41.789 15.787  1.00 21.83  ? 116 THR I OG1 1 
ATOM   9932  C  CG2 . THR E  1 117 ? -59.115  -40.352 14.538  1.00 20.29  ? 116 THR I CG2 1 
ATOM   9933  N  N   . LEU E  1 118 ? -59.327  -37.627 16.401  1.00 20.52  ? 117 LEU I N   1 
ATOM   9934  C  CA  . LEU E  1 118 ? -60.376  -36.634 16.103  1.00 19.77  ? 117 LEU I CA  1 
ATOM   9935  C  C   . LEU E  1 118 ? -60.818  -36.846 14.648  1.00 20.21  ? 117 LEU I C   1 
ATOM   9936  O  O   . LEU E  1 118 ? -59.978  -37.047 13.784  1.00 19.85  ? 117 LEU I O   1 
ATOM   9937  C  CB  . LEU E  1 118 ? -59.784  -35.245 16.317  1.00 20.54  ? 117 LEU I CB  1 
ATOM   9938  C  CG  . LEU E  1 118 ? -60.720  -34.068 16.087  1.00 21.04  ? 117 LEU I CG  1 
ATOM   9939  C  CD1 . LEU E  1 118 ? -61.784  -34.007 17.174  1.00 20.73  ? 117 LEU I CD1 1 
ATOM   9940  C  CD2 . LEU E  1 118 ? -59.912  -32.778 16.039  1.00 21.75  ? 117 LEU I CD2 1 
ATOM   9941  N  N   . VAL E  1 119 ? -62.131  -36.838 14.413  1.00 19.32  ? 118 VAL I N   1 
ATOM   9942  C  CA  . VAL E  1 119 ? -62.733  -37.103 13.116  1.00 19.68  ? 118 VAL I CA  1 
ATOM   9943  C  C   . VAL E  1 119 ? -63.682  -35.958 12.784  1.00 18.89  ? 118 VAL I C   1 
ATOM   9944  O  O   . VAL E  1 119 ? -64.504  -35.544 13.624  1.00 18.25  ? 118 VAL I O   1 
ATOM   9945  C  CB  . VAL E  1 119 ? -63.511  -38.428 13.122  1.00 20.31  ? 118 VAL I CB  1 
ATOM   9946  C  CG1 . VAL E  1 119 ? -64.242  -38.651 11.809  1.00 21.50  ? 118 VAL I CG1 1 
ATOM   9947  C  CG2 . VAL E  1 119 ? -62.603  -39.581 13.469  1.00 20.95  ? 118 VAL I CG2 1 
ATOM   9948  N  N   . VAL E  1 120 ? -63.636  -35.507 11.534  1.00 19.54  ? 119 VAL I N   1 
ATOM   9949  C  CA  . VAL E  1 120 ? -64.673  -34.613 11.036  1.00 20.28  ? 119 VAL I CA  1 
ATOM   9950  C  C   . VAL E  1 120 ? -65.446  -35.364 9.948   1.00 20.68  ? 119 VAL I C   1 
ATOM   9951  O  O   . VAL E  1 120 ? -64.836  -36.029 9.107   1.00 20.17  ? 119 VAL I O   1 
ATOM   9952  C  CB  . VAL E  1 120 ? -64.109  -33.257 10.556  1.00 21.75  ? 119 VAL I CB  1 
ATOM   9953  C  CG1 . VAL E  1 120 ? -63.093  -33.393 9.440   1.00 22.44  ? 119 VAL I CG1 1 
ATOM   9954  C  CG2 . VAL E  1 120 ? -65.210  -32.293 10.147  1.00 22.15  ? 119 VAL I CG2 1 
ATOM   9955  N  N   . HIS E  1 121 ? -66.778  -35.239 9.996   1.00 19.13  ? 120 HIS I N   1 
ATOM   9956  C  CA  . HIS E  1 121 ? -67.686  -36.093 9.247   1.00 20.86  ? 120 HIS I CA  1 
ATOM   9957  C  C   . HIS E  1 121 ? -68.304  -35.346 8.059   1.00 22.36  ? 120 HIS I C   1 
ATOM   9958  O  O   . HIS E  1 121 ? -68.295  -34.125 7.985   1.00 22.21  ? 120 HIS I O   1 
ATOM   9959  C  CB  . HIS E  1 121 ? -68.787  -36.610 10.171  1.00 19.50  ? 120 HIS I CB  1 
ATOM   9960  C  CG  . HIS E  1 121 ? -68.347  -37.716 11.061  1.00 20.44  ? 120 HIS I CG  1 
ATOM   9961  N  ND1 . HIS E  1 121 ? -68.485  -39.026 10.696  1.00 19.98  ? 120 HIS I ND1 1 
ATOM   9962  C  CD2 . HIS E  1 121 ? -67.818  -37.723 12.308  1.00 21.96  ? 120 HIS I CD2 1 
ATOM   9963  C  CE1 . HIS E  1 121 ? -68.079  -39.813 11.684  1.00 20.61  ? 120 HIS I CE1 1 
ATOM   9964  N  NE2 . HIS E  1 121 ? -67.670  -39.045 12.697  1.00 22.32  ? 120 HIS I NE2 1 
ATOM   9965  N  N   . GLU E  1 122 ? -68.901  -36.150 7.179   1.00 23.72  ? 121 GLU I N   1 
ATOM   9966  C  CA  . GLU E  1 122 ? -69.535  -35.781 5.924   1.00 24.79  ? 121 GLU I CA  1 
ATOM   9967  C  C   . GLU E  1 122 ? -70.757  -34.890 6.173   1.00 23.48  ? 121 GLU I C   1 
ATOM   9968  O  O   . GLU E  1 122 ? -70.965  -33.894 5.489   1.00 21.80  ? 121 GLU I O   1 
ATOM   9969  C  CB  . GLU E  1 122 ? -69.879  -37.114 5.230   1.00 28.01  ? 121 GLU I CB  1 
ATOM   9970  C  CG  . GLU E  1 122 ? -70.622  -37.012 3.909   1.00 34.75  ? 121 GLU I CG  1 
ATOM   9971  C  CD  . GLU E  1 122 ? -71.368  -38.288 3.482   1.00 37.08  ? 121 GLU I CD  1 
ATOM   9972  O  OE1 . GLU E  1 122 ? -71.950  -38.266 2.385   1.00 45.22  ? 121 GLU I OE1 1 
ATOM   9973  O  OE2 . GLU E  1 122 ? -71.419  -39.290 4.261   1.00 36.02  ? 121 GLU I OE2 1 
ATOM   9974  N  N   . LYS E  1 123 ? -71.569  -35.253 7.164   1.00 25.08  ? 122 LYS I N   1 
ATOM   9975  C  CA  . LYS E  1 123 ? -72.882  -34.650 7.402   1.00 26.10  ? 122 LYS I CA  1 
ATOM   9976  C  C   . LYS E  1 123 ? -72.951  -34.061 8.818   1.00 23.08  ? 122 LYS I C   1 
ATOM   9977  O  O   . LYS E  1 123 ? -72.095  -34.315 9.656   1.00 20.22  ? 122 LYS I O   1 
ATOM   9978  C  CB  . LYS E  1 123 ? -73.971  -35.733 7.279   1.00 29.50  ? 122 LYS I CB  1 
ATOM   9979  C  CG  . LYS E  1 123 ? -74.072  -36.395 5.917   1.00 35.55  ? 122 LYS I CG  1 
ATOM   9980  C  CD  . LYS E  1 123 ? -75.275  -37.280 5.759   1.00 40.20  ? 122 LYS I CD  1 
ATOM   9981  C  CE  . LYS E  1 123 ? -75.102  -38.616 6.438   1.00 47.26  ? 122 LYS I CE  1 
ATOM   9982  N  NZ  . LYS E  1 123 ? -76.404  -39.241 6.785   1.00 55.27  ? 122 LYS I NZ  1 
ATOM   9983  N  N   . ALA E  1 124 ? -74.019  -33.308 9.064   1.00 21.92  ? 123 ALA I N   1 
ATOM   9984  C  CA  . ALA E  1 124 ? -74.383  -32.808 10.393  1.00 22.38  ? 123 ALA I CA  1 
ATOM   9985  C  C   . ALA E  1 124 ? -74.645  -33.972 11.357  1.00 23.30  ? 123 ALA I C   1 
ATOM   9986  O  O   . ALA E  1 124 ? -75.211  -34.981 10.995  1.00 22.18  ? 123 ALA I O   1 
ATOM   9987  C  CB  . ALA E  1 124 ? -75.603  -31.920 10.274  1.00 24.04  ? 123 ALA I CB  1 
ATOM   9988  N  N   . ASP E  1 125 ? -74.157  -33.819 12.585  1.00 20.50  ? 124 ASP I N   1 
ATOM   9989  C  CA  . ASP E  1 125 ? -74.486  -34.632 13.702  1.00 21.19  ? 124 ASP I CA  1 
ATOM   9990  C  C   . ASP E  1 125 ? -75.878  -34.201 14.184  1.00 21.96  ? 124 ASP I C   1 
ATOM   9991  O  O   . ASP E  1 125 ? -76.082  -33.012 14.485  1.00 19.96  ? 124 ASP I O   1 
ATOM   9992  C  CB  . ASP E  1 125 ? -73.403  -34.450 14.774  1.00 21.24  ? 124 ASP I CB  1 
ATOM   9993  C  CG  . ASP E  1 125 ? -73.493  -35.337 16.009  1.00 21.95  ? 124 ASP I CG  1 
ATOM   9994  O  OD1 . ASP E  1 125 ? -74.565  -35.859 16.278  1.00 21.55  ? 124 ASP I OD1 1 
ATOM   9995  O  OD2 . ASP E  1 125 ? -72.470  -35.466 16.714  1.00 24.92  ? 124 ASP I OD2 1 
ATOM   9996  N  N   . ASP E  1 126 ? -76.817  -35.165 14.287  1.00 20.37  ? 125 ASP I N   1 
ATOM   9997  C  CA  . ASP E  1 126 ? -78.202  -34.871 14.756  1.00 21.28  ? 125 ASP I CA  1 
ATOM   9998  C  C   . ASP E  1 126 ? -78.265  -34.803 16.287  1.00 20.49  ? 125 ASP I C   1 
ATOM   9999  O  O   . ASP E  1 126 ? -79.335  -34.647 16.867  1.00 19.06  ? 125 ASP I O   1 
ATOM   10000 C  CB  . ASP E  1 126 ? -79.200  -35.888 14.189  1.00 23.62  ? 125 ASP I CB  1 
ATOM   10001 C  CG  . ASP E  1 126 ? -79.071  -37.333 14.670  1.00 23.64  ? 125 ASP I CG  1 
ATOM   10002 O  OD1 . ASP E  1 126 ? -79.595  -38.197 13.958  1.00 23.85  ? 125 ASP I OD1 1 
ATOM   10003 O  OD2 . ASP E  1 126 ? -78.514  -37.578 15.781  1.00 23.11  ? 125 ASP I OD2 1 
ATOM   10004 N  N   . LEU E  1 127 ? -77.102  -34.893 16.937  1.00 22.22  ? 126 LEU I N   1 
ATOM   10005 C  CA  . LEU E  1 127 ? -76.933  -34.745 18.396  1.00 21.16  ? 126 LEU I CA  1 
ATOM   10006 C  C   . LEU E  1 127 ? -77.765  -35.791 19.154  1.00 21.71  ? 126 LEU I C   1 
ATOM   10007 O  O   . LEU E  1 127 ? -78.169  -35.560 20.295  1.00 19.84  ? 126 LEU I O   1 
ATOM   10008 C  CB  . LEU E  1 127 ? -77.285  -33.314 18.806  1.00 23.08  ? 126 LEU I CB  1 
ATOM   10009 C  CG  . LEU E  1 127 ? -76.550  -32.214 18.026  1.00 24.80  ? 126 LEU I CG  1 
ATOM   10010 C  CD1 . LEU E  1 127 ? -76.952  -30.846 18.537  1.00 24.17  ? 126 LEU I CD1 1 
ATOM   10011 C  CD2 . LEU E  1 127 ? -75.040  -32.402 18.069  1.00 24.02  ? 126 LEU I CD2 1 
ATOM   10012 N  N   . GLY E  1 128 ? -77.944  -36.965 18.535  1.00 22.75  ? 127 GLY I N   1 
ATOM   10013 C  CA  . GLY E  1 128 ? -78.636  -38.081 19.150  1.00 23.93  ? 127 GLY I CA  1 
ATOM   10014 C  C   . GLY E  1 128 ? -80.138  -37.895 19.163  1.00 23.70  ? 127 GLY I C   1 
ATOM   10015 O  O   . GLY E  1 128 ? -80.819  -38.620 19.877  1.00 23.98  ? 127 GLY I O   1 
ATOM   10016 N  N   . LYS E  1 129 ? -80.662  -36.967 18.351  1.00 22.07  ? 128 LYS I N   1 
ATOM   10017 C  CA  . LYS E  1 129 ? -82.101  -36.615 18.363  1.00 25.14  ? 128 LYS I CA  1 
ATOM   10018 C  C   . LYS E  1 129 ? -82.807  -37.073 17.085  1.00 22.97  ? 128 LYS I C   1 
ATOM   10019 O  O   . LYS E  1 129 ? -83.861  -36.556 16.739  1.00 23.55  ? 128 LYS I O   1 
ATOM   10020 C  CB  . LYS E  1 129 ? -82.241  -35.100 18.529  1.00 27.67  ? 128 LYS I CB  1 
ATOM   10021 C  CG  . LYS E  1 129 ? -81.745  -34.604 19.877  1.00 31.11  ? 128 LYS I CG  1 
ATOM   10022 C  CD  . LYS E  1 129 ? -81.914  -33.124 20.089  1.00 39.37  ? 128 LYS I CD  1 
ATOM   10023 C  CE  . LYS E  1 129 ? -81.662  -32.751 21.538  1.00 49.42  ? 128 LYS I CE  1 
ATOM   10024 N  NZ  . LYS E  1 129 ? -80.948  -31.454 21.640  1.00 58.59  ? 128 LYS I NZ  1 
ATOM   10025 N  N   . GLY E  1 130 ? -82.206  -38.019 16.373  1.00 21.25  ? 129 GLY I N   1 
ATOM   10026 C  CA  . GLY E  1 130 ? -82.712  -38.451 15.065  1.00 21.86  ? 129 GLY I CA  1 
ATOM   10027 C  C   . GLY E  1 130 ? -83.726  -39.604 15.131  1.00 21.55  ? 129 GLY I C   1 
ATOM   10028 O  O   . GLY E  1 130 ? -84.349  -39.939 14.111  1.00 22.69  ? 129 GLY I O   1 
ATOM   10029 N  N   . GLY E  1 131 ? -83.846  -40.265 16.283  1.00 21.78  ? 130 GLY I N   1 
ATOM   10030 C  CA  . GLY E  1 131 ? -84.933  -41.214 16.555  1.00 22.48  ? 130 GLY I CA  1 
ATOM   10031 C  C   . GLY E  1 131 ? -84.739  -42.592 15.947  1.00 24.74  ? 130 GLY I C   1 
ATOM   10032 O  O   . GLY E  1 131 ? -85.593  -43.486 16.133  1.00 23.75  ? 130 GLY I O   1 
ATOM   10033 N  N   . ASN E  1 132 ? -83.591  -42.810 15.299  1.00 24.96  ? 131 ASN I N   1 
ATOM   10034 C  CA  . ASN E  1 132 ? -83.257  -44.085 14.757  1.00 24.56  ? 131 ASN I CA  1 
ATOM   10035 C  C   . ASN E  1 132 ? -82.059  -44.605 15.541  1.00 25.13  ? 131 ASN I C   1 
ATOM   10036 O  O   . ASN E  1 132 ? -81.470  -43.927 16.402  1.00 23.59  ? 131 ASN I O   1 
ATOM   10037 C  CB  . ASN E  1 132 ? -83.058  -44.072 13.230  1.00 25.60  ? 131 ASN I CB  1 
ATOM   10038 C  CG  . ASN E  1 132 ? -81.842  -43.300 12.750  1.00 27.89  ? 131 ASN I CG  1 
ATOM   10039 O  OD1 . ASN E  1 132 ? -81.188  -42.605 13.529  1.00 25.67  ? 131 ASN I OD1 1 
ATOM   10040 N  ND2 . ASN E  1 132 ? -81.542  -43.412 11.465  1.00 26.87  ? 131 ASN I ND2 1 
ATOM   10041 N  N   . GLU E  1 133 ? -81.739  -45.861 15.274  1.00 25.63  ? 132 GLU I N   1 
ATOM   10042 C  CA  . GLU E  1 133 ? -80.675  -46.553 15.972  1.00 28.37  ? 132 GLU I CA  1 
ATOM   10043 C  C   . GLU E  1 133 ? -79.319  -45.883 15.690  1.00 27.19  ? 132 GLU I C   1 
ATOM   10044 O  O   . GLU E  1 133 ? -78.484  -45.733 16.574  1.00 26.25  ? 132 GLU I O   1 
ATOM   10045 C  CB  . GLU E  1 133 ? -80.700  -48.003 15.505  1.00 37.38  ? 132 GLU I CB  1 
ATOM   10046 C  CG  . GLU E  1 133 ? -79.987  -48.928 16.450  1.00 48.13  ? 132 GLU I CG  1 
ATOM   10047 C  CD  . GLU E  1 133 ? -80.029  -50.382 16.010  1.00 59.30  ? 132 GLU I CD  1 
ATOM   10048 O  OE1 . GLU E  1 133 ? -79.294  -51.181 16.633  1.00 64.31  ? 132 GLU I OE1 1 
ATOM   10049 O  OE2 . GLU E  1 133 ? -80.801  -50.706 15.042  1.00 60.29  ? 132 GLU I OE2 1 
ATOM   10050 N  N   . GLU E  1 134 ? -79.128  -45.437 14.453  1.00 25.57  ? 133 GLU I N   1 
ATOM   10051 C  CA  . GLU E  1 134 ? -77.873  -44.809 14.049  1.00 28.69  ? 133 GLU I CA  1 
ATOM   10052 C  C   . GLU E  1 134 ? -77.642  -43.515 14.846  1.00 26.76  ? 133 GLU I C   1 
ATOM   10053 O  O   . GLU E  1 134 ? -76.518  -43.187 15.191  1.00 24.52  ? 133 GLU I O   1 
ATOM   10054 C  CB  . GLU E  1 134 ? -77.873  -44.545 12.542  1.00 29.86  ? 133 GLU I CB  1 
ATOM   10055 C  CG  . GLU E  1 134 ? -76.508  -44.166 11.997  1.00 34.57  ? 133 GLU I CG  1 
ATOM   10056 C  CD  . GLU E  1 134 ? -75.476  -45.259 12.254  1.00 37.73  ? 133 GLU I CD  1 
ATOM   10057 O  OE1 . GLU E  1 134 ? -75.757  -46.417 11.896  1.00 43.32  ? 133 GLU I OE1 1 
ATOM   10058 O  OE2 . GLU E  1 134 ? -74.429  -44.972 12.869  1.00 40.49  ? 133 GLU I OE2 1 
ATOM   10059 N  N   . SER E  1 135 ? -78.720  -42.794 15.169  1.00 25.65  ? 134 SER I N   1 
ATOM   10060 C  CA  . SER E  1 135 ? -78.599  -41.528 15.862  1.00 25.34  ? 134 SER I CA  1 
ATOM   10061 C  C   . SER E  1 135 ? -77.944  -41.733 17.231  1.00 25.47  ? 134 SER I C   1 
ATOM   10062 O  O   . SER E  1 135 ? -77.147  -40.902 17.656  1.00 23.46  ? 134 SER I O   1 
ATOM   10063 C  CB  . SER E  1 135 ? -79.942  -40.850 15.986  1.00 24.82  ? 134 SER I CB  1 
ATOM   10064 O  OG  . SER E  1 135 ? -79.840  -39.646 16.735  1.00 22.53  ? 134 SER I OG  1 
ATOM   10065 N  N   . THR E  1 136 ? -78.277  -42.855 17.892  1.00 25.10  ? 135 THR I N   1 
ATOM   10066 C  CA  . THR E  1 136 ? -77.803  -43.175 19.229  1.00 25.96  ? 135 THR I CA  1 
ATOM   10067 C  C   . THR E  1 136 ? -76.340  -43.639 19.190  1.00 23.90  ? 135 THR I C   1 
ATOM   10068 O  O   . THR E  1 136 ? -75.773  -43.792 20.225  1.00 25.04  ? 135 THR I O   1 
ATOM   10069 C  CB  . THR E  1 136 ? -78.639  -44.291 19.894  1.00 28.85  ? 135 THR I CB  1 
ATOM   10070 O  OG1 . THR E  1 136 ? -78.408  -45.550 19.251  1.00 30.86  ? 135 THR I OG1 1 
ATOM   10071 C  CG2 . THR E  1 136 ? -80.122  -44.007 19.884  1.00 30.91  ? 135 THR I CG2 1 
ATOM   10072 N  N   . LYS E  1 137 ? -75.765  -43.888 18.004  1.00 26.64  ? 136 LYS I N   1 
ATOM   10073 C  CA  . LYS E  1 137 ? -74.381  -44.350 17.879  1.00 28.44  ? 136 LYS I CA  1 
ATOM   10074 C  C   . LYS E  1 137 ? -73.479  -43.253 17.307  1.00 25.98  ? 136 LYS I C   1 
ATOM   10075 O  O   . LYS E  1 137 ? -72.425  -43.001 17.865  1.00 25.00  ? 136 LYS I O   1 
ATOM   10076 C  CB  . LYS E  1 137 ? -74.291  -45.613 17.021  1.00 33.01  ? 136 LYS I CB  1 
ATOM   10077 C  CG  . LYS E  1 137 ? -75.157  -46.749 17.541  1.00 41.53  ? 136 LYS I CG  1 
ATOM   10078 C  CD  . LYS E  1 137 ? -74.518  -48.110 17.447  1.00 54.05  ? 136 LYS I CD  1 
ATOM   10079 C  CE  . LYS E  1 137 ? -74.539  -48.678 16.043  1.00 60.28  ? 136 LYS I CE  1 
ATOM   10080 N  NZ  . LYS E  1 137 ? -75.914  -49.024 15.606  1.00 65.67  ? 136 LYS I NZ  1 
ATOM   10081 N  N   . THR E  1 138 ? -73.883  -42.652 16.181  1.00 26.62  ? 137 THR I N   1 
ATOM   10082 C  CA  . THR E  1 138 ? -73.033  -41.764 15.439  1.00 25.48  ? 137 THR I CA  1 
ATOM   10083 C  C   . THR E  1 138 ? -73.675  -40.408 15.143  1.00 26.07  ? 137 THR I C   1 
ATOM   10084 O  O   . THR E  1 138 ? -73.042  -39.588 14.466  1.00 24.66  ? 137 THR I O   1 
ATOM   10085 C  CB  . THR E  1 138 ? -72.656  -42.373 14.084  1.00 26.59  ? 137 THR I CB  1 
ATOM   10086 O  OG1 . THR E  1 138 ? -73.845  -42.442 13.287  1.00 26.00  ? 137 THR I OG1 1 
ATOM   10087 C  CG2 . THR E  1 138 ? -71.959  -43.708 14.227  1.00 27.49  ? 137 THR I CG2 1 
ATOM   10088 N  N   . GLY E  1 139 ? -74.938  -40.202 15.540  1.00 23.20  ? 138 GLY I N   1 
ATOM   10089 C  CA  . GLY E  1 139 ? -75.666  -38.953 15.217  1.00 22.73  ? 138 GLY I CA  1 
ATOM   10090 C  C   . GLY E  1 139 ? -75.961  -38.831 13.725  1.00 21.60  ? 138 GLY I C   1 
ATOM   10091 O  O   . GLY E  1 139 ? -76.305  -37.746 13.236  1.00 20.84  ? 138 GLY I O   1 
ATOM   10092 N  N   . ASN E  1 140 ? -75.873  -39.949 12.996  1.00 21.87  ? 139 ASN I N   1 
ATOM   10093 C  CA  . ASN E  1 140 ? -76.134  -39.981 11.535  1.00 22.80  ? 139 ASN I CA  1 
ATOM   10094 C  C   . ASN E  1 140 ? -75.159  -39.044 10.809  1.00 22.55  ? 139 ASN I C   1 
ATOM   10095 O  O   . ASN E  1 140 ? -75.495  -38.455 9.794   1.00 25.45  ? 139 ASN I O   1 
ATOM   10096 C  CB  . ASN E  1 140 ? -77.600  -39.646 11.202  1.00 23.14  ? 139 ASN I CB  1 
ATOM   10097 C  CG  . ASN E  1 140 ? -78.566  -40.763 11.588  1.00 25.60  ? 139 ASN I CG  1 
ATOM   10098 O  OD1 . ASN E  1 140 ? -78.570  -41.812 10.960  1.00 26.38  ? 139 ASN I OD1 1 
ATOM   10099 N  ND2 . ASN E  1 140 ? -79.354  -40.569 12.635  1.00 22.83  ? 139 ASN I ND2 1 
ATOM   10100 N  N   . ALA E  1 141 ? -73.942  -38.883 11.327  1.00 21.83  ? 140 ALA I N   1 
ATOM   10101 C  CA  . ALA E  1 141 ? -73.006  -37.898 10.766  1.00 22.63  ? 140 ALA I CA  1 
ATOM   10102 C  C   . ALA E  1 141 ? -72.328  -38.411 9.479   1.00 23.84  ? 140 ALA I C   1 
ATOM   10103 O  O   . ALA E  1 141 ? -71.616  -37.670 8.815   1.00 22.15  ? 140 ALA I O   1 
ATOM   10104 C  CB  . ALA E  1 141 ? -71.978  -37.525 11.795  1.00 21.80  ? 140 ALA I CB  1 
ATOM   10105 N  N   . GLY E  1 142 ? -72.463  -39.708 9.200   1.00 25.17  ? 141 GLY I N   1 
ATOM   10106 C  CA  . GLY E  1 142 ? -72.005  -40.277 7.949   1.00 24.99  ? 141 GLY I CA  1 
ATOM   10107 C  C   . GLY E  1 142 ? -70.506  -40.479 7.929   1.00 24.00  ? 141 GLY I C   1 
ATOM   10108 O  O   . GLY E  1 142 ? -69.892  -40.665 8.975   1.00 23.02  ? 141 GLY I O   1 
ATOM   10109 N  N   . SER E  1 143 ? -69.950  -40.431 6.712   1.00 25.18  ? 142 SER I N   1 
ATOM   10110 C  CA  . SER E  1 143 ? -68.549  -40.737 6.392   1.00 26.00  ? 142 SER I CA  1 
ATOM   10111 C  C   . SER E  1 143 ? -67.581  -39.861 7.179   1.00 22.45  ? 142 SER I C   1 
ATOM   10112 O  O   . SER E  1 143 ? -67.843  -38.698 7.439   1.00 23.27  ? 142 SER I O   1 
ATOM   10113 C  CB  . SER E  1 143 ? -68.278  -40.523 4.916   1.00 29.62  ? 142 SER I CB  1 
ATOM   10114 O  OG  . SER E  1 143 ? -68.760  -41.630 4.212   1.00 39.29  ? 142 SER I OG  1 
ATOM   10115 N  N   . ARG E  1 144 ? -66.407  -40.428 7.405   1.00 21.97  ? 143 ARG I N   1 
ATOM   10116 C  CA  . ARG E  1 144 ? -65.281  -39.771 8.014   1.00 24.60  ? 143 ARG I CA  1 
ATOM   10117 C  C   . ARG E  1 144 ? -64.448  -39.085 6.923   1.00 24.54  ? 143 ARG I C   1 
ATOM   10118 O  O   . ARG E  1 144 ? -63.744  -39.750 6.165   1.00 26.13  ? 143 ARG I O   1 
ATOM   10119 C  CB  . ARG E  1 144 ? -64.466  -40.840 8.733   1.00 23.87  ? 143 ARG I CB  1 
ATOM   10120 C  CG  . ARG E  1 144 ? -65.290  -41.626 9.743   1.00 23.42  ? 143 ARG I CG  1 
ATOM   10121 C  CD  . ARG E  1 144 ? -64.534  -42.735 10.447  1.00 22.97  ? 143 ARG I CD  1 
ATOM   10122 N  NE  . ARG E  1 144 ? -65.474  -43.514 11.237  1.00 22.58  ? 143 ARG I NE  1 
ATOM   10123 C  CZ  . ARG E  1 144 ? -65.174  -44.306 12.248  1.00 21.95  ? 143 ARG I CZ  1 
ATOM   10124 N  NH1 . ARG E  1 144 ? -66.160  -44.917 12.889  1.00 22.27  ? 143 ARG I NH1 1 
ATOM   10125 N  NH2 . ARG E  1 144 ? -63.911  -44.525 12.591  1.00 22.26  ? 143 ARG I NH2 1 
ATOM   10126 N  N   . LEU E  1 145 ? -64.494  -37.755 6.865   1.00 23.57  ? 144 LEU I N   1 
ATOM   10127 C  CA  . LEU E  1 145 ? -63.840  -37.015 5.768   1.00 22.67  ? 144 LEU I CA  1 
ATOM   10128 C  C   . LEU E  1 145 ? -62.354  -36.845 6.061   1.00 22.66  ? 144 LEU I C   1 
ATOM   10129 O  O   . LEU E  1 145 ? -61.527  -36.855 5.150   1.00 22.71  ? 144 LEU I O   1 
ATOM   10130 C  CB  . LEU E  1 145 ? -64.497  -35.648 5.600   1.00 24.59  ? 144 LEU I CB  1 
ATOM   10131 C  CG  . LEU E  1 145 ? -65.949  -35.645 5.131   1.00 27.84  ? 144 LEU I CG  1 
ATOM   10132 C  CD1 . LEU E  1 145 ? -66.387  -34.222 4.872   1.00 29.89  ? 144 LEU I CD1 1 
ATOM   10133 C  CD2 . LEU E  1 145 ? -66.154  -36.496 3.886   1.00 29.66  ? 144 LEU I CD2 1 
ATOM   10134 N  N   . ALA E  1 146 ? -62.012  -36.645 7.335   1.00 21.20  ? 145 ALA I N   1 
ATOM   10135 C  CA  . ALA E  1 146 ? -60.643  -36.485 7.709   1.00 20.60  ? 145 ALA I CA  1 
ATOM   10136 C  C   . ALA E  1 146 ? -60.469  -36.828 9.188   1.00 22.56  ? 145 ALA I C   1 
ATOM   10137 O  O   . ALA E  1 146 ? -61.421  -36.702 9.976   1.00 21.94  ? 145 ALA I O   1 
ATOM   10138 C  CB  . ALA E  1 146 ? -60.177  -35.081 7.430   1.00 21.54  ? 145 ALA I CB  1 
ATOM   10139 N  N   . CYS E  1 147 ? -59.225  -37.164 9.562   1.00 20.55  ? 146 CYS I N   1 
ATOM   10140 C  CA  . CYS E  1 147 ? -58.953  -37.506 10.931  1.00 22.76  ? 146 CYS I CA  1 
ATOM   10141 C  C   . CYS E  1 147 ? -57.461  -37.399 11.218  1.00 22.02  ? 146 CYS I C   1 
ATOM   10142 O  O   . CYS E  1 147 ? -56.659  -37.227 10.314  1.00 21.35  ? 146 CYS I O   1 
ATOM   10143 C  CB  . CYS E  1 147 ? -59.454  -38.904 11.251  1.00 25.35  ? 146 CYS I CB  1 
ATOM   10144 S  SG  . CYS E  1 147 ? -58.596  -40.192 10.321  1.00 29.00  ? 146 CYS I SG  1 
ATOM   10145 N  N   . GLY E  1 148 ? -57.124  -37.488 12.501  1.00 21.15  ? 147 GLY I N   1 
ATOM   10146 C  CA  . GLY E  1 148 ? -55.749  -37.609 12.919  1.00 22.05  ? 147 GLY I CA  1 
ATOM   10147 C  C   . GLY E  1 148 ? -55.699  -37.962 14.393  1.00 22.23  ? 147 GLY I C   1 
ATOM   10148 O  O   . GLY E  1 148 ? -56.686  -37.858 15.101  1.00 19.83  ? 147 GLY I O   1 
ATOM   10149 N  N   . VAL E  1 149 ? -54.531  -38.388 14.831  1.00 21.22  ? 148 VAL I N   1 
ATOM   10150 C  CA  . VAL E  1 149 ? -54.310  -38.776 16.185  1.00 23.39  ? 148 VAL I CA  1 
ATOM   10151 C  C   . VAL E  1 149 ? -53.990  -37.518 16.989  1.00 21.89  ? 148 VAL I C   1 
ATOM   10152 O  O   . VAL E  1 149 ? -53.225  -36.689 16.553  1.00 22.91  ? 148 VAL I O   1 
ATOM   10153 C  CB  . VAL E  1 149 ? -53.173  -39.810 16.279  1.00 24.13  ? 148 VAL I CB  1 
ATOM   10154 C  CG1 . VAL E  1 149 ? -52.955  -40.280 17.706  1.00 23.22  ? 148 VAL I CG1 1 
ATOM   10155 C  CG2 . VAL E  1 149 ? -53.402  -40.989 15.359  1.00 26.28  ? 148 VAL I CG2 1 
ATOM   10156 N  N   . ILE E  1 150 ? -54.562  -37.428 18.181  1.00 22.57  ? 149 ILE I N   1 
ATOM   10157 C  CA  . ILE E  1 150 ? -54.370  -36.288 19.053  1.00 22.21  ? 149 ILE I CA  1 
ATOM   10158 C  C   . ILE E  1 150 ? -53.063  -36.481 19.824  1.00 22.09  ? 149 ILE I C   1 
ATOM   10159 O  O   . ILE E  1 150 ? -52.951  -37.419 20.601  1.00 21.60  ? 149 ILE I O   1 
ATOM   10160 C  CB  . ILE E  1 150 ? -55.579  -36.146 19.993  1.00 22.33  ? 149 ILE I CB  1 
ATOM   10161 C  CG1 . ILE E  1 150 ? -56.875  -35.956 19.197  1.00 21.53  ? 149 ILE I CG1 1 
ATOM   10162 C  CG2 . ILE E  1 150 ? -55.357  -35.022 20.998  1.00 23.67  ? 149 ILE I CG2 1 
ATOM   10163 C  CD1 . ILE E  1 150 ? -58.145  -36.311 19.962  1.00 21.42  ? 149 ILE I CD1 1 
ATOM   10164 N  N   . GLY E  1 151 ? -52.126  -35.544 19.649  1.00 21.96  ? 150 GLY I N   1 
ATOM   10165 C  CA  . GLY E  1 151 ? -50.810  -35.635 20.225  1.00 22.54  ? 150 GLY I CA  1 
ATOM   10166 C  C   . GLY E  1 151 ? -50.554  -34.555 21.252  1.00 22.58  ? 150 GLY I C   1 
ATOM   10167 O  O   . GLY E  1 151 ? -51.168  -33.493 21.246  1.00 22.63  ? 150 GLY I O   1 
ATOM   10168 N  N   . ILE E  1 152 ? -49.613  -34.836 22.143  1.00 21.88  ? 151 ILE I N   1 
ATOM   10169 C  CA  . ILE E  1 152 ? -49.132  -33.842 23.125  1.00 24.50  ? 151 ILE I CA  1 
ATOM   10170 C  C   . ILE E  1 152 ? -48.390  -32.717 22.389  1.00 25.76  ? 151 ILE I C   1 
ATOM   10171 O  O   . ILE E  1 152 ? -47.524  -32.987 21.557  1.00 24.16  ? 151 ILE I O   1 
ATOM   10172 C  CB  . ILE E  1 152 ? -48.233  -34.516 24.172  1.00 24.65  ? 151 ILE I CB  1 
ATOM   10173 C  CG1 . ILE E  1 152 ? -49.006  -35.598 24.934  1.00 24.47  ? 151 ILE I CG1 1 
ATOM   10174 C  CG2 . ILE E  1 152 ? -47.615  -33.481 25.088  1.00 24.21  ? 151 ILE I CG2 1 
ATOM   10175 C  CD1 . ILE E  1 152 ? -48.134  -36.571 25.697  1.00 25.43  ? 151 ILE I CD1 1 
ATOM   10176 N  N   . ALA E  1 153 ? -48.758  -31.466 22.696  1.00 26.08  ? 152 ALA I N   1 
ATOM   10177 C  CA  . ALA E  1 153 ? -48.156  -30.279 22.072  1.00 31.01  ? 152 ALA I CA  1 
ATOM   10178 C  C   . ALA E  1 153 ? -47.332  -29.536 23.132  1.00 32.90  ? 152 ALA I C   1 
ATOM   10179 O  O   . ALA E  1 153 ? -47.555  -29.769 24.281  1.00 36.89  ? 152 ALA I O   1 
ATOM   10180 C  CB  . ALA E  1 153 ? -49.262  -29.430 21.494  1.00 28.59  ? 152 ALA I CB  1 
ATOM   10181 N  N   . GLN E  1 154 ? -46.486  -28.570 22.752  1.00 52.97  ? 153 GLN I N   1 
ATOM   10182 C  CA  . GLN E  1 154 ? -45.368  -28.063 23.652  1.00 62.73  ? 153 GLN I CA  1 
ATOM   10183 C  C   . GLN E  1 154 ? -45.893  -27.414 24.953  1.00 71.99  ? 153 GLN I C   1 
ATOM   10184 O  O   . GLN E  1 154 ? -45.719  -26.224 25.184  1.00 76.94  ? 153 GLN I O   1 
ATOM   10185 C  CB  . GLN E  1 154 ? -44.424  -27.146 22.872  1.00 69.70  ? 153 GLN I CB  1 
ATOM   10186 C  CG  . GLN E  1 154 ? -43.187  -26.717 23.664  1.00 74.67  ? 153 GLN I CG  1 
ATOM   10187 C  CD  . GLN E  1 154 ? -41.930  -26.608 22.828  1.00 79.14  ? 153 GLN I CD  1 
ATOM   10188 O  OE1 . GLN E  1 154 ? -40.827  -26.377 23.341  1.00 73.37  ? 153 GLN I OE1 1 
ATOM   10189 N  NE2 . GLN E  1 154 ? -42.084  -26.795 21.522  1.00 77.80  ? 153 GLN I NE2 1 
ATOM   10190 N  N   . GLY E  1 155 ? -46.477  -28.237 25.836  1.00 78.74  ? 154 GLY I N   1 
ATOM   10191 C  CA  . GLY E  1 155 ? -47.011  -27.817 27.133  1.00 76.70  ? 154 GLY I CA  1 
ATOM   10192 C  C   . GLY E  1 155 ? -46.411  -28.640 28.264  1.00 78.04  ? 154 GLY I C   1 
ATOM   10193 O  O   . GLY E  1 155 ? -45.214  -28.952 28.228  1.00 78.70  ? 154 GLY I O   1 
ATOM   10194 N  N   . ALA E  1 156 ? -47.254  -29.030 29.232  1.00 73.70  ? 155 ALA I N   1 
ATOM   10195 C  CA  . ALA E  1 156 ? -46.825  -29.551 30.544  1.00 74.99  ? 155 ALA I CA  1 
ATOM   10196 C  C   . ALA E  1 156 ? -47.779  -30.652 31.047  1.00 76.43  ? 155 ALA I C   1 
ATOM   10197 O  O   . ALA E  1 156 ? -48.698  -31.061 30.336  1.00 78.11  ? 155 ALA I O   1 
ATOM   10198 C  CB  . ALA E  1 156 ? -46.752  -28.401 31.526  1.00 72.06  ? 155 ALA I CB  1 
ATOM   10199 N  N   . ALA E  1 157 ? -47.491  -31.154 32.260  1.00 77.22  ? 156 ALA I N   1 
ATOM   10200 C  CA  . ALA E  1 157 ? -48.429  -31.837 33.189  1.00 71.14  ? 156 ALA I CA  1 
ATOM   10201 C  C   . ALA E  1 157 ? -49.565  -32.548 32.442  1.00 69.85  ? 156 ALA I C   1 
ATOM   10202 O  O   . ALA E  1 157 ? -50.643  -32.778 33.006  1.00 68.24  ? 156 ALA I O   1 
ATOM   10203 C  CB  . ALA E  1 157 ? -48.974  -30.824 34.168  1.00 67.14  ? 156 ALA I CB  1 
ATOM   10204 N  N   . GLY E  1 167 ? -48.691  -36.232 31.899  1.00 65.39  ? 166 GLY I N   1 
ATOM   10205 C  CA  . GLY E  1 167 ? -50.041  -35.778 31.437  1.00 63.83  ? 166 GLY I CA  1 
ATOM   10206 C  C   . GLY E  1 167 ? -50.315  -36.219 30.003  1.00 68.76  ? 166 GLY I C   1 
ATOM   10207 O  O   . GLY E  1 167 ? -49.821  -35.640 29.000  1.00 50.84  ? 166 GLY I O   1 
ATOM   10208 N  N   . GLY E  1 168 ? -51.126  -37.260 29.861  1.00 58.15  ? 167 GLY I N   1 
ATOM   10209 C  CA  . GLY E  1 168 ? -51.363  -37.731 28.551  1.00 53.75  ? 167 GLY I CA  1 
ATOM   10210 C  C   . GLY E  1 168 ? -52.234  -38.955 28.547  1.00 47.04  ? 167 GLY I C   1 
ATOM   10211 O  O   . GLY E  1 168 ? -53.401  -38.881 28.969  1.00 39.31  ? 167 GLY I O   1 
ATOM   10212 N  N   . GLY E  1 169 ? -51.640  -40.062 28.076  1.00 40.42  ? 168 GLY I N   1 
ATOM   10213 C  CA  . GLY E  1 169 ? -52.372  -41.213 27.680  1.00 40.82  ? 168 GLY I CA  1 
ATOM   10214 C  C   . GLY E  1 169 ? -51.885  -42.495 28.317  1.00 42.95  ? 168 GLY I C   1 
ATOM   10215 O  O   . GLY E  1 169 ? -50.708  -42.607 28.692  1.00 33.86  ? 168 GLY I O   1 
ATOM   10216 N  N   . SER E  1 170 ? -52.827  -43.450 28.386  1.00 49.36  ? 169 SER I N   1 
ATOM   10217 C  CA  . SER E  1 170 ? -52.646  -44.781 28.928  1.00 59.59  ? 169 SER I CA  1 
ATOM   10218 C  C   . SER E  1 170 ? -53.293  -45.796 27.973  1.00 58.91  ? 169 SER I C   1 
ATOM   10219 O  O   . SER E  1 170 ? -54.270  -45.413 27.317  1.00 57.55  ? 169 SER I O   1 
ATOM   10220 C  CB  . SER E  1 170 ? -53.214  -44.875 30.341  1.00 69.47  ? 169 SER I CB  1 
ATOM   10221 O  OG  . SER E  1 170 ? -54.346  -44.030 30.515  1.00 80.16  ? 169 SER I OG  1 
ATOM   10222 N  N   . ALA E  1 171 ? -52.732  -47.033 27.904  1.00 44.45  ? 170 ALA I N   1 
ATOM   10223 C  CA  . ALA E  1 171 ? -53.237  -48.175 27.094  1.00 43.68  ? 170 ALA I CA  1 
ATOM   10224 C  C   . ALA E  1 171 ? -52.343  -49.431 27.224  1.00 37.57  ? 170 ALA I C   1 
ATOM   10225 O  O   . ALA E  1 171 ? -51.215  -49.353 27.642  1.00 43.27  ? 170 ALA I O   1 
ATOM   10226 C  CB  . ALA E  1 171 ? -53.325  -47.755 25.649  1.00 46.86  ? 170 ALA I CB  1 
ATOM   10227 N  N   . THR E  1 172 ? -52.871  -50.597 26.843  1.00 35.25  ? 171 THR I N   1 
ATOM   10228 C  CA  . THR E  1 172 ? -52.104  -51.850 26.795  1.00 34.98  ? 171 THR I CA  1 
ATOM   10229 C  C   . THR E  1 172 ? -51.643  -52.148 25.360  1.00 30.83  ? 171 THR I C   1 
ATOM   10230 O  O   . THR E  1 172 ? -50.729  -52.921 25.184  1.00 31.27  ? 171 THR I O   1 
ATOM   10231 C  CB  . THR E  1 172 ? -52.889  -53.044 27.342  1.00 37.82  ? 171 THR I CB  1 
ATOM   10232 O  OG1 . THR E  1 172 ? -53.895  -53.356 26.386  1.00 38.83  ? 171 THR I OG1 1 
ATOM   10233 C  CG2 . THR E  1 172 ? -53.531  -52.767 28.683  1.00 40.51  ? 171 THR I CG2 1 
ATOM   10234 N  N   . LYS E  1 173 ? -52.261  -51.525 24.351  1.00 29.04  ? 172 LYS I N   1 
ATOM   10235 C  CA  . LYS E  1 173 ? -51.802  -51.589 22.962  1.00 29.71  ? 172 LYS I CA  1 
ATOM   10236 C  C   . LYS E  1 173 ? -51.748  -50.193 22.335  1.00 26.65  ? 172 LYS I C   1 
ATOM   10237 O  O   . LYS E  1 173 ? -52.631  -49.357 22.567  1.00 26.44  ? 172 LYS I O   1 
ATOM   10238 C  CB  . LYS E  1 173 ? -52.737  -52.471 22.145  1.00 33.49  ? 172 LYS I CB  1 
ATOM   10239 C  CG  . LYS E  1 173 ? -52.643  -53.949 22.467  1.00 42.22  ? 172 LYS I CG  1 
ATOM   10240 C  CD  . LYS E  1 173 ? -52.039  -54.743 21.346  1.00 51.19  ? 172 LYS I CD  1 
ATOM   10241 C  CE  . LYS E  1 173 ? -53.004  -54.954 20.202  1.00 52.23  ? 172 LYS I CE  1 
ATOM   10242 N  NZ  . LYS E  1 173 ? -52.301  -55.529 19.034  1.00 58.33  ? 172 LYS I NZ  1 
ATOM   10243 N  N   . ALA E  1 174 ? -50.715  -49.953 21.523  1.00 23.24  ? 173 ALA I N   1 
ATOM   10244 C  CA  . ALA E  1 174 ? -50.607  -48.712 20.774  1.00 23.13  ? 173 ALA I CA  1 
ATOM   10245 C  C   . ALA E  1 174 ? -50.144  -49.035 19.355  1.00 24.20  ? 173 ALA I C   1 
ATOM   10246 O  O   . ALA E  1 174 ? -49.697  -50.151 19.059  1.00 24.36  ? 173 ALA I O   1 
ATOM   10247 C  CB  . ALA E  1 174 ? -49.681  -47.746 21.491  1.00 22.38  ? 173 ALA I CB  1 
ATOM   10248 N  N   . VAL E  1 175 ? -50.263  -48.049 18.468  1.00 24.15  ? 174 VAL I N   1 
ATOM   10249 C  CA  . VAL E  1 175 ? -49.873  -48.227 17.076  1.00 24.23  ? 174 VAL I CA  1 
ATOM   10250 C  C   . VAL E  1 175 ? -49.445  -46.867 16.550  1.00 25.60  ? 174 VAL I C   1 
ATOM   10251 O  O   . VAL E  1 175 ? -49.892  -45.810 17.044  1.00 24.77  ? 174 VAL I O   1 
ATOM   10252 C  CB  . VAL E  1 175 ? -51.012  -48.847 16.238  1.00 25.47  ? 174 VAL I CB  1 
ATOM   10253 C  CG1 . VAL E  1 175 ? -52.169  -47.886 16.074  1.00 25.98  ? 174 VAL I CG1 1 
ATOM   10254 C  CG2 . VAL E  1 175 ? -50.528  -49.321 14.885  1.00 27.29  ? 174 VAL I CG2 1 
ATOM   10255 N  N   . CYS E  1 176 ? -48.560  -46.900 15.559  1.00 24.96  ? 175 CYS I N   1 
ATOM   10256 C  CA  . CYS E  1 176 ? -48.059  -45.727 14.955  1.00 24.38  ? 175 CYS I CA  1 
ATOM   10257 C  C   . CYS E  1 176 ? -47.920  -45.972 13.452  1.00 24.86  ? 175 CYS I C   1 
ATOM   10258 O  O   . CYS E  1 176 ? -47.311  -46.973 13.049  1.00 24.10  ? 175 CYS I O   1 
ATOM   10259 C  CB  . CYS E  1 176 ? -46.708  -45.364 15.562  1.00 25.07  ? 175 CYS I CB  1 
ATOM   10260 S  SG  . CYS E  1 176 ? -46.012  -43.816 14.932  1.00 29.22  ? 175 CYS I SG  1 
ATOM   10261 N  N   . VAL E  1 177 ? -48.495  -45.061 12.662  1.00 23.00  ? 176 VAL I N   1 
ATOM   10262 C  CA  . VAL E  1 177 ? -48.314  -44.984 11.221  1.00 25.03  ? 176 VAL I CA  1 
ATOM   10263 C  C   . VAL E  1 177 ? -47.272  -43.904 10.920  1.00 24.75  ? 176 VAL I C   1 
ATOM   10264 O  O   . VAL E  1 177 ? -47.462  -42.736 11.192  1.00 25.99  ? 176 VAL I O   1 
ATOM   10265 C  CB  . VAL E  1 177 ? -49.646  -44.736 10.501  1.00 26.19  ? 176 VAL I CB  1 
ATOM   10266 C  CG1 . VAL E  1 177 ? -49.464  -44.690 8.985   1.00 27.01  ? 176 VAL I CG1 1 
ATOM   10267 C  CG2 . VAL E  1 177 ? -50.661  -45.807 10.870  1.00 28.51  ? 176 VAL I CG2 1 
ATOM   10268 N  N   . LEU E  1 178 ? -46.118  -44.340 10.416  1.00 27.54  ? 177 LEU I N   1 
ATOM   10269 C  CA  . LEU E  1 178 ? -45.005  -43.481 10.075  1.00 28.01  ? 177 LEU I CA  1 
ATOM   10270 C  C   . LEU E  1 178 ? -45.164  -43.027 8.618   1.00 28.99  ? 177 LEU I C   1 
ATOM   10271 O  O   . LEU E  1 178 ? -45.320  -43.864 7.736   1.00 29.88  ? 177 LEU I O   1 
ATOM   10272 C  CB  . LEU E  1 178 ? -43.699  -44.269 10.200  1.00 32.76  ? 177 LEU I CB  1 
ATOM   10273 C  CG  . LEU E  1 178 ? -43.294  -44.764 11.587  1.00 35.21  ? 177 LEU I CG  1 
ATOM   10274 C  CD1 . LEU E  1 178 ? -42.196  -45.808 11.462  1.00 39.79  ? 177 LEU I CD1 1 
ATOM   10275 C  CD2 . LEU E  1 178 ? -42.803  -43.621 12.443  1.00 37.58  ? 177 LEU I CD2 1 
ATOM   10276 N  N   . LYS E  1 179 ? -45.091  -41.716 8.389   1.00 28.93  ? 178 LYS I N   1 
ATOM   10277 C  CA  . LYS E  1 179 ? -45.052  -41.111 7.049   1.00 31.73  ? 178 LYS I CA  1 
ATOM   10278 C  C   . LYS E  1 179 ? -44.128  -39.903 7.101   1.00 28.69  ? 178 LYS I C   1 
ATOM   10279 O  O   . LYS E  1 179 ? -43.860  -39.352 8.173   1.00 26.24  ? 178 LYS I O   1 
ATOM   10280 C  CB  . LYS E  1 179 ? -46.407  -40.572 6.581   1.00 37.22  ? 178 LYS I CB  1 
ATOM   10281 C  CG  . LYS E  1 179 ? -47.588  -41.508 6.749   1.00 44.48  ? 178 LYS I CG  1 
ATOM   10282 C  CD  . LYS E  1 179 ? -47.905  -42.350 5.539   1.00 54.73  ? 178 LYS I CD  1 
ATOM   10283 C  CE  . LYS E  1 179 ? -49.386  -42.675 5.447   1.00 61.47  ? 178 LYS I CE  1 
ATOM   10284 N  NZ  . LYS E  1 179 ? -49.616  -44.011 4.848   1.00 68.42  ? 178 LYS I NZ  1 
ATOM   10285 N  N   . GLY E  1 180 ? -43.705  -39.447 5.925   1.00 31.23  ? 179 GLY I N   1 
ATOM   10286 C  CA  . GLY E  1 180 ? -42.823  -38.280 5.832   1.00 32.92  ? 179 GLY I CA  1 
ATOM   10287 C  C   . GLY E  1 180 ? -42.925  -37.623 4.473   1.00 34.57  ? 179 GLY I C   1 
ATOM   10288 O  O   . GLY E  1 180 ? -43.774  -37.983 3.681   1.00 33.81  ? 179 GLY I O   1 
ATOM   10289 N  N   . ASP E  1 181 ? -42.015  -36.682 4.216   1.00 38.47  ? 180 ASP I N   1 
ATOM   10290 C  CA  . ASP E  1 181 ? -41.969  -35.940 2.963   1.00 44.14  ? 180 ASP I CA  1 
ATOM   10291 C  C   . ASP E  1 181 ? -41.484  -36.839 1.821   1.00 44.14  ? 180 ASP I C   1 
ATOM   10292 O  O   . ASP E  1 181 ? -41.702  -36.509 0.672   1.00 47.82  ? 180 ASP I O   1 
ATOM   10293 C  CB  . ASP E  1 181 ? -41.083  -34.701 3.098   1.00 49.50  ? 180 ASP I CB  1 
ATOM   10294 C  CG  . ASP E  1 181 ? -41.734  -33.617 3.945   1.00 59.19  ? 180 ASP I CG  1 
ATOM   10295 O  OD1 . ASP E  1 181 ? -42.981  -33.523 3.912   1.00 66.09  ? 180 ASP I OD1 1 
ATOM   10296 O  OD2 . ASP E  1 181 ? -40.997  -32.891 4.650   1.00 72.62  ? 180 ASP I OD2 1 
ATOM   10297 N  N   . GLY E  1 182 ? -40.836  -37.959 2.157   1.00 42.11  ? 181 GLY I N   1 
ATOM   10298 C  CA  . GLY E  1 182 ? -40.265  -38.856 1.203   1.00 39.73  ? 181 GLY I CA  1 
ATOM   10299 C  C   . GLY E  1 182 ? -41.043  -40.161 1.102   1.00 36.94  ? 181 GLY I C   1 
ATOM   10300 O  O   . GLY E  1 182 ? -42.249  -40.211 1.340   1.00 38.18  ? 181 GLY I O   1 
ATOM   10301 N  N   . PRO E  1 183 ? -40.355  -41.255 0.713   1.00 32.10  ? 182 PRO I N   1 
ATOM   10302 C  CA  . PRO E  1 183 ? -40.982  -42.567 0.573   1.00 33.53  ? 182 PRO I CA  1 
ATOM   10303 C  C   . PRO E  1 183 ? -41.033  -43.448 1.815   1.00 28.70  ? 182 PRO I C   1 
ATOM   10304 O  O   . PRO E  1 183 ? -41.593  -44.527 1.753   1.00 32.88  ? 182 PRO I O   1 
ATOM   10305 C  CB  . PRO E  1 183 ? -40.027  -43.245 -0.422  1.00 34.08  ? 182 PRO I CB  1 
ATOM   10306 C  CG  . PRO E  1 183 ? -38.670  -42.705 -0.032  1.00 30.93  ? 182 PRO I CG  1 
ATOM   10307 C  CD  . PRO E  1 183 ? -38.935  -41.264 0.337   1.00 34.57  ? 182 PRO I CD  1 
ATOM   10308 N  N   . VAL E  1 184 ? -40.446  -43.006 2.925   1.00 30.46  ? 183 VAL I N   1 
ATOM   10309 C  CA  . VAL E  1 184 ? -40.402  -43.846 4.113   1.00 31.13  ? 183 VAL I CA  1 
ATOM   10310 C  C   . VAL E  1 184 ? -41.817  -43.954 4.699   1.00 32.00  ? 183 VAL I C   1 
ATOM   10311 O  O   . VAL E  1 184 ? -42.493  -42.940 4.953   1.00 33.19  ? 183 VAL I O   1 
ATOM   10312 C  CB  . VAL E  1 184 ? -39.403  -43.325 5.154   1.00 32.16  ? 183 VAL I CB  1 
ATOM   10313 C  CG1 . VAL E  1 184 ? -39.418  -44.190 6.403   1.00 33.24  ? 183 VAL I CG1 1 
ATOM   10314 C  CG2 . VAL E  1 184 ? -37.990  -43.253 4.598   1.00 34.03  ? 183 VAL I CG2 1 
ATOM   10315 N  N   . GLN E  1 185 ? -42.255  -45.187 4.940   1.00 32.88  ? 184 GLN I N   1 
ATOM   10316 C  CA  . GLN E  1 185 ? -43.519  -45.417 5.585   1.00 35.69  ? 184 GLN I CA  1 
ATOM   10317 C  C   . GLN E  1 185 ? -43.504  -46.754 6.313   1.00 34.45  ? 184 GLN I C   1 
ATOM   10318 O  O   . GLN E  1 185 ? -42.752  -47.666 5.979   1.00 30.22  ? 184 GLN I O   1 
ATOM   10319 C  CB  . GLN E  1 185 ? -44.658  -45.411 4.574   1.00 42.80  ? 184 GLN I CB  1 
ATOM   10320 C  CG  . GLN E  1 185 ? -44.394  -46.289 3.373   1.00 49.02  ? 184 GLN I CG  1 
ATOM   10321 C  CD  . GLN E  1 185 ? -45.169  -45.792 2.179   1.00 58.40  ? 184 GLN I CD  1 
ATOM   10322 O  OE1 . GLN E  1 185 ? -46.374  -45.586 2.254   1.00 55.61  ? 184 GLN I OE1 1 
ATOM   10323 N  NE2 . GLN E  1 185 ? -44.474  -45.610 1.065   1.00 67.50  ? 184 GLN I NE2 1 
ATOM   10324 N  N   . GLY E  1 186 ? -44.393  -46.865 7.293   1.00 28.93  ? 185 GLY I N   1 
ATOM   10325 C  CA  . GLY E  1 186 ? -44.426  -48.034 8.099   1.00 31.35  ? 185 GLY I CA  1 
ATOM   10326 C  C   . GLY E  1 186 ? -45.527  -48.006 9.135   1.00 30.97  ? 185 GLY I C   1 
ATOM   10327 O  O   . GLY E  1 186 ? -46.191  -46.993 9.343   1.00 31.27  ? 185 GLY I O   1 
ATOM   10328 N  N   . ILE E  1 187 ? -45.697  -49.165 9.768   1.00 29.83  ? 186 ILE I N   1 
ATOM   10329 C  CA  . ILE E  1 187 ? -46.609  -49.367 10.856  1.00 30.56  ? 186 ILE I CA  1 
ATOM   10330 C  C   . ILE E  1 187 ? -45.840  -50.068 11.987  1.00 29.54  ? 186 ILE I C   1 
ATOM   10331 O  O   . ILE E  1 187 ? -45.262  -51.140 11.780  1.00 27.50  ? 186 ILE I O   1 
ATOM   10332 C  CB  . ILE E  1 187 ? -47.827  -50.178 10.383  1.00 30.38  ? 186 ILE I CB  1 
ATOM   10333 C  CG1 . ILE E  1 187 ? -48.599  -49.413 9.300   1.00 31.67  ? 186 ILE I CG1 1 
ATOM   10334 C  CG2 . ILE E  1 187 ? -48.704  -50.567 11.568  1.00 30.09  ? 186 ILE I CG2 1 
ATOM   10335 C  CD1 . ILE E  1 187 ? -49.779  -50.151 8.737   1.00 33.77  ? 186 ILE I CD1 1 
ATOM   10336 N  N   . ILE E  1 188 ? -45.858  -49.456 13.172  1.00 25.88  ? 187 ILE I N   1 
ATOM   10337 C  CA  . ILE E  1 188 ? -45.236  -50.001 14.375  1.00 26.54  ? 187 ILE I CA  1 
ATOM   10338 C  C   . ILE E  1 188 ? -46.311  -50.223 15.446  1.00 27.74  ? 187 ILE I C   1 
ATOM   10339 O  O   . ILE E  1 188 ? -47.105  -49.315 15.758  1.00 27.24  ? 187 ILE I O   1 
ATOM   10340 C  CB  . ILE E  1 188 ? -44.122  -49.073 14.871  1.00 26.90  ? 187 ILE I CB  1 
ATOM   10341 C  CG1 . ILE E  1 188 ? -43.058  -48.833 13.792  1.00 30.22  ? 187 ILE I CG1 1 
ATOM   10342 C  CG2 . ILE E  1 188 ? -43.510  -49.613 16.152  1.00 28.93  ? 187 ILE I CG2 1 
ATOM   10343 C  CD1 . ILE E  1 188 ? -42.260  -50.080 13.408  1.00 31.65  ? 187 ILE I CD1 1 
ATOM   10344 N  N   . ASN E  1 189 ? -46.301  -51.431 16.009  1.00 23.92  ? 188 ASN I N   1 
ATOM   10345 C  CA  . ASN E  1 189 ? -47.195  -51.851 17.030  1.00 26.73  ? 188 ASN I CA  1 
ATOM   10346 C  C   . ASN E  1 189 ? -46.459  -51.834 18.368  1.00 26.01  ? 188 ASN I C   1 
ATOM   10347 O  O   . ASN E  1 189 ? -45.262  -52.065 18.418  1.00 27.76  ? 188 ASN I O   1 
ATOM   10348 C  CB  . ASN E  1 189 ? -47.744  -53.246 16.733  1.00 28.46  ? 188 ASN I CB  1 
ATOM   10349 C  CG  . ASN E  1 189 ? -48.420  -53.315 15.383  1.00 32.06  ? 188 ASN I CG  1 
ATOM   10350 O  OD1 . ASN E  1 189 ? -49.534  -52.817 15.216  1.00 32.11  ? 188 ASN I OD1 1 
ATOM   10351 N  ND2 . ASN E  1 189 ? -47.735  -53.914 14.421  1.00 29.58  ? 188 ASN I ND2 1 
ATOM   10352 N  N   . PHE E  1 190 ? -47.212  -51.573 19.440  1.00 25.22  ? 189 PHE I N   1 
ATOM   10353 C  CA  . PHE E  1 190 ? -46.721  -51.611 20.801  1.00 25.38  ? 189 PHE I CA  1 
ATOM   10354 C  C   . PHE E  1 190 ? -47.702  -52.414 21.656  1.00 25.93  ? 189 PHE I C   1 
ATOM   10355 O  O   . PHE E  1 190 ? -48.915  -52.308 21.493  1.00 25.68  ? 189 PHE I O   1 
ATOM   10356 C  CB  . PHE E  1 190 ? -46.585  -50.212 21.411  1.00 26.21  ? 189 PHE I CB  1 
ATOM   10357 C  CG  . PHE E  1 190 ? -45.787  -49.219 20.612  1.00 25.43  ? 189 PHE I CG  1 
ATOM   10358 C  CD1 . PHE E  1 190 ? -44.521  -48.848 21.006  1.00 25.75  ? 189 PHE I CD1 1 
ATOM   10359 C  CD2 . PHE E  1 190 ? -46.327  -48.629 19.484  1.00 26.94  ? 189 PHE I CD2 1 
ATOM   10360 C  CE1 . PHE E  1 190 ? -43.788  -47.934 20.272  1.00 28.92  ? 189 PHE I CE1 1 
ATOM   10361 C  CE2 . PHE E  1 190 ? -45.604  -47.695 18.764  1.00 26.69  ? 189 PHE I CE2 1 
ATOM   10362 C  CZ  . PHE E  1 190 ? -44.336  -47.350 19.154  1.00 26.95  ? 189 PHE I CZ  1 
ATOM   10363 N  N   . GLU E  1 191 ? -47.169  -53.206 22.589  1.00 26.25  ? 190 GLU I N   1 
ATOM   10364 C  CA  . GLU E  1 191 ? -47.988  -53.925 23.523  1.00 27.26  ? 190 GLU I CA  1 
ATOM   10365 C  C   . GLU E  1 191 ? -47.295  -53.969 24.884  1.00 28.51  ? 190 GLU I C   1 
ATOM   10366 O  O   . GLU E  1 191 ? -46.090  -54.173 24.970  1.00 29.30  ? 190 GLU I O   1 
ATOM   10367 C  CB  . GLU E  1 191 ? -48.285  -55.332 23.015  1.00 33.82  ? 190 GLU I CB  1 
ATOM   10368 C  CG  . GLU E  1 191 ? -49.335  -56.030 23.847  1.00 41.01  ? 190 GLU I CG  1 
ATOM   10369 C  CD  . GLU E  1 191 ? -49.813  -57.348 23.263  1.00 50.84  ? 190 GLU I CD  1 
ATOM   10370 O  OE1 . GLU E  1 191 ? -48.956  -58.134 22.805  1.00 50.71  ? 190 GLU I OE1 1 
ATOM   10371 O  OE2 . GLU E  1 191 ? -51.041  -57.588 23.276  1.00 58.82  ? 190 GLU I OE2 1 
ATOM   10372 N  N   . GLN E  1 192 ? -48.090  -53.772 25.938  1.00 25.73  ? 191 GLN I N   1 
ATOM   10373 C  CA  . GLN E  1 192 ? -47.627  -53.776 27.309  1.00 26.83  ? 191 GLN I CA  1 
ATOM   10374 C  C   . GLN E  1 192 ? -48.697  -54.480 28.137  1.00 29.47  ? 191 GLN I C   1 
ATOM   10375 O  O   . GLN E  1 192 ? -49.753  -53.938 28.360  1.00 32.30  ? 191 GLN I O   1 
ATOM   10376 C  CB  . GLN E  1 192 ? -47.368  -52.347 27.788  1.00 25.08  ? 191 GLN I CB  1 
ATOM   10377 C  CG  . GLN E  1 192 ? -46.696  -52.280 29.153  1.00 25.40  ? 191 GLN I CG  1 
ATOM   10378 C  CD  . GLN E  1 192 ? -46.498  -50.867 29.634  1.00 26.42  ? 191 GLN I CD  1 
ATOM   10379 O  OE1 . GLN E  1 192 ? -47.204  -49.949 29.210  1.00 25.22  ? 191 GLN I OE1 1 
ATOM   10380 N  NE2 . GLN E  1 192 ? -45.549  -50.675 30.542  1.00 25.27  ? 191 GLN I NE2 1 
ATOM   10381 N  N   . LYS E  1 193 ? -48.392  -55.702 28.554  1.00 34.85  ? 192 LYS I N   1 
ATOM   10382 C  CA  . LYS E  1 193 ? -49.331  -56.598 29.216  1.00 41.26  ? 192 LYS I CA  1 
ATOM   10383 C  C   . LYS E  1 193 ? -49.627  -56.074 30.629  1.00 35.05  ? 192 LYS I C   1 
ATOM   10384 O  O   . LYS E  1 193 ? -50.752  -56.127 31.079  1.00 37.51  ? 192 LYS I O   1 
ATOM   10385 C  CB  . LYS E  1 193 ? -48.749  -58.020 29.248  1.00 50.47  ? 192 LYS I CB  1 
ATOM   10386 C  CG  . LYS E  1 193 ? -48.374  -58.604 27.887  1.00 59.90  ? 192 LYS I CG  1 
ATOM   10387 C  CD  . LYS E  1 193 ? -46.956  -59.193 27.796  1.00 72.69  ? 192 LYS I CD  1 
ATOM   10388 C  CE  . LYS E  1 193 ? -45.828  -58.170 27.846  1.00 78.74  ? 192 LYS I CE  1 
ATOM   10389 N  NZ  . LYS E  1 193 ? -45.788  -57.271 26.661  1.00 74.27  ? 192 LYS I NZ  1 
ATOM   10390 N  N   . GLU E  1 194 ? -48.606  -55.574 31.325  1.00 31.76  ? 193 GLU I N   1 
ATOM   10391 C  CA  . GLU E  1 194 ? -48.816  -54.973 32.635  1.00 35.62  ? 193 GLU I CA  1 
ATOM   10392 C  C   . GLU E  1 194 ? -48.138  -53.610 32.688  1.00 28.72  ? 193 GLU I C   1 
ATOM   10393 O  O   . GLU E  1 194 ? -47.118  -53.375 32.028  1.00 27.92  ? 193 GLU I O   1 
ATOM   10394 C  CB  . GLU E  1 194 ? -48.311  -55.831 33.802  1.00 44.03  ? 193 GLU I CB  1 
ATOM   10395 C  CG  . GLU E  1 194 ? -47.137  -56.722 33.466  1.00 51.67  ? 193 GLU I CG  1 
ATOM   10396 C  CD  . GLU E  1 194 ? -47.536  -58.147 33.143  1.00 54.03  ? 193 GLU I CD  1 
ATOM   10397 O  OE1 . GLU E  1 194 ? -48.701  -58.505 33.406  1.00 57.67  ? 193 GLU I OE1 1 
ATOM   10398 O  OE2 . GLU E  1 194 ? -46.678  -58.893 32.634  1.00 71.56  ? 193 GLU I OE2 1 
ATOM   10399 N  N   . SER E  1 195 ? -48.706  -52.739 33.524  1.00 27.90  ? 194 SER I N   1 
ATOM   10400 C  CA  . SER E  1 195 ? -48.352  -51.329 33.537  1.00 26.69  ? 194 SER I CA  1 
ATOM   10401 C  C   . SER E  1 195 ? -46.902  -51.149 33.988  1.00 26.10  ? 194 SER I C   1 
ATOM   10402 O  O   . SER E  1 195 ? -46.267  -50.134 33.689  1.00 26.83  ? 194 SER I O   1 
ATOM   10403 C  CB  . SER E  1 195 ? -49.307  -50.540 34.394  1.00 28.66  ? 194 SER I CB  1 
ATOM   10404 O  OG  . SER E  1 195 ? -49.310  -50.991 35.738  1.00 31.60  ? 194 SER I OG  1 
ATOM   10405 N  N   . ASN E  1 196 ? -46.378  -52.117 34.747  1.00 26.07  ? 195 ASN I N   1 
ATOM   10406 C  CA  . ASN E  1 196 ? -45.009  -51.998 35.220  1.00 26.81  ? 195 ASN I CA  1 
ATOM   10407 C  C   . ASN E  1 196 ? -44.113  -53.030 34.527  1.00 30.66  ? 195 ASN I C   1 
ATOM   10408 O  O   . ASN E  1 196 ? -43.038  -53.319 35.011  1.00 33.83  ? 195 ASN I O   1 
ATOM   10409 C  CB  . ASN E  1 196 ? -44.935  -52.093 36.744  1.00 28.27  ? 195 ASN I CB  1 
ATOM   10410 C  CG  . ASN E  1 196 ? -45.320  -53.454 37.287  1.00 28.99  ? 195 ASN I CG  1 
ATOM   10411 O  OD1 . ASN E  1 196 ? -46.149  -54.156 36.704  1.00 28.12  ? 195 ASN I OD1 1 
ATOM   10412 N  ND2 . ASN E  1 196 ? -44.729  -53.819 38.421  1.00 30.85  ? 195 ASN I ND2 1 
ATOM   10413 N  N   . GLY E  1 197 ? -44.590  -53.599 33.415  1.00 30.52  ? 196 GLY I N   1 
ATOM   10414 C  CA  . GLY E  1 197 ? -43.854  -54.558 32.620  1.00 29.72  ? 196 GLY I CA  1 
ATOM   10415 C  C   . GLY E  1 197 ? -43.266  -53.892 31.374  1.00 31.61  ? 196 GLY I C   1 
ATOM   10416 O  O   . GLY E  1 197 ? -43.494  -52.705 31.111  1.00 28.47  ? 196 GLY I O   1 
ATOM   10417 N  N   . PRO E  1 198 ? -42.490  -54.644 30.572  1.00 31.69  ? 197 PRO I N   1 
ATOM   10418 C  CA  . PRO E  1 198 ? -41.852  -54.086 29.385  1.00 31.38  ? 197 PRO I CA  1 
ATOM   10419 C  C   . PRO E  1 198 ? -42.844  -53.829 28.239  1.00 28.08  ? 197 PRO I C   1 
ATOM   10420 O  O   . PRO E  1 198 ? -43.953  -54.404 28.200  1.00 28.37  ? 197 PRO I O   1 
ATOM   10421 C  CB  . PRO E  1 198 ? -40.801  -55.145 29.010  1.00 32.73  ? 197 PRO I CB  1 
ATOM   10422 C  CG  . PRO E  1 198 ? -41.325  -56.441 29.597  1.00 37.92  ? 197 PRO I CG  1 
ATOM   10423 C  CD  . PRO E  1 198 ? -42.192  -56.071 30.782  1.00 34.80  ? 197 PRO I CD  1 
ATOM   10424 N  N   . VAL E  1 199 ? -42.434  -52.960 27.310  1.00 28.86  ? 198 VAL I N   1 
ATOM   10425 C  CA  . VAL E  1 199 ? -43.198  -52.730 26.084  1.00 27.77  ? 198 VAL I CA  1 
ATOM   10426 C  C   . VAL E  1 199 ? -42.572  -53.519 24.928  1.00 28.25  ? 198 VAL I C   1 
ATOM   10427 O  O   . VAL E  1 199 ? -41.388  -53.314 24.621  1.00 27.30  ? 198 VAL I O   1 
ATOM   10428 C  CB  . VAL E  1 199 ? -43.251  -51.234 25.736  1.00 27.73  ? 198 VAL I CB  1 
ATOM   10429 C  CG1 . VAL E  1 199 ? -44.049  -50.991 24.472  1.00 26.20  ? 198 VAL I CG1 1 
ATOM   10430 C  CG2 . VAL E  1 199 ? -43.776  -50.391 26.893  1.00 29.27  ? 198 VAL I CG2 1 
ATOM   10431 N  N   . LYS E  1 200 ? -43.383  -54.347 24.263  1.00 26.35  ? 199 LYS I N   1 
ATOM   10432 C  CA  . LYS E  1 200 ? -42.986  -54.990 23.034  1.00 30.55  ? 199 LYS I CA  1 
ATOM   10433 C  C   . LYS E  1 200 ? -43.313  -54.055 21.871  1.00 30.68  ? 199 LYS I C   1 
ATOM   10434 O  O   . LYS E  1 200 ? -44.419  -53.494 21.840  1.00 29.14  ? 199 LYS I O   1 
ATOM   10435 C  CB  . LYS E  1 200 ? -43.732  -56.306 22.816  1.00 34.51  ? 199 LYS I CB  1 
ATOM   10436 C  CG  . LYS E  1 200 ? -43.409  -57.429 23.787  1.00 46.19  ? 199 LYS I CG  1 
ATOM   10437 C  CD  . LYS E  1 200 ? -43.986  -58.771 23.314  1.00 55.41  ? 199 LYS I CD  1 
ATOM   10438 C  CE  . LYS E  1 200 ? -43.512  -59.963 24.123  1.00 63.61  ? 199 LYS I CE  1 
ATOM   10439 N  NZ  . LYS E  1 200 ? -44.268  -60.090 25.392  1.00 69.75  ? 199 LYS I NZ  1 
ATOM   10440 N  N   . VAL E  1 201 ? -42.367  -53.923 20.936  1.00 28.68  ? 200 VAL I N   1 
ATOM   10441 C  CA  . VAL E  1 201 ? -42.434  -53.007 19.797  1.00 30.26  ? 200 VAL I CA  1 
ATOM   10442 C  C   . VAL E  1 201 ? -42.122  -53.804 18.527  1.00 32.04  ? 200 VAL I C   1 
ATOM   10443 O  O   . VAL E  1 201 ? -41.036  -54.360 18.430  1.00 34.09  ? 200 VAL I O   1 
ATOM   10444 C  CB  . VAL E  1 201 ? -41.442  -51.841 19.940  1.00 29.21  ? 200 VAL I CB  1 
ATOM   10445 C  CG1 . VAL E  1 201 ? -41.586  -50.828 18.817  1.00 29.92  ? 200 VAL I CG1 1 
ATOM   10446 C  CG2 . VAL E  1 201 ? -41.530  -51.148 21.285  1.00 30.58  ? 200 VAL I CG2 1 
ATOM   10447 N  N   . TRP E  1 202 ? -43.039  -53.835 17.553  1.00 29.81  ? 201 TRP I N   1 
ATOM   10448 C  CA  . TRP E  1 202 ? -42.791  -54.587 16.333  1.00 30.05  ? 201 TRP I CA  1 
ATOM   10449 C  C   . TRP E  1 202 ? -43.579  -54.022 15.151  1.00 29.62  ? 201 TRP I C   1 
ATOM   10450 O  O   . TRP E  1 202 ? -44.623  -53.441 15.311  1.00 28.41  ? 201 TRP I O   1 
ATOM   10451 C  CB  . TRP E  1 202 ? -43.128  -56.066 16.558  1.00 32.63  ? 201 TRP I CB  1 
ATOM   10452 C  CG  . TRP E  1 202 ? -44.591  -56.360 16.534  1.00 32.15  ? 201 TRP I CG  1 
ATOM   10453 C  CD1 . TRP E  1 202 ? -45.311  -56.822 15.470  1.00 33.07  ? 201 TRP I CD1 1 
ATOM   10454 C  CD2 . TRP E  1 202 ? -45.529  -56.191 17.615  1.00 31.75  ? 201 TRP I CD2 1 
ATOM   10455 N  NE1 . TRP E  1 202 ? -46.627  -56.969 15.818  1.00 34.81  ? 201 TRP I NE1 1 
ATOM   10456 C  CE2 . TRP E  1 202 ? -46.790  -56.593 17.128  1.00 33.97  ? 201 TRP I CE2 1 
ATOM   10457 C  CE3 . TRP E  1 202 ? -45.428  -55.754 18.937  1.00 32.49  ? 201 TRP I CE3 1 
ATOM   10458 C  CZ2 . TRP E  1 202 ? -47.938  -56.564 17.916  1.00 36.83  ? 201 TRP I CZ2 1 
ATOM   10459 C  CZ3 . TRP E  1 202 ? -46.564  -55.711 19.715  1.00 36.04  ? 201 TRP I CZ3 1 
ATOM   10460 C  CH2 . TRP E  1 202 ? -47.804  -56.110 19.209  1.00 37.56  ? 201 TRP I CH2 1 
ATOM   10461 N  N   . GLY E  1 203 ? -43.063  -54.259 13.946  1.00 28.95  ? 202 GLY I N   1 
ATOM   10462 C  CA  . GLY E  1 203 ? -43.705  -53.859 12.722  1.00 28.35  ? 202 GLY I CA  1 
ATOM   10463 C  C   . GLY E  1 203 ? -42.683  -53.772 11.616  1.00 28.95  ? 202 GLY I C   1 
ATOM   10464 O  O   . GLY E  1 203 ? -41.678  -54.453 11.673  1.00 32.92  ? 202 GLY I O   1 
ATOM   10465 N  N   . SER E  1 204 ? -42.932  -52.932 10.616  1.00 28.82  ? 203 SER I N   1 
ATOM   10466 C  CA  . SER E  1 204 ? -41.956  -52.747 9.564   1.00 31.22  ? 203 SER I CA  1 
ATOM   10467 C  C   . SER E  1 204 ? -42.079  -51.365 8.945   1.00 30.40  ? 203 SER I C   1 
ATOM   10468 O  O   . SER E  1 204 ? -43.130  -50.715 9.025   1.00 28.68  ? 203 SER I O   1 
ATOM   10469 C  CB  . SER E  1 204 ? -42.048  -53.815 8.508   1.00 37.63  ? 203 SER I CB  1 
ATOM   10470 O  OG  . SER E  1 204 ? -43.381  -53.990 8.094   1.00 39.58  ? 203 SER I OG  1 
ATOM   10471 N  N   . ILE E  1 205 ? -40.940  -50.926 8.410   1.00 28.66  ? 204 ILE I N   1 
ATOM   10472 C  CA  . ILE E  1 205 ? -40.749  -49.661 7.749   1.00 31.43  ? 204 ILE I CA  1 
ATOM   10473 C  C   . ILE E  1 205 ? -40.151  -49.977 6.374   1.00 34.69  ? 204 ILE I C   1 
ATOM   10474 O  O   . ILE E  1 205 ? -39.226  -50.809 6.287   1.00 35.51  ? 204 ILE I O   1 
ATOM   10475 C  CB  . ILE E  1 205 ? -39.826  -48.766 8.591   1.00 30.99  ? 204 ILE I CB  1 
ATOM   10476 C  CG1 . ILE E  1 205 ? -40.279  -48.737 10.057  1.00 33.34  ? 204 ILE I CG1 1 
ATOM   10477 C  CG2 . ILE E  1 205 ? -39.725  -47.373 7.994   1.00 30.52  ? 204 ILE I CG2 1 
ATOM   10478 C  CD1 . ILE E  1 205 ? -39.369  -47.960 10.985  1.00 32.06  ? 204 ILE I CD1 1 
ATOM   10479 N  N   . LYS E  1 206 ? -40.678  -49.339 5.327   1.00 32.18  ? 205 LYS I N   1 
ATOM   10480 C  CA  . LYS E  1 206 ? -40.160  -49.490 3.963   1.00 34.01  ? 205 LYS I CA  1 
ATOM   10481 C  C   . LYS E  1 206 ? -39.710  -48.118 3.447   1.00 33.99  ? 205 LYS I C   1 
ATOM   10482 O  O   . LYS E  1 206 ? -39.994  -47.091 4.075   1.00 30.53  ? 205 LYS I O   1 
ATOM   10483 C  CB  . LYS E  1 206 ? -41.198  -50.191 3.089   1.00 36.25  ? 205 LYS I CB  1 
ATOM   10484 C  CG  . LYS E  1 206 ? -42.518  -49.470 2.937   1.00 43.11  ? 205 LYS I CG  1 
ATOM   10485 C  CD  . LYS E  1 206 ? -43.518  -50.247 2.116   1.00 46.62  ? 205 LYS I CD  1 
ATOM   10486 C  CE  . LYS E  1 206 ? -44.499  -49.341 1.405   1.00 48.99  ? 205 LYS I CE  1 
ATOM   10487 N  NZ  . LYS E  1 206 ? -45.800  -50.018 1.218   1.00 52.85  ? 205 LYS I NZ  1 
ATOM   10488 N  N   . GLY E  1 207 ? -38.932  -48.126 2.351   1.00 30.43  ? 206 GLY I N   1 
ATOM   10489 C  CA  . GLY E  1 207 ? -38.469  -46.910 1.681   1.00 30.09  ? 206 GLY I CA  1 
ATOM   10490 C  C   . GLY E  1 207 ? -37.193  -46.375 2.280   1.00 29.03  ? 206 GLY I C   1 
ATOM   10491 O  O   . GLY E  1 207 ? -36.821  -45.231 2.051   1.00 31.04  ? 206 GLY I O   1 
ATOM   10492 N  N   . LEU E  1 208 ? -36.502  -47.216 3.056   1.00 31.62  ? 207 LEU I N   1 
ATOM   10493 C  CA  . LEU E  1 208 ? -35.260  -46.819 3.703   1.00 32.05  ? 207 LEU I CA  1 
ATOM   10494 C  C   . LEU E  1 208 ? -34.072  -47.226 2.822   1.00 34.91  ? 207 LEU I C   1 
ATOM   10495 O  O   . LEU E  1 208 ? -34.178  -48.142 2.026   1.00 34.42  ? 207 LEU I O   1 
ATOM   10496 C  CB  . LEU E  1 208 ? -35.156  -47.514 5.061   1.00 32.67  ? 207 LEU I CB  1 
ATOM   10497 C  CG  . LEU E  1 208 ? -36.164  -47.074 6.120   1.00 32.52  ? 207 LEU I CG  1 
ATOM   10498 C  CD1 . LEU E  1 208 ? -36.219  -48.082 7.261   1.00 35.13  ? 207 LEU I CD1 1 
ATOM   10499 C  CD2 . LEU E  1 208 ? -35.809  -45.703 6.651   1.00 32.75  ? 207 LEU I CD2 1 
ATOM   10500 N  N   . THR E  1 209 ? -32.953  -46.522 2.974   1.00 35.94  ? 208 THR I N   1 
ATOM   10501 C  CA  . THR E  1 209 ? -31.676  -47.001 2.472   1.00 39.23  ? 208 THR I CA  1 
ATOM   10502 C  C   . THR E  1 209 ? -31.232  -48.176 3.348   1.00 39.28  ? 208 THR I C   1 
ATOM   10503 O  O   . THR E  1 209 ? -31.436  -48.190 4.569   1.00 33.55  ? 208 THR I O   1 
ATOM   10504 C  CB  . THR E  1 209 ? -30.629  -45.886 2.465   1.00 39.13  ? 208 THR I CB  1 
ATOM   10505 O  OG1 . THR E  1 209 ? -30.559  -45.362 3.791   1.00 38.76  ? 208 THR I OG1 1 
ATOM   10506 C  CG2 . THR E  1 209 ? -30.969  -44.781 1.490   1.00 38.97  ? 208 THR I CG2 1 
ATOM   10507 N  N   . GLU E  1 210 ? -30.638  -49.179 2.711   1.00 37.81  ? 209 GLU I N   1 
ATOM   10508 C  CA  . GLU E  1 210 ? -30.094  -50.336 3.420   1.00 39.68  ? 209 GLU I CA  1 
ATOM   10509 C  C   . GLU E  1 210 ? -29.128  -49.860 4.508   1.00 36.03  ? 209 GLU I C   1 
ATOM   10510 O  O   . GLU E  1 210 ? -28.353  -48.938 4.297   1.00 39.20  ? 209 GLU I O   1 
ATOM   10511 C  CB  . GLU E  1 210 ? -29.396  -51.245 2.411   1.00 45.18  ? 209 GLU I CB  1 
ATOM   10512 C  CG  . GLU E  1 210 ? -28.571  -52.341 3.044   1.00 47.18  ? 209 GLU I CG  1 
ATOM   10513 C  CD  . GLU E  1 210 ? -27.814  -53.161 2.015   1.00 52.79  ? 209 GLU I CD  1 
ATOM   10514 O  OE1 . GLU E  1 210 ? -27.354  -54.257 2.377   1.00 51.33  ? 209 GLU I OE1 1 
ATOM   10515 O  OE2 . GLU E  1 210 ? -27.696  -52.696 0.852   1.00 51.36  ? 209 GLU I OE2 1 
ATOM   10516 N  N   . GLY E  1 211 ? -29.208  -50.482 5.683   1.00 35.76  ? 210 GLY I N   1 
ATOM   10517 C  CA  . GLY E  1 211 ? -28.352  -50.127 6.826   1.00 36.38  ? 210 GLY I CA  1 
ATOM   10518 C  C   . GLY E  1 211 ? -29.135  -49.644 8.044   1.00 37.67  ? 210 GLY I C   1 
ATOM   10519 O  O   . GLY E  1 211 ? -30.350  -49.839 8.144   1.00 33.48  ? 210 GLY I O   1 
ATOM   10520 N  N   . LEU E  1 212 ? -28.421  -48.992 8.971   1.00 40.13  ? 211 LEU I N   1 
ATOM   10521 C  CA  . LEU E  1 212 ? -28.940  -48.681 10.299  1.00 40.91  ? 211 LEU I CA  1 
ATOM   10522 C  C   . LEU E  1 212 ? -29.623  -47.313 10.283  1.00 40.51  ? 211 LEU I C   1 
ATOM   10523 O  O   . LEU E  1 212 ? -29.117  -46.368 9.680   1.00 38.74  ? 211 LEU I O   1 
ATOM   10524 C  CB  . LEU E  1 212 ? -27.803  -48.678 11.325  1.00 45.86  ? 211 LEU I CB  1 
ATOM   10525 C  CG  . LEU E  1 212 ? -27.184  -50.027 11.696  1.00 48.96  ? 211 LEU I CG  1 
ATOM   10526 C  CD1 . LEU E  1 212 ? -26.387  -49.906 12.983  1.00 51.82  ? 211 LEU I CD1 1 
ATOM   10527 C  CD2 . LEU E  1 212 ? -28.226  -51.115 11.850  1.00 52.63  ? 211 LEU I CD2 1 
ATOM   10528 N  N   . HIS E  1 213 ? -30.759  -47.220 10.986  1.00 34.43  ? 212 HIS I N   1 
ATOM   10529 C  CA  . HIS E  1 213 ? -31.523  -45.969 11.077  1.00 32.65  ? 212 HIS I CA  1 
ATOM   10530 C  C   . HIS E  1 213 ? -31.939  -45.724 12.534  1.00 30.69  ? 212 HIS I C   1 
ATOM   10531 O  O   . HIS E  1 213 ? -32.509  -46.602 13.170  1.00 31.18  ? 212 HIS I O   1 
ATOM   10532 C  CB  . HIS E  1 213 ? -32.724  -46.018 10.135  1.00 31.20  ? 212 HIS I CB  1 
ATOM   10533 C  CG  . HIS E  1 213 ? -32.354  -46.019 8.690   1.00 33.01  ? 212 HIS I CG  1 
ATOM   10534 N  ND1 . HIS E  1 213 ? -32.042  -44.853 8.000   1.00 35.40  ? 212 HIS I ND1 1 
ATOM   10535 C  CD2 . HIS E  1 213 ? -32.244  -47.025 7.797   1.00 34.68  ? 212 HIS I CD2 1 
ATOM   10536 C  CE1 . HIS E  1 213 ? -31.747  -45.149 6.750   1.00 34.59  ? 212 HIS I CE1 1 
ATOM   10537 N  NE2 . HIS E  1 213 ? -31.876  -46.473 6.596   1.00 33.60  ? 212 HIS I NE2 1 
ATOM   10538 N  N   . GLY E  1 214 ? -31.600  -44.544 13.058  1.00 29.36  ? 213 GLY I N   1 
ATOM   10539 C  CA  . GLY E  1 214 ? -31.995  -44.168 14.399  1.00 33.03  ? 213 GLY I CA  1 
ATOM   10540 C  C   . GLY E  1 214 ? -33.515  -44.216 14.538  1.00 31.93  ? 213 GLY I C   1 
ATOM   10541 O  O   . GLY E  1 214 ? -34.249  -43.879 13.604  1.00 28.69  ? 213 GLY I O   1 
ATOM   10542 N  N   . PHE E  1 215 ? -33.968  -44.623 15.717  1.00 29.96  ? 214 PHE I N   1 
ATOM   10543 C  CA  . PHE E  1 215 ? -35.355  -44.926 16.009  1.00 29.17  ? 214 PHE I CA  1 
ATOM   10544 C  C   . PHE E  1 215 ? -35.642  -44.425 17.420  1.00 28.27  ? 214 PHE I C   1 
ATOM   10545 O  O   . PHE E  1 215 ? -35.140  -44.994 18.380  1.00 27.82  ? 214 PHE I O   1 
ATOM   10546 C  CB  . PHE E  1 215 ? -35.568  -46.434 15.876  1.00 28.58  ? 214 PHE I CB  1 
ATOM   10547 C  CG  . PHE E  1 215 ? -36.985  -46.947 15.851  1.00 29.37  ? 214 PHE I CG  1 
ATOM   10548 C  CD1 . PHE E  1 215 ? -37.889  -46.536 14.880  1.00 30.44  ? 214 PHE I CD1 1 
ATOM   10549 C  CD2 . PHE E  1 215 ? -37.402  -47.899 16.769  1.00 30.49  ? 214 PHE I CD2 1 
ATOM   10550 C  CE1 . PHE E  1 215 ? -39.163  -47.096 14.820  1.00 30.22  ? 214 PHE I CE1 1 
ATOM   10551 C  CE2 . PHE E  1 215 ? -38.686  -48.428 16.722  1.00 30.94  ? 214 PHE I CE2 1 
ATOM   10552 C  CZ  . PHE E  1 215 ? -39.562  -48.025 15.744  1.00 28.41  ? 214 PHE I CZ  1 
ATOM   10553 N  N   . HIS E  1 216 ? -36.390  -43.320 17.518  1.00 28.68  ? 215 HIS I N   1 
ATOM   10554 C  CA  . HIS E  1 216 ? -36.604  -42.642 18.776  1.00 30.32  ? 215 HIS I CA  1 
ATOM   10555 C  C   . HIS E  1 216 ? -38.057  -42.204 18.952  1.00 28.96  ? 215 HIS I C   1 
ATOM   10556 O  O   . HIS E  1 216 ? -38.761  -41.928 17.968  1.00 25.57  ? 215 HIS I O   1 
ATOM   10557 C  CB  . HIS E  1 216 ? -35.797  -41.350 18.867  1.00 33.91  ? 215 HIS I CB  1 
ATOM   10558 C  CG  . HIS E  1 216 ? -34.381  -41.466 18.439  1.00 38.86  ? 215 HIS I CG  1 
ATOM   10559 N  ND1 . HIS E  1 216 ? -33.775  -40.511 17.639  1.00 38.53  ? 215 HIS I ND1 1 
ATOM   10560 C  CD2 . HIS E  1 216 ? -33.441  -42.392 18.718  1.00 38.20  ? 215 HIS I CD2 1 
ATOM   10561 C  CE1 . HIS E  1 216 ? -32.526  -40.867 17.424  1.00 38.45  ? 215 HIS I CE1 1 
ATOM   10562 N  NE2 . HIS E  1 216 ? -32.302  -42.009 18.068  1.00 37.16  ? 215 HIS I NE2 1 
ATOM   10563 N  N   . VAL E  1 217 ? -38.434  -42.033 20.223  1.00 28.13  ? 216 VAL I N   1 
ATOM   10564 C  CA  . VAL E  1 217 ? -39.621  -41.308 20.582  1.00 28.89  ? 216 VAL I CA  1 
ATOM   10565 C  C   . VAL E  1 217 ? -39.208  -39.884 20.929  1.00 28.32  ? 216 VAL I C   1 
ATOM   10566 O  O   . VAL E  1 217 ? -38.354  -39.670 21.783  1.00 28.97  ? 216 VAL I O   1 
ATOM   10567 C  CB  . VAL E  1 217 ? -40.365  -41.971 21.750  1.00 28.50  ? 216 VAL I CB  1 
ATOM   10568 C  CG1 . VAL E  1 217 ? -41.641  -41.224 22.120  1.00 27.05  ? 216 VAL I CG1 1 
ATOM   10569 C  CG2 . VAL E  1 217 ? -40.654  -43.424 21.436  1.00 29.35  ? 216 VAL I CG2 1 
ATOM   10570 N  N   . HIS E  1 218 ? -39.842  -38.938 20.238  1.00 25.28  ? 217 HIS I N   1 
ATOM   10571 C  CA  . HIS E  1 218 ? -39.671  -37.530 20.440  1.00 24.91  ? 217 HIS I CA  1 
ATOM   10572 C  C   . HIS E  1 218 ? -40.820  -37.020 21.309  1.00 25.06  ? 217 HIS I C   1 
ATOM   10573 O  O   . HIS E  1 218 ? -41.894  -37.624 21.374  1.00 26.26  ? 217 HIS I O   1 
ATOM   10574 C  CB  . HIS E  1 218 ? -39.564  -36.822 19.085  1.00 26.83  ? 217 HIS I CB  1 
ATOM   10575 C  CG  . HIS E  1 218 ? -38.236  -37.002 18.413  1.00 28.66  ? 217 HIS I CG  1 
ATOM   10576 N  ND1 . HIS E  1 218 ? -37.400  -35.936 18.174  1.00 29.83  ? 217 HIS I ND1 1 
ATOM   10577 C  CD2 . HIS E  1 218 ? -37.585  -38.101 17.952  1.00 28.60  ? 217 HIS I CD2 1 
ATOM   10578 C  CE1 . HIS E  1 218 ? -36.310  -36.359 17.558  1.00 29.80  ? 217 HIS I CE1 1 
ATOM   10579 N  NE2 . HIS E  1 218 ? -36.386  -37.684 17.414  1.00 30.67  ? 217 HIS I NE2 1 
ATOM   10580 N  N   . GLU E  1 219 ? -40.582  -35.894 21.967  1.00 25.41  ? 218 GLU I N   1 
ATOM   10581 C  CA  . GLU E  1 219 ? -41.413  -35.443 23.076  1.00 28.33  ? 218 GLU I CA  1 
ATOM   10582 C  C   . GLU E  1 219 ? -42.862  -35.130 22.660  1.00 25.18  ? 218 GLU I C   1 
ATOM   10583 O  O   . GLU E  1 219 ? -43.798  -35.472 23.377  1.00 25.46  ? 218 GLU I O   1 
ATOM   10584 C  CB  . GLU E  1 219 ? -40.811  -34.192 23.711  1.00 30.70  ? 218 GLU I CB  1 
ATOM   10585 C  CG  . GLU E  1 219 ? -41.488  -33.864 25.013  1.00 32.70  ? 218 GLU I CG  1 
ATOM   10586 C  CD  . GLU E  1 219 ? -40.849  -32.734 25.783  1.00 36.77  ? 218 GLU I CD  1 
ATOM   10587 O  OE1 . GLU E  1 219 ? -41.455  -32.310 26.772  1.00 40.13  ? 218 GLU I OE1 1 
ATOM   10588 O  OE2 . GLU E  1 219 ? -39.770  -32.282 25.373  1.00 37.03  ? 218 GLU I OE2 1 
ATOM   10589 N  N   . PHE E  1 220 ? -43.047  -34.441 21.536  1.00 26.61  ? 219 PHE I N   1 
ATOM   10590 C  CA  . PHE E  1 220 ? -44.365  -33.910 21.191  1.00 27.28  ? 219 PHE I CA  1 
ATOM   10591 C  C   . PHE E  1 220 ? -44.988  -34.696 20.045  1.00 28.35  ? 219 PHE I C   1 
ATOM   10592 O  O   . PHE E  1 220 ? -44.326  -34.943 19.029  1.00 29.08  ? 219 PHE I O   1 
ATOM   10593 C  CB  . PHE E  1 220 ? -44.269  -32.436 20.796  1.00 29.29  ? 219 PHE I CB  1 
ATOM   10594 C  CG  . PHE E  1 220 ? -43.624  -31.605 21.862  1.00 29.18  ? 219 PHE I CG  1 
ATOM   10595 C  CD1 . PHE E  1 220 ? -44.165  -31.574 23.135  1.00 30.79  ? 219 PHE I CD1 1 
ATOM   10596 C  CD2 . PHE E  1 220 ? -42.456  -30.900 21.615  1.00 30.74  ? 219 PHE I CD2 1 
ATOM   10597 C  CE1 . PHE E  1 220 ? -43.555  -30.843 24.142  1.00 31.27  ? 219 PHE I CE1 1 
ATOM   10598 C  CE2 . PHE E  1 220 ? -41.848  -30.169 22.627  1.00 30.44  ? 219 PHE I CE2 1 
ATOM   10599 C  CZ  . PHE E  1 220 ? -42.403  -30.140 23.884  1.00 30.40  ? 219 PHE I CZ  1 
ATOM   10600 N  N   . GLY E  1 221 ? -46.286  -34.983 20.190  1.00 24.76  ? 220 GLY I N   1 
ATOM   10601 C  CA  . GLY E  1 221 ? -47.094  -35.589 19.138  1.00 26.53  ? 220 GLY I CA  1 
ATOM   10602 C  C   . GLY E  1 221 ? -47.681  -34.520 18.228  1.00 26.01  ? 220 GLY I C   1 
ATOM   10603 O  O   . GLY E  1 221 ? -48.887  -34.486 17.979  1.00 26.35  ? 220 GLY I O   1 
ATOM   10604 N  N   . ASP E  1 222 ? -46.804  -33.621 17.780  1.00 27.26  ? 221 ASP I N   1 
ATOM   10605 C  CA  . ASP E  1 222 ? -47.126  -32.412 17.038  1.00 25.91  ? 221 ASP I CA  1 
ATOM   10606 C  C   . ASP E  1 222 ? -46.550  -32.548 15.636  1.00 25.35  ? 221 ASP I C   1 
ATOM   10607 O  O   . ASP E  1 222 ? -45.339  -32.455 15.437  1.00 24.92  ? 221 ASP I O   1 
ATOM   10608 C  CB  . ASP E  1 222 ? -46.559  -31.162 17.715  1.00 27.72  ? 221 ASP I CB  1 
ATOM   10609 C  CG  . ASP E  1 222 ? -47.005  -29.854 17.063  1.00 29.44  ? 221 ASP I CG  1 
ATOM   10610 O  OD1 . ASP E  1 222 ? -47.057  -28.840 17.777  1.00 33.47  ? 221 ASP I OD1 1 
ATOM   10611 O  OD2 . ASP E  1 222 ? -47.295  -29.866 15.848  1.00 31.04  ? 221 ASP I OD2 1 
ATOM   10612 N  N   . ASN E  1 223 ? -47.447  -32.769 14.684  1.00 26.31  ? 222 ASN I N   1 
ATOM   10613 C  CA  . ASN E  1 223 ? -47.120  -33.002 13.300  1.00 30.97  ? 222 ASN I CA  1 
ATOM   10614 C  C   . ASN E  1 223 ? -47.459  -31.799 12.411  1.00 27.97  ? 222 ASN I C   1 
ATOM   10615 O  O   . ASN E  1 223 ? -47.495  -31.936 11.202  1.00 27.58  ? 222 ASN I O   1 
ATOM   10616 C  CB  . ASN E  1 223 ? -47.894  -34.210 12.787  1.00 37.34  ? 222 ASN I CB  1 
ATOM   10617 C  CG  . ASN E  1 223 ? -46.966  -35.336 12.423  1.00 49.91  ? 222 ASN I CG  1 
ATOM   10618 O  OD1 . ASN E  1 223 ? -46.520  -35.397 11.276  1.00 62.38  ? 222 ASN I OD1 1 
ATOM   10619 N  ND2 . ASN E  1 223 ? -46.653  -36.190 13.394  1.00 50.41  ? 222 ASN I ND2 1 
ATOM   10620 N  N   . THR E  1 224 ? -47.730  -30.644 13.013  1.00 28.79  ? 223 THR I N   1 
ATOM   10621 C  CA  . THR E  1 224 ? -48.172  -29.470 12.263  1.00 32.28  ? 223 THR I CA  1 
ATOM   10622 C  C   . THR E  1 224 ? -47.098  -28.999 11.278  1.00 33.01  ? 223 THR I C   1 
ATOM   10623 O  O   . THR E  1 224 ? -47.445  -28.382 10.286  1.00 32.83  ? 223 THR I O   1 
ATOM   10624 C  CB  . THR E  1 224 ? -48.548  -28.304 13.182  1.00 32.46  ? 223 THR I CB  1 
ATOM   10625 O  OG1 . THR E  1 224 ? -47.435  -27.974 13.998  1.00 31.76  ? 223 THR I OG1 1 
ATOM   10626 C  CG2 . THR E  1 224 ? -49.733  -28.616 14.068  1.00 33.03  ? 223 THR I CG2 1 
ATOM   10627 N  N   . ALA E  1 225 ? -45.820  -29.267 11.578  1.00 33.01  ? 224 ALA I N   1 
ATOM   10628 C  CA  . ALA E  1 225 ? -44.705  -29.020 10.635  1.00 34.17  ? 224 ALA I CA  1 
ATOM   10629 C  C   . ALA E  1 225 ? -44.043  -30.353 10.237  1.00 35.22  ? 224 ALA I C   1 
ATOM   10630 O  O   . ALA E  1 225 ? -42.828  -30.462 10.127  1.00 38.92  ? 224 ALA I O   1 
ATOM   10631 C  CB  . ALA E  1 225 ? -43.720  -28.064 11.263  1.00 32.64  ? 224 ALA I CB  1 
ATOM   10632 N  N   . GLY E  1 226 ? -44.857  -31.379 9.990   1.00 35.06  ? 225 GLY I N   1 
ATOM   10633 C  CA  . GLY E  1 226 ? -44.338  -32.741 9.817   1.00 33.86  ? 225 GLY I CA  1 
ATOM   10634 C  C   . GLY E  1 226 ? -43.514  -33.170 11.027  1.00 32.03  ? 225 GLY I C   1 
ATOM   10635 O  O   . GLY E  1 226 ? -43.875  -32.900 12.167  1.00 30.73  ? 225 GLY I O   1 
ATOM   10636 N  N   . CYS E  1 227 ? -42.368  -33.814 10.788  1.00 32.14  ? 226 CYS I N   1 
ATOM   10637 C  CA  . CYS E  1 227 ? -41.555  -34.388 11.876  1.00 34.11  ? 226 CYS I CA  1 
ATOM   10638 C  C   . CYS E  1 227 ? -40.821  -33.290 12.654  1.00 31.64  ? 226 CYS I C   1 
ATOM   10639 O  O   . CYS E  1 227 ? -40.429  -33.466 13.813  1.00 29.71  ? 226 CYS I O   1 
ATOM   10640 C  CB  . CYS E  1 227 ? -40.602  -35.430 11.307  1.00 36.23  ? 226 CYS I CB  1 
ATOM   10641 S  SG  . CYS E  1 227 ? -41.510  -36.718 10.414  1.00 41.15  ? 226 CYS I SG  1 
ATOM   10642 N  N   . THR E  1 228 ? -40.705  -32.125 12.034  1.00 34.92  ? 227 THR I N   1 
ATOM   10643 C  CA  . THR E  1 228 ? -39.939  -31.022 12.572  1.00 35.91  ? 227 THR I CA  1 
ATOM   10644 C  C   . THR E  1 228 ? -40.538  -30.507 13.887  1.00 35.56  ? 227 THR I C   1 
ATOM   10645 O  O   . THR E  1 228 ? -39.810  -30.026 14.738  1.00 40.50  ? 227 THR I O   1 
ATOM   10646 C  CB  . THR E  1 228 ? -39.869  -29.900 11.535  1.00 41.20  ? 227 THR I CB  1 
ATOM   10647 O  OG1 . THR E  1 228 ? -39.658  -30.495 10.252  1.00 45.70  ? 227 THR I OG1 1 
ATOM   10648 C  CG2 . THR E  1 228 ? -38.781  -28.904 11.848  1.00 44.70  ? 227 THR I CG2 1 
ATOM   10649 N  N   . SER E  1 229 ? -41.868  -30.577 14.044  1.00 30.31  ? 228 SER I N   1 
ATOM   10650 C  CA  . SER E  1 229 ? -42.548  -30.017 15.218  1.00 29.36  ? 228 SER I CA  1 
ATOM   10651 C  C   . SER E  1 229 ? -42.566  -31.011 16.386  1.00 26.17  ? 228 SER I C   1 
ATOM   10652 O  O   . SER E  1 229 ? -43.037  -30.688 17.439  1.00 25.36  ? 228 SER I O   1 
ATOM   10653 C  CB  . SER E  1 229 ? -43.948  -29.547 14.841  1.00 28.23  ? 228 SER I CB  1 
ATOM   10654 O  OG  . SER E  1 229 ? -44.530  -30.423 13.900  1.00 26.39  ? 228 SER I OG  1 
ATOM   10655 N  N   . ALA E  1 230 ? -42.018  -32.220 16.205  1.00 27.74  ? 229 ALA I N   1 
ATOM   10656 C  CA  . ALA E  1 230 ? -42.007  -33.238 17.270  1.00 27.26  ? 229 ALA I CA  1 
ATOM   10657 C  C   . ALA E  1 230 ? -41.074  -32.871 18.435  1.00 28.22  ? 229 ALA I C   1 
ATOM   10658 O  O   . ALA E  1 230 ? -41.145  -33.501 19.506  1.00 24.69  ? 229 ALA I O   1 
ATOM   10659 C  CB  . ALA E  1 230 ? -41.633  -34.584 16.706  1.00 29.23  ? 229 ALA I CB  1 
ATOM   10660 N  N   . GLY E  1 231 ? -40.168  -31.914 18.215  1.00 28.03  ? 230 GLY I N   1 
ATOM   10661 C  CA  . GLY E  1 231 ? -39.276  -31.446 19.242  1.00 29.89  ? 230 GLY I CA  1 
ATOM   10662 C  C   . GLY E  1 231 ? -38.135  -32.427 19.490  1.00 30.74  ? 230 GLY I C   1 
ATOM   10663 O  O   . GLY E  1 231 ? -37.801  -33.244 18.626  1.00 30.25  ? 230 GLY I O   1 
ATOM   10664 N  N   . PRO E  1 232 ? -37.495  -32.366 20.679  1.00 32.85  ? 231 PRO I N   1 
ATOM   10665 C  CA  . PRO E  1 232 ? -36.338  -33.210 20.979  1.00 34.03  ? 231 PRO I CA  1 
ATOM   10666 C  C   . PRO E  1 232 ? -36.779  -34.608 21.427  1.00 32.91  ? 231 PRO I C   1 
ATOM   10667 O  O   . PRO E  1 232 ? -37.974  -34.887 21.510  1.00 28.62  ? 231 PRO I O   1 
ATOM   10668 C  CB  . PRO E  1 232 ? -35.665  -32.440 22.119  1.00 36.19  ? 231 PRO I CB  1 
ATOM   10669 C  CG  . PRO E  1 232 ? -36.838  -31.854 22.871  1.00 37.31  ? 231 PRO I CG  1 
ATOM   10670 C  CD  . PRO E  1 232 ? -37.841  -31.478 21.797  1.00 35.61  ? 231 PRO I CD  1 
ATOM   10671 N  N   . HIS E  1 233 ? -35.801  -35.467 21.698  1.00 32.38  ? 232 HIS I N   1 
ATOM   10672 C  CA  . HIS E  1 233 ? -36.042  -36.788 22.205  1.00 34.24  ? 232 HIS I CA  1 
ATOM   10673 C  C   . HIS E  1 233 ? -36.847  -36.677 23.496  1.00 32.28  ? 232 HIS I C   1 
ATOM   10674 O  O   . HIS E  1 233 ? -36.621  -35.789 24.266  1.00 31.90  ? 232 HIS I O   1 
ATOM   10675 C  CB  . HIS E  1 233 ? -34.713  -37.515 22.424  1.00 37.87  ? 232 HIS I CB  1 
ATOM   10676 C  CG  . HIS E  1 233 ? -34.040  -37.850 21.142  1.00 43.18  ? 232 HIS I CG  1 
ATOM   10677 N  ND1 . HIS E  1 233 ? -32.898  -38.617 21.082  1.00 47.46  ? 232 HIS I ND1 1 
ATOM   10678 C  CD2 . HIS E  1 233 ? -34.388  -37.562 19.866  1.00 48.61  ? 232 HIS I CD2 1 
ATOM   10679 C  CE1 . HIS E  1 233 ? -32.540  -38.761 19.814  1.00 50.77  ? 232 HIS I CE1 1 
ATOM   10680 N  NE2 . HIS E  1 233 ? -33.471  -38.143 19.025  1.00 50.45  ? 232 HIS I NE2 1 
ATOM   10681 N  N   . PHE E  1 234 ? -37.770  -37.610 23.711  1.00 29.47  ? 233 PHE I N   1 
ATOM   10682 C  CA  . PHE E  1 234 ? -38.510  -37.675 24.936  1.00 31.75  ? 233 PHE I CA  1 
ATOM   10683 C  C   . PHE E  1 234 ? -37.556  -38.006 26.095  1.00 35.05  ? 233 PHE I C   1 
ATOM   10684 O  O   . PHE E  1 234 ? -36.963  -39.093 26.116  1.00 35.14  ? 233 PHE I O   1 
ATOM   10685 C  CB  . PHE E  1 234 ? -39.633  -38.707 24.825  1.00 29.43  ? 233 PHE I CB  1 
ATOM   10686 C  CG  . PHE E  1 234 ? -40.454  -38.870 26.076  1.00 30.28  ? 233 PHE I CG  1 
ATOM   10687 C  CD1 . PHE E  1 234 ? -40.808  -40.135 26.528  1.00 32.08  ? 233 PHE I CD1 1 
ATOM   10688 C  CD2 . PHE E  1 234 ? -40.899  -37.764 26.785  1.00 30.83  ? 233 PHE I CD2 1 
ATOM   10689 C  CE1 . PHE E  1 234 ? -41.573  -40.284 27.675  1.00 32.17  ? 233 PHE I CE1 1 
ATOM   10690 C  CE2 . PHE E  1 234 ? -41.647  -37.918 27.942  1.00 29.92  ? 233 PHE I CE2 1 
ATOM   10691 C  CZ  . PHE E  1 234 ? -41.991  -39.173 28.379  1.00 30.92  ? 233 PHE I CZ  1 
ATOM   10692 N  N   . ASN E  1 235 ? -37.434  -37.073 27.055  1.00 34.51  ? 234 ASN I N   1 
ATOM   10693 C  CA  . ASN E  1 235 ? -36.376  -37.133 28.068  1.00 41.06  ? 234 ASN I CA  1 
ATOM   10694 C  C   . ASN E  1 235 ? -36.871  -36.576 29.401  1.00 42.49  ? 234 ASN I C   1 
ATOM   10695 O  O   . ASN E  1 235 ? -36.370  -35.558 29.878  1.00 42.94  ? 234 ASN I O   1 
ATOM   10696 C  CB  . ASN E  1 235 ? -35.135  -36.372 27.594  1.00 42.59  ? 234 ASN I CB  1 
ATOM   10697 C  CG  . ASN E  1 235 ? -33.990  -36.415 28.583  1.00 47.59  ? 234 ASN I CG  1 
ATOM   10698 O  OD1 . ASN E  1 235 ? -33.208  -35.462 28.663  1.00 49.41  ? 234 ASN I OD1 1 
ATOM   10699 N  ND2 . ASN E  1 235 ? -33.876  -37.517 29.314  1.00 42.54  ? 234 ASN I ND2 1 
ATOM   10700 N  N   . PRO E  1 236 ? -37.844  -37.236 30.067  1.00 43.98  ? 235 PRO I N   1 
ATOM   10701 C  CA  . PRO E  1 236 ? -38.397  -36.710 31.318  1.00 46.85  ? 235 PRO I CA  1 
ATOM   10702 C  C   . PRO E  1 236 ? -37.400  -36.698 32.498  1.00 50.49  ? 235 PRO I C   1 
ATOM   10703 O  O   . PRO E  1 236 ? -37.485  -35.839 33.367  1.00 54.85  ? 235 PRO I O   1 
ATOM   10704 C  CB  . PRO E  1 236 ? -39.576  -37.655 31.600  1.00 43.35  ? 235 PRO I CB  1 
ATOM   10705 C  CG  . PRO E  1 236 ? -39.177  -38.952 30.927  1.00 44.43  ? 235 PRO I CG  1 
ATOM   10706 C  CD  . PRO E  1 236 ? -38.433  -38.527 29.677  1.00 39.76  ? 235 PRO I CD  1 
ATOM   10707 N  N   . LEU E  1 237 ? -36.459  -37.644 32.521  1.00 53.47  ? 236 LEU I N   1 
ATOM   10708 C  CA  . LEU E  1 237 ? -35.506  -37.784 33.632  1.00 59.26  ? 236 LEU I CA  1 
ATOM   10709 C  C   . LEU E  1 237 ? -34.314  -36.826 33.463  1.00 63.73  ? 236 LEU I C   1 
ATOM   10710 O  O   . LEU E  1 237 ? -33.458  -36.750 34.343  1.00 69.50  ? 236 LEU I O   1 
ATOM   10711 C  CB  . LEU E  1 237 ? -35.062  -39.248 33.703  1.00 59.31  ? 236 LEU I CB  1 
ATOM   10712 C  CG  . LEU E  1 237 ? -36.172  -40.237 34.055  1.00 62.16  ? 236 LEU I CG  1 
ATOM   10713 C  CD1 . LEU E  1 237 ? -35.620  -41.646 34.203  1.00 59.32  ? 236 LEU I CD1 1 
ATOM   10714 C  CD2 . LEU E  1 237 ? -36.904  -39.816 35.325  1.00 64.81  ? 236 LEU I CD2 1 
ATOM   10715 N  N   . SER E  1 238 ? -34.263  -36.118 32.326  1.00 66.00  ? 237 SER I N   1 
ATOM   10716 C  CA  . SER E  1 238 ? -33.390  -34.968 32.101  1.00 66.52  ? 237 SER I CA  1 
ATOM   10717 C  C   . SER E  1 238 ? -31.907  -35.382 32.077  1.00 65.42  ? 237 SER I C   1 
ATOM   10718 O  O   . SER E  1 238 ? -31.083  -34.784 32.763  1.00 69.97  ? 237 SER I O   1 
ATOM   10719 C  CB  . SER E  1 238 ? -33.675  -33.907 33.144  1.00 68.82  ? 237 SER I CB  1 
ATOM   10720 O  OG  . SER E  1 238 ? -33.218  -32.637 32.711  1.00 73.78  ? 237 SER I OG  1 
ATOM   10721 N  N   . ARG E  1 239 ? -31.563  -36.388 31.261  1.00 65.08  ? 238 ARG I N   1 
ATOM   10722 C  CA  . ARG E  1 239 ? -30.185  -36.919 31.193  1.00 72.76  ? 238 ARG I CA  1 
ATOM   10723 C  C   . ARG E  1 239 ? -29.696  -37.002 29.734  1.00 69.45  ? 238 ARG I C   1 
ATOM   10724 O  O   . ARG E  1 239 ? -30.350  -36.500 28.824  1.00 66.81  ? 238 ARG I O   1 
ATOM   10725 C  CB  . ARG E  1 239 ? -30.115  -38.254 31.939  1.00 77.72  ? 238 ARG I CB  1 
ATOM   10726 C  CG  . ARG E  1 239 ? -30.995  -39.362 31.381  1.00 81.74  ? 238 ARG I CG  1 
ATOM   10727 C  CD  . ARG E  1 239 ? -30.997  -40.551 32.326  1.00 84.50  ? 238 ARG I CD  1 
ATOM   10728 N  NE  . ARG E  1 239 ? -31.355  -40.168 33.686  1.00 83.25  ? 238 ARG I NE  1 
ATOM   10729 C  CZ  . ARG E  1 239 ? -31.255  -40.955 34.751  1.00 82.79  ? 238 ARG I CZ  1 
ATOM   10730 N  NH1 . ARG E  1 239 ? -31.486  -40.455 35.951  1.00 84.93  ? 238 ARG I NH1 1 
ATOM   10731 N  NH2 . ARG E  1 239 ? -30.940  -42.232 34.619  1.00 76.73  ? 238 ARG I NH2 1 
ATOM   10732 N  N   . LYS E  1 240 ? -28.503  -37.584 29.539  1.00 68.01  ? 239 LYS I N   1 
ATOM   10733 C  CA  . LYS E  1 240 ? -27.820  -37.619 28.239  1.00 70.84  ? 239 LYS I CA  1 
ATOM   10734 C  C   . LYS E  1 240 ? -28.374  -38.772 27.393  1.00 64.27  ? 239 LYS I C   1 
ATOM   10735 O  O   . LYS E  1 240 ? -28.874  -39.773 27.921  1.00 53.44  ? 239 LYS I O   1 
ATOM   10736 C  CB  . LYS E  1 240 ? -26.301  -37.757 28.411  1.00 76.23  ? 239 LYS I CB  1 
ATOM   10737 C  CG  . LYS E  1 240 ? -25.608  -36.607 29.137  1.00 81.45  ? 239 LYS I CG  1 
ATOM   10738 C  CD  . LYS E  1 240 ? -25.578  -35.308 28.359  1.00 86.36  ? 239 LYS I CD  1 
ATOM   10739 C  CE  . LYS E  1 240 ? -26.787  -34.424 28.589  1.00 94.47  ? 239 LYS I CE  1 
ATOM   10740 N  NZ  . LYS E  1 240 ? -27.171  -33.686 27.358  1.00 97.70  ? 239 LYS I NZ  1 
ATOM   10741 N  N   . HIS E  1 241 ? -28.285  -38.597 26.068  1.00 62.46  ? 240 HIS I N   1 
ATOM   10742 C  CA  . HIS E  1 241 ? -28.665  -39.613 25.097  1.00 61.58  ? 240 HIS I CA  1 
ATOM   10743 C  C   . HIS E  1 241 ? -27.744  -40.827 25.270  1.00 60.47  ? 240 HIS I C   1 
ATOM   10744 O  O   . HIS E  1 241 ? -26.543  -40.670 25.495  1.00 58.16  ? 240 HIS I O   1 
ATOM   10745 C  CB  . HIS E  1 241 ? -28.612  -39.048 23.662  1.00 62.73  ? 240 HIS I CB  1 
ATOM   10746 C  CG  . HIS E  1 241 ? -28.845  -40.065 22.591  1.00 61.01  ? 240 HIS I CG  1 
ATOM   10747 N  ND1 . HIS E  1 241 ? -30.115  -40.460 22.183  1.00 58.08  ? 240 HIS I ND1 1 
ATOM   10748 C  CD2 . HIS E  1 241 ? -27.971  -40.777 21.845  1.00 63.04  ? 240 HIS I CD2 1 
ATOM   10749 C  CE1 . HIS E  1 241 ? -30.003  -41.362 21.226  1.00 60.65  ? 240 HIS I CE1 1 
ATOM   10750 N  NE2 . HIS E  1 241 ? -28.701  -41.577 21.005  1.00 67.35  ? 240 HIS I NE2 1 
ATOM   10751 N  N   . GLY E  1 242 ? -28.329  -42.026 25.175  1.00 55.36  ? 241 GLY I N   1 
ATOM   10752 C  CA  . GLY E  1 242 ? -27.571  -43.264 25.040  1.00 57.62  ? 241 GLY I CA  1 
ATOM   10753 C  C   . GLY E  1 242 ? -28.299  -44.294 24.192  1.00 57.23  ? 241 GLY I C   1 
ATOM   10754 O  O   . GLY E  1 242 ? -29.327  -43.999 23.565  1.00 57.62  ? 241 GLY I O   1 
ATOM   10755 N  N   . GLY E  1 243 ? -27.735  -45.505 24.155  1.00 57.21  ? 242 GLY I N   1 
ATOM   10756 C  CA  . GLY E  1 243 ? -28.417  -46.680 23.624  1.00 59.25  ? 242 GLY I CA  1 
ATOM   10757 C  C   . GLY E  1 243 ? -29.495  -47.165 24.588  1.00 60.60  ? 242 GLY I C   1 
ATOM   10758 O  O   . GLY E  1 243 ? -29.460  -46.815 25.769  1.00 58.51  ? 242 GLY I O   1 
ATOM   10759 N  N   . PRO E  1 244 ? -30.479  -47.970 24.114  1.00 61.91  ? 243 PRO I N   1 
ATOM   10760 C  CA  . PRO E  1 244 ? -31.512  -48.548 24.979  1.00 65.23  ? 243 PRO I CA  1 
ATOM   10761 C  C   . PRO E  1 244 ? -31.013  -49.168 26.298  1.00 68.94  ? 243 PRO I C   1 
ATOM   10762 O  O   . PRO E  1 244 ? -31.703  -49.062 27.326  1.00 64.64  ? 243 PRO I O   1 
ATOM   10763 C  CB  . PRO E  1 244 ? -32.137  -49.656 24.112  1.00 63.74  ? 243 PRO I CB  1 
ATOM   10764 C  CG  . PRO E  1 244 ? -31.929  -49.184 22.691  1.00 63.50  ? 243 PRO I CG  1 
ATOM   10765 C  CD  . PRO E  1 244 ? -30.653  -48.362 22.708  1.00 60.78  ? 243 PRO I CD  1 
ATOM   10766 N  N   . LYS E  1 245 ? -29.832  -49.801 26.265  1.00 70.85  ? 244 LYS I N   1 
ATOM   10767 C  CA  . LYS E  1 245 ? -29.288  -50.502 27.432  1.00 76.76  ? 244 LYS I CA  1 
ATOM   10768 C  C   . LYS E  1 245 ? -28.275  -49.626 28.191  1.00 74.21  ? 244 LYS I C   1 
ATOM   10769 O  O   . LYS E  1 245 ? -27.485  -50.151 28.963  1.00 81.68  ? 244 LYS I O   1 
ATOM   10770 C  CB  . LYS E  1 245 ? -28.694  -51.845 26.995  1.00 81.66  ? 244 LYS I CB  1 
ATOM   10771 C  CG  . LYS E  1 245 ? -29.721  -52.858 26.502  1.00 87.30  ? 244 LYS I CG  1 
ATOM   10772 C  CD  . LYS E  1 245 ? -29.320  -54.302 26.723  1.00 92.19  ? 244 LYS I CD  1 
ATOM   10773 C  CE  . LYS E  1 245 ? -29.709  -54.840 28.084  1.00 94.52  ? 244 LYS I CE  1 
ATOM   10774 N  NZ  . LYS E  1 245 ? -29.020  -56.121 28.378  1.00 94.14  ? 244 LYS I NZ  1 
ATOM   10775 N  N   . ASP E  1 246 ? -28.312  -48.302 27.993  1.00 74.02  ? 245 ASP I N   1 
ATOM   10776 C  CA  . ASP E  1 246 ? -27.639  -47.345 28.885  1.00 79.58  ? 245 ASP I CA  1 
ATOM   10777 C  C   . ASP E  1 246 ? -28.587  -46.958 30.026  1.00 79.31  ? 245 ASP I C   1 
ATOM   10778 O  O   . ASP E  1 246 ? -29.791  -46.778 29.805  1.00 78.62  ? 245 ASP I O   1 
ATOM   10779 C  CB  . ASP E  1 246 ? -27.228  -46.053 28.170  1.00 84.76  ? 245 ASP I CB  1 
ATOM   10780 C  CG  . ASP E  1 246 ? -25.911  -46.122 27.416  1.00 89.63  ? 245 ASP I CG  1 
ATOM   10781 O  OD1 . ASP E  1 246 ? -25.183  -45.103 27.425  1.00 92.49  ? 245 ASP I OD1 1 
ATOM   10782 O  OD2 . ASP E  1 246 ? -25.632  -47.179 26.816  1.00 86.78  ? 245 ASP I OD2 1 
ATOM   10783 N  N   . GLU E  1 247 ? -28.029  -46.805 31.234  1.00 82.24  ? 246 GLU I N   1 
ATOM   10784 C  CA  . GLU E  1 247 ? -28.716  -46.123 32.332  1.00 83.58  ? 246 GLU I CA  1 
ATOM   10785 C  C   . GLU E  1 247 ? -28.874  -44.651 31.932  1.00 80.47  ? 246 GLU I C   1 
ATOM   10786 O  O   . GLU E  1 247 ? -29.979  -44.102 31.962  1.00 76.17  ? 246 GLU I O   1 
ATOM   10787 C  CB  . GLU E  1 247 ? -27.959  -46.291 33.655  1.00 87.31  ? 246 GLU I CB  1 
ATOM   10788 C  CG  . GLU E  1 247 ? -28.807  -46.004 34.892  1.00 92.59  ? 246 GLU I CG  1 
ATOM   10789 C  CD  . GLU E  1 247 ? -28.509  -44.703 35.625  1.00 97.36  ? 246 GLU I CD  1 
ATOM   10790 O  OE1 . GLU E  1 247 ? -28.286  -44.761 36.857  1.00 100.92 ? 246 GLU I OE1 1 
ATOM   10791 O  OE2 . GLU E  1 247 ? -28.508  -43.633 34.975  1.00 97.38  ? 246 GLU I OE2 1 
ATOM   10792 N  N   . GLU E  1 248 ? -27.759  -44.038 31.517  1.00 77.53  ? 247 GLU I N   1 
ATOM   10793 C  CA  . GLU E  1 248 ? -27.771  -42.701 30.935  1.00 77.23  ? 247 GLU I CA  1 
ATOM   10794 C  C   . GLU E  1 248 ? -28.344  -42.788 29.510  1.00 73.05  ? 247 GLU I C   1 
ATOM   10795 O  O   . GLU E  1 248 ? -27.619  -43.028 28.531  1.00 67.14  ? 247 GLU I O   1 
ATOM   10796 C  CB  . GLU E  1 248 ? -26.369  -42.084 30.963  1.00 78.13  ? 247 GLU I CB  1 
ATOM   10797 C  CG  . GLU E  1 248 ? -26.380  -40.567 30.860  1.00 80.68  ? 247 GLU I CG  1 
ATOM   10798 C  CD  . GLU E  1 248 ? -26.891  -39.825 32.089  1.00 81.42  ? 247 GLU I CD  1 
ATOM   10799 O  OE1 . GLU E  1 248 ? -26.911  -38.576 32.050  1.00 82.70  ? 247 GLU I OE1 1 
ATOM   10800 O  OE2 . GLU E  1 248 ? -27.279  -40.487 33.077  1.00 81.32  ? 247 GLU I OE2 1 
ATOM   10801 N  N   . ARG E  1 249 ? -29.666  -42.614 29.418  1.00 64.63  ? 248 ARG I N   1 
ATOM   10802 C  CA  . ARG E  1 249 ? -30.389  -42.584 28.147  1.00 58.49  ? 248 ARG I CA  1 
ATOM   10803 C  C   . ARG E  1 249 ? -31.652  -41.743 28.314  1.00 52.70  ? 248 ARG I C   1 
ATOM   10804 O  O   . ARG E  1 249 ? -32.188  -41.633 29.419  1.00 53.59  ? 248 ARG I O   1 
ATOM   10805 C  CB  . ARG E  1 249 ? -30.787  -43.995 27.704  1.00 54.33  ? 248 ARG I CB  1 
ATOM   10806 C  CG  . ARG E  1 249 ? -31.973  -44.576 28.461  1.00 50.25  ? 248 ARG I CG  1 
ATOM   10807 C  CD  . ARG E  1 249 ? -32.481  -45.865 27.844  1.00 49.52  ? 248 ARG I CD  1 
ATOM   10808 N  NE  . ARG E  1 249 ? -33.709  -45.702 27.068  1.00 50.02  ? 248 ARG I NE  1 
ATOM   10809 C  CZ  . ARG E  1 249 ? -34.528  -46.703 26.753  1.00 46.74  ? 248 ARG I CZ  1 
ATOM   10810 N  NH1 . ARG E  1 249 ? -35.675  -46.462 26.135  1.00 38.28  ? 248 ARG I NH1 1 
ATOM   10811 N  NH2 . ARG E  1 249 ? -34.192  -47.946 27.071  1.00 45.13  ? 248 ARG I NH2 1 
ATOM   10812 N  N   . HIS E  1 250 ? -32.116  -41.171 27.203  1.00 47.60  ? 249 HIS I N   1 
ATOM   10813 C  CA  . HIS E  1 250 ? -33.450  -40.618 27.123  1.00 45.08  ? 249 HIS I CA  1 
ATOM   10814 C  C   . HIS E  1 250 ? -34.444  -41.782 27.180  1.00 41.36  ? 249 HIS I C   1 
ATOM   10815 O  O   . HIS E  1 250 ? -34.183  -42.872 26.647  1.00 38.48  ? 249 HIS I O   1 
ATOM   10816 C  CB  . HIS E  1 250 ? -33.618  -39.790 25.842  1.00 46.64  ? 249 HIS I CB  1 
ATOM   10817 C  CG  . HIS E  1 250 ? -32.636  -38.676 25.697  1.00 48.89  ? 249 HIS I CG  1 
ATOM   10818 N  ND1 . HIS E  1 250 ? -32.111  -38.304 24.469  1.00 47.67  ? 249 HIS I ND1 1 
ATOM   10819 C  CD2 . HIS E  1 250 ? -32.073  -37.861 26.618  1.00 51.25  ? 249 HIS I CD2 1 
ATOM   10820 C  CE1 . HIS E  1 250 ? -31.302  -37.273 24.641  1.00 51.11  ? 249 HIS I CE1 1 
ATOM   10821 N  NE2 . HIS E  1 250 ? -31.256  -36.986 25.953  1.00 48.84  ? 249 HIS I NE2 1 
ATOM   10822 N  N   . VAL E  1 251 ? -35.603  -41.548 27.795  1.00 38.92  ? 250 VAL I N   1 
ATOM   10823 C  CA  . VAL E  1 251 ? -36.659  -42.534 27.717  1.00 35.81  ? 250 VAL I CA  1 
ATOM   10824 C  C   . VAL E  1 251 ? -36.909  -42.899 26.239  1.00 34.07  ? 250 VAL I C   1 
ATOM   10825 O  O   . VAL E  1 251 ? -37.030  -44.077 25.906  1.00 35.31  ? 250 VAL I O   1 
ATOM   10826 C  CB  . VAL E  1 251 ? -37.915  -42.056 28.460  1.00 38.20  ? 250 VAL I CB  1 
ATOM   10827 C  CG1 . VAL E  1 251 ? -39.117  -42.961 28.199  1.00 36.74  ? 250 VAL I CG1 1 
ATOM   10828 C  CG2 . VAL E  1 251 ? -37.632  -41.956 29.958  1.00 39.16  ? 250 VAL I CG2 1 
ATOM   10829 N  N   . GLY E  1 252 ? -36.836  -41.914 25.340  1.00 35.72  ? 251 GLY I N   1 
ATOM   10830 C  CA  . GLY E  1 252 ? -37.198  -42.102 23.918  1.00 38.78  ? 251 GLY I CA  1 
ATOM   10831 C  C   . GLY E  1 252 ? -36.155  -42.824 23.058  1.00 40.16  ? 251 GLY I C   1 
ATOM   10832 O  O   . GLY E  1 252 ? -36.413  -43.094 21.886  1.00 35.35  ? 251 GLY I O   1 
ATOM   10833 N  N   A SER E  1 253 ? -34.963  -43.090 23.595  0.45 41.07  ? 252 SER I N   1 
ATOM   10834 C  CA  A SER E  1 253 ? -33.876  -43.617 22.775  0.45 41.91  ? 252 SER I CA  1 
ATOM   10835 C  C   A SER E  1 253 ? -34.037  -45.133 22.612  0.45 37.75  ? 252 SER I C   1 
ATOM   10836 O  O   A SER E  1 253 ? -33.642  -45.901 23.486  0.45 41.28  ? 252 SER I O   1 
ATOM   10837 C  CB  A SER E  1 253 ? -32.545  -43.192 23.366  0.45 44.92  ? 252 SER I CB  1 
ATOM   10838 O  OG  A SER E  1 253 ? -32.340  -41.783 23.187  0.45 48.22  ? 252 SER I OG  1 
ATOM   10839 N  N   B ASP E  1 253 ? -35.006  -43.160 23.670  0.55 37.61  ? 252 ASP I N   1 
ATOM   10840 C  CA  B ASP E  1 253 ? -33.874  -43.773 22.989  0.55 37.65  ? 252 ASP I CA  1 
ATOM   10841 C  C   B ASP E  1 253 ? -34.171  -45.243 22.696  0.55 34.44  ? 252 ASP I C   1 
ATOM   10842 O  O   B ASP E  1 253 ? -33.972  -46.100 23.558  0.55 36.87  ? 252 ASP I O   1 
ATOM   10843 C  CB  B ASP E  1 253 ? -32.611  -43.662 23.855  0.55 38.00  ? 252 ASP I CB  1 
ATOM   10844 C  CG  B ASP E  1 253 ? -32.192  -42.222 24.069  0.55 40.12  ? 252 ASP I CG  1 
ATOM   10845 O  OD1 B ASP E  1 253 ? -32.763  -41.362 23.372  0.55 44.42  ? 252 ASP I OD1 1 
ATOM   10846 O  OD2 B ASP E  1 253 ? -31.322  -41.963 24.927  0.55 39.32  ? 252 ASP I OD2 1 
ATOM   10847 N  N   . LEU E  1 254 ? -34.647  -45.542 21.488  1.00 33.87  ? 253 LEU I N   1 
ATOM   10848 C  CA  . LEU E  1 254 ? -34.926  -46.943 21.163  1.00 36.07  ? 253 LEU I CA  1 
ATOM   10849 C  C   . LEU E  1 254 ? -33.874  -47.524 20.200  1.00 36.42  ? 253 LEU I C   1 
ATOM   10850 O  O   . LEU E  1 254 ? -34.069  -48.581 19.657  1.00 38.78  ? 253 LEU I O   1 
ATOM   10851 C  CB  . LEU E  1 254 ? -36.351  -47.060 20.604  1.00 36.04  ? 253 LEU I CB  1 
ATOM   10852 C  CG  . LEU E  1 254 ? -37.473  -46.822 21.622  1.00 38.29  ? 253 LEU I CG  1 
ATOM   10853 C  CD1 . LEU E  1 254 ? -38.826  -47.082 20.983  1.00 40.21  ? 253 LEU I CD1 1 
ATOM   10854 C  CD2 . LEU E  1 254 ? -37.296  -47.697 22.853  1.00 39.07  ? 253 LEU I CD2 1 
ATOM   10855 N  N   . GLY E  1 255 ? -32.736  -46.852 20.018  1.00 36.31  ? 254 GLY I N   1 
ATOM   10856 C  CA  . GLY E  1 255 ? -31.616  -47.461 19.282  1.00 37.63  ? 254 GLY I CA  1 
ATOM   10857 C  C   . GLY E  1 255 ? -31.765  -47.326 17.780  1.00 32.74  ? 254 GLY I C   1 
ATOM   10858 O  O   . GLY E  1 255 ? -32.071  -46.250 17.299  1.00 35.48  ? 254 GLY I O   1 
ATOM   10859 N  N   . ASN E  1 256 ? -31.541  -48.430 17.060  1.00 33.60  ? 255 ASN I N   1 
ATOM   10860 C  CA  . ASN E  1 256 ? -31.479  -48.449 15.608  1.00 34.38  ? 255 ASN I CA  1 
ATOM   10861 C  C   . ASN E  1 256 ? -32.348  -49.579 15.083  1.00 34.13  ? 255 ASN I C   1 
ATOM   10862 O  O   . ASN E  1 256 ? -32.549  -50.562 15.751  1.00 34.39  ? 255 ASN I O   1 
ATOM   10863 C  CB  . ASN E  1 256 ? -30.061  -48.656 15.069  1.00 36.09  ? 255 ASN I CB  1 
ATOM   10864 C  CG  . ASN E  1 256 ? -29.171  -47.463 15.325  1.00 39.06  ? 255 ASN I CG  1 
ATOM   10865 O  OD1 . ASN E  1 256 ? -29.408  -46.389 14.769  1.00 38.82  ? 255 ASN I OD1 1 
ATOM   10866 N  ND2 . ASN E  1 256 ? -28.165  -47.627 16.180  1.00 39.33  ? 255 ASN I ND2 1 
ATOM   10867 N  N   . VAL E  1 257 ? -32.891  -49.371 13.884  1.00 33.74  ? 256 VAL I N   1 
ATOM   10868 C  CA  . VAL E  1 257 ? -33.498  -50.412 13.107  1.00 33.36  ? 256 VAL I CA  1 
ATOM   10869 C  C   . VAL E  1 257 ? -32.620  -50.589 11.866  1.00 31.63  ? 256 VAL I C   1 
ATOM   10870 O  O   . VAL E  1 257 ? -31.898  -49.681 11.474  1.00 34.29  ? 256 VAL I O   1 
ATOM   10871 C  CB  . VAL E  1 257 ? -34.965  -50.089 12.751  1.00 35.12  ? 256 VAL I CB  1 
ATOM   10872 C  CG1 . VAL E  1 257 ? -35.800  -49.878 14.009  1.00 36.33  ? 256 VAL I CG1 1 
ATOM   10873 C  CG2 . VAL E  1 257 ? -35.088  -48.882 11.831  1.00 35.53  ? 256 VAL I CG2 1 
ATOM   10874 N  N   . THR E  1 258 ? -32.690  -51.783 11.292  1.00 32.83  ? 257 THR I N   1 
ATOM   10875 C  CA  . THR E  1 258 ? -31.862  -52.189 10.167  1.00 35.04  ? 257 THR I CA  1 
ATOM   10876 C  C   . THR E  1 258 ? -32.732  -52.457 8.944   1.00 30.06  ? 257 THR I C   1 
ATOM   10877 O  O   . THR E  1 258 ? -33.565  -53.384 8.938   1.00 31.43  ? 257 THR I O   1 
ATOM   10878 C  CB  . THR E  1 258 ? -31.119  -53.491 10.499  1.00 37.65  ? 257 THR I CB  1 
ATOM   10879 O  OG1 . THR E  1 258 ? -30.326  -53.200 11.642  1.00 37.38  ? 257 THR I OG1 1 
ATOM   10880 C  CG2 . THR E  1 258 ? -30.256  -53.992 9.363   1.00 41.79  ? 257 THR I CG2 1 
ATOM   10881 N  N   . ALA E  1 259 ? -32.502  -51.688 7.890   1.00 30.63  ? 258 ALA I N   1 
ATOM   10882 C  CA  . ALA E  1 259 ? -33.168  -51.943 6.646   1.00 32.99  ? 258 ALA I CA  1 
ATOM   10883 C  C   . ALA E  1 259 ? -32.289  -52.874 5.805   1.00 32.84  ? 258 ALA I C   1 
ATOM   10884 O  O   . ALA E  1 259 ? -31.075  -52.665 5.700   1.00 29.59  ? 258 ALA I O   1 
ATOM   10885 C  CB  . ALA E  1 259 ? -33.432  -50.649 5.915   1.00 33.36  ? 258 ALA I CB  1 
ATOM   10886 N  N   . ASP E  1 260 ? -32.946  -53.848 5.181   1.00 33.50  ? 259 ASP I N   1 
ATOM   10887 C  CA  . ASP E  1 260 ? -32.321  -54.798 4.296   1.00 36.88  ? 259 ASP I CA  1 
ATOM   10888 C  C   . ASP E  1 260 ? -32.097  -54.133 2.934   1.00 40.23  ? 259 ASP I C   1 
ATOM   10889 O  O   . ASP E  1 260 ? -32.249  -52.898 2.760   1.00 38.49  ? 259 ASP I O   1 
ATOM   10890 C  CB  . ASP E  1 260 ? -33.160  -56.072 4.239   1.00 35.71  ? 259 ASP I CB  1 
ATOM   10891 C  CG  . ASP E  1 260 ? -34.523  -55.935 3.579   1.00 39.40  ? 259 ASP I CG  1 
ATOM   10892 O  OD1 . ASP E  1 260 ? -35.354  -56.855 3.780   1.00 37.30  ? 259 ASP I OD1 1 
ATOM   10893 O  OD2 . ASP E  1 260 ? -34.745  -54.936 2.840   1.00 38.51  ? 259 ASP I OD2 1 
ATOM   10894 N  N   . LYS E  1 261 ? -31.727  -54.956 1.951   1.00 42.82  ? 260 LYS I N   1 
ATOM   10895 C  CA  . LYS E  1 261 ? -31.367  -54.449 0.643   1.00 45.40  ? 260 LYS I CA  1 
ATOM   10896 C  C   . LYS E  1 261 ? -32.627  -54.052 -0.140  1.00 39.33  ? 260 LYS I C   1 
ATOM   10897 O  O   . LYS E  1 261 ? -32.515  -53.339 -1.114  1.00 41.44  ? 260 LYS I O   1 
ATOM   10898 C  CB  . LYS E  1 261 ? -30.509  -55.479 -0.097  1.00 52.21  ? 260 LYS I CB  1 
ATOM   10899 C  CG  . LYS E  1 261 ? -31.251  -56.716 -0.585  1.00 62.17  ? 260 LYS I CG  1 
ATOM   10900 C  CD  . LYS E  1 261 ? -30.346  -57.917 -0.839  1.00 73.04  ? 260 LYS I CD  1 
ATOM   10901 C  CE  . LYS E  1 261 ? -28.934  -57.543 -1.255  1.00 80.12  ? 260 LYS I CE  1 
ATOM   10902 N  NZ  . LYS E  1 261 ? -28.215  -58.683 -1.878  1.00 86.39  ? 260 LYS I NZ  1 
ATOM   10903 N  N   . ASP E  1 262 ? -33.810  -54.517 0.280   1.00 34.91  ? 261 ASP I N   1 
ATOM   10904 C  CA  . ASP E  1 262 ? -35.060  -54.066 -0.298  1.00 37.79  ? 261 ASP I CA  1 
ATOM   10905 C  C   . ASP E  1 262 ? -35.539  -52.754 0.357   1.00 35.57  ? 261 ASP I C   1 
ATOM   10906 O  O   . ASP E  1 262 ? -36.591  -52.246 0.003   1.00 35.22  ? 261 ASP I O   1 
ATOM   10907 C  CB  . ASP E  1 262 ? -36.110  -55.165 -0.191  1.00 43.35  ? 261 ASP I CB  1 
ATOM   10908 C  CG  . ASP E  1 262 ? -35.779  -56.363 -1.069  1.00 49.69  ? 261 ASP I CG  1 
ATOM   10909 O  OD1 . ASP E  1 262 ? -35.994  -57.497 -0.603  1.00 53.69  ? 261 ASP I OD1 1 
ATOM   10910 O  OD2 . ASP E  1 262 ? -35.295  -56.149 -2.208  1.00 55.95  ? 261 ASP I OD2 1 
ATOM   10911 N  N   . GLY E  1 263 ? -34.762  -52.210 1.297   1.00 34.00  ? 262 GLY I N   1 
ATOM   10912 C  CA  . GLY E  1 263 ? -35.088  -50.972 1.999   1.00 32.88  ? 262 GLY I CA  1 
ATOM   10913 C  C   . GLY E  1 263 ? -36.168  -51.160 3.055   1.00 34.55  ? 262 GLY I C   1 
ATOM   10914 O  O   . GLY E  1 263 ? -36.863  -50.198 3.400   1.00 32.62  ? 262 GLY I O   1 
ATOM   10915 N  N   . VAL E  1 264 ? -36.294  -52.389 3.576   1.00 33.41  ? 263 VAL I N   1 
ATOM   10916 C  CA  . VAL E  1 264 ? -37.302  -52.765 4.551   1.00 34.46  ? 263 VAL I CA  1 
ATOM   10917 C  C   . VAL E  1 264 ? -36.628  -53.120 5.884   1.00 37.98  ? 263 VAL I C   1 
ATOM   10918 O  O   . VAL E  1 264 ? -35.748  -53.999 5.937   1.00 34.47  ? 263 VAL I O   1 
ATOM   10919 C  CB  . VAL E  1 264 ? -38.124  -53.971 4.068   1.00 36.21  ? 263 VAL I CB  1 
ATOM   10920 C  CG1 . VAL E  1 264 ? -39.137  -54.398 5.115   1.00 36.24  ? 263 VAL I CG1 1 
ATOM   10921 C  CG2 . VAL E  1 264 ? -38.812  -53.698 2.745   1.00 38.32  ? 263 VAL I CG2 1 
ATOM   10922 N  N   . ALA E  1 265 ? -37.100  -52.484 6.960   1.00 34.39  ? 264 ALA I N   1 
ATOM   10923 C  CA  . ALA E  1 265 ? -36.654  -52.744 8.316   1.00 35.49  ? 264 ALA I CA  1 
ATOM   10924 C  C   . ALA E  1 265 ? -37.782  -53.444 9.072   1.00 39.44  ? 264 ALA I C   1 
ATOM   10925 O  O   . ALA E  1 265 ? -38.860  -52.874 9.245   1.00 37.61  ? 264 ALA I O   1 
ATOM   10926 C  CB  . ALA E  1 265 ? -36.270  -51.455 8.993   1.00 36.19  ? 264 ALA I CB  1 
ATOM   10927 N  N   . ASP E  1 266 ? -37.527  -54.693 9.465   1.00 38.44  ? 265 ASP I N   1 
ATOM   10928 C  CA  . ASP E  1 266 ? -38.401  -55.450 10.327  1.00 40.61  ? 265 ASP I CA  1 
ATOM   10929 C  C   . ASP E  1 266 ? -37.993  -55.151 11.767  1.00 40.58  ? 265 ASP I C   1 
ATOM   10930 O  O   . ASP E  1 266 ? -36.854  -55.365 12.151  1.00 45.09  ? 265 ASP I O   1 
ATOM   10931 C  CB  . ASP E  1 266 ? -38.353  -56.938 9.987   1.00 46.59  ? 265 ASP I CB  1 
ATOM   10932 C  CG  . ASP E  1 266 ? -39.018  -57.244 8.656   1.00 54.94  ? 265 ASP I CG  1 
ATOM   10933 O  OD1 . ASP E  1 266 ? -40.050  -56.604 8.353   1.00 61.00  ? 265 ASP I OD1 1 
ATOM   10934 O  OD2 . ASP E  1 266 ? -38.489  -58.104 7.916   1.00 70.67  ? 265 ASP I OD2 1 
ATOM   10935 N  N   . VAL E  1 267 ? -38.939  -54.616 12.540  1.00 36.64  ? 266 VAL I N   1 
ATOM   10936 C  CA  . VAL E  1 267 ? -38.661  -54.072 13.850  1.00 35.24  ? 266 VAL I CA  1 
ATOM   10937 C  C   . VAL E  1 267 ? -39.184  -55.065 14.880  1.00 30.46  ? 266 VAL I C   1 
ATOM   10938 O  O   . VAL E  1 267 ? -40.275  -55.589 14.747  1.00 29.63  ? 266 VAL I O   1 
ATOM   10939 C  CB  . VAL E  1 267 ? -39.288  -52.674 14.017  1.00 34.93  ? 266 VAL I CB  1 
ATOM   10940 C  CG1 . VAL E  1 267 ? -39.140  -52.151 15.432  1.00 34.70  ? 266 VAL I CG1 1 
ATOM   10941 C  CG2 . VAL E  1 267 ? -38.702  -51.692 13.015  1.00 34.50  ? 266 VAL I CG2 1 
ATOM   10942 N  N   . SER E  1 268 ? -38.355  -55.341 15.878  1.00 33.63  ? 267 SER I N   1 
ATOM   10943 C  CA  . SER E  1 268 ? -38.712  -56.240 16.928  1.00 34.77  ? 267 SER I CA  1 
ATOM   10944 C  C   . SER E  1 268 ? -37.881  -55.899 18.161  1.00 36.72  ? 267 SER I C   1 
ATOM   10945 O  O   . SER E  1 268 ? -36.744  -56.281 18.237  1.00 43.52  ? 267 SER I O   1 
ATOM   10946 C  CB  . SER E  1 268 ? -38.502  -57.656 16.493  1.00 40.09  ? 267 SER I CB  1 
ATOM   10947 O  OG  . SER E  1 268 ? -38.807  -58.537 17.558  1.00 47.58  ? 267 SER I OG  1 
ATOM   10948 N  N   . ILE E  1 269 ? -38.473  -55.154 19.095  1.00 32.80  ? 268 ILE I N   1 
ATOM   10949 C  CA  . ILE E  1 269 ? -37.784  -54.541 20.214  1.00 34.94  ? 268 ILE I CA  1 
ATOM   10950 C  C   . ILE E  1 269 ? -38.592  -54.857 21.477  1.00 34.23  ? 268 ILE I C   1 
ATOM   10951 O  O   . ILE E  1 269 ? -39.827  -54.997 21.426  1.00 29.69  ? 268 ILE I O   1 
ATOM   10952 C  CB  . ILE E  1 269 ? -37.659  -53.022 19.990  1.00 38.72  ? 268 ILE I CB  1 
ATOM   10953 C  CG1 . ILE E  1 269 ? -36.642  -52.677 18.906  1.00 43.19  ? 268 ILE I CG1 1 
ATOM   10954 C  CG2 . ILE E  1 269 ? -37.353  -52.285 21.283  1.00 42.40  ? 268 ILE I CG2 1 
ATOM   10955 C  CD1 . ILE E  1 269 ? -36.793  -51.268 18.369  1.00 45.68  ? 268 ILE I CD1 1 
ATOM   10956 N  N   . GLU E  1 270 ? -37.890  -55.000 22.599  1.00 34.15  ? 269 GLU I N   1 
ATOM   10957 C  CA  . GLU E  1 270 ? -38.524  -55.060 23.904  1.00 35.27  ? 269 GLU I CA  1 
ATOM   10958 C  C   . GLU E  1 270 ? -37.792  -54.077 24.813  1.00 37.44  ? 269 GLU I C   1 
ATOM   10959 O  O   . GLU E  1 270 ? -36.564  -54.147 24.924  1.00 36.25  ? 269 GLU I O   1 
ATOM   10960 C  CB  . GLU E  1 270 ? -38.505  -56.481 24.458  1.00 38.36  ? 269 GLU I CB  1 
ATOM   10961 C  CG  . GLU E  1 270 ? -39.417  -56.640 25.655  1.00 45.74  ? 269 GLU I CG  1 
ATOM   10962 C  CD  . GLU E  1 270 ? -39.215  -57.895 26.479  1.00 52.74  ? 269 GLU I CD  1 
ATOM   10963 O  OE1 . GLU E  1 270 ? -39.535  -58.985 25.969  1.00 63.33  ? 269 GLU I OE1 1 
ATOM   10964 O  OE2 . GLU E  1 270 ? -38.749  -57.773 27.633  1.00 59.24  ? 269 GLU I OE2 1 
ATOM   10965 N  N   . ASP E  1 271 ? -38.539  -53.133 25.403  1.00 31.80  ? 270 ASP I N   1 
ATOM   10966 C  CA  . ASP E  1 271 ? -37.937  -52.074 26.175  1.00 32.34  ? 270 ASP I CA  1 
ATOM   10967 C  C   . ASP E  1 271 ? -38.701  -51.865 27.484  1.00 31.21  ? 270 ASP I C   1 
ATOM   10968 O  O   . ASP E  1 271 ? -39.934  -51.792 27.510  1.00 32.72  ? 270 ASP I O   1 
ATOM   10969 C  CB  . ASP E  1 271 ? -37.878  -50.762 25.406  1.00 33.62  ? 270 ASP I CB  1 
ATOM   10970 C  CG  . ASP E  1 271 ? -36.965  -49.756 26.077  1.00 38.26  ? 270 ASP I CG  1 
ATOM   10971 O  OD1 . ASP E  1 271 ? -37.466  -48.888 26.811  1.00 32.40  ? 270 ASP I OD1 1 
ATOM   10972 O  OD2 . ASP E  1 271 ? -35.746  -49.859 25.867  1.00 44.56  ? 270 ASP I OD2 1 
ATOM   10973 N  N   . SER E  1 272 ? -37.958  -51.701 28.576  1.00 32.13  ? 271 SER I N   1 
ATOM   10974 C  CA  . SER E  1 272 ? -38.597  -51.567 29.882  1.00 35.34  ? 271 SER I CA  1 
ATOM   10975 C  C   . SER E  1 272 ? -38.426  -50.148 30.444  1.00 31.38  ? 271 SER I C   1 
ATOM   10976 O  O   . SER E  1 272 ? -38.696  -49.921 31.604  1.00 35.27  ? 271 SER I O   1 
ATOM   10977 C  CB  . SER E  1 272 ? -38.067  -52.623 30.822  1.00 38.56  ? 271 SER I CB  1 
ATOM   10978 O  OG  . SER E  1 272 ? -36.686  -52.413 31.033  1.00 41.57  ? 271 SER I OG  1 
ATOM   10979 N  N   . VAL E  1 273 ? -37.997  -49.189 29.620  1.00 29.53  ? 272 VAL I N   1 
ATOM   10980 C  CA  . VAL E  1 273 ? -37.901  -47.800 30.071  1.00 30.40  ? 272 VAL I CA  1 
ATOM   10981 C  C   . VAL E  1 273 ? -39.120  -47.033 29.560  1.00 29.24  ? 272 VAL I C   1 
ATOM   10982 O  O   . VAL E  1 273 ? -39.729  -46.282 30.335  1.00 28.10  ? 272 VAL I O   1 
ATOM   10983 C  CB  . VAL E  1 273 ? -36.588  -47.136 29.631  1.00 30.58  ? 272 VAL I CB  1 
ATOM   10984 C  CG1 . VAL E  1 273 ? -36.520  -45.661 30.026  1.00 31.12  ? 272 VAL I CG1 1 
ATOM   10985 C  CG2 . VAL E  1 273 ? -35.395  -47.904 30.199  1.00 33.08  ? 272 VAL I CG2 1 
ATOM   10986 N  N   . ILE E  1 274 ? -39.454  -47.216 28.273  1.00 26.53  ? 273 ILE I N   1 
ATOM   10987 C  CA  . ILE E  1 274 ? -40.723  -46.654 27.750  1.00 28.46  ? 273 ILE I CA  1 
ATOM   10988 C  C   . ILE E  1 274 ? -41.896  -47.389 28.426  1.00 25.88  ? 273 ILE I C   1 
ATOM   10989 O  O   . ILE E  1 274 ? -41.762  -48.522 28.931  1.00 26.96  ? 273 ILE I O   1 
ATOM   10990 C  CB  . ILE E  1 274 ? -40.822  -46.739 26.215  1.00 27.86  ? 273 ILE I CB  1 
ATOM   10991 C  CG1 . ILE E  1 274 ? -40.788  -48.195 25.741  1.00 28.70  ? 273 ILE I CG1 1 
ATOM   10992 C  CG2 . ILE E  1 274 ? -39.741  -45.880 25.582  1.00 29.35  ? 273 ILE I CG2 1 
ATOM   10993 C  CD1 . ILE E  1 274 ? -41.290  -48.415 24.330  1.00 29.79  ? 273 ILE I CD1 1 
ATOM   10994 N  N   . SER E  1 275 ? -43.050  -46.724 28.427  1.00 23.95  ? 274 SER I N   1 
ATOM   10995 C  CA  . SER E  1 275 ? -44.308  -47.263 28.936  1.00 23.05  ? 274 SER I CA  1 
ATOM   10996 C  C   . SER E  1 275 ? -45.437  -46.808 28.013  1.00 23.82  ? 274 SER I C   1 
ATOM   10997 O  O   . SER E  1 275 ? -45.268  -45.852 27.235  1.00 21.81  ? 274 SER I O   1 
ATOM   10998 C  CB  . SER E  1 275 ? -44.574  -46.820 30.372  1.00 21.90  ? 274 SER I CB  1 
ATOM   10999 O  OG  . SER E  1 275 ? -45.638  -47.572 30.943  1.00 23.30  ? 274 SER I OG  1 
ATOM   11000 N  N   . LEU E  1 276 ? -46.584  -47.493 28.109  1.00 24.17  ? 275 LEU I N   1 
ATOM   11001 C  CA  . LEU E  1 276 ? -47.783  -47.045 27.444  1.00 24.48  ? 275 LEU I CA  1 
ATOM   11002 C  C   . LEU E  1 276 ? -48.763  -46.386 28.436  1.00 25.96  ? 275 LEU I C   1 
ATOM   11003 O  O   . LEU E  1 276 ? -49.900  -46.097 28.061  1.00 24.49  ? 275 LEU I O   1 
ATOM   11004 C  CB  . LEU E  1 276 ? -48.425  -48.237 26.741  1.00 24.23  ? 275 LEU I CB  1 
ATOM   11005 C  CG  . LEU E  1 276 ? -47.601  -48.879 25.630  1.00 24.31  ? 275 LEU I CG  1 
ATOM   11006 C  CD1 . LEU E  1 276 ? -48.460  -49.891 24.881  1.00 24.81  ? 275 LEU I CD1 1 
ATOM   11007 C  CD2 . LEU E  1 276 ? -47.017  -47.855 24.658  1.00 23.27  ? 275 LEU I CD2 1 
ATOM   11008 N  N   . SER E  1 277 ? -48.304  -46.109 29.660  1.00 26.28  ? 276 SER I N   1 
ATOM   11009 C  CA  . SER E  1 277 ? -49.078  -45.392 30.693  1.00 26.44  ? 276 SER I CA  1 
ATOM   11010 C  C   . SER E  1 277 ? -48.119  -44.729 31.688  1.00 27.04  ? 276 SER I C   1 
ATOM   11011 O  O   . SER E  1 277 ? -46.932  -45.012 31.707  1.00 25.68  ? 276 SER I O   1 
ATOM   11012 C  CB  . SER E  1 277 ? -50.065  -46.304 31.382  1.00 25.53  ? 276 SER I CB  1 
ATOM   11013 O  OG  . SER E  1 277 ? -49.395  -47.347 32.059  1.00 26.18  ? 276 SER I OG  1 
ATOM   11014 N  N   . GLY E  1 278 ? -48.653  -43.779 32.466  1.00 28.26  ? 277 GLY I N   1 
ATOM   11015 C  CA  . GLY E  1 278 ? -47.911  -43.095 33.500  1.00 27.20  ? 277 GLY I CA  1 
ATOM   11016 C  C   . GLY E  1 278 ? -46.838  -42.171 32.959  1.00 30.40  ? 277 GLY I C   1 
ATOM   11017 O  O   . GLY E  1 278 ? -46.936  -41.644 31.849  1.00 30.90  ? 277 GLY I O   1 
ATOM   11018 N  N   . ASP E  1 279 ? -45.796  -41.989 33.778  1.00 31.80  ? 278 ASP I N   1 
ATOM   11019 C  CA  . ASP E  1 279 ? -44.766  -40.950 33.626  1.00 35.34  ? 278 ASP I CA  1 
ATOM   11020 C  C   . ASP E  1 279 ? -44.004  -41.104 32.298  1.00 31.80  ? 278 ASP I C   1 
ATOM   11021 O  O   . ASP E  1 279 ? -43.626  -40.127 31.635  1.00 29.21  ? 278 ASP I O   1 
ATOM   11022 C  CB  . ASP E  1 279 ? -43.770  -41.026 34.793  1.00 41.68  ? 278 ASP I CB  1 
ATOM   11023 C  CG  . ASP E  1 279 ? -44.399  -41.126 36.181  1.00 48.78  ? 278 ASP I CG  1 
ATOM   11024 O  OD1 . ASP E  1 279 ? -45.039  -42.199 36.510  1.00 41.87  ? 278 ASP I OD1 1 
ATOM   11025 O  OD2 . ASP E  1 279 ? -44.248  -40.134 36.933  1.00 53.75  ? 278 ASP I OD2 1 
ATOM   11026 N  N   . HIS E  1 280 ? -43.689  -42.347 31.953  1.00 27.33  ? 279 HIS I N   1 
ATOM   11027 C  CA  . HIS E  1 280 ? -42.878  -42.618 30.790  1.00 27.88  ? 279 HIS I CA  1 
ATOM   11028 C  C   . HIS E  1 280 ? -43.754  -42.986 29.580  1.00 28.33  ? 279 HIS I C   1 
ATOM   11029 O  O   . HIS E  1 280 ? -43.238  -43.562 28.607  1.00 27.23  ? 279 HIS I O   1 
ATOM   11030 C  CB  . HIS E  1 280 ? -41.865  -43.711 31.141  1.00 29.85  ? 279 HIS I CB  1 
ATOM   11031 C  CG  . HIS E  1 280 ? -40.744  -43.211 31.982  1.00 32.64  ? 279 HIS I CG  1 
ATOM   11032 N  ND1 . HIS E  1 280 ? -39.631  -43.981 32.259  1.00 32.99  ? 279 HIS I ND1 1 
ATOM   11033 C  CD2 . HIS E  1 280 ? -40.549  -42.014 32.578  1.00 33.72  ? 279 HIS I CD2 1 
ATOM   11034 C  CE1 . HIS E  1 280 ? -38.803  -43.277 33.001  1.00 33.36  ? 279 HIS I CE1 1 
ATOM   11035 N  NE2 . HIS E  1 280 ? -39.343  -42.065 33.208  1.00 33.72  ? 279 HIS I NE2 1 
ATOM   11036 N  N   . SER E  1 281 ? -45.064  -42.676 29.651  1.00 25.63  ? 280 SER I N   1 
ATOM   11037 C  CA  . SER E  1 281 ? -45.973  -42.978 28.584  1.00 26.16  ? 280 SER I CA  1 
ATOM   11038 C  C   . SER E  1 281 ? -45.517  -42.265 27.304  1.00 23.67  ? 280 SER I C   1 
ATOM   11039 O  O   . SER E  1 281 ? -45.207  -41.089 27.323  1.00 24.24  ? 280 SER I O   1 
ATOM   11040 C  CB  . SER E  1 281 ? -47.389  -42.604 28.891  1.00 25.86  ? 280 SER I CB  1 
ATOM   11041 O  OG  . SER E  1 281 ? -48.196  -42.906 27.758  1.00 25.46  ? 280 SER I OG  1 
ATOM   11042 N  N   . ILE E  1 282 ? -45.513  -43.021 26.210  1.00 23.45  ? 281 ILE I N   1 
ATOM   11043 C  CA  . ILE E  1 282 ? -45.217  -42.504 24.899  1.00 25.33  ? 281 ILE I CA  1 
ATOM   11044 C  C   . ILE E  1 282 ? -46.505  -42.292 24.096  1.00 22.32  ? 281 ILE I C   1 
ATOM   11045 O  O   . ILE E  1 282 ? -46.435  -41.887 22.941  1.00 24.28  ? 281 ILE I O   1 
ATOM   11046 C  CB  . ILE E  1 282 ? -44.232  -43.437 24.185  1.00 24.72  ? 281 ILE I CB  1 
ATOM   11047 C  CG1 . ILE E  1 282 ? -44.831  -44.817 23.907  1.00 26.72  ? 281 ILE I CG1 1 
ATOM   11048 C  CG2 . ILE E  1 282 ? -42.937  -43.501 24.985  1.00 28.54  ? 281 ILE I CG2 1 
ATOM   11049 C  CD1 . ILE E  1 282 ? -43.888  -45.760 23.191  1.00 27.62  ? 281 ILE I CD1 1 
ATOM   11050 N  N   . ILE E  1 283 ? -47.659  -42.587 24.686  1.00 22.80  ? 282 ILE I N   1 
ATOM   11051 C  CA  . ILE E  1 283 ? -48.947  -42.348 24.030  1.00 22.52  ? 282 ILE I CA  1 
ATOM   11052 C  C   . ILE E  1 283 ? -49.042  -40.844 23.760  1.00 22.28  ? 282 ILE I C   1 
ATOM   11053 O  O   . ILE E  1 283 ? -48.824  -40.044 24.648  1.00 22.45  ? 282 ILE I O   1 
ATOM   11054 C  CB  . ILE E  1 283 ? -50.138  -42.836 24.886  1.00 24.23  ? 282 ILE I CB  1 
ATOM   11055 C  CG1 . ILE E  1 283 ? -50.075  -44.331 25.205  1.00 26.16  ? 282 ILE I CG1 1 
ATOM   11056 C  CG2 . ILE E  1 283 ? -51.477  -42.443 24.247  1.00 22.71  ? 282 ILE I CG2 1 
ATOM   11057 C  CD1 . ILE E  1 283 ? -50.150  -45.241 24.022  1.00 26.55  ? 282 ILE I CD1 1 
ATOM   11058 N  N   . GLY E  1 284 ? -49.334  -40.475 22.512  1.00 21.84  ? 283 GLY I N   1 
ATOM   11059 C  CA  . GLY E  1 284 ? -49.486  -39.092 22.126  1.00 21.93  ? 283 GLY I CA  1 
ATOM   11060 C  C   . GLY E  1 284 ? -48.169  -38.389 21.846  1.00 23.45  ? 283 GLY I C   1 
ATOM   11061 O  O   . GLY E  1 284 ? -48.152  -37.175 21.629  1.00 22.60  ? 283 GLY I O   1 
ATOM   11062 N  N   . ARG E  1 285 ? -47.058  -39.136 21.845  1.00 23.02  ? 284 ARG I N   1 
ATOM   11063 C  CA  . ARG E  1 285 ? -45.774  -38.591 21.443  1.00 24.09  ? 284 ARG I CA  1 
ATOM   11064 C  C   . ARG E  1 285 ? -45.507  -39.064 20.008  1.00 24.17  ? 284 ARG I C   1 
ATOM   11065 O  O   . ARG E  1 285 ? -46.360  -39.738 19.405  1.00 24.38  ? 284 ARG I O   1 
ATOM   11066 C  CB  . ARG E  1 285 ? -44.730  -38.977 22.498  1.00 24.25  ? 284 ARG I CB  1 
ATOM   11067 C  CG  . ARG E  1 285 ? -45.154  -38.587 23.910  1.00 23.56  ? 284 ARG I CG  1 
ATOM   11068 C  CD  . ARG E  1 285 ? -44.022  -38.561 24.918  1.00 25.75  ? 284 ARG I CD  1 
ATOM   11069 N  NE  . ARG E  1 285 ? -44.510  -38.332 26.269  1.00 25.60  ? 284 ARG I NE  1 
ATOM   11070 C  CZ  . ARG E  1 285 ? -44.608  -37.146 26.859  1.00 25.56  ? 284 ARG I CZ  1 
ATOM   11071 N  NH1 . ARG E  1 285 ? -44.999  -37.086 28.119  1.00 24.28  ? 284 ARG I NH1 1 
ATOM   11072 N  NH2 . ARG E  1 285 ? -44.289  -36.039 26.212  1.00 24.85  ? 284 ARG I NH2 1 
ATOM   11073 N  N   . THR E  1 286 ? -44.369  -38.670 19.441  1.00 23.37  ? 285 THR I N   1 
ATOM   11074 C  CA  . THR E  1 286 ? -44.046  -38.958 18.026  1.00 25.37  ? 285 THR I CA  1 
ATOM   11075 C  C   . THR E  1 286 ? -42.925  -39.997 17.962  1.00 25.41  ? 285 THR I C   1 
ATOM   11076 O  O   . THR E  1 286 ? -41.876  -39.851 18.587  1.00 26.50  ? 285 THR I O   1 
ATOM   11077 C  CB  . THR E  1 286 ? -43.635  -37.696 17.248  1.00 26.41  ? 285 THR I CB  1 
ATOM   11078 O  OG1 . THR E  1 286 ? -44.714  -36.759 17.222  1.00 26.81  ? 285 THR I OG1 1 
ATOM   11079 C  CG2 . THR E  1 286 ? -43.262  -37.984 15.810  1.00 25.76  ? 285 THR I CG2 1 
ATOM   11080 N  N   . LEU E  1 287 ? -43.145  -41.037 17.169  1.00 24.51  ? 286 LEU I N   1 
ATOM   11081 C  CA  . LEU E  1 287 ? -42.094  -41.976 16.854  1.00 25.24  ? 286 LEU I CA  1 
ATOM   11082 C  C   . LEU E  1 287 ? -41.438  -41.486 15.562  1.00 26.26  ? 286 LEU I C   1 
ATOM   11083 O  O   . LEU E  1 287 ? -42.153  -41.138 14.615  1.00 25.59  ? 286 LEU I O   1 
ATOM   11084 C  CB  . LEU E  1 287 ? -42.713  -43.359 16.672  1.00 25.53  ? 286 LEU I CB  1 
ATOM   11085 C  CG  . LEU E  1 287 ? -41.739  -44.494 16.390  1.00 26.39  ? 286 LEU I CG  1 
ATOM   11086 C  CD1 . LEU E  1 287 ? -40.816  -44.736 17.581  1.00 25.53  ? 286 LEU I CD1 1 
ATOM   11087 C  CD2 . LEU E  1 287 ? -42.519  -45.747 16.028  1.00 26.54  ? 286 LEU I CD2 1 
ATOM   11088 N  N   . VAL E  1 288 ? -40.104  -41.482 15.527  1.00 25.43  ? 287 VAL I N   1 
ATOM   11089 C  CA  . VAL E  1 288 ? -39.336  -40.931 14.410  1.00 26.30  ? 287 VAL I CA  1 
ATOM   11090 C  C   . VAL E  1 288 ? -38.291  -41.969 13.959  1.00 29.00  ? 287 VAL I C   1 
ATOM   11091 O  O   . VAL E  1 288 ? -37.561  -42.515 14.778  1.00 27.79  ? 287 VAL I O   1 
ATOM   11092 C  CB  . VAL E  1 288 ? -38.650  -39.616 14.812  1.00 27.59  ? 287 VAL I CB  1 
ATOM   11093 C  CG1 . VAL E  1 288 ? -37.777  -39.098 13.688  1.00 29.94  ? 287 VAL I CG1 1 
ATOM   11094 C  CG2 . VAL E  1 288 ? -39.645  -38.556 15.257  1.00 29.66  ? 287 VAL I CG2 1 
ATOM   11095 N  N   . VAL E  1 289 ? -38.207  -42.199 12.645  1.00 30.52  ? 288 VAL I N   1 
ATOM   11096 C  CA  . VAL E  1 289 ? -37.100  -42.924 12.053  1.00 30.77  ? 288 VAL I CA  1 
ATOM   11097 C  C   . VAL E  1 289 ? -36.211  -41.932 11.293  1.00 32.10  ? 288 VAL I C   1 
ATOM   11098 O  O   . VAL E  1 289 ? -36.711  -41.084 10.523  1.00 30.65  ? 288 VAL I O   1 
ATOM   11099 C  CB  . VAL E  1 289 ? -37.582  -44.083 11.163  1.00 31.23  ? 288 VAL I CB  1 
ATOM   11100 C  CG1 . VAL E  1 289 ? -38.381  -43.606 9.965   1.00 32.46  ? 288 VAL I CG1 1 
ATOM   11101 C  CG2 . VAL E  1 289 ? -36.408  -44.936 10.720  1.00 32.38  ? 288 VAL I CG2 1 
ATOM   11102 N  N   . HIS E  1 290 ? -34.893  -42.064 11.513  1.00 29.67  ? 289 HIS I N   1 
ATOM   11103 C  CA  . HIS E  1 290 ? -33.880  -41.107 11.069  1.00 31.94  ? 289 HIS I CA  1 
ATOM   11104 C  C   . HIS E  1 290 ? -33.082  -41.603 9.841   1.00 31.88  ? 289 HIS I C   1 
ATOM   11105 O  O   . HIS E  1 290 ? -33.026  -42.813 9.517   1.00 32.74  ? 289 HIS I O   1 
ATOM   11106 C  CB  . HIS E  1 290 ? -32.929  -40.805 12.226  1.00 31.48  ? 289 HIS I CB  1 
ATOM   11107 C  CG  . HIS E  1 290 ? -33.465  -39.856 13.243  1.00 31.25  ? 289 HIS I CG  1 
ATOM   11108 N  ND1 . HIS E  1 290 ? -33.305  -38.497 13.113  1.00 34.05  ? 289 HIS I ND1 1 
ATOM   11109 C  CD2 . HIS E  1 290 ? -34.091  -40.056 14.422  1.00 31.50  ? 289 HIS I CD2 1 
ATOM   11110 C  CE1 . HIS E  1 290 ? -33.833  -37.887 14.158  1.00 33.56  ? 289 HIS I CE1 1 
ATOM   11111 N  NE2 . HIS E  1 290 ? -34.307  -38.816 14.995  1.00 34.26  ? 289 HIS I NE2 1 
ATOM   11112 N  N   . GLU E  1 291 ? -32.448  -40.626 9.195   1.00 34.54  ? 290 GLU I N   1 
ATOM   11113 C  CA  . GLU E  1 291 ? -31.592  -40.754 7.995   1.00 37.63  ? 290 GLU I CA  1 
ATOM   11114 C  C   . GLU E  1 291 ? -30.405  -41.699 8.239   1.00 37.98  ? 290 GLU I C   1 
ATOM   11115 O  O   . GLU E  1 291 ? -30.172  -42.617 7.456   1.00 38.30  ? 290 GLU I O   1 
ATOM   11116 C  CB  . GLU E  1 291 ? -31.078  -39.357 7.664   1.00 44.45  ? 290 GLU I CB  1 
ATOM   11117 C  CG  . GLU E  1 291 ? -30.205  -39.267 6.432   1.00 47.77  ? 290 GLU I CG  1 
ATOM   11118 C  CD  . GLU E  1 291 ? -29.730  -37.842 6.225   1.00 54.13  ? 290 GLU I CD  1 
ATOM   11119 O  OE1 . GLU E  1 291 ? -29.623  -37.432 5.057   1.00 67.38  ? 290 GLU I OE1 1 
ATOM   11120 O  OE2 . GLU E  1 291 ? -29.495  -37.139 7.240   1.00 50.51  ? 290 GLU I OE2 1 
ATOM   11121 N  N   . LYS E  1 292 ? -29.699  -41.484 9.351   1.00 38.06  ? 291 LYS I N   1 
ATOM   11122 C  CA  . LYS E  1 292 ? -28.427  -42.144 9.654   1.00 41.75  ? 291 LYS I CA  1 
ATOM   11123 C  C   . LYS E  1 292 ? -28.556  -42.967 10.935  1.00 40.70  ? 291 LYS I C   1 
ATOM   11124 O  O   . LYS E  1 292 ? -29.563  -42.881 11.651  1.00 38.62  ? 291 LYS I O   1 
ATOM   11125 C  CB  . LYS E  1 292 ? -27.314  -41.103 9.821   1.00 44.26  ? 291 LYS I CB  1 
ATOM   11126 C  CG  . LYS E  1 292 ? -27.277  -40.046 8.721   1.00 52.73  ? 291 LYS I CG  1 
ATOM   11127 C  CD  . LYS E  1 292 ? -26.075  -39.135 8.746   1.00 57.54  ? 291 LYS I CD  1 
ATOM   11128 C  CE  . LYS E  1 292 ? -25.848  -38.493 10.095  1.00 64.45  ? 291 LYS I CE  1 
ATOM   11129 N  NZ  . LYS E  1 292 ? -24.978  -37.299 9.980   1.00 71.27  ? 291 LYS I NZ  1 
ATOM   11130 N  N   . ALA E  1 293 ? -27.514  -43.760 11.206  1.00 39.01  ? 292 ALA I N   1 
ATOM   11131 C  CA  . ALA E  1 293 ? -27.411  -44.554 12.417  1.00 40.13  ? 292 ALA I CA  1 
ATOM   11132 C  C   . ALA E  1 293 ? -27.337  -43.630 13.641  1.00 40.70  ? 292 ALA I C   1 
ATOM   11133 O  O   . ALA E  1 293 ? -26.803  -42.540 13.592  1.00 41.12  ? 292 ALA I O   1 
ATOM   11134 C  CB  . ALA E  1 293 ? -26.213  -45.471 12.343  1.00 41.34  ? 292 ALA I CB  1 
ATOM   11135 N  N   . ASP E  1 294 ? -27.936  -44.092 14.737  1.00 41.16  ? 293 ASP I N   1 
ATOM   11136 C  CA  . ASP E  1 294 ? -27.783  -43.494 16.032  1.00 43.79  ? 293 ASP I CA  1 
ATOM   11137 C  C   . ASP E  1 294 ? -26.513  -44.096 16.637  1.00 43.28  ? 293 ASP I C   1 
ATOM   11138 O  O   . ASP E  1 294 ? -26.457  -45.302 16.827  1.00 45.58  ? 293 ASP I O   1 
ATOM   11139 C  CB  . ASP E  1 294 ? -29.037  -43.771 16.868  1.00 46.21  ? 293 ASP I CB  1 
ATOM   11140 C  CG  . ASP E  1 294 ? -28.992  -43.293 18.310  1.00 48.65  ? 293 ASP I CG  1 
ATOM   11141 O  OD1 . ASP E  1 294 ? -27.939  -42.769 18.732  1.00 47.04  ? 293 ASP I OD1 1 
ATOM   11142 O  OD2 . ASP E  1 294 ? -30.014  -43.471 19.008  1.00 51.18  ? 293 ASP I OD2 1 
ATOM   11143 N  N   . ASP E  1 295 ? -25.506  -43.258 16.908  1.00 50.92  ? 294 ASP I N   1 
ATOM   11144 C  CA  . ASP E  1 295 ? -24.203  -43.740 17.455  1.00 60.67  ? 294 ASP I CA  1 
ATOM   11145 C  C   . ASP E  1 295 ? -24.337  -44.085 18.948  1.00 60.90  ? 294 ASP I C   1 
ATOM   11146 O  O   . ASP E  1 295 ? -23.362  -44.484 19.583  1.00 65.73  ? 294 ASP I O   1 
ATOM   11147 C  CB  . ASP E  1 295 ? -23.079  -42.724 17.225  1.00 58.86  ? 294 ASP I CB  1 
ATOM   11148 C  CG  . ASP E  1 295 ? -23.257  -41.401 17.953  1.00 61.53  ? 294 ASP I CG  1 
ATOM   11149 O  OD1 . ASP E  1 295 ? -22.629  -40.405 17.517  1.00 63.68  ? 294 ASP I OD1 1 
ATOM   11150 O  OD2 . ASP E  1 295 ? -24.016  -41.371 18.956  1.00 56.23  ? 294 ASP I OD2 1 
ATOM   11151 N  N   . LEU E  1 296 ? -25.536  -43.861 19.502  1.00 60.20  ? 295 LEU I N   1 
ATOM   11152 C  CA  . LEU E  1 296 ? -25.953  -44.271 20.844  1.00 60.76  ? 295 LEU I CA  1 
ATOM   11153 C  C   . LEU E  1 296 ? -25.189  -43.471 21.912  1.00 63.78  ? 295 LEU I C   1 
ATOM   11154 O  O   . LEU E  1 296 ? -24.934  -43.974 23.006  1.00 66.55  ? 295 LEU I O   1 
ATOM   11155 C  CB  . LEU E  1 296 ? -25.766  -45.785 21.000  1.00 61.16  ? 295 LEU I CB  1 
ATOM   11156 C  CG  . LEU E  1 296 ? -26.464  -46.653 19.949  1.00 62.58  ? 295 LEU I CG  1 
ATOM   11157 C  CD1 . LEU E  1 296 ? -26.267  -48.132 20.235  1.00 66.73  ? 295 LEU I CD1 1 
ATOM   11158 C  CD2 . LEU E  1 296 ? -27.949  -46.350 19.871  1.00 61.68  ? 295 LEU I CD2 1 
ATOM   11159 N  N   . GLY E  1 297 ? -24.874  -42.206 21.600  1.00 65.33  ? 296 GLY I N   1 
ATOM   11160 C  CA  . GLY E  1 297 ? -24.285  -41.260 22.546  1.00 67.76  ? 296 GLY I CA  1 
ATOM   11161 C  C   . GLY E  1 297 ? -22.810  -41.523 22.820  1.00 76.11  ? 296 GLY I C   1 
ATOM   11162 O  O   . GLY E  1 297 ? -22.301  -41.112 23.862  1.00 76.59  ? 296 GLY I O   1 
ATOM   11163 N  N   . LYS E  1 298 ? -22.124  -42.180 21.871  1.00 83.13  ? 297 LYS I N   1 
ATOM   11164 C  CA  . LYS E  1 298 ? -20.717  -42.606 22.008  1.00 84.35  ? 297 LYS I CA  1 
ATOM   11165 C  C   . LYS E  1 298 ? -19.899  -42.071 20.820  1.00 85.60  ? 297 LYS I C   1 
ATOM   11166 O  O   . LYS E  1 298 ? -18.977  -42.741 20.340  1.00 82.23  ? 297 LYS I O   1 
ATOM   11167 C  CB  . LYS E  1 298 ? -20.638  -44.137 22.093  1.00 84.24  ? 297 LYS I CB  1 
ATOM   11168 C  CG  . LYS E  1 298 ? -21.512  -44.786 23.163  1.00 83.23  ? 297 LYS I CG  1 
ATOM   11169 C  CD  . LYS E  1 298 ? -22.065  -46.138 22.766  1.00 83.41  ? 297 LYS I CD  1 
ATOM   11170 C  CE  . LYS E  1 298 ? -22.731  -46.893 23.900  1.00 84.29  ? 297 LYS I CE  1 
ATOM   11171 N  NZ  . LYS E  1 298 ? -23.818  -46.119 24.548  1.00 87.10  ? 297 LYS I NZ  1 
ATOM   11172 N  N   . GLY E  1 299 ? -20.241  -40.853 20.371  1.00 86.23  ? 298 GLY I N   1 
ATOM   11173 C  CA  . GLY E  1 299 ? -19.672  -40.222 19.173  1.00 84.77  ? 298 GLY I CA  1 
ATOM   11174 C  C   . GLY E  1 299 ? -18.554  -39.236 19.489  1.00 83.49  ? 298 GLY I C   1 
ATOM   11175 O  O   . GLY E  1 299 ? -17.853  -38.796 18.580  1.00 83.72  ? 298 GLY I O   1 
ATOM   11176 N  N   . GLY E  1 300 ? -18.402  -38.874 20.769  1.00 84.19  ? 299 GLY I N   1 
ATOM   11177 C  CA  . GLY E  1 300 ? -17.339  -37.971 21.229  1.00 88.95  ? 299 GLY I CA  1 
ATOM   11178 C  C   . GLY E  1 300 ? -17.510  -36.543 20.721  1.00 88.63  ? 299 GLY I C   1 
ATOM   11179 O  O   . GLY E  1 300 ? -16.519  -35.838 20.520  1.00 88.17  ? 299 GLY I O   1 
ATOM   11180 N  N   . ASN E  1 301 ? -18.767  -36.125 20.509  1.00 87.66  ? 300 ASN I N   1 
ATOM   11181 C  CA  . ASN E  1 301 ? -19.132  -34.725 20.222  1.00 83.69  ? 300 ASN I CA  1 
ATOM   11182 C  C   . ASN E  1 301 ? -20.452  -34.395 20.944  1.00 85.06  ? 300 ASN I C   1 
ATOM   11183 O  O   . ASN E  1 301 ? -21.087  -35.271 21.540  1.00 81.38  ? 300 ASN I O   1 
ATOM   11184 C  CB  . ASN E  1 301 ? -19.164  -34.435 18.714  1.00 80.57  ? 300 ASN I CB  1 
ATOM   11185 C  CG  . ASN E  1 301 ? -19.970  -35.423 17.894  1.00 82.16  ? 300 ASN I CG  1 
ATOM   11186 O  OD1 . ASN E  1 301 ? -19.549  -35.825 16.811  1.00 87.20  ? 300 ASN I OD1 1 
ATOM   11187 N  ND2 . ASN E  1 301 ? -21.139  -35.807 18.378  1.00 74.15  ? 300 ASN I ND2 1 
ATOM   11188 N  N   . GLU E  1 302 ? -20.852  -33.118 20.896  1.00 89.34  ? 301 GLU I N   1 
ATOM   11189 C  CA  . GLU E  1 302 ? -21.995  -32.608 21.656  1.00 92.12  ? 301 GLU I CA  1 
ATOM   11190 C  C   . GLU E  1 302 ? -23.312  -33.176 21.109  1.00 90.09  ? 301 GLU I C   1 
ATOM   11191 O  O   . GLU E  1 302 ? -24.185  -33.562 21.889  1.00 89.50  ? 301 GLU I O   1 
ATOM   11192 C  CB  . GLU E  1 302 ? -22.016  -31.078 21.631  1.00 95.92  ? 301 GLU I CB  1 
ATOM   11193 C  CG  . GLU E  1 302 ? -23.027  -30.483 22.595  1.00 104.70 ? 301 GLU I CG  1 
ATOM   11194 C  CD  . GLU E  1 302 ? -22.531  -29.277 23.375  1.00 114.04 ? 301 GLU I CD  1 
ATOM   11195 O  OE1 . GLU E  1 302 ? -22.477  -28.176 22.788  1.00 118.98 ? 301 GLU I OE1 1 
ATOM   11196 O  OE2 . GLU E  1 302 ? -22.197  -29.442 24.568  1.00 122.52 ? 301 GLU I OE2 1 
ATOM   11197 N  N   . GLU E  1 303 ? -23.450  -33.206 19.776  1.00 84.91  ? 302 GLU I N   1 
ATOM   11198 C  CA  . GLU E  1 303 ? -24.646  -33.738 19.097  1.00 83.76  ? 302 GLU I CA  1 
ATOM   11199 C  C   . GLU E  1 303 ? -24.892  -35.205 19.497  1.00 79.21  ? 302 GLU I C   1 
ATOM   11200 O  O   . GLU E  1 303 ? -26.053  -35.637 19.559  1.00 72.77  ? 302 GLU I O   1 
ATOM   11201 C  CB  . GLU E  1 303 ? -24.526  -33.622 17.570  1.00 87.09  ? 302 GLU I CB  1 
ATOM   11202 C  CG  . GLU E  1 303 ? -25.165  -32.370 16.985  1.00 89.82  ? 302 GLU I CG  1 
ATOM   11203 C  CD  . GLU E  1 303 ? -26.675  -32.256 17.137  1.00 88.70  ? 302 GLU I CD  1 
ATOM   11204 O  OE1 . GLU E  1 303 ? -27.351  -33.300 17.274  1.00 84.78  ? 302 GLU I OE1 1 
ATOM   11205 O  OE2 . GLU E  1 303 ? -27.175  -31.115 17.118  1.00 95.23  ? 302 GLU I OE2 1 
ATOM   11206 N  N   . SER E  1 304 ? -23.817  -35.962 19.768  1.00 69.74  ? 303 SER I N   1 
ATOM   11207 C  CA  . SER E  1 304 ? -23.911  -37.394 20.111  1.00 69.03  ? 303 SER I CA  1 
ATOM   11208 C  C   . SER E  1 304 ? -24.725  -37.584 21.402  1.00 70.96  ? 303 SER I C   1 
ATOM   11209 O  O   . SER E  1 304 ? -25.545  -38.506 21.504  1.00 68.11  ? 303 SER I O   1 
ATOM   11210 C  CB  . SER E  1 304 ? -22.545  -38.025 20.232  1.00 65.19  ? 303 SER I CB  1 
ATOM   11211 O  OG  . SER E  1 304 ? -22.656  -39.401 20.561  1.00 54.21  ? 303 SER I OG  1 
ATOM   11212 N  N   . THR E  1 305 ? -24.506  -36.680 22.365  1.00 67.18  ? 304 THR I N   1 
ATOM   11213 C  CA  . THR E  1 305 ? -25.145  -36.707 23.678  1.00 68.57  ? 304 THR I CA  1 
ATOM   11214 C  C   . THR E  1 305 ? -26.559  -36.098 23.613  1.00 69.03  ? 304 THR I C   1 
ATOM   11215 O  O   . THR E  1 305 ? -27.260  -36.084 24.631  1.00 66.87  ? 304 THR I O   1 
ATOM   11216 C  CB  . THR E  1 305 ? -24.269  -35.970 24.702  1.00 69.54  ? 304 THR I CB  1 
ATOM   11217 O  OG1 . THR E  1 305 ? -24.263  -34.581 24.358  1.00 68.73  ? 304 THR I OG1 1 
ATOM   11218 C  CG2 . THR E  1 305 ? -22.849  -36.495 24.757  1.00 69.46  ? 304 THR I CG2 1 
ATOM   11219 N  N   . LYS E  1 306 ? -26.962  -35.599 22.431  1.00 71.29  ? 305 LYS I N   1 
ATOM   11220 C  CA  . LYS E  1 306 ? -28.261  -34.932 22.181  1.00 73.38  ? 305 LYS I CA  1 
ATOM   11221 C  C   . LYS E  1 306 ? -29.174  -35.844 21.344  1.00 72.23  ? 305 LYS I C   1 
ATOM   11222 O  O   . LYS E  1 306 ? -30.296  -36.155 21.763  1.00 62.41  ? 305 LYS I O   1 
ATOM   11223 C  CB  . LYS E  1 306 ? -28.038  -33.613 21.431  1.00 79.25  ? 305 LYS I CB  1 
ATOM   11224 C  CG  . LYS E  1 306 ? -28.991  -32.471 21.766  1.00 86.88  ? 305 LYS I CG  1 
ATOM   11225 C  CD  . LYS E  1 306 ? -28.978  -32.031 23.224  1.00 92.35  ? 305 LYS I CD  1 
ATOM   11226 C  CE  . LYS E  1 306 ? -27.612  -32.061 23.882  1.00 93.52  ? 305 LYS I CE  1 
ATOM   11227 N  NZ  . LYS E  1 306 ? -26.639  -31.183 23.191  1.00 96.93  ? 305 LYS I NZ  1 
ATOM   11228 N  N   . THR E  1 307 ? -28.674  -36.236 20.158  1.00 70.27  ? 306 THR I N   1 
ATOM   11229 C  CA  . THR E  1 307 ? -29.446  -36.906 19.078  1.00 67.70  ? 306 THR I CA  1 
ATOM   11230 C  C   . THR E  1 307 ? -28.818  -38.240 18.644  1.00 60.84  ? 306 THR I C   1 
ATOM   11231 O  O   . THR E  1 307 ? -29.443  -38.989 17.893  1.00 59.19  ? 306 THR I O   1 
ATOM   11232 C  CB  . THR E  1 307 ? -29.547  -36.025 17.819  1.00 70.89  ? 306 THR I CB  1 
ATOM   11233 O  OG1 . THR E  1 307 ? -28.245  -35.822 17.260  1.00 63.82  ? 306 THR I OG1 1 
ATOM   11234 C  CG2 . THR E  1 307 ? -30.197  -34.683 18.083  1.00 70.37  ? 306 THR I CG2 1 
ATOM   11235 N  N   . GLY E  1 308 ? -27.581  -38.517 19.088  1.00 61.62  ? 307 GLY I N   1 
ATOM   11236 C  CA  . GLY E  1 308 ? -26.784  -39.660 18.609  1.00 56.16  ? 307 GLY I CA  1 
ATOM   11237 C  C   . GLY E  1 308 ? -26.338  -39.501 17.160  1.00 55.02  ? 307 GLY I C   1 
ATOM   11238 O  O   . GLY E  1 308 ? -25.979  -40.499 16.516  1.00 51.37  ? 307 GLY I O   1 
ATOM   11239 N  N   . ASN E  1 309 ? -26.350  -38.244 16.672  1.00 53.38  ? 308 ASN I N   1 
ATOM   11240 C  CA  . ASN E  1 309 ? -25.947  -37.830 15.315  1.00 52.45  ? 308 ASN I CA  1 
ATOM   11241 C  C   . ASN E  1 309 ? -26.806  -38.528 14.252  1.00 50.33  ? 308 ASN I C   1 
ATOM   11242 O  O   . ASN E  1 309 ? -26.308  -38.821 13.157  1.00 50.54  ? 308 ASN I O   1 
ATOM   11243 C  CB  . ASN E  1 309 ? -24.453  -38.085 15.051  1.00 55.09  ? 308 ASN I CB  1 
ATOM   11244 C  CG  . ASN E  1 309 ? -23.544  -37.188 15.868  1.00 55.77  ? 308 ASN I CG  1 
ATOM   11245 O  OD1 . ASN E  1 309 ? -23.496  -35.978 15.653  1.00 60.56  ? 308 ASN I OD1 1 
ATOM   11246 N  ND2 . ASN E  1 309 ? -22.835  -37.766 16.823  1.00 54.26  ? 308 ASN I ND2 1 
ATOM   11247 N  N   . ALA E  1 310 ? -28.098  -38.758 14.539  1.00 49.02  ? 309 ALA I N   1 
ATOM   11248 C  CA  . ALA E  1 310 ? -28.920  -39.649 13.688  1.00 46.47  ? 309 ALA I CA  1 
ATOM   11249 C  C   . ALA E  1 310 ? -29.424  -38.918 12.429  1.00 42.39  ? 309 ALA I C   1 
ATOM   11250 O  O   . ALA E  1 310 ? -30.000  -39.540 11.522  1.00 40.50  ? 309 ALA I O   1 
ATOM   11251 C  CB  . ALA E  1 310 ? -30.052  -40.254 14.491  1.00 45.55  ? 309 ALA I CB  1 
ATOM   11252 N  N   . GLY E  1 311 ? -29.209  -37.604 12.357  1.00 41.52  ? 310 GLY I N   1 
ATOM   11253 C  CA  . GLY E  1 311 ? -29.499  -36.863 11.136  1.00 42.01  ? 310 GLY I CA  1 
ATOM   11254 C  C   . GLY E  1 311 ? -30.986  -36.577 11.023  1.00 44.83  ? 310 GLY I C   1 
ATOM   11255 O  O   . GLY E  1 311 ? -31.718  -36.646 12.014  1.00 43.48  ? 310 GLY I O   1 
ATOM   11256 N  N   . SER E  1 312 ? -31.434  -36.270 9.807   1.00 40.93  ? 311 SER I N   1 
ATOM   11257 C  CA  . SER E  1 312 ? -32.756  -35.750 9.596   1.00 41.26  ? 311 SER I CA  1 
ATOM   11258 C  C   . SER E  1 312 ? -33.811  -36.838 9.844   1.00 38.04  ? 311 SER I C   1 
ATOM   11259 O  O   . SER E  1 312 ? -33.512  -38.041 9.937   1.00 37.24  ? 311 SER I O   1 
ATOM   11260 C  CB  . SER E  1 312 ? -32.879  -35.158 8.217   1.00 45.03  ? 311 SER I CB  1 
ATOM   11261 O  OG  . SER E  1 312 ? -32.881  -36.177 7.237   1.00 47.00  ? 311 SER I OG  1 
ATOM   11262 N  N   . ARG E  1 313 ? -35.055  -36.368 9.981   1.00 37.34  ? 312 ARG I N   1 
ATOM   11263 C  CA  . ARG E  1 313 ? -36.210  -37.173 10.331  1.00 34.19  ? 312 ARG I CA  1 
ATOM   11264 C  C   . ARG E  1 313 ? -36.913  -37.542 9.026   1.00 34.28  ? 312 ARG I C   1 
ATOM   11265 O  O   . ARG E  1 313 ? -37.494  -36.684 8.366   1.00 37.26  ? 312 ARG I O   1 
ATOM   11266 C  CB  . ARG E  1 313 ? -37.116  -36.371 11.278  1.00 33.18  ? 312 ARG I CB  1 
ATOM   11267 C  CG  . ARG E  1 313 ? -36.367  -35.796 12.469  1.00 32.09  ? 312 ARG I CG  1 
ATOM   11268 C  CD  . ARG E  1 313 ? -37.103  -34.713 13.216  1.00 32.88  ? 312 ARG I CD  1 
ATOM   11269 N  NE  . ARG E  1 313 ? -36.328  -34.321 14.383  1.00 33.06  ? 312 ARG I NE  1 
ATOM   11270 C  CZ  . ARG E  1 313 ? -36.798  -33.658 15.433  1.00 36.25  ? 312 ARG I CZ  1 
ATOM   11271 N  NH1 . ARG E  1 313 ? -35.953  -33.248 16.364  1.00 32.35  ? 312 ARG I NH1 1 
ATOM   11272 N  NH2 . ARG E  1 313 ? -38.100  -33.409 15.552  1.00 31.62  ? 312 ARG I NH2 1 
ATOM   11273 N  N   . LEU E  1 314 ? -36.852  -38.824 8.674   1.00 30.46  ? 313 LEU I N   1 
ATOM   11274 C  CA  . LEU E  1 314 ? -37.321  -39.333 7.390   1.00 30.68  ? 313 LEU I CA  1 
ATOM   11275 C  C   . LEU E  1 314 ? -38.841  -39.549 7.401   1.00 31.34  ? 313 LEU I C   1 
ATOM   11276 O  O   . LEU E  1 314 ? -39.530  -39.325 6.414   1.00 28.67  ? 313 LEU I O   1 
ATOM   11277 C  CB  . LEU E  1 314 ? -36.599  -40.663 7.151   1.00 34.40  ? 313 LEU I CB  1 
ATOM   11278 C  CG  . LEU E  1 314 ? -35.391  -40.634 6.218   1.00 39.13  ? 313 LEU I CG  1 
ATOM   11279 C  CD1 . LEU E  1 314 ? -34.504  -39.434 6.463   1.00 41.39  ? 313 LEU I CD1 1 
ATOM   11280 C  CD2 . LEU E  1 314 ? -34.592  -41.920 6.344   1.00 40.13  ? 313 LEU I CD2 1 
ATOM   11281 N  N   . ALA E  1 315 ? -39.342  -40.129 8.489   1.00 29.13  ? 314 ALA I N   1 
ATOM   11282 C  CA  . ALA E  1 315 ? -40.778  -40.358 8.670   1.00 28.10  ? 314 ALA I CA  1 
ATOM   11283 C  C   . ALA E  1 315 ? -41.084  -40.347 10.172  1.00 27.45  ? 314 ALA I C   1 
ATOM   11284 O  O   . ALA E  1 315 ? -40.173  -40.550 11.028  1.00 26.17  ? 314 ALA I O   1 
ATOM   11285 C  CB  . ALA E  1 315 ? -41.215  -41.648 8.034   1.00 27.94  ? 314 ALA I CB  1 
ATOM   11286 N  N   . CYS E  1 316 ? -42.345  -40.039 10.479  1.00 26.22  ? 315 CYS I N   1 
ATOM   11287 C  CA  . CYS E  1 316 ? -42.806  -40.024 11.842  1.00 26.76  ? 315 CYS I CA  1 
ATOM   11288 C  C   . CYS E  1 316 ? -44.322  -40.218 11.887  1.00 26.28  ? 315 CYS I C   1 
ATOM   11289 O  O   . CYS E  1 316 ? -45.020  -40.206 10.860  1.00 25.17  ? 315 CYS I O   1 
ATOM   11290 C  CB  . CYS E  1 316 ? -42.414  -38.727 12.528  1.00 29.64  ? 315 CYS I CB  1 
ATOM   11291 S  SG  . CYS E  1 316 ? -43.134  -37.271 11.736  1.00 34.25  ? 315 CYS I SG  1 
ATOM   11292 N  N   . GLY E  1 317 ? -44.807  -40.425 13.102  1.00 25.11  ? 316 GLY I N   1 
ATOM   11293 C  CA  . GLY E  1 317 ? -46.235  -40.540 13.379  1.00 26.06  ? 316 GLY I CA  1 
ATOM   11294 C  C   . GLY E  1 317 ? -46.483  -40.366 14.857  1.00 26.08  ? 316 GLY I C   1 
ATOM   11295 O  O   . GLY E  1 317 ? -45.572  -40.604 15.672  1.00 24.79  ? 316 GLY I O   1 
ATOM   11296 N  N   . VAL E  1 318 ? -47.708  -39.959 15.193  1.00 24.44  ? 317 VAL I N   1 
ATOM   11297 C  CA  . VAL E  1 318 ? -48.167  -39.893 16.576  1.00 24.43  ? 317 VAL I CA  1 
ATOM   11298 C  C   . VAL E  1 318 ? -48.539  -41.309 17.021  1.00 22.71  ? 317 VAL I C   1 
ATOM   11299 O  O   . VAL E  1 318 ? -49.183  -42.055 16.291  1.00 24.09  ? 317 VAL I O   1 
ATOM   11300 C  CB  . VAL E  1 318 ? -49.359  -38.925 16.716  1.00 26.24  ? 317 VAL I CB  1 
ATOM   11301 C  CG1 . VAL E  1 318 ? -49.823  -38.797 18.159  1.00 25.76  ? 317 VAL I CG1 1 
ATOM   11302 C  CG2 . VAL E  1 318 ? -49.022  -37.560 16.144  1.00 26.76  ? 317 VAL I CG2 1 
ATOM   11303 N  N   . ILE E  1 319 ? -48.101  -41.667 18.222  1.00 22.75  ? 318 ILE I N   1 
ATOM   11304 C  CA  . ILE E  1 319 ? -48.374  -42.937 18.798  1.00 24.24  ? 318 ILE I CA  1 
ATOM   11305 C  C   . ILE E  1 319 ? -49.765  -42.885 19.429  1.00 23.52  ? 318 ILE I C   1 
ATOM   11306 O  O   . ILE E  1 319 ? -50.017  -42.104 20.362  1.00 22.98  ? 318 ILE I O   1 
ATOM   11307 C  CB  . ILE E  1 319 ? -47.289  -43.302 19.825  1.00 25.40  ? 318 ILE I CB  1 
ATOM   11308 C  CG1 . ILE E  1 319 ? -45.912  -43.347 19.152  1.00 26.10  ? 318 ILE I CG1 1 
ATOM   11309 C  CG2 . ILE E  1 319 ? -47.644  -44.602 20.540  1.00 24.77  ? 318 ILE I CG2 1 
ATOM   11310 C  CD1 . ILE E  1 319 ? -44.750  -43.215 20.109  1.00 27.83  ? 318 ILE I CD1 1 
ATOM   11311 N  N   . GLY E  1 320 ? -50.649  -43.729 18.917  1.00 21.38  ? 319 GLY I N   1 
ATOM   11312 C  CA  . GLY E  1 320 ? -52.036  -43.738 19.318  1.00 24.84  ? 319 GLY I CA  1 
ATOM   11313 C  C   . GLY E  1 320 ? -52.432  -45.040 19.978  1.00 25.67  ? 319 GLY I C   1 
ATOM   11314 O  O   . GLY E  1 320 ? -51.796  -46.086 19.784  1.00 25.51  ? 319 GLY I O   1 
ATOM   11315 N  N   . ILE E  1 321 ? -53.517  -44.962 20.734  1.00 24.82  ? 320 ILE I N   1 
ATOM   11316 C  CA  . ILE E  1 321 ? -54.115  -46.095 21.405  1.00 26.01  ? 320 ILE I CA  1 
ATOM   11317 C  C   . ILE E  1 321 ? -54.691  -47.021 20.331  1.00 25.96  ? 320 ILE I C   1 
ATOM   11318 O  O   . ILE E  1 321 ? -55.416  -46.573 19.445  1.00 25.32  ? 320 ILE I O   1 
ATOM   11319 C  CB  . ILE E  1 321 ? -55.175  -45.593 22.416  1.00 25.44  ? 320 ILE I CB  1 
ATOM   11320 C  CG1 . ILE E  1 321 ? -54.528  -44.729 23.501  1.00 26.63  ? 320 ILE I CG1 1 
ATOM   11321 C  CG2 . ILE E  1 321 ? -55.977  -46.747 23.006  1.00 26.76  ? 320 ILE I CG2 1 
ATOM   11322 C  CD1 . ILE E  1 321 ? -55.494  -43.889 24.310  1.00 27.43  ? 320 ILE I CD1 1 
ATOM   11323 N  N   . ALA E  1 322 ? -54.374  -48.314 20.415  1.00 25.22  ? 321 ALA I N   1 
ATOM   11324 C  CA  . ALA E  1 322 ? -54.855  -49.328 19.444  1.00 27.84  ? 321 ALA I CA  1 
ATOM   11325 C  C   . ALA E  1 322 ? -55.918  -50.193 20.137  1.00 29.83  ? 321 ALA I C   1 
ATOM   11326 O  O   . ALA E  1 322 ? -55.900  -50.299 21.350  1.00 37.58  ? 321 ALA I O   1 
ATOM   11327 C  CB  . ALA E  1 322 ? -53.685  -50.161 18.974  1.00 27.22  ? 321 ALA I CB  1 
ATOM   11328 N  N   . GLN E  1 323 ? -56.764  -50.890 19.384  1.00 39.60  ? 322 GLN I N   1 
ATOM   11329 C  CA  . GLN E  1 323 ? -57.704  -51.837 20.036  1.00 48.28  ? 322 GLN I CA  1 
ATOM   11330 C  C   . GLN E  1 323 ? -56.940  -53.065 20.525  1.00 54.85  ? 322 GLN I C   1 
ATOM   11331 O  O   . GLN E  1 323 ? -56.179  -53.593 19.703  1.00 56.54  ? 322 GLN I O   1 
ATOM   11332 C  CB  . GLN E  1 323 ? -58.824  -52.321 19.124  1.00 50.63  ? 322 GLN I CB  1 
ATOM   11333 C  CG  . GLN E  1 323 ? -59.780  -53.269 19.855  1.00 59.10  ? 322 GLN I CG  1 
ATOM   11334 C  CD  . GLN E  1 323 ? -61.201  -53.285 19.330  1.00 61.68  ? 322 GLN I CD  1 
ATOM   11335 O  OE1 . GLN E  1 323 ? -61.447  -53.409 18.131  1.00 63.80  ? 322 GLN I OE1 1 
ATOM   11336 N  NE2 . GLN E  1 323 ? -62.161  -53.170 20.235  1.00 64.88  ? 322 GLN I NE2 1 
ATOM   11337 O  OXT . GLN E  1 323 ? -57.098  -53.502 21.686  1.00 54.44  ? 322 GLN I OXT 1 
HETATM 11338 ZN ZN  . ZN  F  2 .   ? -63.790  -44.105 96.181  0.30 49.75  ? 401 ZN  A ZN  1 
HETATM 11339 CU CU  A CU  G  3 .   ? -66.862  -42.651 90.467  0.50 37.61  ? 402 CU  A CU  1 
HETATM 11340 CU CU  B CU  G  3 .   ? -66.235  -42.127 90.794  0.30 39.19  ? 402 CU  A CU  1 
HETATM 11341 ZN ZN  . ZN  H  2 .   ? -103.003 -43.301 93.192  0.80 30.23  ? 403 ZN  A ZN  1 
HETATM 11342 CU CU  A CU  I  3 .   ? -99.026  -41.644 88.228  0.85 31.93  ? 404 CU  A CU  1 
HETATM 11343 CU CU  B CU  I  3 .   ? -100.283 -42.099 88.049  0.15 31.90  ? 404 CU  A CU  1 
HETATM 11344 ZN ZN  . ZN  J  2 .   ? -33.264  -16.996 28.457  0.50 54.64  ? 401 ZN  C ZN  1 
HETATM 11345 CU CU  . CU  K  3 .   ? -34.611  -14.313 22.666  0.75 49.93  ? 402 CU  C CU  1 
HETATM 11346 ZN ZN  . ZN  L  2 .   ? -53.810  16.434  25.154  0.50 33.28  ? 403 ZN  C ZN  1 
HETATM 11347 CU CU  A CU  M  3 .   ? -51.318  13.103  19.974  0.60 32.43  ? 404 CU  C CU  1 
HETATM 11348 CU CU  B CU  M  3 .   ? -52.269  13.470  20.100  0.20 30.69  ? 404 CU  C CU  1 
HETATM 11349 ZN ZN  . ZN  N  2 .   ? -66.028  20.073  48.778  0.40 29.46  ? 401 ZN  E ZN  1 
HETATM 11350 CU CU  A CU  O  3 .   ? -67.345  17.175  54.664  0.60 28.49  ? 402 CU  E CU  1 
HETATM 11351 CU CU  B CU  O  3 .   ? -66.379  17.491  54.317  0.30 25.57  ? 402 CU  E CU  1 
HETATM 11352 ZN ZN  . ZN  P  2 .   ? -85.853  -13.537 51.577  0.70 25.42  ? 403 ZN  E ZN  1 
HETATM 11353 CU CU  A CU  Q  3 .   ? -83.088  -10.513 56.886  0.70 23.11  ? 404 CU  E CU  1 
HETATM 11354 CU CU  B CU  Q  3 .   ? -84.038  -10.990 56.727  0.30 21.04  ? 404 CU  E CU  1 
HETATM 11355 C  C1  . MLI R  4 .   ? -80.420  7.308   35.732  0.50 51.04  ? 405 MLI E C1  1 
HETATM 11356 C  C2  . MLI R  4 .   ? -81.815  6.720   35.778  0.50 52.57  ? 405 MLI E C2  1 
HETATM 11357 C  C3  . MLI R  4 .   ? -79.393  6.292   35.270  0.50 50.88  ? 405 MLI E C3  1 
HETATM 11358 O  O6  . MLI R  4 .   ? -82.087  5.722   35.066  0.50 54.34  ? 405 MLI E O6  1 
HETATM 11359 O  O7  . MLI R  4 .   ? -82.651  7.258   36.536  0.50 49.54  ? 405 MLI E O7  1 
HETATM 11360 O  O8  . MLI R  4 .   ? -78.779  6.520   34.206  0.50 51.94  ? 405 MLI E O8  1 
HETATM 11361 O  O9  . MLI R  4 .   ? -79.170  5.269   35.956  0.50 50.49  ? 405 MLI E O9  1 
HETATM 11362 ZN ZN  . ZN  S  2 .   ? -66.170  -31.855 51.392  0.70 26.51  ? 401 ZN  G ZN  1 
HETATM 11363 CU CU  A CU  T  3 .   ? -64.707  -35.771 56.642  0.60 23.88  ? 402 CU  G CU  1 
HETATM 11364 CU CU  B CU  T  3 .   ? -64.618  -34.705 56.451  0.30 21.81  ? 402 CU  G CU  1 
HETATM 11365 ZN ZN  . ZN  U  2 .   ? -46.990  -65.744 48.513  0.55 34.68  ? 403 ZN  G ZN  1 
HETATM 11366 CU CU  A CU  V  3 .   ? -48.412  -62.852 54.400  0.50 27.07  ? 404 CU  G CU  1 
HETATM 11367 CU CU  B CU  V  3 .   ? -48.588  -63.880 54.042  0.30 28.65  ? 404 CU  G CU  1 
HETATM 11368 ZN ZN  . ZN  W  2 .   ? -71.065  -40.106 19.855  0.70 23.12  ? 401 ZN  I ZN  1 
HETATM 11369 CU CU  A CU  X  3 .   ? -67.052  -39.093 14.597  0.70 24.65  ? 402 CU  I CU  1 
HETATM 11370 CU CU  B CU  X  3 .   ? -67.906  -39.693 14.794  0.30 23.23  ? 402 CU  I CU  1 
HETATM 11371 ZN ZN  . ZN  Y  2 .   ? -32.021  -39.629 22.802  0.50 43.04  ? 403 ZN  I ZN  1 
HETATM 11372 CU CU  A CU  Z  3 .   ? -35.090  -39.168 16.849  0.60 35.94  ? 404 CU  I CU  1 
HETATM 11373 CU CU  B CU  Z  3 .   ? -34.409  -38.537 17.126  0.30 33.39  ? 404 CU  I CU  1 
HETATM 11374 O  O   . HOH AA 5 .   ? -65.652  -45.279 95.842  0.70 91.86  ? 501 HOH A O   1 
HETATM 11375 O  O   . HOH AA 5 .   ? -97.062  -42.350 105.182 1.00 45.60  ? 502 HOH A O   1 
HETATM 11376 O  O   . HOH AA 5 .   ? -71.520  -51.234 104.394 1.00 64.89  ? 503 HOH A O   1 
HETATM 11377 O  O   . HOH AA 5 .   ? -110.622 -37.243 96.294  1.00 59.50  ? 504 HOH A O   1 
HETATM 11378 O  O   . HOH AA 5 .   ? -67.105  -45.484 103.413 1.00 47.92  ? 505 HOH A O   1 
HETATM 11379 O  O   . HOH AA 5 .   ? -66.740  -57.156 79.988  1.00 45.85  ? 506 HOH A O   1 
HETATM 11380 O  O   . HOH AA 5 .   ? -80.430  -43.381 102.849 1.00 67.20  ? 507 HOH A O   1 
HETATM 11381 O  O   . HOH AA 5 .   ? -95.744  -22.296 91.603  1.00 66.38  ? 508 HOH A O   1 
HETATM 11382 O  O   . HOH AA 5 .   ? -48.804  -46.981 91.530  1.00 52.27  ? 509 HOH A O   1 
HETATM 11383 O  O   . HOH AA 5 .   ? -92.883  -45.917 78.920  1.00 53.26  ? 510 HOH A O   1 
HETATM 11384 O  O   . HOH AA 5 .   ? -105.392 -31.561 81.487  1.00 47.93  ? 511 HOH A O   1 
HETATM 11385 O  O   . HOH AA 5 .   ? -74.012  -56.232 101.792 1.00 53.32  ? 512 HOH A O   1 
HETATM 11386 O  O   . HOH AA 5 .   ? -76.937  -49.970 105.808 1.00 63.70  ? 513 HOH A O   1 
HETATM 11387 O  O   . HOH AA 5 .   ? -94.828  -19.531 81.923  1.00 48.86  ? 514 HOH A O   1 
HETATM 11388 O  O   . HOH AA 5 .   ? -67.213  -43.885 75.551  1.00 31.76  ? 515 HOH A O   1 
HETATM 11389 O  O   . HOH AA 5 .   ? -86.685  -38.687 114.048 1.00 48.60  ? 516 HOH A O   1 
HETATM 11390 O  O   . HOH AA 5 .   ? -91.771  -40.401 114.192 1.00 69.91  ? 517 HOH A O   1 
HETATM 11391 O  O   . HOH AA 5 .   ? -75.471  -41.817 77.008  1.00 32.98  ? 518 HOH A O   1 
HETATM 11392 O  O   . HOH AA 5 .   ? -89.076  -53.372 88.553  1.00 47.37  ? 519 HOH A O   1 
HETATM 11393 O  O   . HOH AA 5 .   ? -77.163  -32.593 95.497  1.00 46.33  ? 520 HOH A O   1 
HETATM 11394 O  O   . HOH AA 5 .   ? -62.796  -48.787 93.494  1.00 61.02  ? 521 HOH A O   1 
HETATM 11395 O  O   . HOH AA 5 .   ? -74.673  -45.806 72.594  1.00 48.23  ? 522 HOH A O   1 
HETATM 11396 O  O   . HOH AA 5 .   ? -88.700  -35.359 77.731  1.00 40.96  ? 523 HOH A O   1 
HETATM 11397 O  O   . HOH AA 5 .   ? -76.676  -50.526 70.384  1.00 46.50  ? 524 HOH A O   1 
HETATM 11398 O  O   . HOH AA 5 .   ? -87.383  -54.957 95.204  1.00 69.42  ? 525 HOH A O   1 
HETATM 11399 O  O   . HOH AA 5 .   ? -65.566  -49.010 71.737  1.00 40.53  ? 526 HOH A O   1 
HETATM 11400 O  O   . HOH AA 5 .   ? -85.661  -54.166 86.570  1.00 57.61  ? 527 HOH A O   1 
HETATM 11401 O  O   . HOH AA 5 .   ? -77.223  -39.897 76.202  1.00 66.52  ? 528 HOH A O   1 
HETATM 11402 O  O   . HOH AA 5 .   ? -71.826  -37.796 80.132  1.00 58.55  ? 529 HOH A O   1 
HETATM 11403 O  O   . HOH AA 5 .   ? -77.486  -45.245 102.583 1.00 53.88  ? 530 HOH A O   1 
HETATM 11404 O  O   . HOH AA 5 .   ? -100.991 -48.804 93.671  1.00 62.87  ? 531 HOH A O   1 
HETATM 11405 O  O   . HOH AA 5 .   ? -80.035  -30.307 93.751  1.00 47.67  ? 532 HOH A O   1 
HETATM 11406 O  O   . HOH AA 5 .   ? -82.039  -45.303 86.867  1.00 24.99  ? 533 HOH A O   1 
HETATM 11407 O  O   . HOH AA 5 .   ? -108.940 -37.357 83.746  1.00 33.12  ? 534 HOH A O   1 
HETATM 11408 O  O   . HOH AA 5 .   ? -117.792 -38.095 91.789  1.00 43.48  ? 535 HOH A O   1 
HETATM 11409 O  O   . HOH AA 5 .   ? -114.882 -42.838 92.290  1.00 28.37  ? 536 HOH A O   1 
HETATM 11410 O  O   . HOH AA 5 .   ? -100.557 -32.886 99.643  1.00 49.30  ? 537 HOH A O   1 
HETATM 11411 O  O   . HOH AA 5 .   ? -110.055 -42.506 97.655  1.00 44.79  ? 538 HOH A O   1 
HETATM 11412 O  O   . HOH AA 5 .   ? -95.254  -34.819 111.627 1.00 67.79  ? 539 HOH A O   1 
HETATM 11413 O  O   . HOH AA 5 .   ? -100.722 -46.738 100.355 1.00 31.57  ? 540 HOH A O   1 
HETATM 11414 O  O   . HOH AA 5 .   ? -97.461  -18.155 84.184  1.00 58.22  ? 541 HOH A O   1 
HETATM 11415 O  O   . HOH AA 5 .   ? -90.640  -31.712 107.399 1.00 46.14  ? 542 HOH A O   1 
HETATM 11416 O  O   . HOH AA 5 .   ? -109.133 -49.906 100.464 1.00 62.75  ? 543 HOH A O   1 
HETATM 11417 O  O   . HOH AA 5 .   ? -105.763 -48.675 93.991  1.00 38.34  ? 544 HOH A O   1 
HETATM 11418 O  O   . HOH AA 5 .   ? -60.491  -47.606 77.695  1.00 52.20  ? 545 HOH A O   1 
HETATM 11419 O  O   . HOH AA 5 .   ? -102.022 -44.952 101.756 1.00 37.32  ? 546 HOH A O   1 
HETATM 11420 O  O   . HOH AA 5 .   ? -62.859  -44.003 77.687  1.00 44.64  ? 547 HOH A O   1 
HETATM 11421 O  O   . HOH AA 5 .   ? -86.681  -37.615 106.312 1.00 52.54  ? 548 HOH A O   1 
HETATM 11422 O  O   . HOH AA 5 .   ? -92.166  -47.817 77.173  1.00 65.21  ? 549 HOH A O   1 
HETATM 11423 O  O   . HOH AA 5 .   ? -86.938  -40.882 82.922  1.00 58.82  ? 550 HOH A O   1 
HETATM 11424 O  O   . HOH AA 5 .   ? -94.041  -37.426 106.096 1.00 46.97  ? 551 HOH A O   1 
HETATM 11425 O  O   . HOH AA 5 .   ? -90.175  -29.433 104.878 1.00 60.28  ? 552 HOH A O   1 
HETATM 11426 O  O   . HOH AA 5 .   ? -90.288  -46.941 100.948 1.00 40.04  ? 553 HOH A O   1 
HETATM 11427 O  O   . HOH AA 5 .   ? -104.093 -30.160 79.650  1.00 56.02  ? 554 HOH A O   1 
HETATM 11428 O  O   . HOH AA 5 .   ? -102.562 -43.412 84.415  1.00 45.75  ? 555 HOH A O   1 
HETATM 11429 O  O   . HOH AA 5 .   ? -96.826  -32.433 76.151  1.00 36.75  ? 556 HOH A O   1 
HETATM 11430 O  O   . HOH AA 5 .   ? -101.659 -31.381 93.945  1.00 30.23  ? 557 HOH A O   1 
HETATM 11431 O  O   . HOH AA 5 .   ? -67.480  -58.399 98.593  1.00 63.13  ? 558 HOH A O   1 
HETATM 11432 O  O   . HOH AA 5 .   ? -83.766  -38.061 88.868  1.00 23.20  ? 559 HOH A O   1 
HETATM 11433 O  O   . HOH AA 5 .   ? -84.264  -27.696 77.638  1.00 52.63  ? 560 HOH A O   1 
HETATM 11434 O  O   . HOH AA 5 .   ? -79.679  -36.174 105.414 1.00 60.00  ? 561 HOH A O   1 
HETATM 11435 O  O   . HOH AA 5 .   ? -83.463  -54.911 84.246  1.00 48.02  ? 562 HOH A O   1 
HETATM 11436 O  O   . HOH AA 5 .   ? -79.848  -35.442 83.515  1.00 63.07  ? 563 HOH A O   1 
HETATM 11437 O  O   . HOH AA 5 .   ? -75.871  -38.847 74.154  1.00 42.73  ? 564 HOH A O   1 
HETATM 11438 O  O   . HOH AA 5 .   ? -96.613  -49.264 105.171 1.00 53.96  ? 565 HOH A O   1 
HETATM 11439 O  O   . HOH AA 5 .   ? -98.120  -23.576 75.461  1.00 40.91  ? 566 HOH A O   1 
HETATM 11440 O  O   . HOH AA 5 .   ? -102.367 -42.186 87.088  1.00 67.59  ? 567 HOH A O   1 
HETATM 11441 O  O   . HOH AA 5 .   ? -104.409 -38.509 104.158 1.00 58.22  ? 568 HOH A O   1 
HETATM 11442 O  O   . HOH AA 5 .   ? -110.847 -40.166 102.557 1.00 63.24  ? 569 HOH A O   1 
HETATM 11443 O  O   . HOH AA 5 .   ? -93.040  -36.144 77.090  1.00 33.47  ? 570 HOH A O   1 
HETATM 11444 O  O   . HOH AA 5 .   ? -100.620 -34.061 103.740 1.00 59.91  ? 571 HOH A O   1 
HETATM 11445 O  O   . HOH AA 5 .   ? -96.794  -50.073 96.381  1.00 39.65  ? 572 HOH A O   1 
HETATM 11446 O  O   . HOH AA 5 .   ? -84.253  -47.038 86.755  1.00 27.75  ? 573 HOH A O   1 
HETATM 11447 O  O   . HOH AA 5 .   ? -101.491 -33.724 77.808  1.00 33.19  ? 574 HOH A O   1 
HETATM 11448 O  O   . HOH AA 5 .   ? -81.838  -55.832 101.340 1.00 64.96  ? 575 HOH A O   1 
HETATM 11449 O  O   . HOH AA 5 .   ? -74.666  -32.198 94.508  1.00 55.91  ? 576 HOH A O   1 
HETATM 11450 O  O   . HOH AA 5 .   ? -61.078  -55.581 77.109  1.00 55.35  ? 577 HOH A O   1 
HETATM 11451 O  O   . HOH AA 5 .   ? -103.823 -38.002 93.492  1.00 31.86  ? 578 HOH A O   1 
HETATM 11452 O  O   . HOH AA 5 .   ? -92.037  -43.579 106.166 1.00 41.97  ? 579 HOH A O   1 
HETATM 11453 O  O   . HOH AA 5 .   ? -107.475 -42.382 80.855  1.00 64.86  ? 580 HOH A O   1 
HETATM 11454 O  O   . HOH AA 5 .   ? -67.485  -40.654 109.025 1.00 58.94  ? 581 HOH A O   1 
HETATM 11455 O  O   . HOH AA 5 .   ? -77.837  -48.982 109.013 1.00 66.23  ? 582 HOH A O   1 
HETATM 11456 O  O   . HOH AA 5 .   ? -112.945 -39.154 85.551  1.00 28.26  ? 583 HOH A O   1 
HETATM 11457 O  O   . HOH AA 5 .   ? -104.951 -49.193 85.332  1.00 55.56  ? 584 HOH A O   1 
HETATM 11458 O  O   . HOH AA 5 .   ? -86.913  -46.062 99.889  1.00 44.67  ? 585 HOH A O   1 
HETATM 11459 O  O   . HOH AA 5 .   ? -63.472  -36.833 79.138  1.00 69.69  ? 586 HOH A O   1 
HETATM 11460 O  O   . HOH AA 5 .   ? -59.581  -38.839 88.851  1.00 63.82  ? 587 HOH A O   1 
HETATM 11461 O  O   . HOH AA 5 .   ? -64.575  -39.242 95.903  1.00 52.51  ? 588 HOH A O   1 
HETATM 11462 O  O   . HOH AA 5 .   ? -91.359  -52.910 86.964  1.00 60.18  ? 589 HOH A O   1 
HETATM 11463 O  O   . HOH AA 5 .   ? -66.856  -35.789 84.477  1.00 48.92  ? 590 HOH A O   1 
HETATM 11464 O  O   . HOH AA 5 .   ? -83.399  -30.726 95.783  1.00 46.83  ? 591 HOH A O   1 
HETATM 11465 O  O   . HOH AA 5 .   ? -99.749  -52.550 97.236  1.00 68.26  ? 592 HOH A O   1 
HETATM 11466 O  O   . HOH AA 5 .   ? -81.636  -36.694 90.091  1.00 28.19  ? 593 HOH A O   1 
HETATM 11467 O  O   . HOH AA 5 .   ? -93.334  -25.324 77.989  1.00 34.60  ? 594 HOH A O   1 
HETATM 11468 O  O   . HOH AA 5 .   ? -96.611  -21.110 85.927  1.00 38.85  ? 595 HOH A O   1 
HETATM 11469 O  O   . HOH AA 5 .   ? -70.214  -49.979 72.032  1.00 38.75  ? 596 HOH A O   1 
HETATM 11470 O  O   . HOH AA 5 .   ? -105.686 -43.526 83.610  1.00 41.64  ? 597 HOH A O   1 
HETATM 11471 O  O   . HOH AA 5 .   ? -97.826  -23.331 86.934  1.00 30.19  ? 598 HOH A O   1 
HETATM 11472 O  O   . HOH AA 5 .   ? -90.722  -21.408 85.556  1.00 46.44  ? 599 HOH A O   1 
HETATM 11473 O  O   . HOH AA 5 .   ? -95.428  -22.892 75.095  1.00 54.33  ? 600 HOH A O   1 
HETATM 11474 O  O   . HOH AA 5 .   ? -97.857  -44.117 79.562  1.00 34.48  ? 601 HOH A O   1 
HETATM 11475 O  O   . HOH AA 5 .   ? -71.294  -40.920 77.352  1.00 29.96  ? 602 HOH A O   1 
HETATM 11476 O  O   . HOH AA 5 .   ? -111.046 -44.148 94.249  1.00 44.91  ? 603 HOH A O   1 
HETATM 11477 O  O   . HOH AA 5 .   ? -104.958 -27.580 77.155  1.00 49.97  ? 604 HOH A O   1 
HETATM 11478 O  O   . HOH AA 5 .   ? -66.576  -60.143 74.748  1.00 66.21  ? 605 HOH A O   1 
HETATM 11479 O  O   . HOH AA 5 .   ? -101.924 -47.220 90.297  1.00 31.10  ? 606 HOH A O   1 
HETATM 11480 O  O   . HOH AA 5 .   ? -107.422 -33.642 81.598  1.00 45.13  ? 607 HOH A O   1 
HETATM 11481 O  O   . HOH AA 5 .   ? -64.485  -40.022 90.982  1.00 56.93  ? 608 HOH A O   1 
HETATM 11482 O  O   . HOH AA 5 .   ? -79.728  -47.949 78.240  1.00 58.09  ? 609 HOH A O   1 
HETATM 11483 O  O   . HOH AA 5 .   ? -80.627  -44.898 100.770 1.00 54.11  ? 610 HOH A O   1 
HETATM 11484 O  O   . HOH AA 5 .   ? -106.388 -35.658 105.188 1.00 65.03  ? 611 HOH A O   1 
HETATM 11485 O  O   . HOH AA 5 .   ? -105.492 -49.525 104.631 1.00 61.55  ? 612 HOH A O   1 
HETATM 11486 O  O   . HOH AA 5 .   ? -68.896  -33.442 92.185  1.00 53.50  ? 613 HOH A O   1 
HETATM 11487 O  O   . HOH AA 5 .   ? -78.525  -39.932 83.675  1.00 54.47  ? 614 HOH A O   1 
HETATM 11488 O  O   . HOH AA 5 .   ? -91.832  -51.602 96.664  1.00 45.83  ? 615 HOH A O   1 
HETATM 11489 O  O   . HOH AA 5 .   ? -87.281  -48.288 106.341 1.00 50.10  ? 616 HOH A O   1 
HETATM 11490 O  O   . HOH AA 5 .   ? -85.047  -26.778 90.723  1.00 37.49  ? 617 HOH A O   1 
HETATM 11491 O  O   . HOH AA 5 .   ? -100.032 -28.921 98.870  1.00 44.83  ? 618 HOH A O   1 
HETATM 11492 O  O   . HOH AA 5 .   ? -100.977 -44.091 86.798  1.00 39.66  ? 619 HOH A O   1 
HETATM 11493 O  O   . HOH AA 5 .   ? -101.299 -19.016 82.027  1.00 47.61  ? 620 HOH A O   1 
HETATM 11494 O  O   . HOH AA 5 .   ? -81.510  -41.926 86.650  1.00 35.02  ? 621 HOH A O   1 
HETATM 11495 O  O   . HOH AA 5 .   ? -83.032  -55.336 88.735  1.00 46.94  ? 622 HOH A O   1 
HETATM 11496 O  O   . HOH AA 5 .   ? -89.140  -53.362 84.600  1.00 57.92  ? 623 HOH A O   1 
HETATM 11497 O  O   . HOH AA 5 .   ? -91.486  -43.385 78.846  1.00 45.84  ? 624 HOH A O   1 
HETATM 11498 O  O   . HOH AA 5 .   ? -99.002  -31.621 104.395 1.00 54.37  ? 625 HOH A O   1 
HETATM 11499 O  O   . HOH AA 5 .   ? -95.791  -20.471 74.818  1.00 50.30  ? 626 HOH A O   1 
HETATM 11500 O  O   . HOH AA 5 .   ? -98.943  -32.420 78.108  1.00 31.45  ? 627 HOH A O   1 
HETATM 11501 O  O   . HOH AA 5 .   ? -50.937  -47.774 90.331  1.00 61.04  ? 628 HOH A O   1 
HETATM 11502 O  O   . HOH AA 5 .   ? -97.055  -32.992 109.280 1.00 67.95  ? 629 HOH A O   1 
HETATM 11503 O  O   . HOH AA 5 .   ? -77.990  -61.542 96.495  1.00 57.47  ? 630 HOH A O   1 
HETATM 11504 O  O   . HOH AA 5 .   ? -86.872  -26.897 88.967  1.00 32.43  ? 631 HOH A O   1 
HETATM 11505 O  O   . HOH AA 5 .   ? -101.539 -25.947 75.769  1.00 36.05  ? 632 HOH A O   1 
HETATM 11506 O  O   . HOH AA 5 .   ? -87.362  -55.994 101.151 1.00 71.14  ? 633 HOH A O   1 
HETATM 11507 O  O   . HOH AA 5 .   ? -107.347 -28.955 82.869  1.00 38.85  ? 634 HOH A O   1 
HETATM 11508 O  O   . HOH AA 5 .   ? -90.183  -51.643 98.447  1.00 59.42  ? 635 HOH A O   1 
HETATM 11509 O  O   . HOH AA 5 .   ? -111.984 -44.141 81.693  1.00 57.62  ? 636 HOH A O   1 
HETATM 11510 O  O   . HOH AA 5 .   ? -93.507  -49.824 108.366 1.00 95.39  ? 637 HOH A O   1 
HETATM 11511 O  O   . HOH AA 5 .   ? -94.591  -50.571 106.570 1.00 77.68  ? 638 HOH A O   1 
HETATM 11512 O  O   . HOH AA 5 .   ? -65.158  -44.800 77.091  1.00 36.48  ? 639 HOH A O   1 
HETATM 11513 O  O   . HOH AA 5 .   ? -84.038  -40.744 86.745  1.00 34.84  ? 640 HOH A O   1 
HETATM 11514 O  O   . HOH AA 5 .   ? -82.438  -30.283 78.997  1.00 61.82  ? 641 HOH A O   1 
HETATM 11515 O  O   . HOH AA 5 .   ? -57.264  -46.128 82.005  1.00 56.12  ? 642 HOH A O   1 
HETATM 11516 O  O   . HOH AA 5 .   ? -71.630  -33.979 84.431  1.00 60.55  ? 643 HOH A O   1 
HETATM 11517 O  O   . HOH AA 5 .   ? -78.793  -55.125 81.494  1.00 57.65  ? 644 HOH A O   1 
HETATM 11518 O  O   . HOH AA 5 .   ? -94.099  -25.912 98.433  1.00 48.79  ? 645 HOH A O   1 
HETATM 11519 O  O   . HOH AA 5 .   ? -84.243  -24.437 78.213  1.00 57.22  ? 646 HOH A O   1 
HETATM 11520 O  O   . HOH AA 5 .   ? -112.505 -48.174 84.360  1.00 38.33  ? 647 HOH A O   1 
HETATM 11521 O  O   . HOH AA 5 .   ? -116.689 -33.774 97.062  1.00 53.78  ? 648 HOH A O   1 
HETATM 11522 O  O   . HOH AA 5 .   ? -66.062  -47.861 103.926 1.00 57.55  ? 649 HOH A O   1 
HETATM 11523 O  O   . HOH AA 5 .   ? -66.101  -57.157 95.217  1.00 66.12  ? 650 HOH A O   1 
HETATM 11524 O  O   . HOH AA 5 .   ? -103.822 -22.995 83.429  1.00 47.32  ? 651 HOH A O   1 
HETATM 11525 O  O   . HOH AA 5 .   ? -72.778  -35.955 82.737  1.00 62.98  ? 652 HOH A O   1 
HETATM 11526 O  O   . HOH AA 5 .   ? -62.275  -48.962 71.702  1.00 44.65  ? 653 HOH A O   1 
HETATM 11527 O  O   . HOH AA 5 .   ? -67.500  -62.243 87.338  1.00 67.22  ? 654 HOH A O   1 
HETATM 11528 O  O   . HOH AA 5 .   ? -66.714  -56.035 83.703  1.00 51.17  ? 655 HOH A O   1 
HETATM 11529 O  O   . HOH AA 5 .   ? -64.864  -37.757 89.900  1.00 58.86  ? 656 HOH A O   1 
HETATM 11530 O  O   . HOH AA 5 .   ? -86.256  -53.892 102.192 1.00 76.47  ? 657 HOH A O   1 
HETATM 11531 O  O   . HOH AA 5 .   ? -108.587 -48.823 103.576 1.00 69.58  ? 658 HOH A O   1 
HETATM 11532 O  O   . HOH AA 5 .   ? -99.744  -45.587 81.944  1.00 52.63  ? 659 HOH A O   1 
HETATM 11533 O  O   . HOH AA 5 .   ? -92.702  -41.106 78.405  1.00 44.85  ? 660 HOH A O   1 
HETATM 11534 O  O   . HOH AA 5 .   ? -60.935  -39.618 103.719 1.00 62.21  ? 661 HOH A O   1 
HETATM 11535 O  O   . HOH AA 5 .   ? -101.482 -40.525 74.876  1.00 60.75  ? 662 HOH A O   1 
HETATM 11536 O  O   . HOH AA 5 .   ? -57.383  -50.518 80.187  1.00 55.66  ? 663 HOH A O   1 
HETATM 11537 O  O   . HOH AA 5 .   ? -93.172  -22.767 75.522  1.00 49.26  ? 664 HOH A O   1 
HETATM 11538 O  O   . HOH AA 5 .   ? -98.501  -50.074 86.291  1.00 48.87  ? 665 HOH A O   1 
HETATM 11539 O  O   . HOH AA 5 .   ? -100.721 -45.381 84.278  1.00 48.39  ? 666 HOH A O   1 
HETATM 11540 O  O   . HOH AA 5 .   ? -107.283 -33.646 97.451  1.00 34.96  ? 667 HOH A O   1 
HETATM 11541 O  O   . HOH AA 5 .   ? -111.091 -41.078 81.453  1.00 61.62  ? 668 HOH A O   1 
HETATM 11542 O  O   . HOH AA 5 .   ? -52.803  -40.451 87.797  1.00 72.07  ? 669 HOH A O   1 
HETATM 11543 O  O   . HOH AA 5 .   ? -111.978 -46.741 82.016  1.00 40.61  ? 670 HOH A O   1 
HETATM 11544 O  O   . HOH AA 5 .   ? -46.946  -39.379 96.877  1.00 66.06  ? 671 HOH A O   1 
HETATM 11545 O  O   . HOH AA 5 .   ? -83.766  -45.790 77.994  1.00 61.54  ? 672 HOH A O   1 
HETATM 11546 O  O   . HOH AA 5 .   ? -88.168  -41.858 80.867  1.00 55.89  ? 673 HOH A O   1 
HETATM 11547 O  O   . HOH AA 5 .   ? -106.658 -51.449 96.558  1.00 62.89  ? 674 HOH A O   1 
HETATM 11548 O  O   . HOH AA 5 .   ? -76.814  -63.025 85.729  1.00 74.10  ? 675 HOH A O   1 
HETATM 11549 O  O   . HOH AA 5 .   ? -75.894  -67.182 105.570 1.00 71.77  ? 676 HOH A O   1 
HETATM 11550 O  O   . HOH AA 5 .   ? -100.629 -37.865 74.761  1.00 69.89  ? 677 HOH A O   1 
HETATM 11551 O  O   . HOH AA 5 .   ? -67.482  -56.902 86.045  1.00 45.32  ? 678 HOH A O   1 
HETATM 11552 O  O   . HOH AA 5 .   ? -100.245 -38.088 107.667 1.00 59.94  ? 679 HOH A O   1 
HETATM 11553 O  O   . HOH AA 5 .   ? -102.853 -44.543 79.440  1.00 61.61  ? 680 HOH A O   1 
HETATM 11554 O  O   . HOH AA 5 .   ? -99.842  -50.980 94.133  1.00 69.40  ? 681 HOH A O   1 
HETATM 11555 O  O   . HOH AA 5 .   ? -80.153  -33.238 82.648  1.00 69.84  ? 682 HOH A O   1 
HETATM 11556 O  O   . HOH AA 5 .   ? -72.283  -52.921 70.863  1.00 62.07  ? 683 HOH A O   1 
HETATM 11557 O  O   . HOH AA 5 .   ? -84.029  -31.097 82.848  1.00 50.87  ? 684 HOH A O   1 
HETATM 11558 O  O   . HOH AA 5 .   ? -91.730  -34.170 71.067  1.00 56.91  ? 685 HOH A O   1 
HETATM 11559 O  O   . HOH AA 5 .   ? -103.138 -42.423 75.328  1.00 75.46  ? 686 HOH A O   1 
HETATM 11560 O  O   . HOH AA 5 .   ? -93.242  -50.943 102.705 1.00 64.82  ? 687 HOH A O   1 
HETATM 11561 O  O   . HOH AA 5 .   ? -86.792  -27.559 84.308  1.00 56.96  ? 688 HOH A O   1 
HETATM 11562 O  O   . HOH AA 5 .   ? -92.569  -20.809 77.069  1.00 61.69  ? 689 HOH A O   1 
HETATM 11563 O  O   . HOH AA 5 .   ? -87.964  -45.899 76.477  1.00 66.94  ? 690 HOH A O   1 
HETATM 11564 O  O   . HOH AA 5 .   ? -110.627 -33.118 87.830  1.00 59.15  ? 691 HOH A O   1 
HETATM 11565 O  O   . HOH AA 5 .   ? -77.176  -37.798 83.366  1.00 60.65  ? 692 HOH A O   1 
HETATM 11566 O  O   . HOH AA 5 .   ? -85.518  -29.370 82.878  1.00 56.53  ? 693 HOH A O   1 
HETATM 11567 O  O   . HOH AA 5 .   ? -86.967  -23.965 85.606  1.00 56.23  ? 694 HOH A O   1 
HETATM 11568 O  O   . HOH AA 5 .   ? -75.607  -36.564 82.141  1.00 63.81  ? 695 HOH A O   1 
HETATM 11569 O  O   . HOH AA 5 .   ? -106.031 -29.889 77.450  1.00 63.71  ? 696 HOH A O   1 
HETATM 11570 O  O   . HOH AA 5 .   ? -96.285  -28.792 73.517  1.00 54.20  ? 697 HOH A O   1 
HETATM 11571 O  O   . HOH AA 5 .   ? -103.175 -27.493 75.019  1.00 65.81  ? 698 HOH A O   1 
HETATM 11572 O  O   . HOH AA 5 .   ? -89.042  -42.403 78.729  1.00 67.43  ? 699 HOH A O   1 
HETATM 11573 O  O   . HOH AA 5 .   ? -77.268  -35.497 74.848  1.00 63.04  ? 700 HOH A O   1 
HETATM 11574 O  O   . HOH AA 5 .   ? -81.350  -52.722 107.876 0.50 65.81  ? 701 HOH A O   1 
HETATM 11575 O  O   . HOH AA 5 .   ? -77.861  -42.095 76.077  1.00 59.84  ? 702 HOH A O   1 
HETATM 11576 O  O   . HOH AA 5 .   ? -98.331  -43.017 75.150  1.00 61.99  ? 703 HOH A O   1 
HETATM 11577 O  O   . HOH AA 5 .   ? -91.153  -22.949 78.119  1.00 54.71  ? 704 HOH A O   1 
HETATM 11578 O  O   . HOH AA 5 .   ? -116.925 -38.196 94.396  1.00 43.40  ? 705 HOH A O   1 
HETATM 11579 O  O   . HOH AA 5 .   ? -58.701  -36.512 85.176  1.00 58.18  ? 706 HOH A O   1 
HETATM 11580 O  O   . HOH AA 5 .   ? -113.855 -34.552 89.584  1.00 56.87  ? 707 HOH A O   1 
HETATM 11581 O  O   . HOH AA 5 .   ? -68.693  -40.435 76.424  1.00 50.43  ? 708 HOH A O   1 
HETATM 11582 O  O   . HOH AA 5 .   ? -110.794 -32.408 89.783  1.00 54.52  ? 709 HOH A O   1 
HETATM 11583 O  O   . HOH AA 5 .   ? -111.441 -38.582 83.448  1.00 47.90  ? 710 HOH A O   1 
HETATM 11584 O  O   . HOH AA 5 .   ? -117.029 -41.968 93.710  1.00 48.40  ? 711 HOH A O   1 
HETATM 11585 O  O   . HOH AA 5 .   ? -92.179  -25.920 75.243  1.00 53.17  ? 712 HOH A O   1 
HETATM 11586 O  O   . HOH AA 5 .   ? -95.503  -35.815 75.741  1.00 49.94  ? 713 HOH A O   1 
HETATM 11587 O  O   . HOH AA 5 .   ? -116.223 -40.162 95.410  1.00 59.72  ? 714 HOH A O   1 
HETATM 11588 O  O   . HOH AA 5 .   ? -90.846  -53.197 82.084  1.00 58.97  ? 715 HOH A O   1 
HETATM 11589 O  O   . HOH AA 5 .   ? -86.072  -26.198 86.404  1.00 45.46  ? 716 HOH A O   1 
HETATM 11590 O  O   . HOH AA 5 .   ? -75.390  -54.054 73.588  1.00 57.08  ? 717 HOH A O   1 
HETATM 11591 O  O   . HOH AA 5 .   ? -81.098  -30.051 96.229  1.00 54.35  ? 718 HOH A O   1 
HETATM 11592 O  O   . HOH AA 5 .   ? -77.845  -28.146 94.638  1.00 51.11  ? 719 HOH A O   1 
HETATM 11593 O  O   . HOH AA 5 .   ? -100.597 -45.556 79.197  1.00 64.98  ? 720 HOH A O   1 
HETATM 11594 O  O   . HOH AA 5 .   ? -72.961  -50.434 70.758  1.00 50.26  ? 721 HOH A O   1 
HETATM 11595 O  O   . HOH AA 5 .   ? -77.056  -51.667 108.674 1.00 64.17  ? 722 HOH A O   1 
HETATM 11596 O  O   . HOH AA 5 .   ? -94.165  -35.273 70.997  1.00 58.39  ? 723 HOH A O   1 
HETATM 11597 O  O   . HOH AA 5 .   ? -68.289  -30.987 82.244  1.00 61.33  ? 724 HOH A O   1 
HETATM 11598 O  O   . HOH AA 5 .   ? -97.381  -34.360 74.489  1.00 58.45  ? 725 HOH A O   1 
HETATM 11599 O  O   . HOH AA 5 .   ? -109.815 -31.332 83.144  1.00 62.36  ? 726 HOH A O   1 
HETATM 11600 O  O   . HOH BA 5 .   ? -58.592  -15.463 24.416  1.00 63.51  ? 501 HOH C O   1 
HETATM 11601 O  O   . HOH BA 5 .   ? -54.556  3.493   12.297  1.00 59.28  ? 502 HOH C O   1 
HETATM 11602 O  O   . HOH BA 5 .   ? -36.923  -20.653 26.897  1.00 48.29  ? 503 HOH C O   1 
HETATM 11603 O  O   . HOH BA 5 .   ? -31.185  0.603   25.863  1.00 69.54  ? 504 HOH C O   1 
HETATM 11604 O  O   . HOH BA 5 .   ? -34.074  9.067   12.478  1.00 63.54  ? 505 HOH C O   1 
HETATM 11605 O  O   . HOH BA 5 .   ? -57.024  25.435  16.247  1.00 30.74  ? 506 HOH C O   1 
HETATM 11606 O  O   . HOH BA 5 .   ? -28.114  -18.388 20.242  1.00 58.28  ? 507 HOH C O   1 
HETATM 11607 O  O   . HOH BA 5 .   ? -34.930  13.869  36.341  1.00 61.54  ? 508 HOH C O   1 
HETATM 11608 O  O   . HOH BA 5 .   ? -36.860  -23.200 13.618  1.00 57.95  ? 509 HOH C O   1 
HETATM 11609 O  O   . HOH BA 5 .   ? -34.295  -13.710 35.867  1.00 56.17  ? 510 HOH C O   1 
HETATM 11610 O  O   . HOH BA 5 .   ? -53.661  -23.532 14.688  1.00 36.81  ? 511 HOH C O   1 
HETATM 11611 O  O   . HOH BA 5 .   ? -42.256  9.698   39.167  1.00 62.96  ? 512 HOH C O   1 
HETATM 11612 O  O   . HOH BA 5 .   ? -45.758  -3.369  19.892  1.00 37.76  ? 513 HOH C O   1 
HETATM 11613 O  O   . HOH BA 5 .   ? -53.122  16.215  33.772  1.00 48.14  ? 514 HOH C O   1 
HETATM 11614 O  O   . HOH BA 5 .   ? -48.425  -2.424  20.359  1.00 39.52  ? 515 HOH C O   1 
HETATM 11615 O  O   . HOH BA 5 .   ? -37.994  -1.309  35.990  1.00 62.26  ? 516 HOH C O   1 
HETATM 11616 O  O   . HOH BA 5 .   ? -53.970  13.926  32.877  1.00 40.75  ? 517 HOH C O   1 
HETATM 11617 O  O   . HOH BA 5 .   ? -47.647  22.312  33.555  1.00 58.67  ? 518 HOH C O   1 
HETATM 11618 O  O   . HOH BA 5 .   ? -49.860  19.870  23.997  1.00 34.98  ? 519 HOH C O   1 
HETATM 11619 O  O   . HOH BA 5 .   ? -40.390  2.022   20.110  1.00 36.52  ? 520 HOH C O   1 
HETATM 11620 O  O   . HOH BA 5 .   ? -49.924  3.232   37.956  1.00 67.36  ? 521 HOH C O   1 
HETATM 11621 O  O   . HOH BA 5 .   ? -32.092  -15.894 22.426  1.00 80.25  ? 522 HOH C O   1 
HETATM 11622 O  O   . HOH BA 5 .   ? -36.853  14.902  6.271   1.00 48.13  ? 523 HOH C O   1 
HETATM 11623 O  O   . HOH BA 5 .   ? -45.340  -22.053 23.400  1.00 47.63  ? 524 HOH C O   1 
HETATM 11624 O  O   . HOH BA 5 .   ? -43.776  -24.950 20.699  1.00 60.09  ? 525 HOH C O   1 
HETATM 11625 O  O   . HOH BA 5 .   ? -41.533  13.935  36.270  1.00 68.81  ? 526 HOH C O   1 
HETATM 11626 O  O   . HOH BA 5 .   ? -33.528  2.241   32.251  1.00 58.99  ? 527 HOH C O   1 
HETATM 11627 O  O   . HOH BA 5 .   ? -56.030  23.819  28.770  1.00 56.43  ? 528 HOH C O   1 
HETATM 11628 O  O   . HOH BA 5 .   ? -42.428  20.581  28.847  1.00 45.06  ? 529 HOH C O   1 
HETATM 11629 O  O   . HOH BA 5 .   ? -43.896  -21.919 25.591  1.00 45.90  ? 530 HOH C O   1 
HETATM 11630 O  O   . HOH BA 5 .   ? -37.699  1.174   20.991  1.00 42.12  ? 531 HOH C O   1 
HETATM 11631 O  O   . HOH BA 5 .   ? -45.246  -20.787 30.461  1.00 56.32  ? 532 HOH C O   1 
HETATM 11632 O  O   . HOH BA 5 .   ? -55.320  14.799  16.851  1.00 57.16  ? 533 HOH C O   1 
HETATM 11633 O  O   . HOH BA 5 .   ? -50.724  23.258  11.607  1.00 53.19  ? 534 HOH C O   1 
HETATM 11634 O  O   . HOH BA 5 .   ? -56.156  31.416  20.062  1.00 47.03  ? 535 HOH C O   1 
HETATM 11635 O  O   . HOH BA 5 .   ? -46.724  -17.707 6.868   1.00 48.00  ? 536 HOH C O   1 
HETATM 11636 O  O   . HOH BA 5 .   ? -38.888  20.390  17.549  1.00 45.84  ? 537 HOH C O   1 
HETATM 11637 O  O   . HOH BA 5 .   ? -39.657  -2.080  38.163  1.00 66.39  ? 538 HOH C O   1 
HETATM 11638 O  O   . HOH BA 5 .   ? -54.024  22.856  14.071  1.00 52.09  ? 539 HOH C O   1 
HETATM 11639 O  O   . HOH BA 5 .   ? -43.059  0.662   18.988  1.00 47.82  ? 540 HOH C O   1 
HETATM 11640 O  O   . HOH BA 5 .   ? -48.637  5.104   34.155  1.00 44.98  ? 541 HOH C O   1 
HETATM 11641 O  O   . HOH BA 5 .   ? -57.434  16.897  16.068  1.00 41.94  ? 542 HOH C O   1 
HETATM 11642 O  O   . HOH BA 5 .   ? -43.275  21.196  22.803  1.00 38.05  ? 543 HOH C O   1 
HETATM 11643 O  O   . HOH BA 5 .   ? -36.137  21.228  14.588  1.00 44.02  ? 544 HOH C O   1 
HETATM 11644 O  O   . HOH BA 5 .   ? -42.643  2.057   15.531  1.00 55.92  ? 545 HOH C O   1 
HETATM 11645 O  O   . HOH BA 5 .   ? -60.002  27.091  23.308  1.00 31.38  ? 546 HOH C O   1 
HETATM 11646 O  O   . HOH BA 5 .   ? -55.406  8.370   30.564  1.00 52.29  ? 547 HOH C O   1 
HETATM 11647 O  O   . HOH BA 5 .   ? -52.423  27.279  26.093  1.00 49.89  ? 548 HOH C O   1 
HETATM 11648 O  O   . HOH BA 5 .   ? -38.112  23.149  23.569  1.00 51.33  ? 549 HOH C O   1 
HETATM 11649 O  O   . HOH BA 5 .   ? -55.189  -4.945  21.115  1.00 51.84  ? 550 HOH C O   1 
HETATM 11650 O  O   . HOH BA 5 .   ? -38.845  -16.520 8.288   1.00 52.15  ? 551 HOH C O   1 
HETATM 11651 O  O   . HOH BA 5 .   ? -48.268  17.458  7.851   1.00 55.34  ? 552 HOH C O   1 
HETATM 11652 O  O   . HOH BA 5 .   ? -34.482  -29.128 24.801  1.00 51.64  ? 553 HOH C O   1 
HETATM 11653 O  O   . HOH BA 5 .   ? -57.927  31.773  21.591  1.00 43.25  ? 554 HOH C O   1 
HETATM 11654 O  O   . HOH BA 5 .   ? -58.804  2.253   18.569  1.00 66.16  ? 555 HOH C O   1 
HETATM 11655 O  O   . HOH BA 5 .   ? -54.887  -7.321  19.670  1.00 47.55  ? 556 HOH C O   1 
HETATM 11656 O  O   . HOH BA 5 .   ? -46.743  -22.557 19.200  1.00 49.79  ? 557 HOH C O   1 
HETATM 11657 O  O   . HOH BA 5 .   ? -36.080  -27.778 22.802  1.00 47.61  ? 558 HOH C O   1 
HETATM 11658 O  O   . HOH BA 5 .   ? -59.810  16.556  27.231  1.00 51.21  ? 559 HOH C O   1 
HETATM 11659 O  O   . HOH BA 5 .   ? -46.649  1.615   5.331   1.00 65.61  ? 560 HOH C O   1 
HETATM 11660 O  O   . HOH BA 5 .   ? -45.960  9.042   7.918   1.00 56.01  ? 561 HOH C O   1 
HETATM 11661 O  O   . HOH BA 5 .   ? -57.748  -2.686  28.858  1.00 67.98  ? 562 HOH C O   1 
HETATM 11662 O  O   . HOH BA 5 .   ? -45.059  -1.803  37.747  1.00 62.08  ? 563 HOH C O   1 
HETATM 11663 O  O   . HOH BA 5 .   ? -54.178  -7.505  24.503  1.00 53.12  ? 564 HOH C O   1 
HETATM 11664 O  O   . HOH BA 5 .   ? -54.803  13.433  19.289  1.00 51.72  ? 565 HOH C O   1 
HETATM 11665 O  O   . HOH BA 5 .   ? -54.640  9.339   12.254  1.00 53.17  ? 566 HOH C O   1 
HETATM 11666 O  O   . HOH BA 5 .   ? -37.887  -27.174 14.758  1.00 58.69  ? 567 HOH C O   1 
HETATM 11667 O  O   . HOH BA 5 .   ? -50.163  20.341  34.906  1.00 57.25  ? 568 HOH C O   1 
HETATM 11668 O  O   . HOH BA 5 .   ? -39.797  25.518  10.502  1.00 57.42  ? 569 HOH C O   1 
HETATM 11669 O  O   . HOH BA 5 .   ? -62.134  25.511  23.386  1.00 55.67  ? 570 HOH C O   1 
HETATM 11670 O  O   . HOH BA 5 .   ? -43.587  -28.388 19.221  1.00 45.06  ? 571 HOH C O   1 
HETATM 11671 O  O   . HOH BA 5 .   ? -46.312  25.603  11.457  1.00 48.94  ? 572 HOH C O   1 
HETATM 11672 O  O   . HOH BA 5 .   ? -35.820  -1.767  34.156  1.00 58.39  ? 573 HOH C O   1 
HETATM 11673 O  O   . HOH BA 5 .   ? -42.869  -2.067  18.845  1.00 34.65  ? 574 HOH C O   1 
HETATM 11674 O  O   . HOH BA 5 .   ? -39.162  22.022  27.111  1.00 51.80  ? 575 HOH C O   1 
HETATM 11675 O  O   . HOH BA 5 .   ? -38.270  -18.172 10.105  1.00 47.56  ? 576 HOH C O   1 
HETATM 11676 O  O   . HOH BA 5 .   ? -49.498  -23.043 14.543  1.00 46.93  ? 577 HOH C O   1 
HETATM 11677 O  O   . HOH BA 5 .   ? -57.178  13.175  23.471  1.00 43.80  ? 578 HOH C O   1 
HETATM 11678 O  O   . HOH BA 5 .   ? -30.280  -11.038 15.293  1.00 51.19  ? 579 HOH C O   1 
HETATM 11679 O  O   . HOH BA 5 .   ? -41.980  -24.001 25.136  1.00 52.80  ? 580 HOH C O   1 
HETATM 11680 O  O   . HOH BA 5 .   ? -46.043  16.196  7.790   1.00 51.41  ? 581 HOH C O   1 
HETATM 11681 O  O   . HOH BA 5 .   ? -46.476  2.423   32.806  1.00 62.22  ? 582 HOH C O   1 
HETATM 11682 O  O   . HOH BA 5 .   ? -54.707  -10.416 18.251  1.00 57.26  ? 583 HOH C O   1 
HETATM 11683 O  O   . HOH BA 5 .   ? -34.150  -2.815  32.715  1.00 56.21  ? 584 HOH C O   1 
HETATM 11684 O  O   . HOH BA 5 .   ? -45.622  2.155   14.600  1.00 54.24  ? 585 HOH C O   1 
HETATM 11685 O  O   . HOH BA 5 .   ? -42.804  20.738  32.865  1.00 61.10  ? 586 HOH C O   1 
HETATM 11686 O  O   . HOH BA 5 .   ? -51.524  -24.124 13.133  1.00 50.00  ? 587 HOH C O   1 
HETATM 11687 O  O   . HOH BA 5 .   ? -48.218  -22.600 28.560  1.00 55.52  ? 588 HOH C O   1 
HETATM 11688 O  O   . HOH BA 5 .   ? -33.808  -25.055 14.995  1.00 57.10  ? 589 HOH C O   1 
HETATM 11689 O  O   . HOH BA 5 .   ? -29.451  -13.027 19.567  1.00 58.05  ? 590 HOH C O   1 
HETATM 11690 O  O   . HOH BA 5 .   ? -47.192  25.463  26.688  1.00 41.20  ? 591 HOH C O   1 
HETATM 11691 O  O   . HOH BA 5 .   ? -54.334  -2.550  30.320  1.00 59.99  ? 592 HOH C O   1 
HETATM 11692 O  O   . HOH BA 5 .   ? -56.282  12.032  17.557  1.00 52.21  ? 593 HOH C O   1 
HETATM 11693 O  O   . HOH BA 5 .   ? -42.402  -1.571  38.333  1.00 56.58  ? 594 HOH C O   1 
HETATM 11694 O  O   . HOH BA 5 .   ? -42.341  20.841  3.606   1.00 59.25  ? 595 HOH C O   1 
HETATM 11695 O  O   . HOH BA 5 .   ? -58.442  8.010   20.144  1.00 54.48  ? 596 HOH C O   1 
HETATM 11696 O  O   . HOH BA 5 .   ? -64.814  20.877  17.557  1.00 44.41  ? 597 HOH C O   1 
HETATM 11697 O  O   . HOH BA 5 .   ? -49.832  28.714  31.808  1.00 61.33  ? 598 HOH C O   1 
HETATM 11698 O  O   . HOH BA 5 .   ? -56.040  11.469  15.333  1.00 62.02  ? 599 HOH C O   1 
HETATM 11699 O  O   . HOH BA 5 .   ? -45.459  -20.899 34.500  1.00 55.48  ? 600 HOH C O   1 
HETATM 11700 O  O   . HOH BA 5 .   ? -57.063  23.880  12.423  1.00 61.59  ? 601 HOH C O   1 
HETATM 11701 O  O   . HOH BA 5 .   ? -58.112  -0.152  17.536  1.00 60.88  ? 602 HOH C O   1 
HETATM 11702 O  O   . HOH BA 5 .   ? -55.394  -13.327 33.163  1.00 58.59  ? 603 HOH C O   1 
HETATM 11703 O  O   . HOH BA 5 .   ? -19.403  -23.806 25.601  1.00 58.27  ? 604 HOH C O   1 
HETATM 11704 O  O   . HOH BA 5 .   ? -28.250  -13.574 17.535  1.00 59.60  ? 605 HOH C O   1 
HETATM 11705 O  O   . HOH BA 5 .   ? -43.031  20.183  26.361  1.00 89.69  ? 606 HOH C O   1 
HETATM 11706 O  O   . HOH BA 5 .   ? -31.807  9.893   18.444  1.00 64.73  ? 607 HOH C O   1 
HETATM 11707 O  O   . HOH BA 5 .   ? -52.028  27.802  32.851  1.00 60.00  ? 608 HOH C O   1 
HETATM 11708 O  O   . HOH BA 5 .   ? -61.497  15.055  30.612  1.00 62.08  ? 609 HOH C O   1 
HETATM 11709 O  O   . HOH BA 5 .   ? -34.115  22.459  25.324  1.00 74.27  ? 610 HOH C O   1 
HETATM 11710 O  O   . HOH BA 5 .   ? -54.778  -17.265 18.467  1.00 50.78  ? 611 HOH C O   1 
HETATM 11711 O  O   . HOH BA 5 .   ? -54.898  -18.391 20.315  1.00 56.18  ? 612 HOH C O   1 
HETATM 11712 O  O   . HOH BA 5 .   ? -65.340  25.054  27.395  1.00 67.74  ? 613 HOH C O   1 
HETATM 11713 O  O   . HOH BA 5 .   ? -30.796  -13.997 21.890  1.00 65.45  ? 614 HOH C O   1 
HETATM 11714 O  O   . HOH BA 5 .   ? -63.865  20.067  15.240  1.00 53.19  ? 615 HOH C O   1 
HETATM 11715 O  O   . HOH BA 5 .   ? -49.126  27.092  18.516  1.00 48.19  ? 616 HOH C O   1 
HETATM 11716 O  O   . HOH BA 5 .   ? -53.209  1.704   32.167  1.00 66.46  ? 617 HOH C O   1 
HETATM 11717 O  O   . HOH BA 5 .   ? -55.784  24.333  9.709   1.00 64.24  ? 618 HOH C O   1 
HETATM 11718 O  O   . HOH BA 5 .   ? -50.969  -11.794 12.824  1.00 64.06  ? 619 HOH C O   1 
HETATM 11719 O  O   . HOH BA 5 .   ? -56.765  12.056  21.051  1.00 56.35  ? 620 HOH C O   1 
HETATM 11720 O  O   . HOH BA 5 .   ? -47.430  2.248   13.101  1.00 53.98  ? 621 HOH C O   1 
HETATM 11721 O  O   . HOH BA 5 .   ? -34.675  2.042   36.607  1.00 61.95  ? 622 HOH C O   1 
HETATM 11722 O  O   . HOH BA 5 .   ? -44.577  -21.124 3.546   1.00 68.95  ? 623 HOH C O   1 
HETATM 11723 O  O   . HOH BA 5 .   ? -45.270  24.778  24.426  1.00 47.55  ? 624 HOH C O   1 
HETATM 11724 O  O   . HOH BA 5 .   ? -43.234  15.843  3.060   1.00 64.80  ? 625 HOH C O   1 
HETATM 11725 O  O   . HOH BA 5 .   ? -60.023  29.730  23.905  1.00 44.39  ? 626 HOH C O   1 
HETATM 11726 O  O   . HOH BA 5 .   ? -41.909  22.531  27.107  1.00 56.53  ? 627 HOH C O   1 
HETATM 11727 O  O   . HOH BA 5 .   ? -29.191  15.149  26.162  1.00 76.35  ? 628 HOH C O   1 
HETATM 11728 O  O   . HOH BA 5 .   ? -56.630  31.860  23.941  1.00 46.87  ? 629 HOH C O   1 
HETATM 11729 O  O   . HOH BA 5 .   ? -45.033  -22.030 28.130  1.00 60.11  ? 630 HOH C O   1 
HETATM 11730 O  O   . HOH BA 5 .   ? -51.209  27.828  17.422  1.00 58.99  ? 631 HOH C O   1 
HETATM 11731 O  O   . HOH BA 5 .   ? -58.012  30.233  25.596  1.00 48.16  ? 632 HOH C O   1 
HETATM 11732 O  O   . HOH BA 5 .   ? -41.023  27.554  13.668  1.00 51.49  ? 633 HOH C O   1 
HETATM 11733 O  O   . HOH BA 5 .   ? -40.878  16.530  2.404   1.00 62.03  ? 634 HOH C O   1 
HETATM 11734 O  O   . HOH BA 5 .   ? -56.890  -2.305  31.197  1.00 74.26  ? 635 HOH C O   1 
HETATM 11735 O  O   . HOH BA 5 .   ? -56.394  9.781   10.271  1.00 66.81  ? 636 HOH C O   1 
HETATM 11736 O  O   . HOH BA 5 .   ? -34.677  -17.880 8.797   1.00 64.59  ? 637 HOH C O   1 
HETATM 11737 O  O   . HOH BA 5 .   ? -55.428  24.896  14.307  1.00 55.27  ? 638 HOH C O   1 
HETATM 11738 O  O   . HOH BA 5 .   ? -52.740  29.871  18.309  1.00 53.77  ? 639 HOH C O   1 
HETATM 11739 O  O   . HOH BA 5 .   ? -37.151  -14.319 3.592   1.00 65.59  ? 640 HOH C O   1 
HETATM 11740 O  O   . HOH BA 5 .   ? -35.928  3.308   39.326  1.00 65.06  ? 641 HOH C O   1 
HETATM 11741 O  O   . HOH CA 5 .   ? -61.960  -0.227  49.962  1.00 61.16  ? 501 HOH E O   1 
HETATM 11742 O  O   . HOH CA 5 .   ? -79.980  4.106   63.926  1.00 56.92  ? 502 HOH E O   1 
HETATM 11743 O  O   . HOH CA 5 .   ? -65.309  -9.794  42.140  1.00 65.20  ? 503 HOH E O   1 
HETATM 11744 O  O   . HOH CA 5 .   ? -69.679  1.249   39.557  1.00 69.07  ? 504 HOH E O   1 
HETATM 11745 O  O   . HOH CA 5 .   ? -71.923  -4.511  38.821  1.00 85.91  ? 505 HOH E O   1 
HETATM 11746 O  O   . HOH CA 5 .   ? -85.088  7.224   40.020  1.00 71.30  ? 506 HOH E O   1 
HETATM 11747 O  O   . HOH CA 5 .   ? -76.575  7.159   34.019  1.00 61.59  ? 507 HOH E O   1 
HETATM 11748 O  O   . HOH CA 5 .   ? -77.066  1.566   60.345  1.00 49.51  ? 508 HOH E O   1 
HETATM 11749 O  O   . HOH CA 5 .   ? -88.470  6.168   60.663  1.00 53.79  ? 509 HOH E O   1 
HETATM 11750 O  O   . HOH CA 5 .   ? -83.632  5.231   41.114  1.00 64.36  ? 510 HOH E O   1 
HETATM 11751 O  O   . HOH CA 5 .   ? -82.981  -0.118  40.194  1.00 60.46  ? 511 HOH E O   1 
HETATM 11752 O  O   . HOH CA 5 .   ? -93.188  -16.541 42.991  1.00 59.34  ? 512 HOH E O   1 
HETATM 11753 O  O   . HOH CA 5 .   ? -63.282  2.715   51.295  1.00 42.66  ? 513 HOH E O   1 
HETATM 11754 O  O   . HOH CA 5 .   ? -77.318  27.572  57.384  1.00 52.07  ? 514 HOH E O   1 
HETATM 11755 O  O   . HOH CA 5 .   ? -83.986  24.504  69.198  1.00 58.64  ? 515 HOH E O   1 
HETATM 11756 O  O   . HOH CA 5 .   ? -78.493  7.199   68.768  1.00 55.49  ? 516 HOH E O   1 
HETATM 11757 O  O   . HOH CA 5 .   ? -75.233  -0.398  69.202  1.00 52.62  ? 517 HOH E O   1 
HETATM 11758 O  O   . HOH CA 5 .   ? -73.884  0.501   61.094  1.00 44.29  ? 518 HOH E O   1 
HETATM 11759 O  O   . HOH CA 5 .   ? -62.333  7.825   63.068  1.00 58.03  ? 519 HOH E O   1 
HETATM 11760 O  O   . HOH CA 5 .   ? -83.954  -23.951 49.740  1.00 46.29  ? 520 HOH E O   1 
HETATM 11761 O  O   . HOH CA 5 .   ? -63.426  -17.947 67.233  1.00 43.87  ? 521 HOH E O   1 
HETATM 11762 O  O   . HOH CA 5 .   ? -77.163  4.290   62.082  1.00 42.94  ? 522 HOH E O   1 
HETATM 11763 O  O   . HOH CA 5 .   ? -69.543  -20.247 52.774  1.00 41.40  ? 523 HOH E O   1 
HETATM 11764 O  O   . HOH CA 5 .   ? -63.206  13.920  36.765  1.00 53.22  ? 524 HOH E O   1 
HETATM 11765 O  O   . HOH CA 5 .   ? -78.851  0.042   64.190  1.00 53.09  ? 525 HOH E O   1 
HETATM 11766 O  O   . HOH CA 5 .   ? -74.063  -4.159  68.550  1.00 42.80  ? 526 HOH E O   1 
HETATM 11767 O  O   . HOH CA 5 .   ? -74.759  -5.550  37.781  1.00 44.53  ? 527 HOH E O   1 
HETATM 11768 O  O   . HOH CA 5 .   ? -80.276  -18.600 42.375  1.00 49.25  ? 528 HOH E O   1 
HETATM 11769 O  O   . HOH CA 5 .   ? -94.835  -15.436 61.648  1.00 56.43  ? 529 HOH E O   1 
HETATM 11770 O  O   . HOH CA 5 .   ? -88.045  3.933   54.322  1.00 35.06  ? 530 HOH E O   1 
HETATM 11771 O  O   . HOH CA 5 .   ? -62.453  13.046  42.060  1.00 56.47  ? 531 HOH E O   1 
HETATM 11772 O  O   . HOH CA 5 .   ? -82.431  11.082  33.951  1.00 24.30  ? 532 HOH E O   1 
HETATM 11773 O  O   . HOH CA 5 .   ? -83.449  9.822   40.990  1.00 31.23  ? 533 HOH E O   1 
HETATM 11774 O  O   . HOH CA 5 .   ? -96.119  -14.957 58.187  1.00 53.14  ? 534 HOH E O   1 
HETATM 11775 O  O   . HOH CA 5 .   ? -74.369  9.392   32.419  1.00 42.83  ? 535 HOH E O   1 
HETATM 11776 O  O   . HOH CA 5 .   ? -80.959  31.049  76.990  1.00 70.71  ? 536 HOH E O   1 
HETATM 11777 O  O   . HOH CA 5 .   ? -79.107  0.643   40.769  1.00 50.58  ? 537 HOH E O   1 
HETATM 11778 O  O   . HOH CA 5 .   ? -86.329  21.518  51.528  1.00 55.11  ? 538 HOH E O   1 
HETATM 11779 O  O   . HOH CA 5 .   ? -67.342  17.053  41.324  1.00 30.31  ? 539 HOH E O   1 
HETATM 11780 O  O   . HOH CA 5 .   ? -87.134  -12.234 60.153  1.00 43.63  ? 540 HOH E O   1 
HETATM 11781 O  O   . HOH CA 5 .   ? -75.359  6.063   60.887  1.00 31.26  ? 541 HOH E O   1 
HETATM 11782 O  O   . HOH CA 5 .   ? -73.485  10.742  67.920  1.00 28.26  ? 542 HOH E O   1 
HETATM 11783 O  O   . HOH CA 5 .   ? -85.061  -12.898 42.893  1.00 26.62  ? 543 HOH E O   1 
HETATM 11784 O  O   . HOH CA 5 .   ? -74.560  -17.419 47.011  1.00 41.87  ? 544 HOH E O   1 
HETATM 11785 O  O   . HOH CA 5 .   ? -77.954  23.671  46.974  1.00 48.90  ? 545 HOH E O   1 
HETATM 11786 O  O   . HOH CA 5 .   ? -68.925  26.855  63.823  1.00 48.39  ? 546 HOH E O   1 
HETATM 11787 O  O   . HOH CA 5 .   ? -84.524  1.480   44.308  1.00 53.21  ? 547 HOH E O   1 
HETATM 11788 O  O   . HOH CA 5 .   ? -68.798  19.386  40.613  1.00 39.84  ? 548 HOH E O   1 
HETATM 11789 O  O   . HOH CA 5 .   ? -87.170  -15.927 70.151  1.00 56.48  ? 549 HOH E O   1 
HETATM 11790 O  O   . HOH CA 5 .   ? -88.601  -23.397 59.868  1.00 21.19  ? 550 HOH E O   1 
HETATM 11791 O  O   . HOH CA 5 .   ? -70.155  26.715  65.945  1.00 47.66  ? 551 HOH E O   1 
HETATM 11792 O  O   . HOH CA 5 .   ? -77.206  13.553  71.244  1.00 33.48  ? 552 HOH E O   1 
HETATM 11793 O  O   . HOH CA 5 .   ? -78.776  19.923  70.843  1.00 28.95  ? 553 HOH E O   1 
HETATM 11794 O  O   . HOH CA 5 .   ? -81.231  25.801  61.698  1.00 34.46  ? 554 HOH E O   1 
HETATM 11795 O  O   . HOH CA 5 .   ? -77.868  6.129   57.481  1.00 17.88  ? 555 HOH E O   1 
HETATM 11796 O  O   . HOH CA 5 .   ? -63.897  27.351  59.033  1.00 50.19  ? 556 HOH E O   1 
HETATM 11797 O  O   . HOH CA 5 .   ? -73.874  -10.710 40.393  1.00 39.33  ? 557 HOH E O   1 
HETATM 11798 O  O   . HOH CA 5 .   ? -68.083  -4.404  38.936  1.00 48.99  ? 558 HOH E O   1 
HETATM 11799 O  O   . HOH CA 5 .   ? -60.703  9.244   46.024  1.00 52.56  ? 559 HOH E O   1 
HETATM 11800 O  O   . HOH CA 5 .   ? -86.349  -10.596 43.889  1.00 24.28  ? 560 HOH E O   1 
HETATM 11801 O  O   . HOH CA 5 .   ? -77.752  -20.379 67.271  1.00 46.02  ? 561 HOH E O   1 
HETATM 11802 O  O   . HOH CA 5 .   ? -77.420  33.481  70.592  1.00 63.20  ? 562 HOH E O   1 
HETATM 11803 O  O   . HOH CA 5 .   ? -75.148  -18.452 53.116  1.00 20.28  ? 563 HOH E O   1 
HETATM 11804 O  O   . HOH CA 5 .   ? -74.152  28.741  72.447  1.00 61.27  ? 564 HOH E O   1 
HETATM 11805 O  O   . HOH CA 5 .   ? -69.939  23.576  50.506  1.00 33.92  ? 565 HOH E O   1 
HETATM 11806 O  O   . HOH CA 5 .   ? -60.660  22.541  39.218  1.00 70.94  ? 566 HOH E O   1 
HETATM 11807 O  O   . HOH CA 5 .   ? -68.271  -0.359  68.685  1.00 61.86  ? 567 HOH E O   1 
HETATM 11808 O  O   . HOH CA 5 .   ? -64.734  -3.438  51.599  1.00 38.89  ? 568 HOH E O   1 
HETATM 11809 O  O   . HOH CA 5 .   ? -87.498  7.345   56.245  1.00 41.97  ? 569 HOH E O   1 
HETATM 11810 O  O   . HOH CA 5 .   ? -89.709  -4.241  59.338  1.00 46.47  ? 570 HOH E O   1 
HETATM 11811 O  O   . HOH CA 5 .   ? -86.959  9.794   57.903  1.00 42.62  ? 571 HOH E O   1 
HETATM 11812 O  O   . HOH CA 5 .   ? -57.857  18.159  54.079  1.00 60.14  ? 572 HOH E O   1 
HETATM 11813 O  O   . HOH CA 5 .   ? -81.781  -17.064 52.282  1.00 23.00  ? 573 HOH E O   1 
HETATM 11814 O  O   . HOH CA 5 .   ? -91.643  -2.886  50.297  1.00 55.43  ? 574 HOH E O   1 
HETATM 11815 O  O   . HOH CA 5 .   ? -85.433  -12.757 57.525  1.00 61.65  ? 575 HOH E O   1 
HETATM 11816 O  O   . HOH CA 5 .   ? -85.601  -20.667 62.117  1.00 29.77  ? 576 HOH E O   1 
HETATM 11817 O  O   . HOH CA 5 .   ? -68.045  22.454  66.633  1.00 46.04  ? 577 HOH E O   1 
HETATM 11818 O  O   . HOH CA 5 .   ? -63.288  -3.082  55.515  1.00 39.42  ? 578 HOH E O   1 
HETATM 11819 O  O   . HOH CA 5 .   ? -70.011  13.581  36.674  1.00 56.72  ? 579 HOH E O   1 
HETATM 11820 O  O   . HOH CA 5 .   ? -68.457  -13.269 70.096  1.00 23.33  ? 580 HOH E O   1 
HETATM 11821 O  O   . HOH CA 5 .   ? -91.827  -23.946 52.641  1.00 23.24  ? 581 HOH E O   1 
HETATM 11822 O  O   . HOH CA 5 .   ? -73.715  24.942  41.186  1.00 51.89  ? 582 HOH E O   1 
HETATM 11823 O  O   . HOH CA 5 .   ? -80.325  17.010  40.621  1.00 26.81  ? 583 HOH E O   1 
HETATM 11824 O  O   . HOH CA 5 .   ? -60.100  20.398  63.265  1.00 61.75  ? 584 HOH E O   1 
HETATM 11825 O  O   . HOH CA 5 .   ? -73.074  19.539  72.081  1.00 30.47  ? 585 HOH E O   1 
HETATM 11826 O  O   . HOH CA 5 .   ? -78.503  0.907   44.641  1.00 33.10  ? 586 HOH E O   1 
HETATM 11827 O  O   . HOH CA 5 .   ? -70.837  19.174  69.199  1.00 36.15  ? 587 HOH E O   1 
HETATM 11828 O  O   . HOH CA 5 .   ? -72.283  0.601   57.095  1.00 17.94  ? 588 HOH E O   1 
HETATM 11829 O  O   . HOH CA 5 .   ? -65.153  -18.850 62.918  1.00 33.04  ? 589 HOH E O   1 
HETATM 11830 O  O   . HOH CA 5 .   ? -81.705  23.371  43.015  1.00 55.37  ? 590 HOH E O   1 
HETATM 11831 O  O   . HOH CA 5 .   ? -63.086  -0.675  54.066  1.00 46.41  ? 591 HOH E O   1 
HETATM 11832 O  O   . HOH CA 5 .   ? -78.817  -2.360  74.981  1.00 60.81  ? 592 HOH E O   1 
HETATM 11833 O  O   . HOH CA 5 .   ? -64.122  -14.370 56.382  1.00 40.40  ? 593 HOH E O   1 
HETATM 11834 O  O   . HOH CA 5 .   ? -90.120  20.297  53.570  1.00 58.85  ? 594 HOH E O   1 
HETATM 11835 O  O   . HOH CA 5 .   ? -70.110  -3.617  40.007  1.00 42.03  ? 595 HOH E O   1 
HETATM 11836 O  O   . HOH CA 5 .   ? -87.022  16.389  41.539  1.00 32.45  ? 596 HOH E O   1 
HETATM 11837 O  O   . HOH CA 5 .   ? -82.805  22.699  38.543  1.00 62.80  ? 597 HOH E O   1 
HETATM 11838 O  O   . HOH CA 5 .   ? -88.235  24.655  54.316  1.00 39.27  ? 598 HOH E O   1 
HETATM 11839 O  O   . HOH CA 5 .   ? -79.317  -21.120 65.059  1.00 48.35  ? 599 HOH E O   1 
HETATM 11840 O  O   . HOH CA 5 .   ? -76.590  -12.547 70.211  1.00 24.99  ? 600 HOH E O   1 
HETATM 11841 O  O   . HOH CA 5 .   ? -69.833  1.660   56.061  1.00 20.70  ? 601 HOH E O   1 
HETATM 11842 O  O   . HOH CA 5 .   ? -76.630  19.247  37.521  1.00 63.89  ? 602 HOH E O   1 
HETATM 11843 O  O   . HOH CA 5 .   ? -81.127  -1.924  43.191  1.00 32.86  ? 603 HOH E O   1 
HETATM 11844 O  O   . HOH CA 5 .   ? -70.692  28.180  69.400  1.00 54.32  ? 604 HOH E O   1 
HETATM 11845 O  O   . HOH CA 5 .   ? -88.801  2.023   55.804  1.00 41.22  ? 605 HOH E O   1 
HETATM 11846 O  O   . HOH CA 5 .   ? -91.801  -13.409 49.817  1.00 31.58  ? 606 HOH E O   1 
HETATM 11847 O  O   . HOH CA 5 .   ? -86.423  10.003  53.758  1.00 35.85  ? 607 HOH E O   1 
HETATM 11848 O  O   . HOH CA 5 .   ? -101.938 -20.738 56.312  1.00 39.11  ? 608 HOH E O   1 
HETATM 11849 O  O   . HOH CA 5 .   ? -72.286  6.671   61.507  1.00 44.90  ? 609 HOH E O   1 
HETATM 11850 O  O   . HOH CA 5 .   ? -80.516  5.057   57.276  1.00 22.77  ? 610 HOH E O   1 
HETATM 11851 O  O   . HOH CA 5 .   ? -74.400  5.567   44.063  1.00 41.20  ? 611 HOH E O   1 
HETATM 11852 O  O   . HOH CA 5 .   ? -66.794  -15.131 73.068  1.00 48.49  ? 612 HOH E O   1 
HETATM 11853 O  O   . HOH CA 5 .   ? -90.985  17.572  50.747  1.00 57.95  ? 613 HOH E O   1 
HETATM 11854 O  O   . HOH CA 5 .   ? -69.792  -25.777 71.218  1.00 45.47  ? 614 HOH E O   1 
HETATM 11855 O  O   . HOH CA 5 .   ? -60.697  19.936  45.692  1.00 46.49  ? 615 HOH E O   1 
HETATM 11856 O  O   . HOH CA 5 .   ? -89.790  -28.794 53.549  1.00 33.61  ? 616 HOH E O   1 
HETATM 11857 O  O   . HOH CA 5 .   ? -93.638  -11.774 46.312  1.00 62.55  ? 617 HOH E O   1 
HETATM 11858 O  O   . HOH CA 5 .   ? -86.315  12.226  34.163  1.00 29.14  ? 618 HOH E O   1 
HETATM 11859 O  O   . HOH CA 5 .   ? -79.558  -15.774 68.474  1.00 26.87  ? 619 HOH E O   1 
HETATM 11860 O  O   . HOH CA 5 .   ? -88.268  -20.705 47.518  1.00 40.01  ? 620 HOH E O   1 
HETATM 11861 O  O   . HOH CA 5 .   ? -93.632  -6.206  44.732  1.00 73.04  ? 621 HOH E O   1 
HETATM 11862 O  O   . HOH CA 5 .   ? -69.115  32.435  48.937  1.00 56.83  ? 622 HOH E O   1 
HETATM 11863 O  O   . HOH CA 5 .   ? -63.867  17.564  54.588  1.00 48.10  ? 623 HOH E O   1 
HETATM 11864 O  O   . HOH CA 5 .   ? -82.267  -24.990 44.094  1.00 56.37  ? 624 HOH E O   1 
HETATM 11865 O  O   . HOH CA 5 .   ? -77.895  -23.145 55.928  1.00 45.73  ? 625 HOH E O   1 
HETATM 11866 O  O   . HOH CA 5 .   ? -82.295  25.534  64.052  1.00 51.45  ? 626 HOH E O   1 
HETATM 11867 O  O   . HOH CA 5 .   ? -87.359  -28.294 55.952  1.00 31.43  ? 627 HOH E O   1 
HETATM 11868 O  O   . HOH CA 5 .   ? -74.891  -11.352 38.345  1.00 46.96  ? 628 HOH E O   1 
HETATM 11869 O  O   . HOH CA 5 .   ? -67.610  28.941  40.513  1.00 48.37  ? 629 HOH E O   1 
HETATM 11870 O  O   . HOH CA 5 .   ? -89.620  -8.979  50.092  1.00 48.59  ? 630 HOH E O   1 
HETATM 11871 O  O   . HOH CA 5 .   ? -65.838  1.036   44.700  1.00 41.71  ? 631 HOH E O   1 
HETATM 11872 O  O   . HOH CA 5 .   ? -88.220  22.160  46.767  1.00 62.51  ? 632 HOH E O   1 
HETATM 11873 O  O   . HOH CA 5 .   ? -78.002  -5.724  38.679  1.00 23.42  ? 633 HOH E O   1 
HETATM 11874 O  O   . HOH CA 5 .   ? -70.550  20.941  67.399  1.00 37.06  ? 634 HOH E O   1 
HETATM 11875 O  O   . HOH CA 5 .   ? -83.330  25.974  57.747  1.00 42.41  ? 635 HOH E O   1 
HETATM 11876 O  O   . HOH CA 5 .   ? -93.146  -11.548 57.788  1.00 54.62  ? 636 HOH E O   1 
HETATM 11877 O  O   . HOH CA 5 .   ? -77.122  -7.225  68.870  1.00 31.80  ? 637 HOH E O   1 
HETATM 11878 O  O   . HOH CA 5 .   ? -72.525  8.326   41.821  1.00 29.33  ? 638 HOH E O   1 
HETATM 11879 O  O   . HOH CA 5 .   ? -60.548  21.568  57.121  1.00 51.44  ? 639 HOH E O   1 
HETATM 11880 O  O   . HOH CA 5 .   ? -63.236  25.337  65.801  1.00 67.78  ? 640 HOH E O   1 
HETATM 11881 O  O   . HOH CA 5 .   ? -86.068  -11.852 69.897  1.00 67.13  ? 641 HOH E O   1 
HETATM 11882 O  O   . HOH CA 5 .   ? -80.440  18.732  38.074  1.00 38.82  ? 642 HOH E O   1 
HETATM 11883 O  O   . HOH CA 5 .   ? -79.483  25.039  58.685  1.00 36.46  ? 643 HOH E O   1 
HETATM 11884 O  O   . HOH CA 5 .   ? -86.945  5.386   47.031  1.00 40.21  ? 644 HOH E O   1 
HETATM 11885 O  O   . HOH CA 5 .   ? -86.186  -7.395  64.825  1.00 34.19  ? 645 HOH E O   1 
HETATM 11886 O  O   . HOH CA 5 .   ? -78.291  4.893   39.142  1.00 40.37  ? 646 HOH E O   1 
HETATM 11887 O  O   . HOH CA 5 .   ? -73.418  -5.798  33.501  1.00 58.99  ? 647 HOH E O   1 
HETATM 11888 O  O   . HOH CA 5 .   ? -70.500  13.822  67.727  1.00 26.78  ? 648 HOH E O   1 
HETATM 11889 O  O   . HOH CA 5 .   ? -72.589  5.035   42.190  1.00 45.69  ? 649 HOH E O   1 
HETATM 11890 O  O   . HOH CA 5 .   ? -72.876  26.297  71.529  1.00 38.48  ? 650 HOH E O   1 
HETATM 11891 O  O   . HOH CA 5 .   ? -70.468  29.954  63.186  1.00 41.61  ? 651 HOH E O   1 
HETATM 11892 O  O   . HOH CA 5 .   ? -66.878  27.911  62.447  1.00 42.31  ? 652 HOH E O   1 
HETATM 11893 O  O   . HOH CA 5 .   ? -67.482  -18.886 61.496  1.00 28.15  ? 653 HOH E O   1 
HETATM 11894 O  O   . HOH CA 5 .   ? -61.549  2.257   54.972  1.00 51.45  ? 654 HOH E O   1 
HETATM 11895 O  O   . HOH CA 5 .   ? -92.169  11.951  38.231  1.00 62.56  ? 655 HOH E O   1 
HETATM 11896 O  O   . HOH CA 5 .   ? -74.981  -2.574  71.525  1.00 54.67  ? 656 HOH E O   1 
HETATM 11897 O  O   . HOH CA 5 .   ? -74.985  4.840   58.385  1.00 24.72  ? 657 HOH E O   1 
HETATM 11898 O  O   . HOH CA 5 .   ? -96.371  -21.262 61.565  1.00 25.26  ? 658 HOH E O   1 
HETATM 11899 O  O   . HOH CA 5 .   ? -89.040  -14.745 60.977  1.00 35.58  ? 659 HOH E O   1 
HETATM 11900 O  O   . HOH CA 5 .   ? -75.113  2.008   58.485  1.00 24.59  ? 660 HOH E O   1 
HETATM 11901 O  O   . HOH CA 5 .   ? -82.777  -16.424 41.581  1.00 55.48  ? 661 HOH E O   1 
HETATM 11902 O  O   . HOH CA 5 .   ? -86.548  -10.800 57.636  1.00 37.81  ? 662 HOH E O   1 
HETATM 11903 O  O   . HOH CA 5 .   ? -76.715  5.349   68.548  1.00 61.21  ? 663 HOH E O   1 
HETATM 11904 O  O   . HOH CA 5 .   ? -76.924  0.222   62.371  1.00 50.66  ? 664 HOH E O   1 
HETATM 11905 O  O   . HOH CA 5 .   ? -62.553  14.061  61.831  1.00 41.40  ? 665 HOH E O   1 
HETATM 11906 O  O   . HOH CA 5 .   ? -86.292  21.151  58.341  1.00 47.96  ? 666 HOH E O   1 
HETATM 11907 O  O   . HOH CA 5 .   ? -85.006  23.380  72.223  1.00 69.15  ? 667 HOH E O   1 
HETATM 11908 O  O   . HOH CA 5 .   ? -87.823  -5.118  47.218  1.00 32.61  ? 668 HOH E O   1 
HETATM 11909 O  O   . HOH CA 5 .   ? -80.431  -5.366  68.225  1.00 41.72  ? 669 HOH E O   1 
HETATM 11910 O  O   . HOH CA 5 .   ? -66.650  6.331   44.164  1.00 39.16  ? 670 HOH E O   1 
HETATM 11911 O  O   . HOH CA 5 .   ? -78.083  23.598  42.998  1.00 39.33  ? 671 HOH E O   1 
HETATM 11912 O  O   . HOH CA 5 .   ? -90.491  18.167  52.852  1.00 54.35  ? 672 HOH E O   1 
HETATM 11913 O  O   . HOH CA 5 .   ? -82.025  -21.158 64.793  1.00 37.98  ? 673 HOH E O   1 
HETATM 11914 O  O   . HOH CA 5 .   ? -85.251  14.750  60.623  1.00 43.53  ? 674 HOH E O   1 
HETATM 11915 O  O   . HOH CA 5 .   ? -83.809  20.090  35.252  1.00 69.06  ? 675 HOH E O   1 
HETATM 11916 O  O   . HOH CA 5 .   ? -98.433  -17.009 59.691  1.00 44.50  ? 676 HOH E O   1 
HETATM 11917 O  O   . HOH CA 5 .   ? -66.457  -23.593 67.207  1.00 41.24  ? 677 HOH E O   1 
HETATM 11918 O  O   . HOH CA 5 .   ? -76.202  1.175   38.945  1.00 46.07  ? 678 HOH E O   1 
HETATM 11919 O  O   . HOH CA 5 .   ? -77.500  30.425  65.358  1.00 45.33  ? 679 HOH E O   1 
HETATM 11920 O  O   . HOH CA 5 .   ? -84.587  -30.698 49.691  1.00 40.79  ? 680 HOH E O   1 
HETATM 11921 O  O   . HOH CA 5 .   ? -84.540  -2.588  41.320  1.00 51.93  ? 681 HOH E O   1 
HETATM 11922 O  O   . HOH CA 5 .   ? -82.452  -2.392  65.680  1.00 43.34  ? 682 HOH E O   1 
HETATM 11923 O  O   . HOH CA 5 .   ? -80.764  30.481  68.692  1.00 44.72  ? 683 HOH E O   1 
HETATM 11924 O  O   . HOH CA 5 .   ? -89.048  -10.373 53.634  1.00 26.93  ? 684 HOH E O   1 
HETATM 11925 O  O   . HOH CA 5 .   ? -77.618  -14.669 38.181  1.00 57.58  ? 685 HOH E O   1 
HETATM 11926 O  O   . HOH CA 5 .   ? -70.694  6.945   69.910  1.00 58.83  ? 686 HOH E O   1 
HETATM 11927 O  O   . HOH CA 5 .   ? -91.120  -6.560  46.215  1.00 54.98  ? 687 HOH E O   1 
HETATM 11928 O  O   . HOH CA 5 .   ? -89.467  -5.961  48.714  1.00 50.59  ? 688 HOH E O   1 
HETATM 11929 O  O   . HOH CA 5 .   ? -77.280  -14.493 68.467  1.00 26.34  ? 689 HOH E O   1 
HETATM 11930 O  O   . HOH CA 5 .   ? -77.947  -23.641 64.111  1.00 35.51  ? 690 HOH E O   1 
HETATM 11931 O  O   . HOH CA 5 .   ? -62.296  16.899  50.031  1.00 37.65  ? 691 HOH E O   1 
HETATM 11932 O  O   . HOH CA 5 .   ? -63.369  -13.373 58.706  1.00 51.79  ? 692 HOH E O   1 
HETATM 11933 O  O   . HOH CA 5 .   ? -90.332  -13.619 38.862  1.00 50.85  ? 693 HOH E O   1 
HETATM 11934 O  O   . HOH CA 5 .   ? -61.974  4.618   52.516  1.00 46.81  ? 694 HOH E O   1 
HETATM 11935 O  O   . HOH CA 5 .   ? -66.781  32.742  52.696  1.00 47.48  ? 695 HOH E O   1 
HETATM 11936 O  O   . HOH CA 5 .   ? -87.810  -9.518  60.031  1.00 44.48  ? 696 HOH E O   1 
HETATM 11937 O  O   . HOH CA 5 .   ? -63.052  -6.696  57.447  1.00 49.23  ? 697 HOH E O   1 
HETATM 11938 O  O   . HOH CA 5 .   ? -66.521  -20.883 74.739  1.00 65.39  ? 698 HOH E O   1 
HETATM 11939 O  O   . HOH CA 5 .   ? -53.757  25.429  53.090  1.00 60.59  ? 699 HOH E O   1 
HETATM 11940 O  O   . HOH CA 5 .   ? -78.965  22.181  74.291  1.00 51.75  ? 700 HOH E O   1 
HETATM 11941 O  O   . HOH CA 5 .   ? -86.473  -0.229  46.505  1.00 39.50  ? 701 HOH E O   1 
HETATM 11942 O  O   . HOH CA 5 .   ? -89.422  -24.252 49.040  1.00 41.71  ? 702 HOH E O   1 
HETATM 11943 O  O   . HOH CA 5 .   ? -64.426  -7.931  59.135  1.00 44.54  ? 703 HOH E O   1 
HETATM 11944 O  O   . HOH CA 5 .   ? -67.046  -10.179 39.684  1.00 38.50  ? 704 HOH E O   1 
HETATM 11945 O  O   . HOH CA 5 .   ? -70.976  -23.684 64.686  1.00 41.44  ? 705 HOH E O   1 
HETATM 11946 O  O   . HOH CA 5 .   ? -71.184  -19.051 48.728  1.00 34.88  ? 706 HOH E O   1 
HETATM 11947 O  O   . HOH CA 5 .   ? -86.804  -23.182 48.707  1.00 44.96  ? 707 HOH E O   1 
HETATM 11948 O  O   . HOH CA 5 .   ? -94.819  -11.671 60.248  1.00 54.44  ? 708 HOH E O   1 
HETATM 11949 O  O   . HOH CA 5 .   ? -86.075  -22.736 43.250  1.00 48.70  ? 709 HOH E O   1 
HETATM 11950 O  O   . HOH CA 5 .   ? -65.163  11.542  43.957  1.00 42.40  ? 710 HOH E O   1 
HETATM 11951 O  O   . HOH CA 5 .   ? -66.550  28.679  43.987  1.00 69.05  ? 711 HOH E O   1 
HETATM 11952 O  O   . HOH CA 5 .   ? -66.457  8.980   63.720  1.00 45.07  ? 712 HOH E O   1 
HETATM 11953 O  O   . HOH CA 5 .   ? -70.445  7.107   62.681  1.00 52.43  ? 713 HOH E O   1 
HETATM 11954 O  O   . HOH CA 5 .   ? -81.076  25.422  48.986  1.00 34.78  ? 714 HOH E O   1 
HETATM 11955 O  O   . HOH CA 5 .   ? -67.128  -4.906  34.455  1.00 62.53  ? 715 HOH E O   1 
HETATM 11956 O  O   . HOH CA 5 .   ? -73.003  28.668  47.902  1.00 44.06  ? 716 HOH E O   1 
HETATM 11957 O  O   . HOH CA 5 .   ? -75.183  -17.483 43.452  1.00 46.35  ? 717 HOH E O   1 
HETATM 11958 O  O   . HOH CA 5 .   ? -79.277  -22.349 49.065  1.00 29.96  ? 718 HOH E O   1 
HETATM 11959 O  O   . HOH CA 5 .   ? -75.286  8.387   68.147  1.00 47.66  ? 719 HOH E O   1 
HETATM 11960 O  O   . HOH CA 5 .   ? -88.483  18.143  40.004  1.00 58.14  ? 720 HOH E O   1 
HETATM 11961 O  O   . HOH CA 5 .   ? -86.223  10.414  40.673  1.00 37.51  ? 721 HOH E O   1 
HETATM 11962 O  O   . HOH CA 5 .   ? -91.019  -3.444  47.065  1.00 61.95  ? 722 HOH E O   1 
HETATM 11963 O  O   . HOH CA 5 .   ? -75.087  33.971  68.687  1.00 59.13  ? 723 HOH E O   1 
HETATM 11964 O  O   . HOH CA 5 .   ? -77.735  -23.225 66.734  1.00 52.81  ? 724 HOH E O   1 
HETATM 11965 O  O   . HOH CA 5 .   ? -93.011  -8.387  46.275  1.00 63.70  ? 725 HOH E O   1 
HETATM 11966 O  O   . HOH CA 5 .   ? -90.574  14.651  57.022  1.00 49.89  ? 726 HOH E O   1 
HETATM 11967 O  O   . HOH CA 5 .   ? -60.302  -8.079  54.343  1.00 53.70  ? 727 HOH E O   1 
HETATM 11968 O  O   . HOH CA 5 .   ? -81.582  -23.586 41.178  1.00 62.14  ? 728 HOH E O   1 
HETATM 11969 O  O   . HOH CA 5 .   ? -66.117  1.258   41.303  1.00 54.34  ? 729 HOH E O   1 
HETATM 11970 O  O   . HOH CA 5 .   ? -77.278  0.550   70.713  1.00 50.33  ? 730 HOH E O   1 
HETATM 11971 O  O   . HOH CA 5 .   ? -91.712  -9.505  49.305  1.00 56.90  ? 731 HOH E O   1 
HETATM 11972 O  O   . HOH CA 5 .   ? -72.126  -17.171 42.772  1.00 57.00  ? 732 HOH E O   1 
HETATM 11973 O  O   . HOH CA 5 .   ? -62.039  16.395  56.212  1.00 47.14  ? 733 HOH E O   1 
HETATM 11974 O  O   . HOH CA 5 .   ? -65.419  19.768  35.059  1.00 60.29  ? 734 HOH E O   1 
HETATM 11975 O  O   . HOH CA 5 .   ? -63.892  1.625   43.436  1.00 60.00  ? 735 HOH E O   1 
HETATM 11976 O  O   . HOH CA 5 .   ? -90.818  22.600  52.819  1.00 52.17  ? 736 HOH E O   1 
HETATM 11977 O  O   . HOH CA 5 .   ? -87.276  17.595  35.325  1.00 50.73  ? 737 HOH E O   1 
HETATM 11978 O  O   . HOH CA 5 .   ? -75.718  -24.621 67.526  1.00 59.35  ? 738 HOH E O   1 
HETATM 11979 O  O   . HOH CA 5 .   ? -83.982  -24.124 42.407  1.00 55.80  ? 739 HOH E O   1 
HETATM 11980 O  O   . HOH CA 5 .   ? -96.343  -18.668 59.412  1.00 28.28  ? 740 HOH E O   1 
HETATM 11981 O  O   . HOH CA 5 .   ? -86.917  13.023  59.847  1.00 38.53  ? 741 HOH E O   1 
HETATM 11982 O  O   . HOH CA 5 .   ? -81.496  -4.405  66.449  1.00 48.51  ? 742 HOH E O   1 
HETATM 11983 O  O   . HOH CA 5 .   ? -74.831  -8.986  37.923  1.00 58.61  ? 743 HOH E O   1 
HETATM 11984 O  O   . HOH CA 5 .   ? -86.414  20.448  60.572  1.00 71.53  ? 744 HOH E O   1 
HETATM 11985 O  O   . HOH CA 5 .   ? -74.876  5.145   40.028  1.00 51.73  ? 745 HOH E O   1 
HETATM 11986 O  O   . HOH CA 5 .   ? -90.408  -5.698  57.201  1.00 44.34  ? 746 HOH E O   1 
HETATM 11987 O  O   . HOH CA 5 .   ? -73.182  -14.176 36.788  1.00 50.77  ? 747 HOH E O   1 
HETATM 11988 O  O   . HOH CA 5 .   ? -67.103  11.401  64.861  1.00 50.53  ? 748 HOH E O   1 
HETATM 11989 O  O   . HOH CA 5 .   ? -74.820  21.039  71.865  1.00 51.84  ? 749 HOH E O   1 
HETATM 11990 O  O   . HOH CA 5 .   ? -87.976  -8.897  62.071  1.00 47.86  ? 750 HOH E O   1 
HETATM 11991 O  O   . HOH CA 5 .   ? -90.071  -8.975  57.615  1.00 55.20  ? 751 HOH E O   1 
HETATM 11992 O  O   . HOH CA 5 .   ? -65.853  -15.056 49.512  1.00 45.60  ? 752 HOH E O   1 
HETATM 11993 O  O   . HOH CA 5 .   ? -90.450  -4.392  41.800  1.00 59.98  ? 753 HOH E O   1 
HETATM 11994 O  O   . HOH CA 5 .   ? -91.797  23.094  51.022  1.00 50.30  ? 754 HOH E O   1 
HETATM 11995 O  O   . HOH CA 5 .   ? -85.509  27.214  74.250  1.00 64.32  ? 755 HOH E O   1 
HETATM 11996 O  O   . HOH CA 5 .   ? -68.201  4.981   42.753  1.00 51.66  ? 756 HOH E O   1 
HETATM 11997 O  O   . HOH CA 5 .   ? -77.181  -10.088 38.934  1.00 45.84  ? 757 HOH E O   1 
HETATM 11998 O  O   . HOH CA 5 .   ? -67.899  1.951   63.626  1.00 56.31  ? 758 HOH E O   1 
HETATM 11999 O  O   . HOH CA 5 .   ? -79.461  23.865  75.653  1.00 65.99  ? 759 HOH E O   1 
HETATM 12000 O  O   . HOH CA 5 .   ? -80.269  24.337  55.965  1.00 38.59  ? 760 HOH E O   1 
HETATM 12001 O  O   . HOH CA 5 .   ? -103.424 -17.774 58.432  1.00 65.28  ? 761 HOH E O   1 
HETATM 12002 O  O   . HOH CA 5 .   ? -82.407  7.595   65.057  1.00 57.51  ? 762 HOH E O   1 
HETATM 12003 O  O   . HOH CA 5 .   ? -74.616  -6.010  74.598  1.00 54.03  ? 763 HOH E O   1 
HETATM 12004 O  O   . HOH CA 5 .   ? -79.737  8.335   71.088  1.00 53.84  ? 764 HOH E O   1 
HETATM 12005 O  O   . HOH CA 5 .   ? -69.383  -1.127  38.955  1.00 63.18  ? 765 HOH E O   1 
HETATM 12006 O  O   . HOH CA 5 .   ? -77.624  -21.630 41.657  1.00 60.75  ? 766 HOH E O   1 
HETATM 12007 O  O   . HOH CA 5 .   ? -60.123  12.184  53.254  1.00 46.11  ? 767 HOH E O   1 
HETATM 12008 O  O   . HOH CA 5 .   ? -83.156  -25.886 55.552  1.00 58.81  ? 768 HOH E O   1 
HETATM 12009 O  O   . HOH CA 5 .   ? -80.356  0.887   38.838  1.00 72.69  ? 769 HOH E O   1 
HETATM 12010 O  O   . HOH CA 5 .   ? -95.598  -1.240  51.068  1.00 63.51  ? 770 HOH E O   1 
HETATM 12011 O  O   . HOH CA 5 .   ? -65.191  -7.066  62.493  1.00 50.11  ? 771 HOH E O   1 
HETATM 12012 O  O   . HOH CA 5 .   ? -82.195  27.214  59.536  1.00 50.20  ? 772 HOH E O   1 
HETATM 12013 O  O   . HOH CA 5 .   ? -80.873  10.648  72.189  1.00 75.25  ? 773 HOH E O   1 
HETATM 12014 O  O   . HOH CA 5 .   ? -66.533  11.824  72.554  1.00 37.56  ? 774 HOH E O   1 
HETATM 12015 O  O   . HOH CA 5 .   ? -88.302  -9.365  56.132  1.00 37.53  ? 775 HOH E O   1 
HETATM 12016 O  O   . HOH CA 5 .   ? -87.527  18.942  45.178  1.00 54.67  ? 776 HOH E O   1 
HETATM 12017 O  O   . HOH CA 5 .   ? -93.486  20.407  52.023  1.00 56.90  ? 777 HOH E O   1 
HETATM 12018 O  O   . HOH CA 5 .   ? -65.668  -12.026 38.523  1.00 63.60  ? 778 HOH E O   1 
HETATM 12019 O  O   . HOH CA 5 .   ? -80.087  -25.987 43.681  1.00 67.80  ? 779 HOH E O   1 
HETATM 12020 O  O   . HOH CA 5 .   ? -81.774  -24.631 57.919  1.00 47.74  ? 780 HOH E O   1 
HETATM 12021 O  O   . HOH CA 5 .   ? -82.616  20.236  38.023  1.00 58.14  ? 781 HOH E O   1 
HETATM 12022 O  O   . HOH CA 5 .   ? -59.059  23.183  58.588  1.00 63.45  ? 782 HOH E O   1 
HETATM 12023 O  O   . HOH CA 5 .   ? -80.525  10.012  64.921  1.00 52.81  ? 783 HOH E O   1 
HETATM 12024 O  O   . HOH CA 5 .   ? -95.302  -18.078 61.837  1.00 38.68  ? 784 HOH E O   1 
HETATM 12025 O  O   . HOH CA 5 .   ? -62.426  15.983  52.665  1.00 43.59  ? 785 HOH E O   1 
HETATM 12026 O  O   . HOH CA 5 .   ? -86.515  17.086  61.167  1.00 54.90  ? 786 HOH E O   1 
HETATM 12027 O  O   . HOH CA 5 .   ? -89.389  -12.278 64.955  1.00 57.10  ? 787 HOH E O   1 
HETATM 12028 O  O   . HOH CA 5 .   ? -66.019  -8.287  64.479  1.00 51.73  ? 788 HOH E O   1 
HETATM 12029 O  O   . HOH CA 5 .   ? -89.536  10.918  55.139  1.00 65.19  ? 789 HOH E O   1 
HETATM 12030 O  O   . HOH CA 5 .   ? -61.247  -4.764  52.757  1.00 63.44  ? 790 HOH E O   1 
HETATM 12031 O  O   . HOH CA 5 .   ? -78.383  10.188  73.399  1.00 41.73  ? 791 HOH E O   1 
HETATM 12032 O  O   . HOH CA 5 .   ? -73.624  28.596  53.102  1.00 42.33  ? 792 HOH E O   1 
HETATM 12033 O  O   . HOH CA 5 .   ? -81.890  26.423  55.776  1.00 53.47  ? 793 HOH E O   1 
HETATM 12034 O  O   . HOH CA 5 .   ? -87.405  -3.408  44.972  1.00 59.68  ? 794 HOH E O   1 
HETATM 12035 O  O   . HOH CA 5 .   ? -83.564  -14.108 41.282  1.00 50.66  ? 795 HOH E O   1 
HETATM 12036 O  O   . HOH CA 5 .   ? -66.855  -18.741 49.360  1.00 53.07  ? 796 HOH E O   1 
HETATM 12037 O  O   . HOH CA 5 .   ? -71.355  30.792  69.166  1.00 70.42  ? 797 HOH E O   1 
HETATM 12038 O  O   . HOH CA 5 .   ? -67.065  -4.800  64.458  1.00 63.80  ? 798 HOH E O   1 
HETATM 12039 O  O   . HOH CA 5 .   ? -82.451  -7.419  35.692  1.00 61.35  ? 799 HOH E O   1 
HETATM 12040 O  O   . HOH CA 5 .   ? -58.685  7.295   55.578  1.00 65.11  ? 800 HOH E O   1 
HETATM 12041 O  O   . HOH CA 5 .   ? -68.396  -2.797  64.137  1.00 57.42  ? 801 HOH E O   1 
HETATM 12042 O  O   . HOH CA 5 .   ? -72.224  6.008   39.660  1.00 63.11  ? 802 HOH E O   1 
HETATM 12043 O  O   . HOH CA 5 .   ? -81.067  -24.444 49.393  1.00 48.15  ? 803 HOH E O   1 
HETATM 12044 O  O   . HOH CA 5 .   ? -86.055  -2.121  43.273  1.00 51.50  ? 804 HOH E O   1 
HETATM 12045 O  O   . HOH CA 5 .   ? -65.740  9.960   41.976  1.00 58.51  ? 805 HOH E O   1 
HETATM 12046 O  O   . HOH CA 5 .   ? -60.818  17.490  47.556  1.00 66.55  ? 806 HOH E O   1 
HETATM 12047 O  O   . HOH CA 5 .   ? -60.086  -15.318 41.960  1.00 72.33  ? 807 HOH E O   1 
HETATM 12048 O  O   . HOH CA 5 .   ? -77.455  -16.945 39.113  1.00 54.67  ? 808 HOH E O   1 
HETATM 12049 O  O   . HOH CA 5 .   ? -84.006  -9.843  69.881  1.00 54.58  ? 809 HOH E O   1 
HETATM 12050 O  O   . HOH CA 5 .   ? -91.818  -22.872 48.671  1.00 55.85  ? 810 HOH E O   1 
HETATM 12051 O  O   . HOH CA 5 .   ? -84.290  -21.656 64.280  1.00 51.53  ? 811 HOH E O   1 
HETATM 12052 O  O   . HOH CA 5 .   ? -92.977  2.386   45.030  1.00 65.33  ? 812 HOH E O   1 
HETATM 12053 O  O   . HOH CA 5 .   ? -80.142  -8.168  70.489  1.00 65.06  ? 813 HOH E O   1 
HETATM 12054 O  O   . HOH CA 5 .   ? -60.373  4.587   54.398  1.00 61.27  ? 814 HOH E O   1 
HETATM 12055 O  O   . HOH CA 5 .   ? -85.034  -26.786 56.713  1.00 54.65  ? 815 HOH E O   1 
HETATM 12056 O  O   . HOH CA 5 .   ? -61.141  -19.585 66.883  1.00 61.72  ? 816 HOH E O   1 
HETATM 12057 O  O   . HOH CA 5 .   ? -87.948  -2.049  68.002  1.00 68.28  ? 817 HOH E O   1 
HETATM 12058 O  O   . HOH CA 5 .   ? -90.221  1.391   61.078  1.00 56.84  ? 818 HOH E O   1 
HETATM 12059 O  O   . HOH CA 5 .   ? -66.942  -0.583  64.434  1.00 64.98  ? 819 HOH E O   1 
HETATM 12060 O  O   . HOH CA 5 .   ? -89.291  16.918  45.707  1.00 50.98  ? 820 HOH E O   1 
HETATM 12061 O  O   . HOH CA 5 .   ? -81.551  11.824  66.197  1.00 58.50  ? 821 HOH E O   1 
HETATM 12062 O  O   . HOH CA 5 .   ? -72.969  19.320  37.580  1.00 54.91  ? 822 HOH E O   1 
HETATM 12063 O  O   . HOH CA 5 .   ? -75.607  -25.321 63.382  1.00 60.75  ? 823 HOH E O   1 
HETATM 12064 O  O   . HOH CA 5 .   ? -91.329  -10.565 51.504  1.00 49.91  ? 824 HOH E O   1 
HETATM 12065 O  O   . HOH CA 5 .   ? -70.882  5.891   65.346  1.00 56.24  ? 825 HOH E O   1 
HETATM 12066 O  O   . HOH CA 5 .   ? -89.775  3.817   60.648  1.00 56.72  ? 826 HOH E O   1 
HETATM 12067 O  O   . HOH CA 5 .   ? -72.564  2.267   58.909  1.00 54.46  ? 827 HOH E O   1 
HETATM 12068 O  O   . HOH CA 5 .   ? -65.605  -13.237 72.902  1.00 64.56  ? 828 HOH E O   1 
HETATM 12069 O  O   . HOH CA 5 .   ? -82.390  14.147  65.839  1.00 65.28  ? 829 HOH E O   1 
HETATM 12070 O  O   . HOH CA 5 .   ? -61.595  -11.905 49.774  1.00 61.03  ? 830 HOH E O   1 
HETATM 12071 O  O   . HOH CA 5 .   ? -79.996  -25.123 56.909  1.00 46.61  ? 831 HOH E O   1 
HETATM 12072 O  O   . HOH CA 5 .   ? -88.659  -22.204 40.678  1.00 60.43  ? 832 HOH E O   1 
HETATM 12073 O  O   . HOH CA 5 .   ? -78.107  25.091  49.233  1.00 52.38  ? 833 HOH E O   1 
HETATM 12074 O  O   . HOH CA 5 .   ? -93.722  6.292   53.025  1.00 59.47  ? 834 HOH E O   1 
HETATM 12075 O  O   . HOH CA 5 .   ? -60.160  15.232  63.202  1.00 63.66  ? 835 HOH E O   1 
HETATM 12076 O  O   . HOH CA 5 .   ? -68.487  7.250   64.260  1.00 57.58  ? 836 HOH E O   1 
HETATM 12077 O  O   . HOH CA 5 .   ? -68.804  15.895  68.795  1.00 50.40  ? 837 HOH E O   1 
HETATM 12078 O  O   . HOH CA 5 .   ? -72.101  2.423   61.414  1.00 47.75  ? 838 HOH E O   1 
HETATM 12079 O  O   . HOH CA 5 .   ? -80.670  18.597  72.213  1.00 53.99  ? 839 HOH E O   1 
HETATM 12080 O  O   . HOH CA 5 .   ? -64.603  -10.436 65.073  1.00 70.16  ? 840 HOH E O   1 
HETATM 12081 O  O   . HOH CA 5 .   ? -103.221 -18.691 52.348  1.00 63.97  ? 841 HOH E O   1 
HETATM 12082 O  O   . HOH CA 5 .   ? -90.053  -26.722 49.851  1.00 34.20  ? 842 HOH E O   1 
HETATM 12083 O  O   . HOH CA 5 .   ? -92.318  -26.430 51.447  1.00 30.00  ? 843 HOH E O   1 
HETATM 12084 O  O   . HOH CA 5 .   ? -66.056  30.406  42.449  1.00 63.98  ? 844 HOH E O   1 
HETATM 12085 O  O   . HOH CA 5 .   ? -63.821  -13.900 70.799  1.00 55.75  ? 845 HOH E O   1 
HETATM 12086 O  O   . HOH CA 5 .   ? -67.645  0.909   38.573  1.00 53.12  ? 846 HOH E O   1 
HETATM 12087 O  O   . HOH CA 5 .   ? -88.531  -28.547 51.206  1.00 31.12  ? 847 HOH E O   1 
HETATM 12088 O  O   . HOH CA 5 .   ? -82.006  -13.418 39.238  1.00 53.16  ? 848 HOH E O   1 
HETATM 12089 O  O   . HOH CA 5 .   ? -86.477  28.735  72.422  1.00 70.60  ? 849 HOH E O   1 
HETATM 12090 O  O   . HOH CA 5 .   ? -60.410  -0.429  54.525  1.00 64.95  ? 850 HOH E O   1 
HETATM 12091 O  O   . HOH CA 5 .   ? -62.270  -4.192  57.703  1.00 63.39  ? 851 HOH E O   1 
HETATM 12092 O  O   . HOH CA 5 .   ? -62.154  -14.072 51.199  1.00 62.07  ? 852 HOH E O   1 
HETATM 12093 O  O   . HOH CA 5 .   ? -87.469  -22.655 61.909  1.00 45.08  ? 853 HOH E O   1 
HETATM 12094 O  O   . HOH CA 5 .   ? -90.389  7.086   56.861  1.00 57.66  ? 854 HOH E O   1 
HETATM 12095 O  O   . HOH CA 5 .   ? -72.996  4.652   64.327  1.00 68.92  ? 855 HOH E O   1 
HETATM 12096 O  O   . HOH CA 5 .   ? -59.579  16.164  49.110  1.00 64.57  ? 856 HOH E O   1 
HETATM 12097 O  O   . HOH CA 5 .   ? -90.090  -23.101 43.024  1.00 76.68  ? 857 HOH E O   1 
HETATM 12098 O  O   . HOH CA 5 .   ? -91.517  8.545   54.861  1.00 58.51  ? 858 HOH E O   1 
HETATM 12099 O  O   . HOH CA 5 .   ? -87.499  21.723  39.263  1.00 58.31  ? 859 HOH E O   1 
HETATM 12100 O  O   . HOH CA 5 .   ? -64.665  -11.957 69.894  1.00 59.60  ? 860 HOH E O   1 
HETATM 12101 O  O   . HOH CA 5 .   ? -67.978  -16.492 37.284  1.00 62.39  ? 861 HOH E O   1 
HETATM 12102 O  O   . HOH CA 5 .   ? -80.615  -26.935 41.341  1.00 72.39  ? 862 HOH E O   1 
HETATM 12103 O  O   . HOH CA 5 .   ? -59.739  13.100  46.032  1.00 56.34  ? 863 HOH E O   1 
HETATM 12104 O  O   . HOH CA 5 .   ? -61.714  -3.186  59.944  1.00 69.53  ? 864 HOH E O   1 
HETATM 12105 O  O   . HOH CA 5 .   ? -91.790  -22.406 39.154  1.00 63.31  ? 865 HOH E O   1 
HETATM 12106 O  O   . HOH CA 5 .   ? -93.834  -6.682  52.573  1.00 60.02  ? 866 HOH E O   1 
HETATM 12107 O  O   . HOH CA 5 .   ? -81.306  -28.240 57.710  1.00 52.68  ? 867 HOH E O   1 
HETATM 12108 O  O   . HOH CA 5 .   ? -82.688  -28.435 60.012  1.00 72.52  ? 868 HOH E O   1 
HETATM 12109 O  O   . HOH DA 5 .   ? -56.922  -46.387 59.485  1.00 49.35  ? 501 HOH G O   1 
HETATM 12110 O  O   . HOH DA 5 .   ? -62.176  -16.793 55.969  1.00 48.11  ? 502 HOH G O   1 
HETATM 12111 O  O   . HOH DA 5 .   ? -62.710  -19.182 59.656  1.00 59.39  ? 503 HOH G O   1 
HETATM 12112 O  O   . HOH DA 5 .   ? -65.709  -23.990 42.671  1.00 51.55  ? 504 HOH G O   1 
HETATM 12113 O  O   . HOH DA 5 .   ? -59.511  -47.217 69.138  1.00 59.67  ? 505 HOH G O   1 
HETATM 12114 O  O   . HOH DA 5 .   ? -64.587  -54.024 67.353  1.00 51.65  ? 506 HOH G O   1 
HETATM 12115 O  O   . HOH DA 5 .   ? -63.236  -59.379 51.320  1.00 45.33  ? 507 HOH G O   1 
HETATM 12116 O  O   . HOH DA 5 .   ? -58.173  -62.400 62.593  1.00 51.91  ? 508 HOH G O   1 
HETATM 12117 O  O   . HOH DA 5 .   ? -66.243  -59.442 49.848  1.00 53.14  ? 509 HOH G O   1 
HETATM 12118 O  O   . HOH DA 5 .   ? -38.296  -43.808 45.377  1.00 60.33  ? 510 HOH G O   1 
HETATM 12119 O  O   . HOH DA 5 .   ? -37.094  -69.171 46.618  1.00 65.55  ? 511 HOH G O   1 
HETATM 12120 O  O   . HOH DA 5 .   ? -60.531  -52.209 39.524  1.00 59.91  ? 512 HOH G O   1 
HETATM 12121 O  O   . HOH DA 5 .   ? -40.645  -52.333 35.151  1.00 55.75  ? 513 HOH G O   1 
HETATM 12122 O  O   . HOH DA 5 .   ? -75.651  -54.859 48.122  1.00 64.47  ? 514 HOH G O   1 
HETATM 12123 O  O   . HOH DA 5 .   ? -62.926  -46.617 67.909  1.00 33.46  ? 515 HOH G O   1 
HETATM 12124 O  O   . HOH DA 5 .   ? -35.860  -48.609 56.970  1.00 46.98  ? 516 HOH G O   1 
HETATM 12125 O  O   . HOH DA 5 .   ? -38.180  -64.575 65.546  1.00 58.45  ? 517 HOH G O   1 
HETATM 12126 O  O   . HOH DA 5 .   ? -56.155  -53.614 38.665  1.00 65.22  ? 518 HOH G O   1 
HETATM 12127 O  O   . HOH DA 5 .   ? -45.559  -52.044 70.533  1.00 49.93  ? 519 HOH G O   1 
HETATM 12128 O  O   . HOH DA 5 .   ? -54.136  -32.303 49.558  1.00 46.29  ? 520 HOH G O   1 
HETATM 12129 O  O   . HOH DA 5 .   ? -46.935  -47.515 33.423  1.00 28.07  ? 521 HOH G O   1 
HETATM 12130 O  O   . HOH DA 5 .   ? -39.500  -62.073 40.154  1.00 54.61  ? 522 HOH G O   1 
HETATM 12131 O  O   . HOH DA 5 .   ? -44.258  -59.986 68.718  1.00 35.74  ? 523 HOH G O   1 
HETATM 12132 O  O   . HOH DA 5 .   ? -47.769  -38.543 59.672  1.00 59.02  ? 524 HOH G O   1 
HETATM 12133 O  O   . HOH DA 5 .   ? -59.456  -49.007 60.813  1.00 37.64  ? 525 HOH G O   1 
HETATM 12134 O  O   . HOH DA 5 .   ? -79.994  -49.569 66.864  1.00 46.37  ? 526 HOH G O   1 
HETATM 12135 O  O   . HOH DA 5 .   ? -65.537  -45.654 37.510  1.00 43.67  ? 527 HOH G O   1 
HETATM 12136 O  O   . HOH DA 5 .   ? -58.192  -38.375 40.671  1.00 52.38  ? 528 HOH G O   1 
HETATM 12137 O  O   . HOH DA 5 .   ? -70.224  -42.336 38.254  1.00 43.96  ? 529 HOH G O   1 
HETATM 12138 O  O   . HOH DA 5 .   ? -54.996  -65.713 42.002  1.00 58.78  ? 530 HOH G O   1 
HETATM 12139 O  O   . HOH DA 5 .   ? -82.991  -47.649 65.253  1.00 53.52  ? 531 HOH G O   1 
HETATM 12140 O  O   . HOH DA 5 .   ? -73.056  -24.511 59.864  1.00 25.25  ? 532 HOH G O   1 
HETATM 12141 O  O   . HOH DA 5 .   ? -55.586  -37.707 64.651  1.00 58.91  ? 533 HOH G O   1 
HETATM 12142 O  O   . HOH DA 5 .   ? -53.894  -50.532 60.667  1.00 38.29  ? 534 HOH G O   1 
HETATM 12143 O  O   . HOH DA 5 .   ? -75.335  -34.189 65.527  1.00 46.67  ? 535 HOH G O   1 
HETATM 12144 O  O   . HOH DA 5 .   ? -80.104  -42.711 53.310  1.00 41.86  ? 536 HOH G O   1 
HETATM 12145 O  O   . HOH DA 5 .   ? -47.788  -46.033 67.978  1.00 62.17  ? 537 HOH G O   1 
HETATM 12146 O  O   . HOH DA 5 .   ? -65.726  -50.263 39.841  1.00 41.01  ? 538 HOH G O   1 
HETATM 12147 O  O   . HOH DA 5 .   ? -37.614  -59.346 51.791  1.00 30.88  ? 539 HOH G O   1 
HETATM 12148 O  O   . HOH DA 5 .   ? -52.306  -53.284 31.916  1.00 48.28  ? 540 HOH G O   1 
HETATM 12149 O  O   . HOH DA 5 .   ? -50.514  -53.788 67.494  1.00 31.86  ? 541 HOH G O   1 
HETATM 12150 O  O   . HOH DA 5 .   ? -72.265  -28.483 62.034  1.00 33.48  ? 542 HOH G O   1 
HETATM 12151 O  O   . HOH DA 5 .   ? -58.402  -46.238 61.783  1.00 42.20  ? 543 HOH G O   1 
HETATM 12152 O  O   . HOH DA 5 .   ? -35.647  -76.899 50.144  1.00 42.06  ? 544 HOH G O   1 
HETATM 12153 O  O   . HOH DA 5 .   ? -37.872  -57.308 45.854  1.00 36.44  ? 545 HOH G O   1 
HETATM 12154 O  O   . HOH DA 5 .   ? -58.933  -65.147 46.565  1.00 50.62  ? 546 HOH G O   1 
HETATM 12155 O  O   . HOH DA 5 .   ? -49.241  -63.348 40.959  1.00 27.72  ? 547 HOH G O   1 
HETATM 12156 O  O   . HOH DA 5 .   ? -57.406  -45.383 44.193  1.00 39.16  ? 548 HOH G O   1 
HETATM 12157 O  O   . HOH DA 5 .   ? -75.592  -38.819 53.419  1.00 23.59  ? 549 HOH G O   1 
HETATM 12158 O  O   . HOH DA 5 .   ? -56.280  -43.529 42.630  1.00 48.66  ? 550 HOH G O   1 
HETATM 12159 O  O   . HOH DA 5 .   ? -62.004  -61.789 52.921  1.00 51.16  ? 551 HOH G O   1 
HETATM 12160 O  O   . HOH DA 5 .   ? -66.446  -32.917 42.626  1.00 30.97  ? 552 HOH G O   1 
HETATM 12161 O  O   . HOH DA 5 .   ? -55.443  -51.419 43.709  1.00 46.88  ? 553 HOH G O   1 
HETATM 12162 O  O   . HOH DA 5 .   ? -42.807  -52.242 39.793  1.00 32.71  ? 554 HOH G O   1 
HETATM 12163 O  O   . HOH DA 5 .   ? -50.039  -70.189 45.878  1.00 41.08  ? 555 HOH G O   1 
HETATM 12164 O  O   . HOH DA 5 .   ? -77.057  -36.309 70.673  1.00 48.08  ? 556 HOH G O   1 
HETATM 12165 O  O   . HOH DA 5 .   ? -69.093  -40.751 70.236  1.00 30.53  ? 557 HOH G O   1 
HETATM 12166 O  O   . HOH DA 5 .   ? -54.447  -47.753 61.594  1.00 48.71  ? 558 HOH G O   1 
HETATM 12167 O  O   . HOH DA 5 .   ? -75.309  -39.680 47.216  1.00 38.78  ? 559 HOH G O   1 
HETATM 12168 O  O   . HOH DA 5 .   ? -52.836  -48.217 56.910  1.00 21.54  ? 560 HOH G O   1 
HETATM 12169 O  O   . HOH DA 5 .   ? -77.102  -20.782 53.489  1.00 32.51  ? 561 HOH G O   1 
HETATM 12170 O  O   . HOH DA 5 .   ? -46.586  -63.229 40.169  1.00 35.95  ? 562 HOH G O   1 
HETATM 12171 O  O   . HOH DA 5 .   ? -45.542  -43.629 39.857  1.00 47.23  ? 563 HOH G O   1 
HETATM 12172 O  O   . HOH DA 5 .   ? -41.167  -70.686 58.863  1.00 37.67  ? 564 HOH G O   1 
HETATM 12173 O  O   . HOH DA 5 .   ? -49.482  -65.951 54.480  1.00 55.61  ? 565 HOH G O   1 
HETATM 12174 O  O   . HOH DA 5 .   ? -42.393  -73.729 40.150  1.00 64.06  ? 566 HOH G O   1 
HETATM 12175 O  O   . HOH DA 5 .   ? -80.933  -37.819 48.991  1.00 43.46  ? 567 HOH G O   1 
HETATM 12176 O  O   . HOH DA 5 .   ? -44.160  -44.726 33.462  1.00 33.11  ? 568 HOH G O   1 
HETATM 12177 O  O   . HOH DA 5 .   ? -64.734  -60.413 54.912  1.00 58.36  ? 569 HOH G O   1 
HETATM 12178 O  O   . HOH DA 5 .   ? -54.252  -54.545 41.555  1.00 32.92  ? 570 HOH G O   1 
HETATM 12179 O  O   . HOH DA 5 .   ? -49.913  -38.567 53.285  1.00 38.05  ? 571 HOH G O   1 
HETATM 12180 O  O   . HOH DA 5 .   ? -80.610  -47.317 63.208  1.00 35.69  ? 572 HOH G O   1 
HETATM 12181 O  O   . HOH DA 5 .   ? -67.249  -51.910 38.773  1.00 43.47  ? 573 HOH G O   1 
HETATM 12182 O  O   . HOH DA 5 .   ? -47.505  -45.788 40.206  1.00 32.92  ? 574 HOH G O   1 
HETATM 12183 O  O   . HOH DA 5 .   ? -66.134  -57.816 53.877  1.00 45.82  ? 575 HOH G O   1 
HETATM 12184 O  O   . HOH DA 5 .   ? -60.343  -50.557 56.695  1.00 19.40  ? 576 HOH G O   1 
HETATM 12185 O  O   . HOH DA 5 .   ? -70.730  -20.050 46.297  1.00 59.88  ? 577 HOH G O   1 
HETATM 12186 O  O   . HOH DA 5 .   ? -42.869  -64.168 66.234  1.00 43.24  ? 578 HOH G O   1 
HETATM 12187 O  O   . HOH DA 5 .   ? -75.078  -35.856 67.572  1.00 47.19  ? 579 HOH G O   1 
HETATM 12188 O  O   . HOH DA 5 .   ? -31.224  -50.163 51.864  1.00 59.28  ? 580 HOH G O   1 
HETATM 12189 O  O   . HOH DA 5 .   ? -41.744  -70.516 43.857  1.00 51.33  ? 581 HOH G O   1 
HETATM 12190 O  O   . HOH DA 5 .   ? -77.452  -50.323 56.607  1.00 42.65  ? 582 HOH G O   1 
HETATM 12191 O  O   . HOH DA 5 .   ? -67.863  -49.088 70.659  1.00 45.44  ? 583 HOH G O   1 
HETATM 12192 O  O   . HOH DA 5 .   ? -52.358  -45.454 56.548  1.00 22.35  ? 584 HOH G O   1 
HETATM 12193 O  O   . HOH DA 5 .   ? -63.744  -42.726 38.425  1.00 28.92  ? 585 HOH G O   1 
HETATM 12194 O  O   . HOH DA 5 .   ? -41.131  -76.456 48.537  1.00 37.47  ? 586 HOH G O   1 
HETATM 12195 O  O   . HOH DA 5 .   ? -45.115  -42.012 56.853  1.00 39.84  ? 587 HOH G O   1 
HETATM 12196 O  O   . HOH DA 5 .   ? -70.477  -36.395 68.457  1.00 40.34  ? 588 HOH G O   1 
HETATM 12197 O  O   . HOH DA 5 .   ? -71.734  -26.417 47.446  1.00 36.76  ? 589 HOH G O   1 
HETATM 12198 O  O   . HOH DA 5 .   ? -74.049  -34.485 42.700  1.00 48.67  ? 590 HOH G O   1 
HETATM 12199 O  O   . HOH DA 5 .   ? -64.085  -42.446 68.583  1.00 29.56  ? 591 HOH G O   1 
HETATM 12200 O  O   . HOH DA 5 .   ? -60.873  -46.710 71.257  1.00 47.07  ? 592 HOH G O   1 
HETATM 12201 O  O   . HOH DA 5 .   ? -63.897  -32.934 43.665  1.00 24.84  ? 593 HOH G O   1 
HETATM 12202 O  O   . HOH DA 5 .   ? -57.347  -44.986 40.152  1.00 55.99  ? 594 HOH G O   1 
HETATM 12203 O  O   . HOH DA 5 .   ? -63.351  -32.579 57.245  1.00 36.97  ? 595 HOH G O   1 
HETATM 12204 O  O   . HOH DA 5 .   ? -45.440  -42.878 52.645  1.00 36.92  ? 596 HOH G O   1 
HETATM 12205 O  O   . HOH DA 5 .   ? -41.767  -64.061 49.774  1.00 32.25  ? 597 HOH G O   1 
HETATM 12206 O  O   . HOH DA 5 .   ? -60.762  -53.191 55.873  1.00 24.49  ? 598 HOH G O   1 
HETATM 12207 O  O   . HOH DA 5 .   ? -76.220  -28.436 42.076  1.00 66.40  ? 599 HOH G O   1 
HETATM 12208 O  O   . HOH DA 5 .   ? -71.962  -21.446 52.519  1.00 23.43  ? 600 HOH G O   1 
HETATM 12209 O  O   . HOH DA 5 .   ? -67.738  -55.136 51.555  1.00 32.15  ? 601 HOH G O   1 
HETATM 12210 O  O   . HOH DA 5 .   ? -71.257  -33.711 52.270  1.00 24.00  ? 602 HOH G O   1 
HETATM 12211 O  O   . HOH DA 5 .   ? -40.284  -74.136 56.202  1.00 37.92  ? 603 HOH G O   1 
HETATM 12212 O  O   . HOH DA 5 .   ? -48.404  -38.474 46.659  1.00 57.62  ? 604 HOH G O   1 
HETATM 12213 O  O   . HOH DA 5 .   ? -42.753  -61.433 66.977  1.00 41.27  ? 605 HOH G O   1 
HETATM 12214 O  O   . HOH DA 5 .   ? -63.049  -26.849 49.486  1.00 37.04  ? 606 HOH G O   1 
HETATM 12215 O  O   . HOH DA 5 .   ? -51.264  -67.102 50.009  1.00 29.48  ? 607 HOH G O   1 
HETATM 12216 O  O   . HOH DA 5 .   ? -70.071  -43.740 40.231  1.00 41.32  ? 608 HOH G O   1 
HETATM 12217 O  O   . HOH DA 5 .   ? -69.706  -24.563 50.273  1.00 28.73  ? 609 HOH G O   1 
HETATM 12218 O  O   . HOH DA 5 .   ? -68.147  -56.602 55.563  1.00 40.35  ? 610 HOH G O   1 
HETATM 12219 O  O   . HOH DA 5 .   ? -51.182  -59.346 36.238  1.00 55.60  ? 611 HOH G O   1 
HETATM 12220 O  O   . HOH DA 5 .   ? -54.965  -53.400 61.376  1.00 49.31  ? 612 HOH G O   1 
HETATM 12221 O  O   . HOH DA 5 .   ? -61.806  -30.544 53.062  1.00 26.45  ? 613 HOH G O   1 
HETATM 12222 O  O   . HOH DA 5 .   ? -76.817  -40.079 72.181  1.00 39.91  ? 614 HOH G O   1 
HETATM 12223 O  O   . HOH DA 5 .   ? -46.944  -40.457 55.769  1.00 45.43  ? 615 HOH G O   1 
HETATM 12224 O  O   . HOH DA 5 .   ? -75.450  -42.824 71.869  1.00 37.76  ? 616 HOH G O   1 
HETATM 12225 O  O   . HOH DA 5 .   ? -52.589  -54.442 70.708  1.00 49.17  ? 617 HOH G O   1 
HETATM 12226 O  O   . HOH DA 5 .   ? -73.556  -47.334 70.404  1.00 26.64  ? 618 HOH G O   1 
HETATM 12227 O  O   . HOH DA 5 .   ? -42.010  -43.661 58.430  1.00 52.94  ? 619 HOH G O   1 
HETATM 12228 O  O   . HOH DA 5 .   ? -39.710  -53.567 69.940  1.00 36.88  ? 620 HOH G O   1 
HETATM 12229 O  O   . HOH DA 5 .   ? -81.646  -40.082 65.266  1.00 51.71  ? 621 HOH G O   1 
HETATM 12230 O  O   . HOH DA 5 .   ? -65.188  -28.476 60.743  1.00 35.15  ? 622 HOH G O   1 
HETATM 12231 O  O   . HOH DA 5 .   ? -53.004  -60.070 64.625  1.00 53.08  ? 623 HOH G O   1 
HETATM 12232 O  O   . HOH DA 5 .   ? -54.490  -38.128 45.789  1.00 39.42  ? 624 HOH G O   1 
HETATM 12233 O  O   . HOH DA 5 .   ? -58.172  -34.299 46.375  1.00 36.60  ? 625 HOH G O   1 
HETATM 12234 O  O   . HOH DA 5 .   ? -57.552  -40.344 65.099  1.00 40.69  ? 626 HOH G O   1 
HETATM 12235 O  O   . HOH DA 5 .   ? -60.134  -34.486 64.446  1.00 35.10  ? 627 HOH G O   1 
HETATM 12236 O  O   . HOH DA 5 .   ? -58.791  -41.730 42.546  1.00 30.13  ? 628 HOH G O   1 
HETATM 12237 O  O   . HOH DA 5 .   ? -74.191  -31.345 64.948  1.00 41.87  ? 629 HOH G O   1 
HETATM 12238 O  O   . HOH DA 5 .   ? -49.185  -40.454 45.977  1.00 37.31  ? 630 HOH G O   1 
HETATM 12239 O  O   . HOH DA 5 .   ? -78.240  -33.953 64.792  1.00 37.82  ? 631 HOH G O   1 
HETATM 12240 O  O   . HOH DA 5 .   ? -55.419  -50.230 57.992  1.00 27.20  ? 632 HOH G O   1 
HETATM 12241 O  O   . HOH DA 5 .   ? -42.683  -56.579 36.630  1.00 54.84  ? 633 HOH G O   1 
HETATM 12242 O  O   . HOH DA 5 .   ? -72.711  -49.767 39.671  1.00 41.32  ? 634 HOH G O   1 
HETATM 12243 O  O   . HOH DA 5 .   ? -57.782  -48.671 58.111  1.00 28.25  ? 635 HOH G O   1 
HETATM 12244 O  O   . HOH DA 5 .   ? -53.133  -65.308 61.844  1.00 39.33  ? 636 HOH G O   1 
HETATM 12245 O  O   . HOH DA 5 .   ? -49.543  -69.448 36.501  1.00 60.69  ? 637 HOH G O   1 
HETATM 12246 O  O   . HOH DA 5 .   ? -61.638  -22.114 58.021  1.00 52.75  ? 638 HOH G O   1 
HETATM 12247 O  O   . HOH DA 5 .   ? -64.219  -31.189 59.709  1.00 46.56  ? 639 HOH G O   1 
HETATM 12248 O  O   . HOH DA 5 .   ? -31.603  -60.051 63.833  1.00 53.31  ? 640 HOH G O   1 
HETATM 12249 O  O   . HOH DA 5 .   ? -49.166  -58.039 67.370  1.00 33.65  ? 641 HOH G O   1 
HETATM 12250 O  O   . HOH DA 5 .   ? -39.258  -69.049 61.542  1.00 51.26  ? 642 HOH G O   1 
HETATM 12251 O  O   . HOH DA 5 .   ? -54.268  -47.791 38.539  1.00 39.56  ? 643 HOH G O   1 
HETATM 12252 O  O   . HOH DA 5 .   ? -66.560  -64.307 48.875  1.00 72.14  ? 644 HOH G O   1 
HETATM 12253 O  O   . HOH DA 5 .   ? -32.790  -52.877 62.920  1.00 45.51  ? 645 HOH G O   1 
HETATM 12254 O  O   . HOH DA 5 .   ? -76.770  -51.607 58.836  1.00 48.69  ? 646 HOH G O   1 
HETATM 12255 O  O   . HOH DA 5 .   ? -54.920  -62.168 43.976  1.00 43.78  ? 647 HOH G O   1 
HETATM 12256 O  O   . HOH DA 5 .   ? -79.560  -40.616 72.809  1.00 48.85  ? 648 HOH G O   1 
HETATM 12257 O  O   . HOH DA 5 .   ? -55.724  -64.940 38.993  1.00 65.82  ? 649 HOH G O   1 
HETATM 12258 O  O   . HOH DA 5 .   ? -37.854  -57.265 42.083  1.00 43.29  ? 650 HOH G O   1 
HETATM 12259 O  O   . HOH DA 5 .   ? -48.799  -80.210 52.299  1.00 53.90  ? 651 HOH G O   1 
HETATM 12260 O  O   . HOH DA 5 .   ? -40.036  -46.115 40.194  1.00 35.10  ? 652 HOH G O   1 
HETATM 12261 O  O   . HOH DA 5 .   ? -59.095  -41.020 73.676  1.00 74.28  ? 653 HOH G O   1 
HETATM 12262 O  O   . HOH DA 5 .   ? -36.471  -47.542 59.262  1.00 55.20  ? 654 HOH G O   1 
HETATM 12263 O  O   . HOH DA 5 .   ? -33.796  -54.259 61.380  1.00 32.78  ? 655 HOH G O   1 
HETATM 12264 O  O   . HOH DA 5 .   ? -42.148  -62.923 38.834  1.00 58.51  ? 656 HOH G O   1 
HETATM 12265 O  O   . HOH DA 5 .   ? -77.985  -41.801 49.026  1.00 33.45  ? 657 HOH G O   1 
HETATM 12266 O  O   . HOH DA 5 .   ? -50.950  -36.677 54.907  1.00 52.06  ? 658 HOH G O   1 
HETATM 12267 O  O   . HOH DA 5 .   ? -57.715  -30.513 45.198  1.00 60.17  ? 659 HOH G O   1 
HETATM 12268 O  O   . HOH DA 5 .   ? -34.056  -55.459 45.517  1.00 52.68  ? 660 HOH G O   1 
HETATM 12269 O  O   . HOH DA 5 .   ? -79.433  -45.297 61.987  1.00 27.24  ? 661 HOH G O   1 
HETATM 12270 O  O   . HOH DA 5 .   ? -48.812  -78.252 53.718  1.00 47.66  ? 662 HOH G O   1 
HETATM 12271 O  O   . HOH DA 5 .   ? -75.008  -39.176 43.307  1.00 44.75  ? 663 HOH G O   1 
HETATM 12272 O  O   . HOH DA 5 .   ? -58.619  -47.621 38.573  1.00 39.76  ? 664 HOH G O   1 
HETATM 12273 O  O   . HOH DA 5 .   ? -55.717  -59.667 63.536  1.00 47.18  ? 665 HOH G O   1 
HETATM 12274 O  O   . HOH DA 5 .   ? -65.776  -27.490 65.259  1.00 60.87  ? 666 HOH G O   1 
HETATM 12275 O  O   . HOH DA 5 .   ? -70.456  -39.060 68.753  1.00 33.90  ? 667 HOH G O   1 
HETATM 12276 O  O   . HOH DA 5 .   ? -37.984  -58.929 40.110  1.00 59.52  ? 668 HOH G O   1 
HETATM 12277 O  O   . HOH DA 5 .   ? -63.522  -34.590 69.799  1.00 57.33  ? 669 HOH G O   1 
HETATM 12278 O  O   . HOH DA 5 .   ? -77.588  -30.855 41.496  1.00 67.04  ? 670 HOH G O   1 
HETATM 12279 O  O   . HOH DA 5 .   ? -59.903  -66.061 48.724  1.00 55.02  ? 671 HOH G O   1 
HETATM 12280 O  O   . HOH DA 5 .   ? -58.740  -58.510 44.022  1.00 46.78  ? 672 HOH G O   1 
HETATM 12281 O  O   . HOH DA 5 .   ? -76.017  -33.408 41.277  1.00 80.83  ? 673 HOH G O   1 
HETATM 12282 O  O   . HOH DA 5 .   ? -51.788  -67.058 56.314  1.00 52.49  ? 674 HOH G O   1 
HETATM 12283 O  O   . HOH DA 5 .   ? -74.113  -56.881 54.179  1.00 52.86  ? 675 HOH G O   1 
HETATM 12284 O  O   . HOH DA 5 .   ? -61.433  -31.850 59.294  1.00 48.58  ? 676 HOH G O   1 
HETATM 12285 O  O   . HOH DA 5 .   ? -63.634  -56.415 44.523  1.00 41.14  ? 677 HOH G O   1 
HETATM 12286 O  O   . HOH DA 5 .   ? -60.703  -52.190 65.054  1.00 54.55  ? 678 HOH G O   1 
HETATM 12287 O  O   . HOH DA 5 .   ? -36.680  -61.237 70.695  1.00 55.61  ? 679 HOH G O   1 
HETATM 12288 O  O   . HOH DA 5 .   ? -35.612  -49.068 50.264  1.00 48.59  ? 680 HOH G O   1 
HETATM 12289 O  O   . HOH DA 5 .   ? -68.040  -52.470 34.574  1.00 60.24  ? 681 HOH G O   1 
HETATM 12290 O  O   . HOH DA 5 .   ? -64.510  -27.793 38.666  1.00 55.12  ? 682 HOH G O   1 
HETATM 12291 O  O   . HOH DA 5 .   ? -38.373  -69.039 39.905  1.00 48.04  ? 683 HOH G O   1 
HETATM 12292 O  O   . HOH DA 5 .   ? -35.107  -55.673 48.071  1.00 35.07  ? 684 HOH G O   1 
HETATM 12293 O  O   . HOH DA 5 .   ? -68.934  -43.872 37.338  1.00 52.28  ? 685 HOH G O   1 
HETATM 12294 O  O   . HOH DA 5 .   ? -38.901  -41.659 55.949  1.00 66.25  ? 686 HOH G O   1 
HETATM 12295 O  O   . HOH DA 5 .   ? -55.409  -50.664 39.991  1.00 48.88  ? 687 HOH G O   1 
HETATM 12296 O  O   . HOH DA 5 .   ? -71.118  -33.240 41.299  1.00 50.39  ? 688 HOH G O   1 
HETATM 12297 O  O   . HOH DA 5 .   ? -48.208  -70.750 57.463  1.00 49.91  ? 689 HOH G O   1 
HETATM 12298 O  O   . HOH DA 5 .   ? -36.306  -56.907 38.307  1.00 70.29  ? 690 HOH G O   1 
HETATM 12299 O  O   . HOH DA 5 .   ? -71.627  -53.427 58.693  1.00 49.90  ? 691 HOH G O   1 
HETATM 12300 O  O   . HOH DA 5 .   ? -41.553  -45.593 59.381  1.00 51.87  ? 692 HOH G O   1 
HETATM 12301 O  O   . HOH DA 5 .   ? -41.229  -46.644 71.121  1.00 59.33  ? 693 HOH G O   1 
HETATM 12302 O  O   . HOH DA 5 .   ? -73.375  -23.613 48.857  1.00 39.48  ? 694 HOH G O   1 
HETATM 12303 O  O   . HOH DA 5 .   ? -52.607  -66.846 58.864  1.00 65.17  ? 695 HOH G O   1 
HETATM 12304 O  O   . HOH DA 5 .   ? -48.738  -37.703 57.155  1.00 56.41  ? 696 HOH G O   1 
HETATM 12305 O  O   . HOH DA 5 .   ? -36.185  -67.483 39.192  1.00 56.93  ? 697 HOH G O   1 
HETATM 12306 O  O   . HOH DA 5 .   ? -39.128  -45.597 43.385  1.00 58.70  ? 698 HOH G O   1 
HETATM 12307 O  O   . HOH DA 5 .   ? -53.935  -40.090 43.861  1.00 53.50  ? 699 HOH G O   1 
HETATM 12308 O  O   . HOH DA 5 .   ? -35.126  -66.267 62.113  1.00 51.46  ? 700 HOH G O   1 
HETATM 12309 O  O   . HOH DA 5 .   ? -68.419  -41.768 38.855  1.00 48.76  ? 701 HOH G O   1 
HETATM 12310 O  O   . HOH DA 5 .   ? -36.145  -52.776 37.780  1.00 66.37  ? 702 HOH G O   1 
HETATM 12311 O  O   . HOH DA 5 .   ? -36.256  -53.947 41.934  1.00 54.51  ? 703 HOH G O   1 
HETATM 12312 O  O   . HOH DA 5 .   ? -41.024  -52.606 37.326  1.00 35.64  ? 704 HOH G O   1 
HETATM 12313 O  O   . HOH DA 5 .   ? -47.973  -47.070 64.801  1.00 56.62  ? 705 HOH G O   1 
HETATM 12314 O  O   . HOH DA 5 .   ? -77.251  -33.270 49.483  1.00 27.27  ? 706 HOH G O   1 
HETATM 12315 O  O   . HOH DA 5 .   ? -60.392  -30.426 49.403  1.00 55.11  ? 707 HOH G O   1 
HETATM 12316 O  O   . HOH DA 5 .   ? -66.341  -27.088 62.850  1.00 55.67  ? 708 HOH G O   1 
HETATM 12317 O  O   . HOH DA 5 .   ? -74.437  -26.885 43.538  1.00 50.35  ? 709 HOH G O   1 
HETATM 12318 O  O   . HOH DA 5 .   ? -77.853  -30.591 49.597  1.00 40.48  ? 710 HOH G O   1 
HETATM 12319 O  O   . HOH DA 5 .   ? -71.121  -31.558 37.172  1.00 69.07  ? 711 HOH G O   1 
HETATM 12320 O  O   . HOH DA 5 .   ? -65.208  -20.377 59.252  1.00 34.61  ? 712 HOH G O   1 
HETATM 12321 O  O   . HOH DA 5 .   ? -71.018  -55.534 57.357  1.00 50.18  ? 713 HOH G O   1 
HETATM 12322 O  O   . HOH DA 5 .   ? -61.029  -57.846 64.528  1.00 60.51  ? 714 HOH G O   1 
HETATM 12323 O  O   . HOH DA 5 .   ? -35.796  -64.029 47.112  1.00 38.14  ? 715 HOH G O   1 
HETATM 12324 O  O   . HOH DA 5 .   ? -60.076  -40.233 66.311  1.00 47.75  ? 716 HOH G O   1 
HETATM 12325 O  O   . HOH DA 5 .   ? -38.821  -46.658 34.526  1.00 62.63  ? 717 HOH G O   1 
HETATM 12326 O  O   . HOH DA 5 .   ? -59.377  -30.361 56.949  1.00 56.39  ? 718 HOH G O   1 
HETATM 12327 O  O   . HOH DA 5 .   ? -73.918  -26.074 48.750  1.00 48.08  ? 719 HOH G O   1 
HETATM 12328 O  O   . HOH DA 5 .   ? -70.268  -52.636 62.768  1.00 53.76  ? 720 HOH G O   1 
HETATM 12329 O  O   . HOH DA 5 .   ? -77.217  -48.692 49.825  1.00 51.71  ? 721 HOH G O   1 
HETATM 12330 O  O   . HOH DA 5 .   ? -57.011  -31.518 56.498  1.00 45.24  ? 722 HOH G O   1 
HETATM 12331 O  O   . HOH DA 5 .   ? -72.746  -38.421 38.527  1.00 58.12  ? 723 HOH G O   1 
HETATM 12332 O  O   . HOH DA 5 .   ? -29.369  -56.691 66.812  1.00 45.92  ? 724 HOH G O   1 
HETATM 12333 O  O   . HOH DA 5 .   ? -61.137  -25.943 46.151  1.00 54.60  ? 725 HOH G O   1 
HETATM 12334 O  O   . HOH DA 5 .   ? -61.244  -31.626 55.925  1.00 42.84  ? 726 HOH G O   1 
HETATM 12335 O  O   . HOH DA 5 .   ? -56.496  -66.783 53.396  1.00 45.69  ? 727 HOH G O   1 
HETATM 12336 O  O   . HOH DA 5 .   ? -38.537  -51.789 36.852  1.00 56.26  ? 728 HOH G O   1 
HETATM 12337 O  O   . HOH DA 5 .   ? -33.262  -51.579 49.475  1.00 55.46  ? 729 HOH G O   1 
HETATM 12338 O  O   . HOH DA 5 .   ? -74.970  -36.765 42.448  1.00 59.50  ? 730 HOH G O   1 
HETATM 12339 O  O   . HOH DA 5 .   ? -69.286  -55.218 49.680  1.00 68.00  ? 731 HOH G O   1 
HETATM 12340 O  O   . HOH DA 5 .   ? -56.561  -41.456 40.064  1.00 64.29  ? 732 HOH G O   1 
HETATM 12341 O  O   . HOH DA 5 .   ? -56.933  -35.352 44.400  1.00 58.51  ? 733 HOH G O   1 
HETATM 12342 O  O   . HOH DA 5 .   ? -56.870  -43.087 66.012  1.00 68.68  ? 734 HOH G O   1 
HETATM 12343 O  O   . HOH DA 5 .   ? -48.553  -43.243 39.580  1.00 75.23  ? 735 HOH G O   1 
HETATM 12344 O  O   . HOH DA 5 .   ? -82.258  -49.283 60.082  1.00 47.09  ? 736 HOH G O   1 
HETATM 12345 O  O   . HOH DA 5 .   ? -32.678  -63.571 40.876  1.00 66.68  ? 737 HOH G O   1 
HETATM 12346 O  O   . HOH DA 5 .   ? -59.288  -56.510 42.463  1.00 49.68  ? 738 HOH G O   1 
HETATM 12347 O  O   . HOH DA 5 .   ? -68.931  -19.834 48.790  1.00 59.08  ? 739 HOH G O   1 
HETATM 12348 O  O   . HOH DA 5 .   ? -50.797  -71.896 42.091  1.00 68.51  ? 740 HOH G O   1 
HETATM 12349 O  O   . HOH DA 5 .   ? -57.478  -43.745 63.755  1.00 56.96  ? 741 HOH G O   1 
HETATM 12350 O  O   . HOH DA 5 .   ? -74.615  -37.213 39.574  1.00 62.38  ? 742 HOH G O   1 
HETATM 12351 O  O   . HOH DA 5 .   ? -50.336  -45.707 35.594  1.00 44.30  ? 743 HOH G O   1 
HETATM 12352 O  O   . HOH DA 5 .   ? -56.390  -48.011 39.473  1.00 59.55  ? 744 HOH G O   1 
HETATM 12353 O  O   . HOH DA 5 .   ? -45.462  -40.975 59.313  1.00 61.72  ? 745 HOH G O   1 
HETATM 12354 O  O   . HOH DA 5 .   ? -73.936  -42.907 37.142  1.00 51.23  ? 746 HOH G O   1 
HETATM 12355 O  O   . HOH DA 5 .   ? -65.172  -21.305 61.696  1.00 40.39  ? 747 HOH G O   1 
HETATM 12356 O  O   . HOH DA 5 .   ? -80.028  -45.594 49.728  1.00 55.59  ? 748 HOH G O   1 
HETATM 12357 O  O   . HOH DA 5 .   ? -65.653  -52.768 64.025  1.00 57.89  ? 749 HOH G O   1 
HETATM 12358 O  O   . HOH DA 5 .   ? -56.078  -61.000 41.947  1.00 56.54  ? 750 HOH G O   1 
HETATM 12359 O  O   . HOH DA 5 .   ? -76.637  -42.459 42.756  1.00 44.60  ? 751 HOH G O   1 
HETATM 12360 O  O   . HOH DA 5 .   ? -57.643  -47.294 67.167  1.00 61.11  ? 752 HOH G O   1 
HETATM 12361 O  O   . HOH DA 5 .   ? -56.114  -32.926 40.756  1.00 64.55  ? 753 HOH G O   1 
HETATM 12362 O  O   . HOH DA 5 .   ? -61.782  -33.003 69.440  1.00 61.15  ? 754 HOH G O   1 
HETATM 12363 O  O   . HOH DA 5 .   ? -44.295  -62.235 39.104  1.00 47.94  ? 755 HOH G O   1 
HETATM 12364 O  O   . HOH DA 5 .   ? -49.519  -43.781 37.339  1.00 69.89  ? 756 HOH G O   1 
HETATM 12365 O  O   . HOH DA 5 .   ? -55.949  -55.477 62.719  1.00 58.31  ? 757 HOH G O   1 
HETATM 12366 O  O   . HOH DA 5 .   ? -56.156  -35.542 66.832  1.00 64.36  ? 758 HOH G O   1 
HETATM 12367 O  O   . HOH DA 5 .   ? -29.846  -50.485 72.870  1.00 68.59  ? 759 HOH G O   1 
HETATM 12368 O  O   . HOH DA 5 .   ? -62.540  -29.466 64.377  1.00 55.97  ? 760 HOH G O   1 
HETATM 12369 O  O   . HOH DA 5 .   ? -73.488  -29.251 64.303  1.00 63.44  ? 761 HOH G O   1 
HETATM 12370 O  O   . HOH DA 5 .   ? -58.847  -50.728 58.755  1.00 50.65  ? 762 HOH G O   1 
HETATM 12371 O  O   . HOH DA 5 .   ? -52.492  -52.049 68.518  1.00 60.71  ? 763 HOH G O   1 
HETATM 12372 O  O   . HOH DA 5 .   ? -45.547  -47.337 65.230  1.00 61.92  ? 764 HOH G O   1 
HETATM 12373 O  O   . HOH DA 5 .   ? -67.816  -35.772 70.383  1.00 66.22  ? 765 HOH G O   1 
HETATM 12374 O  O   . HOH DA 5 .   ? -55.585  -52.409 35.608  1.00 71.70  ? 766 HOH G O   1 
HETATM 12375 O  O   . HOH DA 5 .   ? -78.413  -28.369 55.500  1.00 53.24  ? 767 HOH G O   1 
HETATM 12376 O  O   . HOH DA 5 .   ? -78.697  -51.251 68.617  1.00 57.11  ? 768 HOH G O   1 
HETATM 12377 O  O   . HOH DA 5 .   ? -35.055  -68.261 54.731  1.00 52.72  ? 769 HOH G O   1 
HETATM 12378 O  O   . HOH DA 5 .   ? -78.253  -30.249 57.370  1.00 52.01  ? 770 HOH G O   1 
HETATM 12379 O  O   . HOH DA 5 .   ? -60.498  -64.530 53.535  1.00 63.65  ? 771 HOH G O   1 
HETATM 12380 O  O   . HOH DA 5 .   ? -68.081  -52.583 64.274  1.00 61.36  ? 772 HOH G O   1 
HETATM 12381 O  O   . HOH DA 5 .   ? -49.230  -38.765 43.173  1.00 55.21  ? 773 HOH G O   1 
HETATM 12382 O  O   . HOH DA 5 .   ? -56.684  -51.030 38.283  1.00 53.16  ? 774 HOH G O   1 
HETATM 12383 O  O   . HOH DA 5 .   ? -71.206  -57.752 53.432  1.00 60.78  ? 775 HOH G O   1 
HETATM 12384 O  O   . HOH DA 5 .   ? -68.696  -33.758 41.196  1.00 48.82  ? 776 HOH G O   1 
HETATM 12385 O  O   . HOH DA 5 .   ? -61.534  -55.207 63.989  1.00 57.74  ? 777 HOH G O   1 
HETATM 12386 O  O   . HOH DA 5 .   ? -65.389  -28.522 34.705  1.00 52.60  ? 778 HOH G O   1 
HETATM 12387 O  O   . HOH DA 5 .   ? -53.028  -50.081 33.459  1.00 64.15  ? 779 HOH G O   1 
HETATM 12388 O  O   . HOH DA 5 .   ? -57.382  -45.672 65.513  1.00 67.04  ? 780 HOH G O   1 
HETATM 12389 O  O   . HOH DA 5 .   ? -56.333  -58.906 40.458  1.00 55.10  ? 781 HOH G O   1 
HETATM 12390 O  O   . HOH DA 5 .   ? -43.336  -47.689 64.841  1.00 67.91  ? 782 HOH G O   1 
HETATM 12391 O  O   . HOH DA 5 .   ? -34.523  -70.358 52.484  1.00 62.17  ? 783 HOH G O   1 
HETATM 12392 O  O   . HOH DA 5 .   ? -60.939  -28.578 50.977  1.00 47.29  ? 784 HOH G O   1 
HETATM 12393 O  O   . HOH DA 5 .   ? -81.049  -35.681 67.982  1.00 61.85  ? 785 HOH G O   1 
HETATM 12394 O  O   . HOH DA 5 .   ? -76.928  -39.364 49.163  1.00 47.36  ? 786 HOH G O   1 
HETATM 12395 O  O   . HOH DA 5 .   ? -47.808  -60.163 68.331  1.00 47.26  ? 787 HOH G O   1 
HETATM 12396 O  O   . HOH DA 5 .   ? -40.595  -48.740 71.493  1.00 54.12  ? 788 HOH G O   1 
HETATM 12397 O  O   . HOH DA 5 .   ? -45.627  -40.929 62.475  1.00 67.59  ? 789 HOH G O   1 
HETATM 12398 O  O   . HOH DA 5 .   ? -52.382  -68.992 48.039  1.00 51.27  ? 790 HOH G O   1 
HETATM 12399 O  O   . HOH DA 5 .   ? -49.473  -36.411 59.589  1.00 60.56  ? 791 HOH G O   1 
HETATM 12400 O  O   . HOH DA 5 .   ? -65.083  -40.334 69.921  1.00 44.30  ? 792 HOH G O   1 
HETATM 12401 O  O   . HOH DA 5 .   ? -50.272  -41.190 40.135  1.00 61.01  ? 793 HOH G O   1 
HETATM 12402 O  O   . HOH DA 5 .   ? -77.338  -21.932 51.132  1.00 33.44  ? 794 HOH G O   1 
HETATM 12403 O  O   . HOH DA 5 .   ? -72.308  -23.759 42.012  1.00 61.51  ? 795 HOH G O   1 
HETATM 12404 O  O   . HOH DA 5 .   ? -31.976  -64.562 64.324  1.00 56.95  ? 796 HOH G O   1 
HETATM 12405 O  O   . HOH DA 5 .   ? -73.955  -20.006 51.373  1.00 29.81  ? 797 HOH G O   1 
HETATM 12406 O  O   . HOH DA 5 .   ? -68.415  -35.539 38.886  1.00 56.14  ? 798 HOH G O   1 
HETATM 12407 O  O   . HOH DA 5 .   ? -75.318  -21.869 49.631  1.00 51.82  ? 799 HOH G O   1 
HETATM 12408 O  O   . HOH DA 5 .   ? -38.733  -77.716 47.509  1.00 41.94  ? 800 HOH G O   1 
HETATM 12409 O  O   . HOH DA 5 .   ? -63.612  -62.517 57.022  1.00 57.96  ? 801 HOH G O   1 
HETATM 12410 O  O   . HOH DA 5 .   ? -45.577  -64.528 68.265  1.00 60.77  ? 802 HOH G O   1 
HETATM 12411 O  O   . HOH DA 5 .   ? -71.152  -23.684 46.943  1.00 57.67  ? 803 HOH G O   1 
HETATM 12412 O  O   . HOH DA 5 .   ? -72.395  -25.590 62.097  1.00 42.15  ? 804 HOH G O   1 
HETATM 12413 O  O   . HOH DA 5 .   ? -79.610  -31.929 57.489  1.00 59.28  ? 805 HOH G O   1 
HETATM 12414 O  O   . HOH DA 5 .   ? -58.573  -51.453 61.206  1.00 41.64  ? 806 HOH G O   1 
HETATM 12415 O  O   . HOH DA 5 .   ? -67.099  -60.790 54.148  1.00 65.83  ? 807 HOH G O   1 
HETATM 12416 O  O   . HOH DA 5 .   ? -78.254  -29.698 59.362  1.00 55.79  ? 808 HOH G O   1 
HETATM 12417 O  O   . HOH DA 5 .   ? -73.067  -32.684 34.607  1.00 60.33  ? 809 HOH G O   1 
HETATM 12418 O  O   . HOH DA 5 .   ? -72.163  -31.832 69.190  1.00 70.79  ? 810 HOH G O   1 
HETATM 12419 O  O   . HOH DA 5 .   ? -67.720  -40.118 72.235  1.00 59.68  ? 811 HOH G O   1 
HETATM 12420 O  O   . HOH DA 5 .   ? -63.219  -41.606 75.205  1.00 60.90  ? 812 HOH G O   1 
HETATM 12421 O  O   . HOH DA 5 .   ? -74.688  -26.370 61.160  1.00 48.24  ? 813 HOH G O   1 
HETATM 12422 O  O   . HOH DA 5 .   ? -50.095  -59.908 73.700  1.00 56.50  ? 814 HOH G O   1 
HETATM 12423 O  O   . HOH DA 5 .   ? -34.162  -72.649 52.998  1.00 53.86  ? 815 HOH G O   1 
HETATM 12424 O  O   . HOH DA 5 .   ? -74.750  -52.589 67.144  1.00 56.76  ? 816 HOH G O   1 
HETATM 12425 O  O   . HOH DA 5 .   ? -43.602  -68.072 30.444  1.00 65.00  ? 817 HOH G O   1 
HETATM 12426 O  O   . HOH DA 5 .   ? -36.135  -45.428 50.132  1.00 71.77  ? 818 HOH G O   1 
HETATM 12427 O  O   . HOH DA 5 .   ? -76.914  -36.272 39.805  1.00 68.01  ? 819 HOH G O   1 
HETATM 12428 O  O   . HOH DA 5 .   ? -35.980  -68.823 60.926  1.00 52.40  ? 820 HOH G O   1 
HETATM 12429 O  O   . HOH DA 5 .   ? -33.759  -67.839 60.337  1.00 62.07  ? 821 HOH G O   1 
HETATM 12430 O  O   . HOH DA 5 .   ? -80.945  -30.296 58.615  1.00 48.73  ? 822 HOH G O   1 
HETATM 12431 O  O   . HOH DA 5 .   ? -32.226  -68.369 55.674  1.00 55.65  ? 823 HOH G O   1 
HETATM 12432 O  O   . HOH DA 5 .   ? -31.757  -70.302 54.154  1.00 54.84  ? 824 HOH G O   1 
HETATM 12433 O  O   . HOH EA 5 .   ? -53.726  -40.044 11.168  1.00 45.83  ? 501 HOH I O   1 
HETATM 12434 O  O   . HOH EA 5 .   ? -45.140  -35.270 14.698  1.00 51.34  ? 502 HOH I O   1 
HETATM 12435 O  O   . HOH EA 5 .   ? -78.802  -33.415 21.733  1.00 56.21  ? 503 HOH I O   1 
HETATM 12436 O  O   . HOH EA 5 .   ? -38.542  -30.286 16.593  1.00 70.43  ? 504 HOH I O   1 
HETATM 12437 O  O   . HOH EA 5 .   ? -56.305  -35.645 1.290   1.00 60.29  ? 505 HOH I O   1 
HETATM 12438 O  O   . HOH EA 5 .   ? -56.393  -51.751 23.232  1.00 61.54  ? 506 HOH I O   1 
HETATM 12439 O  O   . HOH EA 5 .   ? -57.020  -50.645 16.981  1.00 43.25  ? 507 HOH I O   1 
HETATM 12440 O  O   . HOH EA 5 .   ? -55.808  -51.807 10.508  1.00 55.33  ? 508 HOH I O   1 
HETATM 12441 O  O   . HOH EA 5 .   ? -47.198  -38.218 31.734  1.00 64.26  ? 509 HOH I O   1 
HETATM 12442 O  O   . HOH EA 5 .   ? -59.346  -35.067 3.528   1.00 87.85  ? 510 HOH I O   1 
HETATM 12443 O  O   . HOH EA 5 .   ? -63.919  -32.258 33.307  1.00 35.64  ? 511 HOH I O   1 
HETATM 12444 O  O   . HOH EA 5 .   ? -44.801  -40.609 39.326  1.00 61.84  ? 512 HOH I O   1 
HETATM 12445 O  O   . HOH EA 5 .   ? -48.845  -40.774 10.461  1.00 42.55  ? 513 HOH I O   1 
HETATM 12446 O  O   . HOH EA 5 .   ? -72.871  -32.655 29.027  1.00 49.77  ? 514 HOH I O   1 
HETATM 12447 O  O   . HOH EA 5 .   ? -33.498  -48.533 -0.368  1.00 51.87  ? 515 HOH I O   1 
HETATM 12448 O  O   . HOH EA 5 .   ? -73.468  -44.353 32.352  1.00 55.46  ? 516 HOH I O   1 
HETATM 12449 O  O   . HOH EA 5 .   ? -34.699  -40.786 21.855  0.50 69.52  ? 517 HOH I O   1 
HETATM 12450 O  O   . HOH EA 5 .   ? -68.609  -22.372 18.990  1.00 34.27  ? 518 HOH I O   1 
HETATM 12451 O  O   . HOH EA 5 .   ? -43.686  -38.313 0.480   1.00 54.15  ? 519 HOH I O   1 
HETATM 12452 O  O   . HOH EA 5 .   ? -28.403  -46.439 4.705   1.00 59.01  ? 520 HOH I O   1 
HETATM 12453 O  O   . HOH EA 5 .   ? -34.815  -55.491 9.601   1.00 59.29  ? 521 HOH I O   1 
HETATM 12454 O  O   . HOH EA 5 .   ? -35.374  -43.215 2.619   1.00 32.56  ? 522 HOH I O   1 
HETATM 12455 O  O   . HOH EA 5 .   ? -43.829  -41.180 3.663   1.00 36.15  ? 523 HOH I O   1 
HETATM 12456 O  O   . HOH EA 5 .   ? -61.842  -17.892 7.949   1.00 62.28  ? 524 HOH I O   1 
HETATM 12457 O  O   . HOH EA 5 .   ? -46.923  -25.756 22.971  1.00 51.21  ? 525 HOH I O   1 
HETATM 12458 O  O   . HOH EA 5 .   ? -77.397  -45.320 28.397  1.00 48.82  ? 526 HOH I O   1 
HETATM 12459 O  O   . HOH EA 5 .   ? -56.802  -34.380 3.492   1.00 42.22  ? 527 HOH I O   1 
HETATM 12460 O  O   . HOH EA 5 .   ? -58.625  -34.583 33.900  1.00 49.79  ? 528 HOH I O   1 
HETATM 12461 O  O   . HOH EA 5 .   ? -41.862  -39.264 37.347  1.00 60.09  ? 529 HOH I O   1 
HETATM 12462 O  O   . HOH EA 5 .   ? -48.457  -26.688 17.514  1.00 45.28  ? 530 HOH I O   1 
HETATM 12463 O  O   . HOH EA 5 .   ? -65.076  -19.134 8.880   1.00 34.77  ? 531 HOH I O   1 
HETATM 12464 O  O   . HOH EA 5 .   ? -42.802  -37.914 32.707  1.00 57.22  ? 532 HOH I O   1 
HETATM 12465 O  O   . HOH EA 5 .   ? -45.998  -28.644 20.205  1.00 46.85  ? 533 HOH I O   1 
HETATM 12466 O  O   . HOH EA 5 .   ? -38.830  -29.862 25.374  1.00 42.10  ? 534 HOH I O   1 
HETATM 12467 O  O   . HOH EA 5 .   ? -77.111  -36.001 9.548   1.00 31.34  ? 535 HOH I O   1 
HETATM 12468 O  O   . HOH EA 5 .   ? -61.936  -24.551 1.930   1.00 30.31  ? 536 HOH I O   1 
HETATM 12469 O  O   . HOH EA 5 .   ? -48.085  -49.312 37.302  1.00 26.76  ? 537 HOH I O   1 
HETATM 12470 O  O   . HOH EA 5 .   ? -53.035  -36.763 10.331  1.00 44.42  ? 538 HOH I O   1 
HETATM 12471 O  O   . HOH EA 5 .   ? -73.920  -30.572 6.356   1.00 44.33  ? 539 HOH I O   1 
HETATM 12472 O  O   . HOH EA 5 .   ? -55.869  -43.536 28.172  1.00 54.15  ? 540 HOH I O   1 
HETATM 12473 O  O   . HOH EA 5 .   ? -72.559  -29.311 4.245   1.00 47.21  ? 541 HOH I O   1 
HETATM 12474 O  O   . HOH EA 5 .   ? -68.884  -28.426 24.726  1.00 39.41  ? 542 HOH I O   1 
HETATM 12475 O  O   . HOH EA 5 .   ? -32.959  -36.603 16.962  1.00 50.27  ? 543 HOH I O   1 
HETATM 12476 O  O   . HOH EA 5 .   ? -35.319  -39.506 30.258  1.00 45.76  ? 544 HOH I O   1 
HETATM 12477 O  O   . HOH EA 5 .   ? -27.323  -47.771 2.173   1.00 57.74  ? 545 HOH I O   1 
HETATM 12478 O  O   . HOH EA 5 .   ? -62.996  -18.261 5.380   1.00 43.15  ? 546 HOH I O   1 
HETATM 12479 O  O   . HOH EA 5 .   ? -41.308  -30.870 8.013   1.00 45.10  ? 547 HOH I O   1 
HETATM 12480 O  O   . HOH EA 5 .   ? -78.362  -38.325 24.204  1.00 40.46  ? 548 HOH I O   1 
HETATM 12481 O  O   . HOH EA 5 .   ? -41.146  -57.522 13.174  1.00 49.72  ? 549 HOH I O   1 
HETATM 12482 O  O   . HOH EA 5 .   ? -39.618  -40.102 3.889   1.00 36.27  ? 550 HOH I O   1 
HETATM 12483 O  O   . HOH EA 5 .   ? -54.751  -31.697 31.665  1.00 41.08  ? 551 HOH I O   1 
HETATM 12484 O  O   . HOH EA 5 .   ? -58.609  -42.096 28.169  1.00 36.68  ? 552 HOH I O   1 
HETATM 12485 O  O   . HOH EA 5 .   ? -51.479  -52.648 13.412  1.00 47.28  ? 553 HOH I O   1 
HETATM 12486 O  O   . HOH EA 5 .   ? -70.640  -41.508 11.384  1.00 43.26  ? 554 HOH I O   1 
HETATM 12487 O  O   . HOH EA 5 .   ? -50.069  -42.863 13.917  1.00 23.82  ? 555 HOH I O   1 
HETATM 12488 O  O   . HOH EA 5 .   ? -31.125  -44.597 21.147  1.00 54.54  ? 556 HOH I O   1 
HETATM 12489 O  O   . HOH EA 5 .   ? -25.383  -42.028 27.470  1.00 60.90  ? 557 HOH I O   1 
HETATM 12490 O  O   . HOH EA 5 .   ? -86.011  -35.810 18.126  1.00 37.85  ? 558 HOH I O   1 
HETATM 12491 O  O   . HOH EA 5 .   ? -49.590  -49.577 30.348  1.00 34.44  ? 559 HOH I O   1 
HETATM 12492 O  O   . HOH EA 5 .   ? -73.656  -45.415 21.575  1.00 32.37  ? 560 HOH I O   1 
HETATM 12493 O  O   . HOH EA 5 .   ? -64.648  -50.403 20.984  1.00 49.35  ? 561 HOH I O   1 
HETATM 12494 O  O   . HOH EA 5 .   ? -68.032  -48.151 25.616  1.00 53.81  ? 562 HOH I O   1 
HETATM 12495 O  O   . HOH EA 5 .   ? -71.989  -34.861 19.285  1.00 20.64  ? 563 HOH I O   1 
HETATM 12496 O  O   . HOH EA 5 .   ? -69.873  -28.254 18.635  1.00 23.64  ? 564 HOH I O   1 
HETATM 12497 O  O   . HOH EA 5 .   ? -56.925  -51.514 13.349  1.00 49.59  ? 565 HOH I O   1 
HETATM 12498 O  O   . HOH EA 5 .   ? -52.010  -35.342 14.568  1.00 19.99  ? 566 HOH I O   1 
HETATM 12499 O  O   . HOH EA 5 .   ? -49.316  -40.531 31.259  1.00 53.35  ? 567 HOH I O   1 
HETATM 12500 O  O   . HOH EA 5 .   ? -51.026  -52.277 17.395  1.00 44.70  ? 568 HOH I O   1 
HETATM 12501 O  O   . HOH EA 5 .   ? -24.358  -43.317 25.581  1.00 66.25  ? 569 HOH I O   1 
HETATM 12502 O  O   . HOH EA 5 .   ? -58.932  -19.619 9.154   1.00 57.99  ? 570 HOH I O   1 
HETATM 12503 O  O   . HOH EA 5 .   ? -27.969  -35.483 14.594  1.00 50.26  ? 571 HOH I O   1 
HETATM 12504 O  O   . HOH EA 5 .   ? -58.940  -26.035 32.205  1.00 38.25  ? 572 HOH I O   1 
HETATM 12505 O  O   . HOH EA 5 .   ? -66.527  -16.494 6.953   1.00 52.77  ? 573 HOH I O   1 
HETATM 12506 O  O   . HOH EA 5 .   ? -45.458  -39.404 29.464  1.00 30.56  ? 574 HOH I O   1 
HETATM 12507 O  O   . HOH EA 5 .   ? -66.634  -23.436 -0.915  1.00 48.95  ? 575 HOH I O   1 
HETATM 12508 O  O   . HOH EA 5 .   ? -65.364  -31.965 1.300   1.00 34.58  ? 576 HOH I O   1 
HETATM 12509 O  O   . HOH EA 5 .   ? -81.095  -37.508 11.790  1.00 22.09  ? 577 HOH I O   1 
HETATM 12510 O  O   . HOH EA 5 .   ? -41.820  -50.586 30.740  1.00 32.61  ? 578 HOH I O   1 
HETATM 12511 O  O   . HOH EA 5 .   ? -73.461  -27.129 1.539   1.00 45.08  ? 579 HOH I O   1 
HETATM 12512 O  O   . HOH EA 5 .   ? -48.118  -25.413 14.654  1.00 50.43  ? 580 HOH I O   1 
HETATM 12513 O  O   . HOH EA 5 .   ? -68.706  -42.053 27.496  1.00 23.02  ? 581 HOH I O   1 
HETATM 12514 O  O   . HOH EA 5 .   ? -34.192  -41.573 31.278  1.00 52.86  ? 582 HOH I O   1 
HETATM 12515 O  O   . HOH EA 5 .   ? -38.726  -34.663 27.051  1.00 56.25  ? 583 HOH I O   1 
HETATM 12516 O  O   . HOH EA 5 .   ? -73.684  -42.124 10.575  1.00 32.94  ? 584 HOH I O   1 
HETATM 12517 O  O   . HOH EA 5 .   ? -28.072  -54.754 11.729  1.00 66.10  ? 585 HOH I O   1 
HETATM 12518 O  O   . HOH EA 5 .   ? -65.013  -47.880 11.956  1.00 46.33  ? 586 HOH I O   1 
HETATM 12519 O  O   . HOH EA 5 .   ? -70.060  -39.988 28.667  1.00 29.91  ? 587 HOH I O   1 
HETATM 12520 O  O   . HOH EA 5 .   ? -79.954  -43.119 8.973   1.00 46.13  ? 588 HOH I O   1 
HETATM 12521 O  O   . HOH EA 5 .   ? -69.082  -29.164 28.562  1.00 44.13  ? 589 HOH I O   1 
HETATM 12522 O  O   . HOH EA 5 .   ? -51.903  -26.987 20.224  1.00 39.36  ? 590 HOH I O   1 
HETATM 12523 O  O   . HOH EA 5 .   ? -54.916  -41.347 30.792  1.00 52.59  ? 591 HOH I O   1 
HETATM 12524 O  O   . HOH EA 5 .   ? -64.069  -22.764 -1.267  1.00 50.30  ? 592 HOH I O   1 
HETATM 12525 O  O   . HOH EA 5 .   ? -83.014  -40.064 19.030  1.00 21.87  ? 593 HOH I O   1 
HETATM 12526 O  O   . HOH EA 5 .   ? -61.160  -44.443 6.402   1.00 64.71  ? 594 HOH I O   1 
HETATM 12527 O  O   . HOH EA 5 .   ? -53.972  -47.916 30.214  1.00 64.95  ? 595 HOH I O   1 
HETATM 12528 O  O   . HOH EA 5 .   ? -62.575  -31.697 31.536  1.00 40.64  ? 596 HOH I O   1 
HETATM 12529 O  O   . HOH EA 5 .   ? -54.585  -38.775 9.308   1.00 48.39  ? 597 HOH I O   1 
HETATM 12530 O  O   . HOH EA 5 .   ? -49.998  -33.729 15.549  1.00 26.02  ? 598 HOH I O   1 
HETATM 12531 O  O   . HOH EA 5 .   ? -44.336  -33.516 27.372  1.00 37.93  ? 599 HOH I O   1 
HETATM 12532 O  O   . HOH EA 5 .   ? -54.150  -29.605 32.841  1.00 52.12  ? 600 HOH I O   1 
HETATM 12533 O  O   . HOH EA 5 .   ? -64.485  -20.305 -1.911  1.00 48.32  ? 601 HOH I O   1 
HETATM 12534 O  O   . HOH EA 5 .   ? -38.311  -50.082 0.348   1.00 46.16  ? 602 HOH I O   1 
HETATM 12535 O  O   . HOH EA 5 .   ? -48.602  -32.472 8.152   1.00 54.94  ? 603 HOH I O   1 
HETATM 12536 O  O   . HOH EA 5 .   ? -51.238  -42.771 32.183  1.00 41.22  ? 604 HOH I O   1 
HETATM 12537 O  O   . HOH EA 5 .   ? -70.146  -40.036 13.845  1.00 61.47  ? 605 HOH I O   1 
HETATM 12538 O  O   . HOH EA 5 .   ? -47.733  -45.564 6.206   1.00 70.18  ? 606 HOH I O   1 
HETATM 12539 O  O   . HOH EA 5 .   ? -59.803  -47.453 24.710  1.00 39.95  ? 607 HOH I O   1 
HETATM 12540 O  O   . HOH EA 5 .   ? -54.924  -41.281 26.815  1.00 32.71  ? 608 HOH I O   1 
HETATM 12541 O  O   . HOH EA 5 .   ? -53.596  -51.731 15.077  1.00 43.58  ? 609 HOH I O   1 
HETATM 12542 O  O   . HOH EA 5 .   ? -48.888  -53.325 37.225  1.00 31.43  ? 610 HOH I O   1 
HETATM 12543 O  O   . HOH EA 5 .   ? -76.876  -43.967 30.461  1.00 57.19  ? 611 HOH I O   1 
HETATM 12544 O  O   . HOH EA 5 .   ? -64.696  -46.018 24.224  1.00 33.01  ? 612 HOH I O   1 
HETATM 12545 O  O   . HOH EA 5 .   ? -48.761  -39.684 27.432  1.00 46.70  ? 613 HOH I O   1 
HETATM 12546 O  O   . HOH EA 5 .   ? -53.540  -39.163 32.455  1.00 43.25  ? 614 HOH I O   1 
HETATM 12547 O  O   . HOH EA 5 .   ? -60.356  -37.554 32.922  1.00 26.37  ? 615 HOH I O   1 
HETATM 12548 O  O   . HOH EA 5 .   ? -61.537  -35.396 2.732   1.00 37.33  ? 616 HOH I O   1 
HETATM 12549 O  O   . HOH EA 5 .   ? -69.630  -33.126 3.112   1.00 33.89  ? 617 HOH I O   1 
HETATM 12550 O  O   . HOH EA 5 .   ? -52.214  -44.682 14.111  1.00 24.98  ? 618 HOH I O   1 
HETATM 12551 O  O   . HOH EA 5 .   ? -29.460  -34.788 26.027  1.00 58.71  ? 619 HOH I O   1 
HETATM 12552 O  O   . HOH EA 5 .   ? -59.063  -50.454 15.319  1.00 48.07  ? 620 HOH I O   1 
HETATM 12553 O  O   . HOH EA 5 .   ? -79.117  -40.969 21.245  1.00 35.26  ? 621 HOH I O   1 
HETATM 12554 O  O   . HOH EA 5 .   ? -68.903  -47.995 30.998  1.00 55.76  ? 622 HOH I O   1 
HETATM 12555 O  O   . HOH EA 5 .   ? -52.824  -26.068 22.453  1.00 58.83  ? 623 HOH I O   1 
HETATM 12556 O  O   . HOH EA 5 .   ? -70.166  -47.114 22.239  1.00 57.20  ? 624 HOH I O   1 
HETATM 12557 O  O   . HOH EA 5 .   ? -59.425  -42.407 5.796   1.00 51.87  ? 625 HOH I O   1 
HETATM 12558 O  O   . HOH EA 5 .   ? -34.555  -53.728 12.614  1.00 42.05  ? 626 HOH I O   1 
HETATM 12559 O  O   . HOH EA 5 .   ? -69.999  -18.043 4.820   1.00 36.16  ? 627 HOH I O   1 
HETATM 12560 O  O   . HOH EA 5 .   ? -69.956  -44.456 17.763  1.00 27.10  ? 628 HOH I O   1 
HETATM 12561 O  O   . HOH EA 5 .   ? -75.207  -45.918 30.333  1.00 48.96  ? 629 HOH I O   1 
HETATM 12562 O  O   . HOH EA 5 .   ? -35.138  -59.510 4.858   1.00 65.36  ? 630 HOH I O   1 
HETATM 12563 O  O   . HOH EA 5 .   ? -53.466  -18.929 26.693  1.00 62.57  ? 631 HOH I O   1 
HETATM 12564 O  O   . HOH EA 5 .   ? -45.633  -55.833 30.052  1.00 39.51  ? 632 HOH I O   1 
HETATM 12565 O  O   . HOH EA 5 .   ? -40.494  -51.730 32.947  1.00 42.26  ? 633 HOH I O   1 
HETATM 12566 O  O   . HOH EA 5 .   ? -67.839  -43.892 9.631   1.00 50.30  ? 634 HOH I O   1 
HETATM 12567 O  O   . HOH EA 5 .   ? -75.727  -27.585 7.451   1.00 36.33  ? 635 HOH I O   1 
HETATM 12568 O  O   . HOH EA 5 .   ? -34.437  -52.237 24.512  1.00 51.95  ? 636 HOH I O   1 
HETATM 12569 O  O   . HOH EA 5 .   ? -67.162  -25.458 0.100   1.00 55.90  ? 637 HOH I O   1 
HETATM 12570 O  O   . HOH EA 5 .   ? -30.970  -42.572 4.676   1.00 44.35  ? 638 HOH I O   1 
HETATM 12571 O  O   . HOH EA 5 .   ? -71.264  -39.721 31.192  1.00 69.23  ? 639 HOH I O   1 
HETATM 12572 O  O   . HOH EA 5 .   ? -50.495  -52.263 30.601  1.00 41.58  ? 640 HOH I O   1 
HETATM 12573 O  O   . HOH EA 5 .   ? -49.745  -39.691 13.153  1.00 34.18  ? 641 HOH I O   1 
HETATM 12574 O  O   . HOH EA 5 .   ? -68.970  -42.089 13.835  1.00 40.49  ? 642 HOH I O   1 
HETATM 12575 O  O   . HOH EA 5 .   ? -75.860  -32.694 6.914   1.00 34.17  ? 643 HOH I O   1 
HETATM 12576 O  O   . HOH EA 5 .   ? -46.536  -37.866 9.761   1.00 51.39  ? 644 HOH I O   1 
HETATM 12577 O  O   . HOH EA 5 .   ? -44.922  -56.771 36.471  1.00 49.98  ? 645 HOH I O   1 
HETATM 12578 O  O   . HOH EA 5 .   ? -25.305  -44.368 9.431   1.00 50.55  ? 646 HOH I O   1 
HETATM 12579 O  O   . HOH EA 5 .   ? -28.596  -54.075 6.278   1.00 60.78  ? 647 HOH I O   1 
HETATM 12580 O  O   . HOH EA 5 .   ? -35.817  -56.603 7.247   1.00 54.73  ? 648 HOH I O   1 
HETATM 12581 O  O   . HOH EA 5 .   ? -35.849  -57.876 13.245  1.00 64.25  ? 649 HOH I O   1 
HETATM 12582 O  O   . HOH EA 5 .   ? -50.677  -23.308 20.272  1.00 57.39  ? 650 HOH I O   1 
HETATM 12583 O  O   . HOH EA 5 .   ? -40.150  -36.216 6.417   1.00 56.54  ? 651 HOH I O   1 
HETATM 12584 O  O   . HOH EA 5 .   ? -33.305  -43.821 4.036   1.00 44.12  ? 652 HOH I O   1 
HETATM 12585 O  O   . HOH EA 5 .   ? -50.896  -25.534 15.858  1.00 46.85  ? 653 HOH I O   1 
HETATM 12586 O  O   . HOH EA 5 .   ? -32.936  -34.842 21.635  1.00 41.91  ? 654 HOH I O   1 
HETATM 12587 O  O   . HOH EA 5 .   ? -69.947  -25.829 -0.167  1.00 40.59  ? 655 HOH I O   1 
HETATM 12588 O  O   . HOH EA 5 .   ? -35.818  -59.252 8.437   1.00 59.91  ? 656 HOH I O   1 
HETATM 12589 O  O   . HOH EA 5 .   ? -34.382  -54.758 26.819  1.00 49.90  ? 657 HOH I O   1 
HETATM 12590 O  O   . HOH EA 5 .   ? -67.335  -31.810 3.097   1.00 25.74  ? 658 HOH I O   1 
HETATM 12591 O  O   . HOH EA 5 .   ? -52.239  -38.509 12.963  1.00 30.82  ? 659 HOH I O   1 
HETATM 12592 O  O   . HOH EA 5 .   ? -48.673  -30.365 26.999  1.00 39.59  ? 660 HOH I O   1 
HETATM 12593 O  O   . HOH EA 5 .   ? -63.949  -34.228 32.469  1.00 45.90  ? 661 HOH I O   1 
HETATM 12594 O  O   . HOH EA 5 .   ? -60.491  -44.626 29.863  1.00 52.19  ? 662 HOH I O   1 
HETATM 12595 O  O   . HOH EA 5 .   ? -65.958  -43.253 6.593   1.00 31.78  ? 663 HOH I O   1 
HETATM 12596 O  O   . HOH EA 5 .   ? -80.629  -46.525 12.127  1.00 29.69  ? 664 HOH I O   1 
HETATM 12597 O  O   . HOH EA 5 .   ? -35.036  -52.212 28.288  1.00 45.39  ? 665 HOH I O   1 
HETATM 12598 O  O   . HOH EA 5 .   ? -61.898  -22.157 -0.790  1.00 46.03  ? 666 HOH I O   1 
HETATM 12599 O  O   . HOH EA 5 .   ? -70.112  -43.693 2.538   1.00 70.48  ? 667 HOH I O   1 
HETATM 12600 O  O   . HOH EA 5 .   ? -35.365  -33.410 9.757   1.00 43.53  ? 668 HOH I O   1 
HETATM 12601 O  O   . HOH EA 5 .   ? -41.684  -34.180 7.899   1.00 53.17  ? 669 HOH I O   1 
HETATM 12602 O  O   . HOH EA 5 .   ? -30.588  -57.602 2.764   1.00 52.97  ? 670 HOH I O   1 
HETATM 12603 O  O   . HOH EA 5 .   ? -48.160  -38.124 29.271  1.00 50.02  ? 671 HOH I O   1 
HETATM 12604 O  O   . HOH EA 5 .   ? -83.531  -41.726 25.454  1.00 59.96  ? 672 HOH I O   1 
HETATM 12605 O  O   . HOH EA 5 .   ? -30.377  -48.697 -0.253  1.00 38.61  ? 673 HOH I O   1 
HETATM 12606 O  O   . HOH EA 5 .   ? -55.039  -50.359 24.446  1.00 42.49  ? 674 HOH I O   1 
HETATM 12607 O  O   . HOH EA 5 .   ? -35.541  -54.318 15.527  1.00 46.28  ? 675 HOH I O   1 
HETATM 12608 O  O   . HOH EA 5 .   ? -77.554  -48.532 13.095  1.00 58.43  ? 676 HOH I O   1 
HETATM 12609 O  O   . HOH EA 5 .   ? -25.528  -48.662 8.151   1.00 45.16  ? 677 HOH I O   1 
HETATM 12610 O  O   . HOH EA 5 .   ? -68.569  -24.805 23.018  1.00 36.96  ? 678 HOH I O   1 
HETATM 12611 O  O   . HOH EA 5 .   ? -45.243  -36.330 8.693   1.00 60.69  ? 679 HOH I O   1 
HETATM 12612 O  O   . HOH EA 5 .   ? -75.388  -30.135 22.482  1.00 23.26  ? 680 HOH I O   1 
HETATM 12613 O  O   . HOH EA 5 .   ? -57.403  -19.632 22.838  1.00 62.38  ? 681 HOH I O   1 
HETATM 12614 O  O   . HOH EA 5 .   ? -55.354  -24.120 12.964  1.00 42.71  ? 682 HOH I O   1 
HETATM 12615 O  O   . HOH EA 5 .   ? -46.830  -53.607 10.855  1.00 53.61  ? 683 HOH I O   1 
HETATM 12616 O  O   . HOH EA 5 .   ? -33.382  -34.519 15.225  1.00 50.58  ? 684 HOH I O   1 
HETATM 12617 O  O   . HOH EA 5 .   ? -47.794  -21.538 21.881  1.00 39.99  ? 685 HOH I O   1 
HETATM 12618 O  O   . HOH EA 5 .   ? -67.999  -32.732 33.434  1.00 54.61  ? 686 HOH I O   1 
HETATM 12619 O  O   . HOH EA 5 .   ? -58.475  -47.030 26.585  1.00 50.20  ? 687 HOH I O   1 
HETATM 12620 O  O   . HOH EA 5 .   ? -68.777  -43.726 11.753  1.00 46.01  ? 688 HOH I O   1 
HETATM 12621 O  O   . HOH EA 5 .   ? -65.525  -49.876 23.550  1.00 66.61  ? 689 HOH I O   1 
HETATM 12622 O  O   . HOH EA 5 .   ? -34.804  -55.173 22.276  1.00 45.08  ? 690 HOH I O   1 
HETATM 12623 O  O   . HOH EA 5 .   ? -38.545  -28.495 23.230  1.00 42.62  ? 691 HOH I O   1 
HETATM 12624 O  O   . HOH EA 5 .   ? -46.646  -38.802 38.415  1.00 58.64  ? 692 HOH I O   1 
HETATM 12625 O  O   . HOH EA 5 .   ? -22.158  -46.382 17.422  1.00 86.76  ? 693 HOH I O   1 
HETATM 12626 O  O   . HOH EA 5 .   ? -55.942  -50.502 27.403  1.00 45.73  ? 694 HOH I O   1 
HETATM 12627 O  O   . HOH EA 5 .   ? -70.465  -23.075 -0.560  1.00 58.19  ? 695 HOH I O   1 
HETATM 12628 O  O   . HOH EA 5 .   ? -31.244  -36.160 15.077  1.00 60.62  ? 696 HOH I O   1 
HETATM 12629 O  O   . HOH EA 5 .   ? -62.032  -21.921 21.995  1.00 52.17  ? 697 HOH I O   1 
HETATM 12630 O  O   . HOH EA 5 .   ? -72.252  -21.482 7.002   1.00 47.15  ? 698 HOH I O   1 
HETATM 12631 O  O   . HOH EA 5 .   ? -55.110  -42.339 33.098  1.00 58.74  ? 699 HOH I O   1 
HETATM 12632 O  O   . HOH EA 5 .   ? -65.835  -16.713 -2.496  1.00 63.82  ? 700 HOH I O   1 
HETATM 12633 O  O   . HOH EA 5 .   ? -52.202  -45.106 6.345   1.00 67.33  ? 701 HOH I O   1 
HETATM 12634 O  O   . HOH EA 5 .   ? -57.512  -43.696 30.508  1.00 55.89  ? 702 HOH I O   1 
HETATM 12635 O  O   . HOH EA 5 .   ? -76.258  -41.464 33.311  1.00 73.39  ? 703 HOH I O   1 
HETATM 12636 O  O   . HOH EA 5 .   ? -60.930  -40.263 4.742   1.00 48.40  ? 704 HOH I O   1 
HETATM 12637 O  O   . HOH EA 5 .   ? -64.331  -51.463 18.605  1.00 58.62  ? 705 HOH I O   1 
HETATM 12638 O  O   . HOH EA 5 .   ? -67.310  -26.310 29.177  1.00 50.33  ? 706 HOH I O   1 
HETATM 12639 O  O   . HOH EA 5 .   ? -63.133  -46.683 26.133  1.00 50.45  ? 707 HOH I O   1 
HETATM 12640 O  O   . HOH EA 5 .   ? -59.408  -20.463 13.511  1.00 55.99  ? 708 HOH I O   1 
HETATM 12641 O  O   . HOH EA 5 .   ? -55.756  -33.023 -0.017  1.00 60.60  ? 709 HOH I O   1 
HETATM 12642 O  O   . HOH EA 5 .   ? -67.211  -50.035 27.349  1.00 66.62  ? 710 HOH I O   1 
HETATM 12643 O  O   . HOH EA 5 .   ? -79.971  -45.655 9.708   1.00 33.01  ? 711 HOH I O   1 
HETATM 12644 O  O   . HOH EA 5 .   ? -82.934  -42.980 22.797  1.00 53.38  ? 712 HOH I O   1 
HETATM 12645 O  O   . HOH EA 5 .   ? -72.075  -35.283 30.025  1.00 58.26  ? 713 HOH I O   1 
HETATM 12646 O  O   . HOH EA 5 .   ? -66.392  -48.017 14.238  1.00 42.52  ? 714 HOH I O   1 
HETATM 12647 O  O   . HOH EA 5 .   ? -20.631  -46.318 19.412  1.00 72.51  ? 715 HOH I O   1 
HETATM 12648 O  O   . HOH EA 5 .   ? -64.860  -26.576 -0.456  1.00 63.86  ? 716 HOH I O   1 
HETATM 12649 O  O   . HOH EA 5 .   ? -36.576  -55.261 28.028  1.00 58.90  ? 717 HOH I O   1 
HETATM 12650 O  O   . HOH EA 5 .   ? -64.125  -29.085 -1.420  1.00 51.55  ? 718 HOH I O   1 
HETATM 12651 O  O   . HOH EA 5 .   ? -65.857  -46.053 9.117   1.00 58.18  ? 719 HOH I O   1 
HETATM 12652 O  O   . HOH EA 5 .   ? -65.095  -40.354 3.162   1.00 58.15  ? 720 HOH I O   1 
HETATM 12653 O  O   . HOH EA 5 .   ? -43.417  -27.745 30.833  1.00 62.69  ? 721 HOH I O   1 
HETATM 12654 O  O   . HOH EA 5 .   ? -33.426  -52.286 26.557  1.00 57.56  ? 722 HOH I O   1 
HETATM 12655 O  O   . HOH EA 5 .   ? -40.069  -54.290 33.583  1.00 57.99  ? 723 HOH I O   1 
HETATM 12656 O  O   . HOH EA 5 .   ? -46.245  -33.978 28.889  1.00 50.14  ? 724 HOH I O   1 
HETATM 12657 O  O   . HOH EA 5 .   ? -58.073  -24.022 29.263  1.00 57.44  ? 725 HOH I O   1 
HETATM 12658 O  O   . HOH EA 5 .   ? -34.532  -57.116 15.711  1.00 66.54  ? 726 HOH I O   1 
HETATM 12659 O  O   . HOH EA 5 .   ? -50.487  -42.019 2.150   1.00 73.12  ? 727 HOH I O   1 
HETATM 12660 O  O   . HOH EA 5 .   ? -63.781  -39.794 35.648  1.00 58.04  ? 728 HOH I O   1 
HETATM 12661 O  O   . HOH EA 5 .   ? -61.215  -45.933 27.782  1.00 52.87  ? 729 HOH I O   1 
HETATM 12662 O  O   . HOH EA 5 .   ? -34.305  -56.749 25.415  1.00 56.09  ? 730 HOH I O   1 
HETATM 12663 O  O   . HOH EA 5 .   ? -80.583  -31.511 15.953  1.00 56.65  ? 731 HOH I O   1 
HETATM 12664 O  O   . HOH EA 5 .   ? -79.232  -28.358 25.938  1.00 67.52  ? 732 HOH I O   1 
HETATM 12665 O  O   . HOH EA 5 .   ? -40.322  -34.603 29.179  1.00 63.41  ? 733 HOH I O   1 
HETATM 12666 O  O   . HOH EA 5 .   ? -50.712  -47.097 6.169   1.00 59.69  ? 734 HOH I O   1 
HETATM 12667 O  O   . HOH EA 5 .   ? -54.274  -27.755 6.952   1.00 64.95  ? 735 HOH I O   1 
HETATM 12668 O  O   . HOH EA 5 .   ? -55.751  -46.482 4.134   1.00 67.90  ? 736 HOH I O   1 
HETATM 12669 O  O   . HOH EA 5 .   ? -35.898  -31.195 12.772  1.00 58.23  ? 737 HOH I O   1 
HETATM 12670 O  O   . HOH EA 5 .   ? -51.468  -47.414 34.945  1.00 44.96  ? 738 HOH I O   1 
HETATM 12671 O  O   . HOH EA 5 .   ? -66.563  -21.346 22.783  1.00 58.09  ? 739 HOH I O   1 
HETATM 12672 O  O   . HOH EA 5 .   ? -53.083  -29.414 7.853   1.00 56.07  ? 740 HOH I O   1 
HETATM 12673 O  O   . HOH EA 5 .   ? -73.295  -48.110 24.837  1.00 56.72  ? 741 HOH I O   1 
HETATM 12674 O  O   . HOH EA 5 .   ? -36.220  -29.808 18.452  1.00 56.44  ? 742 HOH I O   1 
HETATM 12675 O  O   . HOH EA 5 .   ? -49.849  -26.021 19.709  1.00 67.85  ? 743 HOH I O   1 
HETATM 12676 O  O   . HOH EA 5 .   ? -68.834  -44.481 15.336  1.00 38.80  ? 744 HOH I O   1 
HETATM 12677 O  O   . HOH EA 5 .   ? -67.082  -35.097 32.946  1.00 53.98  ? 745 HOH I O   1 
HETATM 12678 O  O   . HOH EA 5 .   ? -33.444  -34.330 18.824  1.00 59.56  ? 746 HOH I O   1 
HETATM 12679 O  O   . HOH EA 5 .   ? -24.706  -49.131 4.868   1.00 67.39  ? 747 HOH I O   1 
HETATM 12680 O  O   . HOH EA 5 .   ? -78.833  -30.531 14.675  1.00 50.09  ? 748 HOH I O   1 
HETATM 12681 O  O   . HOH EA 5 .   ? -62.612  -39.101 -0.776  1.00 72.17  ? 749 HOH I O   1 
HETATM 12682 O  O   . HOH EA 5 .   ? -69.851  -26.797 22.901  1.00 49.68  ? 750 HOH I O   1 
HETATM 12683 O  O   . HOH EA 5 .   ? -70.882  -27.432 32.159  1.00 67.55  ? 751 HOH I O   1 
HETATM 12684 O  O   . HOH EA 5 .   ? -57.366  -52.245 27.379  1.00 53.82  ? 752 HOH I O   1 
HETATM 12685 O  O   . HOH EA 5 .   ? -52.479  -49.547 31.198  1.00 60.66  ? 753 HOH I O   1 
HETATM 12686 O  O   . HOH EA 5 .   ? -54.986  -25.520 8.563   1.00 57.96  ? 754 HOH I O   1 
HETATM 12687 O  O   . HOH EA 5 .   ? -44.746  -51.163 5.603   1.00 56.50  ? 755 HOH I O   1 
HETATM 12688 O  O   . HOH EA 5 .   ? -56.435  -41.032 7.427   1.00 61.25  ? 756 HOH I O   1 
HETATM 12689 O  O   . HOH EA 5 .   ? -65.035  -48.844 5.542   1.00 69.68  ? 757 HOH I O   1 
HETATM 12690 O  O   . HOH EA 5 .   ? -77.371  -34.360 7.472   1.00 55.18  ? 758 HOH I O   1 
HETATM 12691 O  O   . HOH EA 5 .   ? -56.551  -21.309 12.596  1.00 60.86  ? 759 HOH I O   1 
HETATM 12692 O  O   . HOH EA 5 .   ? -55.937  -46.435 33.134  1.00 65.65  ? 760 HOH I O   1 
HETATM 12693 O  O   . HOH EA 5 .   ? -61.493  -46.015 31.981  1.00 59.47  ? 761 HOH I O   1 
HETATM 12694 O  O   . HOH EA 5 .   ? -78.786  -30.898 12.558  1.00 50.76  ? 762 HOH I O   1 
HETATM 12695 O  O   . HOH EA 5 .   ? -75.691  -47.790 25.062  1.00 64.21  ? 763 HOH I O   1 
HETATM 12696 O  O   . HOH EA 5 .   ? -66.661  -26.399 33.460  1.00 74.17  ? 764 HOH I O   1 
HETATM 12697 O  O   . HOH EA 5 .   ? -50.127  -40.501 34.229  1.00 56.36  ? 765 HOH I O   1 
HETATM 12698 O  O   . HOH EA 5 .   ? -50.930  -36.578 12.580  1.00 46.19  ? 766 HOH I O   1 
HETATM 12699 O  O   . HOH EA 5 .   ? -59.832  -20.286 21.994  1.00 60.41  ? 767 HOH I O   1 
HETATM 12700 O  O   . HOH EA 5 .   ? -48.184  -47.699 5.764   1.00 62.85  ? 768 HOH I O   1 
HETATM 12701 O  O   . HOH EA 5 .   ? -37.181  -39.768 2.794   1.00 55.49  ? 769 HOH I O   1 
HETATM 12702 O  O   . HOH EA 5 .   ? -67.933  -12.023 4.059   1.00 68.92  ? 770 HOH I O   1 
HETATM 12703 O  O   . HOH EA 5 .   ? -59.650  -22.377 1.770   1.00 57.32  ? 771 HOH I O   1 
HETATM 12704 O  O   . HOH EA 5 .   ? -68.722  -37.121 32.549  1.00 52.59  ? 772 HOH I O   1 
HETATM 12705 O  O   . HOH EA 5 .   ? -46.858  -49.740 5.567   1.00 66.31  ? 773 HOH I O   1 
HETATM 12706 O  O   . HOH EA 5 .   ? -71.227  -46.535 19.852  1.00 53.58  ? 774 HOH I O   1 
HETATM 12707 O  O   . HOH EA 5 .   ? -60.586  -20.173 0.603   1.00 66.85  ? 775 HOH I O   1 
HETATM 12708 O  O   . HOH EA 5 .   ? -85.057  -39.005 20.223  1.00 31.86  ? 776 HOH I O   1 
HETATM 12709 O  O   . HOH EA 5 .   ? -63.911  -35.186 1.440   1.00 54.54  ? 777 HOH I O   1 
HETATM 12710 O  O   . HOH EA 5 .   ? -75.593  -23.725 5.252   1.00 63.95  ? 778 HOH I O   1 
HETATM 12711 O  O   . HOH EA 5 .   ? -36.055  -30.338 26.365  1.00 52.63  ? 779 HOH I O   1 
HETATM 12712 O  O   . HOH EA 5 .   ? -71.099  -47.101 17.744  1.00 54.60  ? 780 HOH I O   1 
HETATM 12713 O  O   . HOH EA 5 .   ? -73.315  -22.446 -2.600  1.00 61.48  ? 781 HOH I O   1 
HETATM 12714 O  O   . HOH EA 5 .   ? -85.107  -34.996 20.579  1.00 40.75  ? 782 HOH I O   1 
HETATM 12715 O  O   . HOH EA 5 .   ? -59.530  -51.475 11.093  1.00 58.91  ? 783 HOH I O   1 
HETATM 12716 O  O   . HOH EA 5 .   ? -54.916  -49.923 30.635  1.00 59.73  ? 784 HOH I O   1 
HETATM 12717 O  O   . HOH EA 5 .   ? -76.822  -29.669 7.514   1.00 67.59  ? 785 HOH I O   1 
HETATM 12718 O  O   . HOH EA 5 .   ? -37.225  -38.927 -1.301  1.00 67.12  ? 786 HOH I O   1 
HETATM 12719 O  O   . HOH EA 5 .   ? -51.247  -41.526 9.100   1.00 52.79  ? 787 HOH I O   1 
HETATM 12720 O  O   . HOH EA 5 .   ? -70.346  -37.593 30.397  1.00 51.92  ? 788 HOH I O   1 
HETATM 12721 O  O   . HOH EA 5 .   ? -64.047  -38.604 1.433   1.00 67.52  ? 789 HOH I O   1 
HETATM 12722 O  O   . HOH EA 5 .   ? -46.950  -36.299 0.561   1.00 70.02  ? 790 HOH I O   1 
HETATM 12723 O  O   . HOH EA 5 .   ? -56.841  -49.538 29.271  1.00 58.72  ? 791 HOH I O   1 
HETATM 12724 O  O   . HOH EA 5 .   ? -61.642  -27.285 -1.739  1.00 56.71  ? 792 HOH I O   1 
HETATM 12725 O  O   . HOH EA 5 .   ? -45.269  -59.564 19.664  1.00 77.86  ? 793 HOH I O   1 
HETATM 12726 O  O   . HOH EA 5 .   ? -27.381  -56.571 9.508   1.00 59.65  ? 794 HOH I O   1 
HETATM 12727 O  O   . HOH EA 5 .   ? -65.831  -34.117 0.121   1.00 59.84  ? 795 HOH I O   1 
HETATM 12728 O  O   . HOH EA 5 .   ? -58.369  -51.467 4.702   1.00 61.10  ? 796 HOH I O   1 
HETATM 12729 O  O   . HOH EA 5 .   ? -49.241  -51.055 5.001   1.00 72.54  ? 797 HOH I O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   0   ?   ?   ?   A . n 
A 1 2   ALA 2   1   1   ALA ALA A . n 
A 1 3   THR 3   2   2   THR THR A . n 
A 1 4   LYS 4   3   3   LYS LYS A . n 
A 1 5   ALA 5   4   4   ALA ALA A . n 
A 1 6   VAL 6   5   5   VAL VAL A . n 
A 1 7   CYS 7   6   6   CYS CYS A . n 
A 1 8   VAL 8   7   7   VAL VAL A . n 
A 1 9   LEU 9   8   8   LEU LEU A . n 
A 1 10  LYS 10  9   9   LYS LYS A . n 
A 1 11  GLY 11  10  10  GLY GLY A . n 
A 1 12  ASP 12  11  11  ASP ASP A . n 
A 1 13  GLY 13  12  12  GLY GLY A . n 
A 1 14  PRO 14  13  13  PRO PRO A . n 
A 1 15  VAL 15  14  14  VAL VAL A . n 
A 1 16  GLN 16  15  15  GLN GLN A . n 
A 1 17  GLY 17  16  16  GLY GLY A . n 
A 1 18  ILE 18  17  17  ILE ILE A . n 
A 1 19  ILE 19  18  18  ILE ILE A . n 
A 1 20  ASN 20  19  19  ASN ASN A . n 
A 1 21  PHE 21  20  20  PHE PHE A . n 
A 1 22  GLU 22  21  21  GLU GLU A . n 
A 1 23  GLN 23  22  22  GLN GLN A . n 
A 1 24  LYS 24  23  23  LYS LYS A . n 
A 1 25  GLU 25  24  24  GLU GLU A . n 
A 1 26  SER 26  25  25  SER SER A . n 
A 1 27  ASN 27  26  26  ASN ASN A . n 
A 1 28  GLY 28  27  27  GLY GLY A . n 
A 1 29  PRO 29  28  28  PRO PRO A . n 
A 1 30  VAL 30  29  29  VAL VAL A . n 
A 1 31  LYS 31  30  30  LYS LYS A . n 
A 1 32  VAL 32  31  31  VAL VAL A . n 
A 1 33  TRP 33  32  32  TRP TRP A . n 
A 1 34  GLY 34  33  33  GLY GLY A . n 
A 1 35  SER 35  34  34  SER SER A . n 
A 1 36  ILE 36  35  35  ILE ILE A . n 
A 1 37  LYS 37  36  36  LYS LYS A . n 
A 1 38  GLY 38  37  37  GLY GLY A . n 
A 1 39  LEU 39  38  38  LEU LEU A . n 
A 1 40  THR 40  39  39  THR THR A . n 
A 1 41  GLU 41  40  40  GLU GLU A . n 
A 1 42  GLY 42  41  41  GLY GLY A . n 
A 1 43  LEU 43  42  42  LEU LEU A . n 
A 1 44  HIS 44  43  43  HIS HIS A . n 
A 1 45  GLY 45  44  44  GLY GLY A . n 
A 1 46  PHE 46  45  45  PHE PHE A . n 
A 1 47  HIS 47  46  46  HIS HIS A . n 
A 1 48  VAL 48  47  47  VAL VAL A . n 
A 1 49  HIS 49  48  48  HIS HIS A . n 
A 1 50  GLU 50  49  49  GLU GLU A . n 
A 1 51  PHE 51  50  50  PHE PHE A . n 
A 1 52  GLY 52  51  51  GLY GLY A . n 
A 1 53  ASP 53  52  52  ASP ASP A . n 
A 1 54  ASN 54  53  53  ASN ASN A . n 
A 1 55  THR 55  54  54  THR THR A . n 
A 1 56  ALA 56  55  55  ALA ALA A . n 
A 1 57  GLY 57  56  56  GLY GLY A . n 
A 1 58  CYS 58  57  57  CYS CYS A . n 
A 1 59  THR 59  58  58  THR THR A . n 
A 1 60  SER 60  59  59  SER SER A . n 
A 1 61  ALA 61  60  60  ALA ALA A . n 
A 1 62  GLY 62  61  61  GLY GLY A . n 
A 1 63  PRO 63  62  62  PRO PRO A . n 
A 1 64  HIS 64  63  63  HIS HIS A . n 
A 1 65  PHE 65  64  64  PHE PHE A . n 
A 1 66  ASN 66  65  65  ASN ASN A . n 
A 1 67  PRO 67  66  66  PRO PRO A . n 
A 1 68  LEU 68  67  67  LEU LEU A . n 
A 1 69  SER 69  68  68  SER SER A . n 
A 1 70  ARG 70  69  69  ARG ARG A . n 
A 1 71  LYS 71  70  70  LYS LYS A . n 
A 1 72  HIS 72  71  71  HIS HIS A . n 
A 1 73  GLY 73  72  72  GLY GLY A . n 
A 1 74  GLY 74  73  73  GLY GLY A . n 
A 1 75  PRO 75  74  74  PRO PRO A . n 
A 1 76  LYS 76  75  75  LYS LYS A . n 
A 1 77  ASP 77  76  76  ASP ASP A . n 
A 1 78  GLU 78  77  77  GLU GLU A . n 
A 1 79  GLU 79  78  78  GLU GLU A . n 
A 1 80  ARG 80  79  79  ARG ARG A . n 
A 1 81  HIS 81  80  80  HIS HIS A . n 
A 1 82  VAL 82  81  81  VAL VAL A . n 
A 1 83  GLY 83  82  82  GLY GLY A . n 
A 1 84  SER 84  83  83  SER SER A . y 
A 1 84  ASP 84  83  83  ASP ASP A . y 
A 1 85  LEU 85  84  84  LEU LEU A . n 
A 1 86  GLY 86  85  85  GLY GLY A . n 
A 1 87  ASN 87  86  86  ASN ASN A . n 
A 1 88  VAL 88  87  87  VAL VAL A . n 
A 1 89  THR 89  88  88  THR THR A . n 
A 1 90  ALA 90  89  89  ALA ALA A . n 
A 1 91  ASP 91  90  90  ASP ASP A . n 
A 1 92  LYS 92  91  91  LYS LYS A . n 
A 1 93  ASP 93  92  92  ASP ASP A . n 
A 1 94  GLY 94  93  93  GLY GLY A . n 
A 1 95  VAL 95  94  94  VAL VAL A . n 
A 1 96  ALA 96  95  95  ALA ALA A . n 
A 1 97  ASP 97  96  96  ASP ASP A . n 
A 1 98  VAL 98  97  97  VAL VAL A . n 
A 1 99  SER 99  98  98  SER SER A . n 
A 1 100 ILE 100 99  99  ILE ILE A . n 
A 1 101 GLU 101 100 100 GLU GLU A . n 
A 1 102 ASP 102 101 101 ASP ASP A . n 
A 1 103 SER 103 102 102 SER SER A . n 
A 1 104 VAL 104 103 103 VAL VAL A . n 
A 1 105 ILE 105 104 104 ILE ILE A . n 
A 1 106 SER 106 105 105 SER SER A . n 
A 1 107 LEU 107 106 106 LEU LEU A . n 
A 1 108 SER 108 107 107 SER SER A . n 
A 1 109 GLY 109 108 108 GLY GLY A . n 
A 1 110 ASP 110 109 109 ASP ASP A . n 
A 1 111 HIS 111 110 110 HIS HIS A . n 
A 1 112 SER 112 111 111 SER SER A . n 
A 1 113 ILE 113 112 112 ILE ILE A . n 
A 1 114 ILE 114 113 113 ILE ILE A . n 
A 1 115 GLY 115 114 114 GLY GLY A . n 
A 1 116 ARG 116 115 115 ARG ARG A . n 
A 1 117 THR 117 116 116 THR THR A . n 
A 1 118 LEU 118 117 117 LEU LEU A . n 
A 1 119 VAL 119 118 118 VAL VAL A . n 
A 1 120 VAL 120 119 119 VAL VAL A . n 
A 1 121 HIS 121 120 120 HIS HIS A . n 
A 1 122 GLU 122 121 121 GLU GLU A . n 
A 1 123 LYS 123 122 122 LYS LYS A . n 
A 1 124 ALA 124 123 123 ALA ALA A . n 
A 1 125 ASP 125 124 124 ASP ASP A . n 
A 1 126 ASP 126 125 125 ASP ASP A . n 
A 1 127 LEU 127 126 126 LEU LEU A . n 
A 1 128 GLY 128 127 127 GLY GLY A . n 
A 1 129 LYS 129 128 128 LYS LYS A . n 
A 1 130 GLY 130 129 129 GLY GLY A . n 
A 1 131 GLY 131 130 130 GLY GLY A . n 
A 1 132 ASN 132 131 131 ASN ASN A . n 
A 1 133 GLU 133 132 132 GLU GLU A . n 
A 1 134 GLU 134 133 133 GLU GLU A . n 
A 1 135 SER 135 134 134 SER SER A . n 
A 1 136 THR 136 135 135 THR THR A . n 
A 1 137 LYS 137 136 136 LYS LYS A . n 
A 1 138 THR 138 137 137 THR THR A . n 
A 1 139 GLY 139 138 138 GLY GLY A . n 
A 1 140 ASN 140 139 139 ASN ASN A . n 
A 1 141 ALA 141 140 140 ALA ALA A . n 
A 1 142 GLY 142 141 141 GLY GLY A . n 
A 1 143 SER 143 142 142 SER SER A . n 
A 1 144 ARG 144 143 143 ARG ARG A . n 
A 1 145 LEU 145 144 144 LEU LEU A . n 
A 1 146 ALA 146 145 145 ALA ALA A . n 
A 1 147 CYS 147 146 146 CYS CYS A . n 
A 1 148 GLY 148 147 147 GLY GLY A . n 
A 1 149 VAL 149 148 148 VAL VAL A . n 
A 1 150 ILE 150 149 149 ILE ILE A . n 
A 1 151 GLY 151 150 150 GLY GLY A . n 
A 1 152 ILE 152 151 151 ILE ILE A . n 
A 1 153 ALA 153 152 152 ALA ALA A . n 
A 1 154 GLN 154 153 153 GLN GLN A . n 
A 1 155 GLY 155 154 154 GLY GLY A . n 
A 1 156 ALA 156 155 155 ALA ALA A . n 
A 1 157 ALA 157 156 ?   ?   ?   A . n 
A 1 158 ALA 158 157 ?   ?   ?   A . n 
A 1 159 SER 159 158 ?   ?   ?   A . n 
A 1 160 GLY 160 159 ?   ?   ?   A . n 
A 1 161 GLY 161 160 ?   ?   ?   A . n 
A 1 162 GLY 162 161 ?   ?   ?   A . n 
A 1 163 GLY 163 162 ?   ?   ?   A . n 
A 1 164 GLY 164 163 ?   ?   ?   A . n 
A 1 165 SER 165 164 ?   ?   ?   A . n 
A 1 166 GLY 166 165 ?   ?   ?   A . n 
A 1 167 GLY 167 166 166 GLY GLY A . n 
A 1 168 GLY 168 167 167 GLY GLY A . n 
A 1 169 GLY 169 168 168 GLY GLY A . n 
A 1 170 SER 170 169 169 SER SER A . n 
A 1 171 ALA 171 170 170 ALA ALA A . n 
A 1 172 THR 172 171 171 THR THR A . n 
A 1 173 LYS 173 172 172 LYS LYS A . n 
A 1 174 ALA 174 173 173 ALA ALA A . n 
A 1 175 VAL 175 174 174 VAL VAL A . n 
A 1 176 CYS 176 175 175 CYS CYS A . n 
A 1 177 VAL 177 176 176 VAL VAL A . n 
A 1 178 LEU 178 177 177 LEU LEU A . n 
A 1 179 LYS 179 178 178 LYS LYS A . n 
A 1 180 GLY 180 179 179 GLY GLY A . n 
A 1 181 ASP 181 180 180 ASP ASP A . n 
A 1 182 GLY 182 181 181 GLY GLY A . n 
A 1 183 PRO 183 182 182 PRO PRO A . n 
A 1 184 VAL 184 183 183 VAL VAL A . n 
A 1 185 GLN 185 184 184 GLN GLN A . n 
A 1 186 GLY 186 185 185 GLY GLY A . n 
A 1 187 ILE 187 186 186 ILE ILE A . n 
A 1 188 ILE 188 187 187 ILE ILE A . n 
A 1 189 ASN 189 188 188 ASN ASN A . n 
A 1 190 PHE 190 189 189 PHE PHE A . n 
A 1 191 GLU 191 190 190 GLU GLU A . n 
A 1 192 GLN 192 191 191 GLN GLN A . n 
A 1 193 LYS 193 192 192 LYS LYS A . n 
A 1 194 GLU 194 193 193 GLU GLU A . n 
A 1 195 SER 195 194 194 SER SER A . n 
A 1 196 ASN 196 195 195 ASN ASN A . n 
A 1 197 GLY 197 196 196 GLY GLY A . n 
A 1 198 PRO 198 197 197 PRO PRO A . n 
A 1 199 VAL 199 198 198 VAL VAL A . n 
A 1 200 LYS 200 199 199 LYS LYS A . n 
A 1 201 VAL 201 200 200 VAL VAL A . n 
A 1 202 TRP 202 201 201 TRP TRP A . n 
A 1 203 GLY 203 202 202 GLY GLY A . n 
A 1 204 SER 204 203 203 SER SER A . n 
A 1 205 ILE 205 204 204 ILE ILE A . n 
A 1 206 LYS 206 205 205 LYS LYS A . n 
A 1 207 GLY 207 206 206 GLY GLY A . n 
A 1 208 LEU 208 207 207 LEU LEU A . n 
A 1 209 THR 209 208 208 THR THR A . n 
A 1 210 GLU 210 209 209 GLU GLU A . n 
A 1 211 GLY 211 210 210 GLY GLY A . n 
A 1 212 LEU 212 211 211 LEU LEU A . n 
A 1 213 HIS 213 212 212 HIS HIS A . n 
A 1 214 GLY 214 213 213 GLY GLY A . n 
A 1 215 PHE 215 214 214 PHE PHE A . n 
A 1 216 HIS 216 215 215 HIS HIS A . n 
A 1 217 VAL 217 216 216 VAL VAL A . n 
A 1 218 HIS 218 217 217 HIS HIS A . n 
A 1 219 GLU 219 218 218 GLU GLU A . n 
A 1 220 PHE 220 219 219 PHE PHE A . n 
A 1 221 GLY 221 220 220 GLY GLY A . n 
A 1 222 ASP 222 221 221 ASP ASP A . n 
A 1 223 ASN 223 222 222 ASN ASN A . n 
A 1 224 THR 224 223 223 THR THR A . n 
A 1 225 ALA 225 224 224 ALA ALA A . n 
A 1 226 GLY 226 225 225 GLY GLY A . n 
A 1 227 CYS 227 226 226 CYS CYS A . n 
A 1 228 THR 228 227 227 THR THR A . n 
A 1 229 SER 229 228 228 SER SER A . n 
A 1 230 ALA 230 229 229 ALA ALA A . n 
A 1 231 GLY 231 230 230 GLY GLY A . n 
A 1 232 PRO 232 231 231 PRO PRO A . n 
A 1 233 HIS 233 232 232 HIS HIS A . n 
A 1 234 PHE 234 233 233 PHE PHE A . n 
A 1 235 ASN 235 234 234 ASN ASN A . n 
A 1 236 PRO 236 235 235 PRO PRO A . n 
A 1 237 LEU 237 236 236 LEU LEU A . n 
A 1 238 SER 238 237 237 SER SER A . n 
A 1 239 ARG 239 238 238 ARG ARG A . n 
A 1 240 LYS 240 239 239 LYS LYS A . n 
A 1 241 HIS 241 240 240 HIS HIS A . n 
A 1 242 GLY 242 241 241 GLY GLY A . n 
A 1 243 GLY 243 242 242 GLY GLY A . n 
A 1 244 PRO 244 243 243 PRO PRO A . n 
A 1 245 LYS 245 244 244 LYS LYS A . n 
A 1 246 ASP 246 245 245 ASP ASP A . n 
A 1 247 GLU 247 246 246 GLU GLU A . n 
A 1 248 GLU 248 247 247 GLU GLU A . n 
A 1 249 ARG 249 248 248 ARG ARG A . n 
A 1 250 HIS 250 249 249 HIS HIS A . n 
A 1 251 VAL 251 250 250 VAL VAL A . n 
A 1 252 GLY 252 251 251 GLY GLY A . n 
A 1 253 SER 253 252 252 SER SER A . y 
A 1 253 ASP 253 252 252 ASP ASP A . y 
A 1 254 LEU 254 253 253 LEU LEU A . n 
A 1 255 GLY 255 254 254 GLY GLY A . n 
A 1 256 ASN 256 255 255 ASN ASN A . n 
A 1 257 VAL 257 256 256 VAL VAL A . n 
A 1 258 THR 258 257 257 THR THR A . n 
A 1 259 ALA 259 258 258 ALA ALA A . n 
A 1 260 ASP 260 259 259 ASP ASP A . n 
A 1 261 LYS 261 260 260 LYS LYS A . n 
A 1 262 ASP 262 261 261 ASP ASP A . n 
A 1 263 GLY 263 262 262 GLY GLY A . n 
A 1 264 VAL 264 263 263 VAL VAL A . n 
A 1 265 ALA 265 264 264 ALA ALA A . n 
A 1 266 ASP 266 265 265 ASP ASP A . n 
A 1 267 VAL 267 266 266 VAL VAL A . n 
A 1 268 SER 268 267 267 SER SER A . n 
A 1 269 ILE 269 268 268 ILE ILE A . n 
A 1 270 GLU 270 269 269 GLU GLU A . n 
A 1 271 ASP 271 270 270 ASP ASP A . n 
A 1 272 SER 272 271 271 SER SER A . n 
A 1 273 VAL 273 272 272 VAL VAL A . n 
A 1 274 ILE 274 273 273 ILE ILE A . n 
A 1 275 SER 275 274 274 SER SER A . n 
A 1 276 LEU 276 275 275 LEU LEU A . n 
A 1 277 SER 277 276 276 SER SER A . n 
A 1 278 GLY 278 277 277 GLY GLY A . n 
A 1 279 ASP 279 278 278 ASP ASP A . n 
A 1 280 HIS 280 279 279 HIS HIS A . n 
A 1 281 SER 281 280 280 SER SER A . n 
A 1 282 ILE 282 281 281 ILE ILE A . n 
A 1 283 ILE 283 282 282 ILE ILE A . n 
A 1 284 GLY 284 283 283 GLY GLY A . n 
A 1 285 ARG 285 284 284 ARG ARG A . n 
A 1 286 THR 286 285 285 THR THR A . n 
A 1 287 LEU 287 286 286 LEU LEU A . n 
A 1 288 VAL 288 287 287 VAL VAL A . n 
A 1 289 VAL 289 288 288 VAL VAL A . n 
A 1 290 HIS 290 289 289 HIS HIS A . n 
A 1 291 GLU 291 290 290 GLU GLU A . n 
A 1 292 LYS 292 291 291 LYS LYS A . n 
A 1 293 ALA 293 292 292 ALA ALA A . n 
A 1 294 ASP 294 293 293 ASP ASP A . n 
A 1 295 ASP 295 294 294 ASP ASP A . n 
A 1 296 LEU 296 295 295 LEU LEU A . n 
A 1 297 GLY 297 296 296 GLY GLY A . n 
A 1 298 LYS 298 297 297 LYS LYS A . n 
A 1 299 GLY 299 298 298 GLY GLY A . n 
A 1 300 GLY 300 299 299 GLY GLY A . n 
A 1 301 ASN 301 300 300 ASN ASN A . n 
A 1 302 GLU 302 301 301 GLU GLU A . n 
A 1 303 GLU 303 302 302 GLU GLU A . n 
A 1 304 SER 304 303 303 SER SER A . n 
A 1 305 THR 305 304 304 THR THR A . n 
A 1 306 LYS 306 305 305 LYS LYS A . n 
A 1 307 THR 307 306 306 THR THR A . n 
A 1 308 GLY 308 307 307 GLY GLY A . n 
A 1 309 ASN 309 308 308 ASN ASN A . n 
A 1 310 ALA 310 309 309 ALA ALA A . n 
A 1 311 GLY 311 310 310 GLY GLY A . n 
A 1 312 SER 312 311 311 SER SER A . n 
A 1 313 ARG 313 312 312 ARG ARG A . n 
A 1 314 LEU 314 313 313 LEU LEU A . n 
A 1 315 ALA 315 314 314 ALA ALA A . n 
A 1 316 CYS 316 315 315 CYS CYS A . n 
A 1 317 GLY 317 316 316 GLY GLY A . n 
A 1 318 VAL 318 317 317 VAL VAL A . n 
A 1 319 ILE 319 318 318 ILE ILE A . n 
A 1 320 GLY 320 319 319 GLY GLY A . n 
A 1 321 ILE 321 320 320 ILE ILE A . n 
A 1 322 ALA 322 321 321 ALA ALA A . n 
A 1 323 GLN 323 322 322 GLN GLN A . n 
B 1 1   MET 1   0   ?   ?   ?   C . n 
B 1 2   ALA 2   1   1   ALA ALA C . n 
B 1 3   THR 3   2   2   THR THR C . n 
B 1 4   LYS 4   3   3   LYS LYS C . n 
B 1 5   ALA 5   4   4   ALA ALA C . n 
B 1 6   VAL 6   5   5   VAL VAL C . n 
B 1 7   CYS 7   6   6   CYS CYS C . n 
B 1 8   VAL 8   7   7   VAL VAL C . n 
B 1 9   LEU 9   8   8   LEU LEU C . n 
B 1 10  LYS 10  9   9   LYS LYS C . n 
B 1 11  GLY 11  10  10  GLY GLY C . n 
B 1 12  ASP 12  11  11  ASP ASP C . n 
B 1 13  GLY 13  12  12  GLY GLY C . n 
B 1 14  PRO 14  13  13  PRO PRO C . n 
B 1 15  VAL 15  14  14  VAL VAL C . n 
B 1 16  GLN 16  15  15  GLN GLN C . n 
B 1 17  GLY 17  16  16  GLY GLY C . n 
B 1 18  ILE 18  17  17  ILE ILE C . n 
B 1 19  ILE 19  18  18  ILE ILE C . n 
B 1 20  ASN 20  19  19  ASN ASN C . n 
B 1 21  PHE 21  20  20  PHE PHE C . n 
B 1 22  GLU 22  21  21  GLU GLU C . n 
B 1 23  GLN 23  22  22  GLN GLN C . n 
B 1 24  LYS 24  23  23  LYS LYS C . n 
B 1 25  GLU 25  24  24  GLU GLU C . n 
B 1 26  SER 26  25  25  SER SER C . n 
B 1 27  ASN 27  26  26  ASN ASN C . n 
B 1 28  GLY 28  27  27  GLY GLY C . n 
B 1 29  PRO 29  28  28  PRO PRO C . n 
B 1 30  VAL 30  29  29  VAL VAL C . n 
B 1 31  LYS 31  30  30  LYS LYS C . n 
B 1 32  VAL 32  31  31  VAL VAL C . n 
B 1 33  TRP 33  32  32  TRP TRP C . n 
B 1 34  GLY 34  33  33  GLY GLY C . n 
B 1 35  SER 35  34  34  SER SER C . n 
B 1 36  ILE 36  35  35  ILE ILE C . n 
B 1 37  LYS 37  36  36  LYS LYS C . n 
B 1 38  GLY 38  37  37  GLY GLY C . n 
B 1 39  LEU 39  38  38  LEU LEU C . n 
B 1 40  THR 40  39  39  THR THR C . n 
B 1 41  GLU 41  40  40  GLU GLU C . n 
B 1 42  GLY 42  41  41  GLY GLY C . n 
B 1 43  LEU 43  42  42  LEU LEU C . n 
B 1 44  HIS 44  43  43  HIS HIS C . n 
B 1 45  GLY 45  44  44  GLY GLY C . n 
B 1 46  PHE 46  45  45  PHE PHE C . n 
B 1 47  HIS 47  46  46  HIS HIS C . n 
B 1 48  VAL 48  47  47  VAL VAL C . n 
B 1 49  HIS 49  48  48  HIS HIS C . n 
B 1 50  GLU 50  49  49  GLU GLU C . n 
B 1 51  PHE 51  50  50  PHE PHE C . n 
B 1 52  GLY 52  51  51  GLY GLY C . n 
B 1 53  ASP 53  52  52  ASP ASP C . n 
B 1 54  ASN 54  53  53  ASN ASN C . n 
B 1 55  THR 55  54  54  THR THR C . n 
B 1 56  ALA 56  55  55  ALA ALA C . n 
B 1 57  GLY 57  56  56  GLY GLY C . n 
B 1 58  CYS 58  57  57  CYS CYS C . n 
B 1 59  THR 59  58  58  THR THR C . n 
B 1 60  SER 60  59  59  SER SER C . n 
B 1 61  ALA 61  60  60  ALA ALA C . n 
B 1 62  GLY 62  61  61  GLY GLY C . n 
B 1 63  PRO 63  62  62  PRO PRO C . n 
B 1 64  HIS 64  63  63  HIS HIS C . n 
B 1 65  PHE 65  64  64  PHE PHE C . n 
B 1 66  ASN 66  65  65  ASN ASN C . n 
B 1 67  PRO 67  66  66  PRO PRO C . n 
B 1 68  LEU 68  67  67  LEU LEU C . n 
B 1 69  SER 69  68  68  SER SER C . n 
B 1 70  ARG 70  69  69  ARG ARG C . n 
B 1 71  LYS 71  70  70  LYS LYS C . n 
B 1 72  HIS 72  71  71  HIS HIS C . n 
B 1 73  GLY 73  72  72  GLY GLY C . n 
B 1 74  GLY 74  73  73  GLY GLY C . n 
B 1 75  PRO 75  74  74  PRO PRO C . n 
B 1 76  LYS 76  75  75  LYS LYS C . n 
B 1 77  ASP 77  76  76  ASP ASP C . n 
B 1 78  GLU 78  77  77  GLU GLU C . n 
B 1 79  GLU 79  78  78  GLU GLU C . n 
B 1 80  ARG 80  79  79  ARG ARG C . n 
B 1 81  HIS 81  80  80  HIS HIS C . n 
B 1 82  VAL 82  81  81  VAL VAL C . n 
B 1 83  GLY 83  82  82  GLY GLY C . n 
B 1 84  SER 84  83  83  SER SER C . y 
B 1 84  ASP 84  83  83  ASP ASP C . y 
B 1 85  LEU 85  84  84  LEU LEU C . n 
B 1 86  GLY 86  85  85  GLY GLY C . n 
B 1 87  ASN 87  86  86  ASN ASN C . n 
B 1 88  VAL 88  87  87  VAL VAL C . n 
B 1 89  THR 89  88  88  THR THR C . n 
B 1 90  ALA 90  89  89  ALA ALA C . n 
B 1 91  ASP 91  90  90  ASP ASP C . n 
B 1 92  LYS 92  91  91  LYS LYS C . n 
B 1 93  ASP 93  92  92  ASP ASP C . n 
B 1 94  GLY 94  93  93  GLY GLY C . n 
B 1 95  VAL 95  94  94  VAL VAL C . n 
B 1 96  ALA 96  95  95  ALA ALA C . n 
B 1 97  ASP 97  96  96  ASP ASP C . n 
B 1 98  VAL 98  97  97  VAL VAL C . n 
B 1 99  SER 99  98  98  SER SER C . n 
B 1 100 ILE 100 99  99  ILE ILE C . n 
B 1 101 GLU 101 100 100 GLU GLU C . n 
B 1 102 ASP 102 101 101 ASP ASP C . n 
B 1 103 SER 103 102 102 SER SER C . n 
B 1 104 VAL 104 103 103 VAL VAL C . n 
B 1 105 ILE 105 104 104 ILE ILE C . n 
B 1 106 SER 106 105 105 SER SER C . n 
B 1 107 LEU 107 106 106 LEU LEU C . n 
B 1 108 SER 108 107 107 SER SER C . n 
B 1 109 GLY 109 108 108 GLY GLY C . n 
B 1 110 ASP 110 109 109 ASP ASP C . n 
B 1 111 HIS 111 110 110 HIS HIS C . n 
B 1 112 SER 112 111 111 SER SER C . n 
B 1 113 ILE 113 112 112 ILE ILE C . n 
B 1 114 ILE 114 113 113 ILE ILE C . n 
B 1 115 GLY 115 114 114 GLY GLY C . n 
B 1 116 ARG 116 115 115 ARG ARG C . n 
B 1 117 THR 117 116 116 THR THR C . n 
B 1 118 LEU 118 117 117 LEU LEU C . n 
B 1 119 VAL 119 118 118 VAL VAL C . n 
B 1 120 VAL 120 119 119 VAL VAL C . n 
B 1 121 HIS 121 120 120 HIS HIS C . n 
B 1 122 GLU 122 121 121 GLU GLU C . n 
B 1 123 LYS 123 122 122 LYS LYS C . n 
B 1 124 ALA 124 123 123 ALA ALA C . n 
B 1 125 ASP 125 124 124 ASP ASP C . n 
B 1 126 ASP 126 125 125 ASP ASP C . n 
B 1 127 LEU 127 126 126 LEU LEU C . n 
B 1 128 GLY 128 127 127 GLY GLY C . n 
B 1 129 LYS 129 128 128 LYS LYS C . n 
B 1 130 GLY 130 129 129 GLY GLY C . n 
B 1 131 GLY 131 130 130 GLY GLY C . n 
B 1 132 ASN 132 131 131 ASN ASN C . n 
B 1 133 GLU 133 132 132 GLU GLU C . n 
B 1 134 GLU 134 133 133 GLU GLU C . n 
B 1 135 SER 135 134 134 SER SER C . n 
B 1 136 THR 136 135 135 THR THR C . n 
B 1 137 LYS 137 136 136 LYS LYS C . n 
B 1 138 THR 138 137 137 THR THR C . n 
B 1 139 GLY 139 138 138 GLY GLY C . n 
B 1 140 ASN 140 139 139 ASN ASN C . n 
B 1 141 ALA 141 140 140 ALA ALA C . n 
B 1 142 GLY 142 141 141 GLY GLY C . n 
B 1 143 SER 143 142 142 SER SER C . n 
B 1 144 ARG 144 143 143 ARG ARG C . n 
B 1 145 LEU 145 144 144 LEU LEU C . n 
B 1 146 ALA 146 145 145 ALA ALA C . n 
B 1 147 CYS 147 146 146 CYS CYS C . n 
B 1 148 GLY 148 147 147 GLY GLY C . n 
B 1 149 VAL 149 148 148 VAL VAL C . n 
B 1 150 ILE 150 149 149 ILE ILE C . n 
B 1 151 GLY 151 150 150 GLY GLY C . n 
B 1 152 ILE 152 151 151 ILE ILE C . n 
B 1 153 ALA 153 152 152 ALA ALA C . n 
B 1 154 GLN 154 153 153 GLN GLN C . n 
B 1 155 GLY 155 154 154 GLY GLY C . n 
B 1 156 ALA 156 155 ?   ?   ?   C . n 
B 1 157 ALA 157 156 ?   ?   ?   C . n 
B 1 158 ALA 158 157 ?   ?   ?   C . n 
B 1 159 SER 159 158 ?   ?   ?   C . n 
B 1 160 GLY 160 159 ?   ?   ?   C . n 
B 1 161 GLY 161 160 ?   ?   ?   C . n 
B 1 162 GLY 162 161 ?   ?   ?   C . n 
B 1 163 GLY 163 162 ?   ?   ?   C . n 
B 1 164 GLY 164 163 ?   ?   ?   C . n 
B 1 165 SER 165 164 ?   ?   ?   C . n 
B 1 166 GLY 166 165 ?   ?   ?   C . n 
B 1 167 GLY 167 166 166 GLY GLY C . n 
B 1 168 GLY 168 167 167 GLY GLY C . n 
B 1 169 GLY 169 168 168 GLY GLY C . n 
B 1 170 SER 170 169 169 SER SER C . n 
B 1 171 ALA 171 170 170 ALA ALA C . n 
B 1 172 THR 172 171 171 THR THR C . n 
B 1 173 LYS 173 172 172 LYS LYS C . n 
B 1 174 ALA 174 173 173 ALA ALA C . n 
B 1 175 VAL 175 174 174 VAL VAL C . n 
B 1 176 CYS 176 175 175 CYS CYS C . n 
B 1 177 VAL 177 176 176 VAL VAL C . n 
B 1 178 LEU 178 177 177 LEU LEU C . n 
B 1 179 LYS 179 178 178 LYS LYS C . n 
B 1 180 GLY 180 179 179 GLY GLY C . n 
B 1 181 ASP 181 180 180 ASP ASP C . n 
B 1 182 GLY 182 181 181 GLY GLY C . n 
B 1 183 PRO 183 182 182 PRO PRO C . n 
B 1 184 VAL 184 183 183 VAL VAL C . n 
B 1 185 GLN 185 184 184 GLN GLN C . n 
B 1 186 GLY 186 185 185 GLY GLY C . n 
B 1 187 ILE 187 186 186 ILE ILE C . n 
B 1 188 ILE 188 187 187 ILE ILE C . n 
B 1 189 ASN 189 188 188 ASN ASN C . n 
B 1 190 PHE 190 189 189 PHE PHE C . n 
B 1 191 GLU 191 190 190 GLU GLU C . n 
B 1 192 GLN 192 191 191 GLN GLN C . n 
B 1 193 LYS 193 192 192 LYS LYS C . n 
B 1 194 GLU 194 193 193 GLU GLU C . n 
B 1 195 SER 195 194 194 SER SER C . n 
B 1 196 ASN 196 195 195 ASN ASN C . n 
B 1 197 GLY 197 196 196 GLY GLY C . n 
B 1 198 PRO 198 197 197 PRO PRO C . n 
B 1 199 VAL 199 198 198 VAL VAL C . n 
B 1 200 LYS 200 199 199 LYS LYS C . n 
B 1 201 VAL 201 200 200 VAL VAL C . n 
B 1 202 TRP 202 201 201 TRP TRP C . n 
B 1 203 GLY 203 202 202 GLY GLY C . n 
B 1 204 SER 204 203 203 SER SER C . n 
B 1 205 ILE 205 204 204 ILE ILE C . n 
B 1 206 LYS 206 205 205 LYS LYS C . n 
B 1 207 GLY 207 206 206 GLY GLY C . n 
B 1 208 LEU 208 207 207 LEU LEU C . n 
B 1 209 THR 209 208 208 THR THR C . n 
B 1 210 GLU 210 209 209 GLU GLU C . n 
B 1 211 GLY 211 210 210 GLY GLY C . n 
B 1 212 LEU 212 211 211 LEU LEU C . n 
B 1 213 HIS 213 212 212 HIS HIS C . n 
B 1 214 GLY 214 213 213 GLY GLY C . n 
B 1 215 PHE 215 214 214 PHE PHE C . n 
B 1 216 HIS 216 215 215 HIS HIS C . n 
B 1 217 VAL 217 216 216 VAL VAL C . n 
B 1 218 HIS 218 217 217 HIS HIS C . n 
B 1 219 GLU 219 218 218 GLU GLU C . n 
B 1 220 PHE 220 219 219 PHE PHE C . n 
B 1 221 GLY 221 220 220 GLY GLY C . n 
B 1 222 ASP 222 221 221 ASP ASP C . n 
B 1 223 ASN 223 222 222 ASN ASN C . n 
B 1 224 THR 224 223 223 THR THR C . n 
B 1 225 ALA 225 224 224 ALA ALA C . n 
B 1 226 GLY 226 225 225 GLY GLY C . n 
B 1 227 CYS 227 226 226 CYS CYS C . n 
B 1 228 THR 228 227 227 THR THR C . n 
B 1 229 SER 229 228 228 SER SER C . n 
B 1 230 ALA 230 229 229 ALA ALA C . n 
B 1 231 GLY 231 230 230 GLY GLY C . n 
B 1 232 PRO 232 231 231 PRO PRO C . n 
B 1 233 HIS 233 232 232 HIS HIS C . n 
B 1 234 PHE 234 233 233 PHE PHE C . n 
B 1 235 ASN 235 234 234 ASN ASN C . n 
B 1 236 PRO 236 235 235 PRO PRO C . n 
B 1 237 LEU 237 236 236 LEU LEU C . n 
B 1 238 SER 238 237 237 SER SER C . n 
B 1 239 ARG 239 238 238 ARG ARG C . n 
B 1 240 LYS 240 239 239 LYS LYS C . n 
B 1 241 HIS 241 240 240 HIS HIS C . n 
B 1 242 GLY 242 241 241 GLY GLY C . n 
B 1 243 GLY 243 242 242 GLY GLY C . n 
B 1 244 PRO 244 243 243 PRO PRO C . n 
B 1 245 LYS 245 244 244 LYS LYS C . n 
B 1 246 ASP 246 245 245 ASP ASP C . n 
B 1 247 GLU 247 246 246 GLU GLU C . n 
B 1 248 GLU 248 247 247 GLU GLU C . n 
B 1 249 ARG 249 248 248 ARG ARG C . n 
B 1 250 HIS 250 249 249 HIS HIS C . n 
B 1 251 VAL 251 250 250 VAL VAL C . n 
B 1 252 GLY 252 251 251 GLY GLY C . n 
B 1 253 SER 253 252 252 SER SER C . y 
B 1 253 ASP 253 252 252 ASP ASP C . y 
B 1 254 LEU 254 253 253 LEU LEU C . n 
B 1 255 GLY 255 254 254 GLY GLY C . n 
B 1 256 ASN 256 255 255 ASN ASN C . n 
B 1 257 VAL 257 256 256 VAL VAL C . n 
B 1 258 THR 258 257 257 THR THR C . n 
B 1 259 ALA 259 258 258 ALA ALA C . n 
B 1 260 ASP 260 259 259 ASP ASP C . n 
B 1 261 LYS 261 260 260 LYS LYS C . n 
B 1 262 ASP 262 261 261 ASP ASP C . n 
B 1 263 GLY 263 262 262 GLY GLY C . n 
B 1 264 VAL 264 263 263 VAL VAL C . n 
B 1 265 ALA 265 264 264 ALA ALA C . n 
B 1 266 ASP 266 265 265 ASP ASP C . n 
B 1 267 VAL 267 266 266 VAL VAL C . n 
B 1 268 SER 268 267 267 SER SER C . n 
B 1 269 ILE 269 268 268 ILE ILE C . n 
B 1 270 GLU 270 269 269 GLU GLU C . n 
B 1 271 ASP 271 270 270 ASP ASP C . n 
B 1 272 SER 272 271 271 SER SER C . n 
B 1 273 VAL 273 272 272 VAL VAL C . n 
B 1 274 ILE 274 273 273 ILE ILE C . n 
B 1 275 SER 275 274 274 SER SER C . n 
B 1 276 LEU 276 275 275 LEU LEU C . n 
B 1 277 SER 277 276 276 SER SER C . n 
B 1 278 GLY 278 277 277 GLY GLY C . n 
B 1 279 ASP 279 278 278 ASP ASP C . n 
B 1 280 HIS 280 279 279 HIS HIS C . n 
B 1 281 SER 281 280 280 SER SER C . n 
B 1 282 ILE 282 281 281 ILE ILE C . n 
B 1 283 ILE 283 282 282 ILE ILE C . n 
B 1 284 GLY 284 283 283 GLY GLY C . n 
B 1 285 ARG 285 284 284 ARG ARG C . n 
B 1 286 THR 286 285 285 THR THR C . n 
B 1 287 LEU 287 286 286 LEU LEU C . n 
B 1 288 VAL 288 287 287 VAL VAL C . n 
B 1 289 VAL 289 288 288 VAL VAL C . n 
B 1 290 HIS 290 289 289 HIS HIS C . n 
B 1 291 GLU 291 290 290 GLU GLU C . n 
B 1 292 LYS 292 291 291 LYS LYS C . n 
B 1 293 ALA 293 292 292 ALA ALA C . n 
B 1 294 ASP 294 293 293 ASP ASP C . n 
B 1 295 ASP 295 294 294 ASP ASP C . n 
B 1 296 LEU 296 295 295 LEU LEU C . n 
B 1 297 GLY 297 296 296 GLY GLY C . n 
B 1 298 LYS 298 297 297 LYS LYS C . n 
B 1 299 GLY 299 298 298 GLY GLY C . n 
B 1 300 GLY 300 299 299 GLY GLY C . n 
B 1 301 ASN 301 300 300 ASN ASN C . n 
B 1 302 GLU 302 301 301 GLU GLU C . n 
B 1 303 GLU 303 302 302 GLU GLU C . n 
B 1 304 SER 304 303 303 SER SER C . n 
B 1 305 THR 305 304 304 THR THR C . n 
B 1 306 LYS 306 305 305 LYS LYS C . n 
B 1 307 THR 307 306 306 THR THR C . n 
B 1 308 GLY 308 307 307 GLY GLY C . n 
B 1 309 ASN 309 308 308 ASN ASN C . n 
B 1 310 ALA 310 309 309 ALA ALA C . n 
B 1 311 GLY 311 310 310 GLY GLY C . n 
B 1 312 SER 312 311 311 SER SER C . n 
B 1 313 ARG 313 312 312 ARG ARG C . n 
B 1 314 LEU 314 313 313 LEU LEU C . n 
B 1 315 ALA 315 314 314 ALA ALA C . n 
B 1 316 CYS 316 315 315 CYS CYS C . n 
B 1 317 GLY 317 316 316 GLY GLY C . n 
B 1 318 VAL 318 317 317 VAL VAL C . n 
B 1 319 ILE 319 318 318 ILE ILE C . n 
B 1 320 GLY 320 319 319 GLY GLY C . n 
B 1 321 ILE 321 320 320 ILE ILE C . n 
B 1 322 ALA 322 321 321 ALA ALA C . n 
B 1 323 GLN 323 322 322 GLN GLN C . n 
C 1 1   MET 1   0   ?   ?   ?   E . n 
C 1 2   ALA 2   1   1   ALA ALA E . n 
C 1 3   THR 3   2   2   THR THR E . n 
C 1 4   LYS 4   3   3   LYS LYS E . n 
C 1 5   ALA 5   4   4   ALA ALA E . n 
C 1 6   VAL 6   5   5   VAL VAL E . n 
C 1 7   CYS 7   6   6   CYS CYS E . n 
C 1 8   VAL 8   7   7   VAL VAL E . n 
C 1 9   LEU 9   8   8   LEU LEU E . n 
C 1 10  LYS 10  9   9   LYS LYS E . n 
C 1 11  GLY 11  10  10  GLY GLY E . n 
C 1 12  ASP 12  11  11  ASP ASP E . n 
C 1 13  GLY 13  12  12  GLY GLY E . n 
C 1 14  PRO 14  13  13  PRO PRO E . n 
C 1 15  VAL 15  14  14  VAL VAL E . n 
C 1 16  GLN 16  15  15  GLN GLN E . n 
C 1 17  GLY 17  16  16  GLY GLY E . n 
C 1 18  ILE 18  17  17  ILE ILE E . n 
C 1 19  ILE 19  18  18  ILE ILE E . n 
C 1 20  ASN 20  19  19  ASN ASN E . n 
C 1 21  PHE 21  20  20  PHE PHE E . n 
C 1 22  GLU 22  21  21  GLU GLU E . n 
C 1 23  GLN 23  22  22  GLN GLN E . n 
C 1 24  LYS 24  23  23  LYS LYS E . n 
C 1 25  GLU 25  24  24  GLU GLU E . n 
C 1 26  SER 26  25  25  SER SER E . n 
C 1 27  ASN 27  26  26  ASN ASN E . n 
C 1 28  GLY 28  27  27  GLY GLY E . n 
C 1 29  PRO 29  28  28  PRO PRO E . n 
C 1 30  VAL 30  29  29  VAL VAL E . n 
C 1 31  LYS 31  30  30  LYS LYS E . n 
C 1 32  VAL 32  31  31  VAL VAL E . n 
C 1 33  TRP 33  32  32  TRP TRP E . n 
C 1 34  GLY 34  33  33  GLY GLY E . n 
C 1 35  SER 35  34  34  SER SER E . n 
C 1 36  ILE 36  35  35  ILE ILE E . n 
C 1 37  LYS 37  36  36  LYS LYS E . n 
C 1 38  GLY 38  37  37  GLY GLY E . n 
C 1 39  LEU 39  38  38  LEU LEU E . n 
C 1 40  THR 40  39  39  THR THR E . n 
C 1 41  GLU 41  40  40  GLU GLU E . n 
C 1 42  GLY 42  41  41  GLY GLY E . n 
C 1 43  LEU 43  42  42  LEU LEU E . n 
C 1 44  HIS 44  43  43  HIS HIS E . n 
C 1 45  GLY 45  44  44  GLY GLY E . n 
C 1 46  PHE 46  45  45  PHE PHE E . n 
C 1 47  HIS 47  46  46  HIS HIS E . n 
C 1 48  VAL 48  47  47  VAL VAL E . n 
C 1 49  HIS 49  48  48  HIS HIS E . n 
C 1 50  GLU 50  49  49  GLU GLU E . n 
C 1 51  PHE 51  50  50  PHE PHE E . n 
C 1 52  GLY 52  51  51  GLY GLY E . n 
C 1 53  ASP 53  52  52  ASP ASP E . n 
C 1 54  ASN 54  53  53  ASN ASN E . n 
C 1 55  THR 55  54  54  THR THR E . n 
C 1 56  ALA 56  55  55  ALA ALA E . n 
C 1 57  GLY 57  56  56  GLY GLY E . n 
C 1 58  CYS 58  57  57  CYS CYS E . n 
C 1 59  THR 59  58  58  THR THR E . n 
C 1 60  SER 60  59  59  SER SER E . n 
C 1 61  ALA 61  60  60  ALA ALA E . n 
C 1 62  GLY 62  61  61  GLY GLY E . n 
C 1 63  PRO 63  62  62  PRO PRO E . n 
C 1 64  HIS 64  63  63  HIS HIS E . n 
C 1 65  PHE 65  64  64  PHE PHE E . n 
C 1 66  ASN 66  65  65  ASN ASN E . n 
C 1 67  PRO 67  66  66  PRO PRO E . n 
C 1 68  LEU 68  67  67  LEU LEU E . n 
C 1 69  SER 69  68  68  SER SER E . n 
C 1 70  ARG 70  69  69  ARG ARG E . n 
C 1 71  LYS 71  70  70  LYS LYS E . n 
C 1 72  HIS 72  71  71  HIS HIS E . n 
C 1 73  GLY 73  72  72  GLY GLY E . n 
C 1 74  GLY 74  73  73  GLY GLY E . n 
C 1 75  PRO 75  74  74  PRO PRO E . n 
C 1 76  LYS 76  75  75  LYS LYS E . n 
C 1 77  ASP 77  76  76  ASP ASP E . n 
C 1 78  GLU 78  77  77  GLU GLU E . n 
C 1 79  GLU 79  78  78  GLU GLU E . n 
C 1 80  ARG 80  79  79  ARG ARG E . n 
C 1 81  HIS 81  80  80  HIS HIS E . n 
C 1 82  VAL 82  81  81  VAL VAL E . n 
C 1 83  GLY 83  82  82  GLY GLY E . n 
C 1 84  SER 84  83  83  SER SER E . y 
C 1 84  ASP 84  83  83  ASP ASP E . y 
C 1 85  LEU 85  84  84  LEU LEU E . n 
C 1 86  GLY 86  85  85  GLY GLY E . n 
C 1 87  ASN 87  86  86  ASN ASN E . n 
C 1 88  VAL 88  87  87  VAL VAL E . n 
C 1 89  THR 89  88  88  THR THR E . n 
C 1 90  ALA 90  89  89  ALA ALA E . n 
C 1 91  ASP 91  90  90  ASP ASP E . n 
C 1 92  LYS 92  91  91  LYS LYS E . n 
C 1 93  ASP 93  92  92  ASP ASP E . n 
C 1 94  GLY 94  93  93  GLY GLY E . n 
C 1 95  VAL 95  94  94  VAL VAL E . n 
C 1 96  ALA 96  95  95  ALA ALA E . n 
C 1 97  ASP 97  96  96  ASP ASP E . n 
C 1 98  VAL 98  97  97  VAL VAL E . n 
C 1 99  SER 99  98  98  SER SER E . n 
C 1 100 ILE 100 99  99  ILE ILE E . n 
C 1 101 GLU 101 100 100 GLU GLU E . n 
C 1 102 ASP 102 101 101 ASP ASP E . n 
C 1 103 SER 103 102 102 SER SER E . n 
C 1 104 VAL 104 103 103 VAL VAL E . n 
C 1 105 ILE 105 104 104 ILE ILE E . n 
C 1 106 SER 106 105 105 SER SER E . n 
C 1 107 LEU 107 106 106 LEU LEU E . n 
C 1 108 SER 108 107 107 SER SER E . n 
C 1 109 GLY 109 108 108 GLY GLY E . n 
C 1 110 ASP 110 109 109 ASP ASP E . n 
C 1 111 HIS 111 110 110 HIS HIS E . n 
C 1 112 SER 112 111 111 SER SER E . n 
C 1 113 ILE 113 112 112 ILE ILE E . n 
C 1 114 ILE 114 113 113 ILE ILE E . n 
C 1 115 GLY 115 114 114 GLY GLY E . n 
C 1 116 ARG 116 115 115 ARG ARG E . n 
C 1 117 THR 117 116 116 THR THR E . n 
C 1 118 LEU 118 117 117 LEU LEU E . n 
C 1 119 VAL 119 118 118 VAL VAL E . n 
C 1 120 VAL 120 119 119 VAL VAL E . n 
C 1 121 HIS 121 120 120 HIS HIS E . n 
C 1 122 GLU 122 121 121 GLU GLU E . n 
C 1 123 LYS 123 122 122 LYS LYS E . n 
C 1 124 ALA 124 123 123 ALA ALA E . n 
C 1 125 ASP 125 124 124 ASP ASP E . n 
C 1 126 ASP 126 125 125 ASP ASP E . n 
C 1 127 LEU 127 126 126 LEU LEU E . n 
C 1 128 GLY 128 127 127 GLY GLY E . n 
C 1 129 LYS 129 128 128 LYS LYS E . n 
C 1 130 GLY 130 129 129 GLY GLY E . n 
C 1 131 GLY 131 130 130 GLY GLY E . n 
C 1 132 ASN 132 131 131 ASN ASN E . n 
C 1 133 GLU 133 132 132 GLU GLU E . n 
C 1 134 GLU 134 133 133 GLU GLU E . n 
C 1 135 SER 135 134 134 SER SER E . n 
C 1 136 THR 136 135 135 THR THR E . n 
C 1 137 LYS 137 136 136 LYS LYS E . n 
C 1 138 THR 138 137 137 THR THR E . n 
C 1 139 GLY 139 138 138 GLY GLY E . n 
C 1 140 ASN 140 139 139 ASN ASN E . n 
C 1 141 ALA 141 140 140 ALA ALA E . n 
C 1 142 GLY 142 141 141 GLY GLY E . n 
C 1 143 SER 143 142 142 SER SER E . n 
C 1 144 ARG 144 143 143 ARG ARG E . n 
C 1 145 LEU 145 144 144 LEU LEU E . n 
C 1 146 ALA 146 145 145 ALA ALA E . n 
C 1 147 CYS 147 146 146 CYS CYS E . n 
C 1 148 GLY 148 147 147 GLY GLY E . n 
C 1 149 VAL 149 148 148 VAL VAL E . n 
C 1 150 ILE 150 149 149 ILE ILE E . n 
C 1 151 GLY 151 150 150 GLY GLY E . n 
C 1 152 ILE 152 151 151 ILE ILE E . n 
C 1 153 ALA 153 152 152 ALA ALA E . n 
C 1 154 GLN 154 153 153 GLN GLN E . n 
C 1 155 GLY 155 154 154 GLY GLY E . n 
C 1 156 ALA 156 155 155 ALA ALA E . n 
C 1 157 ALA 157 156 156 ALA ALA E . n 
C 1 158 ALA 158 157 ?   ?   ?   E . n 
C 1 159 SER 159 158 ?   ?   ?   E . n 
C 1 160 GLY 160 159 ?   ?   ?   E . n 
C 1 161 GLY 161 160 ?   ?   ?   E . n 
C 1 162 GLY 162 161 ?   ?   ?   E . n 
C 1 163 GLY 163 162 ?   ?   ?   E . n 
C 1 164 GLY 164 163 ?   ?   ?   E . n 
C 1 165 SER 165 164 ?   ?   ?   E . n 
C 1 166 GLY 166 165 ?   ?   ?   E . n 
C 1 167 GLY 167 166 166 GLY GLY E . n 
C 1 168 GLY 168 167 167 GLY GLY E . n 
C 1 169 GLY 169 168 168 GLY GLY E . n 
C 1 170 SER 170 169 169 SER SER E . n 
C 1 171 ALA 171 170 170 ALA ALA E . n 
C 1 172 THR 172 171 171 THR THR E . n 
C 1 173 LYS 173 172 172 LYS LYS E . n 
C 1 174 ALA 174 173 173 ALA ALA E . n 
C 1 175 VAL 175 174 174 VAL VAL E . n 
C 1 176 CYS 176 175 175 CYS CYS E . n 
C 1 177 VAL 177 176 176 VAL VAL E . n 
C 1 178 LEU 178 177 177 LEU LEU E . n 
C 1 179 LYS 179 178 178 LYS LYS E . n 
C 1 180 GLY 180 179 179 GLY GLY E . n 
C 1 181 ASP 181 180 180 ASP ASP E . n 
C 1 182 GLY 182 181 181 GLY GLY E . n 
C 1 183 PRO 183 182 182 PRO PRO E . n 
C 1 184 VAL 184 183 183 VAL VAL E . n 
C 1 185 GLN 185 184 184 GLN GLN E . n 
C 1 186 GLY 186 185 185 GLY GLY E . n 
C 1 187 ILE 187 186 186 ILE ILE E . n 
C 1 188 ILE 188 187 187 ILE ILE E . n 
C 1 189 ASN 189 188 188 ASN ASN E . n 
C 1 190 PHE 190 189 189 PHE PHE E . n 
C 1 191 GLU 191 190 190 GLU GLU E . n 
C 1 192 GLN 192 191 191 GLN GLN E . n 
C 1 193 LYS 193 192 192 LYS LYS E . n 
C 1 194 GLU 194 193 193 GLU GLU E . n 
C 1 195 SER 195 194 194 SER SER E . n 
C 1 196 ASN 196 195 195 ASN ASN E . n 
C 1 197 GLY 197 196 196 GLY GLY E . n 
C 1 198 PRO 198 197 197 PRO PRO E . n 
C 1 199 VAL 199 198 198 VAL VAL E . n 
C 1 200 LYS 200 199 199 LYS LYS E . n 
C 1 201 VAL 201 200 200 VAL VAL E . n 
C 1 202 TRP 202 201 201 TRP TRP E . n 
C 1 203 GLY 203 202 202 GLY GLY E . n 
C 1 204 SER 204 203 203 SER SER E . n 
C 1 205 ILE 205 204 204 ILE ILE E . n 
C 1 206 LYS 206 205 205 LYS LYS E . n 
C 1 207 GLY 207 206 206 GLY GLY E . n 
C 1 208 LEU 208 207 207 LEU LEU E . n 
C 1 209 THR 209 208 208 THR THR E . n 
C 1 210 GLU 210 209 209 GLU GLU E . n 
C 1 211 GLY 211 210 210 GLY GLY E . n 
C 1 212 LEU 212 211 211 LEU LEU E . n 
C 1 213 HIS 213 212 212 HIS HIS E . n 
C 1 214 GLY 214 213 213 GLY GLY E . n 
C 1 215 PHE 215 214 214 PHE PHE E . n 
C 1 216 HIS 216 215 215 HIS HIS E . n 
C 1 217 VAL 217 216 216 VAL VAL E . n 
C 1 218 HIS 218 217 217 HIS HIS E . n 
C 1 219 GLU 219 218 218 GLU GLU E . n 
C 1 220 PHE 220 219 219 PHE PHE E . n 
C 1 221 GLY 221 220 220 GLY GLY E . n 
C 1 222 ASP 222 221 221 ASP ASP E . n 
C 1 223 ASN 223 222 222 ASN ASN E . n 
C 1 224 THR 224 223 223 THR THR E . n 
C 1 225 ALA 225 224 224 ALA ALA E . n 
C 1 226 GLY 226 225 225 GLY GLY E . n 
C 1 227 CYS 227 226 226 CYS CYS E . n 
C 1 228 THR 228 227 227 THR THR E . n 
C 1 229 SER 229 228 228 SER SER E . n 
C 1 230 ALA 230 229 229 ALA ALA E . n 
C 1 231 GLY 231 230 230 GLY GLY E . n 
C 1 232 PRO 232 231 231 PRO PRO E . n 
C 1 233 HIS 233 232 232 HIS HIS E . n 
C 1 234 PHE 234 233 233 PHE PHE E . n 
C 1 235 ASN 235 234 234 ASN ASN E . n 
C 1 236 PRO 236 235 235 PRO PRO E . n 
C 1 237 LEU 237 236 236 LEU LEU E . n 
C 1 238 SER 238 237 237 SER SER E . n 
C 1 239 ARG 239 238 238 ARG ARG E . n 
C 1 240 LYS 240 239 239 LYS LYS E . n 
C 1 241 HIS 241 240 240 HIS HIS E . n 
C 1 242 GLY 242 241 241 GLY GLY E . n 
C 1 243 GLY 243 242 242 GLY GLY E . n 
C 1 244 PRO 244 243 243 PRO PRO E . n 
C 1 245 LYS 245 244 244 LYS LYS E . n 
C 1 246 ASP 246 245 245 ASP ASP E . n 
C 1 247 GLU 247 246 246 GLU GLU E . n 
C 1 248 GLU 248 247 247 GLU GLU E . n 
C 1 249 ARG 249 248 248 ARG ARG E . n 
C 1 250 HIS 250 249 249 HIS HIS E . n 
C 1 251 VAL 251 250 250 VAL VAL E . n 
C 1 252 GLY 252 251 251 GLY GLY E . n 
C 1 253 SER 253 252 252 SER SER E . y 
C 1 253 ASP 253 252 252 ASP ASP E . y 
C 1 254 LEU 254 253 253 LEU LEU E . n 
C 1 255 GLY 255 254 254 GLY GLY E . n 
C 1 256 ASN 256 255 255 ASN ASN E . n 
C 1 257 VAL 257 256 256 VAL VAL E . n 
C 1 258 THR 258 257 257 THR THR E . n 
C 1 259 ALA 259 258 258 ALA ALA E . n 
C 1 260 ASP 260 259 259 ASP ASP E . n 
C 1 261 LYS 261 260 260 LYS LYS E . n 
C 1 262 ASP 262 261 261 ASP ASP E . n 
C 1 263 GLY 263 262 262 GLY GLY E . n 
C 1 264 VAL 264 263 263 VAL VAL E . n 
C 1 265 ALA 265 264 264 ALA ALA E . n 
C 1 266 ASP 266 265 265 ASP ASP E . n 
C 1 267 VAL 267 266 266 VAL VAL E . n 
C 1 268 SER 268 267 267 SER SER E . n 
C 1 269 ILE 269 268 268 ILE ILE E . n 
C 1 270 GLU 270 269 269 GLU GLU E . n 
C 1 271 ASP 271 270 270 ASP ASP E . n 
C 1 272 SER 272 271 271 SER SER E . n 
C 1 273 VAL 273 272 272 VAL VAL E . n 
C 1 274 ILE 274 273 273 ILE ILE E . n 
C 1 275 SER 275 274 274 SER SER E . n 
C 1 276 LEU 276 275 275 LEU LEU E . n 
C 1 277 SER 277 276 276 SER SER E . n 
C 1 278 GLY 278 277 277 GLY GLY E . n 
C 1 279 ASP 279 278 278 ASP ASP E . n 
C 1 280 HIS 280 279 279 HIS HIS E . n 
C 1 281 SER 281 280 280 SER SER E . n 
C 1 282 ILE 282 281 281 ILE ILE E . n 
C 1 283 ILE 283 282 282 ILE ILE E . n 
C 1 284 GLY 284 283 283 GLY GLY E . n 
C 1 285 ARG 285 284 284 ARG ARG E . n 
C 1 286 THR 286 285 285 THR THR E . n 
C 1 287 LEU 287 286 286 LEU LEU E . n 
C 1 288 VAL 288 287 287 VAL VAL E . n 
C 1 289 VAL 289 288 288 VAL VAL E . n 
C 1 290 HIS 290 289 289 HIS HIS E . n 
C 1 291 GLU 291 290 290 GLU GLU E . n 
C 1 292 LYS 292 291 291 LYS LYS E . n 
C 1 293 ALA 293 292 292 ALA ALA E . n 
C 1 294 ASP 294 293 293 ASP ASP E . n 
C 1 295 ASP 295 294 294 ASP ASP E . n 
C 1 296 LEU 296 295 295 LEU LEU E . n 
C 1 297 GLY 297 296 296 GLY GLY E . n 
C 1 298 LYS 298 297 297 LYS LYS E . n 
C 1 299 GLY 299 298 298 GLY GLY E . n 
C 1 300 GLY 300 299 299 GLY GLY E . n 
C 1 301 ASN 301 300 300 ASN ASN E . n 
C 1 302 GLU 302 301 301 GLU GLU E . n 
C 1 303 GLU 303 302 302 GLU GLU E . n 
C 1 304 SER 304 303 303 SER SER E . n 
C 1 305 THR 305 304 304 THR THR E . n 
C 1 306 LYS 306 305 305 LYS LYS E . n 
C 1 307 THR 307 306 306 THR THR E . n 
C 1 308 GLY 308 307 307 GLY GLY E . n 
C 1 309 ASN 309 308 308 ASN ASN E . n 
C 1 310 ALA 310 309 309 ALA ALA E . n 
C 1 311 GLY 311 310 310 GLY GLY E . n 
C 1 312 SER 312 311 311 SER SER E . n 
C 1 313 ARG 313 312 312 ARG ARG E . n 
C 1 314 LEU 314 313 313 LEU LEU E . n 
C 1 315 ALA 315 314 314 ALA ALA E . n 
C 1 316 CYS 316 315 315 CYS CYS E . n 
C 1 317 GLY 317 316 316 GLY GLY E . n 
C 1 318 VAL 318 317 317 VAL VAL E . n 
C 1 319 ILE 319 318 318 ILE ILE E . n 
C 1 320 GLY 320 319 319 GLY GLY E . n 
C 1 321 ILE 321 320 320 ILE ILE E . n 
C 1 322 ALA 322 321 321 ALA ALA E . n 
C 1 323 GLN 323 322 322 GLN GLN E . n 
D 1 1   MET 1   0   ?   ?   ?   G . n 
D 1 2   ALA 2   1   1   ALA ALA G . n 
D 1 3   THR 3   2   2   THR THR G . n 
D 1 4   LYS 4   3   3   LYS LYS G . n 
D 1 5   ALA 5   4   4   ALA ALA G . n 
D 1 6   VAL 6   5   5   VAL VAL G . n 
D 1 7   CYS 7   6   6   CYS CYS G . n 
D 1 8   VAL 8   7   7   VAL VAL G . n 
D 1 9   LEU 9   8   8   LEU LEU G . n 
D 1 10  LYS 10  9   9   LYS LYS G . n 
D 1 11  GLY 11  10  10  GLY GLY G . n 
D 1 12  ASP 12  11  11  ASP ASP G . n 
D 1 13  GLY 13  12  12  GLY GLY G . n 
D 1 14  PRO 14  13  13  PRO PRO G . n 
D 1 15  VAL 15  14  14  VAL VAL G . n 
D 1 16  GLN 16  15  15  GLN GLN G . n 
D 1 17  GLY 17  16  16  GLY GLY G . n 
D 1 18  ILE 18  17  17  ILE ILE G . n 
D 1 19  ILE 19  18  18  ILE ILE G . n 
D 1 20  ASN 20  19  19  ASN ASN G . n 
D 1 21  PHE 21  20  20  PHE PHE G . n 
D 1 22  GLU 22  21  21  GLU GLU G . n 
D 1 23  GLN 23  22  22  GLN GLN G . n 
D 1 24  LYS 24  23  23  LYS LYS G . n 
D 1 25  GLU 25  24  24  GLU GLU G . n 
D 1 26  SER 26  25  25  SER SER G . n 
D 1 27  ASN 27  26  26  ASN ASN G . n 
D 1 28  GLY 28  27  27  GLY GLY G . n 
D 1 29  PRO 29  28  28  PRO PRO G . n 
D 1 30  VAL 30  29  29  VAL VAL G . n 
D 1 31  LYS 31  30  30  LYS LYS G . n 
D 1 32  VAL 32  31  31  VAL VAL G . n 
D 1 33  TRP 33  32  32  TRP TRP G . n 
D 1 34  GLY 34  33  33  GLY GLY G . n 
D 1 35  SER 35  34  34  SER SER G . n 
D 1 36  ILE 36  35  35  ILE ILE G . n 
D 1 37  LYS 37  36  36  LYS LYS G . n 
D 1 38  GLY 38  37  37  GLY GLY G . n 
D 1 39  LEU 39  38  38  LEU LEU G . n 
D 1 40  THR 40  39  39  THR THR G . n 
D 1 41  GLU 41  40  40  GLU GLU G . n 
D 1 42  GLY 42  41  41  GLY GLY G . n 
D 1 43  LEU 43  42  42  LEU LEU G . n 
D 1 44  HIS 44  43  43  HIS HIS G . n 
D 1 45  GLY 45  44  44  GLY GLY G . n 
D 1 46  PHE 46  45  45  PHE PHE G . n 
D 1 47  HIS 47  46  46  HIS HIS G . n 
D 1 48  VAL 48  47  47  VAL VAL G . n 
D 1 49  HIS 49  48  48  HIS HIS G . n 
D 1 50  GLU 50  49  49  GLU GLU G . n 
D 1 51  PHE 51  50  50  PHE PHE G . n 
D 1 52  GLY 52  51  51  GLY GLY G . n 
D 1 53  ASP 53  52  52  ASP ASP G . n 
D 1 54  ASN 54  53  53  ASN ASN G . n 
D 1 55  THR 55  54  54  THR THR G . n 
D 1 56  ALA 56  55  55  ALA ALA G . n 
D 1 57  GLY 57  56  56  GLY GLY G . n 
D 1 58  CYS 58  57  57  CYS CYS G . n 
D 1 59  THR 59  58  58  THR THR G . n 
D 1 60  SER 60  59  59  SER SER G . n 
D 1 61  ALA 61  60  60  ALA ALA G . n 
D 1 62  GLY 62  61  61  GLY GLY G . n 
D 1 63  PRO 63  62  62  PRO PRO G . n 
D 1 64  HIS 64  63  63  HIS HIS G . n 
D 1 65  PHE 65  64  64  PHE PHE G . n 
D 1 66  ASN 66  65  65  ASN ASN G . n 
D 1 67  PRO 67  66  66  PRO PRO G . n 
D 1 68  LEU 68  67  67  LEU LEU G . n 
D 1 69  SER 69  68  68  SER SER G . n 
D 1 70  ARG 70  69  69  ARG ARG G . n 
D 1 71  LYS 71  70  70  LYS LYS G . n 
D 1 72  HIS 72  71  71  HIS HIS G . n 
D 1 73  GLY 73  72  72  GLY GLY G . n 
D 1 74  GLY 74  73  73  GLY GLY G . n 
D 1 75  PRO 75  74  74  PRO PRO G . n 
D 1 76  LYS 76  75  75  LYS LYS G . n 
D 1 77  ASP 77  76  76  ASP ASP G . n 
D 1 78  GLU 78  77  77  GLU GLU G . n 
D 1 79  GLU 79  78  78  GLU GLU G . n 
D 1 80  ARG 80  79  79  ARG ARG G . n 
D 1 81  HIS 81  80  80  HIS HIS G . n 
D 1 82  VAL 82  81  81  VAL VAL G . n 
D 1 83  GLY 83  82  82  GLY GLY G . n 
D 1 84  SER 84  83  83  SER SER G . y 
D 1 84  ASP 84  83  83  ASP ASP G . y 
D 1 85  LEU 85  84  84  LEU LEU G . n 
D 1 86  GLY 86  85  85  GLY GLY G . n 
D 1 87  ASN 87  86  86  ASN ASN G . n 
D 1 88  VAL 88  87  87  VAL VAL G . n 
D 1 89  THR 89  88  88  THR THR G . n 
D 1 90  ALA 90  89  89  ALA ALA G . n 
D 1 91  ASP 91  90  90  ASP ASP G . n 
D 1 92  LYS 92  91  91  LYS LYS G . n 
D 1 93  ASP 93  92  92  ASP ASP G . n 
D 1 94  GLY 94  93  93  GLY GLY G . n 
D 1 95  VAL 95  94  94  VAL VAL G . n 
D 1 96  ALA 96  95  95  ALA ALA G . n 
D 1 97  ASP 97  96  96  ASP ASP G . n 
D 1 98  VAL 98  97  97  VAL VAL G . n 
D 1 99  SER 99  98  98  SER SER G . n 
D 1 100 ILE 100 99  99  ILE ILE G . n 
D 1 101 GLU 101 100 100 GLU GLU G . n 
D 1 102 ASP 102 101 101 ASP ASP G . n 
D 1 103 SER 103 102 102 SER SER G . n 
D 1 104 VAL 104 103 103 VAL VAL G . n 
D 1 105 ILE 105 104 104 ILE ILE G . n 
D 1 106 SER 106 105 105 SER SER G . n 
D 1 107 LEU 107 106 106 LEU LEU G . n 
D 1 108 SER 108 107 107 SER SER G . n 
D 1 109 GLY 109 108 108 GLY GLY G . n 
D 1 110 ASP 110 109 109 ASP ASP G . n 
D 1 111 HIS 111 110 110 HIS HIS G . n 
D 1 112 SER 112 111 111 SER SER G . n 
D 1 113 ILE 113 112 112 ILE ILE G . n 
D 1 114 ILE 114 113 113 ILE ILE G . n 
D 1 115 GLY 115 114 114 GLY GLY G . n 
D 1 116 ARG 116 115 115 ARG ARG G . n 
D 1 117 THR 117 116 116 THR THR G . n 
D 1 118 LEU 118 117 117 LEU LEU G . n 
D 1 119 VAL 119 118 118 VAL VAL G . n 
D 1 120 VAL 120 119 119 VAL VAL G . n 
D 1 121 HIS 121 120 120 HIS HIS G . n 
D 1 122 GLU 122 121 121 GLU GLU G . n 
D 1 123 LYS 123 122 122 LYS LYS G . n 
D 1 124 ALA 124 123 123 ALA ALA G . n 
D 1 125 ASP 125 124 124 ASP ASP G . n 
D 1 126 ASP 126 125 125 ASP ASP G . n 
D 1 127 LEU 127 126 126 LEU LEU G . n 
D 1 128 GLY 128 127 127 GLY GLY G . n 
D 1 129 LYS 129 128 128 LYS LYS G . n 
D 1 130 GLY 130 129 129 GLY GLY G . n 
D 1 131 GLY 131 130 130 GLY GLY G . n 
D 1 132 ASN 132 131 131 ASN ASN G . n 
D 1 133 GLU 133 132 132 GLU GLU G . n 
D 1 134 GLU 134 133 133 GLU GLU G . n 
D 1 135 SER 135 134 134 SER SER G . n 
D 1 136 THR 136 135 135 THR THR G . n 
D 1 137 LYS 137 136 136 LYS LYS G . n 
D 1 138 THR 138 137 137 THR THR G . n 
D 1 139 GLY 139 138 138 GLY GLY G . n 
D 1 140 ASN 140 139 139 ASN ASN G . n 
D 1 141 ALA 141 140 140 ALA ALA G . n 
D 1 142 GLY 142 141 141 GLY GLY G . n 
D 1 143 SER 143 142 142 SER SER G . n 
D 1 144 ARG 144 143 143 ARG ARG G . n 
D 1 145 LEU 145 144 144 LEU LEU G . n 
D 1 146 ALA 146 145 145 ALA ALA G . n 
D 1 147 CYS 147 146 146 CYS CYS G . n 
D 1 148 GLY 148 147 147 GLY GLY G . n 
D 1 149 VAL 149 148 148 VAL VAL G . n 
D 1 150 ILE 150 149 149 ILE ILE G . n 
D 1 151 GLY 151 150 150 GLY GLY G . n 
D 1 152 ILE 152 151 151 ILE ILE G . n 
D 1 153 ALA 153 152 152 ALA ALA G . n 
D 1 154 GLN 154 153 153 GLN GLN G . n 
D 1 155 GLY 155 154 154 GLY GLY G . n 
D 1 156 ALA 156 155 155 ALA ALA G . n 
D 1 157 ALA 157 156 156 ALA ALA G . n 
D 1 158 ALA 158 157 ?   ?   ?   G . n 
D 1 159 SER 159 158 ?   ?   ?   G . n 
D 1 160 GLY 160 159 ?   ?   ?   G . n 
D 1 161 GLY 161 160 ?   ?   ?   G . n 
D 1 162 GLY 162 161 ?   ?   ?   G . n 
D 1 163 GLY 163 162 ?   ?   ?   G . n 
D 1 164 GLY 164 163 ?   ?   ?   G . n 
D 1 165 SER 165 164 ?   ?   ?   G . n 
D 1 166 GLY 166 165 ?   ?   ?   G . n 
D 1 167 GLY 167 166 166 GLY GLY G . n 
D 1 168 GLY 168 167 167 GLY GLY G . n 
D 1 169 GLY 169 168 168 GLY GLY G . n 
D 1 170 SER 170 169 169 SER SER G . n 
D 1 171 ALA 171 170 170 ALA ALA G . n 
D 1 172 THR 172 171 171 THR THR G . n 
D 1 173 LYS 173 172 172 LYS LYS G . n 
D 1 174 ALA 174 173 173 ALA ALA G . n 
D 1 175 VAL 175 174 174 VAL VAL G . n 
D 1 176 CYS 176 175 175 CYS CYS G . n 
D 1 177 VAL 177 176 176 VAL VAL G . n 
D 1 178 LEU 178 177 177 LEU LEU G . n 
D 1 179 LYS 179 178 178 LYS LYS G . n 
D 1 180 GLY 180 179 179 GLY GLY G . n 
D 1 181 ASP 181 180 180 ASP ASP G . n 
D 1 182 GLY 182 181 181 GLY GLY G . n 
D 1 183 PRO 183 182 182 PRO PRO G . n 
D 1 184 VAL 184 183 183 VAL VAL G . n 
D 1 185 GLN 185 184 184 GLN GLN G . n 
D 1 186 GLY 186 185 185 GLY GLY G . n 
D 1 187 ILE 187 186 186 ILE ILE G . n 
D 1 188 ILE 188 187 187 ILE ILE G . n 
D 1 189 ASN 189 188 188 ASN ASN G . n 
D 1 190 PHE 190 189 189 PHE PHE G . n 
D 1 191 GLU 191 190 190 GLU GLU G . n 
D 1 192 GLN 192 191 191 GLN GLN G . n 
D 1 193 LYS 193 192 192 LYS LYS G . n 
D 1 194 GLU 194 193 193 GLU GLU G . n 
D 1 195 SER 195 194 194 SER SER G . n 
D 1 196 ASN 196 195 195 ASN ASN G . n 
D 1 197 GLY 197 196 196 GLY GLY G . n 
D 1 198 PRO 198 197 197 PRO PRO G . n 
D 1 199 VAL 199 198 198 VAL VAL G . n 
D 1 200 LYS 200 199 199 LYS LYS G . n 
D 1 201 VAL 201 200 200 VAL VAL G . n 
D 1 202 TRP 202 201 201 TRP TRP G . n 
D 1 203 GLY 203 202 202 GLY GLY G . n 
D 1 204 SER 204 203 203 SER SER G . n 
D 1 205 ILE 205 204 204 ILE ILE G . n 
D 1 206 LYS 206 205 205 LYS LYS G . n 
D 1 207 GLY 207 206 206 GLY GLY G . n 
D 1 208 LEU 208 207 207 LEU LEU G . n 
D 1 209 THR 209 208 208 THR THR G . n 
D 1 210 GLU 210 209 209 GLU GLU G . n 
D 1 211 GLY 211 210 210 GLY GLY G . n 
D 1 212 LEU 212 211 211 LEU LEU G . n 
D 1 213 HIS 213 212 212 HIS HIS G . n 
D 1 214 GLY 214 213 213 GLY GLY G . n 
D 1 215 PHE 215 214 214 PHE PHE G . n 
D 1 216 HIS 216 215 215 HIS HIS G . n 
D 1 217 VAL 217 216 216 VAL VAL G . n 
D 1 218 HIS 218 217 217 HIS HIS G . n 
D 1 219 GLU 219 218 218 GLU GLU G . n 
D 1 220 PHE 220 219 219 PHE PHE G . n 
D 1 221 GLY 221 220 220 GLY GLY G . n 
D 1 222 ASP 222 221 221 ASP ASP G . n 
D 1 223 ASN 223 222 222 ASN ASN G . n 
D 1 224 THR 224 223 223 THR THR G . n 
D 1 225 ALA 225 224 224 ALA ALA G . n 
D 1 226 GLY 226 225 225 GLY GLY G . n 
D 1 227 CYS 227 226 226 CYS CYS G . n 
D 1 228 THR 228 227 227 THR THR G . n 
D 1 229 SER 229 228 228 SER SER G . n 
D 1 230 ALA 230 229 229 ALA ALA G . n 
D 1 231 GLY 231 230 230 GLY GLY G . n 
D 1 232 PRO 232 231 231 PRO PRO G . n 
D 1 233 HIS 233 232 232 HIS HIS G . n 
D 1 234 PHE 234 233 233 PHE PHE G . n 
D 1 235 ASN 235 234 234 ASN ASN G . n 
D 1 236 PRO 236 235 235 PRO PRO G . n 
D 1 237 LEU 237 236 236 LEU LEU G . n 
D 1 238 SER 238 237 237 SER SER G . n 
D 1 239 ARG 239 238 238 ARG ARG G . n 
D 1 240 LYS 240 239 239 LYS LYS G . n 
D 1 241 HIS 241 240 240 HIS HIS G . n 
D 1 242 GLY 242 241 241 GLY GLY G . n 
D 1 243 GLY 243 242 242 GLY GLY G . n 
D 1 244 PRO 244 243 243 PRO PRO G . n 
D 1 245 LYS 245 244 244 LYS LYS G . n 
D 1 246 ASP 246 245 245 ASP ASP G . n 
D 1 247 GLU 247 246 246 GLU GLU G . n 
D 1 248 GLU 248 247 247 GLU GLU G . n 
D 1 249 ARG 249 248 248 ARG ARG G . n 
D 1 250 HIS 250 249 249 HIS HIS G . n 
D 1 251 VAL 251 250 250 VAL VAL G . n 
D 1 252 GLY 252 251 251 GLY GLY G . n 
D 1 253 SER 253 252 252 SER SER G . y 
D 1 253 ASP 253 252 252 ASP ASP G . y 
D 1 254 LEU 254 253 253 LEU LEU G . n 
D 1 255 GLY 255 254 254 GLY GLY G . n 
D 1 256 ASN 256 255 255 ASN ASN G . n 
D 1 257 VAL 257 256 256 VAL VAL G . n 
D 1 258 THR 258 257 257 THR THR G . n 
D 1 259 ALA 259 258 258 ALA ALA G . n 
D 1 260 ASP 260 259 259 ASP ASP G . n 
D 1 261 LYS 261 260 260 LYS LYS G . n 
D 1 262 ASP 262 261 261 ASP ASP G . n 
D 1 263 GLY 263 262 262 GLY GLY G . n 
D 1 264 VAL 264 263 263 VAL VAL G . n 
D 1 265 ALA 265 264 264 ALA ALA G . n 
D 1 266 ASP 266 265 265 ASP ASP G . n 
D 1 267 VAL 267 266 266 VAL VAL G . n 
D 1 268 SER 268 267 267 SER SER G . n 
D 1 269 ILE 269 268 268 ILE ILE G . n 
D 1 270 GLU 270 269 269 GLU GLU G . n 
D 1 271 ASP 271 270 270 ASP ASP G . n 
D 1 272 SER 272 271 271 SER SER G . n 
D 1 273 VAL 273 272 272 VAL VAL G . n 
D 1 274 ILE 274 273 273 ILE ILE G . n 
D 1 275 SER 275 274 274 SER SER G . n 
D 1 276 LEU 276 275 275 LEU LEU G . n 
D 1 277 SER 277 276 276 SER SER G . n 
D 1 278 GLY 278 277 277 GLY GLY G . n 
D 1 279 ASP 279 278 278 ASP ASP G . n 
D 1 280 HIS 280 279 279 HIS HIS G . n 
D 1 281 SER 281 280 280 SER SER G . n 
D 1 282 ILE 282 281 281 ILE ILE G . n 
D 1 283 ILE 283 282 282 ILE ILE G . n 
D 1 284 GLY 284 283 283 GLY GLY G . n 
D 1 285 ARG 285 284 284 ARG ARG G . n 
D 1 286 THR 286 285 285 THR THR G . n 
D 1 287 LEU 287 286 286 LEU LEU G . n 
D 1 288 VAL 288 287 287 VAL VAL G . n 
D 1 289 VAL 289 288 288 VAL VAL G . n 
D 1 290 HIS 290 289 289 HIS HIS G . n 
D 1 291 GLU 291 290 290 GLU GLU G . n 
D 1 292 LYS 292 291 291 LYS LYS G . n 
D 1 293 ALA 293 292 292 ALA ALA G . n 
D 1 294 ASP 294 293 293 ASP ASP G . n 
D 1 295 ASP 295 294 294 ASP ASP G . n 
D 1 296 LEU 296 295 295 LEU LEU G . n 
D 1 297 GLY 297 296 296 GLY GLY G . n 
D 1 298 LYS 298 297 297 LYS LYS G . n 
D 1 299 GLY 299 298 298 GLY GLY G . n 
D 1 300 GLY 300 299 299 GLY GLY G . n 
D 1 301 ASN 301 300 300 ASN ASN G . n 
D 1 302 GLU 302 301 301 GLU GLU G . n 
D 1 303 GLU 303 302 302 GLU GLU G . n 
D 1 304 SER 304 303 303 SER SER G . n 
D 1 305 THR 305 304 304 THR THR G . n 
D 1 306 LYS 306 305 305 LYS LYS G . n 
D 1 307 THR 307 306 306 THR THR G . n 
D 1 308 GLY 308 307 307 GLY GLY G . n 
D 1 309 ASN 309 308 308 ASN ASN G . n 
D 1 310 ALA 310 309 309 ALA ALA G . n 
D 1 311 GLY 311 310 310 GLY GLY G . n 
D 1 312 SER 312 311 311 SER SER G . n 
D 1 313 ARG 313 312 312 ARG ARG G . n 
D 1 314 LEU 314 313 313 LEU LEU G . n 
D 1 315 ALA 315 314 314 ALA ALA G . n 
D 1 316 CYS 316 315 315 CYS CYS G . n 
D 1 317 GLY 317 316 316 GLY GLY G . n 
D 1 318 VAL 318 317 317 VAL VAL G . n 
D 1 319 ILE 319 318 318 ILE ILE G . n 
D 1 320 GLY 320 319 319 GLY GLY G . n 
D 1 321 ILE 321 320 320 ILE ILE G . n 
D 1 322 ALA 322 321 321 ALA ALA G . n 
D 1 323 GLN 323 322 322 GLN GLN G . n 
E 1 1   MET 1   0   ?   ?   ?   I . n 
E 1 2   ALA 2   1   1   ALA ALA I . n 
E 1 3   THR 3   2   2   THR THR I . n 
E 1 4   LYS 4   3   3   LYS LYS I . n 
E 1 5   ALA 5   4   4   ALA ALA I . n 
E 1 6   VAL 6   5   5   VAL VAL I . n 
E 1 7   CYS 7   6   6   CYS CYS I . n 
E 1 8   VAL 8   7   7   VAL VAL I . n 
E 1 9   LEU 9   8   8   LEU LEU I . n 
E 1 10  LYS 10  9   9   LYS LYS I . n 
E 1 11  GLY 11  10  10  GLY GLY I . n 
E 1 12  ASP 12  11  11  ASP ASP I . n 
E 1 13  GLY 13  12  12  GLY GLY I . n 
E 1 14  PRO 14  13  13  PRO PRO I . n 
E 1 15  VAL 15  14  14  VAL VAL I . n 
E 1 16  GLN 16  15  15  GLN GLN I . n 
E 1 17  GLY 17  16  16  GLY GLY I . n 
E 1 18  ILE 18  17  17  ILE ILE I . n 
E 1 19  ILE 19  18  18  ILE ILE I . n 
E 1 20  ASN 20  19  19  ASN ASN I . n 
E 1 21  PHE 21  20  20  PHE PHE I . n 
E 1 22  GLU 22  21  21  GLU GLU I . n 
E 1 23  GLN 23  22  22  GLN GLN I . n 
E 1 24  LYS 24  23  23  LYS LYS I . n 
E 1 25  GLU 25  24  24  GLU GLU I . n 
E 1 26  SER 26  25  25  SER SER I . n 
E 1 27  ASN 27  26  26  ASN ASN I . n 
E 1 28  GLY 28  27  27  GLY GLY I . n 
E 1 29  PRO 29  28  28  PRO PRO I . n 
E 1 30  VAL 30  29  29  VAL VAL I . n 
E 1 31  LYS 31  30  30  LYS LYS I . n 
E 1 32  VAL 32  31  31  VAL VAL I . n 
E 1 33  TRP 33  32  32  TRP TRP I . n 
E 1 34  GLY 34  33  33  GLY GLY I . n 
E 1 35  SER 35  34  34  SER SER I . n 
E 1 36  ILE 36  35  35  ILE ILE I . n 
E 1 37  LYS 37  36  36  LYS LYS I . n 
E 1 38  GLY 38  37  37  GLY GLY I . n 
E 1 39  LEU 39  38  38  LEU LEU I . n 
E 1 40  THR 40  39  39  THR THR I . n 
E 1 41  GLU 41  40  40  GLU GLU I . n 
E 1 42  GLY 42  41  41  GLY GLY I . n 
E 1 43  LEU 43  42  42  LEU LEU I . n 
E 1 44  HIS 44  43  43  HIS HIS I . n 
E 1 45  GLY 45  44  44  GLY GLY I . n 
E 1 46  PHE 46  45  45  PHE PHE I . n 
E 1 47  HIS 47  46  46  HIS HIS I . n 
E 1 48  VAL 48  47  47  VAL VAL I . n 
E 1 49  HIS 49  48  48  HIS HIS I . n 
E 1 50  GLU 50  49  49  GLU GLU I . n 
E 1 51  PHE 51  50  50  PHE PHE I . n 
E 1 52  GLY 52  51  51  GLY GLY I . n 
E 1 53  ASP 53  52  52  ASP ASP I . n 
E 1 54  ASN 54  53  53  ASN ASN I . n 
E 1 55  THR 55  54  54  THR THR I . n 
E 1 56  ALA 56  55  55  ALA ALA I . n 
E 1 57  GLY 57  56  56  GLY GLY I . n 
E 1 58  CYS 58  57  57  CYS CYS I . n 
E 1 59  THR 59  58  58  THR THR I . n 
E 1 60  SER 60  59  59  SER SER I . n 
E 1 61  ALA 61  60  60  ALA ALA I . n 
E 1 62  GLY 62  61  61  GLY GLY I . n 
E 1 63  PRO 63  62  62  PRO PRO I . n 
E 1 64  HIS 64  63  63  HIS HIS I . n 
E 1 65  PHE 65  64  64  PHE PHE I . n 
E 1 66  ASN 66  65  65  ASN ASN I . n 
E 1 67  PRO 67  66  66  PRO PRO I . n 
E 1 68  LEU 68  67  67  LEU LEU I . n 
E 1 69  SER 69  68  68  SER SER I . n 
E 1 70  ARG 70  69  69  ARG ARG I . n 
E 1 71  LYS 71  70  70  LYS LYS I . n 
E 1 72  HIS 72  71  71  HIS HIS I . n 
E 1 73  GLY 73  72  72  GLY GLY I . n 
E 1 74  GLY 74  73  73  GLY GLY I . n 
E 1 75  PRO 75  74  74  PRO PRO I . n 
E 1 76  LYS 76  75  75  LYS LYS I . n 
E 1 77  ASP 77  76  76  ASP ASP I . n 
E 1 78  GLU 78  77  77  GLU GLU I . n 
E 1 79  GLU 79  78  78  GLU GLU I . n 
E 1 80  ARG 80  79  79  ARG ARG I . n 
E 1 81  HIS 81  80  80  HIS HIS I . n 
E 1 82  VAL 82  81  81  VAL VAL I . n 
E 1 83  GLY 83  82  82  GLY GLY I . n 
E 1 84  SER 84  83  83  SER SER I . y 
E 1 84  ASP 84  83  83  ASP ASP I . y 
E 1 85  LEU 85  84  84  LEU LEU I . n 
E 1 86  GLY 86  85  85  GLY GLY I . n 
E 1 87  ASN 87  86  86  ASN ASN I . n 
E 1 88  VAL 88  87  87  VAL VAL I . n 
E 1 89  THR 89  88  88  THR THR I . n 
E 1 90  ALA 90  89  89  ALA ALA I . n 
E 1 91  ASP 91  90  90  ASP ASP I . n 
E 1 92  LYS 92  91  91  LYS LYS I . n 
E 1 93  ASP 93  92  92  ASP ASP I . n 
E 1 94  GLY 94  93  93  GLY GLY I . n 
E 1 95  VAL 95  94  94  VAL VAL I . n 
E 1 96  ALA 96  95  95  ALA ALA I . n 
E 1 97  ASP 97  96  96  ASP ASP I . n 
E 1 98  VAL 98  97  97  VAL VAL I . n 
E 1 99  SER 99  98  98  SER SER I . n 
E 1 100 ILE 100 99  99  ILE ILE I . n 
E 1 101 GLU 101 100 100 GLU GLU I . n 
E 1 102 ASP 102 101 101 ASP ASP I . n 
E 1 103 SER 103 102 102 SER SER I . n 
E 1 104 VAL 104 103 103 VAL VAL I . n 
E 1 105 ILE 105 104 104 ILE ILE I . n 
E 1 106 SER 106 105 105 SER SER I . n 
E 1 107 LEU 107 106 106 LEU LEU I . n 
E 1 108 SER 108 107 107 SER SER I . n 
E 1 109 GLY 109 108 108 GLY GLY I . n 
E 1 110 ASP 110 109 109 ASP ASP I . n 
E 1 111 HIS 111 110 110 HIS HIS I . n 
E 1 112 SER 112 111 111 SER SER I . n 
E 1 113 ILE 113 112 112 ILE ILE I . n 
E 1 114 ILE 114 113 113 ILE ILE I . n 
E 1 115 GLY 115 114 114 GLY GLY I . n 
E 1 116 ARG 116 115 115 ARG ARG I . n 
E 1 117 THR 117 116 116 THR THR I . n 
E 1 118 LEU 118 117 117 LEU LEU I . n 
E 1 119 VAL 119 118 118 VAL VAL I . n 
E 1 120 VAL 120 119 119 VAL VAL I . n 
E 1 121 HIS 121 120 120 HIS HIS I . n 
E 1 122 GLU 122 121 121 GLU GLU I . n 
E 1 123 LYS 123 122 122 LYS LYS I . n 
E 1 124 ALA 124 123 123 ALA ALA I . n 
E 1 125 ASP 125 124 124 ASP ASP I . n 
E 1 126 ASP 126 125 125 ASP ASP I . n 
E 1 127 LEU 127 126 126 LEU LEU I . n 
E 1 128 GLY 128 127 127 GLY GLY I . n 
E 1 129 LYS 129 128 128 LYS LYS I . n 
E 1 130 GLY 130 129 129 GLY GLY I . n 
E 1 131 GLY 131 130 130 GLY GLY I . n 
E 1 132 ASN 132 131 131 ASN ASN I . n 
E 1 133 GLU 133 132 132 GLU GLU I . n 
E 1 134 GLU 134 133 133 GLU GLU I . n 
E 1 135 SER 135 134 134 SER SER I . n 
E 1 136 THR 136 135 135 THR THR I . n 
E 1 137 LYS 137 136 136 LYS LYS I . n 
E 1 138 THR 138 137 137 THR THR I . n 
E 1 139 GLY 139 138 138 GLY GLY I . n 
E 1 140 ASN 140 139 139 ASN ASN I . n 
E 1 141 ALA 141 140 140 ALA ALA I . n 
E 1 142 GLY 142 141 141 GLY GLY I . n 
E 1 143 SER 143 142 142 SER SER I . n 
E 1 144 ARG 144 143 143 ARG ARG I . n 
E 1 145 LEU 145 144 144 LEU LEU I . n 
E 1 146 ALA 146 145 145 ALA ALA I . n 
E 1 147 CYS 147 146 146 CYS CYS I . n 
E 1 148 GLY 148 147 147 GLY GLY I . n 
E 1 149 VAL 149 148 148 VAL VAL I . n 
E 1 150 ILE 150 149 149 ILE ILE I . n 
E 1 151 GLY 151 150 150 GLY GLY I . n 
E 1 152 ILE 152 151 151 ILE ILE I . n 
E 1 153 ALA 153 152 152 ALA ALA I . n 
E 1 154 GLN 154 153 153 GLN GLN I . n 
E 1 155 GLY 155 154 154 GLY GLY I . n 
E 1 156 ALA 156 155 155 ALA ALA I . n 
E 1 157 ALA 157 156 156 ALA ALA I . n 
E 1 158 ALA 158 157 ?   ?   ?   I . n 
E 1 159 SER 159 158 ?   ?   ?   I . n 
E 1 160 GLY 160 159 ?   ?   ?   I . n 
E 1 161 GLY 161 160 ?   ?   ?   I . n 
E 1 162 GLY 162 161 ?   ?   ?   I . n 
E 1 163 GLY 163 162 ?   ?   ?   I . n 
E 1 164 GLY 164 163 ?   ?   ?   I . n 
E 1 165 SER 165 164 ?   ?   ?   I . n 
E 1 166 GLY 166 165 ?   ?   ?   I . n 
E 1 167 GLY 167 166 166 GLY GLY I . n 
E 1 168 GLY 168 167 167 GLY GLY I . n 
E 1 169 GLY 169 168 168 GLY GLY I . n 
E 1 170 SER 170 169 169 SER SER I . n 
E 1 171 ALA 171 170 170 ALA ALA I . n 
E 1 172 THR 172 171 171 THR THR I . n 
E 1 173 LYS 173 172 172 LYS LYS I . n 
E 1 174 ALA 174 173 173 ALA ALA I . n 
E 1 175 VAL 175 174 174 VAL VAL I . n 
E 1 176 CYS 176 175 175 CYS CYS I . n 
E 1 177 VAL 177 176 176 VAL VAL I . n 
E 1 178 LEU 178 177 177 LEU LEU I . n 
E 1 179 LYS 179 178 178 LYS LYS I . n 
E 1 180 GLY 180 179 179 GLY GLY I . n 
E 1 181 ASP 181 180 180 ASP ASP I . n 
E 1 182 GLY 182 181 181 GLY GLY I . n 
E 1 183 PRO 183 182 182 PRO PRO I . n 
E 1 184 VAL 184 183 183 VAL VAL I . n 
E 1 185 GLN 185 184 184 GLN GLN I . n 
E 1 186 GLY 186 185 185 GLY GLY I . n 
E 1 187 ILE 187 186 186 ILE ILE I . n 
E 1 188 ILE 188 187 187 ILE ILE I . n 
E 1 189 ASN 189 188 188 ASN ASN I . n 
E 1 190 PHE 190 189 189 PHE PHE I . n 
E 1 191 GLU 191 190 190 GLU GLU I . n 
E 1 192 GLN 192 191 191 GLN GLN I . n 
E 1 193 LYS 193 192 192 LYS LYS I . n 
E 1 194 GLU 194 193 193 GLU GLU I . n 
E 1 195 SER 195 194 194 SER SER I . n 
E 1 196 ASN 196 195 195 ASN ASN I . n 
E 1 197 GLY 197 196 196 GLY GLY I . n 
E 1 198 PRO 198 197 197 PRO PRO I . n 
E 1 199 VAL 199 198 198 VAL VAL I . n 
E 1 200 LYS 200 199 199 LYS LYS I . n 
E 1 201 VAL 201 200 200 VAL VAL I . n 
E 1 202 TRP 202 201 201 TRP TRP I . n 
E 1 203 GLY 203 202 202 GLY GLY I . n 
E 1 204 SER 204 203 203 SER SER I . n 
E 1 205 ILE 205 204 204 ILE ILE I . n 
E 1 206 LYS 206 205 205 LYS LYS I . n 
E 1 207 GLY 207 206 206 GLY GLY I . n 
E 1 208 LEU 208 207 207 LEU LEU I . n 
E 1 209 THR 209 208 208 THR THR I . n 
E 1 210 GLU 210 209 209 GLU GLU I . n 
E 1 211 GLY 211 210 210 GLY GLY I . n 
E 1 212 LEU 212 211 211 LEU LEU I . n 
E 1 213 HIS 213 212 212 HIS HIS I . n 
E 1 214 GLY 214 213 213 GLY GLY I . n 
E 1 215 PHE 215 214 214 PHE PHE I . n 
E 1 216 HIS 216 215 215 HIS HIS I . n 
E 1 217 VAL 217 216 216 VAL VAL I . n 
E 1 218 HIS 218 217 217 HIS HIS I . n 
E 1 219 GLU 219 218 218 GLU GLU I . n 
E 1 220 PHE 220 219 219 PHE PHE I . n 
E 1 221 GLY 221 220 220 GLY GLY I . n 
E 1 222 ASP 222 221 221 ASP ASP I . n 
E 1 223 ASN 223 222 222 ASN ASN I . n 
E 1 224 THR 224 223 223 THR THR I . n 
E 1 225 ALA 225 224 224 ALA ALA I . n 
E 1 226 GLY 226 225 225 GLY GLY I . n 
E 1 227 CYS 227 226 226 CYS CYS I . n 
E 1 228 THR 228 227 227 THR THR I . n 
E 1 229 SER 229 228 228 SER SER I . n 
E 1 230 ALA 230 229 229 ALA ALA I . n 
E 1 231 GLY 231 230 230 GLY GLY I . n 
E 1 232 PRO 232 231 231 PRO PRO I . n 
E 1 233 HIS 233 232 232 HIS HIS I . n 
E 1 234 PHE 234 233 233 PHE PHE I . n 
E 1 235 ASN 235 234 234 ASN ASN I . n 
E 1 236 PRO 236 235 235 PRO PRO I . n 
E 1 237 LEU 237 236 236 LEU LEU I . n 
E 1 238 SER 238 237 237 SER SER I . n 
E 1 239 ARG 239 238 238 ARG ARG I . n 
E 1 240 LYS 240 239 239 LYS LYS I . n 
E 1 241 HIS 241 240 240 HIS HIS I . n 
E 1 242 GLY 242 241 241 GLY GLY I . n 
E 1 243 GLY 243 242 242 GLY GLY I . n 
E 1 244 PRO 244 243 243 PRO PRO I . n 
E 1 245 LYS 245 244 244 LYS LYS I . n 
E 1 246 ASP 246 245 245 ASP ASP I . n 
E 1 247 GLU 247 246 246 GLU GLU I . n 
E 1 248 GLU 248 247 247 GLU GLU I . n 
E 1 249 ARG 249 248 248 ARG ARG I . n 
E 1 250 HIS 250 249 249 HIS HIS I . n 
E 1 251 VAL 251 250 250 VAL VAL I . n 
E 1 252 GLY 252 251 251 GLY GLY I . n 
E 1 253 SER 253 252 252 SER SER I . y 
E 1 253 ASP 253 252 252 ASP ASP I . y 
E 1 254 LEU 254 253 253 LEU LEU I . n 
E 1 255 GLY 255 254 254 GLY GLY I . n 
E 1 256 ASN 256 255 255 ASN ASN I . n 
E 1 257 VAL 257 256 256 VAL VAL I . n 
E 1 258 THR 258 257 257 THR THR I . n 
E 1 259 ALA 259 258 258 ALA ALA I . n 
E 1 260 ASP 260 259 259 ASP ASP I . n 
E 1 261 LYS 261 260 260 LYS LYS I . n 
E 1 262 ASP 262 261 261 ASP ASP I . n 
E 1 263 GLY 263 262 262 GLY GLY I . n 
E 1 264 VAL 264 263 263 VAL VAL I . n 
E 1 265 ALA 265 264 264 ALA ALA I . n 
E 1 266 ASP 266 265 265 ASP ASP I . n 
E 1 267 VAL 267 266 266 VAL VAL I . n 
E 1 268 SER 268 267 267 SER SER I . n 
E 1 269 ILE 269 268 268 ILE ILE I . n 
E 1 270 GLU 270 269 269 GLU GLU I . n 
E 1 271 ASP 271 270 270 ASP ASP I . n 
E 1 272 SER 272 271 271 SER SER I . n 
E 1 273 VAL 273 272 272 VAL VAL I . n 
E 1 274 ILE 274 273 273 ILE ILE I . n 
E 1 275 SER 275 274 274 SER SER I . n 
E 1 276 LEU 276 275 275 LEU LEU I . n 
E 1 277 SER 277 276 276 SER SER I . n 
E 1 278 GLY 278 277 277 GLY GLY I . n 
E 1 279 ASP 279 278 278 ASP ASP I . n 
E 1 280 HIS 280 279 279 HIS HIS I . n 
E 1 281 SER 281 280 280 SER SER I . n 
E 1 282 ILE 282 281 281 ILE ILE I . n 
E 1 283 ILE 283 282 282 ILE ILE I . n 
E 1 284 GLY 284 283 283 GLY GLY I . n 
E 1 285 ARG 285 284 284 ARG ARG I . n 
E 1 286 THR 286 285 285 THR THR I . n 
E 1 287 LEU 287 286 286 LEU LEU I . n 
E 1 288 VAL 288 287 287 VAL VAL I . n 
E 1 289 VAL 289 288 288 VAL VAL I . n 
E 1 290 HIS 290 289 289 HIS HIS I . n 
E 1 291 GLU 291 290 290 GLU GLU I . n 
E 1 292 LYS 292 291 291 LYS LYS I . n 
E 1 293 ALA 293 292 292 ALA ALA I . n 
E 1 294 ASP 294 293 293 ASP ASP I . n 
E 1 295 ASP 295 294 294 ASP ASP I . n 
E 1 296 LEU 296 295 295 LEU LEU I . n 
E 1 297 GLY 297 296 296 GLY GLY I . n 
E 1 298 LYS 298 297 297 LYS LYS I . n 
E 1 299 GLY 299 298 298 GLY GLY I . n 
E 1 300 GLY 300 299 299 GLY GLY I . n 
E 1 301 ASN 301 300 300 ASN ASN I . n 
E 1 302 GLU 302 301 301 GLU GLU I . n 
E 1 303 GLU 303 302 302 GLU GLU I . n 
E 1 304 SER 304 303 303 SER SER I . n 
E 1 305 THR 305 304 304 THR THR I . n 
E 1 306 LYS 306 305 305 LYS LYS I . n 
E 1 307 THR 307 306 306 THR THR I . n 
E 1 308 GLY 308 307 307 GLY GLY I . n 
E 1 309 ASN 309 308 308 ASN ASN I . n 
E 1 310 ALA 310 309 309 ALA ALA I . n 
E 1 311 GLY 311 310 310 GLY GLY I . n 
E 1 312 SER 312 311 311 SER SER I . n 
E 1 313 ARG 313 312 312 ARG ARG I . n 
E 1 314 LEU 314 313 313 LEU LEU I . n 
E 1 315 ALA 315 314 314 ALA ALA I . n 
E 1 316 CYS 316 315 315 CYS CYS I . n 
E 1 317 GLY 317 316 316 GLY GLY I . n 
E 1 318 VAL 318 317 317 VAL VAL I . n 
E 1 319 ILE 319 318 318 ILE ILE I . n 
E 1 320 GLY 320 319 319 GLY GLY I . n 
E 1 321 ILE 321 320 320 ILE ILE I . n 
E 1 322 ALA 322 321 321 ALA ALA I . n 
E 1 323 GLN 323 322 322 GLN GLN I . n 
# 
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 
F  2 ZN  1   401 401 ZN  ZN  A . 
G  3 CU  1   402 402 CU  CU  A . 
H  2 ZN  1   403 403 ZN  ZN  A . 
I  3 CU  1   404 404 CU  CU  A . 
J  2 ZN  1   401 401 ZN  ZN  C . 
K  3 CU  1   402 402 CU  CU  C . 
L  2 ZN  1   403 403 ZN  ZN  C . 
M  3 CU  1   404 404 CU  CU  C . 
N  2 ZN  1   401 401 ZN  ZN  E . 
O  3 CU  1   402 402 CU  CU  E . 
P  2 ZN  1   403 403 ZN  ZN  E . 
Q  3 CU  1   404 404 CU  CU  E . 
R  4 MLI 1   405 405 MLI MLI E . 
S  2 ZN  1   401 401 ZN  ZN  G . 
T  3 CU  1   402 402 CU  CU  G . 
U  2 ZN  1   403 403 ZN  ZN  G . 
V  3 CU  1   404 404 CU  CU  G . 
W  2 ZN  1   401 401 ZN  ZN  I . 
X  3 CU  1   402 402 CU  CU  I . 
Y  2 ZN  1   403 403 ZN  ZN  I . 
Z  3 CU  1   404 404 CU  CU  I . 
AA 5 HOH 1   501 501 HOH HOH A . 
AA 5 HOH 2   502 502 HOH HOH A . 
AA 5 HOH 3   503 503 HOH HOH A . 
AA 5 HOH 4   504 504 HOH HOH A . 
AA 5 HOH 5   505 505 HOH HOH A . 
AA 5 HOH 6   506 506 HOH HOH A . 
AA 5 HOH 7   507 507 HOH HOH A . 
AA 5 HOH 8   508 508 HOH HOH A . 
AA 5 HOH 9   509 509 HOH HOH A . 
AA 5 HOH 10  510 510 HOH HOH A . 
AA 5 HOH 11  511 511 HOH HOH A . 
AA 5 HOH 12  512 512 HOH HOH A . 
AA 5 HOH 13  513 513 HOH HOH A . 
AA 5 HOH 14  514 514 HOH HOH A . 
AA 5 HOH 15  515 515 HOH HOH A . 
AA 5 HOH 16  516 516 HOH HOH A . 
AA 5 HOH 17  517 517 HOH HOH A . 
AA 5 HOH 18  518 518 HOH HOH A . 
AA 5 HOH 19  519 519 HOH HOH A . 
AA 5 HOH 20  520 520 HOH HOH A . 
AA 5 HOH 21  521 521 HOH HOH A . 
AA 5 HOH 22  522 522 HOH HOH A . 
AA 5 HOH 23  523 523 HOH HOH A . 
AA 5 HOH 24  524 524 HOH HOH A . 
AA 5 HOH 25  525 525 HOH HOH A . 
AA 5 HOH 26  526 526 HOH HOH A . 
AA 5 HOH 27  527 527 HOH HOH A . 
AA 5 HOH 28  528 528 HOH HOH A . 
AA 5 HOH 29  529 529 HOH HOH A . 
AA 5 HOH 30  530 530 HOH HOH A . 
AA 5 HOH 31  531 531 HOH HOH A . 
AA 5 HOH 32  532 532 HOH HOH A . 
AA 5 HOH 33  533 533 HOH HOH A . 
AA 5 HOH 34  534 534 HOH HOH A . 
AA 5 HOH 35  535 535 HOH HOH A . 
AA 5 HOH 36  536 536 HOH HOH A . 
AA 5 HOH 37  537 537 HOH HOH A . 
AA 5 HOH 38  538 538 HOH HOH A . 
AA 5 HOH 39  539 539 HOH HOH A . 
AA 5 HOH 40  540 540 HOH HOH A . 
AA 5 HOH 41  541 541 HOH HOH A . 
AA 5 HOH 42  542 542 HOH HOH A . 
AA 5 HOH 43  543 543 HOH HOH A . 
AA 5 HOH 44  544 544 HOH HOH A . 
AA 5 HOH 45  545 545 HOH HOH A . 
AA 5 HOH 46  546 546 HOH HOH A . 
AA 5 HOH 47  547 547 HOH HOH A . 
AA 5 HOH 48  548 548 HOH HOH A . 
AA 5 HOH 49  549 549 HOH HOH A . 
AA 5 HOH 50  550 550 HOH HOH A . 
AA 5 HOH 51  551 551 HOH HOH A . 
AA 5 HOH 52  552 552 HOH HOH A . 
AA 5 HOH 53  553 553 HOH HOH A . 
AA 5 HOH 54  554 554 HOH HOH A . 
AA 5 HOH 55  555 555 HOH HOH A . 
AA 5 HOH 56  556 556 HOH HOH A . 
AA 5 HOH 57  557 557 HOH HOH A . 
AA 5 HOH 58  558 558 HOH HOH A . 
AA 5 HOH 59  559 559 HOH HOH A . 
AA 5 HOH 60  560 560 HOH HOH A . 
AA 5 HOH 61  561 561 HOH HOH A . 
AA 5 HOH 62  562 562 HOH HOH A . 
AA 5 HOH 63  563 563 HOH HOH A . 
AA 5 HOH 64  564 564 HOH HOH A . 
AA 5 HOH 65  565 565 HOH HOH A . 
AA 5 HOH 66  566 566 HOH HOH A . 
AA 5 HOH 67  567 567 HOH HOH A . 
AA 5 HOH 68  568 568 HOH HOH A . 
AA 5 HOH 69  569 569 HOH HOH A . 
AA 5 HOH 70  570 570 HOH HOH A . 
AA 5 HOH 71  571 571 HOH HOH A . 
AA 5 HOH 72  572 572 HOH HOH A . 
AA 5 HOH 73  573 573 HOH HOH A . 
AA 5 HOH 74  574 574 HOH HOH A . 
AA 5 HOH 75  575 575 HOH HOH A . 
AA 5 HOH 76  576 576 HOH HOH A . 
AA 5 HOH 77  577 577 HOH HOH A . 
AA 5 HOH 78  578 578 HOH HOH A . 
AA 5 HOH 79  579 579 HOH HOH A . 
AA 5 HOH 80  580 580 HOH HOH A . 
AA 5 HOH 81  581 581 HOH HOH A . 
AA 5 HOH 82  582 582 HOH HOH A . 
AA 5 HOH 83  583 583 HOH HOH A . 
AA 5 HOH 84  584 584 HOH HOH A . 
AA 5 HOH 85  585 585 HOH HOH A . 
AA 5 HOH 86  586 586 HOH HOH A . 
AA 5 HOH 87  587 587 HOH HOH A . 
AA 5 HOH 88  588 588 HOH HOH A . 
AA 5 HOH 89  589 589 HOH HOH A . 
AA 5 HOH 90  590 590 HOH HOH A . 
AA 5 HOH 91  591 591 HOH HOH A . 
AA 5 HOH 92  592 592 HOH HOH A . 
AA 5 HOH 93  593 593 HOH HOH A . 
AA 5 HOH 94  594 594 HOH HOH A . 
AA 5 HOH 95  595 595 HOH HOH A . 
AA 5 HOH 96  596 596 HOH HOH A . 
AA 5 HOH 97  597 597 HOH HOH A . 
AA 5 HOH 98  598 598 HOH HOH A . 
AA 5 HOH 99  599 599 HOH HOH A . 
AA 5 HOH 100 600 600 HOH HOH A . 
AA 5 HOH 101 601 601 HOH HOH A . 
AA 5 HOH 102 602 602 HOH HOH A . 
AA 5 HOH 103 603 603 HOH HOH A . 
AA 5 HOH 104 604 604 HOH HOH A . 
AA 5 HOH 105 605 605 HOH HOH A . 
AA 5 HOH 106 606 606 HOH HOH A . 
AA 5 HOH 107 607 607 HOH HOH A . 
AA 5 HOH 108 608 608 HOH HOH A . 
AA 5 HOH 109 609 609 HOH HOH A . 
AA 5 HOH 110 610 610 HOH HOH A . 
AA 5 HOH 111 611 611 HOH HOH A . 
AA 5 HOH 112 612 612 HOH HOH A . 
AA 5 HOH 113 613 613 HOH HOH A . 
AA 5 HOH 114 614 614 HOH HOH A . 
AA 5 HOH 115 615 615 HOH HOH A . 
AA 5 HOH 116 616 616 HOH HOH A . 
AA 5 HOH 117 617 617 HOH HOH A . 
AA 5 HOH 118 618 618 HOH HOH A . 
AA 5 HOH 119 619 619 HOH HOH A . 
AA 5 HOH 120 620 620 HOH HOH A . 
AA 5 HOH 121 621 621 HOH HOH A . 
AA 5 HOH 122 622 622 HOH HOH A . 
AA 5 HOH 123 623 623 HOH HOH A . 
AA 5 HOH 124 624 624 HOH HOH A . 
AA 5 HOH 125 625 625 HOH HOH A . 
AA 5 HOH 126 626 626 HOH HOH A . 
AA 5 HOH 127 627 627 HOH HOH A . 
AA 5 HOH 128 628 628 HOH HOH A . 
AA 5 HOH 129 629 629 HOH HOH A . 
AA 5 HOH 130 630 630 HOH HOH A . 
AA 5 HOH 131 631 631 HOH HOH A . 
AA 5 HOH 132 632 632 HOH HOH A . 
AA 5 HOH 133 633 633 HOH HOH A . 
AA 5 HOH 134 634 634 HOH HOH A . 
AA 5 HOH 135 635 635 HOH HOH A . 
AA 5 HOH 136 636 636 HOH HOH A . 
AA 5 HOH 137 637 637 HOH HOH A . 
AA 5 HOH 138 638 638 HOH HOH A . 
AA 5 HOH 139 639 639 HOH HOH A . 
AA 5 HOH 140 640 640 HOH HOH A . 
AA 5 HOH 141 641 641 HOH HOH A . 
AA 5 HOH 142 642 642 HOH HOH A . 
AA 5 HOH 143 643 643 HOH HOH A . 
AA 5 HOH 144 644 644 HOH HOH A . 
AA 5 HOH 145 645 645 HOH HOH A . 
AA 5 HOH 146 646 646 HOH HOH A . 
AA 5 HOH 147 647 647 HOH HOH A . 
AA 5 HOH 148 648 648 HOH HOH A . 
AA 5 HOH 149 649 649 HOH HOH A . 
AA 5 HOH 150 650 650 HOH HOH A . 
AA 5 HOH 151 651 651 HOH HOH A . 
AA 5 HOH 152 652 652 HOH HOH A . 
AA 5 HOH 153 653 653 HOH HOH A . 
AA 5 HOH 154 654 654 HOH HOH A . 
AA 5 HOH 155 655 655 HOH HOH A . 
AA 5 HOH 156 656 656 HOH HOH A . 
AA 5 HOH 157 657 657 HOH HOH A . 
AA 5 HOH 158 658 658 HOH HOH A . 
AA 5 HOH 159 659 659 HOH HOH A . 
AA 5 HOH 160 660 660 HOH HOH A . 
AA 5 HOH 161 661 661 HOH HOH A . 
AA 5 HOH 162 662 662 HOH HOH A . 
AA 5 HOH 163 663 663 HOH HOH A . 
AA 5 HOH 164 664 664 HOH HOH A . 
AA 5 HOH 165 665 665 HOH HOH A . 
AA 5 HOH 166 666 666 HOH HOH A . 
AA 5 HOH 167 667 667 HOH HOH A . 
AA 5 HOH 168 668 668 HOH HOH A . 
AA 5 HOH 169 669 669 HOH HOH A . 
AA 5 HOH 170 670 670 HOH HOH A . 
AA 5 HOH 171 671 671 HOH HOH A . 
AA 5 HOH 172 672 672 HOH HOH A . 
AA 5 HOH 173 673 673 HOH HOH A . 
AA 5 HOH 174 674 674 HOH HOH A . 
AA 5 HOH 175 675 675 HOH HOH A . 
AA 5 HOH 176 676 676 HOH HOH A . 
AA 5 HOH 177 677 677 HOH HOH A . 
AA 5 HOH 178 678 678 HOH HOH A . 
AA 5 HOH 179 679 679 HOH HOH A . 
AA 5 HOH 180 680 680 HOH HOH A . 
AA 5 HOH 181 681 681 HOH HOH A . 
AA 5 HOH 182 682 682 HOH HOH A . 
AA 5 HOH 183 683 683 HOH HOH A . 
AA 5 HOH 184 684 684 HOH HOH A . 
AA 5 HOH 185 685 685 HOH HOH A . 
AA 5 HOH 186 686 686 HOH HOH A . 
AA 5 HOH 187 687 687 HOH HOH A . 
AA 5 HOH 188 688 688 HOH HOH A . 
AA 5 HOH 189 689 689 HOH HOH A . 
AA 5 HOH 190 690 690 HOH HOH A . 
AA 5 HOH 191 691 691 HOH HOH A . 
AA 5 HOH 192 692 692 HOH HOH A . 
AA 5 HOH 193 693 693 HOH HOH A . 
AA 5 HOH 194 694 694 HOH HOH A . 
AA 5 HOH 195 695 695 HOH HOH A . 
AA 5 HOH 196 696 696 HOH HOH A . 
AA 5 HOH 197 697 697 HOH HOH A . 
AA 5 HOH 198 698 698 HOH HOH A . 
AA 5 HOH 199 699 699 HOH HOH A . 
AA 5 HOH 200 700 700 HOH HOH A . 
AA 5 HOH 201 701 701 HOH HOH A . 
AA 5 HOH 202 702 702 HOH HOH A . 
AA 5 HOH 203 703 703 HOH HOH A . 
AA 5 HOH 204 704 704 HOH HOH A . 
AA 5 HOH 205 705 705 HOH HOH A . 
AA 5 HOH 206 706 706 HOH HOH A . 
AA 5 HOH 207 707 707 HOH HOH A . 
AA 5 HOH 208 708 708 HOH HOH A . 
AA 5 HOH 209 709 709 HOH HOH A . 
AA 5 HOH 210 710 710 HOH HOH A . 
AA 5 HOH 211 711 711 HOH HOH A . 
AA 5 HOH 212 712 712 HOH HOH A . 
AA 5 HOH 213 713 713 HOH HOH A . 
AA 5 HOH 214 714 714 HOH HOH A . 
AA 5 HOH 215 715 715 HOH HOH A . 
AA 5 HOH 216 716 716 HOH HOH A . 
AA 5 HOH 217 717 717 HOH HOH A . 
AA 5 HOH 218 718 718 HOH HOH A . 
AA 5 HOH 219 719 719 HOH HOH A . 
AA 5 HOH 220 720 720 HOH HOH A . 
AA 5 HOH 221 721 721 HOH HOH A . 
AA 5 HOH 222 722 722 HOH HOH A . 
AA 5 HOH 223 723 723 HOH HOH A . 
AA 5 HOH 224 724 724 HOH HOH A . 
AA 5 HOH 225 725 725 HOH HOH A . 
AA 5 HOH 226 726 726 HOH HOH A . 
BA 5 HOH 1   501 501 HOH HOH C . 
BA 5 HOH 2   502 502 HOH HOH C . 
BA 5 HOH 3   503 503 HOH HOH C . 
BA 5 HOH 4   504 504 HOH HOH C . 
BA 5 HOH 5   505 505 HOH HOH C . 
BA 5 HOH 6   506 506 HOH HOH C . 
BA 5 HOH 7   507 507 HOH HOH C . 
BA 5 HOH 8   508 508 HOH HOH C . 
BA 5 HOH 9   509 509 HOH HOH C . 
BA 5 HOH 10  510 510 HOH HOH C . 
BA 5 HOH 11  511 511 HOH HOH C . 
BA 5 HOH 12  512 512 HOH HOH C . 
BA 5 HOH 13  513 513 HOH HOH C . 
BA 5 HOH 14  514 514 HOH HOH C . 
BA 5 HOH 15  515 515 HOH HOH C . 
BA 5 HOH 16  516 516 HOH HOH C . 
BA 5 HOH 17  517 517 HOH HOH C . 
BA 5 HOH 18  518 518 HOH HOH C . 
BA 5 HOH 19  519 519 HOH HOH C . 
BA 5 HOH 20  520 520 HOH HOH C . 
BA 5 HOH 21  521 521 HOH HOH C . 
BA 5 HOH 22  522 522 HOH HOH C . 
BA 5 HOH 23  523 523 HOH HOH C . 
BA 5 HOH 24  524 524 HOH HOH C . 
BA 5 HOH 25  525 525 HOH HOH C . 
BA 5 HOH 26  526 526 HOH HOH C . 
BA 5 HOH 27  527 527 HOH HOH C . 
BA 5 HOH 28  528 528 HOH HOH C . 
BA 5 HOH 29  529 529 HOH HOH C . 
BA 5 HOH 30  530 530 HOH HOH C . 
BA 5 HOH 31  531 531 HOH HOH C . 
BA 5 HOH 32  532 532 HOH HOH C . 
BA 5 HOH 33  533 533 HOH HOH C . 
BA 5 HOH 34  534 534 HOH HOH C . 
BA 5 HOH 35  535 535 HOH HOH C . 
BA 5 HOH 36  536 536 HOH HOH C . 
BA 5 HOH 37  537 537 HOH HOH C . 
BA 5 HOH 38  538 538 HOH HOH C . 
BA 5 HOH 39  539 539 HOH HOH C . 
BA 5 HOH 40  540 540 HOH HOH C . 
BA 5 HOH 41  541 541 HOH HOH C . 
BA 5 HOH 42  542 542 HOH HOH C . 
BA 5 HOH 43  543 543 HOH HOH C . 
BA 5 HOH 44  544 544 HOH HOH C . 
BA 5 HOH 45  545 545 HOH HOH C . 
BA 5 HOH 46  546 546 HOH HOH C . 
BA 5 HOH 47  547 547 HOH HOH C . 
BA 5 HOH 48  548 548 HOH HOH C . 
BA 5 HOH 49  549 549 HOH HOH C . 
BA 5 HOH 50  550 550 HOH HOH C . 
BA 5 HOH 51  551 551 HOH HOH C . 
BA 5 HOH 52  552 552 HOH HOH C . 
BA 5 HOH 53  553 553 HOH HOH C . 
BA 5 HOH 54  554 554 HOH HOH C . 
BA 5 HOH 55  555 555 HOH HOH C . 
BA 5 HOH 56  556 556 HOH HOH C . 
BA 5 HOH 57  557 557 HOH HOH C . 
BA 5 HOH 58  558 558 HOH HOH C . 
BA 5 HOH 59  559 559 HOH HOH C . 
BA 5 HOH 60  560 560 HOH HOH C . 
BA 5 HOH 61  561 561 HOH HOH C . 
BA 5 HOH 62  562 562 HOH HOH C . 
BA 5 HOH 63  563 563 HOH HOH C . 
BA 5 HOH 64  564 564 HOH HOH C . 
BA 5 HOH 65  565 565 HOH HOH C . 
BA 5 HOH 66  566 566 HOH HOH C . 
BA 5 HOH 67  567 567 HOH HOH C . 
BA 5 HOH 68  568 568 HOH HOH C . 
BA 5 HOH 69  569 569 HOH HOH C . 
BA 5 HOH 70  570 570 HOH HOH C . 
BA 5 HOH 71  571 571 HOH HOH C . 
BA 5 HOH 72  572 572 HOH HOH C . 
BA 5 HOH 73  573 573 HOH HOH C . 
BA 5 HOH 74  574 574 HOH HOH C . 
BA 5 HOH 75  575 575 HOH HOH C . 
BA 5 HOH 76  576 576 HOH HOH C . 
BA 5 HOH 77  577 577 HOH HOH C . 
BA 5 HOH 78  578 578 HOH HOH C . 
BA 5 HOH 79  579 579 HOH HOH C . 
BA 5 HOH 80  580 580 HOH HOH C . 
BA 5 HOH 81  581 581 HOH HOH C . 
BA 5 HOH 82  582 582 HOH HOH C . 
BA 5 HOH 83  583 583 HOH HOH C . 
BA 5 HOH 84  584 584 HOH HOH C . 
BA 5 HOH 85  585 585 HOH HOH C . 
BA 5 HOH 86  586 586 HOH HOH C . 
BA 5 HOH 87  587 587 HOH HOH C . 
BA 5 HOH 88  588 588 HOH HOH C . 
BA 5 HOH 89  589 589 HOH HOH C . 
BA 5 HOH 90  590 590 HOH HOH C . 
BA 5 HOH 91  591 591 HOH HOH C . 
BA 5 HOH 92  592 592 HOH HOH C . 
BA 5 HOH 93  593 593 HOH HOH C . 
BA 5 HOH 94  594 594 HOH HOH C . 
BA 5 HOH 95  595 595 HOH HOH C . 
BA 5 HOH 96  596 596 HOH HOH C . 
BA 5 HOH 97  597 597 HOH HOH C . 
BA 5 HOH 98  598 598 HOH HOH C . 
BA 5 HOH 99  599 599 HOH HOH C . 
BA 5 HOH 100 600 600 HOH HOH C . 
BA 5 HOH 101 601 601 HOH HOH C . 
BA 5 HOH 102 602 602 HOH HOH C . 
BA 5 HOH 103 603 603 HOH HOH C . 
BA 5 HOH 104 604 604 HOH HOH C . 
BA 5 HOH 105 605 605 HOH HOH C . 
BA 5 HOH 106 606 606 HOH HOH C . 
BA 5 HOH 107 607 607 HOH HOH C . 
BA 5 HOH 108 608 608 HOH HOH C . 
BA 5 HOH 109 609 609 HOH HOH C . 
BA 5 HOH 110 610 610 HOH HOH C . 
BA 5 HOH 111 611 611 HOH HOH C . 
BA 5 HOH 112 612 612 HOH HOH C . 
BA 5 HOH 113 613 613 HOH HOH C . 
BA 5 HOH 114 614 614 HOH HOH C . 
BA 5 HOH 115 615 615 HOH HOH C . 
BA 5 HOH 116 616 616 HOH HOH C . 
BA 5 HOH 117 617 617 HOH HOH C . 
BA 5 HOH 118 618 618 HOH HOH C . 
BA 5 HOH 119 619 619 HOH HOH C . 
BA 5 HOH 120 620 620 HOH HOH C . 
BA 5 HOH 121 621 621 HOH HOH C . 
BA 5 HOH 122 622 622 HOH HOH C . 
BA 5 HOH 123 623 623 HOH HOH C . 
BA 5 HOH 124 624 624 HOH HOH C . 
BA 5 HOH 125 625 625 HOH HOH C . 
BA 5 HOH 126 626 626 HOH HOH C . 
BA 5 HOH 127 627 627 HOH HOH C . 
BA 5 HOH 128 628 628 HOH HOH C . 
BA 5 HOH 129 629 629 HOH HOH C . 
BA 5 HOH 130 630 630 HOH HOH C . 
BA 5 HOH 131 631 631 HOH HOH C . 
BA 5 HOH 132 632 632 HOH HOH C . 
BA 5 HOH 133 633 633 HOH HOH C . 
BA 5 HOH 134 634 634 HOH HOH C . 
BA 5 HOH 135 635 635 HOH HOH C . 
BA 5 HOH 136 636 636 HOH HOH C . 
BA 5 HOH 137 637 637 HOH HOH C . 
BA 5 HOH 138 638 638 HOH HOH C . 
BA 5 HOH 139 639 639 HOH HOH C . 
BA 5 HOH 140 640 640 HOH HOH C . 
BA 5 HOH 141 641 641 HOH HOH C . 
CA 5 HOH 1   501 501 HOH HOH E . 
CA 5 HOH 2   502 502 HOH HOH E . 
CA 5 HOH 3   503 503 HOH HOH E . 
CA 5 HOH 4   504 504 HOH HOH E . 
CA 5 HOH 5   505 505 HOH HOH E . 
CA 5 HOH 6   506 506 HOH HOH E . 
CA 5 HOH 7   507 507 HOH HOH E . 
CA 5 HOH 8   508 508 HOH HOH E . 
CA 5 HOH 9   509 509 HOH HOH E . 
CA 5 HOH 10  510 510 HOH HOH E . 
CA 5 HOH 11  511 511 HOH HOH E . 
CA 5 HOH 12  512 512 HOH HOH E . 
CA 5 HOH 13  513 513 HOH HOH E . 
CA 5 HOH 14  514 514 HOH HOH E . 
CA 5 HOH 15  515 515 HOH HOH E . 
CA 5 HOH 16  516 516 HOH HOH E . 
CA 5 HOH 17  517 517 HOH HOH E . 
CA 5 HOH 18  518 518 HOH HOH E . 
CA 5 HOH 19  519 519 HOH HOH E . 
CA 5 HOH 20  520 520 HOH HOH E . 
CA 5 HOH 21  521 521 HOH HOH E . 
CA 5 HOH 22  522 522 HOH HOH E . 
CA 5 HOH 23  523 523 HOH HOH E . 
CA 5 HOH 24  524 524 HOH HOH E . 
CA 5 HOH 25  525 525 HOH HOH E . 
CA 5 HOH 26  526 526 HOH HOH E . 
CA 5 HOH 27  527 527 HOH HOH E . 
CA 5 HOH 28  528 528 HOH HOH E . 
CA 5 HOH 29  529 529 HOH HOH E . 
CA 5 HOH 30  530 530 HOH HOH E . 
CA 5 HOH 31  531 531 HOH HOH E . 
CA 5 HOH 32  532 532 HOH HOH E . 
CA 5 HOH 33  533 533 HOH HOH E . 
CA 5 HOH 34  534 534 HOH HOH E . 
CA 5 HOH 35  535 535 HOH HOH E . 
CA 5 HOH 36  536 536 HOH HOH E . 
CA 5 HOH 37  537 537 HOH HOH E . 
CA 5 HOH 38  538 538 HOH HOH E . 
CA 5 HOH 39  539 539 HOH HOH E . 
CA 5 HOH 40  540 540 HOH HOH E . 
CA 5 HOH 41  541 541 HOH HOH E . 
CA 5 HOH 42  542 542 HOH HOH E . 
CA 5 HOH 43  543 543 HOH HOH E . 
CA 5 HOH 44  544 544 HOH HOH E . 
CA 5 HOH 45  545 545 HOH HOH E . 
CA 5 HOH 46  546 546 HOH HOH E . 
CA 5 HOH 47  547 547 HOH HOH E . 
CA 5 HOH 48  548 548 HOH HOH E . 
CA 5 HOH 49  549 549 HOH HOH E . 
CA 5 HOH 50  550 550 HOH HOH E . 
CA 5 HOH 51  551 551 HOH HOH E . 
CA 5 HOH 52  552 552 HOH HOH E . 
CA 5 HOH 53  553 553 HOH HOH E . 
CA 5 HOH 54  554 554 HOH HOH E . 
CA 5 HOH 55  555 555 HOH HOH E . 
CA 5 HOH 56  556 556 HOH HOH E . 
CA 5 HOH 57  557 557 HOH HOH E . 
CA 5 HOH 58  558 558 HOH HOH E . 
CA 5 HOH 59  559 559 HOH HOH E . 
CA 5 HOH 60  560 560 HOH HOH E . 
CA 5 HOH 61  561 561 HOH HOH E . 
CA 5 HOH 62  562 562 HOH HOH E . 
CA 5 HOH 63  563 563 HOH HOH E . 
CA 5 HOH 64  564 564 HOH HOH E . 
CA 5 HOH 65  565 565 HOH HOH E . 
CA 5 HOH 66  566 566 HOH HOH E . 
CA 5 HOH 67  567 567 HOH HOH E . 
CA 5 HOH 68  568 568 HOH HOH E . 
CA 5 HOH 69  569 569 HOH HOH E . 
CA 5 HOH 70  570 570 HOH HOH E . 
CA 5 HOH 71  571 571 HOH HOH E . 
CA 5 HOH 72  572 572 HOH HOH E . 
CA 5 HOH 73  573 573 HOH HOH E . 
CA 5 HOH 74  574 574 HOH HOH E . 
CA 5 HOH 75  575 575 HOH HOH E . 
CA 5 HOH 76  576 576 HOH HOH E . 
CA 5 HOH 77  577 577 HOH HOH E . 
CA 5 HOH 78  578 578 HOH HOH E . 
CA 5 HOH 79  579 579 HOH HOH E . 
CA 5 HOH 80  580 580 HOH HOH E . 
CA 5 HOH 81  581 581 HOH HOH E . 
CA 5 HOH 82  582 582 HOH HOH E . 
CA 5 HOH 83  583 583 HOH HOH E . 
CA 5 HOH 84  584 584 HOH HOH E . 
CA 5 HOH 85  585 585 HOH HOH E . 
CA 5 HOH 86  586 586 HOH HOH E . 
CA 5 HOH 87  587 587 HOH HOH E . 
CA 5 HOH 88  588 588 HOH HOH E . 
CA 5 HOH 89  589 589 HOH HOH E . 
CA 5 HOH 90  590 590 HOH HOH E . 
CA 5 HOH 91  591 591 HOH HOH E . 
CA 5 HOH 92  592 592 HOH HOH E . 
CA 5 HOH 93  593 593 HOH HOH E . 
CA 5 HOH 94  594 594 HOH HOH E . 
CA 5 HOH 95  595 595 HOH HOH E . 
CA 5 HOH 96  596 596 HOH HOH E . 
CA 5 HOH 97  597 597 HOH HOH E . 
CA 5 HOH 98  598 598 HOH HOH E . 
CA 5 HOH 99  599 599 HOH HOH E . 
CA 5 HOH 100 600 600 HOH HOH E . 
CA 5 HOH 101 601 601 HOH HOH E . 
CA 5 HOH 102 602 602 HOH HOH E . 
CA 5 HOH 103 603 603 HOH HOH E . 
CA 5 HOH 104 604 604 HOH HOH E . 
CA 5 HOH 105 605 605 HOH HOH E . 
CA 5 HOH 106 606 606 HOH HOH E . 
CA 5 HOH 107 607 607 HOH HOH E . 
CA 5 HOH 108 608 608 HOH HOH E . 
CA 5 HOH 109 609 609 HOH HOH E . 
CA 5 HOH 110 610 610 HOH HOH E . 
CA 5 HOH 111 611 611 HOH HOH E . 
CA 5 HOH 112 612 612 HOH HOH E . 
CA 5 HOH 113 613 613 HOH HOH E . 
CA 5 HOH 114 614 614 HOH HOH E . 
CA 5 HOH 115 615 615 HOH HOH E . 
CA 5 HOH 116 616 616 HOH HOH E . 
CA 5 HOH 117 617 617 HOH HOH E . 
CA 5 HOH 118 618 618 HOH HOH E . 
CA 5 HOH 119 619 619 HOH HOH E . 
CA 5 HOH 120 620 620 HOH HOH E . 
CA 5 HOH 121 621 621 HOH HOH E . 
CA 5 HOH 122 622 622 HOH HOH E . 
CA 5 HOH 123 623 623 HOH HOH E . 
CA 5 HOH 124 624 624 HOH HOH E . 
CA 5 HOH 125 625 625 HOH HOH E . 
CA 5 HOH 126 626 626 HOH HOH E . 
CA 5 HOH 127 627 627 HOH HOH E . 
CA 5 HOH 128 628 628 HOH HOH E . 
CA 5 HOH 129 629 629 HOH HOH E . 
CA 5 HOH 130 630 630 HOH HOH E . 
CA 5 HOH 131 631 631 HOH HOH E . 
CA 5 HOH 132 632 632 HOH HOH E . 
CA 5 HOH 133 633 633 HOH HOH E . 
CA 5 HOH 134 634 634 HOH HOH E . 
CA 5 HOH 135 635 635 HOH HOH E . 
CA 5 HOH 136 636 636 HOH HOH E . 
CA 5 HOH 137 637 637 HOH HOH E . 
CA 5 HOH 138 638 638 HOH HOH E . 
CA 5 HOH 139 639 639 HOH HOH E . 
CA 5 HOH 140 640 640 HOH HOH E . 
CA 5 HOH 141 641 641 HOH HOH E . 
CA 5 HOH 142 642 642 HOH HOH E . 
CA 5 HOH 143 643 643 HOH HOH E . 
CA 5 HOH 144 644 644 HOH HOH E . 
CA 5 HOH 145 645 645 HOH HOH E . 
CA 5 HOH 146 646 646 HOH HOH E . 
CA 5 HOH 147 647 647 HOH HOH E . 
CA 5 HOH 148 648 648 HOH HOH E . 
CA 5 HOH 149 649 649 HOH HOH E . 
CA 5 HOH 150 650 650 HOH HOH E . 
CA 5 HOH 151 651 651 HOH HOH E . 
CA 5 HOH 152 652 652 HOH HOH E . 
CA 5 HOH 153 653 653 HOH HOH E . 
CA 5 HOH 154 654 654 HOH HOH E . 
CA 5 HOH 155 655 655 HOH HOH E . 
CA 5 HOH 156 656 656 HOH HOH E . 
CA 5 HOH 157 657 657 HOH HOH E . 
CA 5 HOH 158 658 658 HOH HOH E . 
CA 5 HOH 159 659 659 HOH HOH E . 
CA 5 HOH 160 660 660 HOH HOH E . 
CA 5 HOH 161 661 661 HOH HOH E . 
CA 5 HOH 162 662 662 HOH HOH E . 
CA 5 HOH 163 663 663 HOH HOH E . 
CA 5 HOH 164 664 664 HOH HOH E . 
CA 5 HOH 165 665 665 HOH HOH E . 
CA 5 HOH 166 666 666 HOH HOH E . 
CA 5 HOH 167 667 667 HOH HOH E . 
CA 5 HOH 168 668 668 HOH HOH E . 
CA 5 HOH 169 669 669 HOH HOH E . 
CA 5 HOH 170 670 670 HOH HOH E . 
CA 5 HOH 171 671 671 HOH HOH E . 
CA 5 HOH 172 672 672 HOH HOH E . 
CA 5 HOH 173 673 673 HOH HOH E . 
CA 5 HOH 174 674 674 HOH HOH E . 
CA 5 HOH 175 675 675 HOH HOH E . 
CA 5 HOH 176 676 676 HOH HOH E . 
CA 5 HOH 177 677 677 HOH HOH E . 
CA 5 HOH 178 678 678 HOH HOH E . 
CA 5 HOH 179 679 679 HOH HOH E . 
CA 5 HOH 180 680 680 HOH HOH E . 
CA 5 HOH 181 681 681 HOH HOH E . 
CA 5 HOH 182 682 682 HOH HOH E . 
CA 5 HOH 183 683 683 HOH HOH E . 
CA 5 HOH 184 684 684 HOH HOH E . 
CA 5 HOH 185 685 685 HOH HOH E . 
CA 5 HOH 186 686 686 HOH HOH E . 
CA 5 HOH 187 687 687 HOH HOH E . 
CA 5 HOH 188 688 688 HOH HOH E . 
CA 5 HOH 189 689 689 HOH HOH E . 
CA 5 HOH 190 690 690 HOH HOH E . 
CA 5 HOH 191 691 691 HOH HOH E . 
CA 5 HOH 192 692 692 HOH HOH E . 
CA 5 HOH 193 693 693 HOH HOH E . 
CA 5 HOH 194 694 694 HOH HOH E . 
CA 5 HOH 195 695 695 HOH HOH E . 
CA 5 HOH 196 696 696 HOH HOH E . 
CA 5 HOH 197 697 697 HOH HOH E . 
CA 5 HOH 198 698 698 HOH HOH E . 
CA 5 HOH 199 699 699 HOH HOH E . 
CA 5 HOH 200 700 700 HOH HOH E . 
CA 5 HOH 201 701 701 HOH HOH E . 
CA 5 HOH 202 702 702 HOH HOH E . 
CA 5 HOH 203 703 703 HOH HOH E . 
CA 5 HOH 204 704 704 HOH HOH E . 
CA 5 HOH 205 705 705 HOH HOH E . 
CA 5 HOH 206 706 706 HOH HOH E . 
CA 5 HOH 207 707 707 HOH HOH E . 
CA 5 HOH 208 708 708 HOH HOH E . 
CA 5 HOH 209 709 709 HOH HOH E . 
CA 5 HOH 210 710 710 HOH HOH E . 
CA 5 HOH 211 711 711 HOH HOH E . 
CA 5 HOH 212 712 712 HOH HOH E . 
CA 5 HOH 213 713 713 HOH HOH E . 
CA 5 HOH 214 714 714 HOH HOH E . 
CA 5 HOH 215 715 715 HOH HOH E . 
CA 5 HOH 216 716 716 HOH HOH E . 
CA 5 HOH 217 717 717 HOH HOH E . 
CA 5 HOH 218 718 718 HOH HOH E . 
CA 5 HOH 219 719 719 HOH HOH E . 
CA 5 HOH 220 720 720 HOH HOH E . 
CA 5 HOH 221 721 721 HOH HOH E . 
CA 5 HOH 222 722 722 HOH HOH E . 
CA 5 HOH 223 723 723 HOH HOH E . 
CA 5 HOH 224 724 724 HOH HOH E . 
CA 5 HOH 225 725 725 HOH HOH E . 
CA 5 HOH 226 726 726 HOH HOH E . 
CA 5 HOH 227 727 727 HOH HOH E . 
CA 5 HOH 228 728 728 HOH HOH E . 
CA 5 HOH 229 729 729 HOH HOH E . 
CA 5 HOH 230 730 730 HOH HOH E . 
CA 5 HOH 231 731 731 HOH HOH E . 
CA 5 HOH 232 732 732 HOH HOH E . 
CA 5 HOH 233 733 733 HOH HOH E . 
CA 5 HOH 234 734 734 HOH HOH E . 
CA 5 HOH 235 735 735 HOH HOH E . 
CA 5 HOH 236 736 736 HOH HOH E . 
CA 5 HOH 237 737 737 HOH HOH E . 
CA 5 HOH 238 738 738 HOH HOH E . 
CA 5 HOH 239 739 739 HOH HOH E . 
CA 5 HOH 240 740 740 HOH HOH E . 
CA 5 HOH 241 741 741 HOH HOH E . 
CA 5 HOH 242 742 742 HOH HOH E . 
CA 5 HOH 243 743 743 HOH HOH E . 
CA 5 HOH 244 744 744 HOH HOH E . 
CA 5 HOH 245 745 745 HOH HOH E . 
CA 5 HOH 246 746 746 HOH HOH E . 
CA 5 HOH 247 747 747 HOH HOH E . 
CA 5 HOH 248 748 748 HOH HOH E . 
CA 5 HOH 249 749 749 HOH HOH E . 
CA 5 HOH 250 750 750 HOH HOH E . 
CA 5 HOH 251 751 751 HOH HOH E . 
CA 5 HOH 252 752 752 HOH HOH E . 
CA 5 HOH 253 753 753 HOH HOH E . 
CA 5 HOH 254 754 754 HOH HOH E . 
CA 5 HOH 255 755 755 HOH HOH E . 
CA 5 HOH 256 756 756 HOH HOH E . 
CA 5 HOH 257 757 757 HOH HOH E . 
CA 5 HOH 258 758 758 HOH HOH E . 
CA 5 HOH 259 759 759 HOH HOH E . 
CA 5 HOH 260 760 760 HOH HOH E . 
CA 5 HOH 261 761 761 HOH HOH E . 
CA 5 HOH 262 762 762 HOH HOH E . 
CA 5 HOH 263 763 763 HOH HOH E . 
CA 5 HOH 264 764 764 HOH HOH E . 
CA 5 HOH 265 765 765 HOH HOH E . 
CA 5 HOH 266 766 766 HOH HOH E . 
CA 5 HOH 267 767 767 HOH HOH E . 
CA 5 HOH 268 768 768 HOH HOH E . 
CA 5 HOH 269 769 769 HOH HOH E . 
CA 5 HOH 270 770 770 HOH HOH E . 
CA 5 HOH 271 771 771 HOH HOH E . 
CA 5 HOH 272 772 772 HOH HOH E . 
CA 5 HOH 273 773 773 HOH HOH E . 
CA 5 HOH 274 774 774 HOH HOH E . 
CA 5 HOH 275 775 775 HOH HOH E . 
CA 5 HOH 276 776 776 HOH HOH E . 
CA 5 HOH 277 777 777 HOH HOH E . 
CA 5 HOH 278 778 778 HOH HOH E . 
CA 5 HOH 279 779 779 HOH HOH E . 
CA 5 HOH 280 780 780 HOH HOH E . 
CA 5 HOH 281 781 781 HOH HOH E . 
CA 5 HOH 282 782 782 HOH HOH E . 
CA 5 HOH 283 783 783 HOH HOH E . 
CA 5 HOH 284 784 784 HOH HOH E . 
CA 5 HOH 285 785 785 HOH HOH E . 
CA 5 HOH 286 786 786 HOH HOH E . 
CA 5 HOH 287 787 787 HOH HOH E . 
CA 5 HOH 288 788 788 HOH HOH E . 
CA 5 HOH 289 789 789 HOH HOH E . 
CA 5 HOH 290 790 790 HOH HOH E . 
CA 5 HOH 291 791 791 HOH HOH E . 
CA 5 HOH 292 792 792 HOH HOH E . 
CA 5 HOH 293 793 793 HOH HOH E . 
CA 5 HOH 294 794 794 HOH HOH E . 
CA 5 HOH 295 795 795 HOH HOH E . 
CA 5 HOH 296 796 796 HOH HOH E . 
CA 5 HOH 297 797 797 HOH HOH E . 
CA 5 HOH 298 798 798 HOH HOH E . 
CA 5 HOH 299 799 799 HOH HOH E . 
CA 5 HOH 300 800 800 HOH HOH E . 
CA 5 HOH 301 801 801 HOH HOH E . 
CA 5 HOH 302 802 802 HOH HOH E . 
CA 5 HOH 303 803 803 HOH HOH E . 
CA 5 HOH 304 804 804 HOH HOH E . 
CA 5 HOH 305 805 805 HOH HOH E . 
CA 5 HOH 306 806 806 HOH HOH E . 
CA 5 HOH 307 807 807 HOH HOH E . 
CA 5 HOH 308 808 808 HOH HOH E . 
CA 5 HOH 309 809 809 HOH HOH E . 
CA 5 HOH 310 810 810 HOH HOH E . 
CA 5 HOH 311 811 811 HOH HOH E . 
CA 5 HOH 312 812 812 HOH HOH E . 
CA 5 HOH 313 813 813 HOH HOH E . 
CA 5 HOH 314 814 814 HOH HOH E . 
CA 5 HOH 315 815 815 HOH HOH E . 
CA 5 HOH 316 816 816 HOH HOH E . 
CA 5 HOH 317 817 817 HOH HOH E . 
CA 5 HOH 318 818 818 HOH HOH E . 
CA 5 HOH 319 819 819 HOH HOH E . 
CA 5 HOH 320 820 820 HOH HOH E . 
CA 5 HOH 321 821 821 HOH HOH E . 
CA 5 HOH 322 822 822 HOH HOH E . 
CA 5 HOH 323 823 823 HOH HOH E . 
CA 5 HOH 324 824 824 HOH HOH E . 
CA 5 HOH 325 825 825 HOH HOH E . 
CA 5 HOH 326 826 826 HOH HOH E . 
CA 5 HOH 327 827 827 HOH HOH E . 
CA 5 HOH 328 828 828 HOH HOH E . 
CA 5 HOH 329 829 829 HOH HOH E . 
CA 5 HOH 330 830 830 HOH HOH E . 
CA 5 HOH 331 831 831 HOH HOH E . 
CA 5 HOH 332 832 832 HOH HOH E . 
CA 5 HOH 333 833 833 HOH HOH E . 
CA 5 HOH 334 834 834 HOH HOH E . 
CA 5 HOH 335 835 835 HOH HOH E . 
CA 5 HOH 336 836 836 HOH HOH E . 
CA 5 HOH 337 837 837 HOH HOH E . 
CA 5 HOH 338 838 838 HOH HOH E . 
CA 5 HOH 339 839 839 HOH HOH E . 
CA 5 HOH 340 840 840 HOH HOH E . 
CA 5 HOH 341 841 841 HOH HOH E . 
CA 5 HOH 342 842 842 HOH HOH E . 
CA 5 HOH 343 843 843 HOH HOH E . 
CA 5 HOH 344 844 844 HOH HOH E . 
CA 5 HOH 345 845 845 HOH HOH E . 
CA 5 HOH 346 846 846 HOH HOH E . 
CA 5 HOH 347 847 847 HOH HOH E . 
CA 5 HOH 348 848 848 HOH HOH E . 
CA 5 HOH 349 849 849 HOH HOH E . 
CA 5 HOH 350 850 850 HOH HOH E . 
CA 5 HOH 351 851 851 HOH HOH E . 
CA 5 HOH 352 852 852 HOH HOH E . 
CA 5 HOH 353 853 853 HOH HOH E . 
CA 5 HOH 354 854 854 HOH HOH E . 
CA 5 HOH 355 855 855 HOH HOH E . 
CA 5 HOH 356 856 856 HOH HOH E . 
CA 5 HOH 357 857 857 HOH HOH E . 
CA 5 HOH 358 858 858 HOH HOH E . 
CA 5 HOH 359 859 859 HOH HOH E . 
CA 5 HOH 360 860 860 HOH HOH E . 
CA 5 HOH 361 861 861 HOH HOH E . 
CA 5 HOH 362 862 862 HOH HOH E . 
CA 5 HOH 363 863 863 HOH HOH E . 
CA 5 HOH 364 864 864 HOH HOH E . 
CA 5 HOH 365 865 865 HOH HOH E . 
CA 5 HOH 366 866 866 HOH HOH E . 
CA 5 HOH 367 867 867 HOH HOH E . 
CA 5 HOH 368 868 868 HOH HOH E . 
DA 5 HOH 1   501 501 HOH HOH G . 
DA 5 HOH 2   502 502 HOH HOH G . 
DA 5 HOH 3   503 503 HOH HOH G . 
DA 5 HOH 4   504 504 HOH HOH G . 
DA 5 HOH 5   505 505 HOH HOH G . 
DA 5 HOH 6   506 506 HOH HOH G . 
DA 5 HOH 7   507 507 HOH HOH G . 
DA 5 HOH 8   508 508 HOH HOH G . 
DA 5 HOH 9   509 509 HOH HOH G . 
DA 5 HOH 10  510 510 HOH HOH G . 
DA 5 HOH 11  511 511 HOH HOH G . 
DA 5 HOH 12  512 512 HOH HOH G . 
DA 5 HOH 13  513 513 HOH HOH G . 
DA 5 HOH 14  514 514 HOH HOH G . 
DA 5 HOH 15  515 515 HOH HOH G . 
DA 5 HOH 16  516 516 HOH HOH G . 
DA 5 HOH 17  517 517 HOH HOH G . 
DA 5 HOH 18  518 518 HOH HOH G . 
DA 5 HOH 19  519 519 HOH HOH G . 
DA 5 HOH 20  520 520 HOH HOH G . 
DA 5 HOH 21  521 521 HOH HOH G . 
DA 5 HOH 22  522 522 HOH HOH G . 
DA 5 HOH 23  523 523 HOH HOH G . 
DA 5 HOH 24  524 524 HOH HOH G . 
DA 5 HOH 25  525 525 HOH HOH G . 
DA 5 HOH 26  526 526 HOH HOH G . 
DA 5 HOH 27  527 527 HOH HOH G . 
DA 5 HOH 28  528 528 HOH HOH G . 
DA 5 HOH 29  529 529 HOH HOH G . 
DA 5 HOH 30  530 530 HOH HOH G . 
DA 5 HOH 31  531 531 HOH HOH G . 
DA 5 HOH 32  532 532 HOH HOH G . 
DA 5 HOH 33  533 533 HOH HOH G . 
DA 5 HOH 34  534 534 HOH HOH G . 
DA 5 HOH 35  535 535 HOH HOH G . 
DA 5 HOH 36  536 536 HOH HOH G . 
DA 5 HOH 37  537 537 HOH HOH G . 
DA 5 HOH 38  538 538 HOH HOH G . 
DA 5 HOH 39  539 539 HOH HOH G . 
DA 5 HOH 40  540 540 HOH HOH G . 
DA 5 HOH 41  541 541 HOH HOH G . 
DA 5 HOH 42  542 542 HOH HOH G . 
DA 5 HOH 43  543 543 HOH HOH G . 
DA 5 HOH 44  544 544 HOH HOH G . 
DA 5 HOH 45  545 545 HOH HOH G . 
DA 5 HOH 46  546 546 HOH HOH G . 
DA 5 HOH 47  547 547 HOH HOH G . 
DA 5 HOH 48  548 548 HOH HOH G . 
DA 5 HOH 49  549 549 HOH HOH G . 
DA 5 HOH 50  550 550 HOH HOH G . 
DA 5 HOH 51  551 551 HOH HOH G . 
DA 5 HOH 52  552 552 HOH HOH G . 
DA 5 HOH 53  553 553 HOH HOH G . 
DA 5 HOH 54  554 554 HOH HOH G . 
DA 5 HOH 55  555 555 HOH HOH G . 
DA 5 HOH 56  556 556 HOH HOH G . 
DA 5 HOH 57  557 557 HOH HOH G . 
DA 5 HOH 58  558 558 HOH HOH G . 
DA 5 HOH 59  559 559 HOH HOH G . 
DA 5 HOH 60  560 560 HOH HOH G . 
DA 5 HOH 61  561 561 HOH HOH G . 
DA 5 HOH 62  562 562 HOH HOH G . 
DA 5 HOH 63  563 563 HOH HOH G . 
DA 5 HOH 64  564 564 HOH HOH G . 
DA 5 HOH 65  565 565 HOH HOH G . 
DA 5 HOH 66  566 566 HOH HOH G . 
DA 5 HOH 67  567 567 HOH HOH G . 
DA 5 HOH 68  568 568 HOH HOH G . 
DA 5 HOH 69  569 569 HOH HOH G . 
DA 5 HOH 70  570 570 HOH HOH G . 
DA 5 HOH 71  571 571 HOH HOH G . 
DA 5 HOH 72  572 572 HOH HOH G . 
DA 5 HOH 73  573 573 HOH HOH G . 
DA 5 HOH 74  574 574 HOH HOH G . 
DA 5 HOH 75  575 575 HOH HOH G . 
DA 5 HOH 76  576 576 HOH HOH G . 
DA 5 HOH 77  577 577 HOH HOH G . 
DA 5 HOH 78  578 578 HOH HOH G . 
DA 5 HOH 79  579 579 HOH HOH G . 
DA 5 HOH 80  580 580 HOH HOH G . 
DA 5 HOH 81  581 581 HOH HOH G . 
DA 5 HOH 82  582 582 HOH HOH G . 
DA 5 HOH 83  583 583 HOH HOH G . 
DA 5 HOH 84  584 584 HOH HOH G . 
DA 5 HOH 85  585 585 HOH HOH G . 
DA 5 HOH 86  586 586 HOH HOH G . 
DA 5 HOH 87  587 587 HOH HOH G . 
DA 5 HOH 88  588 588 HOH HOH G . 
DA 5 HOH 89  589 589 HOH HOH G . 
DA 5 HOH 90  590 590 HOH HOH G . 
DA 5 HOH 91  591 591 HOH HOH G . 
DA 5 HOH 92  592 592 HOH HOH G . 
DA 5 HOH 93  593 593 HOH HOH G . 
DA 5 HOH 94  594 594 HOH HOH G . 
DA 5 HOH 95  595 595 HOH HOH G . 
DA 5 HOH 96  596 596 HOH HOH G . 
DA 5 HOH 97  597 597 HOH HOH G . 
DA 5 HOH 98  598 598 HOH HOH G . 
DA 5 HOH 99  599 599 HOH HOH G . 
DA 5 HOH 100 600 600 HOH HOH G . 
DA 5 HOH 101 601 601 HOH HOH G . 
DA 5 HOH 102 602 602 HOH HOH G . 
DA 5 HOH 103 603 603 HOH HOH G . 
DA 5 HOH 104 604 604 HOH HOH G . 
DA 5 HOH 105 605 605 HOH HOH G . 
DA 5 HOH 106 606 606 HOH HOH G . 
DA 5 HOH 107 607 607 HOH HOH G . 
DA 5 HOH 108 608 608 HOH HOH G . 
DA 5 HOH 109 609 609 HOH HOH G . 
DA 5 HOH 110 610 610 HOH HOH G . 
DA 5 HOH 111 611 611 HOH HOH G . 
DA 5 HOH 112 612 612 HOH HOH G . 
DA 5 HOH 113 613 613 HOH HOH G . 
DA 5 HOH 114 614 614 HOH HOH G . 
DA 5 HOH 115 615 615 HOH HOH G . 
DA 5 HOH 116 616 616 HOH HOH G . 
DA 5 HOH 117 617 617 HOH HOH G . 
DA 5 HOH 118 618 618 HOH HOH G . 
DA 5 HOH 119 619 619 HOH HOH G . 
DA 5 HOH 120 620 620 HOH HOH G . 
DA 5 HOH 121 621 621 HOH HOH G . 
DA 5 HOH 122 622 622 HOH HOH G . 
DA 5 HOH 123 623 623 HOH HOH G . 
DA 5 HOH 124 624 624 HOH HOH G . 
DA 5 HOH 125 625 625 HOH HOH G . 
DA 5 HOH 126 626 626 HOH HOH G . 
DA 5 HOH 127 627 627 HOH HOH G . 
DA 5 HOH 128 628 628 HOH HOH G . 
DA 5 HOH 129 629 629 HOH HOH G . 
DA 5 HOH 130 630 630 HOH HOH G . 
DA 5 HOH 131 631 631 HOH HOH G . 
DA 5 HOH 132 632 632 HOH HOH G . 
DA 5 HOH 133 633 633 HOH HOH G . 
DA 5 HOH 134 634 634 HOH HOH G . 
DA 5 HOH 135 635 635 HOH HOH G . 
DA 5 HOH 136 636 636 HOH HOH G . 
DA 5 HOH 137 637 637 HOH HOH G . 
DA 5 HOH 138 638 638 HOH HOH G . 
DA 5 HOH 139 639 639 HOH HOH G . 
DA 5 HOH 140 640 640 HOH HOH G . 
DA 5 HOH 141 641 641 HOH HOH G . 
DA 5 HOH 142 642 642 HOH HOH G . 
DA 5 HOH 143 643 643 HOH HOH G . 
DA 5 HOH 144 644 644 HOH HOH G . 
DA 5 HOH 145 645 645 HOH HOH G . 
DA 5 HOH 146 646 646 HOH HOH G . 
DA 5 HOH 147 647 647 HOH HOH G . 
DA 5 HOH 148 648 648 HOH HOH G . 
DA 5 HOH 149 649 649 HOH HOH G . 
DA 5 HOH 150 650 650 HOH HOH G . 
DA 5 HOH 151 651 651 HOH HOH G . 
DA 5 HOH 152 652 652 HOH HOH G . 
DA 5 HOH 153 653 653 HOH HOH G . 
DA 5 HOH 154 654 654 HOH HOH G . 
DA 5 HOH 155 655 655 HOH HOH G . 
DA 5 HOH 156 656 656 HOH HOH G . 
DA 5 HOH 157 657 657 HOH HOH G . 
DA 5 HOH 158 658 658 HOH HOH G . 
DA 5 HOH 159 659 659 HOH HOH G . 
DA 5 HOH 160 660 660 HOH HOH G . 
DA 5 HOH 161 661 661 HOH HOH G . 
DA 5 HOH 162 662 662 HOH HOH G . 
DA 5 HOH 163 663 663 HOH HOH G . 
DA 5 HOH 164 664 664 HOH HOH G . 
DA 5 HOH 165 665 665 HOH HOH G . 
DA 5 HOH 166 666 666 HOH HOH G . 
DA 5 HOH 167 667 667 HOH HOH G . 
DA 5 HOH 168 668 668 HOH HOH G . 
DA 5 HOH 169 669 669 HOH HOH G . 
DA 5 HOH 170 670 670 HOH HOH G . 
DA 5 HOH 171 671 671 HOH HOH G . 
DA 5 HOH 172 672 672 HOH HOH G . 
DA 5 HOH 173 673 673 HOH HOH G . 
DA 5 HOH 174 674 674 HOH HOH G . 
DA 5 HOH 175 675 675 HOH HOH G . 
DA 5 HOH 176 676 676 HOH HOH G . 
DA 5 HOH 177 677 677 HOH HOH G . 
DA 5 HOH 178 678 678 HOH HOH G . 
DA 5 HOH 179 679 679 HOH HOH G . 
DA 5 HOH 180 680 680 HOH HOH G . 
DA 5 HOH 181 681 681 HOH HOH G . 
DA 5 HOH 182 682 682 HOH HOH G . 
DA 5 HOH 183 683 683 HOH HOH G . 
DA 5 HOH 184 684 684 HOH HOH G . 
DA 5 HOH 185 685 685 HOH HOH G . 
DA 5 HOH 186 686 686 HOH HOH G . 
DA 5 HOH 187 687 687 HOH HOH G . 
DA 5 HOH 188 688 688 HOH HOH G . 
DA 5 HOH 189 689 689 HOH HOH G . 
DA 5 HOH 190 690 690 HOH HOH G . 
DA 5 HOH 191 691 691 HOH HOH G . 
DA 5 HOH 192 692 692 HOH HOH G . 
DA 5 HOH 193 693 693 HOH HOH G . 
DA 5 HOH 194 694 694 HOH HOH G . 
DA 5 HOH 195 695 695 HOH HOH G . 
DA 5 HOH 196 696 696 HOH HOH G . 
DA 5 HOH 197 697 697 HOH HOH G . 
DA 5 HOH 198 698 698 HOH HOH G . 
DA 5 HOH 199 699 699 HOH HOH G . 
DA 5 HOH 200 700 700 HOH HOH G . 
DA 5 HOH 201 701 701 HOH HOH G . 
DA 5 HOH 202 702 702 HOH HOH G . 
DA 5 HOH 203 703 703 HOH HOH G . 
DA 5 HOH 204 704 704 HOH HOH G . 
DA 5 HOH 205 705 705 HOH HOH G . 
DA 5 HOH 206 706 706 HOH HOH G . 
DA 5 HOH 207 707 707 HOH HOH G . 
DA 5 HOH 208 708 708 HOH HOH G . 
DA 5 HOH 209 709 709 HOH HOH G . 
DA 5 HOH 210 710 710 HOH HOH G . 
DA 5 HOH 211 711 711 HOH HOH G . 
DA 5 HOH 212 712 712 HOH HOH G . 
DA 5 HOH 213 713 713 HOH HOH G . 
DA 5 HOH 214 714 714 HOH HOH G . 
DA 5 HOH 215 715 715 HOH HOH G . 
DA 5 HOH 216 716 716 HOH HOH G . 
DA 5 HOH 217 717 717 HOH HOH G . 
DA 5 HOH 218 718 718 HOH HOH G . 
DA 5 HOH 219 719 719 HOH HOH G . 
DA 5 HOH 220 720 720 HOH HOH G . 
DA 5 HOH 221 721 721 HOH HOH G . 
DA 5 HOH 222 722 722 HOH HOH G . 
DA 5 HOH 223 723 723 HOH HOH G . 
DA 5 HOH 224 724 724 HOH HOH G . 
DA 5 HOH 225 725 725 HOH HOH G . 
DA 5 HOH 226 726 726 HOH HOH G . 
DA 5 HOH 227 727 727 HOH HOH G . 
DA 5 HOH 228 728 728 HOH HOH G . 
DA 5 HOH 229 729 729 HOH HOH G . 
DA 5 HOH 230 730 730 HOH HOH G . 
DA 5 HOH 231 731 731 HOH HOH G . 
DA 5 HOH 232 732 732 HOH HOH G . 
DA 5 HOH 233 733 733 HOH HOH G . 
DA 5 HOH 234 734 734 HOH HOH G . 
DA 5 HOH 235 735 735 HOH HOH G . 
DA 5 HOH 236 736 736 HOH HOH G . 
DA 5 HOH 237 737 737 HOH HOH G . 
DA 5 HOH 238 738 738 HOH HOH G . 
DA 5 HOH 239 739 739 HOH HOH G . 
DA 5 HOH 240 740 740 HOH HOH G . 
DA 5 HOH 241 741 741 HOH HOH G . 
DA 5 HOH 242 742 742 HOH HOH G . 
DA 5 HOH 243 743 743 HOH HOH G . 
DA 5 HOH 244 744 744 HOH HOH G . 
DA 5 HOH 245 745 745 HOH HOH G . 
DA 5 HOH 246 746 746 HOH HOH G . 
DA 5 HOH 247 747 747 HOH HOH G . 
DA 5 HOH 248 748 748 HOH HOH G . 
DA 5 HOH 249 749 749 HOH HOH G . 
DA 5 HOH 250 750 750 HOH HOH G . 
DA 5 HOH 251 751 751 HOH HOH G . 
DA 5 HOH 252 752 752 HOH HOH G . 
DA 5 HOH 253 753 753 HOH HOH G . 
DA 5 HOH 254 754 754 HOH HOH G . 
DA 5 HOH 255 755 755 HOH HOH G . 
DA 5 HOH 256 756 756 HOH HOH G . 
DA 5 HOH 257 757 757 HOH HOH G . 
DA 5 HOH 258 758 758 HOH HOH G . 
DA 5 HOH 259 759 759 HOH HOH G . 
DA 5 HOH 260 760 760 HOH HOH G . 
DA 5 HOH 261 761 761 HOH HOH G . 
DA 5 HOH 262 762 762 HOH HOH G . 
DA 5 HOH 263 763 763 HOH HOH G . 
DA 5 HOH 264 764 764 HOH HOH G . 
DA 5 HOH 265 765 765 HOH HOH G . 
DA 5 HOH 266 766 766 HOH HOH G . 
DA 5 HOH 267 767 767 HOH HOH G . 
DA 5 HOH 268 768 768 HOH HOH G . 
DA 5 HOH 269 769 769 HOH HOH G . 
DA 5 HOH 270 770 770 HOH HOH G . 
DA 5 HOH 271 771 771 HOH HOH G . 
DA 5 HOH 272 772 772 HOH HOH G . 
DA 5 HOH 273 773 773 HOH HOH G . 
DA 5 HOH 274 774 774 HOH HOH G . 
DA 5 HOH 275 775 775 HOH HOH G . 
DA 5 HOH 276 776 776 HOH HOH G . 
DA 5 HOH 277 777 777 HOH HOH G . 
DA 5 HOH 278 778 778 HOH HOH G . 
DA 5 HOH 279 779 779 HOH HOH G . 
DA 5 HOH 280 780 780 HOH HOH G . 
DA 5 HOH 281 781 781 HOH HOH G . 
DA 5 HOH 282 782 782 HOH HOH G . 
DA 5 HOH 283 783 783 HOH HOH G . 
DA 5 HOH 284 784 784 HOH HOH G . 
DA 5 HOH 285 785 785 HOH HOH G . 
DA 5 HOH 286 786 786 HOH HOH G . 
DA 5 HOH 287 787 787 HOH HOH G . 
DA 5 HOH 288 788 788 HOH HOH G . 
DA 5 HOH 289 789 789 HOH HOH G . 
DA 5 HOH 290 790 790 HOH HOH G . 
DA 5 HOH 291 791 791 HOH HOH G . 
DA 5 HOH 292 792 792 HOH HOH G . 
DA 5 HOH 293 793 793 HOH HOH G . 
DA 5 HOH 294 794 794 HOH HOH G . 
DA 5 HOH 295 795 795 HOH HOH G . 
DA 5 HOH 296 796 796 HOH HOH G . 
DA 5 HOH 297 797 797 HOH HOH G . 
DA 5 HOH 298 798 798 HOH HOH G . 
DA 5 HOH 299 799 799 HOH HOH G . 
DA 5 HOH 300 800 800 HOH HOH G . 
DA 5 HOH 301 801 801 HOH HOH G . 
DA 5 HOH 302 802 802 HOH HOH G . 
DA 5 HOH 303 803 803 HOH HOH G . 
DA 5 HOH 304 804 804 HOH HOH G . 
DA 5 HOH 305 805 805 HOH HOH G . 
DA 5 HOH 306 806 806 HOH HOH G . 
DA 5 HOH 307 807 807 HOH HOH G . 
DA 5 HOH 308 808 808 HOH HOH G . 
DA 5 HOH 309 809 809 HOH HOH G . 
DA 5 HOH 310 810 810 HOH HOH G . 
DA 5 HOH 311 811 811 HOH HOH G . 
DA 5 HOH 312 812 812 HOH HOH G . 
DA 5 HOH 313 813 813 HOH HOH G . 
DA 5 HOH 314 814 814 HOH HOH G . 
DA 5 HOH 315 815 815 HOH HOH G . 
DA 5 HOH 316 816 816 HOH HOH G . 
DA 5 HOH 317 817 817 HOH HOH G . 
DA 5 HOH 318 818 818 HOH HOH G . 
DA 5 HOH 319 819 819 HOH HOH G . 
DA 5 HOH 320 820 820 HOH HOH G . 
DA 5 HOH 321 821 821 HOH HOH G . 
DA 5 HOH 322 822 822 HOH HOH G . 
DA 5 HOH 323 823 823 HOH HOH G . 
DA 5 HOH 324 824 824 HOH HOH G . 
EA 5 HOH 1   501 501 HOH HOH I . 
EA 5 HOH 2   502 502 HOH HOH I . 
EA 5 HOH 3   503 503 HOH HOH I . 
EA 5 HOH 4   504 504 HOH HOH I . 
EA 5 HOH 5   505 505 HOH HOH I . 
EA 5 HOH 6   506 506 HOH HOH I . 
EA 5 HOH 7   507 507 HOH HOH I . 
EA 5 HOH 8   508 508 HOH HOH I . 
EA 5 HOH 9   509 509 HOH HOH I . 
EA 5 HOH 10  510 510 HOH HOH I . 
EA 5 HOH 11  511 511 HOH HOH I . 
EA 5 HOH 12  512 512 HOH HOH I . 
EA 5 HOH 13  513 513 HOH HOH I . 
EA 5 HOH 14  514 514 HOH HOH I . 
EA 5 HOH 15  515 515 HOH HOH I . 
EA 5 HOH 16  516 516 HOH HOH I . 
EA 5 HOH 17  517 517 HOH HOH I . 
EA 5 HOH 18  518 518 HOH HOH I . 
EA 5 HOH 19  519 519 HOH HOH I . 
EA 5 HOH 20  520 520 HOH HOH I . 
EA 5 HOH 21  521 521 HOH HOH I . 
EA 5 HOH 22  522 522 HOH HOH I . 
EA 5 HOH 23  523 523 HOH HOH I . 
EA 5 HOH 24  524 524 HOH HOH I . 
EA 5 HOH 25  525 525 HOH HOH I . 
EA 5 HOH 26  526 526 HOH HOH I . 
EA 5 HOH 27  527 527 HOH HOH I . 
EA 5 HOH 28  528 528 HOH HOH I . 
EA 5 HOH 29  529 529 HOH HOH I . 
EA 5 HOH 30  530 530 HOH HOH I . 
EA 5 HOH 31  531 531 HOH HOH I . 
EA 5 HOH 32  532 532 HOH HOH I . 
EA 5 HOH 33  533 533 HOH HOH I . 
EA 5 HOH 34  534 534 HOH HOH I . 
EA 5 HOH 35  535 535 HOH HOH I . 
EA 5 HOH 36  536 536 HOH HOH I . 
EA 5 HOH 37  537 537 HOH HOH I . 
EA 5 HOH 38  538 538 HOH HOH I . 
EA 5 HOH 39  539 539 HOH HOH I . 
EA 5 HOH 40  540 540 HOH HOH I . 
EA 5 HOH 41  541 541 HOH HOH I . 
EA 5 HOH 42  542 542 HOH HOH I . 
EA 5 HOH 43  543 543 HOH HOH I . 
EA 5 HOH 44  544 544 HOH HOH I . 
EA 5 HOH 45  545 545 HOH HOH I . 
EA 5 HOH 46  546 546 HOH HOH I . 
EA 5 HOH 47  547 547 HOH HOH I . 
EA 5 HOH 48  548 548 HOH HOH I . 
EA 5 HOH 49  549 549 HOH HOH I . 
EA 5 HOH 50  550 550 HOH HOH I . 
EA 5 HOH 51  551 551 HOH HOH I . 
EA 5 HOH 52  552 552 HOH HOH I . 
EA 5 HOH 53  553 553 HOH HOH I . 
EA 5 HOH 54  554 554 HOH HOH I . 
EA 5 HOH 55  555 555 HOH HOH I . 
EA 5 HOH 56  556 556 HOH HOH I . 
EA 5 HOH 57  557 557 HOH HOH I . 
EA 5 HOH 58  558 558 HOH HOH I . 
EA 5 HOH 59  559 559 HOH HOH I . 
EA 5 HOH 60  560 560 HOH HOH I . 
EA 5 HOH 61  561 561 HOH HOH I . 
EA 5 HOH 62  562 562 HOH HOH I . 
EA 5 HOH 63  563 563 HOH HOH I . 
EA 5 HOH 64  564 564 HOH HOH I . 
EA 5 HOH 65  565 565 HOH HOH I . 
EA 5 HOH 66  566 566 HOH HOH I . 
EA 5 HOH 67  567 567 HOH HOH I . 
EA 5 HOH 68  568 568 HOH HOH I . 
EA 5 HOH 69  569 569 HOH HOH I . 
EA 5 HOH 70  570 570 HOH HOH I . 
EA 5 HOH 71  571 571 HOH HOH I . 
EA 5 HOH 72  572 572 HOH HOH I . 
EA 5 HOH 73  573 573 HOH HOH I . 
EA 5 HOH 74  574 574 HOH HOH I . 
EA 5 HOH 75  575 575 HOH HOH I . 
EA 5 HOH 76  576 576 HOH HOH I . 
EA 5 HOH 77  577 577 HOH HOH I . 
EA 5 HOH 78  578 578 HOH HOH I . 
EA 5 HOH 79  579 579 HOH HOH I . 
EA 5 HOH 80  580 580 HOH HOH I . 
EA 5 HOH 81  581 581 HOH HOH I . 
EA 5 HOH 82  582 582 HOH HOH I . 
EA 5 HOH 83  583 583 HOH HOH I . 
EA 5 HOH 84  584 584 HOH HOH I . 
EA 5 HOH 85  585 585 HOH HOH I . 
EA 5 HOH 86  586 586 HOH HOH I . 
EA 5 HOH 87  587 587 HOH HOH I . 
EA 5 HOH 88  588 588 HOH HOH I . 
EA 5 HOH 89  589 589 HOH HOH I . 
EA 5 HOH 90  590 590 HOH HOH I . 
EA 5 HOH 91  591 591 HOH HOH I . 
EA 5 HOH 92  592 592 HOH HOH I . 
EA 5 HOH 93  593 593 HOH HOH I . 
EA 5 HOH 94  594 594 HOH HOH I . 
EA 5 HOH 95  595 595 HOH HOH I . 
EA 5 HOH 96  596 596 HOH HOH I . 
EA 5 HOH 97  597 597 HOH HOH I . 
EA 5 HOH 98  598 598 HOH HOH I . 
EA 5 HOH 99  599 599 HOH HOH I . 
EA 5 HOH 100 600 600 HOH HOH I . 
EA 5 HOH 101 601 601 HOH HOH I . 
EA 5 HOH 102 602 602 HOH HOH I . 
EA 5 HOH 103 603 603 HOH HOH I . 
EA 5 HOH 104 604 604 HOH HOH I . 
EA 5 HOH 105 605 605 HOH HOH I . 
EA 5 HOH 106 606 606 HOH HOH I . 
EA 5 HOH 107 607 607 HOH HOH I . 
EA 5 HOH 108 608 608 HOH HOH I . 
EA 5 HOH 109 609 609 HOH HOH I . 
EA 5 HOH 110 610 610 HOH HOH I . 
EA 5 HOH 111 611 611 HOH HOH I . 
EA 5 HOH 112 612 612 HOH HOH I . 
EA 5 HOH 113 613 613 HOH HOH I . 
EA 5 HOH 114 614 614 HOH HOH I . 
EA 5 HOH 115 615 615 HOH HOH I . 
EA 5 HOH 116 616 616 HOH HOH I . 
EA 5 HOH 117 617 617 HOH HOH I . 
EA 5 HOH 118 618 618 HOH HOH I . 
EA 5 HOH 119 619 619 HOH HOH I . 
EA 5 HOH 120 620 620 HOH HOH I . 
EA 5 HOH 121 621 621 HOH HOH I . 
EA 5 HOH 122 622 622 HOH HOH I . 
EA 5 HOH 123 623 623 HOH HOH I . 
EA 5 HOH 124 624 624 HOH HOH I . 
EA 5 HOH 125 625 625 HOH HOH I . 
EA 5 HOH 126 626 626 HOH HOH I . 
EA 5 HOH 127 627 627 HOH HOH I . 
EA 5 HOH 128 628 628 HOH HOH I . 
EA 5 HOH 129 629 629 HOH HOH I . 
EA 5 HOH 130 630 630 HOH HOH I . 
EA 5 HOH 131 631 631 HOH HOH I . 
EA 5 HOH 132 632 632 HOH HOH I . 
EA 5 HOH 133 633 633 HOH HOH I . 
EA 5 HOH 134 634 634 HOH HOH I . 
EA 5 HOH 135 635 635 HOH HOH I . 
EA 5 HOH 136 636 636 HOH HOH I . 
EA 5 HOH 137 637 637 HOH HOH I . 
EA 5 HOH 138 638 638 HOH HOH I . 
EA 5 HOH 139 639 639 HOH HOH I . 
EA 5 HOH 140 640 640 HOH HOH I . 
EA 5 HOH 141 641 641 HOH HOH I . 
EA 5 HOH 142 642 642 HOH HOH I . 
EA 5 HOH 143 643 643 HOH HOH I . 
EA 5 HOH 144 644 644 HOH HOH I . 
EA 5 HOH 145 645 645 HOH HOH I . 
EA 5 HOH 146 646 646 HOH HOH I . 
EA 5 HOH 147 647 647 HOH HOH I . 
EA 5 HOH 148 648 648 HOH HOH I . 
EA 5 HOH 149 649 649 HOH HOH I . 
EA 5 HOH 150 650 650 HOH HOH I . 
EA 5 HOH 151 651 651 HOH HOH I . 
EA 5 HOH 152 652 652 HOH HOH I . 
EA 5 HOH 153 653 653 HOH HOH I . 
EA 5 HOH 154 654 654 HOH HOH I . 
EA 5 HOH 155 655 655 HOH HOH I . 
EA 5 HOH 156 656 656 HOH HOH I . 
EA 5 HOH 157 657 657 HOH HOH I . 
EA 5 HOH 158 658 658 HOH HOH I . 
EA 5 HOH 159 659 659 HOH HOH I . 
EA 5 HOH 160 660 660 HOH HOH I . 
EA 5 HOH 161 661 661 HOH HOH I . 
EA 5 HOH 162 662 662 HOH HOH I . 
EA 5 HOH 163 663 663 HOH HOH I . 
EA 5 HOH 164 664 664 HOH HOH I . 
EA 5 HOH 165 665 665 HOH HOH I . 
EA 5 HOH 166 666 666 HOH HOH I . 
EA 5 HOH 167 667 667 HOH HOH I . 
EA 5 HOH 168 668 668 HOH HOH I . 
EA 5 HOH 169 669 669 HOH HOH I . 
EA 5 HOH 170 670 670 HOH HOH I . 
EA 5 HOH 171 671 671 HOH HOH I . 
EA 5 HOH 172 672 672 HOH HOH I . 
EA 5 HOH 173 673 673 HOH HOH I . 
EA 5 HOH 174 674 674 HOH HOH I . 
EA 5 HOH 175 675 675 HOH HOH I . 
EA 5 HOH 176 676 676 HOH HOH I . 
EA 5 HOH 177 677 677 HOH HOH I . 
EA 5 HOH 178 678 678 HOH HOH I . 
EA 5 HOH 179 679 679 HOH HOH I . 
EA 5 HOH 180 680 680 HOH HOH I . 
EA 5 HOH 181 681 681 HOH HOH I . 
EA 5 HOH 182 682 682 HOH HOH I . 
EA 5 HOH 183 683 683 HOH HOH I . 
EA 5 HOH 184 684 684 HOH HOH I . 
EA 5 HOH 185 685 685 HOH HOH I . 
EA 5 HOH 186 686 686 HOH HOH I . 
EA 5 HOH 187 687 687 HOH HOH I . 
EA 5 HOH 188 688 688 HOH HOH I . 
EA 5 HOH 189 689 689 HOH HOH I . 
EA 5 HOH 190 690 690 HOH HOH I . 
EA 5 HOH 191 691 691 HOH HOH I . 
EA 5 HOH 192 692 692 HOH HOH I . 
EA 5 HOH 193 693 693 HOH HOH I . 
EA 5 HOH 194 694 694 HOH HOH I . 
EA 5 HOH 195 695 695 HOH HOH I . 
EA 5 HOH 196 696 696 HOH HOH I . 
EA 5 HOH 197 697 697 HOH HOH I . 
EA 5 HOH 198 698 698 HOH HOH I . 
EA 5 HOH 199 699 699 HOH HOH I . 
EA 5 HOH 200 700 700 HOH HOH I . 
EA 5 HOH 201 701 701 HOH HOH I . 
EA 5 HOH 202 702 702 HOH HOH I . 
EA 5 HOH 203 703 703 HOH HOH I . 
EA 5 HOH 204 704 704 HOH HOH I . 
EA 5 HOH 205 705 705 HOH HOH I . 
EA 5 HOH 206 706 706 HOH HOH I . 
EA 5 HOH 207 707 707 HOH HOH I . 
EA 5 HOH 208 708 708 HOH HOH I . 
EA 5 HOH 209 709 709 HOH HOH I . 
EA 5 HOH 210 710 710 HOH HOH I . 
EA 5 HOH 211 711 711 HOH HOH I . 
EA 5 HOH 212 712 712 HOH HOH I . 
EA 5 HOH 213 713 713 HOH HOH I . 
EA 5 HOH 214 714 714 HOH HOH I . 
EA 5 HOH 215 715 715 HOH HOH I . 
EA 5 HOH 216 716 716 HOH HOH I . 
EA 5 HOH 217 717 717 HOH HOH I . 
EA 5 HOH 218 718 718 HOH HOH I . 
EA 5 HOH 219 719 719 HOH HOH I . 
EA 5 HOH 220 720 720 HOH HOH I . 
EA 5 HOH 221 721 721 HOH HOH I . 
EA 5 HOH 222 722 722 HOH HOH I . 
EA 5 HOH 223 723 723 HOH HOH I . 
EA 5 HOH 224 724 724 HOH HOH I . 
EA 5 HOH 225 725 725 HOH HOH I . 
EA 5 HOH 226 726 726 HOH HOH I . 
EA 5 HOH 227 727 727 HOH HOH I . 
EA 5 HOH 228 728 728 HOH HOH I . 
EA 5 HOH 229 729 729 HOH HOH I . 
EA 5 HOH 230 730 730 HOH HOH I . 
EA 5 HOH 231 731 731 HOH HOH I . 
EA 5 HOH 232 732 732 HOH HOH I . 
EA 5 HOH 233 733 733 HOH HOH I . 
EA 5 HOH 234 734 734 HOH HOH I . 
EA 5 HOH 235 735 735 HOH HOH I . 
EA 5 HOH 236 736 736 HOH HOH I . 
EA 5 HOH 237 737 737 HOH HOH I . 
EA 5 HOH 238 738 738 HOH HOH I . 
EA 5 HOH 239 739 739 HOH HOH I . 
EA 5 HOH 240 740 740 HOH HOH I . 
EA 5 HOH 241 741 741 HOH HOH I . 
EA 5 HOH 242 742 742 HOH HOH I . 
EA 5 HOH 243 743 743 HOH HOH I . 
EA 5 HOH 244 744 744 HOH HOH I . 
EA 5 HOH 245 745 745 HOH HOH I . 
EA 5 HOH 246 746 746 HOH HOH I . 
EA 5 HOH 247 747 747 HOH HOH I . 
EA 5 HOH 248 748 748 HOH HOH I . 
EA 5 HOH 249 749 749 HOH HOH I . 
EA 5 HOH 250 750 750 HOH HOH I . 
EA 5 HOH 251 751 751 HOH HOH I . 
EA 5 HOH 252 752 752 HOH HOH I . 
EA 5 HOH 253 753 753 HOH HOH I . 
EA 5 HOH 254 754 754 HOH HOH I . 
EA 5 HOH 255 755 755 HOH HOH I . 
EA 5 HOH 256 756 756 HOH HOH I . 
EA 5 HOH 257 757 757 HOH HOH I . 
EA 5 HOH 258 758 758 HOH HOH I . 
EA 5 HOH 259 759 759 HOH HOH I . 
EA 5 HOH 260 760 760 HOH HOH I . 
EA 5 HOH 261 761 761 HOH HOH I . 
EA 5 HOH 262 762 762 HOH HOH I . 
EA 5 HOH 263 763 763 HOH HOH I . 
EA 5 HOH 264 764 764 HOH HOH I . 
EA 5 HOH 265 765 765 HOH HOH I . 
EA 5 HOH 266 766 766 HOH HOH I . 
EA 5 HOH 267 767 767 HOH HOH I . 
EA 5 HOH 268 768 768 HOH HOH I . 
EA 5 HOH 269 769 769 HOH HOH I . 
EA 5 HOH 270 770 770 HOH HOH I . 
EA 5 HOH 271 771 771 HOH HOH I . 
EA 5 HOH 272 772 772 HOH HOH I . 
EA 5 HOH 273 773 773 HOH HOH I . 
EA 5 HOH 274 774 774 HOH HOH I . 
EA 5 HOH 275 775 775 HOH HOH I . 
EA 5 HOH 276 776 776 HOH HOH I . 
EA 5 HOH 277 777 777 HOH HOH I . 
EA 5 HOH 278 778 778 HOH HOH I . 
EA 5 HOH 279 779 779 HOH HOH I . 
EA 5 HOH 280 780 780 HOH HOH I . 
EA 5 HOH 281 781 781 HOH HOH I . 
EA 5 HOH 282 782 782 HOH HOH I . 
EA 5 HOH 283 783 783 HOH HOH I . 
EA 5 HOH 284 784 784 HOH HOH I . 
EA 5 HOH 285 785 785 HOH HOH I . 
EA 5 HOH 286 786 786 HOH HOH I . 
EA 5 HOH 287 787 787 HOH HOH I . 
EA 5 HOH 288 788 788 HOH HOH I . 
EA 5 HOH 289 789 789 HOH HOH I . 
EA 5 HOH 290 790 790 HOH HOH I . 
EA 5 HOH 291 791 791 HOH HOH I . 
EA 5 HOH 292 792 792 HOH HOH I . 
EA 5 HOH 293 793 793 HOH HOH I . 
EA 5 HOH 294 794 794 HOH HOH I . 
EA 5 HOH 295 795 795 HOH HOH I . 
EA 5 HOH 296 796 796 HOH HOH I . 
EA 5 HOH 297 797 797 HOH HOH I . 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
4 author_defined_assembly ? monomeric 1 
5 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,F,G,H,I,AA   
2 1 B,J,K,L,M,BA   
3 1 C,N,O,P,Q,R,CA 
4 1 D,S,T,U,V,DA   
5 1 E,W,X,Y,Z,EA   
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     701 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   AA 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
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   ND1 ? A  HIS 47  ? A HIS 46  ? 1_555 CU A G CU . ? A CU 402 ? 1_555 NE2 ? A  HIS 49  ? A HIS 48  ? 1_555 143.2 ? 
2   ND1 ? A  HIS 47  ? A HIS 46  ? 1_555 CU A G CU . ? A CU 402 ? 1_555 NE2 ? A  HIS 121 ? A HIS 120 ? 1_555 100.8 ? 
3   NE2 ? A  HIS 49  ? A HIS 48  ? 1_555 CU A G CU . ? A CU 402 ? 1_555 NE2 ? A  HIS 121 ? A HIS 120 ? 1_555 113.7 ? 
4   ND1 ? A  HIS 47  ? A HIS 46  ? 1_555 CU B G CU . ? A CU 402 ? 1_555 NE2 ? A  HIS 49  ? A HIS 48  ? 1_555 126.8 ? 
5   ND1 ? A  HIS 47  ? A HIS 46  ? 1_555 CU B G CU . ? A CU 402 ? 1_555 NE2 ? A  HIS 64  ? A HIS 63  ? 1_555 79.7  ? 
6   NE2 ? A  HIS 49  ? A HIS 48  ? 1_555 CU B G CU . ? A CU 402 ? 1_555 NE2 ? A  HIS 64  ? A HIS 63  ? 1_555 100.8 ? 
7   ND1 ? A  HIS 47  ? A HIS 46  ? 1_555 CU B G CU . ? A CU 402 ? 1_555 NE2 ? A  HIS 121 ? A HIS 120 ? 1_555 95.1  ? 
8   NE2 ? A  HIS 49  ? A HIS 48  ? 1_555 CU B G CU . ? A CU 402 ? 1_555 NE2 ? A  HIS 121 ? A HIS 120 ? 1_555 105.1 ? 
9   NE2 ? A  HIS 64  ? A HIS 63  ? 1_555 CU B G CU . ? A CU 402 ? 1_555 NE2 ? A  HIS 121 ? A HIS 120 ? 1_555 150.8 ? 
10  ND1 ? A  HIS 64  ? A HIS 63  ? 1_555 ZN ? F ZN . ? A ZN 401 ? 1_555 ND1 ? A  HIS 72  ? A HIS 71  ? 1_555 107.5 ? 
11  ND1 ? A  HIS 64  ? A HIS 63  ? 1_555 ZN ? F ZN . ? A ZN 401 ? 1_555 ND1 ? A  HIS 81  ? A HIS 80  ? 1_555 113.9 ? 
12  ND1 ? A  HIS 72  ? A HIS 71  ? 1_555 ZN ? F ZN . ? A ZN 401 ? 1_555 ND1 ? A  HIS 81  ? A HIS 80  ? 1_555 124.7 ? 
13  ND1 ? A  HIS 64  ? A HIS 63  ? 1_555 ZN ? F ZN . ? A ZN 401 ? 1_555 OD1 B A  ASP 84  ? A ASP 83  ? 1_555 98.7  ? 
14  ND1 ? A  HIS 72  ? A HIS 71  ? 1_555 ZN ? F ZN . ? A ZN 401 ? 1_555 OD1 B A  ASP 84  ? A ASP 83  ? 1_555 82.6  ? 
15  ND1 ? A  HIS 81  ? A HIS 80  ? 1_555 ZN ? F ZN . ? A ZN 401 ? 1_555 OD1 B A  ASP 84  ? A ASP 83  ? 1_555 123.4 ? 
16  ND1 ? A  HIS 64  ? A HIS 63  ? 1_555 ZN ? F ZN . ? A ZN 401 ? 1_555 O   ? AA HOH .   ? A HOH 501 ? 1_555 76.4  ? 
17  ND1 ? A  HIS 72  ? A HIS 71  ? 1_555 ZN ? F ZN . ? A ZN 401 ? 1_555 O   ? AA HOH .   ? A HOH 501 ? 1_555 118.2 ? 
18  ND1 ? A  HIS 81  ? A HIS 80  ? 1_555 ZN ? F ZN . ? A ZN 401 ? 1_555 O   ? AA HOH .   ? A HOH 501 ? 1_555 106.2 ? 
19  OD1 B A  ASP 84  ? A ASP 83  ? 1_555 ZN ? F ZN . ? A ZN 401 ? 1_555 O   ? AA HOH .   ? A HOH 501 ? 1_555 37.8  ? 
20  ND1 ? A  HIS 216 ? A HIS 215 ? 1_555 CU A I CU . ? A CU 404 ? 1_555 NE2 ? A  HIS 218 ? A HIS 217 ? 1_555 144.9 ? 
21  ND1 ? A  HIS 216 ? A HIS 215 ? 1_555 CU A I CU . ? A CU 404 ? 1_555 NE2 ? A  HIS 290 ? A HIS 289 ? 1_555 94.7  ? 
22  NE2 ? A  HIS 218 ? A HIS 217 ? 1_555 CU A I CU . ? A CU 404 ? 1_555 NE2 ? A  HIS 290 ? A HIS 289 ? 1_555 119.9 ? 
23  ND1 ? A  HIS 216 ? A HIS 215 ? 1_555 CU B I CU . ? A CU 404 ? 1_555 NE2 ? A  HIS 233 ? A HIS 232 ? 1_555 91.9  ? 
24  ND1 ? A  HIS 216 ? A HIS 215 ? 1_555 CU B I CU . ? A CU 404 ? 1_555 NE2 ? A  HIS 290 ? A HIS 289 ? 1_555 93.9  ? 
25  NE2 ? A  HIS 233 ? A HIS 232 ? 1_555 CU B I CU . ? A CU 404 ? 1_555 NE2 ? A  HIS 290 ? A HIS 289 ? 1_555 173.9 ? 
26  ND1 ? A  HIS 216 ? A HIS 215 ? 1_555 CU B I CU . ? A CU 404 ? 1_555 O   ? AA HOH .   ? A HOH 567 ? 1_555 102.8 ? 
27  NE2 ? A  HIS 233 ? A HIS 232 ? 1_555 CU B I CU . ? A CU 404 ? 1_555 O   ? AA HOH .   ? A HOH 567 ? 1_555 87.9  ? 
28  NE2 ? A  HIS 290 ? A HIS 289 ? 1_555 CU B I CU . ? A CU 404 ? 1_555 O   ? AA HOH .   ? A HOH 567 ? 1_555 88.8  ? 
29  ND1 ? A  HIS 216 ? A HIS 215 ? 1_555 CU B I CU . ? A CU 404 ? 1_555 O   ? AA HOH .   ? A HOH 619 ? 1_555 159.7 ? 
30  NE2 ? A  HIS 233 ? A HIS 232 ? 1_555 CU B I CU . ? A CU 404 ? 1_555 O   ? AA HOH .   ? A HOH 619 ? 1_555 77.7  ? 
31  NE2 ? A  HIS 290 ? A HIS 289 ? 1_555 CU B I CU . ? A CU 404 ? 1_555 O   ? AA HOH .   ? A HOH 619 ? 1_555 96.2  ? 
32  O   ? AA HOH .   ? A HOH 567 ? 1_555 CU B I CU . ? A CU 404 ? 1_555 O   ? AA HOH .   ? A HOH 619 ? 1_555 59.9  ? 
33  ND1 ? A  HIS 233 ? A HIS 232 ? 1_555 ZN ? H ZN . ? A ZN 403 ? 1_555 ND1 ? A  HIS 241 ? A HIS 240 ? 1_555 111.8 ? 
34  ND1 ? A  HIS 233 ? A HIS 232 ? 1_555 ZN ? H ZN . ? A ZN 403 ? 1_555 ND1 ? A  HIS 250 ? A HIS 249 ? 1_555 104.6 ? 
35  ND1 ? A  HIS 241 ? A HIS 240 ? 1_555 ZN ? H ZN . ? A ZN 403 ? 1_555 ND1 ? A  HIS 250 ? A HIS 249 ? 1_555 127.1 ? 
36  ND1 ? A  HIS 233 ? A HIS 232 ? 1_555 ZN ? H ZN . ? A ZN 403 ? 1_555 OG  A A  SER 253 ? A SER 252 ? 1_555 117.2 ? 
37  ND1 ? A  HIS 241 ? A HIS 240 ? 1_555 ZN ? H ZN . ? A ZN 403 ? 1_555 OG  A A  SER 253 ? A SER 252 ? 1_555 82.7  ? 
38  ND1 ? A  HIS 250 ? A HIS 249 ? 1_555 ZN ? H ZN . ? A ZN 403 ? 1_555 OG  A A  SER 253 ? A SER 252 ? 1_555 113.2 ? 
39  ND1 ? A  HIS 233 ? A HIS 232 ? 1_555 ZN ? H ZN . ? A ZN 403 ? 1_555 OD1 B A  ASP 253 ? A ASP 252 ? 1_555 106.0 ? 
40  ND1 ? A  HIS 241 ? A HIS 240 ? 1_555 ZN ? H ZN . ? A ZN 403 ? 1_555 OD1 B A  ASP 253 ? A ASP 252 ? 1_555 89.9  ? 
41  ND1 ? A  HIS 250 ? A HIS 249 ? 1_555 ZN ? H ZN . ? A ZN 403 ? 1_555 OD1 B A  ASP 253 ? A ASP 252 ? 1_555 115.7 ? 
42  OG  A A  SER 253 ? A SER 252 ? 1_555 ZN ? H ZN . ? A ZN 403 ? 1_555 OD1 B A  ASP 253 ? A ASP 252 ? 1_555 11.6  ? 
43  ND1 ? B  HIS 47  ? C HIS 46  ? 1_555 CU ? K CU . ? C CU 402 ? 1_555 NE2 ? B  HIS 49  ? C HIS 48  ? 1_555 137.5 ? 
44  ND1 ? B  HIS 47  ? C HIS 46  ? 1_555 CU ? K CU . ? C CU 402 ? 1_555 NE2 ? B  HIS 121 ? C HIS 120 ? 1_555 107.1 ? 
45  NE2 ? B  HIS 49  ? C HIS 48  ? 1_555 CU ? K CU . ? C CU 402 ? 1_555 NE2 ? B  HIS 121 ? C HIS 120 ? 1_555 113.2 ? 
46  ND1 ? B  HIS 64  ? C HIS 63  ? 1_555 ZN ? J ZN . ? C ZN 401 ? 1_555 ND1 ? B  HIS 72  ? C HIS 71  ? 1_555 111.2 ? 
47  ND1 ? B  HIS 64  ? C HIS 63  ? 1_555 ZN ? J ZN . ? C ZN 401 ? 1_555 ND1 ? B  HIS 81  ? C HIS 80  ? 1_555 102.5 ? 
48  ND1 ? B  HIS 72  ? C HIS 71  ? 1_555 ZN ? J ZN . ? C ZN 401 ? 1_555 ND1 ? B  HIS 81  ? C HIS 80  ? 1_555 125.6 ? 
49  ND1 ? B  HIS 64  ? C HIS 63  ? 1_555 ZN ? J ZN . ? C ZN 401 ? 1_555 OG  A B  SER 84  ? C SER 83  ? 1_555 130.3 ? 
50  ND1 ? B  HIS 72  ? C HIS 71  ? 1_555 ZN ? J ZN . ? C ZN 401 ? 1_555 OG  A B  SER 84  ? C SER 83  ? 1_555 75.9  ? 
51  ND1 ? B  HIS 81  ? C HIS 80  ? 1_555 ZN ? J ZN . ? C ZN 401 ? 1_555 OG  A B  SER 84  ? C SER 83  ? 1_555 112.3 ? 
52  ND1 ? B  HIS 64  ? C HIS 63  ? 1_555 ZN ? J ZN . ? C ZN 401 ? 1_555 OD1 B B  ASP 84  ? C ASP 83  ? 1_555 122.1 ? 
53  ND1 ? B  HIS 72  ? C HIS 71  ? 1_555 ZN ? J ZN . ? C ZN 401 ? 1_555 OD1 B B  ASP 84  ? C ASP 83  ? 1_555 91.7  ? 
54  ND1 ? B  HIS 81  ? C HIS 80  ? 1_555 ZN ? J ZN . ? C ZN 401 ? 1_555 OD1 B B  ASP 84  ? C ASP 83  ? 1_555 105.1 ? 
55  OG  A B  SER 84  ? C SER 83  ? 1_555 ZN ? J ZN . ? C ZN 401 ? 1_555 OD1 B B  ASP 84  ? C ASP 83  ? 1_555 16.0  ? 
56  ND1 ? B  HIS 216 ? C HIS 215 ? 1_555 CU A M CU . ? C CU 404 ? 1_555 NE2 ? B  HIS 218 ? C HIS 217 ? 1_555 141.5 ? 
57  ND1 ? B  HIS 216 ? C HIS 215 ? 1_555 CU A M CU . ? C CU 404 ? 1_555 NE2 ? B  HIS 290 ? C HIS 289 ? 1_555 95.8  ? 
58  NE2 ? B  HIS 218 ? C HIS 217 ? 1_555 CU A M CU . ? C CU 404 ? 1_555 NE2 ? B  HIS 290 ? C HIS 289 ? 1_555 115.2 ? 
59  ND1 ? B  HIS 216 ? C HIS 215 ? 1_555 CU B M CU . ? C CU 404 ? 1_555 NE2 ? B  HIS 218 ? C HIS 217 ? 1_555 129.9 ? 
60  ND1 ? B  HIS 216 ? C HIS 215 ? 1_555 CU B M CU . ? C CU 404 ? 1_555 NE2 ? B  HIS 233 ? C HIS 232 ? 1_555 83.4  ? 
61  NE2 ? B  HIS 218 ? C HIS 217 ? 1_555 CU B M CU . ? C CU 404 ? 1_555 NE2 ? B  HIS 233 ? C HIS 232 ? 1_555 103.0 ? 
62  ND1 ? B  HIS 216 ? C HIS 215 ? 1_555 CU B M CU . ? C CU 404 ? 1_555 NE2 ? B  HIS 290 ? C HIS 289 ? 1_555 91.4  ? 
63  NE2 ? B  HIS 218 ? C HIS 217 ? 1_555 CU B M CU . ? C CU 404 ? 1_555 NE2 ? B  HIS 290 ? C HIS 289 ? 1_555 103.5 ? 
64  NE2 ? B  HIS 233 ? C HIS 232 ? 1_555 CU B M CU . ? C CU 404 ? 1_555 NE2 ? B  HIS 290 ? C HIS 289 ? 1_555 149.2 ? 
65  ND1 ? B  HIS 216 ? C HIS 215 ? 1_555 CU B M CU . ? C CU 404 ? 1_555 O   ? BA HOH .   ? C HOH 565 ? 1_555 131.3 ? 
66  NE2 ? B  HIS 218 ? C HIS 217 ? 1_555 CU B M CU . ? C CU 404 ? 1_555 O   ? BA HOH .   ? C HOH 565 ? 1_555 96.9  ? 
67  NE2 ? B  HIS 233 ? C HIS 232 ? 1_555 CU B M CU . ? C CU 404 ? 1_555 O   ? BA HOH .   ? C HOH 565 ? 1_555 71.9  ? 
68  NE2 ? B  HIS 290 ? C HIS 289 ? 1_555 CU B M CU . ? C CU 404 ? 1_555 O   ? BA HOH .   ? C HOH 565 ? 1_555 89.5  ? 
69  ND1 ? B  HIS 233 ? C HIS 232 ? 1_555 ZN ? L ZN . ? C ZN 403 ? 1_555 ND1 ? B  HIS 241 ? C HIS 240 ? 1_555 114.1 ? 
70  ND1 ? B  HIS 233 ? C HIS 232 ? 1_555 ZN ? L ZN . ? C ZN 403 ? 1_555 ND1 ? B  HIS 250 ? C HIS 249 ? 1_555 105.2 ? 
71  ND1 ? B  HIS 241 ? C HIS 240 ? 1_555 ZN ? L ZN . ? C ZN 403 ? 1_555 ND1 ? B  HIS 250 ? C HIS 249 ? 1_555 121.4 ? 
72  ND1 ? B  HIS 233 ? C HIS 232 ? 1_555 ZN ? L ZN . ? C ZN 403 ? 1_555 OG  A B  SER 253 ? C SER 252 ? 1_555 128.7 ? 
73  ND1 ? B  HIS 241 ? C HIS 240 ? 1_555 ZN ? L ZN . ? C ZN 403 ? 1_555 OG  A B  SER 253 ? C SER 252 ? 1_555 73.1  ? 
74  ND1 ? B  HIS 250 ? C HIS 249 ? 1_555 ZN ? L ZN . ? C ZN 403 ? 1_555 OG  A B  SER 253 ? C SER 252 ? 1_555 113.0 ? 
75  ND1 ? B  HIS 233 ? C HIS 232 ? 1_555 ZN ? L ZN . ? C ZN 403 ? 1_555 OD1 B B  ASP 253 ? C ASP 252 ? 1_555 118.7 ? 
76  ND1 ? B  HIS 241 ? C HIS 240 ? 1_555 ZN ? L ZN . ? C ZN 403 ? 1_555 OD1 B B  ASP 253 ? C ASP 252 ? 1_555 95.1  ? 
77  ND1 ? B  HIS 250 ? C HIS 249 ? 1_555 ZN ? L ZN . ? C ZN 403 ? 1_555 OD1 B B  ASP 253 ? C ASP 252 ? 1_555 102.3 ? 
78  OG  A B  SER 253 ? C SER 252 ? 1_555 ZN ? L ZN . ? C ZN 403 ? 1_555 OD1 B B  ASP 253 ? C ASP 252 ? 1_555 22.0  ? 
79  ND1 ? C  HIS 47  ? E HIS 46  ? 1_555 CU A O CU . ? E CU 402 ? 1_555 NE2 ? C  HIS 49  ? E HIS 48  ? 1_555 137.4 ? 
80  ND1 ? C  HIS 47  ? E HIS 46  ? 1_555 CU A O CU . ? E CU 402 ? 1_555 NE2 ? C  HIS 121 ? E HIS 120 ? 1_555 100.7 ? 
81  NE2 ? C  HIS 49  ? E HIS 48  ? 1_555 CU A O CU . ? E CU 402 ? 1_555 NE2 ? C  HIS 121 ? E HIS 120 ? 1_555 112.9 ? 
82  ND1 ? C  HIS 47  ? E HIS 46  ? 1_555 CU B O CU . ? E CU 402 ? 1_555 NE2 ? C  HIS 49  ? E HIS 48  ? 1_555 127.0 ? 
83  ND1 ? C  HIS 47  ? E HIS 46  ? 1_555 CU B O CU . ? E CU 402 ? 1_555 NE2 ? C  HIS 64  ? E HIS 63  ? 1_555 80.5  ? 
84  NE2 ? C  HIS 49  ? E HIS 48  ? 1_555 CU B O CU . ? E CU 402 ? 1_555 NE2 ? C  HIS 64  ? E HIS 63  ? 1_555 103.5 ? 
85  ND1 ? C  HIS 47  ? E HIS 46  ? 1_555 CU B O CU . ? E CU 402 ? 1_555 NE2 ? C  HIS 121 ? E HIS 120 ? 1_555 94.5  ? 
86  NE2 ? C  HIS 49  ? E HIS 48  ? 1_555 CU B O CU . ? E CU 402 ? 1_555 NE2 ? C  HIS 121 ? E HIS 120 ? 1_555 103.2 ? 
87  NE2 ? C  HIS 64  ? E HIS 63  ? 1_555 CU B O CU . ? E CU 402 ? 1_555 NE2 ? C  HIS 121 ? E HIS 120 ? 1_555 149.7 ? 
88  ND1 ? C  HIS 47  ? E HIS 46  ? 1_555 CU B O CU . ? E CU 402 ? 1_555 O   ? CA HOH .   ? E HOH 623 ? 1_555 130.5 ? 
89  NE2 ? C  HIS 49  ? E HIS 48  ? 1_555 CU B O CU . ? E CU 402 ? 1_555 O   ? CA HOH .   ? E HOH 623 ? 1_555 99.6  ? 
90  NE2 ? C  HIS 64  ? E HIS 63  ? 1_555 CU B O CU . ? E CU 402 ? 1_555 O   ? CA HOH .   ? E HOH 623 ? 1_555 72.6  ? 
91  NE2 ? C  HIS 121 ? E HIS 120 ? 1_555 CU B O CU . ? E CU 402 ? 1_555 O   ? CA HOH .   ? E HOH 623 ? 1_555 89.1  ? 
92  ND1 ? C  HIS 64  ? E HIS 63  ? 1_555 ZN ? N ZN . ? E ZN 401 ? 1_555 ND1 ? C  HIS 72  ? E HIS 71  ? 1_555 109.1 ? 
93  ND1 ? C  HIS 64  ? E HIS 63  ? 1_555 ZN ? N ZN . ? E ZN 401 ? 1_555 ND1 ? C  HIS 81  ? E HIS 80  ? 1_555 108.7 ? 
94  ND1 ? C  HIS 72  ? E HIS 71  ? 1_555 ZN ? N ZN . ? E ZN 401 ? 1_555 ND1 ? C  HIS 81  ? E HIS 80  ? 1_555 123.9 ? 
95  ND1 ? C  HIS 64  ? E HIS 63  ? 1_555 ZN ? N ZN . ? E ZN 401 ? 1_555 OG  A C  SER 84  ? E SER 83  ? 1_555 121.1 ? 
96  ND1 ? C  HIS 72  ? E HIS 71  ? 1_555 ZN ? N ZN . ? E ZN 401 ? 1_555 OG  A C  SER 84  ? E SER 83  ? 1_555 75.6  ? 
97  ND1 ? C  HIS 81  ? E HIS 80  ? 1_555 ZN ? N ZN . ? E ZN 401 ? 1_555 OG  A C  SER 84  ? E SER 83  ? 1_555 115.8 ? 
98  ND1 ? C  HIS 64  ? E HIS 63  ? 1_555 ZN ? N ZN . ? E ZN 401 ? 1_555 OD1 B C  ASP 84  ? E ASP 83  ? 1_555 112.2 ? 
99  ND1 ? C  HIS 72  ? E HIS 71  ? 1_555 ZN ? N ZN . ? E ZN 401 ? 1_555 OD1 B C  ASP 84  ? E ASP 83  ? 1_555 89.6  ? 
100 ND1 ? C  HIS 81  ? E HIS 80  ? 1_555 ZN ? N ZN . ? E ZN 401 ? 1_555 OD1 B C  ASP 84  ? E ASP 83  ? 1_555 112.2 ? 
101 OG  A C  SER 84  ? E SER 83  ? 1_555 ZN ? N ZN . ? E ZN 401 ? 1_555 OD1 B C  ASP 84  ? E ASP 83  ? 1_555 14.8  ? 
102 ND1 ? C  HIS 216 ? E HIS 215 ? 1_555 CU A Q CU . ? E CU 404 ? 1_555 NE2 ? C  HIS 218 ? E HIS 217 ? 1_555 139.7 ? 
103 ND1 ? C  HIS 216 ? E HIS 215 ? 1_555 CU A Q CU . ? E CU 404 ? 1_555 NE2 ? C  HIS 290 ? E HIS 289 ? 1_555 98.0  ? 
104 NE2 ? C  HIS 218 ? E HIS 217 ? 1_555 CU A Q CU . ? E CU 404 ? 1_555 NE2 ? C  HIS 290 ? E HIS 289 ? 1_555 115.7 ? 
105 ND1 ? C  HIS 216 ? E HIS 215 ? 1_555 CU B Q CU . ? E CU 404 ? 1_555 NE2 ? C  HIS 218 ? E HIS 217 ? 1_555 126.7 ? 
106 ND1 ? C  HIS 216 ? E HIS 215 ? 1_555 CU B Q CU . ? E CU 404 ? 1_555 NE2 ? C  HIS 233 ? E HIS 232 ? 1_555 88.5  ? 
107 NE2 ? C  HIS 218 ? E HIS 217 ? 1_555 CU B Q CU . ? E CU 404 ? 1_555 NE2 ? C  HIS 233 ? E HIS 232 ? 1_555 100.2 ? 
108 ND1 ? C  HIS 216 ? E HIS 215 ? 1_555 CU B Q CU . ? E CU 404 ? 1_555 NE2 ? C  HIS 290 ? E HIS 289 ? 1_555 94.1  ? 
109 NE2 ? C  HIS 218 ? E HIS 217 ? 1_555 CU B Q CU . ? E CU 404 ? 1_555 NE2 ? C  HIS 290 ? E HIS 289 ? 1_555 100.1 ? 
110 NE2 ? C  HIS 233 ? E HIS 232 ? 1_555 CU B Q CU . ? E CU 404 ? 1_555 NE2 ? C  HIS 290 ? E HIS 289 ? 1_555 152.5 ? 
111 ND1 ? C  HIS 216 ? E HIS 215 ? 1_555 CU B Q CU . ? E CU 404 ? 1_555 O   ? CA HOH .   ? E HOH 575 ? 1_555 89.2  ? 
112 NE2 ? C  HIS 218 ? E HIS 217 ? 1_555 CU B Q CU . ? E CU 404 ? 1_555 O   ? CA HOH .   ? E HOH 575 ? 1_555 143.7 ? 
113 NE2 ? C  HIS 233 ? E HIS 232 ? 1_555 CU B Q CU . ? E CU 404 ? 1_555 O   ? CA HOH .   ? E HOH 575 ? 1_555 72.4  ? 
114 NE2 ? C  HIS 290 ? E HIS 289 ? 1_555 CU B Q CU . ? E CU 404 ? 1_555 O   ? CA HOH .   ? E HOH 575 ? 1_555 80.2  ? 
115 ND1 ? C  HIS 216 ? E HIS 215 ? 1_555 CU B Q CU . ? E CU 404 ? 1_555 O   ? CA HOH .   ? E HOH 662 ? 1_555 140.4 ? 
116 NE2 ? C  HIS 218 ? E HIS 217 ? 1_555 CU B Q CU . ? E CU 404 ? 1_555 O   ? CA HOH .   ? E HOH 662 ? 1_555 91.2  ? 
117 NE2 ? C  HIS 233 ? E HIS 232 ? 1_555 CU B Q CU . ? E CU 404 ? 1_555 O   ? CA HOH .   ? E HOH 662 ? 1_555 72.0  ? 
118 NE2 ? C  HIS 290 ? E HIS 289 ? 1_555 CU B Q CU . ? E CU 404 ? 1_555 O   ? CA HOH .   ? E HOH 662 ? 1_555 89.2  ? 
119 O   ? CA HOH .   ? E HOH 575 ? 1_555 CU B Q CU . ? E CU 404 ? 1_555 O   ? CA HOH .   ? E HOH 662 ? 1_555 52.5  ? 
120 ND1 ? C  HIS 233 ? E HIS 232 ? 1_555 ZN ? P ZN . ? E ZN 403 ? 1_555 ND1 ? C  HIS 241 ? E HIS 240 ? 1_555 112.9 ? 
121 ND1 ? C  HIS 233 ? E HIS 232 ? 1_555 ZN ? P ZN . ? E ZN 403 ? 1_555 ND1 ? C  HIS 250 ? E HIS 249 ? 1_555 108.9 ? 
122 ND1 ? C  HIS 241 ? E HIS 240 ? 1_555 ZN ? P ZN . ? E ZN 403 ? 1_555 ND1 ? C  HIS 250 ? E HIS 249 ? 1_555 122.9 ? 
123 ND1 ? C  HIS 233 ? E HIS 232 ? 1_555 ZN ? P ZN . ? E ZN 403 ? 1_555 OG  A C  SER 253 ? E SER 252 ? 1_555 125.9 ? 
124 ND1 ? C  HIS 241 ? E HIS 240 ? 1_555 ZN ? P ZN . ? E ZN 403 ? 1_555 OG  A C  SER 253 ? E SER 252 ? 1_555 75.0  ? 
125 ND1 ? C  HIS 250 ? E HIS 249 ? 1_555 ZN ? P ZN . ? E ZN 403 ? 1_555 OG  A C  SER 253 ? E SER 252 ? 1_555 109.0 ? 
126 ND1 ? C  HIS 233 ? E HIS 232 ? 1_555 ZN ? P ZN . ? E ZN 403 ? 1_555 OD1 B C  ASP 253 ? E ASP 252 ? 1_555 107.8 ? 
127 ND1 ? C  HIS 241 ? E HIS 240 ? 1_555 ZN ? P ZN . ? E ZN 403 ? 1_555 OD1 B C  ASP 253 ? E ASP 252 ? 1_555 91.0  ? 
128 ND1 ? C  HIS 250 ? E HIS 249 ? 1_555 ZN ? P ZN . ? E ZN 403 ? 1_555 OD1 B C  ASP 253 ? E ASP 252 ? 1_555 111.3 ? 
129 OG  A C  SER 253 ? E SER 252 ? 1_555 ZN ? P ZN . ? E ZN 403 ? 1_555 OD1 B C  ASP 253 ? E ASP 252 ? 1_555 20.7  ? 
130 ND1 ? D  HIS 47  ? G HIS 46  ? 1_555 CU A T CU . ? G CU 402 ? 1_555 NE2 ? D  HIS 49  ? G HIS 48  ? 1_555 141.3 ? 
131 ND1 ? D  HIS 47  ? G HIS 46  ? 1_555 CU A T CU . ? G CU 402 ? 1_555 NE2 ? D  HIS 121 ? G HIS 120 ? 1_555 94.4  ? 
132 NE2 ? D  HIS 49  ? G HIS 48  ? 1_555 CU A T CU . ? G CU 402 ? 1_555 NE2 ? D  HIS 121 ? G HIS 120 ? 1_555 116.0 ? 
133 ND1 ? D  HIS 47  ? G HIS 46  ? 1_555 CU B T CU . ? G CU 402 ? 1_555 NE2 ? D  HIS 49  ? G HIS 48  ? 1_555 130.0 ? 
134 ND1 ? D  HIS 47  ? G HIS 46  ? 1_555 CU B T CU . ? G CU 402 ? 1_555 NE2 ? D  HIS 64  ? G HIS 63  ? 1_555 89.4  ? 
135 NE2 ? D  HIS 49  ? G HIS 48  ? 1_555 CU B T CU . ? G CU 402 ? 1_555 NE2 ? D  HIS 64  ? G HIS 63  ? 1_555 101.2 ? 
136 ND1 ? D  HIS 47  ? G HIS 46  ? 1_555 CU B T CU . ? G CU 402 ? 1_555 NE2 ? D  HIS 121 ? G HIS 120 ? 1_555 90.0  ? 
137 NE2 ? D  HIS 49  ? G HIS 48  ? 1_555 CU B T CU . ? G CU 402 ? 1_555 NE2 ? D  HIS 121 ? G HIS 120 ? 1_555 100.9 ? 
138 NE2 ? D  HIS 64  ? G HIS 63  ? 1_555 CU B T CU . ? G CU 402 ? 1_555 NE2 ? D  HIS 121 ? G HIS 120 ? 1_555 151.5 ? 
139 ND1 ? D  HIS 47  ? G HIS 46  ? 1_555 CU B T CU . ? G CU 402 ? 1_555 O   ? DA HOH .   ? G HOH 595 ? 1_555 134.2 ? 
140 NE2 ? D  HIS 49  ? G HIS 48  ? 1_555 CU B T CU . ? G CU 402 ? 1_555 O   ? DA HOH .   ? G HOH 595 ? 1_555 94.9  ? 
141 NE2 ? D  HIS 64  ? G HIS 63  ? 1_555 CU B T CU . ? G CU 402 ? 1_555 O   ? DA HOH .   ? G HOH 595 ? 1_555 70.6  ? 
142 NE2 ? D  HIS 121 ? G HIS 120 ? 1_555 CU B T CU . ? G CU 402 ? 1_555 O   ? DA HOH .   ? G HOH 595 ? 1_555 89.9  ? 
143 ND1 ? D  HIS 64  ? G HIS 63  ? 1_555 ZN ? S ZN . ? G ZN 401 ? 1_555 ND1 ? D  HIS 72  ? G HIS 71  ? 1_555 112.9 ? 
144 ND1 ? D  HIS 64  ? G HIS 63  ? 1_555 ZN ? S ZN . ? G ZN 401 ? 1_555 ND1 ? D  HIS 81  ? G HIS 80  ? 1_555 111.8 ? 
145 ND1 ? D  HIS 72  ? G HIS 71  ? 1_555 ZN ? S ZN . ? G ZN 401 ? 1_555 ND1 ? D  HIS 81  ? G HIS 80  ? 1_555 120.4 ? 
146 ND1 ? D  HIS 64  ? G HIS 63  ? 1_555 ZN ? S ZN . ? G ZN 401 ? 1_555 OD1 B D  ASP 84  ? G ASP 83  ? 1_555 107.0 ? 
147 ND1 ? D  HIS 72  ? G HIS 71  ? 1_555 ZN ? S ZN . ? G ZN 401 ? 1_555 OD1 B D  ASP 84  ? G ASP 83  ? 1_555 86.5  ? 
148 ND1 ? D  HIS 81  ? G HIS 80  ? 1_555 ZN ? S ZN . ? G ZN 401 ? 1_555 OD1 B D  ASP 84  ? G ASP 83  ? 1_555 115.2 ? 
149 ND1 ? D  HIS 216 ? G HIS 215 ? 1_555 CU A V CU . ? G CU 404 ? 1_555 NE2 ? D  HIS 218 ? G HIS 217 ? 1_555 138.2 ? 
150 ND1 ? D  HIS 216 ? G HIS 215 ? 1_555 CU A V CU . ? G CU 404 ? 1_555 NE2 ? D  HIS 290 ? G HIS 289 ? 1_555 98.5  ? 
151 NE2 ? D  HIS 218 ? G HIS 217 ? 1_555 CU A V CU . ? G CU 404 ? 1_555 NE2 ? D  HIS 290 ? G HIS 289 ? 1_555 111.3 ? 
152 ND1 ? D  HIS 216 ? G HIS 215 ? 1_555 CU B V CU . ? G CU 404 ? 1_555 NE2 ? D  HIS 218 ? G HIS 217 ? 1_555 131.3 ? 
153 ND1 ? D  HIS 216 ? G HIS 215 ? 1_555 CU B V CU . ? G CU 404 ? 1_555 NE2 ? D  HIS 233 ? G HIS 232 ? 1_555 81.6  ? 
154 NE2 ? D  HIS 218 ? G HIS 217 ? 1_555 CU B V CU . ? G CU 404 ? 1_555 NE2 ? D  HIS 233 ? G HIS 232 ? 1_555 102.8 ? 
155 ND1 ? D  HIS 216 ? G HIS 215 ? 1_555 CU B V CU . ? G CU 404 ? 1_555 NE2 ? D  HIS 290 ? G HIS 289 ? 1_555 94.2  ? 
156 NE2 ? D  HIS 218 ? G HIS 217 ? 1_555 CU B V CU . ? G CU 404 ? 1_555 NE2 ? D  HIS 290 ? G HIS 289 ? 1_555 100.5 ? 
157 NE2 ? D  HIS 233 ? G HIS 232 ? 1_555 CU B V CU . ? G CU 404 ? 1_555 NE2 ? D  HIS 290 ? G HIS 289 ? 1_555 152.2 ? 
158 ND1 ? D  HIS 216 ? G HIS 215 ? 1_555 CU B V CU . ? G CU 404 ? 1_555 O   ? DA HOH .   ? G HOH 565 ? 1_555 126.1 ? 
159 NE2 ? D  HIS 218 ? G HIS 217 ? 1_555 CU B V CU . ? G CU 404 ? 1_555 O   ? DA HOH .   ? G HOH 565 ? 1_555 101.2 ? 
160 NE2 ? D  HIS 233 ? G HIS 232 ? 1_555 CU B V CU . ? G CU 404 ? 1_555 O   ? DA HOH .   ? G HOH 565 ? 1_555 74.6  ? 
161 NE2 ? D  HIS 290 ? G HIS 289 ? 1_555 CU B V CU . ? G CU 404 ? 1_555 O   ? DA HOH .   ? G HOH 565 ? 1_555 86.3  ? 
162 ND1 ? D  HIS 233 ? G HIS 232 ? 1_555 ZN ? U ZN . ? G ZN 403 ? 1_555 ND1 ? D  HIS 241 ? G HIS 240 ? 1_555 110.7 ? 
163 ND1 ? D  HIS 233 ? G HIS 232 ? 1_555 ZN ? U ZN . ? G ZN 403 ? 1_555 ND1 ? D  HIS 250 ? G HIS 249 ? 1_555 111.3 ? 
164 ND1 ? D  HIS 241 ? G HIS 240 ? 1_555 ZN ? U ZN . ? G ZN 403 ? 1_555 ND1 ? D  HIS 250 ? G HIS 249 ? 1_555 126.1 ? 
165 ND1 ? D  HIS 233 ? G HIS 232 ? 1_555 ZN ? U ZN . ? G ZN 403 ? 1_555 OD1 B D  ASP 253 ? G ASP 252 ? 1_555 104.1 ? 
166 ND1 ? D  HIS 241 ? G HIS 240 ? 1_555 ZN ? U ZN . ? G ZN 403 ? 1_555 OD1 B D  ASP 253 ? G ASP 252 ? 1_555 79.2  ? 
167 ND1 ? D  HIS 250 ? G HIS 249 ? 1_555 ZN ? U ZN . ? G ZN 403 ? 1_555 OD1 B D  ASP 253 ? G ASP 252 ? 1_555 120.2 ? 
168 ND1 ? E  HIS 47  ? I HIS 46  ? 1_555 CU A X CU . ? I CU 402 ? 1_555 NE2 ? E  HIS 49  ? I HIS 48  ? 1_555 138.7 ? 
169 ND1 ? E  HIS 47  ? I HIS 46  ? 1_555 CU A X CU . ? I CU 402 ? 1_555 NE2 ? E  HIS 121 ? I HIS 120 ? 1_555 99.8  ? 
170 NE2 ? E  HIS 49  ? I HIS 48  ? 1_555 CU A X CU . ? I CU 402 ? 1_555 NE2 ? E  HIS 121 ? I HIS 120 ? 1_555 115.4 ? 
171 ND1 ? E  HIS 47  ? I HIS 46  ? 1_555 CU B X CU . ? I CU 402 ? 1_555 NE2 ? E  HIS 49  ? I HIS 48  ? 1_555 127.1 ? 
172 ND1 ? E  HIS 47  ? I HIS 46  ? 1_555 CU B X CU . ? I CU 402 ? 1_555 NE2 ? E  HIS 64  ? I HIS 63  ? 1_555 90.3  ? 
173 NE2 ? E  HIS 49  ? I HIS 48  ? 1_555 CU B X CU . ? I CU 402 ? 1_555 NE2 ? E  HIS 64  ? I HIS 63  ? 1_555 101.5 ? 
174 ND1 ? E  HIS 47  ? I HIS 46  ? 1_555 CU B X CU . ? I CU 402 ? 1_555 NE2 ? E  HIS 121 ? I HIS 120 ? 1_555 94.7  ? 
175 NE2 ? E  HIS 49  ? I HIS 48  ? 1_555 CU B X CU . ? I CU 402 ? 1_555 NE2 ? E  HIS 121 ? I HIS 120 ? 1_555 99.1  ? 
176 NE2 ? E  HIS 64  ? I HIS 63  ? 1_555 CU B X CU . ? I CU 402 ? 1_555 NE2 ? E  HIS 121 ? I HIS 120 ? 1_555 149.6 ? 
177 ND1 ? E  HIS 47  ? I HIS 46  ? 1_555 CU B X CU . ? I CU 402 ? 1_555 O   ? EA HOH .   ? I HOH 605 ? 1_555 89.4  ? 
178 NE2 ? E  HIS 49  ? I HIS 48  ? 1_555 CU B X CU . ? I CU 402 ? 1_555 O   ? EA HOH .   ? I HOH 605 ? 1_555 143.4 ? 
179 NE2 ? E  HIS 64  ? I HIS 63  ? 1_555 CU B X CU . ? I CU 402 ? 1_555 O   ? EA HOH .   ? I HOH 605 ? 1_555 73.3  ? 
180 NE2 ? E  HIS 121 ? I HIS 120 ? 1_555 CU B X CU . ? I CU 402 ? 1_555 O   ? EA HOH .   ? I HOH 605 ? 1_555 76.8  ? 
181 ND1 ? E  HIS 64  ? I HIS 63  ? 1_555 ZN ? W ZN . ? I ZN 401 ? 1_555 ND1 ? E  HIS 72  ? I HIS 71  ? 1_555 113.0 ? 
182 ND1 ? E  HIS 64  ? I HIS 63  ? 1_555 ZN ? W ZN . ? I ZN 401 ? 1_555 ND1 ? E  HIS 81  ? I HIS 80  ? 1_555 107.7 ? 
183 ND1 ? E  HIS 72  ? I HIS 71  ? 1_555 ZN ? W ZN . ? I ZN 401 ? 1_555 ND1 ? E  HIS 81  ? I HIS 80  ? 1_555 122.5 ? 
184 ND1 ? E  HIS 64  ? I HIS 63  ? 1_555 ZN ? W ZN . ? I ZN 401 ? 1_555 OG  A E  SER 84  ? I SER 83  ? 1_555 124.3 ? 
185 ND1 ? E  HIS 72  ? I HIS 71  ? 1_555 ZN ? W ZN . ? I ZN 401 ? 1_555 OG  A E  SER 84  ? I SER 83  ? 1_555 78.9  ? 
186 ND1 ? E  HIS 81  ? I HIS 80  ? 1_555 ZN ? W ZN . ? I ZN 401 ? 1_555 OG  A E  SER 84  ? I SER 83  ? 1_555 109.2 ? 
187 ND1 ? E  HIS 64  ? I HIS 63  ? 1_555 ZN ? W ZN . ? I ZN 401 ? 1_555 OD1 B E  ASP 84  ? I ASP 83  ? 1_555 108.0 ? 
188 ND1 ? E  HIS 72  ? I HIS 71  ? 1_555 ZN ? W ZN . ? I ZN 401 ? 1_555 OD1 B E  ASP 84  ? I ASP 83  ? 1_555 93.6  ? 
189 ND1 ? E  HIS 81  ? I HIS 80  ? 1_555 ZN ? W ZN . ? I ZN 401 ? 1_555 OD1 B E  ASP 84  ? I ASP 83  ? 1_555 110.6 ? 
190 OG  A E  SER 84  ? I SER 83  ? 1_555 ZN ? W ZN . ? I ZN 401 ? 1_555 OD1 B E  ASP 84  ? I ASP 83  ? 1_555 18.6  ? 
191 ND1 ? E  HIS 216 ? I HIS 215 ? 1_555 CU A Z CU . ? I CU 404 ? 1_555 NE2 ? E  HIS 218 ? I HIS 217 ? 1_555 141.1 ? 
192 ND1 ? E  HIS 216 ? I HIS 215 ? 1_555 CU A Z CU . ? I CU 404 ? 1_555 NE2 ? E  HIS 290 ? I HIS 289 ? 1_555 102.6 ? 
193 NE2 ? E  HIS 218 ? I HIS 217 ? 1_555 CU A Z CU . ? I CU 404 ? 1_555 NE2 ? E  HIS 290 ? I HIS 289 ? 1_555 111.6 ? 
194 ND1 ? E  HIS 216 ? I HIS 215 ? 1_555 CU B Z CU . ? I CU 404 ? 1_555 NE2 ? E  HIS 218 ? I HIS 217 ? 1_555 127.0 ? 
195 ND1 ? E  HIS 216 ? I HIS 215 ? 1_555 CU B Z CU . ? I CU 404 ? 1_555 NE2 ? E  HIS 233 ? I HIS 232 ? 1_555 80.1  ? 
196 NE2 ? E  HIS 218 ? I HIS 217 ? 1_555 CU B Z CU . ? I CU 404 ? 1_555 NE2 ? E  HIS 233 ? I HIS 232 ? 1_555 102.0 ? 
197 ND1 ? E  HIS 216 ? I HIS 215 ? 1_555 CU B Z CU . ? I CU 404 ? 1_555 NE2 ? E  HIS 290 ? I HIS 289 ? 1_555 96.0  ? 
198 NE2 ? E  HIS 218 ? I HIS 217 ? 1_555 CU B Z CU . ? I CU 404 ? 1_555 NE2 ? E  HIS 290 ? I HIS 289 ? 1_555 103.0 ? 
199 NE2 ? E  HIS 233 ? I HIS 232 ? 1_555 CU B Z CU . ? I CU 404 ? 1_555 NE2 ? E  HIS 290 ? I HIS 289 ? 1_555 151.2 ? 
200 ND1 ? E  HIS 216 ? I HIS 215 ? 1_555 CU B Z CU . ? I CU 404 ? 1_555 O   ? EA HOH .   ? I HOH 543 ? 1_555 125.2 ? 
201 NE2 ? E  HIS 218 ? I HIS 217 ? 1_555 CU B Z CU . ? I CU 404 ? 1_555 O   ? EA HOH .   ? I HOH 543 ? 1_555 103.9 ? 
202 NE2 ? E  HIS 233 ? I HIS 232 ? 1_555 CU B Z CU . ? I CU 404 ? 1_555 O   ? EA HOH .   ? I HOH 543 ? 1_555 69.7  ? 
203 NE2 ? E  HIS 290 ? I HIS 289 ? 1_555 CU B Z CU . ? I CU 404 ? 1_555 O   ? EA HOH .   ? I HOH 543 ? 1_555 90.5  ? 
204 ND1 ? E  HIS 233 ? I HIS 232 ? 1_555 ZN ? Y ZN . ? I ZN 403 ? 1_555 ND1 ? E  HIS 241 ? I HIS 240 ? 1_555 107.8 ? 
205 ND1 ? E  HIS 233 ? I HIS 232 ? 1_555 ZN ? Y ZN . ? I ZN 403 ? 1_555 ND1 ? E  HIS 250 ? I HIS 249 ? 1_555 108.2 ? 
206 ND1 ? E  HIS 241 ? I HIS 240 ? 1_555 ZN ? Y ZN . ? I ZN 403 ? 1_555 ND1 ? E  HIS 250 ? I HIS 249 ? 1_555 119.9 ? 
207 ND1 ? E  HIS 233 ? I HIS 232 ? 1_555 ZN ? Y ZN . ? I ZN 403 ? 1_555 OG  A E  SER 253 ? I SER 252 ? 1_555 122.1 ? 
208 ND1 ? E  HIS 241 ? I HIS 240 ? 1_555 ZN ? Y ZN . ? I ZN 403 ? 1_555 OG  A E  SER 253 ? I SER 252 ? 1_555 78.7  ? 
209 ND1 ? E  HIS 250 ? I HIS 249 ? 1_555 ZN ? Y ZN . ? I ZN 403 ? 1_555 OG  A E  SER 253 ? I SER 252 ? 1_555 117.6 ? 
210 ND1 ? E  HIS 233 ? I HIS 232 ? 1_555 ZN ? Y ZN . ? I ZN 403 ? 1_555 OD1 B E  ASP 253 ? I ASP 252 ? 1_555 119.0 ? 
211 ND1 ? E  HIS 241 ? I HIS 240 ? 1_555 ZN ? Y ZN . ? I ZN 403 ? 1_555 OD1 B E  ASP 253 ? I ASP 252 ? 1_555 94.4  ? 
212 ND1 ? E  HIS 250 ? I HIS 249 ? 1_555 ZN ? Y ZN . ? I ZN 403 ? 1_555 OD1 B E  ASP 253 ? I ASP 252 ? 1_555 107.7 ? 
213 OG  A E  SER 253 ? I SER 252 ? 1_555 ZN ? Y ZN . ? I ZN 403 ? 1_555 OD1 B E  ASP 253 ? I ASP 252 ? 1_555 15.9  ? 
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2019-06-19 
# 
_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         ? 
# 
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       ? ? ? ? ? ? ? ? ? ? ? REFMAC   ? ? ? 5.8.0230 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .        4 
# 
_pdbx_entry_details.entry_id             6DTK 
_pdbx_entry_details.nonpolymer_details   ? 
_pdbx_entry_details.sequence_details     ? 
_pdbx_entry_details.compound_details     
;Chimeric construct: mutated and WT protein chains are linked via linker and form a heterodimer. Due to almost two fold symmetry of the heterodimer and structural similarity to the WT protein (or possible admixture of homodimers formed due to broken linker), the crystal electron density shows an average picture with fractional mixed DS populations on positions 83 and 252.
;
_pdbx_entry_details.source_details       ? 
# 
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   C SER 83  ? A N C LEU 84  ? ? 1.74 
2  1 O   G HOH 529 ? ? O G HOH 701 ? ? 1.99 
3  1 O   G HOH 770 ? ? O G HOH 808 ? ? 2.07 
4  1 O   A HOH 691 ? ? O A HOH 709 ? ? 2.08 
5  1 O   E HOH 780 ? ? O E HOH 831 ? ? 2.10 
6  1 O   E HOH 736 ? ? O E HOH 754 ? ? 2.11 
7  1 ND2 G ASN 53  ? A O G HOH 501 ? ? 2.11 
8  1 O   E HOH 696 ? ? O E HOH 750 ? ? 2.14 
9  1 ND1 A HIS 279 ? ? O A HOH 502 ? ? 2.14 
10 1 O   I HOH 511 ? ? O I HOH 661 ? ? 2.14 
11 1 O   G HOH 743 ? ? O I HOH 738 ? ? 2.15 
12 1 O   I HOH 748 ? ? O I HOH 762 ? ? 2.15 
13 1 O   E GLN 322 ? ? O E HOH 501 ? ? 2.15 
14 1 ND1 A HIS 110 ? ? O A HOH 503 ? ? 2.15 
15 1 O   G HOH 687 ? ? O G HOH 774 ? ? 2.16 
16 1 O   G HOH 770 ? ? O G HOH 805 ? ? 2.16 
17 1 ND2 I ASN 53  ? ? O I HOH 501 ? ? 2.16 
18 1 O   C HOH 611 ? ? O C HOH 612 ? ? 2.17 
19 1 OE1 G GLU 132 ? B O G HOH 502 ? ? 2.17 
20 1 O   I HOH 774 ? ? O I HOH 780 ? ? 2.19 
21 1 ND2 E ASN 222 ? B O E HOH 502 ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    G 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     657 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    I 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     712 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   3_455 
_pdbx_validate_symm_contact.dist              2.14 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            C 
_pdbx_validate_rmsd_bond.auth_asym_id_1            C 
_pdbx_validate_rmsd_bond.auth_comp_id_1            SER 
_pdbx_validate_rmsd_bond.auth_seq_id_1             83 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            A 
_pdbx_validate_rmsd_bond.auth_atom_id_2            O 
_pdbx_validate_rmsd_bond.auth_asym_id_2            C 
_pdbx_validate_rmsd_bond.auth_comp_id_2            SER 
_pdbx_validate_rmsd_bond.auth_seq_id_2             83 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            A 
_pdbx_validate_rmsd_bond.bond_value                1.097 
_pdbx_validate_rmsd_bond.bond_target_value         1.229 
_pdbx_validate_rmsd_bond.bond_deviation            -0.132 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.019 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 O  C SER 83  ? A C  C SER 83  ? A N  C LEU 84  ? ? 97.02 122.70 -25.68 1.60 Y 
2 1 CA G GLU 132 ? ? CB G GLU 132 ? ? CG G GLU 132 ? A 95.04 113.40 -18.36 2.20 N 
3 1 CA G GLU 132 ? ? CB G GLU 132 ? ? CG G GLU 132 ? B 98.61 113.40 -14.79 2.20 N 
4 1 CA G SER 271 ? ? CB G SER 271 ? ? OG G SER 271 ? A 93.69 111.20 -17.51 2.70 N 
5 1 CA G SER 271 ? ? CB G SER 271 ? ? OG G SER 271 ? B 92.71 111.20 -18.49 2.70 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASN A 65  ? ? -152.99 65.02   
2  1 PRO A 74  ? ? -60.25  -70.47  
3  1 ASP A 76  ? ? -173.16 128.13  
4  1 ASN A 131 ? ? -69.22  -179.33 
5  1 LYS A 136 ? ? -131.26 -44.70  
6  1 GLN A 153 ? ? -56.13  96.71   
7  1 ASN A 195 ? ? -149.68 22.97   
8  1 GLU C 40  ? ? -38.14  131.53  
9  1 ALA C 55  ? ? -106.58 42.34   
10 1 GLN C 153 ? ? -8.18   126.97  
11 1 SER C 194 ? ? -29.43  131.27  
12 1 ASN C 195 ? ? -0.75   72.88   
13 1 ASN C 234 ? ? -140.62 59.16   
14 1 ASN G 65  ? ? -148.15 59.03   
15 1 ASN I 26  ? ? 85.54   -55.38  
16 1 ASN I 65  ? ? -144.82 59.56   
17 1 GLN I 153 ? ? -62.54  68.14   
18 1 ALA I 170 ? ? 178.87  162.69  
19 1 ASP I 259 ? ? -78.78  -169.51 
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   ASN 
_pdbx_validate_peptide_omega.auth_asym_id_1   C 
_pdbx_validate_peptide_omega.auth_seq_id_1    195 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_2   C 
_pdbx_validate_peptide_omega.auth_seq_id_2    196 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            149.58 
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             SER 
_pdbx_validate_main_chain_plane.auth_asym_id             C 
_pdbx_validate_main_chain_plane.auth_seq_id              83 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             A 
_pdbx_validate_main_chain_plane.improper_torsion_angle   17.58 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? E HOH 867 ? 6.93 . 
2 1 O ? E HOH 868 ? 7.71 . 
3 1 O ? G HOH 822 ? 6.54 . 
4 1 O ? G HOH 823 ? 6.57 . 
5 1 O ? G HOH 824 ? 7.15 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 0   ? A MET 1   
2  1 Y 1 A ALA 156 ? A ALA 157 
3  1 Y 1 A ALA 157 ? A ALA 158 
4  1 Y 1 A SER 158 ? A SER 159 
5  1 Y 1 A GLY 159 ? A GLY 160 
6  1 Y 1 A GLY 160 ? A GLY 161 
7  1 Y 1 A GLY 161 ? A GLY 162 
8  1 Y 1 A GLY 162 ? A GLY 163 
9  1 Y 1 A GLY 163 ? A GLY 164 
10 1 Y 1 A SER 164 ? A SER 165 
11 1 Y 1 A GLY 165 ? A GLY 166 
12 1 Y 1 C MET 0   ? B MET 1   
13 1 Y 1 C ALA 155 ? B ALA 156 
14 1 Y 1 C ALA 156 ? B ALA 157 
15 1 Y 1 C ALA 157 ? B ALA 158 
16 1 Y 1 C SER 158 ? B SER 159 
17 1 Y 1 C GLY 159 ? B GLY 160 
18 1 Y 1 C GLY 160 ? B GLY 161 
19 1 Y 1 C GLY 161 ? B GLY 162 
20 1 Y 1 C GLY 162 ? B GLY 163 
21 1 Y 1 C GLY 163 ? B GLY 164 
22 1 Y 1 C SER 164 ? B SER 165 
23 1 Y 1 C GLY 165 ? B GLY 166 
24 1 Y 1 E MET 0   ? C MET 1   
25 1 Y 1 E ALA 157 ? C ALA 158 
26 1 Y 1 E SER 158 ? C SER 159 
27 1 Y 1 E GLY 159 ? C GLY 160 
28 1 Y 1 E GLY 160 ? C GLY 161 
29 1 Y 1 E GLY 161 ? C GLY 162 
30 1 Y 1 E GLY 162 ? C GLY 163 
31 1 Y 1 E GLY 163 ? C GLY 164 
32 1 Y 1 E SER 164 ? C SER 165 
33 1 Y 1 E GLY 165 ? C GLY 166 
34 1 Y 1 G MET 0   ? D MET 1   
35 1 Y 1 G ALA 157 ? D ALA 158 
36 1 Y 1 G SER 158 ? D SER 159 
37 1 Y 1 G GLY 159 ? D GLY 160 
38 1 Y 1 G GLY 160 ? D GLY 161 
39 1 Y 1 G GLY 161 ? D GLY 162 
40 1 Y 1 G GLY 162 ? D GLY 163 
41 1 Y 1 G GLY 163 ? D GLY 164 
42 1 Y 1 G SER 164 ? D SER 165 
43 1 Y 1 G GLY 165 ? D GLY 166 
44 1 Y 1 I MET 0   ? E MET 1   
45 1 Y 1 I ALA 157 ? E ALA 158 
46 1 Y 1 I SER 158 ? E SER 159 
47 1 Y 1 I GLY 159 ? E GLY 160 
48 1 Y 1 I GLY 160 ? E GLY 161 
49 1 Y 1 I GLY 161 ? E GLY 162 
50 1 Y 1 I GLY 162 ? E GLY 163 
51 1 Y 1 I GLY 163 ? E GLY 164 
52 1 Y 1 I SER 164 ? E SER 165 
53 1 Y 1 I GLY 165 ? E GLY 166 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'        ZN  
3 'COPPER (II) ION' CU  
4 'MALONATE ION'    MLI 
5 water             HOH 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'native gel electrophoresis' 
_pdbx_struct_assembly_auth_evidence.details                'HETERODIMER FORMED VIA LINKER' 
# 
