data_3S11
# 
_entry.id   3S11 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.281 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   3S11         
RCSB  RCSB065625   
WWPDB D_1000065625 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 3S12 . unspecified 
PDB 3S13 . unspecified 
# 
_pdbx_database_status.entry_id                        3S11 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.recvd_initial_deposition_date   2011-05-14 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'DuBois, R.M.'  1 
'Zaraket, H.'   2 
'Reddivari, M.' 3 
'Heath, R.J.'   4 
'White, S.W.'   5 
'Russell, C.J.' 6 
# 
_citation.id                        primary 
_citation.title                     'Acid stability of the hemagglutinin protein regulates H5N1 influenza virus pathogenicity.' 
_citation.journal_abbrev            'Plos Pathog.' 
_citation.journal_volume            7 
_citation.page_first                e1002398 
_citation.page_last                 e1002398 
_citation.year                      2011 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           1553-7366 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   22144894 
_citation.pdbx_database_id_DOI      10.1371/journal.ppat.1002398 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'DuBois, R.M.'  1 
primary 'Zaraket, H.'   2 
primary 'Reddivari, M.' 3 
primary 'Heath, R.J.'   4 
primary 'White, S.W.'   5 
primary 'Russell, C.J.' 6 
# 
_cell.entry_id           3S11 
_cell.length_a           69.365 
_cell.length_b           241.054 
_cell.length_c           70.061 
_cell.angle_alpha        90.00 
_cell.angle_beta         116.69 
_cell.angle_gamma        90.00 
_cell.Z_PDB              6 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         3S11 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
# 
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 'Hemagglutinin HA1 chain'        37140.812 3   ? ? ? ? 
2 polymer     man 'Hemagglutinin HA2 chain'        20937.143 3   ? ? ? ? 
3 non-polymer man N-ACETYL-D-GLUCOSAMINE           221.208   9   ? ? ? ? 
4 non-polymer syn GLYCEROL                         92.094    3   ? ? ? ? 
5 non-polymer syn 'TRIS(HYDROXYETHYL)AMINOMETHANE' 163.215   1   ? ? ? ? 
6 non-polymer man BETA-D-MANNOSE                   180.156   1   ? ? ? ? 
7 water       nat water                            18.015    133 ? ? ? ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;DLGSADPGDQICIGYHANNSTEQVDTIMEKNVTVTHAQDILEKTHNGKLCDLDGVKPLILRDCSVAGWLLGNPMCDEFIN
VPEWSYIVEKASPANDLCYPGDFNNYEELKHLLSRTNHFEKIQIIPKSSWSNHDASSGVSSACPYHGKSSFFRNVVWLIK
KNSAYPTIKRSYNNTNQEDLLVLWGIHHPNDAAEQTKLYQNPTTYISVGTSTLNQRLVPEIATRPKVNGQSGRMEFFWTI
LKPNDAINFESNGNFIAPEYAYKIVKKGDSAIMKSELEYGNCNTKCQTPMGAINSSMPFHNIHPLTIGECPKYVKSNRLV
LATGLRNTPQR
;
;DLGSADPGDQICIGYHANNSTEQVDTIMEKNVTVTHAQDILEKTHNGKLCDLDGVKPLILRDCSVAGWLLGNPMCDEFIN
VPEWSYIVEKASPANDLCYPGDFNNYEELKHLLSRTNHFEKIQIIPKSSWSNHDASSGVSSACPYHGKSSFFRNVVWLIK
KNSAYPTIKRSYNNTNQEDLLVLWGIHHPNDAAEQTKLYQNPTTYISVGTSTLNQRLVPEIATRPKVNGQSGRMEFFWTI
LKPNDAINFESNGNFIAPEYAYKIVKKGDSAIMKSELEYGNCNTKCQTPMGAINSSMPFHNIHPLTIGECPKYVKSNRLV
LATGLRNTPQR
;
A,C,E ? 
2 'polypeptide(L)' no no 
;GLFGAIAGFIEGGWQGMVDGWYGYHHSNEQGSGYAADKESTQKAIDGVTNKVNSIIDKMNTQFEAVGREFNNLERRIENL
NKKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVKNLYDKVRLQLRDNAKELGNGCFEFYHKCDNECMESVKNGTYDYP
QYSEEARLNREEISGVRSLVPR
;
;GLFGAIAGFIEGGWQGMVDGWYGYHHSNEQGSGYAADKESTQKAIDGVTNKVNSIIDKMNTQFEAVGREFNNLERRIENL
NKKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVKNLYDKVRLQLRDNAKELGNGCFEFYHKCDNECMESVKNGTYDYP
QYSEEARLNREEISGVRSLVPR
;
B,D,F ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ASP n 
1 2   LEU n 
1 3   GLY n 
1 4   SER n 
1 5   ALA n 
1 6   ASP n 
1 7   PRO n 
1 8   GLY n 
1 9   ASP n 
1 10  GLN n 
1 11  ILE n 
1 12  CYS n 
1 13  ILE n 
1 14  GLY n 
1 15  TYR n 
1 16  HIS n 
1 17  ALA n 
1 18  ASN n 
1 19  ASN n 
1 20  SER n 
1 21  THR n 
1 22  GLU n 
1 23  GLN n 
1 24  VAL n 
1 25  ASP n 
1 26  THR n 
1 27  ILE n 
1 28  MET n 
1 29  GLU n 
1 30  LYS n 
1 31  ASN n 
1 32  VAL n 
1 33  THR n 
1 34  VAL n 
1 35  THR n 
1 36  HIS n 
1 37  ALA n 
1 38  GLN n 
1 39  ASP n 
1 40  ILE n 
1 41  LEU n 
1 42  GLU n 
1 43  LYS n 
1 44  THR n 
1 45  HIS n 
1 46  ASN n 
1 47  GLY n 
1 48  LYS n 
1 49  LEU n 
1 50  CYS n 
1 51  ASP n 
1 52  LEU n 
1 53  ASP n 
1 54  GLY n 
1 55  VAL n 
1 56  LYS n 
1 57  PRO n 
1 58  LEU n 
1 59  ILE n 
1 60  LEU n 
1 61  ARG n 
1 62  ASP n 
1 63  CYS n 
1 64  SER n 
1 65  VAL n 
1 66  ALA n 
1 67  GLY n 
1 68  TRP n 
1 69  LEU n 
1 70  LEU n 
1 71  GLY n 
1 72  ASN n 
1 73  PRO n 
1 74  MET n 
1 75  CYS n 
1 76  ASP n 
1 77  GLU n 
1 78  PHE n 
1 79  ILE n 
1 80  ASN n 
1 81  VAL n 
1 82  PRO n 
1 83  GLU n 
1 84  TRP n 
1 85  SER n 
1 86  TYR n 
1 87  ILE n 
1 88  VAL n 
1 89  GLU n 
1 90  LYS n 
1 91  ALA n 
1 92  SER n 
1 93  PRO n 
1 94  ALA n 
1 95  ASN n 
1 96  ASP n 
1 97  LEU n 
1 98  CYS n 
1 99  TYR n 
1 100 PRO n 
1 101 GLY n 
1 102 ASP n 
1 103 PHE n 
1 104 ASN n 
1 105 ASN n 
1 106 TYR n 
1 107 GLU n 
1 108 GLU n 
1 109 LEU n 
1 110 LYS n 
1 111 HIS n 
1 112 LEU n 
1 113 LEU n 
1 114 SER n 
1 115 ARG n 
1 116 THR n 
1 117 ASN n 
1 118 HIS n 
1 119 PHE n 
1 120 GLU n 
1 121 LYS n 
1 122 ILE n 
1 123 GLN n 
1 124 ILE n 
1 125 ILE n 
1 126 PRO n 
1 127 LYS n 
1 128 SER n 
1 129 SER n 
1 130 TRP n 
1 131 SER n 
1 132 ASN n 
1 133 HIS n 
1 134 ASP n 
1 135 ALA n 
1 136 SER n 
1 137 SER n 
1 138 GLY n 
1 139 VAL n 
1 140 SER n 
1 141 SER n 
1 142 ALA n 
1 143 CYS n 
1 144 PRO n 
1 145 TYR n 
1 146 HIS n 
1 147 GLY n 
1 148 LYS n 
1 149 SER n 
1 150 SER n 
1 151 PHE n 
1 152 PHE n 
1 153 ARG n 
1 154 ASN n 
1 155 VAL n 
1 156 VAL n 
1 157 TRP n 
1 158 LEU n 
1 159 ILE n 
1 160 LYS n 
1 161 LYS n 
1 162 ASN n 
1 163 SER n 
1 164 ALA n 
1 165 TYR n 
1 166 PRO n 
1 167 THR n 
1 168 ILE n 
1 169 LYS n 
1 170 ARG n 
1 171 SER n 
1 172 TYR n 
1 173 ASN n 
1 174 ASN n 
1 175 THR n 
1 176 ASN n 
1 177 GLN n 
1 178 GLU n 
1 179 ASP n 
1 180 LEU n 
1 181 LEU n 
1 182 VAL n 
1 183 LEU n 
1 184 TRP n 
1 185 GLY n 
1 186 ILE n 
1 187 HIS n 
1 188 HIS n 
1 189 PRO n 
1 190 ASN n 
1 191 ASP n 
1 192 ALA n 
1 193 ALA n 
1 194 GLU n 
1 195 GLN n 
1 196 THR n 
1 197 LYS n 
1 198 LEU n 
1 199 TYR n 
1 200 GLN n 
1 201 ASN n 
1 202 PRO n 
1 203 THR n 
1 204 THR n 
1 205 TYR n 
1 206 ILE n 
1 207 SER n 
1 208 VAL n 
1 209 GLY n 
1 210 THR n 
1 211 SER n 
1 212 THR n 
1 213 LEU n 
1 214 ASN n 
1 215 GLN n 
1 216 ARG n 
1 217 LEU n 
1 218 VAL n 
1 219 PRO n 
1 220 GLU n 
1 221 ILE n 
1 222 ALA n 
1 223 THR n 
1 224 ARG n 
1 225 PRO n 
1 226 LYS n 
1 227 VAL n 
1 228 ASN n 
1 229 GLY n 
1 230 GLN n 
1 231 SER n 
1 232 GLY n 
1 233 ARG n 
1 234 MET n 
1 235 GLU n 
1 236 PHE n 
1 237 PHE n 
1 238 TRP n 
1 239 THR n 
1 240 ILE n 
1 241 LEU n 
1 242 LYS n 
1 243 PRO n 
1 244 ASN n 
1 245 ASP n 
1 246 ALA n 
1 247 ILE n 
1 248 ASN n 
1 249 PHE n 
1 250 GLU n 
1 251 SER n 
1 252 ASN n 
1 253 GLY n 
1 254 ASN n 
1 255 PHE n 
1 256 ILE n 
1 257 ALA n 
1 258 PRO n 
1 259 GLU n 
1 260 TYR n 
1 261 ALA n 
1 262 TYR n 
1 263 LYS n 
1 264 ILE n 
1 265 VAL n 
1 266 LYS n 
1 267 LYS n 
1 268 GLY n 
1 269 ASP n 
1 270 SER n 
1 271 ALA n 
1 272 ILE n 
1 273 MET n 
1 274 LYS n 
1 275 SER n 
1 276 GLU n 
1 277 LEU n 
1 278 GLU n 
1 279 TYR n 
1 280 GLY n 
1 281 ASN n 
1 282 CYS n 
1 283 ASN n 
1 284 THR n 
1 285 LYS n 
1 286 CYS n 
1 287 GLN n 
1 288 THR n 
1 289 PRO n 
1 290 MET n 
1 291 GLY n 
1 292 ALA n 
1 293 ILE n 
1 294 ASN n 
1 295 SER n 
1 296 SER n 
1 297 MET n 
1 298 PRO n 
1 299 PHE n 
1 300 HIS n 
1 301 ASN n 
1 302 ILE n 
1 303 HIS n 
1 304 PRO n 
1 305 LEU n 
1 306 THR n 
1 307 ILE n 
1 308 GLY n 
1 309 GLU n 
1 310 CYS n 
1 311 PRO n 
1 312 LYS n 
1 313 TYR n 
1 314 VAL n 
1 315 LYS n 
1 316 SER n 
1 317 ASN n 
1 318 ARG n 
1 319 LEU n 
1 320 VAL n 
1 321 LEU n 
1 322 ALA n 
1 323 THR n 
1 324 GLY n 
1 325 LEU n 
1 326 ARG n 
1 327 ASN n 
1 328 THR n 
1 329 PRO n 
1 330 GLN n 
1 331 ARG n 
2 1   GLY n 
2 2   LEU n 
2 3   PHE n 
2 4   GLY n 
2 5   ALA n 
2 6   ILE n 
2 7   ALA n 
2 8   GLY n 
2 9   PHE n 
2 10  ILE n 
2 11  GLU n 
2 12  GLY n 
2 13  GLY n 
2 14  TRP n 
2 15  GLN n 
2 16  GLY n 
2 17  MET n 
2 18  VAL n 
2 19  ASP n 
2 20  GLY n 
2 21  TRP n 
2 22  TYR n 
2 23  GLY n 
2 24  TYR n 
2 25  HIS n 
2 26  HIS n 
2 27  SER n 
2 28  ASN n 
2 29  GLU n 
2 30  GLN n 
2 31  GLY n 
2 32  SER n 
2 33  GLY n 
2 34  TYR n 
2 35  ALA n 
2 36  ALA n 
2 37  ASP n 
2 38  LYS n 
2 39  GLU n 
2 40  SER n 
2 41  THR n 
2 42  GLN n 
2 43  LYS n 
2 44  ALA n 
2 45  ILE n 
2 46  ASP n 
2 47  GLY n 
2 48  VAL n 
2 49  THR n 
2 50  ASN n 
2 51  LYS n 
2 52  VAL n 
2 53  ASN n 
2 54  SER n 
2 55  ILE n 
2 56  ILE n 
2 57  ASP n 
2 58  LYS n 
2 59  MET n 
2 60  ASN n 
2 61  THR n 
2 62  GLN n 
2 63  PHE n 
2 64  GLU n 
2 65  ALA n 
2 66  VAL n 
2 67  GLY n 
2 68  ARG n 
2 69  GLU n 
2 70  PHE n 
2 71  ASN n 
2 72  ASN n 
2 73  LEU n 
2 74  GLU n 
2 75  ARG n 
2 76  ARG n 
2 77  ILE n 
2 78  GLU n 
2 79  ASN n 
2 80  LEU n 
2 81  ASN n 
2 82  LYS n 
2 83  LYS n 
2 84  MET n 
2 85  GLU n 
2 86  ASP n 
2 87  GLY n 
2 88  PHE n 
2 89  LEU n 
2 90  ASP n 
2 91  VAL n 
2 92  TRP n 
2 93  THR n 
2 94  TYR n 
2 95  ASN n 
2 96  ALA n 
2 97  GLU n 
2 98  LEU n 
2 99  LEU n 
2 100 VAL n 
2 101 LEU n 
2 102 MET n 
2 103 GLU n 
2 104 ASN n 
2 105 GLU n 
2 106 ARG n 
2 107 THR n 
2 108 LEU n 
2 109 ASP n 
2 110 PHE n 
2 111 HIS n 
2 112 ASP n 
2 113 SER n 
2 114 ASN n 
2 115 VAL n 
2 116 LYS n 
2 117 ASN n 
2 118 LEU n 
2 119 TYR n 
2 120 ASP n 
2 121 LYS n 
2 122 VAL n 
2 123 ARG n 
2 124 LEU n 
2 125 GLN n 
2 126 LEU n 
2 127 ARG n 
2 128 ASP n 
2 129 ASN n 
2 130 ALA n 
2 131 LYS n 
2 132 GLU n 
2 133 LEU n 
2 134 GLY n 
2 135 ASN n 
2 136 GLY n 
2 137 CYS n 
2 138 PHE n 
2 139 GLU n 
2 140 PHE n 
2 141 TYR n 
2 142 HIS n 
2 143 LYS n 
2 144 CYS n 
2 145 ASP n 
2 146 ASN n 
2 147 GLU n 
2 148 CYS n 
2 149 MET n 
2 150 GLU n 
2 151 SER n 
2 152 VAL n 
2 153 LYS n 
2 154 ASN n 
2 155 GLY n 
2 156 THR n 
2 157 TYR n 
2 158 ASP n 
2 159 TYR n 
2 160 PRO n 
2 161 GLN n 
2 162 TYR n 
2 163 SER n 
2 164 GLU n 
2 165 GLU n 
2 166 ALA n 
2 167 ARG n 
2 168 LEU n 
2 169 ASN n 
2 170 ARG n 
2 171 GLU n 
2 172 GLU n 
2 173 ILE n 
2 174 SER n 
2 175 GLY n 
2 176 VAL n 
2 177 ARG n 
2 178 SER n 
2 179 LEU n 
2 180 VAL n 
2 181 PRO n 
2 182 ARG 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 ? ? ? ? ? ? ? 'A/Goose/Hong Kong/437-10/1999 (H5N1)' ? ? ? ? 'Influenza A virus' 11320 ? ? ? ? ? ? ? 'fall armyworm' 
'Spodoptera frugiperda' 7108 ? ? ? ? ? ? Sf9 ? ? ? ? ? ? ? baculovirus ? ? ? pAcGP67B ? ? 
2 1 sample ? ? ? ? ? ? ? 'A/Goose/Hong Kong/437-10/1999 (H5N1)' ? ? ? ? 'Influenza A virus' 11320 ? ? ? ? ? ? ? 'fall armyworm' 
'Spodoptera frugiperda' 7108 ? ? ? ? ? ? Sf9 ? ? ? ? ? ? ? baculovirus ? ? ? pAcGP67B ? ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
_struct_ref.pdbx_db_isoform 
1 UNP Q9EA62_9INFA Q9EA62 1 
;DQICIGYHANNSTEQVDTIMEKNVTVTHAQDILEKTHNGKLCDLDGVKPLILRDCSVAGWLLGNPMCDEFINVPEWSYIV
EKASPANDLCYPGDFNNYEELKHLLSRTNHFEKIQIIPKSSWSNHDASSGVSSACPYHGKSSFFRNVVWLIKKNSAYPTI
KRSYNNTNQEDLLVLWGIHHPNDAAEQTKLYQNPTTYISVGTSTLNQRLVPEIATRPKVNGQSGRMEFFWTILKPNDAIN
FESNGNFIAPEYAYKIVKKGDSAIMKSELEYGNCNTKCQTPMGAINSSMPFHNIHPLTIGECPKYVKSNRLVLATGLRNT
PQR
;
17  ? 
2 UNP Q9EA62_9INFA Q9EA62 2 
;GLFGAIAGFIEGGWQGMVDGWYGYHHSNEQGSGYAADKESTQKAIDGVTNKVNSIIDKMNTQFEAVGREFNNLERRIENL
NKKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVKNLYDKVRLQLRDNAKELGNGCFEFYHKCDNECMESVKNGTYDYP
QYSEEARLNREEISGV
;
347 ? 
# 
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 3S11 A 9 ? 331 ? Q9EA62 17  ? 339 ? 11 326 
2 2 3S11 B 1 ? 176 ? Q9EA62 347 ? 522 ? 1  176 
3 1 3S11 C 9 ? 331 ? Q9EA62 17  ? 339 ? 11 326 
4 2 3S11 D 1 ? 176 ? Q9EA62 347 ? 522 ? 1  176 
5 1 3S11 E 9 ? 331 ? Q9EA62 17  ? 339 ? 11 326 
6 2 3S11 F 1 ? 176 ? Q9EA62 347 ? 522 ? 1  176 
# 
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 3S11 ASP A 1   ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 3   1  
1 3S11 LEU A 2   ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 4   2  
1 3S11 GLY A 3   ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 5   3  
1 3S11 SER A 4   ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 6   4  
1 3S11 ALA A 5   ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 7   5  
1 3S11 ASP A 6   ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 8   6  
1 3S11 PRO A 7   ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 9   7  
1 3S11 GLY A 8   ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 10  8  
2 3S11 ARG B 177 ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 177 9  
2 3S11 SER B 178 ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 178 10 
2 3S11 LEU B 179 ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 179 11 
2 3S11 VAL B 180 ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 180 12 
2 3S11 PRO B 181 ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 181 13 
2 3S11 ARG B 182 ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 182 14 
3 3S11 ASP C 1   ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 3   15 
3 3S11 LEU C 2   ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 4   16 
3 3S11 GLY C 3   ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 5   17 
3 3S11 SER C 4   ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 6   18 
3 3S11 ALA C 5   ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 7   19 
3 3S11 ASP C 6   ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 8   20 
3 3S11 PRO C 7   ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 9   21 
3 3S11 GLY C 8   ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 10  22 
4 3S11 ARG D 177 ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 177 23 
4 3S11 SER D 178 ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 178 24 
4 3S11 LEU D 179 ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 179 25 
4 3S11 VAL D 180 ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 180 26 
4 3S11 PRO D 181 ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 181 27 
4 3S11 ARG D 182 ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 182 28 
5 3S11 ASP E 1   ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 3   29 
5 3S11 LEU E 2   ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 4   30 
5 3S11 GLY E 3   ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 5   31 
5 3S11 SER E 4   ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 6   32 
5 3S11 ALA E 5   ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 7   33 
5 3S11 ASP E 6   ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 8   34 
5 3S11 PRO E 7   ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 9   35 
5 3S11 GLY E 8   ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 10  36 
6 3S11 ARG F 177 ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 177 37 
6 3S11 SER F 178 ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 178 38 
6 3S11 LEU F 179 ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 179 39 
6 3S11 VAL F 180 ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 180 40 
6 3S11 PRO F 181 ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 181 41 
6 3S11 ARG F 182 ? UNP Q9EA62 ? ? 'EXPRESSION TAG' 182 42 
# 
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 
BMA D-saccharide        . BETA-D-MANNOSE                   ?                               'C6 H12 O6'      180.156 
CYS 'L-peptide linking' y CYSTEINE                         ?                               'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE                        ?                               'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                  ?                               'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                          ?                               'C2 H5 N O2'     75.067  
GOL non-polymer         . GLYCEROL                         'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE                        ?                               'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                            ?                               'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                       ?                               'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                          ?                               'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                           ?                               'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                       ?                               'C5 H11 N O2 S'  149.211 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE           ?                               'C8 H15 N O6'    221.208 
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 
TAM non-polymer         . 'TRIS(HYDROXYETHYL)AMINOMETHANE' ?                               'C7 H17 N O3'    163.215 
THR 'L-peptide linking' y THREONINE                        ?                               'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                       ?                               'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                         ?                               'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                           ?                               'C5 H11 N O2'    117.146 
# 
_exptl.entry_id          3S11 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.00 
_exptl_crystal.density_percent_sol   59.05 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    '23% PEG 3350, 0.1M Tris-Cl pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K' 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'MAR CCD' 
_diffrn_detector.pdbx_collection_date   2010-06-17 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0000 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'APS BEAMLINE 22-ID' 
_diffrn_source.pdbx_synchrotron_site       APS 
_diffrn_source.pdbx_synchrotron_beamline   22-ID 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        1.0000 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     3S11 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             50.000 
_reflns.d_resolution_high            2.500 
_reflns.number_obs                   68017 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         96.000 
_reflns.pdbx_Rmerge_I_obs            0.104 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        10.900 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              4.800 
_reflns.R_free_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.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.number_unique_all 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_chi_squared 
1 1  2.500 2.590  72.800  0.431 ? ? 2.800 ? ? ? ? ? ? 
1 2  2.590 2.690  89.000  0.391 ? ? 3.300 ? ? ? ? ? ? 
1 3  2.690 2.820  98.300  0.353 ? ? 4.100 ? ? ? ? ? ? 
1 4  2.820 2.960  99.900  0.292 ? ? 4.900 ? ? ? ? ? ? 
1 5  2.960 3.150  100.000 0.224 ? ? 5.200 ? ? ? ? ? ? 
1 6  3.150 3.390  100.000 0.160 ? ? 5.400 ? ? ? ? ? ? 
1 7  3.390 3.730  100.000 0.111 ? ? 5.400 ? ? ? ? ? ? 
1 8  3.730 4.270  100.000 0.089 ? ? 5.400 ? ? ? ? ? ? 
1 9  4.270 5.380  100.000 0.075 ? ? 5.400 ? ? ? ? ? ? 
1 10 5.380 50.000 99.900  0.057 ? ? 5.300 ? ? ? ? ? ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 3S11 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     64349 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          . 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             49.07 
_refine.ls_d_res_high                            2.50 
_refine.ls_percent_reflns_obs                    95.93 
_refine.ls_R_factor_obs                          0.22309 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.22086 
_refine.ls_R_factor_R_free                       0.26475 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_number_reflns_R_free                  3457 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            1.000 
_refine.occupancy_max                            1.000 
_refine.correlation_coeff_Fo_to_Fc               0.928 
_refine.correlation_coeff_Fo_to_Fc_free          0.891 
_refine.B_iso_mean                               41.757 
_refine.aniso_B[1][1]                            0.00 
_refine.aniso_B[2][2]                            -0.02 
_refine.aniso_B[3][3]                            0.00 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.01 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.40 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.496 
_refine.pdbx_overall_ESU_R_Free                  0.296 
_refine.overall_SU_ML                            0.226 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             10.182 
_refine.overall_SU_R_Cruickshank_DPI             0.4959 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        11794 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         166 
_refine_hist.number_atoms_solvent             133 
_refine_hist.number_atoms_total               12093 
_refine_hist.d_res_high                       2.50 
_refine_hist.d_res_low                        49.07 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.007  0.022  ? 12253 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.002  0.020  ? 17    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.020  1.950  ? 16590 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            0.879  3.000  ? 36    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       5.279  5.000  ? 1471  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       38.170 25.250 ? 619   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       17.434 15.000 ? 2059  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       19.026 15.000 ? 51    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.070  0.200  ? 1775  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.004  0.021  ? 9364  'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.001  0.020  ? 2     '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' ? 
r_mcbond_it                  0.339  1.500  ? 7349  'X-RAY DIFFRACTION' ? 
r_mcbond_other               0.064  1.500  ? 2     'X-RAY DIFFRACTION' ? 
r_mcangle_it                 0.661  2.000  ? 11845 'X-RAY DIFFRACTION' ? 
r_scbond_it                  0.921  3.000  ? 4904  'X-RAY DIFFRACTION' ? 
r_scangle_it                 1.540  4.500  ? 4745  'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       2.500 
_refine_ls_shell.d_res_low                        2.565 
_refine_ls_shell.number_reflns_R_work             3478 
_refine_ls_shell.R_factor_R_work                  0.314 
_refine_ls_shell.percent_reflns_obs               70.47 
_refine_ls_shell.R_factor_R_free                  0.357 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             200 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.number_reflns_obs                ? 
# 
_struct.entry_id                  3S11 
_struct.title                     'Crystal structure of H5N1 influenza virus hemagglutinin, strain 437-10' 
_struct.pdbx_descriptor           'Hemagglutinin HA1 chain, Hemagglutinin HA2 chain' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3S11 
_struct_keywords.text            'hemagglutinin, viral protein, viral envelope protein, viral fusion protein' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 1 ? 
D N N 2 ? 
E N N 1 ? 
F N N 2 ? 
G N N 3 ? 
H N N 3 ? 
I N N 3 ? 
J N N 4 ? 
K N N 5 ? 
L N N 3 ? 
M N N 3 ? 
N N N 3 ? 
O N N 6 ? 
P N N 4 ? 
Q N N 3 ? 
R N N 3 ? 
S N N 3 ? 
T N N 4 ? 
U N N 7 ? 
V N N 7 ? 
W N N 7 ? 
X N N 7 ? 
Y N N 7 ? 
Z N N 7 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
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  1  SER A 64  ? GLY A 71  ? SER A 65  GLY A 72  1 ? 8  
HELX_P HELX_P2  2  ASN A 72  ? ILE A 79  ? ASN A 73  ILE A 80  5 ? 8  
HELX_P HELX_P3  3  ASN A 105 ? SER A 114 ? ASN A 104 SER A 113 1 ? 10 
HELX_P HELX_P4  4  PRO A 126 ? TRP A 130 ? PRO A 125 TRP A 127 5 ? 5  
HELX_P HELX_P5  5  ASP A 191 ? GLN A 200 ? ASP A 187 GLN A 196 1 ? 10 
HELX_P HELX_P6  6  ASP B 37  ? MET B 59  ? ASP B 37  MET B 59  1 ? 23 
HELX_P HELX_P7  7  GLU B 74  ? ARG B 127 ? GLU B 74  ARG B 127 1 ? 54 
HELX_P HELX_P8  8  ASP B 145 ? ASN B 154 ? ASP B 145 ASN B 154 1 ? 10 
HELX_P HELX_P9  9  TYR B 162 ? ARG B 170 ? TYR B 162 ARG B 170 1 ? 9  
HELX_P HELX_P10 10 SER C 64  ? GLY C 71  ? SER C 65  GLY C 72  1 ? 8  
HELX_P HELX_P11 11 CYS C 75  ? ILE C 79  ? CYS C 76  ILE C 80  5 ? 5  
HELX_P HELX_P12 12 ASN C 105 ? SER C 114 ? ASN C 104 SER C 113 1 ? 10 
HELX_P HELX_P13 13 PRO C 126 ? TRP C 130 ? PRO C 125 TRP C 127 5 ? 5  
HELX_P HELX_P14 14 ASP C 191 ? GLN C 200 ? ASP C 187 GLN C 196 1 ? 10 
HELX_P HELX_P15 15 ASP D 37  ? MET D 59  ? ASP D 37  MET D 59  1 ? 23 
HELX_P HELX_P16 16 GLU D 74  ? ARG D 127 ? GLU D 74  ARG D 127 1 ? 54 
HELX_P HELX_P17 17 ASP D 145 ? ASN D 154 ? ASP D 145 ASN D 154 1 ? 10 
HELX_P HELX_P18 18 ASP D 158 ? GLU D 172 ? ASP D 158 GLU D 172 1 ? 15 
HELX_P HELX_P19 19 SER E 64  ? GLY E 71  ? SER E 65  GLY E 72  1 ? 8  
HELX_P HELX_P20 20 ASN E 72  ? ILE E 79  ? ASN E 73  ILE E 80  5 ? 8  
HELX_P HELX_P21 21 ASN E 105 ? SER E 114 ? ASN E 104 SER E 113 1 ? 10 
HELX_P HELX_P22 22 PRO E 126 ? TRP E 130 ? PRO E 125 TRP E 127 5 ? 5  
HELX_P HELX_P23 23 ASP E 191 ? GLN E 200 ? ASP E 187 GLN E 196 1 ? 10 
HELX_P HELX_P24 24 ASP F 37  ? MET F 59  ? ASP F 37  MET F 59  1 ? 23 
HELX_P HELX_P25 25 GLU F 74  ? ARG F 127 ? GLU F 74  ARG F 127 1 ? 54 
HELX_P HELX_P26 26 ASP F 145 ? GLY F 155 ? ASP F 145 GLY F 155 1 ? 11 
HELX_P HELX_P27 27 ASP F 158 ? ILE F 173 ? ASP F 158 ILE F 173 1 ? 16 
# 
_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 12  SG  ? ? ? 1_555 B CYS 137 SG ? ? A CYS 14  B CYS 137 1_555 ? ? ? ? ? ? ? 2.039 ? 
disulf2  disulf ? ? A CYS 50  SG  ? ? ? 1_555 A CYS 282 SG ? ? A CYS 52  A CYS 277 1_555 ? ? ? ? ? ? ? 2.040 ? 
disulf3  disulf ? ? A CYS 63  SG  ? ? ? 1_555 A CYS 75  SG ? ? A CYS 64  A CYS 76  1_555 ? ? ? ? ? ? ? 2.038 ? 
disulf4  disulf ? ? A CYS 98  SG  ? ? ? 1_555 A CYS 143 SG ? ? A CYS 97  A CYS 139 1_555 ? ? ? ? ? ? ? 2.064 ? 
disulf5  disulf ? ? A CYS 286 SG  ? ? ? 1_555 A CYS 310 SG ? ? A CYS 281 A CYS 305 1_555 ? ? ? ? ? ? ? 2.039 ? 
disulf6  disulf ? ? B CYS 144 SG  ? ? ? 1_555 B CYS 148 SG ? ? B CYS 144 B CYS 148 1_555 ? ? ? ? ? ? ? 2.042 ? 
disulf7  disulf ? ? C CYS 12  SG  ? ? ? 1_555 D CYS 137 SG ? ? C CYS 14  D CYS 137 1_555 ? ? ? ? ? ? ? 2.042 ? 
disulf8  disulf ? ? C CYS 50  SG  ? ? ? 1_555 C CYS 282 SG ? ? C CYS 52  C CYS 277 1_555 ? ? ? ? ? ? ? 2.047 ? 
disulf9  disulf ? ? C CYS 63  SG  ? ? ? 1_555 C CYS 75  SG ? ? C CYS 64  C CYS 76  1_555 ? ? ? ? ? ? ? 2.052 ? 
disulf10 disulf ? ? C CYS 98  SG  ? ? ? 1_555 C CYS 143 SG ? ? C CYS 97  C CYS 139 1_555 ? ? ? ? ? ? ? 2.057 ? 
disulf11 disulf ? ? C CYS 286 SG  ? ? ? 1_555 C CYS 310 SG ? ? C CYS 281 C CYS 305 1_555 ? ? ? ? ? ? ? 2.043 ? 
disulf12 disulf ? ? D CYS 144 SG  ? ? ? 1_555 D CYS 148 SG ? ? D CYS 144 D CYS 148 1_555 ? ? ? ? ? ? ? 2.043 ? 
disulf13 disulf ? ? E CYS 12  SG  ? ? ? 1_555 F CYS 137 SG ? ? E CYS 14  F CYS 137 1_555 ? ? ? ? ? ? ? 2.042 ? 
disulf14 disulf ? ? E CYS 50  SG  ? ? ? 1_555 E CYS 282 SG ? ? E CYS 52  E CYS 277 1_555 ? ? ? ? ? ? ? 2.048 ? 
disulf15 disulf ? ? E CYS 63  SG  ? ? ? 1_555 E CYS 75  SG ? ? E CYS 64  E CYS 76  1_555 ? ? ? ? ? ? ? 2.053 ? 
disulf16 disulf ? ? E CYS 98  SG  ? ? ? 1_555 E CYS 143 SG ? ? E CYS 97  E CYS 139 1_555 ? ? ? ? ? ? ? 2.055 ? 
disulf17 disulf ? ? E CYS 286 SG  ? ? ? 1_555 E CYS 310 SG ? ? E CYS 281 E CYS 305 1_555 ? ? ? ? ? ? ? 2.051 ? 
disulf18 disulf ? ? F CYS 144 SG  ? ? ? 1_555 F CYS 148 SG ? ? F CYS 144 F CYS 148 1_555 ? ? ? ? ? ? ? 2.046 ? 
covale1  covale ? ? A ASN 31  ND2 ? ? ? 1_555 G NAG .   C1 ? ? A ASN 34  A NAG 1   1_555 ? ? ? ? ? ? ? 1.445 ? 
covale2  covale ? ? E ASN 31  ND2 ? ? ? 1_555 Q NAG .   C1 ? ? E ASN 34  E NAG 327 1_555 ? ? ? ? ? ? ? 1.422 ? 
covale3  covale ? ? H NAG .   O4  ? ? ? 1_555 I NAG .   C1 ? ? A NAG 2   A NAG 327 1_555 ? ? ? ? ? ? ? 1.441 ? 
covale4  covale ? ? R NAG .   O4  ? ? ? 1_555 S NAG .   C1 ? ? E NAG 328 E NAG 329 1_555 ? ? ? ? ? ? ? 1.443 ? 
covale5  covale ? ? M NAG .   O4  ? ? ? 1_555 N NAG .   C1 ? ? C NAG 328 C NAG 329 1_555 ? ? ? ? ? ? ? 1.445 ? 
covale6  covale ? ? N NAG .   O4  ? ? ? 1_555 O BMA .   C1 ? ? C NAG 329 C BMA 330 1_555 ? ? ? ? ? ? ? 1.413 ? 
covale7  covale ? ? C ASN 31  ND2 ? ? ? 1_555 L NAG .   C1 ? ? C ASN 34  C NAG 327 1_555 ? ? ? ? ? ? ? 1.576 ? 
covale8  covale ? ? E ASN 173 OD1 ? ? ? 1_555 R NAG .   C1 ? ? E ASN 169 E NAG 328 1_555 ? ? ? ? ? ? ? 1.431 ? 
covale9  covale ? ? A ASN 173 OD1 ? ? ? 1_555 H NAG .   C1 ? ? A ASN 169 A NAG 2   1_555 ? ? ? ? ? ? ? 1.431 ? 
covale10 covale ? ? C ASN 173 OD1 ? ? ? 1_555 M NAG .   C1 ? ? C ASN 169 C NAG 328 1_555 ? ? ? ? ? ? ? 1.433 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A  ? 5 ? 
B  ? 2 ? 
C  ? 2 ? 
D  ? 3 ? 
E  ? 2 ? 
F  ? 3 ? 
G  ? 5 ? 
H  ? 5 ? 
I  ? 2 ? 
J  ? 4 ? 
K  ? 3 ? 
L  ? 5 ? 
M  ? 2 ? 
N  ? 2 ? 
O  ? 3 ? 
P  ? 2 ? 
Q  ? 3 ? 
R  ? 5 ? 
S  ? 5 ? 
T  ? 2 ? 
U  ? 4 ? 
V  ? 3 ? 
W  ? 5 ? 
X  ? 2 ? 
Y  ? 2 ? 
Z  ? 3 ? 
AA ? 2 ? 
AB ? 3 ? 
AC ? 5 ? 
AD ? 5 ? 
AE ? 2 ? 
AF ? 4 ? 
AG ? 3 ? 
# 
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 
A  1 2 ? anti-parallel 
A  2 3 ? anti-parallel 
A  3 4 ? anti-parallel 
A  4 5 ? anti-parallel 
B  1 2 ? anti-parallel 
C  1 2 ? anti-parallel 
D  1 2 ? parallel      
D  2 3 ? parallel      
E  1 2 ? parallel      
F  1 2 ? parallel      
F  2 3 ? parallel      
G  1 2 ? parallel      
G  2 3 ? anti-parallel 
G  3 4 ? anti-parallel 
G  4 5 ? anti-parallel 
H  1 2 ? parallel      
H  2 3 ? anti-parallel 
H  3 4 ? anti-parallel 
H  4 5 ? anti-parallel 
I  1 2 ? anti-parallel 
J  1 2 ? anti-parallel 
J  2 3 ? anti-parallel 
J  3 4 ? anti-parallel 
K  1 2 ? anti-parallel 
K  2 3 ? anti-parallel 
L  1 2 ? anti-parallel 
L  2 3 ? anti-parallel 
L  3 4 ? anti-parallel 
L  4 5 ? anti-parallel 
M  1 2 ? anti-parallel 
N  1 2 ? anti-parallel 
O  1 2 ? parallel      
O  2 3 ? parallel      
P  1 2 ? parallel      
Q  1 2 ? parallel      
Q  2 3 ? parallel      
R  1 2 ? parallel      
R  2 3 ? anti-parallel 
R  3 4 ? anti-parallel 
R  4 5 ? anti-parallel 
S  1 2 ? parallel      
S  2 3 ? anti-parallel 
S  3 4 ? anti-parallel 
S  4 5 ? anti-parallel 
T  1 2 ? anti-parallel 
U  1 2 ? anti-parallel 
U  2 3 ? anti-parallel 
U  3 4 ? anti-parallel 
V  1 2 ? anti-parallel 
V  2 3 ? anti-parallel 
W  1 2 ? anti-parallel 
W  2 3 ? anti-parallel 
W  3 4 ? anti-parallel 
W  4 5 ? anti-parallel 
X  1 2 ? anti-parallel 
Y  1 2 ? anti-parallel 
Z  1 2 ? parallel      
Z  2 3 ? parallel      
AA 1 2 ? parallel      
AB 1 2 ? parallel      
AB 2 3 ? parallel      
AC 1 2 ? parallel      
AC 2 3 ? anti-parallel 
AC 3 4 ? anti-parallel 
AC 4 5 ? anti-parallel 
AD 1 2 ? parallel      
AD 2 3 ? anti-parallel 
AD 3 4 ? anti-parallel 
AD 4 5 ? anti-parallel 
AE 1 2 ? anti-parallel 
AF 1 2 ? anti-parallel 
AF 2 3 ? anti-parallel 
AF 3 4 ? anti-parallel 
AG 1 2 ? anti-parallel 
AG 2 3 ? 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 
A  1 SER B 32  ? ALA B 36  ? SER B 32  ALA B 36  
A  2 TYR B 22  ? SER B 27  ? TYR B 22  SER B 27  
A  3 GLN A 10  ? TYR A 15  ? GLN A 12  TYR A 17  
A  4 CYS B 137 ? PHE B 140 ? CYS B 137 PHE B 140 
A  5 ALA B 130 ? GLU B 132 ? ALA B 130 GLU B 132 
B  1 GLN A 23  ? VAL A 24  ? GLN A 24  VAL A 25  
B  2 VAL A 32  ? THR A 33  A VAL A 35  THR A 35  
C  1 ALA A 37  ? ASP A 39  ? ALA A 39  ASP A 41  
C  2 VAL A 320 ? ALA A 322 ? VAL A 315 ALA A 317 
D  1 LEU A 41  ? GLU A 42  ? LEU A 43  GLU A 44  
D  2 PHE A 299 ? HIS A 300 ? PHE A 294 HIS A 295 
D  3 LYS A 312 ? TYR A 313 ? LYS A 307 TYR A 308 
E  1 LEU A 49  ? LEU A 52  A LEU A 51  LEU A 53  
E  2 TYR A 279 ? THR A 284 ? TYR A 274 THR A 279 
F  1 LEU A 58  ? ILE A 59  ? LEU A 59  ILE A 60  
F  2 ILE A 87  ? GLU A 89  ? ILE A 87  GLU A 89  
F  3 ILE A 272 ? LYS A 274 ? ILE A 267 LYS A 269 
G  1 GLY A 101 ? PHE A 103 ? GLY A 100 PHE A 102 
G  2 ARG A 233 ? LEU A 241 ? ARG A 229 LEU A 237 
G  3 LEU A 180 ? HIS A 188 ? LEU A 176 HIS A 184 
G  4 TYR A 260 ? LYS A 267 ? TYR A 256 LYS A 263 
G  5 THR A 116 ? GLN A 123 ? THR A 115 GLN A 122 
H  1 GLY A 101 ? PHE A 103 ? GLY A 100 PHE A 102 
H  2 ARG A 233 ? LEU A 241 ? ARG A 229 LEU A 237 
H  3 LEU A 180 ? HIS A 188 ? LEU A 176 HIS A 184 
H  4 PHE A 255 ? PRO A 258 ? PHE A 251 PRO A 254 
H  5 VAL A 155 ? TRP A 157 ? VAL A 151 TRP A 153 
I  1 SER A 140 ? TYR A 145 ? SER A 136 TYR A 141 
I  2 LYS A 148 ? SER A 150 ? LYS A 144 SER A 146 
J  1 ILE A 168 ? ASN A 173 ? ILE A 164 ASN A 169 
J  2 ALA A 246 ? SER A 251 ? ALA A 242 SER A 247 
J  3 ILE A 206 ? GLY A 209 ? ILE A 202 GLY A 205 
J  4 ASN A 214 ? LEU A 217 ? ASN A 210 LEU A 213 
K  1 GLY A 291 ? ILE A 293 ? GLY A 286 ILE A 288 
K  2 CYS A 286 ? THR A 288 ? CYS A 281 THR A 283 
K  3 ILE A 307 ? GLY A 308 ? ILE A 302 GLY A 303 
L  1 TYR D 34  ? ALA D 36  ? TYR D 34  ALA D 36  
L  2 TYR D 22  ? SER D 27  ? TYR D 22  SER D 27  
L  3 GLN C 10  ? TYR C 15  ? GLN C 12  TYR C 17  
L  4 CYS D 137 ? PHE D 140 ? CYS D 137 PHE D 140 
L  5 ALA D 130 ? GLU D 132 ? ALA D 130 GLU D 132 
M  1 GLN C 23  ? VAL C 24  ? GLN C 24  VAL C 25  
M  2 VAL C 32  ? THR C 33  A VAL C 35  THR C 35  
N  1 ALA C 37  ? ASP C 39  ? ALA C 39  ASP C 41  
N  2 VAL C 320 ? ALA C 322 ? VAL C 315 ALA C 317 
O  1 LEU C 41  ? GLU C 42  ? LEU C 43  GLU C 44  
O  2 PHE C 299 ? HIS C 300 ? PHE C 294 HIS C 295 
O  3 LYS C 312 ? TYR C 313 ? LYS C 307 TYR C 308 
P  1 LEU C 49  ? LEU C 52  A LEU C 51  LEU C 53  
P  2 TYR C 279 ? THR C 284 ? TYR C 274 THR C 279 
Q  1 LEU C 58  ? ILE C 59  ? LEU C 59  ILE C 60  
Q  2 ILE C 87  ? GLU C 89  ? ILE C 87  GLU C 89  
Q  3 ILE C 272 ? LYS C 274 ? ILE C 267 LYS C 269 
R  1 GLY C 101 ? PHE C 103 ? GLY C 100 PHE C 102 
R  2 ARG C 233 ? LEU C 241 ? ARG C 229 LEU C 237 
R  3 LEU C 180 ? HIS C 188 ? LEU C 176 HIS C 184 
R  4 TYR C 260 ? LYS C 267 ? TYR C 256 LYS C 263 
R  5 THR C 116 ? GLN C 123 ? THR C 115 GLN C 122 
S  1 GLY C 101 ? PHE C 103 ? GLY C 100 PHE C 102 
S  2 ARG C 233 ? LEU C 241 ? ARG C 229 LEU C 237 
S  3 LEU C 180 ? HIS C 188 ? LEU C 176 HIS C 184 
S  4 PHE C 255 ? PRO C 258 ? PHE C 251 PRO C 254 
S  5 VAL C 155 ? TRP C 157 ? VAL C 151 TRP C 153 
T  1 SER C 140 ? PRO C 144 ? SER C 136 PRO C 140 
T  2 SER C 149 ? SER C 150 ? SER C 145 SER C 146 
U  1 ILE C 168 ? ASN C 173 ? ILE C 164 ASN C 169 
U  2 ALA C 246 ? SER C 251 ? ALA C 242 SER C 247 
U  3 ILE C 206 ? GLY C 209 ? ILE C 202 GLY C 205 
U  4 ASN C 214 ? LEU C 217 ? ASN C 210 LEU C 213 
V  1 GLY C 291 ? ILE C 293 ? GLY C 286 ILE C 288 
V  2 CYS C 286 ? THR C 288 ? CYS C 281 THR C 283 
V  3 ILE C 307 ? GLY C 308 ? ILE C 302 GLY C 303 
W  1 SER F 32  ? ALA F 36  ? SER F 32  ALA F 36  
W  2 TYR F 22  ? SER F 27  ? TYR F 22  SER F 27  
W  3 GLN E 10  ? TYR E 15  ? GLN E 12  TYR E 17  
W  4 CYS F 137 ? PHE F 140 ? CYS F 137 PHE F 140 
W  5 ALA F 130 ? GLU F 132 ? ALA F 130 GLU F 132 
X  1 GLN E 23  ? VAL E 24  ? GLN E 24  VAL E 25  
X  2 VAL E 32  ? THR E 33  A VAL E 35  THR E 35  
Y  1 ALA E 37  ? ASP E 39  ? ALA E 39  ASP E 41  
Y  2 VAL E 320 ? ALA E 322 ? VAL E 315 ALA E 317 
Z  1 LEU E 41  ? GLU E 42  ? LEU E 43  GLU E 44  
Z  2 PHE E 299 ? HIS E 300 ? PHE E 294 HIS E 295 
Z  3 LYS E 312 ? TYR E 313 ? LYS E 307 TYR E 308 
AA 1 LEU E 49  ? LEU E 52  A LEU E 51  LEU E 53  
AA 2 TYR E 279 ? THR E 284 ? TYR E 274 THR E 279 
AB 1 LEU E 58  ? ILE E 59  ? LEU E 59  ILE E 60  
AB 2 ILE E 87  ? GLU E 89  ? ILE E 87  GLU E 89  
AB 3 ILE E 272 ? LYS E 274 ? ILE E 267 LYS E 269 
AC 1 GLY E 101 ? PHE E 103 ? GLY E 100 PHE E 102 
AC 2 ARG E 233 ? LEU E 241 ? ARG E 229 LEU E 237 
AC 3 ASP E 179 ? HIS E 188 ? ASP E 175 HIS E 184 
AC 4 TYR E 260 ? LYS E 267 ? TYR E 256 LYS E 263 
AC 5 THR E 116 ? GLN E 123 ? THR E 115 GLN E 122 
AD 1 GLY E 101 ? PHE E 103 ? GLY E 100 PHE E 102 
AD 2 ARG E 233 ? LEU E 241 ? ARG E 229 LEU E 237 
AD 3 ASP E 179 ? HIS E 188 ? ASP E 175 HIS E 184 
AD 4 PHE E 255 ? PRO E 258 ? PHE E 251 PRO E 254 
AD 5 VAL E 155 ? TRP E 157 ? VAL E 151 TRP E 153 
AE 1 SER E 140 ? PRO E 144 ? SER E 136 PRO E 140 
AE 2 SER E 149 ? SER E 150 ? SER E 145 SER E 146 
AF 1 ILE E 168 ? ASN E 173 ? ILE E 164 ASN E 169 
AF 2 ALA E 246 ? SER E 251 ? ALA E 242 SER E 247 
AF 3 ILE E 206 ? GLY E 209 ? ILE E 202 GLY E 205 
AF 4 ASN E 214 ? LEU E 217 ? ASN E 210 LEU E 213 
AG 1 GLY E 291 ? ILE E 293 ? GLY E 286 ILE E 288 
AG 2 CYS E 286 ? THR E 288 ? CYS E 281 THR E 283 
AG 3 ILE E 307 ? GLY E 308 ? ILE E 302 GLY E 303 
# 
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 
A  1 2 O ALA B 35  ? O ALA B 35  N TYR B 24  ? N TYR B 24  
A  2 3 O SER B 27  ? O SER B 27  N GLN A 10  ? N GLN A 12  
A  3 4 N ILE A 11  ? N ILE A 13  O PHE B 138 ? O PHE B 138 
A  4 5 O GLU B 139 ? O GLU B 139 N LYS B 131 ? N LYS B 131 
B  1 2 N VAL A 24  ? N VAL A 25  O VAL A 32  ? O VAL A 35  
C  1 2 N GLN A 38  ? N GLN A 40  O LEU A 321 ? O LEU A 316 
D  1 2 N GLU A 42  ? N GLU A 44  O PHE A 299 ? O PHE A 294 
D  2 3 N HIS A 300 ? N HIS A 295 O LYS A 312 ? O LYS A 307 
E  1 2 N LEU A 49  ? N LEU A 51  O GLY A 280 ? O GLY A 275 
F  1 2 N LEU A 58  ? N LEU A 59  O VAL A 88  ? O VAL A 88  
F  2 3 N ILE A 87  ? N ILE A 87  O MET A 273 ? O MET A 268 
G  1 2 N ASP A 102 ? N ASP A 101 O PHE A 236 ? O PHE A 232 
G  2 3 O LEU A 241 ? O LEU A 237 N LEU A 180 ? N LEU A 176 
G  3 4 N LEU A 181 ? N LEU A 177 O TYR A 262 ? O TYR A 258 
G  4 5 O LYS A 263 ? O LYS A 259 N GLU A 120 ? N GLU A 119 
H  1 2 N ASP A 102 ? N ASP A 101 O PHE A 236 ? O PHE A 232 
H  2 3 O LEU A 241 ? O LEU A 237 N LEU A 180 ? N LEU A 176 
H  3 4 N GLY A 185 ? N GLY A 181 O ILE A 256 ? O ILE A 252 
H  4 5 O ALA A 257 ? O ALA A 253 N VAL A 156 ? N VAL A 152 
I  1 2 N SER A 140 ? N SER A 136 O SER A 150 ? O SER A 146 
J  1 2 N ILE A 168 ? N ILE A 164 O SER A 251 ? O SER A 247 
J  2 3 O GLU A 250 ? O GLU A 246 N SER A 207 ? N SER A 203 
J  3 4 N ILE A 206 ? N ILE A 202 O LEU A 217 ? O LEU A 213 
K  1 2 O ILE A 293 ? O ILE A 288 N CYS A 286 ? N CYS A 281 
K  2 3 N GLN A 287 ? N GLN A 282 O ILE A 307 ? O ILE A 302 
L  1 2 O ALA D 35  ? O ALA D 35  N TYR D 24  ? N TYR D 24  
L  2 3 O HIS D 25  ? O HIS D 25  N CYS C 12  ? N CYS C 14  
L  3 4 N ILE C 11  ? N ILE C 13  O PHE D 138 ? O PHE D 138 
L  4 5 O GLU D 139 ? O GLU D 139 N LYS D 131 ? N LYS D 131 
M  1 2 N VAL C 24  ? N VAL C 25  O VAL C 32  ? O VAL C 35  
N  1 2 N GLN C 38  ? N GLN C 40  O LEU C 321 ? O LEU C 316 
O  1 2 N GLU C 42  ? N GLU C 44  O PHE C 299 ? O PHE C 294 
O  2 3 N HIS C 300 ? N HIS C 295 O LYS C 312 ? O LYS C 307 
P  1 2 N ASP C 51  ? N ASP C 53  O THR C 284 ? O THR C 279 
Q  1 2 N LEU C 58  ? N LEU C 59  O VAL C 88  ? O VAL C 88  
Q  2 3 N ILE C 87  ? N ILE C 87  O MET C 273 ? O MET C 268 
R  1 2 N ASP C 102 ? N ASP C 101 O PHE C 236 ? O PHE C 232 
R  2 3 O LEU C 241 ? O LEU C 237 N LEU C 180 ? N LEU C 176 
R  3 4 N LEU C 181 ? N LEU C 177 O TYR C 262 ? O TYR C 258 
R  4 5 O LYS C 263 ? O LYS C 259 N GLU C 120 ? N GLU C 119 
S  1 2 N ASP C 102 ? N ASP C 101 O PHE C 236 ? O PHE C 232 
S  2 3 O LEU C 241 ? O LEU C 237 N LEU C 180 ? N LEU C 176 
S  3 4 N GLY C 185 ? N GLY C 181 O ILE C 256 ? O ILE C 252 
S  4 5 O ALA C 257 ? O ALA C 253 N VAL C 156 ? N VAL C 152 
T  1 2 N SER C 140 ? N SER C 136 O SER C 150 ? O SER C 146 
U  1 2 N ILE C 168 ? N ILE C 164 O SER C 251 ? O SER C 247 
U  2 3 O ASN C 248 ? O ASN C 244 N GLY C 209 ? N GLY C 205 
U  3 4 N ILE C 206 ? N ILE C 202 O LEU C 217 ? O LEU C 213 
V  1 2 O ILE C 293 ? O ILE C 288 N CYS C 286 ? N CYS C 281 
V  2 3 N GLN C 287 ? N GLN C 282 O ILE C 307 ? O ILE C 302 
W  1 2 O ALA F 35  ? O ALA F 35  N TYR F 24  ? N TYR F 24  
W  2 3 O HIS F 25  ? O HIS F 25  N CYS E 12  ? N CYS E 14  
W  3 4 N ILE E 11  ? N ILE E 13  O PHE F 138 ? O PHE F 138 
W  4 5 O GLU F 139 ? O GLU F 139 N LYS F 131 ? N LYS F 131 
X  1 2 N VAL E 24  ? N VAL E 25  O VAL E 32  ? O VAL E 35  
Y  1 2 N GLN E 38  ? N GLN E 40  O LEU E 321 ? O LEU E 316 
Z  1 2 N GLU E 42  ? N GLU E 44  O PHE E 299 ? O PHE E 294 
Z  2 3 N HIS E 300 ? N HIS E 295 O LYS E 312 ? O LYS E 307 
AA 1 2 N LEU E 49  ? N LEU E 51  O GLY E 280 ? O GLY E 275 
AB 1 2 N LEU E 58  ? N LEU E 59  O VAL E 88  ? O VAL E 88  
AB 2 3 N ILE E 87  ? N ILE E 87  O MET E 273 ? O MET E 268 
AC 1 2 N ASP E 102 ? N ASP E 101 O PHE E 236 ? O PHE E 232 
AC 2 3 O ARG E 233 ? O ARG E 229 N HIS E 188 ? N HIS E 184 
AC 3 4 N ASP E 179 ? N ASP E 175 O ILE E 264 ? O ILE E 260 
AC 4 5 O LYS E 263 ? O LYS E 259 N GLU E 120 ? N GLU E 119 
AD 1 2 N ASP E 102 ? N ASP E 101 O PHE E 236 ? O PHE E 232 
AD 2 3 O ARG E 233 ? O ARG E 229 N HIS E 188 ? N HIS E 184 
AD 3 4 N GLY E 185 ? N GLY E 181 O ILE E 256 ? O ILE E 252 
AD 4 5 O ALA E 257 ? O ALA E 253 N VAL E 156 ? N VAL E 152 
AE 1 2 N SER E 140 ? N SER E 136 O SER E 150 ? O SER E 146 
AF 1 2 N ILE E 168 ? N ILE E 164 O SER E 251 ? O SER E 247 
AF 2 3 O GLU E 250 ? O GLU E 246 N SER E 207 ? N SER E 203 
AF 3 4 N ILE E 206 ? N ILE E 202 O LEU E 217 ? O LEU E 213 
AG 1 2 O ILE E 293 ? O ILE E 288 N CYS E 286 ? N CYS E 281 
AG 2 3 N GLN E 287 ? N GLN E 282 O ILE E 307 ? O ILE E 302 
# 
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 ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG A 1'   
AC2 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 2'   
AC3 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG A 327' 
AC4 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE GOL A 328' 
AC5 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE TAM A 329' 
AC6 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG C 327' 
AC7 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG C 328' 
AC8 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG C 329' 
AC9 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE BMA C 330' 
BC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE GOL C 2'   
BC2 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG E 327' 
BC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG E 328' 
BC4 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG E 329' 
BC5 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE GOL E 330' 
# 
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 1 ASN A 31  ? ASN A 34  . ? 1_555 ? 
2  AC2 5 ASN A 173 ? ASN A 169 . ? 1_555 ? 
3  AC2 5 ASN A 244 ? ASN A 240 . ? 1_555 ? 
4  AC2 5 ALA A 246 ? ALA A 242 . ? 1_555 ? 
5  AC2 5 NAG I .   ? NAG A 327 . ? 1_555 ? 
6  AC2 5 PRO C 225 ? PRO C 221 . ? 1_555 ? 
7  AC3 1 NAG H .   ? NAG A 2   . ? 1_555 ? 
8  AC4 5 ASP A 25  ? ASP A 26  . ? 1_555 ? 
9  AC4 5 ARG A 318 ? ARG A 313 . ? 1_555 ? 
10 AC4 5 VAL A 320 ? VAL A 315 . ? 1_555 ? 
11 AC4 5 LEU B 101 ? LEU B 101 . ? 1_555 ? 
12 AC4 5 ASN B 104 ? ASN B 104 . ? 1_555 ? 
13 AC5 3 GLY A 147 ? GLY A 143 . ? 1_555 ? 
14 AC5 3 HOH U .   ? HOH A 362 . ? 1_555 ? 
15 AC5 3 TYR C 260 ? TYR C 256 . ? 1_656 ? 
16 AC6 1 ASN C 31  ? ASN C 34  . ? 1_555 ? 
17 AC7 5 ASN C 173 ? ASN C 169 . ? 1_555 ? 
18 AC7 5 ASN C 244 ? ASN C 240 . ? 1_555 ? 
19 AC7 5 ASP C 245 ? ASP C 241 . ? 1_555 ? 
20 AC7 5 ALA C 246 ? ALA C 242 . ? 1_555 ? 
21 AC7 5 NAG N .   ? NAG C 329 . ? 1_555 ? 
22 AC8 3 ASN C 244 ? ASN C 240 . ? 1_555 ? 
23 AC8 3 NAG M .   ? NAG C 328 . ? 1_555 ? 
24 AC8 3 BMA O .   ? BMA C 330 . ? 1_555 ? 
25 AC9 3 GLN A 123 ? GLN A 122 . ? 1_455 ? 
26 AC9 3 ILE A 124 ? ILE A 123 . ? 1_455 ? 
27 AC9 3 NAG N .   ? NAG C 329 . ? 1_555 ? 
28 BC1 5 VAL C 24  ? VAL C 25  . ? 1_555 ? 
29 BC1 5 ASP C 25  ? ASP C 26  . ? 1_555 ? 
30 BC1 5 ARG C 318 ? ARG C 313 . ? 1_555 ? 
31 BC1 5 VAL C 320 ? VAL C 315 . ? 1_555 ? 
32 BC1 5 ASN D 104 ? ASN D 104 . ? 1_555 ? 
33 BC2 1 ASN E 31  ? ASN E 34  . ? 1_555 ? 
34 BC3 4 ASN E 173 ? ASN E 169 . ? 1_555 ? 
35 BC3 4 ASN E 244 ? ASN E 240 . ? 1_555 ? 
36 BC3 4 ALA E 246 ? ALA E 242 . ? 1_555 ? 
37 BC3 4 NAG S .   ? NAG E 329 . ? 1_555 ? 
38 BC4 1 NAG R .   ? NAG E 328 . ? 1_555 ? 
39 BC5 5 VAL E 24  ? VAL E 25  . ? 1_555 ? 
40 BC5 5 ASP E 25  ? ASP E 26  . ? 1_555 ? 
41 BC5 5 ARG E 318 ? ARG E 313 . ? 1_555 ? 
42 BC5 5 VAL E 320 ? VAL E 315 . ? 1_555 ? 
43 BC5 5 ASN F 104 ? ASN F 104 . ? 1_555 ? 
# 
_atom_sites.entry_id                    3S11 
_atom_sites.fract_transf_matrix[1][1]   0.014416 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.007248 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.004148 
_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]   0.015975 
_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 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N N   . PRO A 1 7   ? -3.782  -47.182 14.103  1.00 62.62 ? 9   PRO A N   1 
ATOM   2     C CA  . PRO A 1 7   ? -5.228  -47.201 14.340  1.00 62.50 ? 9   PRO A CA  1 
ATOM   3     C C   . PRO A 1 7   ? -5.750  -45.914 14.988  1.00 62.36 ? 9   PRO A C   1 
ATOM   4     O O   . PRO A 1 7   ? -6.897  -45.532 14.750  1.00 62.40 ? 9   PRO A O   1 
ATOM   5     C CB  . PRO A 1 7   ? -5.417  -48.394 15.292  1.00 62.50 ? 9   PRO A CB  1 
ATOM   6     C CG  . PRO A 1 7   ? -4.068  -48.625 15.908  1.00 62.68 ? 9   PRO A CG  1 
ATOM   7     C CD  . PRO A 1 7   ? -3.081  -48.248 14.840  1.00 62.72 ? 9   PRO A CD  1 
ATOM   8     N N   . GLY A 1 8   ? -4.915  -45.261 15.799  1.00 62.10 ? 10  GLY A N   1 
ATOM   9     C CA  . GLY A 1 8   ? -5.306  -44.033 16.492  1.00 61.58 ? 10  GLY A CA  1 
ATOM   10    C C   . GLY A 1 8   ? -4.549  -42.787 16.058  1.00 61.27 ? 10  GLY A C   1 
ATOM   11    O O   . GLY A 1 8   ? -4.411  -41.841 16.838  1.00 61.26 ? 10  GLY A O   1 
ATOM   12    N N   . ASP A 1 9   ? -4.060  -42.783 14.818  1.00 60.90 ? 11  ASP A N   1 
ATOM   13    C CA  . ASP A 1 9   ? -3.339  -41.632 14.264  1.00 60.49 ? 11  ASP A CA  1 
ATOM   14    C C   . ASP A 1 9   ? -4.259  -40.422 14.124  1.00 60.15 ? 11  ASP A C   1 
ATOM   15    O O   . ASP A 1 9   ? -5.417  -40.556 13.712  1.00 60.24 ? 11  ASP A O   1 
ATOM   16    C CB  . ASP A 1 9   ? -2.701  -41.980 12.919  1.00 60.58 ? 11  ASP A CB  1 
ATOM   17    C CG  . ASP A 1 9   ? -1.434  -42.807 13.066  1.00 60.78 ? 11  ASP A CG  1 
ATOM   18    O OD1 . ASP A 1 9   ? -1.092  -43.199 14.203  1.00 61.21 ? 11  ASP A OD1 1 
ATOM   19    O OD2 . ASP A 1 9   ? -0.774  -43.063 12.037  1.00 61.06 ? 11  ASP A OD2 1 
ATOM   20    N N   . GLN A 1 10  ? -3.741  -39.247 14.475  1.00 59.49 ? 12  GLN A N   1 
ATOM   21    C CA  . GLN A 1 10  ? -4.575  -38.056 14.622  1.00 58.83 ? 12  GLN A CA  1 
ATOM   22    C C   . GLN A 1 10  ? -3.945  -36.757 14.134  1.00 58.33 ? 12  GLN A C   1 
ATOM   23    O O   . GLN A 1 10  ? -2.728  -36.566 14.220  1.00 58.36 ? 12  GLN A O   1 
ATOM   24    C CB  . GLN A 1 10  ? -4.999  -37.883 16.083  1.00 58.83 ? 12  GLN A CB  1 
ATOM   25    C CG  . GLN A 1 10  ? -6.185  -38.739 16.497  1.00 58.77 ? 12  GLN A CG  1 
ATOM   26    C CD  . GLN A 1 10  ? -6.796  -38.307 17.819  1.00 58.86 ? 12  GLN A CD  1 
ATOM   27    O OE1 . GLN A 1 10  ? -7.583  -39.041 18.416  1.00 58.61 ? 12  GLN A OE1 1 
ATOM   28    N NE2 . GLN A 1 10  ? -6.441  -37.110 18.281  1.00 59.05 ? 12  GLN A NE2 1 
ATOM   29    N N   . ILE A 1 11  ? -4.802  -35.878 13.615  1.00 57.53 ? 13  ILE A N   1 
ATOM   30    C CA  . ILE A 1 11  ? -4.467  -34.476 13.374  1.00 56.64 ? 13  ILE A CA  1 
ATOM   31    C C   . ILE A 1 11  ? -5.597  -33.592 13.902  1.00 56.11 ? 13  ILE A C   1 
ATOM   32    O O   . ILE A 1 11  ? -6.781  -33.905 13.728  1.00 56.00 ? 13  ILE A O   1 
ATOM   33    C CB  . ILE A 1 11  ? -4.160  -34.176 11.883  1.00 56.60 ? 13  ILE A CB  1 
ATOM   34    C CG1 . ILE A 1 11  ? -3.531  -32.785 11.743  1.00 56.65 ? 13  ILE A CG1 1 
ATOM   35    C CG2 . ILE A 1 11  ? -5.409  -34.336 11.006  1.00 56.47 ? 13  ILE A CG2 1 
ATOM   36    C CD1 . ILE A 1 11  ? -2.658  -32.607 10.519  1.00 56.91 ? 13  ILE A CD1 1 
ATOM   37    N N   . CYS A 1 12  ? -5.221  -32.499 14.559  1.00 55.37 ? 14  CYS A N   1 
ATOM   38    C CA  . CYS A 1 12  ? -6.184  -31.600 15.184  1.00 54.72 ? 14  CYS A CA  1 
ATOM   39    C C   . CYS A 1 12  ? -6.005  -30.156 14.728  1.00 54.01 ? 14  CYS A C   1 
ATOM   40    O O   . CYS A 1 12  ? -4.881  -29.700 14.507  1.00 53.85 ? 14  CYS A O   1 
ATOM   41    C CB  . CYS A 1 12  ? -6.075  -31.684 16.707  1.00 54.94 ? 14  CYS A CB  1 
ATOM   42    S SG  . CYS A 1 12  ? -6.402  -33.328 17.377  1.00 55.66 ? 14  CYS A SG  1 
ATOM   43    N N   . ILE A 1 13  ? -7.127  -29.450 14.596  1.00 53.09 ? 15  ILE A N   1 
ATOM   44    C CA  . ILE A 1 13  ? -7.140  -28.042 14.208  1.00 52.09 ? 15  ILE A CA  1 
ATOM   45    C C   . ILE A 1 13  ? -7.280  -27.175 15.452  1.00 51.38 ? 15  ILE A C   1 
ATOM   46    O O   . ILE A 1 13  ? -8.185  -27.384 16.260  1.00 51.35 ? 15  ILE A O   1 
ATOM   47    C CB  . ILE A 1 13  ? -8.285  -27.747 13.203  1.00 52.12 ? 15  ILE A CB  1 
ATOM   48    C CG1 . ILE A 1 13  ? -8.137  -28.619 11.951  1.00 52.05 ? 15  ILE A CG1 1 
ATOM   49    C CG2 . ILE A 1 13  ? -8.341  -26.259 12.834  1.00 52.08 ? 15  ILE A CG2 1 
ATOM   50    C CD1 . ILE A 1 13  ? -6.793  -28.495 11.253  1.00 51.73 ? 15  ILE A CD1 1 
ATOM   51    N N   . GLY A 1 14  ? -6.381  -26.209 15.607  1.00 50.49 ? 16  GLY A N   1 
ATOM   52    C CA  . GLY A 1 14  ? -6.392  -25.368 16.796  1.00 49.61 ? 16  GLY A CA  1 
ATOM   53    C C   . GLY A 1 14  ? -5.869  -23.957 16.634  1.00 48.90 ? 16  GLY A C   1 
ATOM   54    O O   . GLY A 1 14  ? -5.273  -23.603 15.612  1.00 48.85 ? 16  GLY A O   1 
ATOM   55    N N   . TYR A 1 15  ? -6.092  -23.156 17.671  1.00 48.25 ? 17  TYR A N   1 
ATOM   56    C CA  . TYR A 1 15  ? -5.726  -21.746 17.665  1.00 47.50 ? 17  TYR A CA  1 
ATOM   57    C C   . TYR A 1 15  ? -4.884  -21.367 18.883  1.00 47.53 ? 17  TYR A C   1 
ATOM   58    O O   . TYR A 1 15  ? -4.839  -22.101 19.869  1.00 47.31 ? 17  TYR A O   1 
ATOM   59    C CB  . TYR A 1 15  ? -6.976  -20.859 17.536  1.00 47.07 ? 17  TYR A CB  1 
ATOM   60    C CG  . TYR A 1 15  ? -8.023  -21.048 18.616  1.00 45.19 ? 17  TYR A CG  1 
ATOM   61    C CD1 . TYR A 1 15  ? -8.090  -20.181 19.703  1.00 43.84 ? 17  TYR A CD1 1 
ATOM   62    C CD2 . TYR A 1 15  ? -8.959  -22.079 18.542  1.00 43.47 ? 17  TYR A CD2 1 
ATOM   63    C CE1 . TYR A 1 15  ? -9.049  -20.338 20.696  1.00 42.21 ? 17  TYR A CE1 1 
ATOM   64    C CE2 . TYR A 1 15  ? -9.920  -22.247 19.532  1.00 42.24 ? 17  TYR A CE2 1 
ATOM   65    C CZ  . TYR A 1 15  ? -9.957  -21.371 20.604  1.00 41.51 ? 17  TYR A CZ  1 
ATOM   66    O OH  . TYR A 1 15  ? -10.906 -21.518 21.585  1.00 40.30 ? 17  TYR A OH  1 
ATOM   67    N N   . HIS A 1 16  ? -4.222  -20.215 18.784  1.00 47.66 ? 18  HIS A N   1 
ATOM   68    C CA  . HIS A 1 16  ? -3.256  -19.730 19.770  1.00 47.91 ? 18  HIS A CA  1 
ATOM   69    C C   . HIS A 1 16  ? -3.913  -19.297 21.082  1.00 47.94 ? 18  HIS A C   1 
ATOM   70    O O   . HIS A 1 16  ? -5.033  -18.773 21.093  1.00 47.88 ? 18  HIS A O   1 
ATOM   71    C CB  . HIS A 1 16  ? -2.461  -18.567 19.158  1.00 48.06 ? 18  HIS A CB  1 
ATOM   72    C CG  . HIS A 1 16  ? -1.395  -18.003 20.049  1.00 48.80 ? 18  HIS A CG  1 
ATOM   73    N ND1 . HIS A 1 16  ? -0.097  -18.468 20.044  1.00 49.34 ? 18  HIS A ND1 1 
ATOM   74    C CD2 . HIS A 1 16  ? -1.426  -16.989 20.947  1.00 49.44 ? 18  HIS A CD2 1 
ATOM   75    C CE1 . HIS A 1 16  ? 0.621   -17.777 20.912  1.00 49.39 ? 18  HIS A CE1 1 
ATOM   76    N NE2 . HIS A 1 16  ? -0.162  -16.874 21.475  1.00 49.43 ? 18  HIS A NE2 1 
ATOM   77    N N   . ALA A 1 17  ? -3.213  -19.546 22.185  1.00 47.90 ? 19  ALA A N   1 
ATOM   78    C CA  . ALA A 1 17  ? -3.583  -19.007 23.492  1.00 48.06 ? 19  ALA A CA  1 
ATOM   79    C C   . ALA A 1 17  ? -2.315  -18.604 24.227  1.00 48.17 ? 19  ALA A C   1 
ATOM   80    O O   . ALA A 1 17  ? -1.283  -19.259 24.090  1.00 48.27 ? 19  ALA A O   1 
ATOM   81    C CB  . ALA A 1 17  ? -4.376  -20.021 24.298  1.00 47.83 ? 19  ALA A CB  1 
ATOM   82    N N   . ASN A 1 18  A -2.385  -17.513 24.983  1.00 48.39 ? 19  ASN A N   1 
ATOM   83    C CA  . ASN A 1 18  A -1.223  -17.033 25.731  1.00 48.64 ? 19  ASN A CA  1 
ATOM   84    C C   . ASN A 1 18  A -1.574  -16.483 27.111  1.00 48.91 ? 19  ASN A C   1 
ATOM   85    O O   . ASN A 1 18  A -2.692  -16.669 27.600  1.00 48.87 ? 19  ASN A O   1 
ATOM   86    C CB  . ASN A 1 18  A -0.406  -16.018 24.910  1.00 48.57 ? 19  ASN A CB  1 
ATOM   87    C CG  . ASN A 1 18  A -1.213  -14.782 24.497  1.00 48.60 ? 19  ASN A CG  1 
ATOM   88    O OD1 . ASN A 1 18  A -2.265  -14.479 25.063  1.00 48.14 ? 19  ASN A OD1 1 
ATOM   89    N ND2 . ASN A 1 18  A -0.710  -14.065 23.500  1.00 48.39 ? 19  ASN A ND2 1 
ATOM   90    N N   . ASN A 1 19  ? -0.606  -15.816 27.731  1.00 49.35 ? 20  ASN A N   1 
ATOM   91    C CA  . ASN A 1 19  ? -0.773  -15.259 29.072  1.00 49.76 ? 20  ASN A CA  1 
ATOM   92    C C   . ASN A 1 19  ? -1.104  -13.761 29.067  1.00 49.56 ? 20  ASN A C   1 
ATOM   93    O O   . ASN A 1 19  ? -0.903  -13.064 30.067  1.00 49.71 ? 20  ASN A O   1 
ATOM   94    C CB  . ASN A 1 19  ? 0.471   -15.561 29.927  1.00 49.98 ? 20  ASN A CB  1 
ATOM   95    C CG  . ASN A 1 19  ? 0.561   -17.030 30.336  1.00 50.75 ? 20  ASN A CG  1 
ATOM   96    O OD1 . ASN A 1 19  ? 1.611   -17.669 30.198  1.00 52.01 ? 20  ASN A OD1 1 
ATOM   97    N ND2 . ASN A 1 19  ? -0.546  -17.570 30.842  1.00 50.99 ? 20  ASN A ND2 1 
ATOM   98    N N   . SER A 1 20  ? -1.625  -13.283 27.938  1.00 49.30 ? 21  SER A N   1 
ATOM   99    C CA  . SER A 1 20  ? -2.012  -11.883 27.778  1.00 48.87 ? 21  SER A CA  1 
ATOM   100   C C   . SER A 1 20  ? -3.301  -11.567 28.533  1.00 48.67 ? 21  SER A C   1 
ATOM   101   O O   . SER A 1 20  ? -4.239  -12.371 28.558  1.00 48.63 ? 21  SER A O   1 
ATOM   102   C CB  . SER A 1 20  ? -2.169  -11.537 26.296  1.00 48.82 ? 21  SER A CB  1 
ATOM   103   O OG  . SER A 1 20  ? -2.552  -10.186 26.119  1.00 48.82 ? 21  SER A OG  1 
ATOM   104   N N   . THR A 1 21  ? -3.330  -10.389 29.149  1.00 48.25 ? 22  THR A N   1 
ATOM   105   C CA  . THR A 1 21  ? -4.492  -9.930  29.905  1.00 47.83 ? 22  THR A CA  1 
ATOM   106   C C   . THR A 1 21  ? -5.048  -8.635  29.316  1.00 47.59 ? 22  THR A C   1 
ATOM   107   O O   . THR A 1 21  ? -5.906  -7.981  29.921  1.00 47.45 ? 22  THR A O   1 
ATOM   108   C CB  . THR A 1 21  ? -4.148  -9.702  31.390  1.00 47.85 ? 22  THR A CB  1 
ATOM   109   O OG1 . THR A 1 21  ? -3.033  -8.805  31.487  1.00 47.66 ? 22  THR A OG1 1 
ATOM   110   C CG2 . THR A 1 21  ? -3.822  -11.022 32.083  1.00 47.53 ? 22  THR A CG2 1 
ATOM   111   N N   . GLU A 1 22  ? -4.546  -8.272  28.137  1.00 47.30 ? 23  GLU A N   1 
ATOM   112   C CA  . GLU A 1 22  ? -4.991  -7.078  27.431  1.00 47.23 ? 23  GLU A CA  1 
ATOM   113   C C   . GLU A 1 22  ? -6.447  -7.237  26.992  1.00 46.65 ? 23  GLU A C   1 
ATOM   114   O O   . GLU A 1 22  ? -6.828  -8.265  26.420  1.00 46.55 ? 23  GLU A O   1 
ATOM   115   C CB  . GLU A 1 22  ? -4.089  -6.803  26.226  1.00 47.54 ? 23  GLU A CB  1 
ATOM   116   C CG  . GLU A 1 22  ? -4.042  -5.329  25.804  1.00 49.49 ? 23  GLU A CG  1 
ATOM   117   C CD  . GLU A 1 22  ? -2.898  -4.538  26.441  1.00 51.45 ? 23  GLU A CD  1 
ATOM   118   O OE1 . GLU A 1 22  ? -2.452  -4.891  27.558  1.00 52.22 ? 23  GLU A OE1 1 
ATOM   119   O OE2 . GLU A 1 22  ? -2.452  -3.548  25.815  1.00 51.80 ? 23  GLU A OE2 1 
ATOM   120   N N   . GLN A 1 23  ? -7.247  -6.211  27.275  1.00 45.97 ? 24  GLN A N   1 
ATOM   121   C CA  . GLN A 1 23  ? -8.691  -6.250  27.056  1.00 45.26 ? 24  GLN A CA  1 
ATOM   122   C C   . GLN A 1 23  ? -9.159  -5.244  26.010  1.00 44.75 ? 24  GLN A C   1 
ATOM   123   O O   . GLN A 1 23  ? -8.679  -4.110  25.975  1.00 44.77 ? 24  GLN A O   1 
ATOM   124   C CB  . GLN A 1 23  ? -9.426  -5.985  28.370  1.00 45.31 ? 24  GLN A CB  1 
ATOM   125   C CG  . GLN A 1 23  ? -9.114  -6.988  29.468  1.00 45.68 ? 24  GLN A CG  1 
ATOM   126   C CD  . GLN A 1 23  ? -10.103 -6.938  30.611  1.00 46.08 ? 24  GLN A CD  1 
ATOM   127   O OE1 . GLN A 1 23  ? -10.628 -5.876  30.953  1.00 46.46 ? 24  GLN A OE1 1 
ATOM   128   N NE2 . GLN A 1 23  ? -10.362 -8.093  31.217  1.00 46.33 ? 24  GLN A NE2 1 
ATOM   129   N N   . VAL A 1 24  ? -10.099 -5.669  25.166  1.00 44.15 ? 25  VAL A N   1 
ATOM   130   C CA  . VAL A 1 24  ? -10.768 -4.778  24.207  1.00 43.44 ? 25  VAL A CA  1 
ATOM   131   C C   . VAL A 1 24  ? -12.285 -4.780  24.401  1.00 43.13 ? 25  VAL A C   1 
ATOM   132   O O   . VAL A 1 24  ? -12.844 -5.698  25.010  1.00 42.90 ? 25  VAL A O   1 
ATOM   133   C CB  . VAL A 1 24  ? -10.454 -5.135  22.728  1.00 43.46 ? 25  VAL A CB  1 
ATOM   134   C CG1 . VAL A 1 24  ? -8.963  -5.043  22.443  1.00 43.35 ? 25  VAL A CG1 1 
ATOM   135   C CG2 . VAL A 1 24  ? -11.005 -6.512  22.358  1.00 43.27 ? 25  VAL A CG2 1 
ATOM   136   N N   . ASP A 1 25  ? -12.940 -3.745  23.877  1.00 42.63 ? 26  ASP A N   1 
ATOM   137   C CA  . ASP A 1 25  ? -14.398 -3.663  23.885  1.00 42.15 ? 26  ASP A CA  1 
ATOM   138   C C   . ASP A 1 25  ? -14.989 -3.861  22.486  1.00 41.65 ? 26  ASP A C   1 
ATOM   139   O O   . ASP A 1 25  ? -14.348 -3.551  21.473  1.00 41.31 ? 26  ASP A O   1 
ATOM   140   C CB  . ASP A 1 25  ? -14.864 -2.324  24.469  1.00 42.33 ? 26  ASP A CB  1 
ATOM   141   C CG  . ASP A 1 25  ? -14.545 -2.177  25.955  1.00 43.36 ? 26  ASP A CG  1 
ATOM   142   O OD1 . ASP A 1 25  ? -14.043 -3.144  26.571  1.00 45.21 ? 26  ASP A OD1 1 
ATOM   143   O OD2 . ASP A 1 25  ? -14.803 -1.085  26.513  1.00 43.58 ? 26  ASP A OD2 1 
ATOM   144   N N   . THR A 1 26  ? -16.205 -4.408  22.449  1.00 41.19 ? 27  THR A N   1 
ATOM   145   C CA  . THR A 1 26  ? -17.018 -4.491  21.230  1.00 40.62 ? 27  THR A CA  1 
ATOM   146   C C   . THR A 1 26  ? -18.405 -3.915  21.517  1.00 40.48 ? 27  THR A C   1 
ATOM   147   O O   . THR A 1 26  ? -18.720 -3.593  22.663  1.00 40.38 ? 27  THR A O   1 
ATOM   148   C CB  . THR A 1 26  ? -17.159 -5.949  20.685  1.00 40.56 ? 27  THR A CB  1 
ATOM   149   O OG1 . THR A 1 26  ? -17.885 -6.761  21.618  1.00 40.06 ? 27  THR A OG1 1 
ATOM   150   C CG2 . THR A 1 26  ? -15.800 -6.582  20.401  1.00 40.14 ? 27  THR A CG2 1 
ATOM   151   N N   . ILE A 1 27  ? -19.229 -3.813  20.481  1.00 40.50 ? 28  ILE A N   1 
ATOM   152   C CA  . ILE A 1 27  ? -20.583 -3.302  20.631  1.00 40.37 ? 28  ILE A CA  1 
ATOM   153   C C   . ILE A 1 27  ? -21.438 -4.246  21.470  1.00 40.14 ? 28  ILE A C   1 
ATOM   154   O O   . ILE A 1 27  ? -22.414 -3.825  22.088  1.00 40.15 ? 28  ILE A O   1 
ATOM   155   C CB  . ILE A 1 27  ? -21.262 -3.108  19.263  1.00 40.48 ? 28  ILE A CB  1 
ATOM   156   C CG1 . ILE A 1 27  ? -20.445 -2.154  18.391  1.00 40.94 ? 28  ILE A CG1 1 
ATOM   157   C CG2 . ILE A 1 27  ? -22.680 -2.592  19.441  1.00 40.39 ? 28  ILE A CG2 1 
ATOM   158   C CD1 . ILE A 1 27  ? -20.278 -0.776  18.985  1.00 40.49 ? 28  ILE A CD1 1 
ATOM   159   N N   . MET A 1 28  ? -21.069 -5.523  21.489  1.00 46.25 ? 31  MET A N   1 
ATOM   160   C CA  . MET A 1 28  ? -21.832 -6.522  22.233  1.00 46.01 ? 31  MET A CA  1 
ATOM   161   C C   . MET A 1 28  ? -21.153 -7.054  23.496  1.00 45.80 ? 31  MET A C   1 
ATOM   162   O O   . MET A 1 28  ? -21.835 -7.521  24.407  1.00 45.60 ? 31  MET A O   1 
ATOM   163   C CB  . MET A 1 28  ? -22.211 -7.700  21.327  1.00 46.09 ? 31  MET A CB  1 
ATOM   164   C CG  . MET A 1 28  ? -23.286 -7.386  20.299  1.00 46.25 ? 31  MET A CG  1 
ATOM   165   S SD  . MET A 1 28  ? -24.032 -8.871  19.594  1.00 46.98 ? 31  MET A SD  1 
ATOM   166   C CE  . MET A 1 28  ? -22.588 -9.705  18.945  1.00 46.52 ? 31  MET A CE  1 
ATOM   167   N N   . GLU A 1 29  ? -19.826 -7.000  23.563  1.00 45.73 ? 32  GLU A N   1 
ATOM   168   C CA  . GLU A 1 29  ? -19.152 -7.539  24.739  1.00 45.83 ? 32  GLU A CA  1 
ATOM   169   C C   . GLU A 1 29  ? -18.004 -6.636  25.179  1.00 45.71 ? 32  GLU A C   1 
ATOM   170   O O   . GLU A 1 29  ? -17.087 -6.360  24.407  1.00 45.34 ? 32  GLU A O   1 
ATOM   171   C CB  . GLU A 1 29  ? -18.633 -8.950  24.459  1.00 45.92 ? 32  GLU A CB  1 
ATOM   172   C CG  . GLU A 1 29  ? -18.318 -9.755  25.710  1.00 46.51 ? 32  GLU A CG  1 
ATOM   173   C CD  . GLU A 1 29  ? -17.925 -11.186 25.398  1.00 47.13 ? 32  GLU A CD  1 
ATOM   174   O OE1 . GLU A 1 29  ? -17.875 -11.543 24.203  1.00 47.38 ? 32  GLU A OE1 1 
ATOM   175   O OE2 . GLU A 1 29  ? -17.667 -11.953 26.349  1.00 47.33 ? 32  GLU A OE2 1 
ATOM   176   N N   . LYS A 1 30  ? -18.063 -6.179  26.426  1.00 45.84 ? 33  LYS A N   1 
ATOM   177   C CA  . LYS A 1 30  ? -17.031 -5.310  26.972  1.00 46.20 ? 33  LYS A CA  1 
ATOM   178   C C   . LYS A 1 30  ? -15.972 -6.144  27.702  1.00 46.10 ? 33  LYS A C   1 
ATOM   179   O O   . LYS A 1 30  ? -16.264 -7.232  28.206  1.00 45.90 ? 33  LYS A O   1 
ATOM   180   C CB  . LYS A 1 30  ? -17.657 -4.267  27.905  1.00 46.32 ? 33  LYS A CB  1 
ATOM   181   C CG  . LYS A 1 30  ? -18.579 -3.268  27.194  1.00 47.40 ? 33  LYS A CG  1 
ATOM   182   C CD  . LYS A 1 30  ? -19.626 -2.690  28.151  1.00 49.45 ? 33  LYS A CD  1 
ATOM   183   C CE  . LYS A 1 30  ? -20.896 -2.244  27.412  1.00 50.39 ? 33  LYS A CE  1 
ATOM   184   N NZ  . LYS A 1 30  ? -22.102 -2.198  28.306  1.00 50.01 ? 33  LYS A NZ  1 
ATOM   185   N N   . ASN A 1 31  ? -14.749 -5.627  27.755  1.00 46.19 ? 34  ASN A N   1 
ATOM   186   C CA  . ASN A 1 31  ? -13.668 -6.272  28.494  1.00 46.36 ? 34  ASN A CA  1 
ATOM   187   C C   . ASN A 1 31  ? -13.333 -7.690  28.031  1.00 45.73 ? 34  ASN A C   1 
ATOM   188   O O   . ASN A 1 31  ? -13.100 -8.577  28.852  1.00 45.66 ? 34  ASN A O   1 
ATOM   189   C CB  . ASN A 1 31  ? -13.978 -6.275  29.994  1.00 46.91 ? 34  ASN A CB  1 
ATOM   190   C CG  . ASN A 1 31  ? -13.956 -4.883  30.596  1.00 48.68 ? 34  ASN A CG  1 
ATOM   191   O OD1 . ASN A 1 31  ? -13.401 -3.951  30.014  1.00 54.29 ? 34  ASN A OD1 1 
ATOM   192   N ND2 . ASN A 1 31  ? -14.561 -4.736  31.769  1.00 49.90 ? 34  ASN A ND2 1 
ATOM   193   N N   . VAL A 1 32  ? -13.301 -7.898  26.719  1.00 45.10 ? 35  VAL A N   1 
ATOM   194   C CA  . VAL A 1 32  ? -12.888 -9.179  26.164  1.00 44.27 ? 35  VAL A CA  1 
ATOM   195   C C   . VAL A 1 32  ? -11.372 -9.281  26.261  1.00 43.86 ? 35  VAL A C   1 
ATOM   196   O O   . VAL A 1 32  ? -10.651 -8.402  25.783  1.00 43.53 ? 35  VAL A O   1 
ATOM   197   C CB  . VAL A 1 32  ? -13.315 -9.333  24.689  1.00 44.24 ? 35  VAL A CB  1 
ATOM   198   C CG1 . VAL A 1 32  ? -13.113 -10.774 24.221  1.00 43.99 ? 35  VAL A CG1 1 
ATOM   199   C CG2 . VAL A 1 32  ? -14.760 -8.900  24.499  1.00 44.06 ? 35  VAL A CG2 1 
ATOM   200   N N   . THR A 1 33  A -10.894 -10.348 26.892  1.00 43.44 ? 35  THR A N   1 
ATOM   201   C CA  . THR A 1 33  A -9.462  -10.598 26.960  1.00 43.11 ? 35  THR A CA  1 
ATOM   202   C C   . THR A 1 33  A -8.997  -11.117 25.607  1.00 43.01 ? 35  THR A C   1 
ATOM   203   O O   . THR A 1 33  A -9.497  -12.125 25.097  1.00 42.92 ? 35  THR A O   1 
ATOM   204   C CB  . THR A 1 33  A -9.074  -11.563 28.107  1.00 43.10 ? 35  THR A CB  1 
ATOM   205   O OG1 . THR A 1 33  A -9.691  -11.130 29.325  1.00 42.62 ? 35  THR A OG1 1 
ATOM   206   C CG2 . THR A 1 33  A -7.563  -11.585 28.300  1.00 42.84 ? 35  THR A CG2 1 
ATOM   207   N N   . VAL A 1 34  ? -8.054  -10.393 25.022  1.00 42.97 ? 36  VAL A N   1 
ATOM   208   C CA  . VAL A 1 34  ? -7.578  -10.697 23.688  1.00 42.92 ? 36  VAL A CA  1 
ATOM   209   C C   . VAL A 1 34  ? -6.106  -11.129 23.762  1.00 42.95 ? 36  VAL A C   1 
ATOM   210   O O   . VAL A 1 34  ? -5.436  -10.912 24.779  1.00 42.98 ? 36  VAL A O   1 
ATOM   211   C CB  . VAL A 1 34  ? -7.853  -9.504  22.716  1.00 42.98 ? 36  VAL A CB  1 
ATOM   212   C CG1 . VAL A 1 34  ? -6.701  -8.506  22.694  1.00 42.60 ? 36  VAL A CG1 1 
ATOM   213   C CG2 . VAL A 1 34  ? -8.168  -10.006 21.317  1.00 43.11 ? 36  VAL A CG2 1 
ATOM   214   N N   . THR A 1 35  ? -5.617  -11.741 22.691  1.00 42.87 ? 37  THR A N   1 
ATOM   215   C CA  . THR A 1 35  ? -4.339  -12.437 22.706  1.00 42.88 ? 37  THR A CA  1 
ATOM   216   C C   . THR A 1 35  ? -3.185  -11.533 22.246  1.00 42.95 ? 37  THR A C   1 
ATOM   217   O O   . THR A 1 35  ? -2.048  -11.677 22.707  1.00 43.09 ? 37  THR A O   1 
ATOM   218   C CB  . THR A 1 35  ? -4.456  -13.756 21.891  1.00 42.92 ? 37  THR A CB  1 
ATOM   219   O OG1 . THR A 1 35  ? -3.862  -14.835 22.620  1.00 44.08 ? 37  THR A OG1 1 
ATOM   220   C CG2 . THR A 1 35  ? -3.855  -13.648 20.488  1.00 42.38 ? 37  THR A CG2 1 
ATOM   221   N N   . HIS A 1 36  ? -3.496  -10.611 21.334  1.00 42.73 ? 38  HIS A N   1 
ATOM   222   C CA  . HIS A 1 36  ? -2.610  -9.520  20.941  1.00 42.48 ? 38  HIS A CA  1 
ATOM   223   C C   . HIS A 1 36  ? -3.483  -8.286  20.746  1.00 42.26 ? 38  HIS A C   1 
ATOM   224   O O   . HIS A 1 36  ? -4.509  -8.346  20.064  1.00 42.41 ? 38  HIS A O   1 
ATOM   225   C CB  . HIS A 1 36  ? -1.900  -9.818  19.619  1.00 42.57 ? 38  HIS A CB  1 
ATOM   226   C CG  . HIS A 1 36  ? -0.921  -10.948 19.680  1.00 43.52 ? 38  HIS A CG  1 
ATOM   227   N ND1 . HIS A 1 36  ? -1.309  -12.268 19.764  1.00 43.50 ? 38  HIS A ND1 1 
ATOM   228   C CD2 . HIS A 1 36  ? 0.432   -10.957 19.626  1.00 43.92 ? 38  HIS A CD2 1 
ATOM   229   C CE1 . HIS A 1 36  ? -0.238  -13.040 19.785  1.00 43.66 ? 38  HIS A CE1 1 
ATOM   230   N NE2 . HIS A 1 36  ? 0.832   -12.270 19.700  1.00 43.75 ? 38  HIS A NE2 1 
ATOM   231   N N   . ALA A 1 37  ? -3.085  -7.168  21.338  1.00 41.75 ? 39  ALA A N   1 
ATOM   232   C CA  . ALA A 1 37  ? -3.786  -5.908  21.113  1.00 41.24 ? 39  ALA A CA  1 
ATOM   233   C C   . ALA A 1 37  ? -2.816  -4.793  20.744  1.00 40.90 ? 39  ALA A C   1 
ATOM   234   O O   . ALA A 1 37  ? -1.598  -4.978  20.771  1.00 40.88 ? 39  ALA A O   1 
ATOM   235   C CB  . ALA A 1 37  ? -4.611  -5.528  22.329  1.00 41.02 ? 39  ALA A CB  1 
ATOM   236   N N   . GLN A 1 38  ? -3.367  -3.641  20.380  1.00 40.58 ? 40  GLN A N   1 
ATOM   237   C CA  . GLN A 1 38  ? -2.564  -2.465  20.085  1.00 40.32 ? 40  GLN A CA  1 
ATOM   238   C C   . GLN A 1 38  ? -3.262  -1.227  20.611  1.00 39.99 ? 40  GLN A C   1 
ATOM   239   O O   . GLN A 1 38  ? -4.396  -0.928  20.231  1.00 40.06 ? 40  GLN A O   1 
ATOM   240   C CB  . GLN A 1 38  ? -2.286  -2.343  18.586  1.00 40.31 ? 40  GLN A CB  1 
ATOM   241   C CG  . GLN A 1 38  ? -1.278  -1.251  18.225  1.00 40.79 ? 40  GLN A CG  1 
ATOM   242   C CD  . GLN A 1 38  ? -0.893  -1.266  16.753  1.00 41.49 ? 40  GLN A CD  1 
ATOM   243   O OE1 . GLN A 1 38  ? -0.662  -2.326  16.169  1.00 42.35 ? 40  GLN A OE1 1 
ATOM   244   N NE2 . GLN A 1 38  ? -0.813  -0.085  16.151  1.00 41.12 ? 40  GLN A NE2 1 
ATOM   245   N N   . ASP A 1 39  ? -2.583  -0.536  21.520  1.00 39.75 ? 41  ASP A N   1 
ATOM   246   C CA  . ASP A 1 39  ? -3.038  0.742   22.032  1.00 39.29 ? 41  ASP A CA  1 
ATOM   247   C C   . ASP A 1 39  ? -2.667  1.801   21.003  1.00 38.92 ? 41  ASP A C   1 
ATOM   248   O O   . ASP A 1 39  ? -1.558  1.787   20.460  1.00 38.69 ? 41  ASP A O   1 
ATOM   249   C CB  . ASP A 1 39  ? -2.380  1.042   23.383  1.00 39.43 ? 41  ASP A CB  1 
ATOM   250   C CG  . ASP A 1 39  ? -2.978  2.260   24.076  1.00 40.30 ? 41  ASP A CG  1 
ATOM   251   O OD1 . ASP A 1 39  ? -4.037  2.754   23.633  1.00 41.10 ? 41  ASP A OD1 1 
ATOM   252   O OD2 . ASP A 1 39  ? -2.389  2.728   25.072  1.00 41.85 ? 41  ASP A OD2 1 
ATOM   253   N N   . ILE A 1 40  ? -3.604  2.703   20.728  1.00 38.50 ? 42  ILE A N   1 
ATOM   254   C CA  . ILE A 1 40  ? -3.396  3.759   19.739  1.00 38.27 ? 42  ILE A CA  1 
ATOM   255   C C   . ILE A 1 40  ? -3.610  5.166   20.330  1.00 38.13 ? 42  ILE A C   1 
ATOM   256   O O   . ILE A 1 40  ? -3.640  6.163   19.603  1.00 37.94 ? 42  ILE A O   1 
ATOM   257   C CB  . ILE A 1 40  ? -4.262  3.532   18.462  1.00 38.18 ? 42  ILE A CB  1 
ATOM   258   C CG1 . ILE A 1 40  ? -5.709  3.188   18.832  1.00 38.34 ? 42  ILE A CG1 1 
ATOM   259   C CG2 . ILE A 1 40  ? -3.653  2.433   17.597  1.00 38.03 ? 42  ILE A CG2 1 
ATOM   260   C CD1 . ILE A 1 40  ? -6.686  3.209   17.660  1.00 37.98 ? 42  ILE A CD1 1 
ATOM   261   N N   . LEU A 1 41  ? -3.722  5.229   21.656  1.00 37.83 ? 43  LEU A N   1 
ATOM   262   C CA  . LEU A 1 41  ? -3.968  6.478   22.371  1.00 37.63 ? 43  LEU A CA  1 
ATOM   263   C C   . LEU A 1 41  ? -2.825  6.843   23.329  1.00 37.74 ? 43  LEU A C   1 
ATOM   264   O O   . LEU A 1 41  ? -2.457  6.060   24.210  1.00 37.59 ? 43  LEU A O   1 
ATOM   265   C CB  . LEU A 1 41  ? -5.292  6.386   23.138  1.00 37.55 ? 43  LEU A CB  1 
ATOM   266   C CG  . LEU A 1 41  ? -5.866  7.625   23.832  1.00 37.13 ? 43  LEU A CG  1 
ATOM   267   C CD1 . LEU A 1 41  ? -6.197  8.700   22.828  1.00 36.17 ? 43  LEU A CD1 1 
ATOM   268   C CD2 . LEU A 1 41  ? -7.102  7.254   24.625  1.00 36.99 ? 43  LEU A CD2 1 
ATOM   269   N N   . GLU A 1 42  ? -2.272  8.038   23.134  1.00 37.87 ? 44  GLU A N   1 
ATOM   270   C CA  . GLU A 1 42  ? -1.265  8.604   24.023  1.00 37.82 ? 44  GLU A CA  1 
ATOM   271   C C   . GLU A 1 42  ? -1.945  9.353   25.164  1.00 37.94 ? 44  GLU A C   1 
ATOM   272   O O   . GLU A 1 42  ? -2.757  10.251  24.927  1.00 37.91 ? 44  GLU A O   1 
ATOM   273   C CB  . GLU A 1 42  ? -0.343  9.548   23.247  1.00 37.88 ? 44  GLU A CB  1 
ATOM   274   C CG  . GLU A 1 42  ? 0.762   10.183  24.081  1.00 38.68 ? 44  GLU A CG  1 
ATOM   275   C CD  . GLU A 1 42  ? 1.567   9.154   24.850  1.00 39.57 ? 44  GLU A CD  1 
ATOM   276   O OE1 . GLU A 1 42  ? 2.472   8.530   24.254  1.00 38.81 ? 44  GLU A OE1 1 
ATOM   277   O OE2 . GLU A 1 42  ? 1.277   8.966   26.051  1.00 40.63 ? 44  GLU A OE2 1 
ATOM   278   N N   . LYS A 1 43  ? -1.608  8.988   26.400  1.00 38.00 ? 45  LYS A N   1 
ATOM   279   C CA  . LYS A 1 43  ? -2.247  9.585   27.573  1.00 38.13 ? 45  LYS A CA  1 
ATOM   280   C C   . LYS A 1 43  ? -1.259  10.365  28.431  1.00 38.07 ? 45  LYS A C   1 
ATOM   281   O O   . LYS A 1 43  ? -1.592  10.782  29.543  1.00 37.91 ? 45  LYS A O   1 
ATOM   282   C CB  . LYS A 1 43  ? -2.922  8.509   28.432  1.00 38.29 ? 45  LYS A CB  1 
ATOM   283   C CG  . LYS A 1 43  ? -3.898  7.604   27.694  1.00 39.34 ? 45  LYS A CG  1 
ATOM   284   C CD  . LYS A 1 43  ? -4.151  6.331   28.491  1.00 40.28 ? 45  LYS A CD  1 
ATOM   285   C CE  . LYS A 1 43  ? -4.491  5.167   27.582  1.00 41.00 ? 45  LYS A CE  1 
ATOM   286   N NZ  . LYS A 1 43  ? -3.324  4.709   26.758  1.00 40.83 ? 45  LYS A NZ  1 
ATOM   287   N N   . THR A 1 44  ? -0.053  10.579  27.910  1.00 38.11 ? 46  THR A N   1 
ATOM   288   C CA  . THR A 1 44  ? 1.045   11.082  28.737  1.00 37.98 ? 46  THR A CA  1 
ATOM   289   C C   . THR A 1 44  ? 1.761   12.289  28.129  1.00 37.62 ? 46  THR A C   1 
ATOM   290   O O   . THR A 1 44  ? 1.911   12.387  26.912  1.00 37.80 ? 46  THR A O   1 
ATOM   291   C CB  . THR A 1 44  ? 2.038   9.921   29.099  1.00 37.99 ? 46  THR A CB  1 
ATOM   292   O OG1 . THR A 1 44  ? 2.446   10.039  30.464  1.00 39.05 ? 46  THR A OG1 1 
ATOM   293   C CG2 . THR A 1 44  ? 3.268   9.894   28.194  1.00 37.93 ? 46  THR A CG2 1 
ATOM   294   N N   . HIS A 1 45  ? 2.186   13.207  28.993  1.00 37.44 ? 47  HIS A N   1 
ATOM   295   C CA  . HIS A 1 45  ? 2.940   14.399  28.586  1.00 37.00 ? 47  HIS A CA  1 
ATOM   296   C C   . HIS A 1 45  ? 4.012   14.752  29.622  1.00 37.07 ? 47  HIS A C   1 
ATOM   297   O O   . HIS A 1 45  ? 3.950   14.282  30.754  1.00 36.95 ? 47  HIS A O   1 
ATOM   298   C CB  . HIS A 1 45  ? 1.994   15.585  28.360  1.00 36.65 ? 47  HIS A CB  1 
ATOM   299   C CG  . HIS A 1 45  ? 1.278   16.033  29.595  1.00 35.47 ? 47  HIS A CG  1 
ATOM   300   N ND1 . HIS A 1 45  ? 1.813   16.952  30.471  1.00 34.83 ? 47  HIS A ND1 1 
ATOM   301   C CD2 . HIS A 1 45  ? 0.068   15.694  30.097  1.00 34.68 ? 47  HIS A CD2 1 
ATOM   302   C CE1 . HIS A 1 45  ? 0.966   17.155  31.464  1.00 34.57 ? 47  HIS A CE1 1 
ATOM   303   N NE2 . HIS A 1 45  ? -0.101  16.404  31.261  1.00 34.37 ? 47  HIS A NE2 1 
ATOM   304   N N   . ASN A 1 46  ? 4.979   15.587  29.242  1.00 37.31 ? 48  ASN A N   1 
ATOM   305   C CA  . ASN A 1 46  ? 6.107   15.903  30.128  1.00 37.61 ? 48  ASN A CA  1 
ATOM   306   C C   . ASN A 1 46  ? 5.876   17.070  31.097  1.00 37.80 ? 48  ASN A C   1 
ATOM   307   O O   . ASN A 1 46  ? 6.728   17.361  31.943  1.00 38.03 ? 48  ASN A O   1 
ATOM   308   C CB  . ASN A 1 46  ? 7.416   16.078  29.336  1.00 37.55 ? 48  ASN A CB  1 
ATOM   309   C CG  . ASN A 1 46  ? 7.449   17.352  28.508  1.00 37.79 ? 48  ASN A CG  1 
ATOM   310   O OD1 . ASN A 1 46  ? 6.592   18.227  28.639  1.00 38.42 ? 48  ASN A OD1 1 
ATOM   311   N ND2 . ASN A 1 46  ? 8.455   17.461  27.646  1.00 37.73 ? 48  ASN A ND2 1 
ATOM   312   N N   . GLY A 1 47  ? 4.732   17.737  30.960  1.00 37.87 ? 49  GLY A N   1 
ATOM   313   C CA  . GLY A 1 47  ? 4.342   18.811  31.873  1.00 37.64 ? 49  GLY A CA  1 
ATOM   314   C C   . GLY A 1 47  ? 5.141   20.095  31.734  1.00 37.69 ? 49  GLY A C   1 
ATOM   315   O O   . GLY A 1 47  ? 5.104   20.949  32.621  1.00 37.61 ? 49  GLY A O   1 
ATOM   316   N N   . LYS A 1 48  ? 5.850   20.245  30.617  1.00 37.78 ? 50  LYS A N   1 
ATOM   317   C CA  . LYS A 1 48  ? 6.712   21.408  30.405  1.00 38.04 ? 50  LYS A CA  1 
ATOM   318   C C   . LYS A 1 48  ? 6.488   22.098  29.060  1.00 38.01 ? 50  LYS A C   1 
ATOM   319   O O   . LYS A 1 48  ? 6.009   21.486  28.104  1.00 37.87 ? 50  LYS A O   1 
ATOM   320   C CB  . LYS A 1 48  ? 8.188   21.012  30.558  1.00 38.14 ? 50  LYS A CB  1 
ATOM   321   C CG  . LYS A 1 48  ? 8.572   20.638  31.980  1.00 39.09 ? 50  LYS A CG  1 
ATOM   322   C CD  . LYS A 1 48  ? 9.861   19.840  32.046  1.00 41.14 ? 50  LYS A CD  1 
ATOM   323   C CE  . LYS A 1 48  ? 10.082  19.333  33.465  1.00 42.55 ? 50  LYS A CE  1 
ATOM   324   N NZ  . LYS A 1 48  ? 11.516  19.107  33.773  1.00 43.69 ? 50  LYS A NZ  1 
ATOM   325   N N   . LEU A 1 49  ? 6.837   23.379  29.003  1.00 37.98 ? 51  LEU A N   1 
ATOM   326   C CA  . LEU A 1 49  ? 6.853   24.114  27.752  1.00 38.27 ? 51  LEU A CA  1 
ATOM   327   C C   . LEU A 1 49  ? 8.246   24.027  27.156  1.00 38.64 ? 51  LEU A C   1 
ATOM   328   O O   . LEU A 1 49  ? 9.243   24.259  27.850  1.00 38.96 ? 51  LEU A O   1 
ATOM   329   C CB  . LEU A 1 49  ? 6.450   25.573  27.969  1.00 38.28 ? 51  LEU A CB  1 
ATOM   330   C CG  . LEU A 1 49  ? 5.103   25.860  28.648  1.00 38.28 ? 51  LEU A CG  1 
ATOM   331   C CD1 . LEU A 1 49  ? 4.927   27.360  28.856  1.00 37.48 ? 51  LEU A CD1 1 
ATOM   332   C CD2 . LEU A 1 49  ? 3.921   25.269  27.862  1.00 37.69 ? 51  LEU A CD2 1 
ATOM   333   N N   . CYS A 1 50  ? 8.310   23.680  25.873  1.00 38.82 ? 52  CYS A N   1 
ATOM   334   C CA  . CYS A 1 50  ? 9.575   23.409  25.197  1.00 39.12 ? 52  CYS A CA  1 
ATOM   335   C C   . CYS A 1 50  ? 9.698   24.194  23.910  1.00 39.27 ? 52  CYS A C   1 
ATOM   336   O O   . CYS A 1 50  ? 8.747   24.841  23.472  1.00 39.31 ? 52  CYS A O   1 
ATOM   337   C CB  . CYS A 1 50  ? 9.686   21.922  24.859  1.00 39.12 ? 52  CYS A CB  1 
ATOM   338   S SG  . CYS A 1 50  ? 9.357   20.818  26.223  1.00 40.02 ? 52  CYS A SG  1 
ATOM   339   N N   . ASP A 1 51  ? 10.881  24.122  23.306  1.00 39.54 ? 53  ASP A N   1 
ATOM   340   C CA  . ASP A 1 51  ? 11.088  24.615  21.958  1.00 39.92 ? 53  ASP A CA  1 
ATOM   341   C C   . ASP A 1 51  ? 10.341  23.724  20.987  1.00 40.08 ? 53  ASP A C   1 
ATOM   342   O O   . ASP A 1 51  ? 10.154  22.533  21.241  1.00 40.12 ? 53  ASP A O   1 
ATOM   343   C CB  . ASP A 1 51  ? 12.568  24.590  21.590  1.00 40.09 ? 53  ASP A CB  1 
ATOM   344   C CG  . ASP A 1 51  ? 13.419  25.410  22.525  1.00 40.79 ? 53  ASP A CG  1 
ATOM   345   O OD1 . ASP A 1 51  ? 12.871  26.011  23.472  1.00 42.16 ? 53  ASP A OD1 1 
ATOM   346   O OD2 . ASP A 1 51  ? 14.646  25.451  22.310  1.00 41.88 ? 53  ASP A OD2 1 
ATOM   347   N N   . LEU A 1 52  A 9.911   24.317  19.882  1.00 40.25 ? 53  LEU A N   1 
ATOM   348   C CA  . LEU A 1 52  A 9.359   23.567  18.778  1.00 40.44 ? 53  LEU A CA  1 
ATOM   349   C C   . LEU A 1 52  A 10.448  23.483  17.714  1.00 40.65 ? 53  LEU A C   1 
ATOM   350   O O   . LEU A 1 52  A 10.803  24.490  17.093  1.00 40.53 ? 53  LEU A O   1 
ATOM   351   C CB  . LEU A 1 52  A 8.092   24.247  18.245  1.00 40.35 ? 53  LEU A CB  1 
ATOM   352   C CG  . LEU A 1 52  A 7.056   23.363  17.538  1.00 40.62 ? 53  LEU A CG  1 
ATOM   353   C CD1 . LEU A 1 52  A 6.383   22.388  18.507  1.00 40.00 ? 53  LEU A CD1 1 
ATOM   354   C CD2 . LEU A 1 52  A 6.012   24.218  16.828  1.00 40.28 ? 53  LEU A CD2 1 
ATOM   355   N N   . ASP A 1 53  ? 10.994  22.277  17.544  1.00 40.94 ? 54  ASP A N   1 
ATOM   356   C CA  . ASP A 1 53  ? 12.069  22.005  16.582  1.00 41.31 ? 54  ASP A CA  1 
ATOM   357   C C   . ASP A 1 53  ? 13.246  22.973  16.709  1.00 41.17 ? 54  ASP A C   1 
ATOM   358   O O   . ASP A 1 53  ? 13.652  23.613  15.730  1.00 41.44 ? 54  ASP A O   1 
ATOM   359   C CB  . ASP A 1 53  ? 11.531  22.002  15.145  1.00 41.64 ? 54  ASP A CB  1 
ATOM   360   C CG  . ASP A 1 53  ? 10.430  20.991  14.944  1.00 42.95 ? 54  ASP A CG  1 
ATOM   361   O OD1 . ASP A 1 53  ? 9.265   21.304  15.279  1.00 44.21 ? 54  ASP A OD1 1 
ATOM   362   O OD2 . ASP A 1 53  ? 10.732  19.881  14.456  1.00 44.89 ? 54  ASP A OD2 1 
ATOM   363   N N   . GLY A 1 54  ? 13.778  23.090  17.923  1.00 40.77 ? 55  GLY A N   1 
ATOM   364   C CA  . GLY A 1 54  ? 14.917  23.963  18.182  1.00 40.26 ? 55  GLY A CA  1 
ATOM   365   C C   . GLY A 1 54  ? 14.584  25.434  18.348  1.00 39.95 ? 55  GLY A C   1 
ATOM   366   O O   . GLY A 1 54  ? 15.423  26.201  18.817  1.00 40.12 ? 55  GLY A O   1 
ATOM   367   N N   . VAL A 1 55  ? 13.369  25.835  17.969  1.00 39.47 ? 56  VAL A N   1 
ATOM   368   C CA  . VAL A 1 55  ? 12.949  27.238  18.067  1.00 38.72 ? 56  VAL A CA  1 
ATOM   369   C C   . VAL A 1 55  ? 12.211  27.507  19.379  1.00 38.55 ? 56  VAL A C   1 
ATOM   370   O O   . VAL A 1 55  ? 11.158  26.928  19.641  1.00 38.48 ? 56  VAL A O   1 
ATOM   371   C CB  . VAL A 1 55  ? 12.076  27.672  16.870  1.00 38.63 ? 56  VAL A CB  1 
ATOM   372   C CG1 . VAL A 1 55  ? 11.802  29.171  16.936  1.00 38.64 ? 56  VAL A CG1 1 
ATOM   373   C CG2 . VAL A 1 55  ? 12.751  27.320  15.553  1.00 38.19 ? 56  VAL A CG2 1 
ATOM   374   N N   . LYS A 1 56  ? 12.778  28.395  20.192  1.00 38.35 ? 57  LYS A N   1 
ATOM   375   C CA  . LYS A 1 56  ? 12.233  28.726  21.509  1.00 38.23 ? 57  LYS A CA  1 
ATOM   376   C C   . LYS A 1 56  ? 10.951  29.558  21.412  1.00 37.91 ? 57  LYS A C   1 
ATOM   377   O O   . LYS A 1 56  ? 10.837  30.426  20.547  1.00 37.99 ? 57  LYS A O   1 
ATOM   378   C CB  . LYS A 1 56  ? 13.278  29.476  22.346  1.00 38.18 ? 57  LYS A CB  1 
ATOM   379   C CG  . LYS A 1 56  ? 12.947  29.541  23.826  1.00 38.89 ? 57  LYS A CG  1 
ATOM   380   C CD  . LYS A 1 56  ? 13.728  30.619  24.552  1.00 40.37 ? 57  LYS A CD  1 
ATOM   381   C CE  . LYS A 1 56  ? 13.200  30.775  25.971  1.00 41.63 ? 57  LYS A CE  1 
ATOM   382   N NZ  . LYS A 1 56  ? 13.776  31.956  26.674  1.00 42.75 ? 57  LYS A NZ  1 
ATOM   383   N N   . PRO A 1 57  ? 9.977   29.292  22.299  1.00 37.60 ? 58  PRO A N   1 
ATOM   384   C CA  . PRO A 1 57  ? 8.793   30.147  22.325  1.00 37.46 ? 58  PRO A CA  1 
ATOM   385   C C   . PRO A 1 57  ? 9.041   31.483  23.032  1.00 37.38 ? 58  PRO A C   1 
ATOM   386   O O   . PRO A 1 57  ? 10.054  31.651  23.718  1.00 37.50 ? 58  PRO A O   1 
ATOM   387   C CB  . PRO A 1 57  ? 7.784   29.318  23.121  1.00 37.43 ? 58  PRO A CB  1 
ATOM   388   C CG  . PRO A 1 57  ? 8.612   28.430  23.986  1.00 37.27 ? 58  PRO A CG  1 
ATOM   389   C CD  . PRO A 1 57  ? 9.847   28.130  23.202  1.00 37.54 ? 58  PRO A CD  1 
ATOM   390   N N   . LEU A 1 58  ? 8.119   32.423  22.849  1.00 37.08 ? 59  LEU A N   1 
ATOM   391   C CA  . LEU A 1 58  ? 8.108   33.650  23.627  1.00 36.74 ? 59  LEU A CA  1 
ATOM   392   C C   . LEU A 1 58  ? 7.150   33.484  24.806  1.00 36.78 ? 59  LEU A C   1 
ATOM   393   O O   . LEU A 1 58  ? 5.927   33.500  24.634  1.00 36.84 ? 59  LEU A O   1 
ATOM   394   C CB  . LEU A 1 58  ? 7.707   34.845  22.752  1.00 36.70 ? 59  LEU A CB  1 
ATOM   395   C CG  . LEU A 1 58  ? 7.480   36.213  23.413  1.00 36.32 ? 59  LEU A CG  1 
ATOM   396   C CD1 . LEU A 1 58  ? 8.715   36.683  24.180  1.00 35.49 ? 59  LEU A CD1 1 
ATOM   397   C CD2 . LEU A 1 58  ? 7.044   37.247  22.383  1.00 35.51 ? 59  LEU A CD2 1 
ATOM   398   N N   . ILE A 1 59  ? 7.717   33.296  25.996  1.00 36.63 ? 60  ILE A N   1 
ATOM   399   C CA  . ILE A 1 59  ? 6.939   33.238  27.227  1.00 36.59 ? 60  ILE A CA  1 
ATOM   400   C C   . ILE A 1 59  ? 6.864   34.656  27.806  1.00 36.59 ? 60  ILE A C   1 
ATOM   401   O O   . ILE A 1 59  ? 7.888   35.244  28.151  1.00 36.66 ? 60  ILE A O   1 
ATOM   402   C CB  . ILE A 1 59  ? 7.547   32.231  28.251  1.00 36.61 ? 60  ILE A CB  1 
ATOM   403   C CG1 . ILE A 1 59  ? 7.389   30.787  27.762  1.00 36.97 ? 60  ILE A CG1 1 
ATOM   404   C CG2 . ILE A 1 59  ? 6.875   32.342  29.609  1.00 36.68 ? 60  ILE A CG2 1 
ATOM   405   C CD1 . ILE A 1 59  ? 8.620   30.214  27.104  1.00 37.53 ? 60  ILE A CD1 1 
ATOM   406   N N   . LEU A 1 60  ? 5.654   35.203  27.902  1.00 36.48 ? 61  LEU A N   1 
ATOM   407   C CA  . LEU A 1 60  ? 5.479   36.599  28.312  1.00 36.44 ? 61  LEU A CA  1 
ATOM   408   C C   . LEU A 1 60  ? 5.455   36.803  29.832  1.00 36.69 ? 61  LEU A C   1 
ATOM   409   O O   . LEU A 1 60  ? 5.460   37.939  30.311  1.00 36.60 ? 61  LEU A O   1 
ATOM   410   C CB  . LEU A 1 60  ? 4.247   37.226  27.638  1.00 36.13 ? 61  LEU A CB  1 
ATOM   411   C CG  . LEU A 1 60  ? 4.367   37.603  26.154  1.00 35.57 ? 61  LEU A CG  1 
ATOM   412   C CD1 . LEU A 1 60  ? 3.016   38.007  25.584  1.00 34.35 ? 61  LEU A CD1 1 
ATOM   413   C CD2 . LEU A 1 60  ? 5.392   38.709  25.924  1.00 34.38 ? 61  LEU A CD2 1 
ATOM   414   N N   . ARG A 1 61  ? 5.454   35.696  30.577  1.00 37.02 ? 62  ARG A N   1 
ATOM   415   C CA  . ARG A 1 61  ? 5.541   35.708  32.045  1.00 37.53 ? 62  ARG A CA  1 
ATOM   416   C C   . ARG A 1 61  ? 4.384   36.508  32.652  1.00 37.32 ? 62  ARG A C   1 
ATOM   417   O O   . ARG A 1 61  ? 3.221   36.149  32.481  1.00 37.45 ? 62  ARG A O   1 
ATOM   418   C CB  . ARG A 1 61  ? 6.902   36.246  32.536  1.00 37.63 ? 62  ARG A CB  1 
ATOM   419   C CG  . ARG A 1 61  ? 8.104   35.844  31.689  1.00 39.59 ? 62  ARG A CG  1 
ATOM   420   C CD  . ARG A 1 61  ? 8.940   34.738  32.315  1.00 42.76 ? 62  ARG A CD  1 
ATOM   421   N NE  . ARG A 1 61  ? 10.002  35.271  33.171  1.00 44.69 ? 62  ARG A NE  1 
ATOM   422   C CZ  . ARG A 1 61  ? 10.083  35.079  34.486  1.00 46.16 ? 62  ARG A CZ  1 
ATOM   423   N NH1 . ARG A 1 61  ? 9.167   34.353  35.121  1.00 46.76 ? 62  ARG A NH1 1 
ATOM   424   N NH2 . ARG A 1 61  ? 11.089  35.609  35.170  1.00 46.62 ? 62  ARG A NH2 1 
ATOM   425   N N   . ASP A 1 62  ? 4.710   37.595  33.346  1.00 37.01 ? 63  ASP A N   1 
ATOM   426   C CA  . ASP A 1 62  ? 3.702   38.441  33.974  1.00 36.81 ? 63  ASP A CA  1 
ATOM   427   C C   . ASP A 1 62  ? 3.258   39.610  33.079  1.00 36.26 ? 63  ASP A C   1 
ATOM   428   O O   . ASP A 1 62  ? 2.475   40.457  33.504  1.00 36.36 ? 63  ASP A O   1 
ATOM   429   C CB  . ASP A 1 62  ? 4.202   38.932  35.340  1.00 37.04 ? 63  ASP A CB  1 
ATOM   430   C CG  . ASP A 1 62  ? 4.405   37.786  36.331  1.00 38.36 ? 63  ASP A CG  1 
ATOM   431   O OD1 . ASP A 1 62  ? 3.402   37.152  36.726  1.00 38.68 ? 63  ASP A OD1 1 
ATOM   432   O OD2 . ASP A 1 62  ? 5.568   37.513  36.709  1.00 39.99 ? 63  ASP A OD2 1 
ATOM   433   N N   . CYS A 1 63  ? 3.745   39.640  31.840  1.00 35.40 ? 64  CYS A N   1 
ATOM   434   C CA  . CYS A 1 63  ? 3.349   40.667  30.881  1.00 34.82 ? 64  CYS A CA  1 
ATOM   435   C C   . CYS A 1 63  ? 2.299   40.170  29.897  1.00 33.75 ? 64  CYS A C   1 
ATOM   436   O O   . CYS A 1 63  ? 2.160   38.970  29.668  1.00 33.68 ? 64  CYS A O   1 
ATOM   437   C CB  . CYS A 1 63  ? 4.565   41.191  30.118  1.00 35.11 ? 64  CYS A CB  1 
ATOM   438   S SG  . CYS A 1 63  ? 5.694   42.139  31.148  1.00 37.63 ? 64  CYS A SG  1 
ATOM   439   N N   . SER A 1 64  ? 1.558   41.106  29.319  1.00 32.56 ? 65  SER A N   1 
ATOM   440   C CA  . SER A 1 64  ? 0.588   40.780  28.284  1.00 31.45 ? 65  SER A CA  1 
ATOM   441   C C   . SER A 1 64  ? 1.088   41.265  26.930  1.00 30.69 ? 65  SER A C   1 
ATOM   442   O O   . SER A 1 64  ? 2.053   42.029  26.852  1.00 30.71 ? 65  SER A O   1 
ATOM   443   C CB  . SER A 1 64  ? -0.766  41.411  28.601  1.00 31.30 ? 65  SER A CB  1 
ATOM   444   O OG  . SER A 1 64  ? -0.696  42.820  28.488  1.00 31.31 ? 65  SER A OG  1 
ATOM   445   N N   . VAL A 1 65  ? 0.423   40.820  25.870  1.00 29.76 ? 66  VAL A N   1 
ATOM   446   C CA  . VAL A 1 65  ? 0.735   41.250  24.513  1.00 28.91 ? 66  VAL A CA  1 
ATOM   447   C C   . VAL A 1 65  ? 0.780   42.784  24.408  1.00 28.75 ? 66  VAL A C   1 
ATOM   448   O O   . VAL A 1 65  ? 1.736   43.339  23.867  1.00 28.76 ? 66  VAL A O   1 
ATOM   449   C CB  . VAL A 1 65  ? -0.252  40.621  23.487  1.00 28.86 ? 66  VAL A CB  1 
ATOM   450   C CG1 . VAL A 1 65  ? -0.131  41.282  22.115  1.00 27.77 ? 66  VAL A CG1 1 
ATOM   451   C CG2 . VAL A 1 65  ? -0.027  39.119  23.395  1.00 27.95 ? 66  VAL A CG2 1 
ATOM   452   N N   . ALA A 1 66  ? -0.234  43.460  24.944  1.00 28.56 ? 67  ALA A N   1 
ATOM   453   C CA  . ALA A 1 66  ? -0.245  44.924  24.983  1.00 28.73 ? 67  ALA A CA  1 
ATOM   454   C C   . ALA A 1 66  ? 0.922   45.482  25.798  1.00 28.91 ? 67  ALA A C   1 
ATOM   455   O O   . ALA A 1 66  ? 1.562   46.440  25.375  1.00 29.12 ? 67  ALA A O   1 
ATOM   456   C CB  . ALA A 1 66  ? -1.566  45.445  25.525  1.00 28.66 ? 67  ALA A CB  1 
ATOM   457   N N   . GLY A 1 67  ? 1.193   44.883  26.959  1.00 28.89 ? 68  GLY A N   1 
ATOM   458   C CA  . GLY A 1 67  ? 2.319   45.296  27.794  1.00 29.30 ? 68  GLY A CA  1 
ATOM   459   C C   . GLY A 1 67  ? 3.635   45.199  27.039  1.00 29.70 ? 68  GLY A C   1 
ATOM   460   O O   . GLY A 1 67  ? 4.431   46.146  27.030  1.00 29.74 ? 68  GLY A O   1 
ATOM   461   N N   . TRP A 1 68  ? 3.852   44.057  26.388  1.00 29.75 ? 69  TRP A N   1 
ATOM   462   C CA  . TRP A 1 68  ? 5.029   43.858  25.552  1.00 30.02 ? 69  TRP A CA  1 
ATOM   463   C C   . TRP A 1 68  ? 5.120   44.921  24.459  1.00 30.18 ? 69  TRP A C   1 
ATOM   464   O O   . TRP A 1 68  ? 6.054   45.720  24.446  1.00 30.32 ? 69  TRP A O   1 
ATOM   465   C CB  . TRP A 1 68  ? 5.048   42.431  24.972  1.00 30.04 ? 69  TRP A CB  1 
ATOM   466   C CG  . TRP A 1 68  ? 5.946   42.230  23.785  1.00 30.15 ? 69  TRP A CG  1 
ATOM   467   C CD1 . TRP A 1 68  ? 7.179   42.782  23.581  1.00 30.88 ? 69  TRP A CD1 1 
ATOM   468   C CD2 . TRP A 1 68  ? 5.686   41.400  22.642  1.00 31.05 ? 69  TRP A CD2 1 
ATOM   469   N NE1 . TRP A 1 68  ? 7.698   42.359  22.378  1.00 30.95 ? 69  TRP A NE1 1 
ATOM   470   C CE2 . TRP A 1 68  ? 6.802   41.510  21.783  1.00 31.09 ? 69  TRP A CE2 1 
ATOM   471   C CE3 . TRP A 1 68  ? 4.614   40.581  22.257  1.00 31.03 ? 69  TRP A CE3 1 
ATOM   472   C CZ2 . TRP A 1 68  ? 6.879   40.827  20.562  1.00 31.09 ? 69  TRP A CZ2 1 
ATOM   473   C CZ3 . TRP A 1 68  ? 4.694   39.902  21.044  1.00 30.86 ? 69  TRP A CZ3 1 
ATOM   474   C CH2 . TRP A 1 68  ? 5.819   40.030  20.215  1.00 30.59 ? 69  TRP A CH2 1 
ATOM   475   N N   . LEU A 1 69  ? 4.132   44.954  23.571  1.00 30.37 ? 70  LEU A N   1 
ATOM   476   C CA  . LEU A 1 69  ? 4.201   45.799  22.377  1.00 30.55 ? 70  LEU A CA  1 
ATOM   477   C C   . LEU A 1 69  ? 4.202   47.305  22.632  1.00 30.71 ? 70  LEU A C   1 
ATOM   478   O O   . LEU A 1 69  ? 4.832   48.057  21.885  1.00 30.73 ? 70  LEU A O   1 
ATOM   479   C CB  . LEU A 1 69  ? 3.090   45.429  21.396  1.00 30.61 ? 70  LEU A CB  1 
ATOM   480   C CG  . LEU A 1 69  ? 3.123   43.992  20.880  1.00 30.80 ? 70  LEU A CG  1 
ATOM   481   C CD1 . LEU A 1 69  ? 1.880   43.720  20.042  1.00 31.73 ? 70  LEU A CD1 1 
ATOM   482   C CD2 . LEU A 1 69  ? 4.396   43.722  20.085  1.00 30.85 ? 70  LEU A CD2 1 
ATOM   483   N N   . LEU A 1 70  ? 3.495   47.749  23.668  1.00 30.73 ? 71  LEU A N   1 
ATOM   484   C CA  . LEU A 1 70  ? 3.480   49.171  24.009  1.00 30.98 ? 71  LEU A CA  1 
ATOM   485   C C   . LEU A 1 70  ? 4.718   49.583  24.798  1.00 31.31 ? 71  LEU A C   1 
ATOM   486   O O   . LEU A 1 70  ? 5.065   50.767  24.848  1.00 31.23 ? 71  LEU A O   1 
ATOM   487   C CB  . LEU A 1 70  ? 2.197   49.559  24.763  1.00 30.85 ? 71  LEU A CB  1 
ATOM   488   C CG  . LEU A 1 70  ? 0.883   49.623  23.961  1.00 30.49 ? 71  LEU A CG  1 
ATOM   489   C CD1 . LEU A 1 70  ? -0.278  49.973  24.872  1.00 29.54 ? 71  LEU A CD1 1 
ATOM   490   C CD2 . LEU A 1 70  ? 0.956   50.610  22.790  1.00 28.98 ? 71  LEU A CD2 1 
ATOM   491   N N   . GLY A 1 71  ? 5.376   48.599  25.407  1.00 31.65 ? 72  GLY A N   1 
ATOM   492   C CA  . GLY A 1 71  ? 6.575   48.839  26.194  1.00 32.19 ? 72  GLY A CA  1 
ATOM   493   C C   . GLY A 1 71  ? 6.306   49.257  27.627  1.00 32.73 ? 72  GLY A C   1 
ATOM   494   O O   . GLY A 1 71  ? 6.888   50.233  28.111  1.00 32.71 ? 72  GLY A O   1 
ATOM   495   N N   . ASN A 1 72  ? 5.413   48.529  28.300  1.00 33.11 ? 73  ASN A N   1 
ATOM   496   C CA  . ASN A 1 72  ? 5.202   48.660  29.745  1.00 33.56 ? 73  ASN A CA  1 
ATOM   497   C C   . ASN A 1 72  ? 6.572   48.589  30.435  1.00 34.07 ? 73  ASN A C   1 
ATOM   498   O O   . ASN A 1 72  ? 7.339   47.656  30.166  1.00 34.19 ? 73  ASN A O   1 
ATOM   499   C CB  . ASN A 1 72  ? 4.272   47.531  30.231  1.00 33.29 ? 73  ASN A CB  1 
ATOM   500   C CG  . ASN A 1 72  ? 3.885   47.645  31.712  1.00 33.22 ? 73  ASN A CG  1 
ATOM   501   O OD1 . ASN A 1 72  ? 4.683   48.035  32.563  1.00 32.85 ? 73  ASN A OD1 1 
ATOM   502   N ND2 . ASN A 1 72  ? 2.651   47.263  32.020  1.00 32.53 ? 73  ASN A ND2 1 
ATOM   503   N N   . PRO A 1 73  ? 6.896   49.579  31.300  1.00 34.46 ? 74  PRO A N   1 
ATOM   504   C CA  . PRO A 1 73  ? 8.190   49.637  31.995  1.00 34.89 ? 74  PRO A CA  1 
ATOM   505   C C   . PRO A 1 73  ? 8.566   48.335  32.688  1.00 35.38 ? 74  PRO A C   1 
ATOM   506   O O   . PRO A 1 73  ? 9.746   48.051  32.856  1.00 35.60 ? 74  PRO A O   1 
ATOM   507   C CB  . PRO A 1 73  ? 7.977   50.726  33.044  1.00 34.85 ? 74  PRO A CB  1 
ATOM   508   C CG  . PRO A 1 73  ? 6.969   51.619  32.451  1.00 34.69 ? 74  PRO A CG  1 
ATOM   509   C CD  . PRO A 1 73  ? 6.051   50.738  31.645  1.00 34.69 ? 74  PRO A CD  1 
ATOM   510   N N   . MET A 1 74  ? 7.557   47.550  33.057  1.00 36.04 ? 75  MET A N   1 
ATOM   511   C CA  . MET A 1 74  ? 7.732   46.286  33.763  1.00 36.59 ? 75  MET A CA  1 
ATOM   512   C C   . MET A 1 74  ? 7.920   45.104  32.810  1.00 36.92 ? 75  MET A C   1 
ATOM   513   O O   . MET A 1 74  ? 7.823   43.943  33.219  1.00 36.96 ? 75  MET A O   1 
ATOM   514   C CB  . MET A 1 74  ? 6.519   46.036  34.669  1.00 36.75 ? 75  MET A CB  1 
ATOM   515   C CG  . MET A 1 74  ? 6.284   47.120  35.725  1.00 37.62 ? 75  MET A CG  1 
ATOM   516   S SD  . MET A 1 74  ? 7.061   46.770  37.320  1.00 38.85 ? 75  MET A SD  1 
ATOM   517   C CE  . MET A 1 74  ? 8.799   46.672  36.889  1.00 39.49 ? 75  MET A CE  1 
ATOM   518   N N   . CYS A 1 75  ? 8.191   45.397  31.542  1.00 37.30 ? 76  CYS A N   1 
ATOM   519   C CA  . CYS A 1 75  ? 8.333   44.352  30.534  1.00 37.60 ? 76  CYS A CA  1 
ATOM   520   C C   . CYS A 1 75  ? 9.627   44.488  29.736  1.00 37.65 ? 76  CYS A C   1 
ATOM   521   O O   . CYS A 1 75  ? 9.701   44.054  28.591  1.00 37.72 ? 76  CYS A O   1 
ATOM   522   C CB  . CYS A 1 75  ? 7.108   44.341  29.604  1.00 37.70 ? 76  CYS A CB  1 
ATOM   523   S SG  . CYS A 1 75  ? 5.526   44.045  30.446  1.00 38.21 ? 76  CYS A SG  1 
ATOM   524   N N   . ASP A 1 76  ? 10.650  45.072  30.356  1.00 38.07 ? 77  ASP A N   1 
ATOM   525   C CA  . ASP A 1 76  ? 11.960  45.277  29.706  1.00 38.45 ? 77  ASP A CA  1 
ATOM   526   C C   . ASP A 1 76  ? 12.639  43.992  29.186  1.00 38.30 ? 77  ASP A C   1 
ATOM   527   O O   . ASP A 1 76  ? 13.441  44.055  28.254  1.00 38.36 ? 77  ASP A O   1 
ATOM   528   C CB  . ASP A 1 76  ? 12.912  46.073  30.616  1.00 38.57 ? 77  ASP A CB  1 
ATOM   529   C CG  . ASP A 1 76  ? 12.354  47.453  31.005  1.00 39.71 ? 77  ASP A CG  1 
ATOM   530   O OD1 . ASP A 1 76  ? 11.441  47.966  30.315  1.00 39.38 ? 77  ASP A OD1 1 
ATOM   531   O OD2 . ASP A 1 76  ? 12.838  48.025  32.015  1.00 40.85 ? 77  ASP A OD2 1 
ATOM   532   N N   . GLU A 1 77  ? 12.309  42.838  29.770  1.00 38.11 ? 78  GLU A N   1 
ATOM   533   C CA  . GLU A 1 77  ? 12.769  41.543  29.249  1.00 38.35 ? 78  GLU A CA  1 
ATOM   534   C C   . GLU A 1 77  ? 12.405  41.334  27.768  1.00 38.36 ? 78  GLU A C   1 
ATOM   535   O O   . GLU A 1 77  ? 13.054  40.561  27.054  1.00 38.24 ? 78  GLU A O   1 
ATOM   536   C CB  . GLU A 1 77  ? 12.207  40.386  30.085  1.00 38.39 ? 78  GLU A CB  1 
ATOM   537   C CG  . GLU A 1 77  ? 12.645  39.000  29.598  1.00 39.20 ? 78  GLU A CG  1 
ATOM   538   C CD  . GLU A 1 77  ? 12.063  37.849  30.405  1.00 40.85 ? 78  GLU A CD  1 
ATOM   539   O OE1 . GLU A 1 77  ? 12.474  36.696  30.156  1.00 41.66 ? 78  GLU A OE1 1 
ATOM   540   O OE2 . GLU A 1 77  ? 11.206  38.082  31.284  1.00 41.34 ? 78  GLU A OE2 1 
ATOM   541   N N   . PHE A 1 78  ? 11.372  42.034  27.312  1.00 38.34 ? 79  PHE A N   1 
ATOM   542   C CA  . PHE A 1 78  ? 10.869  41.860  25.954  1.00 38.26 ? 79  PHE A CA  1 
ATOM   543   C C   . PHE A 1 78  ? 11.070  43.100  25.093  1.00 38.58 ? 79  PHE A C   1 
ATOM   544   O O   . PHE A 1 78  ? 10.348  43.317  24.129  1.00 38.93 ? 79  PHE A O   1 
ATOM   545   C CB  . PHE A 1 78  ? 9.405   41.403  26.005  1.00 37.92 ? 79  PHE A CB  1 
ATOM   546   C CG  . PHE A 1 78  ? 9.162   40.308  27.013  1.00 36.32 ? 79  PHE A CG  1 
ATOM   547   C CD1 . PHE A 1 78  ? 9.681   39.029  26.809  1.00 34.22 ? 79  PHE A CD1 1 
ATOM   548   C CD2 . PHE A 1 78  ? 8.455   40.565  28.181  1.00 35.07 ? 79  PHE A CD2 1 
ATOM   549   C CE1 . PHE A 1 78  ? 9.485   38.023  27.742  1.00 32.89 ? 79  PHE A CE1 1 
ATOM   550   C CE2 . PHE A 1 78  ? 8.248   39.561  29.123  1.00 34.28 ? 79  PHE A CE2 1 
ATOM   551   C CZ  . PHE A 1 78  ? 8.766   38.287  28.902  1.00 33.48 ? 79  PHE A CZ  1 
ATOM   552   N N   . ILE A 1 79  ? 12.073  43.899  25.456  1.00 39.06 ? 80  ILE A N   1 
ATOM   553   C CA  . ILE A 1 79  ? 12.484  45.093  24.708  1.00 39.43 ? 80  ILE A CA  1 
ATOM   554   C C   . ILE A 1 79  ? 12.935  44.764  23.272  1.00 39.57 ? 80  ILE A C   1 
ATOM   555   O O   . ILE A 1 79  ? 12.568  45.465  22.328  1.00 39.54 ? 80  ILE A O   1 
ATOM   556   C CB  . ILE A 1 79  ? 13.562  45.898  25.515  1.00 39.46 ? 80  ILE A CB  1 
ATOM   557   C CG1 . ILE A 1 79  ? 12.886  46.856  26.505  1.00 39.76 ? 80  ILE A CG1 1 
ATOM   558   C CG2 . ILE A 1 79  ? 14.549  46.648  24.613  1.00 39.91 ? 80  ILE A CG2 1 
ATOM   559   C CD1 . ILE A 1 79  ? 11.938  47.884  25.883  1.00 39.71 ? 80  ILE A CD1 1 
ATOM   560   N N   . ASN A 1 80  ? 13.730  43.703  23.130  1.00 39.91 ? 81  ASN A N   1 
ATOM   561   C CA  . ASN A 1 80  ? 14.103  43.135  21.833  1.00 40.24 ? 81  ASN A CA  1 
ATOM   562   C C   . ASN A 1 80  ? 13.951  41.623  21.883  1.00 40.03 ? 81  ASN A C   1 
ATOM   563   O O   . ASN A 1 80  ? 14.686  40.944  22.600  1.00 40.50 ? 81  ASN A O   1 
ATOM   564   C CB  . ASN A 1 80  ? 15.546  43.494  21.455  1.00 40.62 ? 81  ASN A CB  1 
ATOM   565   C CG  . ASN A 1 80  ? 15.655  44.817  20.704  1.00 41.72 ? 81  ASN A CG  1 
ATOM   566   O OD1 . ASN A 1 80  ? 14.653  45.401  20.281  1.00 43.20 ? 81  ASN A OD1 1 
ATOM   567   N ND2 . ASN A 1 80  ? 16.887  45.289  20.524  1.00 42.80 ? 81  ASN A ND2 1 
ATOM   568   N N   . VAL A 1 81  ? 12.988  41.101  21.130  1.00 39.55 ? 82  VAL A N   1 
ATOM   569   C CA  . VAL A 1 81  ? 12.671  39.677  21.164  1.00 39.12 ? 82  VAL A CA  1 
ATOM   570   C C   . VAL A 1 81  ? 13.185  38.986  19.897  1.00 38.77 ? 82  VAL A C   1 
ATOM   571   O O   . VAL A 1 81  ? 12.971  39.484  18.790  1.00 38.92 ? 82  VAL A O   1 
ATOM   572   C CB  . VAL A 1 81  ? 11.140  39.452  21.361  1.00 39.13 ? 82  VAL A CB  1 
ATOM   573   C CG1 . VAL A 1 81  ? 10.770  37.983  21.271  1.00 39.57 ? 82  VAL A CG1 1 
ATOM   574   C CG2 . VAL A 1 81  ? 10.697  40.003  22.694  1.00 39.00 ? 82  VAL A CG2 1 
ATOM   575   N N   . PRO A 1 82  A 13.894  37.849  20.060  1.00 38.44 ? 82  PRO A N   1 
ATOM   576   C CA  . PRO A 1 82  A 14.322  37.028  18.919  1.00 38.01 ? 82  PRO A CA  1 
ATOM   577   C C   . PRO A 1 82  A 13.149  36.258  18.291  1.00 37.65 ? 82  PRO A C   1 
ATOM   578   O O   . PRO A 1 82  A 12.057  36.238  18.857  1.00 37.59 ? 82  PRO A O   1 
ATOM   579   C CB  . PRO A 1 82  A 15.309  36.044  19.555  1.00 37.79 ? 82  PRO A CB  1 
ATOM   580   C CG  . PRO A 1 82  A 14.858  35.924  20.975  1.00 38.03 ? 82  PRO A CG  1 
ATOM   581   C CD  . PRO A 1 82  A 14.389  37.306  21.342  1.00 38.43 ? 82  PRO A CD  1 
ATOM   582   N N   . GLU A 1 83  ? 13.383  35.629  17.139  1.00 37.31 ? 83  GLU A N   1 
ATOM   583   C CA  . GLU A 1 83  ? 12.392  34.755  16.507  1.00 36.87 ? 83  GLU A CA  1 
ATOM   584   C C   . GLU A 1 83  ? 11.833  33.720  17.486  1.00 36.26 ? 83  GLU A C   1 
ATOM   585   O O   . GLU A 1 83  ? 12.588  33.089  18.239  1.00 36.30 ? 83  GLU A O   1 
ATOM   586   C CB  . GLU A 1 83  ? 12.985  34.041  15.291  1.00 37.10 ? 83  GLU A CB  1 
ATOM   587   C CG  . GLU A 1 83  ? 11.943  33.281  14.474  1.00 38.49 ? 83  GLU A CG  1 
ATOM   588   C CD  . GLU A 1 83  ? 12.526  32.513  13.311  1.00 40.66 ? 83  GLU A CD  1 
ATOM   589   O OE1 . GLU A 1 83  ? 13.456  33.026  12.651  1.00 41.99 ? 83  GLU A OE1 1 
ATOM   590   O OE2 . GLU A 1 83  ? 12.039  31.394  13.042  1.00 41.76 ? 83  GLU A OE2 1 
ATOM   591   N N   . TRP A 1 84  ? 10.509  33.561  17.467  1.00 35.32 ? 84  TRP A N   1 
ATOM   592   C CA  . TRP A 1 84  ? 9.815   32.607  18.327  1.00 34.47 ? 84  TRP A CA  1 
ATOM   593   C C   . TRP A 1 84  ? 9.058   31.567  17.504  1.00 34.23 ? 84  TRP A C   1 
ATOM   594   O O   . TRP A 1 84  ? 8.800   31.770  16.323  1.00 34.23 ? 84  TRP A O   1 
ATOM   595   C CB  . TRP A 1 84  ? 8.855   33.333  19.279  1.00 34.21 ? 84  TRP A CB  1 
ATOM   596   C CG  . TRP A 1 84  ? 7.705   34.019  18.588  1.00 33.30 ? 84  TRP A CG  1 
ATOM   597   C CD1 . TRP A 1 84  ? 6.539   33.442  18.167  1.00 32.38 ? 84  TRP A CD1 1 
ATOM   598   C CD2 . TRP A 1 84  ? 7.612   35.408  18.241  1.00 32.30 ? 84  TRP A CD2 1 
ATOM   599   N NE1 . TRP A 1 84  ? 5.730   34.380  17.580  1.00 31.70 ? 84  TRP A NE1 1 
ATOM   600   C CE2 . TRP A 1 84  ? 6.358   35.596  17.611  1.00 31.63 ? 84  TRP A CE2 1 
ATOM   601   C CE3 . TRP A 1 84  ? 8.463   36.513  18.403  1.00 31.26 ? 84  TRP A CE3 1 
ATOM   602   C CZ2 . TRP A 1 84  ? 5.934   36.844  17.138  1.00 30.77 ? 84  TRP A CZ2 1 
ATOM   603   C CZ3 . TRP A 1 84  ? 8.042   37.752  17.934  1.00 30.75 ? 84  TRP A CZ3 1 
ATOM   604   C CH2 . TRP A 1 84  ? 6.787   37.907  17.307  1.00 30.97 ? 84  TRP A CH2 1 
ATOM   605   N N   . SER A 1 85  ? 8.709   30.457  18.142  1.00 34.04 ? 85  SER A N   1 
ATOM   606   C CA  . SER A 1 85  ? 7.893   29.419  17.521  1.00 33.81 ? 85  SER A CA  1 
ATOM   607   C C   . SER A 1 85  ? 6.427   29.674  17.849  1.00 33.58 ? 85  SER A C   1 
ATOM   608   O O   . SER A 1 85  ? 5.600   29.816  16.953  1.00 33.85 ? 85  SER A O   1 
ATOM   609   C CB  . SER A 1 85  ? 8.327   28.037  18.015  1.00 33.85 ? 85  SER A CB  1 
ATOM   610   O OG  . SER A 1 85  ? 8.452   28.027  19.427  1.00 33.60 ? 85  SER A OG  1 
ATOM   611   N N   . TYR A 1 86  ? 6.117   29.749  19.140  1.00 33.17 ? 86  TYR A N   1 
ATOM   612   C CA  . TYR A 1 86  ? 4.792   30.146  19.605  1.00 32.71 ? 86  TYR A CA  1 
ATOM   613   C C   . TYR A 1 86  ? 4.913   31.166  20.736  1.00 32.77 ? 86  TYR A C   1 
ATOM   614   O O   . TYR A 1 86  ? 6.015   31.457  21.195  1.00 32.73 ? 86  TYR A O   1 
ATOM   615   C CB  . TYR A 1 86  ? 3.964   28.927  20.034  1.00 32.41 ? 86  TYR A CB  1 
ATOM   616   C CG  . TYR A 1 86  ? 4.597   28.067  21.106  1.00 31.13 ? 86  TYR A CG  1 
ATOM   617   C CD1 . TYR A 1 86  ? 4.164   28.141  22.424  1.00 30.82 ? 86  TYR A CD1 1 
ATOM   618   C CD2 . TYR A 1 86  ? 5.618   27.168  20.800  1.00 30.32 ? 86  TYR A CD2 1 
ATOM   619   C CE1 . TYR A 1 86  ? 4.736   27.347  23.415  1.00 30.47 ? 86  TYR A CE1 1 
ATOM   620   C CE2 . TYR A 1 86  ? 6.199   26.377  21.780  1.00 29.84 ? 86  TYR A CE2 1 
ATOM   621   C CZ  . TYR A 1 86  ? 5.751   26.472  23.085  1.00 29.94 ? 86  TYR A CZ  1 
ATOM   622   O OH  . TYR A 1 86  ? 6.317   25.702  24.069  1.00 29.72 ? 86  TYR A OH  1 
ATOM   623   N N   . ILE A 1 87  ? 3.779   31.716  21.164  1.00 32.82 ? 87  ILE A N   1 
ATOM   624   C CA  . ILE A 1 87  ? 3.736   32.680  22.257  1.00 32.95 ? 87  ILE A CA  1 
ATOM   625   C C   . ILE A 1 87  ? 2.899   32.105  23.392  1.00 33.15 ? 87  ILE A C   1 
ATOM   626   O O   . ILE A 1 87  ? 1.817   31.569  23.154  1.00 32.89 ? 87  ILE A O   1 
ATOM   627   C CB  . ILE A 1 87  ? 3.142   34.040  21.792  1.00 33.19 ? 87  ILE A CB  1 
ATOM   628   C CG1 . ILE A 1 87  ? 4.000   34.646  20.676  1.00 33.08 ? 87  ILE A CG1 1 
ATOM   629   C CG2 . ILE A 1 87  ? 2.992   35.027  22.971  1.00 32.62 ? 87  ILE A CG2 1 
ATOM   630   C CD1 . ILE A 1 87  ? 3.224   35.522  19.722  1.00 34.06 ? 87  ILE A CD1 1 
ATOM   631   N N   . VAL A 1 88  ? 3.407   32.208  24.621  1.00 33.28 ? 88  VAL A N   1 
ATOM   632   C CA  . VAL A 1 88  ? 2.654   31.779  25.796  1.00 33.49 ? 88  VAL A CA  1 
ATOM   633   C C   . VAL A 1 88  ? 2.231   32.993  26.612  1.00 34.09 ? 88  VAL A C   1 
ATOM   634   O O   . VAL A 1 88  ? 3.048   33.868  26.912  1.00 34.25 ? 88  VAL A O   1 
ATOM   635   C CB  . VAL A 1 88  ? 3.450   30.768  26.670  1.00 33.40 ? 88  VAL A CB  1 
ATOM   636   C CG1 . VAL A 1 88  ? 2.696   30.431  27.951  1.00 32.64 ? 88  VAL A CG1 1 
ATOM   637   C CG2 . VAL A 1 88  ? 3.723   29.502  25.893  1.00 32.99 ? 88  VAL A CG2 1 
ATOM   638   N N   . GLU A 1 89  ? 0.947   33.048  26.953  1.00 34.62 ? 89  GLU A N   1 
ATOM   639   C CA  . GLU A 1 89  ? 0.428   34.121  27.785  1.00 35.36 ? 89  GLU A CA  1 
ATOM   640   C C   . GLU A 1 89  ? -0.390  33.554  28.942  1.00 35.52 ? 89  GLU A C   1 
ATOM   641   O O   . GLU A 1 89  ? -1.103  32.566  28.779  1.00 35.51 ? 89  GLU A O   1 
ATOM   642   C CB  . GLU A 1 89  ? -0.416  35.090  26.945  1.00 35.57 ? 89  GLU A CB  1 
ATOM   643   C CG  . GLU A 1 89  ? -0.801  36.385  27.667  1.00 36.63 ? 89  GLU A CG  1 
ATOM   644   C CD  . GLU A 1 89  ? -1.685  37.299  26.824  1.00 38.43 ? 89  GLU A CD  1 
ATOM   645   O OE1 . GLU A 1 89  ? -2.779  36.857  26.400  1.00 38.76 ? 89  GLU A OE1 1 
ATOM   646   O OE2 . GLU A 1 89  ? -1.290  38.468  26.600  1.00 38.39 ? 89  GLU A OE2 1 
ATOM   647   N N   . LYS A 1 90  ? -0.264  34.180  30.108  1.00 35.90 ? 90  LYS A N   1 
ATOM   648   C CA  . LYS A 1 90  ? -1.072  33.841  31.277  1.00 36.39 ? 90  LYS A CA  1 
ATOM   649   C C   . LYS A 1 90  ? -2.521  34.310  31.118  1.00 36.66 ? 90  LYS A C   1 
ATOM   650   O O   . LYS A 1 90  ? -2.803  35.214  30.336  1.00 36.74 ? 90  LYS A O   1 
ATOM   651   C CB  . LYS A 1 90  ? -0.460  34.466  32.532  1.00 36.29 ? 90  LYS A CB  1 
ATOM   652   C CG  . LYS A 1 90  ? 0.747   33.726  33.075  1.00 36.48 ? 90  LYS A CG  1 
ATOM   653   C CD  . LYS A 1 90  ? 1.245   34.367  34.362  1.00 36.27 ? 90  LYS A CD  1 
ATOM   654   C CE  . LYS A 1 90  ? 2.109   33.408  35.162  1.00 36.61 ? 90  LYS A CE  1 
ATOM   655   N NZ  . LYS A 1 90  ? 3.392   33.097  34.480  1.00 36.67 ? 90  LYS A NZ  1 
ATOM   656   N N   . ALA A 1 91  ? -3.431  33.697  31.872  1.00 37.20 ? 91  ALA A N   1 
ATOM   657   C CA  . ALA A 1 91  ? -4.848  34.072  31.856  1.00 37.75 ? 91  ALA A CA  1 
ATOM   658   C C   . ALA A 1 91  ? -5.079  35.512  32.318  1.00 38.18 ? 91  ALA A C   1 
ATOM   659   O O   . ALA A 1 91  ? -5.879  36.231  31.723  1.00 38.57 ? 91  ALA A O   1 
ATOM   660   C CB  . ALA A 1 91  ? -5.670  33.103  32.696  1.00 37.55 ? 91  ALA A CB  1 
ATOM   661   N N   . SER A 1 92  ? -4.378  35.925  33.373  1.00 38.61 ? 92  SER A N   1 
ATOM   662   C CA  . SER A 1 92  ? -4.485  37.291  33.890  1.00 38.88 ? 92  SER A CA  1 
ATOM   663   C C   . SER A 1 92  ? -3.104  37.921  34.126  1.00 38.88 ? 92  SER A C   1 
ATOM   664   O O   . SER A 1 92  ? -2.678  38.076  35.273  1.00 38.87 ? 92  SER A O   1 
ATOM   665   C CB  . SER A 1 92  ? -5.315  37.314  35.179  1.00 39.07 ? 92  SER A CB  1 
ATOM   666   O OG  . SER A 1 92  ? -6.535  36.604  35.016  1.00 39.79 ? 92  SER A OG  1 
ATOM   667   N N   . PRO A 1 93  ? -2.406  38.300  33.039  1.00 38.85 ? 93  PRO A N   1 
ATOM   668   C CA  . PRO A 1 93  ? -1.098  38.940  33.183  1.00 38.74 ? 93  PRO A CA  1 
ATOM   669   C C   . PRO A 1 93  ? -1.210  40.229  34.001  1.00 38.73 ? 93  PRO A C   1 
ATOM   670   O O   . PRO A 1 93  ? -2.125  41.024  33.779  1.00 38.81 ? 93  PRO A O   1 
ATOM   671   C CB  . PRO A 1 93  ? -0.700  39.267  31.737  1.00 38.85 ? 93  PRO A CB  1 
ATOM   672   C CG  . PRO A 1 93  ? -1.632  38.474  30.867  1.00 38.87 ? 93  PRO A CG  1 
ATOM   673   C CD  . PRO A 1 93  ? -2.889  38.346  31.646  1.00 38.80 ? 93  PRO A CD  1 
ATOM   674   N N   . ALA A 1 94  ? -0.297  40.423  34.950  1.00 38.57 ? 94  ALA A N   1 
ATOM   675   C CA  . ALA A 1 94  ? -0.343  41.588  35.830  1.00 38.31 ? 94  ALA A CA  1 
ATOM   676   C C   . ALA A 1 94  ? 0.110   42.863  35.117  1.00 38.15 ? 94  ALA A C   1 
ATOM   677   O O   . ALA A 1 94  ? -0.381  43.951  35.406  1.00 38.29 ? 94  ALA A O   1 
ATOM   678   C CB  . ALA A 1 94  ? 0.498   41.344  37.072  1.00 38.34 ? 94  ALA A CB  1 
ATOM   679   N N   . ASN A 1 95  ? 1.039   42.716  34.179  1.00 37.70 ? 95  ASN A N   1 
ATOM   680   C CA  . ASN A 1 95  ? 1.643   43.856  33.512  1.00 37.35 ? 95  ASN A CA  1 
ATOM   681   C C   . ASN A 1 95  ? 1.013   44.112  32.139  1.00 37.23 ? 95  ASN A C   1 
ATOM   682   O O   . ASN A 1 95  ? 1.462   43.599  31.106  1.00 37.11 ? 95  ASN A O   1 
ATOM   683   C CB  . ASN A 1 95  ? 3.170   43.690  33.448  1.00 37.40 ? 95  ASN A CB  1 
ATOM   684   C CG  . ASN A 1 95  ? 3.792   43.418  34.828  1.00 37.43 ? 95  ASN A CG  1 
ATOM   685   O OD1 . ASN A 1 95  ? 3.269   43.849  35.856  1.00 37.42 ? 95  ASN A OD1 1 
ATOM   686   N ND2 . ASN A 1 95  ? 4.913   42.703  34.844  1.00 36.99 ? 95  ASN A ND2 1 
ATOM   687   N N   . ASP A 1 96  ? -0.170  44.903  32.125  1.00 36.37 ? 96  ASP A N   1 
ATOM   688   C CA  . ASP A 1 96  ? -0.901  45.213  30.903  1.00 35.78 ? 96  ASP A CA  1 
ATOM   689   C C   . ASP A 1 96  ? -0.895  46.653  30.402  1.00 35.45 ? 96  ASP A C   1 
ATOM   690   O O   . ASP A 1 96  ? -0.062  47.028  29.576  1.00 35.21 ? 96  ASP A O   1 
ATOM   691   C CB  . ASP A 1 96  ? -2.371  44.814  31.042  1.00 35.75 ? 96  ASP A CB  1 
ATOM   692   C CG  . ASP A 1 96  ? -3.117  44.869  29.723  1.00 35.15 ? 96  ASP A CG  1 
ATOM   693   O OD1 . ASP A 1 96  ? -2.601  44.325  28.724  1.00 34.94 ? 96  ASP A OD1 1 
ATOM   694   O OD2 . ASP A 1 96  ? -4.218  45.456  29.684  1.00 34.93 ? 96  ASP A OD2 1 
ATOM   695   N N   . LEU A 1 97  A -1.870  47.420  30.808  1.00 35.00 ? 96  LEU A N   1 
ATOM   696   C CA  . LEU A 1 97  A -1.884  48.846  30.554  1.00 34.80 ? 96  LEU A CA  1 
ATOM   697   C C   . LEU A 1 97  A -1.688  49.521  31.896  1.00 34.62 ? 96  LEU A C   1 
ATOM   698   O O   . LEU A 1 97  A -2.639  49.676  32.663  1.00 34.65 ? 96  LEU A O   1 
ATOM   699   C CB  . LEU A 1 97  A -3.203  49.286  29.897  1.00 34.80 ? 96  LEU A CB  1 
ATOM   700   C CG  . LEU A 1 97  A -3.275  49.528  28.380  1.00 35.04 ? 96  LEU A CG  1 
ATOM   701   C CD1 . LEU A 1 97  A -2.463  48.538  27.557  1.00 34.83 ? 96  LEU A CD1 1 
ATOM   702   C CD2 . LEU A 1 97  A -4.723  49.545  27.901  1.00 35.40 ? 96  LEU A CD2 1 
ATOM   703   N N   . CYS A 1 98  ? -0.459  49.867  32.182  1.00 35.14 ? 97  CYS A N   1 
ATOM   704   C CA  . CYS A 1 98  ? -0.152  50.528  33.454  1.00 35.04 ? 97  CYS A CA  1 
ATOM   705   C C   . CYS A 1 98  ? -0.986  51.814  33.604  1.00 34.41 ? 97  CYS A C   1 
ATOM   706   O O   . CYS A 1 98  ? -1.712  51.978  34.593  1.00 34.22 ? 97  CYS A O   1 
ATOM   707   C CB  . CYS A 1 98  ? 1.363   50.758  33.626  1.00 35.15 ? 97  CYS A CB  1 
ATOM   708   S SG  . CYS A 1 98  ? 2.223   51.681  32.292  1.00 37.62 ? 97  CYS A SG  1 
ATOM   709   N N   . TYR A 1 99  ? -0.914  52.702  32.614  1.00 33.72 ? 98  TYR A N   1 
ATOM   710   C CA  . TYR A 1 99  ? -1.881  53.793  32.531  1.00 33.41 ? 98  TYR A CA  1 
ATOM   711   C C   . TYR A 1 99  ? -3.191  53.234  31.973  1.00 33.13 ? 98  TYR A C   1 
ATOM   712   O O   . TYR A 1 99  ? -3.202  52.680  30.874  1.00 33.05 ? 98  TYR A O   1 
ATOM   713   C CB  . TYR A 1 99  ? -1.379  54.957  31.673  1.00 33.19 ? 98  TYR A CB  1 
ATOM   714   C CG  . TYR A 1 99  ? -2.100  56.261  31.969  1.00 33.29 ? 98  TYR A CG  1 
ATOM   715   C CD1 . TYR A 1 99  ? -1.517  57.235  32.789  1.00 32.70 ? 98  TYR A CD1 1 
ATOM   716   C CD2 . TYR A 1 99  ? -3.373  56.515  31.446  1.00 32.81 ? 98  TYR A CD2 1 
ATOM   717   C CE1 . TYR A 1 99  ? -2.183  58.434  33.074  1.00 32.49 ? 98  TYR A CE1 1 
ATOM   718   C CE2 . TYR A 1 99  ? -4.047  57.706  31.719  1.00 32.86 ? 98  TYR A CE2 1 
ATOM   719   C CZ  . TYR A 1 99  ? -3.448  58.662  32.534  1.00 32.80 ? 98  TYR A CZ  1 
ATOM   720   O OH  . TYR A 1 99  ? -4.113  59.836  32.797  1.00 31.62 ? 98  TYR A OH  1 
ATOM   721   N N   . PRO A 1 100 ? -4.299  53.385  32.730  1.00 32.93 ? 99  PRO A N   1 
ATOM   722   C CA  . PRO A 1 100 ? -5.566  52.733  32.388  1.00 32.71 ? 99  PRO A CA  1 
ATOM   723   C C   . PRO A 1 100 ? -6.122  53.168  31.040  1.00 32.57 ? 99  PRO A C   1 
ATOM   724   O O   . PRO A 1 100 ? -5.826  54.268  30.570  1.00 32.07 ? 99  PRO A O   1 
ATOM   725   C CB  . PRO A 1 100 ? -6.506  53.166  33.523  1.00 32.67 ? 99  PRO A CB  1 
ATOM   726   C CG  . PRO A 1 100 ? -5.908  54.418  34.059  1.00 32.78 ? 99  PRO A CG  1 
ATOM   727   C CD  . PRO A 1 100 ? -4.430  54.238  33.927  1.00 32.75 ? 99  PRO A CD  1 
ATOM   728   N N   . GLY A 1 101 ? -6.917  52.291  30.431  1.00 32.84 ? 100 GLY A N   1 
ATOM   729   C CA  . GLY A 1 101 ? -7.556  52.570  29.145  1.00 33.10 ? 100 GLY A CA  1 
ATOM   730   C C   . GLY A 1 101 ? -7.903  51.317  28.366  1.00 33.43 ? 100 GLY A C   1 
ATOM   731   O O   . GLY A 1 101 ? -8.146  50.256  28.940  1.00 33.56 ? 100 GLY A O   1 
ATOM   732   N N   . ASP A 1 102 ? -7.938  51.441  27.046  1.00 33.61 ? 101 ASP A N   1 
ATOM   733   C CA  . ASP A 1 102 ? -8.253  50.309  26.188  1.00 33.75 ? 101 ASP A CA  1 
ATOM   734   C C   . ASP A 1 102 ? -7.295  50.249  25.006  1.00 33.08 ? 101 ASP A C   1 
ATOM   735   O O   . ASP A 1 102 ? -6.672  51.250  24.639  1.00 32.86 ? 101 ASP A O   1 
ATOM   736   C CB  . ASP A 1 102 ? -9.706  50.365  25.682  1.00 34.25 ? 101 ASP A CB  1 
ATOM   737   C CG  . ASP A 1 102 ? -10.670 50.933  26.710  1.00 36.40 ? 101 ASP A CG  1 
ATOM   738   O OD1 . ASP A 1 102 ? -10.741 52.178  26.817  1.00 39.03 ? 101 ASP A OD1 1 
ATOM   739   O OD2 . ASP A 1 102 ? -11.364 50.147  27.403  1.00 38.78 ? 101 ASP A OD2 1 
ATOM   740   N N   . PHE A 1 103 ? -7.192  49.055  24.429  1.00 32.31 ? 102 PHE A N   1 
ATOM   741   C CA  . PHE A 1 103 ? -6.458  48.818  23.206  1.00 31.66 ? 102 PHE A CA  1 
ATOM   742   C C   . PHE A 1 103 ? -7.491  48.516  22.123  1.00 31.21 ? 102 PHE A C   1 
ATOM   743   O O   . PHE A 1 103 ? -8.210  47.529  22.216  1.00 31.27 ? 102 PHE A O   1 
ATOM   744   C CB  . PHE A 1 103 ? -5.531  47.614  23.398  1.00 31.51 ? 102 PHE A CB  1 
ATOM   745   C CG  . PHE A 1 103 ? -4.340  47.602  22.481  1.00 31.81 ? 102 PHE A CG  1 
ATOM   746   C CD1 . PHE A 1 103 ? -3.054  47.717  23.000  1.00 31.41 ? 102 PHE A CD1 1 
ATOM   747   C CD2 . PHE A 1 103 ? -4.499  47.470  21.097  1.00 32.01 ? 102 PHE A CD2 1 
ATOM   748   C CE1 . PHE A 1 103 ? -1.945  47.706  22.164  1.00 31.58 ? 102 PHE A CE1 1 
ATOM   749   C CE2 . PHE A 1 103 ? -3.397  47.460  20.249  1.00 32.04 ? 102 PHE A CE2 1 
ATOM   750   C CZ  . PHE A 1 103 ? -2.114  47.580  20.784  1.00 32.38 ? 102 PHE A CZ  1 
ATOM   751   N N   . ASN A 1 104 ? -7.573  49.377  21.111  1.00 30.98 ? 103 ASN A N   1 
ATOM   752   C CA  . ASN A 1 104 ? -8.540  49.215  20.019  1.00 30.71 ? 103 ASN A CA  1 
ATOM   753   C C   . ASN A 1 104 ? -8.187  48.049  19.097  1.00 30.65 ? 103 ASN A C   1 
ATOM   754   O O   . ASN A 1 104 ? -7.040  47.925  18.656  1.00 30.69 ? 103 ASN A O   1 
ATOM   755   C CB  . ASN A 1 104 ? -8.655  50.510  19.210  1.00 30.62 ? 103 ASN A CB  1 
ATOM   756   C CG  . ASN A 1 104 ? -9.780  50.467  18.184  1.00 30.71 ? 103 ASN A CG  1 
ATOM   757   O OD1 . ASN A 1 104 ? -10.964 50.544  18.532  1.00 29.74 ? 103 ASN A OD1 1 
ATOM   758   N ND2 . ASN A 1 104 ? -9.412  50.353  16.910  1.00 29.25 ? 103 ASN A ND2 1 
ATOM   759   N N   . ASN A 1 105 ? -9.176  47.201  18.816  1.00 30.40 ? 104 ASN A N   1 
ATOM   760   C CA  . ASN A 1 105 ? -8.996  46.002  17.978  1.00 30.24 ? 104 ASN A CA  1 
ATOM   761   C C   . ASN A 1 105 ? -7.894  45.070  18.477  1.00 29.94 ? 104 ASN A C   1 
ATOM   762   O O   . ASN A 1 105 ? -7.076  44.575  17.696  1.00 29.86 ? 104 ASN A O   1 
ATOM   763   C CB  . ASN A 1 105 ? -8.782  46.376  16.505  1.00 30.30 ? 104 ASN A CB  1 
ATOM   764   C CG  . ASN A 1 105 ? -10.067 46.813  15.819  1.00 31.08 ? 104 ASN A CG  1 
ATOM   765   O OD1 . ASN A 1 105 ? -10.040 47.612  14.885  1.00 32.13 ? 104 ASN A OD1 1 
ATOM   766   N ND2 . ASN A 1 105 ? -11.200 46.289  16.279  1.00 31.53 ? 104 ASN A ND2 1 
ATOM   767   N N   . TYR A 1 106 ? -7.897  44.838  19.788  1.00 29.51 ? 105 TYR A N   1 
ATOM   768   C CA  . TYR A 1 106 ? -6.866  44.061  20.466  1.00 29.09 ? 105 TYR A CA  1 
ATOM   769   C C   . TYR A 1 106 ? -6.888  42.597  20.041  1.00 28.74 ? 105 TYR A C   1 
ATOM   770   O O   . TYR A 1 106 ? -5.840  41.995  19.809  1.00 28.58 ? 105 TYR A O   1 
ATOM   771   C CB  . TYR A 1 106 ? -7.036  44.196  21.981  1.00 29.03 ? 105 TYR A CB  1 
ATOM   772   C CG  . TYR A 1 106 ? -5.941  43.575  22.821  1.00 29.58 ? 105 TYR A CG  1 
ATOM   773   C CD1 . TYR A 1 106 ? -4.591  43.850  22.575  1.00 29.84 ? 105 TYR A CD1 1 
ATOM   774   C CD2 . TYR A 1 106 ? -6.256  42.735  23.889  1.00 29.57 ? 105 TYR A CD2 1 
ATOM   775   C CE1 . TYR A 1 106 ? -3.586  43.288  23.362  1.00 29.31 ? 105 TYR A CE1 1 
ATOM   776   C CE2 . TYR A 1 106 ? -5.263  42.176  24.682  1.00 29.51 ? 105 TYR A CE2 1 
ATOM   777   C CZ  . TYR A 1 106 ? -3.933  42.454  24.416  1.00 29.96 ? 105 TYR A CZ  1 
ATOM   778   O OH  . TYR A 1 106 ? -2.953  41.893  25.206  1.00 29.96 ? 105 TYR A OH  1 
ATOM   779   N N   . GLU A 1 107 ? -8.089  42.039  19.920  1.00 28.52 ? 106 GLU A N   1 
ATOM   780   C CA  . GLU A 1 107 ? -8.251  40.633  19.549  1.00 28.32 ? 106 GLU A CA  1 
ATOM   781   C C   . GLU A 1 107 ? -7.817  40.356  18.109  1.00 27.89 ? 106 GLU A C   1 
ATOM   782   O O   . GLU A 1 107 ? -7.242  39.298  17.828  1.00 27.85 ? 106 GLU A O   1 
ATOM   783   C CB  . GLU A 1 107 ? -9.683  40.155  19.800  1.00 28.31 ? 106 GLU A CB  1 
ATOM   784   C CG  . GLU A 1 107 ? -10.043 40.030  21.279  1.00 29.06 ? 106 GLU A CG  1 
ATOM   785   C CD  . GLU A 1 107 ? -10.252 41.377  21.977  1.00 30.99 ? 106 GLU A CD  1 
ATOM   786   O OE1 . GLU A 1 107 ? -10.649 42.365  21.312  1.00 30.79 ? 106 GLU A OE1 1 
ATOM   787   O OE2 . GLU A 1 107 ? -10.021 41.447  23.205  1.00 33.07 ? 106 GLU A OE2 1 
ATOM   788   N N   . GLU A 1 108 ? -8.072  41.308  17.212  1.00 27.31 ? 107 GLU A N   1 
ATOM   789   C CA  . GLU A 1 108 ? -7.592  41.202  15.835  1.00 27.08 ? 107 GLU A CA  1 
ATOM   790   C C   . GLU A 1 108 ? -6.060  41.268  15.770  1.00 27.14 ? 107 GLU A C   1 
ATOM   791   O O   . GLU A 1 108 ? -5.442  40.522  15.008  1.00 26.97 ? 107 GLU A O   1 
ATOM   792   C CB  . GLU A 1 108 ? -8.238  42.259  14.925  1.00 26.86 ? 107 GLU A CB  1 
ATOM   793   C CG  . GLU A 1 108 ? -9.712  41.997  14.583  1.00 26.84 ? 107 GLU A CG  1 
ATOM   794   C CD  . GLU A 1 108 ? -9.929  40.798  13.648  1.00 27.29 ? 107 GLU A CD  1 
ATOM   795   O OE1 . GLU A 1 108 ? -9.253  40.718  12.591  1.00 26.48 ? 107 GLU A OE1 1 
ATOM   796   O OE2 . GLU A 1 108 ? -10.792 39.943  13.965  1.00 26.41 ? 107 GLU A OE2 1 
ATOM   797   N N   . LEU A 1 109 ? -5.455  42.149  16.572  1.00 27.36 ? 108 LEU A N   1 
ATOM   798   C CA  . LEU A 1 109 ? -3.985  42.226  16.666  1.00 27.51 ? 108 LEU A CA  1 
ATOM   799   C C   . LEU A 1 109 ? -3.359  40.923  17.179  1.00 27.29 ? 108 LEU A C   1 
ATOM   800   O O   . LEU A 1 109 ? -2.350  40.471  16.647  1.00 26.73 ? 108 LEU A O   1 
ATOM   801   C CB  . LEU A 1 109 ? -3.520  43.422  17.515  1.00 27.64 ? 108 LEU A CB  1 
ATOM   802   C CG  . LEU A 1 109 ? -1.993  43.612  17.669  1.00 28.46 ? 108 LEU A CG  1 
ATOM   803   C CD1 . LEU A 1 109 ? -1.264  43.718  16.321  1.00 28.80 ? 108 LEU A CD1 1 
ATOM   804   C CD2 . LEU A 1 109 ? -1.665  44.822  18.530  1.00 28.75 ? 108 LEU A CD2 1 
ATOM   805   N N   . LYS A 1 110 ? -3.969  40.322  18.197  1.00 27.55 ? 109 LYS A N   1 
ATOM   806   C CA  . LYS A 1 110 ? -3.495  39.043  18.722  1.00 28.18 ? 109 LYS A CA  1 
ATOM   807   C C   . LYS A 1 110 ? -3.551  37.944  17.667  1.00 28.71 ? 109 LYS A C   1 
ATOM   808   O O   . LYS A 1 110 ? -2.670  37.083  17.612  1.00 28.80 ? 109 LYS A O   1 
ATOM   809   C CB  . LYS A 1 110 ? -4.299  38.621  19.949  1.00 28.04 ? 109 LYS A CB  1 
ATOM   810   C CG  . LYS A 1 110 ? -4.044  39.459  21.186  1.00 28.55 ? 109 LYS A CG  1 
ATOM   811   C CD  . LYS A 1 110 ? -3.950  38.563  22.393  1.00 30.02 ? 109 LYS A CD  1 
ATOM   812   C CE  . LYS A 1 110 ? -4.795  39.072  23.528  1.00 31.22 ? 109 LYS A CE  1 
ATOM   813   N NZ  . LYS A 1 110 ? -4.721  38.144  24.693  1.00 32.13 ? 109 LYS A NZ  1 
ATOM   814   N N   . HIS A 1 111 ? -4.591  37.979  16.837  1.00 29.25 ? 110 HIS A N   1 
ATOM   815   C CA  . HIS A 1 111 ? -4.747  37.022  15.751  1.00 29.68 ? 110 HIS A CA  1 
ATOM   816   C C   . HIS A 1 111 ? -3.678  37.193  14.675  1.00 29.85 ? 110 HIS A C   1 
ATOM   817   O O   . HIS A 1 111 ? -3.184  36.210  14.124  1.00 29.95 ? 110 HIS A O   1 
ATOM   818   C CB  . HIS A 1 111 ? -6.136  37.130  15.123  1.00 29.79 ? 110 HIS A CB  1 
ATOM   819   C CG  . HIS A 1 111 ? -6.364  36.143  14.027  1.00 30.00 ? 110 HIS A CG  1 
ATOM   820   N ND1 . HIS A 1 111 ? -6.002  36.390  12.719  1.00 30.49 ? 110 HIS A ND1 1 
ATOM   821   C CD2 . HIS A 1 111 ? -6.875  34.891  14.048  1.00 30.08 ? 110 HIS A CD2 1 
ATOM   822   C CE1 . HIS A 1 111 ? -6.299  35.338  11.978  1.00 30.20 ? 110 HIS A CE1 1 
ATOM   823   N NE2 . HIS A 1 111 ? -6.830  34.416  12.761  1.00 30.70 ? 110 HIS A NE2 1 
ATOM   824   N N   . LEU A 1 112 ? -3.339  38.439  14.368  1.00 30.20 ? 111 LEU A N   1 
ATOM   825   C CA  . LEU A 1 112 ? -2.261  38.726  13.433  1.00 31.06 ? 111 LEU A CA  1 
ATOM   826   C C   . LEU A 1 112 ? -0.915  38.280  14.012  1.00 31.47 ? 111 LEU A C   1 
ATOM   827   O O   . LEU A 1 112 ? -0.067  37.750  13.296  1.00 31.54 ? 111 LEU A O   1 
ATOM   828   C CB  . LEU A 1 112 ? -2.254  40.208  13.063  1.00 30.96 ? 111 LEU A CB  1 
ATOM   829   C CG  . LEU A 1 112 ? -1.057  40.744  12.268  1.00 32.24 ? 111 LEU A CG  1 
ATOM   830   C CD1 . LEU A 1 112 ? -1.513  41.655  11.134  1.00 32.93 ? 111 LEU A CD1 1 
ATOM   831   C CD2 . LEU A 1 112 ? -0.055  41.463  13.185  1.00 32.51 ? 111 LEU A CD2 1 
ATOM   832   N N   . LEU A 1 113 ? -0.736  38.491  15.311  1.00 32.10 ? 112 LEU A N   1 
ATOM   833   C CA  . LEU A 1 113 ? 0.437   38.001  16.018  1.00 32.89 ? 112 LEU A CA  1 
ATOM   834   C C   . LEU A 1 113 ? 0.618   36.492  15.897  1.00 33.47 ? 112 LEU A C   1 
ATOM   835   O O   . LEU A 1 113 ? 1.751   36.008  15.847  1.00 33.70 ? 112 LEU A O   1 
ATOM   836   C CB  . LEU A 1 113 ? 0.370   38.374  17.496  1.00 32.95 ? 112 LEU A CB  1 
ATOM   837   C CG  . LEU A 1 113 ? 1.325   39.429  18.038  1.00 33.01 ? 112 LEU A CG  1 
ATOM   838   C CD1 . LEU A 1 113 ? 1.274   39.336  19.539  1.00 33.60 ? 112 LEU A CD1 1 
ATOM   839   C CD2 . LEU A 1 113 ? 2.753   39.199  17.556  1.00 33.07 ? 112 LEU A CD2 1 
ATOM   840   N N   . SER A 1 114 ? -0.494  35.757  15.855  1.00 33.85 ? 113 SER A N   1 
ATOM   841   C CA  . SER A 1 114 ? -0.456  34.298  15.768  1.00 34.29 ? 113 SER A CA  1 
ATOM   842   C C   . SER A 1 114 ? -0.091  33.814  14.369  1.00 34.83 ? 113 SER A C   1 
ATOM   843   O O   . SER A 1 114 ? 0.025   32.609  14.141  1.00 35.11 ? 113 SER A O   1 
ATOM   844   C CB  . SER A 1 114 ? -1.785  33.678  16.229  1.00 34.16 ? 113 SER A CB  1 
ATOM   845   O OG  . SER A 1 114 ? -2.816  33.898  15.287  1.00 33.24 ? 113 SER A OG  1 
ATOM   846   N N   . ARG A 1 115 ? 0.075   34.759  13.443  1.00 35.40 ? 114 ARG A N   1 
ATOM   847   C CA  . ARG A 1 115 ? 0.525   34.470  12.077  1.00 35.92 ? 114 ARG A CA  1 
ATOM   848   C C   . ARG A 1 115 ? 1.922   35.064  11.857  1.00 36.17 ? 114 ARG A C   1 
ATOM   849   O O   . ARG A 1 115 ? 2.307   35.371  10.723  1.00 36.21 ? 114 ARG A O   1 
ATOM   850   C CB  . ARG A 1 115 ? -0.452  35.041  11.021  1.00 36.17 ? 114 ARG A CB  1 
ATOM   851   C CG  . ARG A 1 115 ? -1.965  34.816  11.251  1.00 36.25 ? 114 ARG A CG  1 
ATOM   852   C CD  . ARG A 1 115 ? -2.320  33.375  11.583  1.00 36.90 ? 114 ARG A CD  1 
ATOM   853   N NE  . ARG A 1 115 ? -1.847  32.447  10.560  1.00 38.35 ? 114 ARG A NE  1 
ATOM   854   C CZ  . ARG A 1 115 ? -1.499  31.182  10.788  1.00 38.46 ? 114 ARG A CZ  1 
ATOM   855   N NH1 . ARG A 1 115 ? -1.559  30.671  12.015  1.00 37.77 ? 114 ARG A NH1 1 
ATOM   856   N NH2 . ARG A 1 115 ? -1.078  30.427  9.782   1.00 38.41 ? 114 ARG A NH2 1 
ATOM   857   N N   . THR A 1 116 ? 2.672   35.221  12.947  1.00 36.36 ? 115 THR A N   1 
ATOM   858   C CA  . THR A 1 116 ? 3.990   35.851  12.905  1.00 36.74 ? 115 THR A CA  1 
ATOM   859   C C   . THR A 1 116 ? 4.989   35.132  13.807  1.00 37.04 ? 115 THR A C   1 
ATOM   860   O O   . THR A 1 116 ? 4.616   34.596  14.850  1.00 36.97 ? 115 THR A O   1 
ATOM   861   C CB  . THR A 1 116 ? 3.915   37.329  13.330  1.00 36.68 ? 115 THR A CB  1 
ATOM   862   O OG1 . THR A 1 116 ? 2.795   37.956  12.696  1.00 36.59 ? 115 THR A OG1 1 
ATOM   863   C CG2 . THR A 1 116 ? 5.180   38.059  12.931  1.00 36.70 ? 115 THR A CG2 1 
ATOM   864   N N   . ASN A 1 117 ? 6.258   35.131  13.403  1.00 37.43 ? 116 ASN A N   1 
ATOM   865   C CA  . ASN A 1 117 ? 7.314   34.487  14.182  1.00 38.14 ? 116 ASN A CA  1 
ATOM   866   C C   . ASN A 1 117 ? 8.430   35.438  14.610  1.00 38.51 ? 116 ASN A C   1 
ATOM   867   O O   . ASN A 1 117 ? 9.220   35.105  15.494  1.00 38.54 ? 116 ASN A O   1 
ATOM   868   C CB  . ASN A 1 117 ? 7.920   33.303  13.412  1.00 38.09 ? 116 ASN A CB  1 
ATOM   869   C CG  . ASN A 1 117 ? 6.920   32.192  13.152  1.00 38.24 ? 116 ASN A CG  1 
ATOM   870   O OD1 . ASN A 1 117 ? 6.428   32.044  12.032  1.00 38.79 ? 116 ASN A OD1 1 
ATOM   871   N ND2 . ASN A 1 117 ? 6.616   31.404  14.182  1.00 37.60 ? 116 ASN A ND2 1 
ATOM   872   N N   . HIS A 1 118 ? 8.497   36.614  13.990  1.00 39.03 ? 117 HIS A N   1 
ATOM   873   C CA  . HIS A 1 118 ? 9.637   37.507  14.199  1.00 39.78 ? 117 HIS A CA  1 
ATOM   874   C C   . HIS A 1 118 ? 9.288   38.987  14.050  1.00 39.92 ? 117 HIS A C   1 
ATOM   875   O O   . HIS A 1 118 ? 8.924   39.452  12.969  1.00 40.08 ? 117 HIS A O   1 
ATOM   876   C CB  . HIS A 1 118 ? 10.794  37.108  13.262  1.00 39.90 ? 117 HIS A CB  1 
ATOM   877   C CG  . HIS A 1 118 ? 12.121  37.714  13.614  1.00 40.58 ? 117 HIS A CG  1 
ATOM   878   N ND1 . HIS A 1 118 ? 12.393  38.268  14.847  1.00 41.72 ? 117 HIS A ND1 1 
ATOM   879   C CD2 . HIS A 1 118 ? 13.267  37.814  12.898  1.00 41.43 ? 117 HIS A CD2 1 
ATOM   880   C CE1 . HIS A 1 118 ? 13.640  38.707  14.866  1.00 41.91 ? 117 HIS A CE1 1 
ATOM   881   N NE2 . HIS A 1 118 ? 14.192  38.442  13.695  1.00 41.64 ? 117 HIS A NE2 1 
ATOM   882   N N   . PHE A 1 119 ? 9.408   39.711  15.156  1.00 40.32 ? 118 PHE A N   1 
ATOM   883   C CA  . PHE A 1 119 ? 9.239   41.160  15.184  1.00 40.74 ? 118 PHE A CA  1 
ATOM   884   C C   . PHE A 1 119 ? 10.593  41.801  15.430  1.00 41.16 ? 118 PHE A C   1 
ATOM   885   O O   . PHE A 1 119 ? 11.294  41.432  16.379  1.00 41.45 ? 118 PHE A O   1 
ATOM   886   C CB  . PHE A 1 119 ? 8.285   41.562  16.312  1.00 40.70 ? 118 PHE A CB  1 
ATOM   887   C CG  . PHE A 1 119 ? 6.834   41.615  15.916  1.00 40.47 ? 118 PHE A CG  1 
ATOM   888   C CD1 . PHE A 1 119 ? 6.379   41.019  14.747  1.00 40.13 ? 118 PHE A CD1 1 
ATOM   889   C CD2 . PHE A 1 119 ? 5.911   42.242  16.746  1.00 40.83 ? 118 PHE A CD2 1 
ATOM   890   C CE1 . PHE A 1 119 ? 5.033   41.073  14.398  1.00 40.61 ? 118 PHE A CE1 1 
ATOM   891   C CE2 . PHE A 1 119 ? 4.563   42.296  16.408  1.00 40.73 ? 118 PHE A CE2 1 
ATOM   892   C CZ  . PHE A 1 119 ? 4.121   41.710  15.234  1.00 40.38 ? 118 PHE A CZ  1 
ATOM   893   N N   . GLU A 1 120 ? 10.966  42.743  14.568  1.00 41.37 ? 119 GLU A N   1 
ATOM   894   C CA  . GLU A 1 120 ? 12.181  43.526  14.761  1.00 41.58 ? 119 GLU A CA  1 
ATOM   895   C C   . GLU A 1 120 ? 11.788  44.979  15.010  1.00 41.42 ? 119 GLU A C   1 
ATOM   896   O O   . GLU A 1 120 ? 11.130  45.607  14.179  1.00 41.55 ? 119 GLU A O   1 
ATOM   897   C CB  . GLU A 1 120 ? 13.110  43.406  13.548  1.00 41.82 ? 119 GLU A CB  1 
ATOM   898   C CG  . GLU A 1 120 ? 14.561  43.827  13.810  1.00 43.13 ? 119 GLU A CG  1 
ATOM   899   C CD  . GLU A 1 120 ? 15.372  44.035  12.528  1.00 45.10 ? 119 GLU A CD  1 
ATOM   900   O OE1 . GLU A 1 120 ? 15.450  43.097  11.696  1.00 45.57 ? 119 GLU A OE1 1 
ATOM   901   O OE2 . GLU A 1 120 ? 15.945  45.139  12.362  1.00 45.04 ? 119 GLU A OE2 1 
ATOM   902   N N   . LYS A 1 121 ? 12.195  45.495  16.164  1.00 41.18 ? 120 LYS A N   1 
ATOM   903   C CA  . LYS A 1 121 ? 11.842  46.837  16.617  1.00 40.96 ? 120 LYS A CA  1 
ATOM   904   C C   . LYS A 1 121 ? 12.753  47.913  16.015  1.00 40.62 ? 120 LYS A C   1 
ATOM   905   O O   . LYS A 1 121 ? 13.973  47.837  16.135  1.00 40.70 ? 120 LYS A O   1 
ATOM   906   C CB  . LYS A 1 121 ? 11.904  46.869  18.147  1.00 41.09 ? 120 LYS A CB  1 
ATOM   907   C CG  . LYS A 1 121 ? 11.345  48.111  18.811  1.00 41.73 ? 120 LYS A CG  1 
ATOM   908   C CD  . LYS A 1 121 ? 11.154  47.851  20.293  1.00 43.28 ? 120 LYS A CD  1 
ATOM   909   C CE  . LYS A 1 121 ? 11.551  49.060  21.116  1.00 44.93 ? 120 LYS A CE  1 
ATOM   910   N NZ  . LYS A 1 121 ? 11.498  48.789  22.586  1.00 46.45 ? 120 LYS A NZ  1 
ATOM   911   N N   . ILE A 1 122 ? 12.151  48.902  15.359  1.00 40.30 ? 121 ILE A N   1 
ATOM   912   C CA  . ILE A 1 122 ? 12.887  50.049  14.814  1.00 40.00 ? 121 ILE A CA  1 
ATOM   913   C C   . ILE A 1 122 ? 12.281  51.385  15.241  1.00 39.95 ? 121 ILE A C   1 
ATOM   914   O O   . ILE A 1 122 ? 11.077  51.493  15.476  1.00 39.92 ? 121 ILE A O   1 
ATOM   915   C CB  . ILE A 1 122 ? 13.013  50.023  13.261  1.00 39.98 ? 121 ILE A CB  1 
ATOM   916   C CG1 . ILE A 1 122 ? 11.633  50.032  12.589  1.00 39.86 ? 121 ILE A CG1 1 
ATOM   917   C CG2 . ILE A 1 122 ? 13.867  48.835  12.798  1.00 40.04 ? 121 ILE A CG2 1 
ATOM   918   C CD1 . ILE A 1 122 ? 11.599  50.784  11.276  1.00 39.60 ? 121 ILE A CD1 1 
ATOM   919   N N   . GLN A 1 123 ? 13.138  52.396  15.337  1.00 39.91 ? 122 GLN A N   1 
ATOM   920   C CA  . GLN A 1 123 ? 12.739  53.746  15.701  1.00 39.76 ? 122 GLN A CA  1 
ATOM   921   C C   . GLN A 1 123 ? 12.253  54.463  14.449  1.00 39.77 ? 122 GLN A C   1 
ATOM   922   O O   . GLN A 1 123 ? 12.932  54.448  13.421  1.00 39.88 ? 122 GLN A O   1 
ATOM   923   C CB  . GLN A 1 123 ? 13.936  54.475  16.312  1.00 39.66 ? 122 GLN A CB  1 
ATOM   924   C CG  . GLN A 1 123 ? 13.657  55.859  16.857  1.00 39.56 ? 122 GLN A CG  1 
ATOM   925   C CD  . GLN A 1 123 ? 14.915  56.531  17.386  1.00 39.88 ? 122 GLN A CD  1 
ATOM   926   O OE1 . GLN A 1 123 ? 15.923  56.638  16.683  1.00 39.37 ? 122 GLN A OE1 1 
ATOM   927   N NE2 . GLN A 1 123 ? 14.859  56.992  18.632  1.00 39.74 ? 122 GLN A NE2 1 
ATOM   928   N N   . ILE A 1 124 ? 11.075  55.075  14.525  1.00 39.67 ? 123 ILE A N   1 
ATOM   929   C CA  . ILE A 1 124 ? 10.533  55.816  13.383  1.00 39.78 ? 123 ILE A CA  1 
ATOM   930   C C   . ILE A 1 124 ? 10.460  57.319  13.641  1.00 39.99 ? 123 ILE A C   1 
ATOM   931   O O   . ILE A 1 124 ? 10.715  58.118  12.741  1.00 39.94 ? 123 ILE A O   1 
ATOM   932   C CB  . ILE A 1 124 ? 9.157   55.258  12.881  1.00 39.84 ? 123 ILE A CB  1 
ATOM   933   C CG1 . ILE A 1 124 ? 8.162   55.079  14.038  1.00 39.28 ? 123 ILE A CG1 1 
ATOM   934   C CG2 . ILE A 1 124 ? 9.355   53.943  12.113  1.00 39.46 ? 123 ILE A CG2 1 
ATOM   935   C CD1 . ILE A 1 124 ? 6.718   54.935  13.594  1.00 38.57 ? 123 ILE A CD1 1 
ATOM   936   N N   . ILE A 1 125 ? 10.105  57.702  14.864  1.00 40.26 ? 124 ILE A N   1 
ATOM   937   C CA  . ILE A 1 125 ? 10.155  59.110  15.271  1.00 40.56 ? 124 ILE A CA  1 
ATOM   938   C C   . ILE A 1 125 ? 10.995  59.258  16.542  1.00 40.53 ? 124 ILE A C   1 
ATOM   939   O O   . ILE A 1 125 ? 10.523  58.944  17.641  1.00 40.50 ? 124 ILE A O   1 
ATOM   940   C CB  . ILE A 1 125 ? 8.739   59.733  15.446  1.00 40.60 ? 124 ILE A CB  1 
ATOM   941   C CG1 . ILE A 1 125 ? 8.075   59.969  14.087  1.00 40.98 ? 124 ILE A CG1 1 
ATOM   942   C CG2 . ILE A 1 125 ? 8.816   61.068  16.171  1.00 40.59 ? 124 ILE A CG2 1 
ATOM   943   C CD1 . ILE A 1 125 ? 7.276   58.805  13.556  1.00 41.49 ? 124 ILE A CD1 1 
ATOM   944   N N   . PRO A 1 126 ? 12.251  59.723  16.392  1.00 40.67 ? 125 PRO A N   1 
ATOM   945   C CA  . PRO A 1 126 ? 13.156  59.880  17.536  1.00 40.72 ? 125 PRO A CA  1 
ATOM   946   C C   . PRO A 1 126 ? 12.581  60.847  18.563  1.00 40.87 ? 125 PRO A C   1 
ATOM   947   O O   . PRO A 1 126 ? 12.053  61.906  18.195  1.00 40.69 ? 125 PRO A O   1 
ATOM   948   C CB  . PRO A 1 126 ? 14.426  60.474  16.909  1.00 40.50 ? 125 PRO A CB  1 
ATOM   949   C CG  . PRO A 1 126 ? 14.332  60.175  15.460  1.00 40.72 ? 125 PRO A CG  1 
ATOM   950   C CD  . PRO A 1 126 ? 12.870  60.187  15.137  1.00 40.68 ? 125 PRO A CD  1 
ATOM   951   N N   . LYS A 1 127 A 12.678  60.477  19.836  1.00 41.24 ? 125 LYS A N   1 
ATOM   952   C CA  . LYS A 1 127 A 12.205  61.319  20.938  1.00 41.87 ? 125 LYS A CA  1 
ATOM   953   C C   . LYS A 1 127 A 12.834  62.721  20.915  1.00 42.07 ? 125 LYS A C   1 
ATOM   954   O O   . LYS A 1 127 A 12.243  63.678  21.410  1.00 42.20 ? 125 LYS A O   1 
ATOM   955   C CB  . LYS A 1 127 A 12.473  60.631  22.280  1.00 41.84 ? 125 LYS A CB  1 
ATOM   956   C CG  . LYS A 1 127 A 11.799  61.290  23.474  1.00 42.69 ? 125 LYS A CG  1 
ATOM   957   C CD  . LYS A 1 127 A 12.160  60.601  24.781  1.00 43.60 ? 125 LYS A CD  1 
ATOM   958   C CE  . LYS A 1 127 A 11.066  59.650  25.229  1.00 43.99 ? 125 LYS A CE  1 
ATOM   959   N NZ  . LYS A 1 127 A 11.337  59.147  26.600  1.00 44.21 ? 125 LYS A NZ  1 
ATOM   960   N N   . SER A 1 128 B 14.017  62.827  20.311  1.00 42.38 ? 125 SER A N   1 
ATOM   961   C CA  . SER A 1 128 B 14.788  64.071  20.252  1.00 42.59 ? 125 SER A CA  1 
ATOM   962   C C   . SER A 1 128 B 14.233  65.087  19.257  1.00 42.56 ? 125 SER A C   1 
ATOM   963   O O   . SER A 1 128 B 14.556  66.277  19.336  1.00 42.60 ? 125 SER A O   1 
ATOM   964   C CB  . SER A 1 128 B 16.241  63.768  19.876  1.00 42.66 ? 125 SER A CB  1 
ATOM   965   O OG  . SER A 1 128 B 16.646  62.498  20.360  1.00 43.49 ? 125 SER A OG  1 
ATOM   966   N N   . SER A 1 129 ? 13.408  64.621  18.322  1.00 42.51 ? 126 SER A N   1 
ATOM   967   C CA  . SER A 1 129 ? 12.906  65.470  17.234  1.00 42.38 ? 126 SER A CA  1 
ATOM   968   C C   . SER A 1 129 ? 11.740  66.385  17.635  1.00 42.38 ? 126 SER A C   1 
ATOM   969   O O   . SER A 1 129 ? 11.258  67.169  16.819  1.00 42.45 ? 126 SER A O   1 
ATOM   970   C CB  . SER A 1 129 ? 12.521  64.614  16.019  1.00 42.38 ? 126 SER A CB  1 
ATOM   971   O OG  . SER A 1 129 ? 11.425  63.759  16.309  1.00 42.02 ? 126 SER A OG  1 
ATOM   972   N N   . TRP A 1 130 ? 11.286  66.280  18.883  1.00 42.47 ? 127 TRP A N   1 
ATOM   973   C CA  . TRP A 1 130 ? 10.218  67.144  19.394  1.00 42.61 ? 127 TRP A CA  1 
ATOM   974   C C   . TRP A 1 130 ? 10.802  68.387  20.057  1.00 42.87 ? 127 TRP A C   1 
ATOM   975   O O   . TRP A 1 130 ? 11.050  68.398  21.263  1.00 43.21 ? 127 TRP A O   1 
ATOM   976   C CB  . TRP A 1 130 ? 9.335   66.385  20.390  1.00 42.42 ? 127 TRP A CB  1 
ATOM   977   C CG  . TRP A 1 130 ? 8.696   65.159  19.813  1.00 41.97 ? 127 TRP A CG  1 
ATOM   978   C CD1 . TRP A 1 130 ? 9.043   63.865  20.058  1.00 40.87 ? 127 TRP A CD1 1 
ATOM   979   C CD2 . TRP A 1 130 ? 7.604   65.115  18.886  1.00 41.26 ? 127 TRP A CD2 1 
ATOM   980   N NE1 . TRP A 1 130 ? 8.237   63.016  19.345  1.00 40.75 ? 127 TRP A NE1 1 
ATOM   981   C CE2 . TRP A 1 130 ? 7.343   63.754  18.615  1.00 41.10 ? 127 TRP A CE2 1 
ATOM   982   C CE3 . TRP A 1 130 ? 6.824   66.093  18.254  1.00 40.77 ? 127 TRP A CE3 1 
ATOM   983   C CZ2 . TRP A 1 130 ? 6.327   63.340  17.741  1.00 40.78 ? 127 TRP A CZ2 1 
ATOM   984   C CZ3 . TRP A 1 130 ? 5.814   65.682  17.383  1.00 40.93 ? 127 TRP A CZ3 1 
ATOM   985   C CH2 . TRP A 1 130 ? 5.576   64.315  17.137  1.00 40.61 ? 127 TRP A CH2 1 
ATOM   986   N N   . SER A 1 131 ? 11.024  69.431  19.269  1.00 43.04 ? 128 SER A N   1 
ATOM   987   C CA  . SER A 1 131 ? 11.658  70.644  19.786  1.00 43.27 ? 128 SER A CA  1 
ATOM   988   C C   . SER A 1 131 ? 10.661  71.686  20.296  1.00 43.18 ? 128 SER A C   1 
ATOM   989   O O   . SER A 1 131 ? 11.028  72.546  21.102  1.00 43.60 ? 128 SER A O   1 
ATOM   990   C CB  . SER A 1 131 ? 12.572  71.260  18.731  1.00 43.28 ? 128 SER A CB  1 
ATOM   991   O OG  . SER A 1 131 ? 11.845  71.511  17.544  1.00 44.20 ? 128 SER A OG  1 
ATOM   992   N N   . ASN A 1 132 ? 9.413   71.607  19.836  1.00 42.78 ? 129 ASN A N   1 
ATOM   993   C CA  . ASN A 1 132 ? 8.371   72.556  20.249  1.00 42.44 ? 129 ASN A CA  1 
ATOM   994   C C   . ASN A 1 132 ? 7.350   71.955  21.217  1.00 41.86 ? 129 ASN A C   1 
ATOM   995   O O   . ASN A 1 132 ? 6.370   72.603  21.592  1.00 41.71 ? 129 ASN A O   1 
ATOM   996   C CB  . ASN A 1 132 ? 7.660   73.141  19.025  1.00 42.69 ? 129 ASN A CB  1 
ATOM   997   C CG  . ASN A 1 132 ? 8.632   73.664  17.981  1.00 43.69 ? 129 ASN A CG  1 
ATOM   998   O OD1 . ASN A 1 132 ? 8.686   73.153  16.862  1.00 44.39 ? 129 ASN A OD1 1 
ATOM   999   N ND2 . ASN A 1 132 ? 9.415   74.676  18.347  1.00 43.95 ? 129 ASN A ND2 1 
ATOM   1000  N N   . HIS A 1 133 ? 7.583   70.710  21.612  1.00 41.25 ? 130 HIS A N   1 
ATOM   1001  C CA  . HIS A 1 133 ? 6.721   70.033  22.568  1.00 40.60 ? 130 HIS A CA  1 
ATOM   1002  C C   . HIS A 1 133 ? 7.571   69.424  23.671  1.00 40.51 ? 130 HIS A C   1 
ATOM   1003  O O   . HIS A 1 133 ? 8.760   69.158  23.472  1.00 40.30 ? 130 HIS A O   1 
ATOM   1004  C CB  . HIS A 1 133 ? 5.878   68.964  21.866  1.00 40.43 ? 130 HIS A CB  1 
ATOM   1005  C CG  . HIS A 1 133 ? 5.019   69.509  20.766  1.00 39.54 ? 130 HIS A CG  1 
ATOM   1006  N ND1 . HIS A 1 133 ? 5.496   69.733  19.491  1.00 38.79 ? 130 HIS A ND1 1 
ATOM   1007  C CD2 . HIS A 1 133 ? 3.723   69.897  20.756  1.00 38.34 ? 130 HIS A CD2 1 
ATOM   1008  C CE1 . HIS A 1 133 ? 4.529   70.230  18.742  1.00 38.34 ? 130 HIS A CE1 1 
ATOM   1009  N NE2 . HIS A 1 133 ? 3.441   70.336  19.485  1.00 38.43 ? 130 HIS A NE2 1 
ATOM   1010  N N   . ASP A 1 134 ? 6.961   69.232  24.836  1.00 40.31 ? 131 ASP A N   1 
ATOM   1011  C CA  . ASP A 1 134 ? 7.624   68.584  25.953  1.00 40.25 ? 131 ASP A CA  1 
ATOM   1012  C C   . ASP A 1 134 ? 7.527   67.065  25.823  1.00 40.27 ? 131 ASP A C   1 
ATOM   1013  O O   . ASP A 1 134 ? 6.466   66.471  26.031  1.00 40.27 ? 131 ASP A O   1 
ATOM   1014  C CB  . ASP A 1 134 ? 7.037   69.064  27.286  1.00 40.19 ? 131 ASP A CB  1 
ATOM   1015  C CG  . ASP A 1 134 ? 7.776   68.499  28.500  1.00 40.26 ? 131 ASP A CG  1 
ATOM   1016  O OD1 . ASP A 1 134 ? 7.584   69.046  29.608  1.00 40.38 ? 131 ASP A OD1 1 
ATOM   1017  O OD2 . ASP A 1 134 ? 8.537   67.510  28.361  1.00 39.98 ? 131 ASP A OD2 1 
ATOM   1018  N N   . ALA A 1 135 ? 8.656   66.450  25.489  1.00 40.45 ? 132 ALA A N   1 
ATOM   1019  C CA  . ALA A 1 135 ? 8.753   65.002  25.344  1.00 40.58 ? 132 ALA A CA  1 
ATOM   1020  C C   . ALA A 1 135 ? 9.380   64.306  26.563  1.00 40.72 ? 132 ALA A C   1 
ATOM   1021  O O   . ALA A 1 135 ? 9.678   63.106  26.512  1.00 40.87 ? 132 ALA A O   1 
ATOM   1022  C CB  . ALA A 1 135 ? 9.527   64.659  24.075  1.00 40.61 ? 132 ALA A CB  1 
ATOM   1023  N N   . SER A 1 136 ? 9.562   65.041  27.661  1.00 40.71 ? 133 SER A N   1 
ATOM   1024  C CA  . SER A 1 136 ? 10.164  64.445  28.857  1.00 40.81 ? 133 SER A CA  1 
ATOM   1025  C C   . SER A 1 136 ? 9.241   64.323  30.072  1.00 40.61 ? 133 SER A C   1 
ATOM   1026  O O   . SER A 1 136 ? 9.387   63.384  30.856  1.00 40.88 ? 133 SER A O   1 
ATOM   1027  C CB  . SER A 1 136 ? 11.481  65.139  29.237  1.00 40.98 ? 133 SER A CB  1 
ATOM   1028  O OG  . SER A 1 136 ? 11.280  66.504  29.571  1.00 42.16 ? 133 SER A OG  1 
ATOM   1029  N N   . SER A 1 137 A 8.292   65.245  30.232  1.00 40.32 ? 133 SER A N   1 
ATOM   1030  C CA  . SER A 1 137 A 7.436   65.237  31.431  1.00 40.19 ? 133 SER A CA  1 
ATOM   1031  C C   . SER A 1 137 A 6.153   64.404  31.322  1.00 39.81 ? 133 SER A C   1 
ATOM   1032  O O   . SER A 1 137 A 5.324   64.404  32.241  1.00 39.88 ? 133 SER A O   1 
ATOM   1033  C CB  . SER A 1 137 A 7.123   66.666  31.902  1.00 40.39 ? 133 SER A CB  1 
ATOM   1034  O OG  . SER A 1 137 A 6.253   67.340  31.008  1.00 41.55 ? 133 SER A OG  1 
ATOM   1035  N N   . GLY A 1 138 ? 6.002   63.677  30.215  1.00 39.35 ? 134 GLY A N   1 
ATOM   1036  C CA  . GLY A 1 138 ? 4.843   62.809  30.004  1.00 38.51 ? 134 GLY A CA  1 
ATOM   1037  C C   . GLY A 1 138 ? 5.002   61.458  30.677  1.00 37.97 ? 134 GLY A C   1 
ATOM   1038  O O   . GLY A 1 138 ? 5.040   60.420  30.010  1.00 37.97 ? 134 GLY A O   1 
ATOM   1039  N N   . VAL A 1 139 ? 5.099   61.485  32.005  1.00 37.36 ? 135 VAL A N   1 
ATOM   1040  C CA  . VAL A 1 139 ? 5.259   60.289  32.833  1.00 36.49 ? 135 VAL A CA  1 
ATOM   1041  C C   . VAL A 1 139 ? 4.189   60.257  33.925  1.00 36.08 ? 135 VAL A C   1 
ATOM   1042  O O   . VAL A 1 139 ? 3.610   61.285  34.262  1.00 35.69 ? 135 VAL A O   1 
ATOM   1043  C CB  . VAL A 1 139 ? 6.675   60.211  33.471  1.00 36.65 ? 135 VAL A CB  1 
ATOM   1044  C CG1 . VAL A 1 139 ? 7.717   59.858  32.423  1.00 36.52 ? 135 VAL A CG1 1 
ATOM   1045  C CG2 . VAL A 1 139 ? 7.041   61.519  34.183  1.00 36.34 ? 135 VAL A CG2 1 
ATOM   1046  N N   . SER A 1 140 ? 3.937   59.075  34.480  1.00 35.86 ? 136 SER A N   1 
ATOM   1047  C CA  . SER A 1 140 ? 2.835   58.893  35.421  1.00 35.65 ? 136 SER A CA  1 
ATOM   1048  C C   . SER A 1 140 ? 3.167   57.935  36.561  1.00 35.60 ? 136 SER A C   1 
ATOM   1049  O O   . SER A 1 140 ? 3.925   56.978  36.383  1.00 35.68 ? 136 SER A O   1 
ATOM   1050  C CB  . SER A 1 140 ? 1.592   58.398  34.677  1.00 35.39 ? 136 SER A CB  1 
ATOM   1051  O OG  . SER A 1 140 ? 0.571   58.023  35.588  1.00 35.67 ? 136 SER A OG  1 
ATOM   1052  N N   . SER A 1 141 ? 2.569   58.189  37.724  1.00 35.51 ? 137 SER A N   1 
ATOM   1053  C CA  . SER A 1 141 ? 2.678   57.289  38.871  1.00 35.75 ? 137 SER A CA  1 
ATOM   1054  C C   . SER A 1 141 ? 1.888   55.991  38.660  1.00 36.01 ? 137 SER A C   1 
ATOM   1055  O O   . SER A 1 141 ? 1.921   55.088  39.503  1.00 35.80 ? 137 SER A O   1 
ATOM   1056  C CB  . SER A 1 141 ? 2.235   57.990  40.160  1.00 35.63 ? 137 SER A CB  1 
ATOM   1057  O OG  . SER A 1 141 ? 0.898   58.451  40.060  1.00 35.76 ? 137 SER A OG  1 
ATOM   1058  N N   . ALA A 1 142 ? 1.185   55.903  37.532  1.00 36.47 ? 138 ALA A N   1 
ATOM   1059  C CA  . ALA A 1 142 ? 0.494   54.676  37.142  1.00 37.01 ? 138 ALA A CA  1 
ATOM   1060  C C   . ALA A 1 142 ? 1.473   53.665  36.546  1.00 37.33 ? 138 ALA A C   1 
ATOM   1061  O O   . ALA A 1 142 ? 1.189   52.468  36.517  1.00 37.37 ? 138 ALA A O   1 
ATOM   1062  C CB  . ALA A 1 142 ? -0.620  54.979  36.159  1.00 37.03 ? 138 ALA A CB  1 
ATOM   1063  N N   . CYS A 1 143 ? 2.623   54.158  36.083  1.00 37.65 ? 139 CYS A N   1 
ATOM   1064  C CA  . CYS A 1 143 ? 3.663   53.315  35.488  1.00 38.08 ? 139 CYS A CA  1 
ATOM   1065  C C   . CYS A 1 143 ? 5.008   53.478  36.214  1.00 38.17 ? 139 CYS A C   1 
ATOM   1066  O O   . CYS A 1 143 ? 5.974   53.974  35.624  1.00 38.09 ? 139 CYS A O   1 
ATOM   1067  C CB  . CYS A 1 143 ? 3.834   53.649  34.001  1.00 37.98 ? 139 CYS A CB  1 
ATOM   1068  S SG  . CYS A 1 143 ? 2.306   53.609  33.025  1.00 39.29 ? 139 CYS A SG  1 
ATOM   1069  N N   . PRO A 1 144 ? 5.082   53.052  37.493  1.00 38.20 ? 140 PRO A N   1 
ATOM   1070  C CA  . PRO A 1 144 ? 6.309   53.287  38.250  1.00 38.21 ? 140 PRO A CA  1 
ATOM   1071  C C   . PRO A 1 144 ? 7.408   52.300  37.883  1.00 38.27 ? 140 PRO A C   1 
ATOM   1072  O O   . PRO A 1 144 ? 7.121   51.170  37.487  1.00 38.45 ? 140 PRO A O   1 
ATOM   1073  C CB  . PRO A 1 144 ? 5.873   53.078  39.703  1.00 38.15 ? 140 PRO A CB  1 
ATOM   1074  C CG  . PRO A 1 144 ? 4.728   52.126  39.635  1.00 38.27 ? 140 PRO A CG  1 
ATOM   1075  C CD  . PRO A 1 144 ? 4.117   52.229  38.250  1.00 38.40 ? 140 PRO A CD  1 
ATOM   1076  N N   . TYR A 1 145 ? 8.654   52.742  37.995  1.00 38.17 ? 141 TYR A N   1 
ATOM   1077  C CA  . TYR A 1 145 ? 9.802   51.858  37.850  1.00 38.24 ? 141 TYR A CA  1 
ATOM   1078  C C   . TYR A 1 145 ? 10.855  52.263  38.869  1.00 37.69 ? 141 TYR A C   1 
ATOM   1079  O O   . TYR A 1 145 ? 11.337  53.402  38.848  1.00 37.67 ? 141 TYR A O   1 
ATOM   1080  C CB  . TYR A 1 145 ? 10.370  51.915  36.430  1.00 38.48 ? 141 TYR A CB  1 
ATOM   1081  C CG  . TYR A 1 145 ? 11.279  50.750  36.088  1.00 40.14 ? 141 TYR A CG  1 
ATOM   1082  C CD1 . TYR A 1 145 ? 10.750  49.516  35.712  1.00 41.82 ? 141 TYR A CD1 1 
ATOM   1083  C CD2 . TYR A 1 145 ? 12.666  50.879  36.137  1.00 41.92 ? 141 TYR A CD2 1 
ATOM   1084  C CE1 . TYR A 1 145 ? 11.577  48.437  35.395  1.00 42.85 ? 141 TYR A CE1 1 
ATOM   1085  C CE2 . TYR A 1 145 ? 13.505  49.798  35.820  1.00 42.83 ? 141 TYR A CE2 1 
ATOM   1086  C CZ  . TYR A 1 145 ? 12.949  48.586  35.447  1.00 43.32 ? 141 TYR A CZ  1 
ATOM   1087  O OH  . TYR A 1 145 ? 13.759  47.515  35.127  1.00 44.74 ? 141 TYR A OH  1 
ATOM   1088  N N   . HIS A 1 146 ? 11.190  51.336  39.766  1.00 37.11 ? 142 HIS A N   1 
ATOM   1089  C CA  . HIS A 1 146 ? 12.145  51.591  40.850  1.00 36.86 ? 142 HIS A CA  1 
ATOM   1090  C C   . HIS A 1 146 ? 11.792  52.875  41.603  1.00 36.52 ? 142 HIS A C   1 
ATOM   1091  O O   . HIS A 1 146 ? 12.669  53.649  41.996  1.00 36.41 ? 142 HIS A O   1 
ATOM   1092  C CB  . HIS A 1 146 ? 13.581  51.648  40.306  1.00 36.96 ? 142 HIS A CB  1 
ATOM   1093  C CG  . HIS A 1 146 ? 14.132  50.315  39.897  1.00 37.39 ? 142 HIS A CG  1 
ATOM   1094  N ND1 . HIS A 1 146 ? 15.452  50.136  39.543  1.00 38.02 ? 142 HIS A ND1 1 
ATOM   1095  C CD2 . HIS A 1 146 ? 13.549  49.096  39.801  1.00 37.21 ? 142 HIS A CD2 1 
ATOM   1096  C CE1 . HIS A 1 146 ? 15.655  48.868  39.232  1.00 37.86 ? 142 HIS A CE1 1 
ATOM   1097  N NE2 . HIS A 1 146 ? 14.516  48.216  39.383  1.00 37.98 ? 142 HIS A NE2 1 
ATOM   1098  N N   . GLY A 1 147 ? 10.491  53.098  41.774  1.00 36.19 ? 143 GLY A N   1 
ATOM   1099  C CA  . GLY A 1 147 ? 9.986   54.265  42.480  1.00 35.73 ? 143 GLY A CA  1 
ATOM   1100  C C   . GLY A 1 147 ? 9.986   55.564  41.695  1.00 35.41 ? 143 GLY A C   1 
ATOM   1101  O O   . GLY A 1 147 ? 9.772   56.634  42.264  1.00 35.48 ? 143 GLY A O   1 
ATOM   1102  N N   . LYS A 1 148 ? 10.226  55.499  40.393  1.00 34.90 ? 144 LYS A N   1 
ATOM   1103  C CA  . LYS A 1 148 ? 10.160  56.718  39.592  1.00 34.59 ? 144 LYS A CA  1 
ATOM   1104  C C   . LYS A 1 148 ? 9.014   56.673  38.578  1.00 33.84 ? 144 LYS A C   1 
ATOM   1105  O O   . LYS A 1 148 ? 8.753   55.637  37.967  1.00 33.84 ? 144 LYS A O   1 
ATOM   1106  C CB  . LYS A 1 148 ? 11.519  57.041  38.944  1.00 34.78 ? 144 LYS A CB  1 
ATOM   1107  C CG  . LYS A 1 148 ? 12.649  57.222  39.969  1.00 35.97 ? 144 LYS A CG  1 
ATOM   1108  C CD  . LYS A 1 148 ? 13.819  58.044  39.446  1.00 38.94 ? 144 LYS A CD  1 
ATOM   1109  C CE  . LYS A 1 148 ? 13.814  59.492  39.996  1.00 40.64 ? 144 LYS A CE  1 
ATOM   1110  N NZ  . LYS A 1 148 ? 12.816  60.403  39.330  1.00 41.11 ? 144 LYS A NZ  1 
ATOM   1111  N N   . SER A 1 149 ? 8.312   57.794  38.443  1.00 33.04 ? 145 SER A N   1 
ATOM   1112  C CA  . SER A 1 149 ? 7.226   57.924  37.477  1.00 32.04 ? 145 SER A CA  1 
ATOM   1113  C C   . SER A 1 149 ? 7.742   57.705  36.072  1.00 31.76 ? 145 SER A C   1 
ATOM   1114  O O   . SER A 1 149 ? 8.722   58.325  35.666  1.00 31.79 ? 145 SER A O   1 
ATOM   1115  C CB  . SER A 1 149 ? 6.571   59.295  37.578  1.00 31.76 ? 145 SER A CB  1 
ATOM   1116  O OG  . SER A 1 149 ? 5.612   59.298  38.609  1.00 30.84 ? 145 SER A OG  1 
ATOM   1117  N N   . SER A 1 150 ? 7.088   56.807  35.341  1.00 31.21 ? 146 SER A N   1 
ATOM   1118  C CA  . SER A 1 150 ? 7.502   56.488  33.983  1.00 30.79 ? 146 SER A CA  1 
ATOM   1119  C C   . SER A 1 150 ? 6.315   56.420  33.016  1.00 30.50 ? 146 SER A C   1 
ATOM   1120  O O   . SER A 1 150 ? 5.205   56.870  33.335  1.00 30.59 ? 146 SER A O   1 
ATOM   1121  C CB  . SER A 1 150 ? 8.309   55.188  33.965  1.00 30.61 ? 146 SER A CB  1 
ATOM   1122  O OG  . SER A 1 150 ? 9.089   55.103  32.786  1.00 30.74 ? 146 SER A OG  1 
ATOM   1123  N N   . PHE A 1 151 ? 6.561   55.861  31.835  1.00 30.00 ? 147 PHE A N   1 
ATOM   1124  C CA  . PHE A 1 151 ? 5.530   55.681  30.824  1.00 29.62 ? 147 PHE A CA  1 
ATOM   1125  C C   . PHE A 1 151 ? 5.879   54.484  29.943  1.00 29.33 ? 147 PHE A C   1 
ATOM   1126  O O   . PHE A 1 151 ? 6.937   53.872  30.120  1.00 29.26 ? 147 PHE A O   1 
ATOM   1127  C CB  . PHE A 1 151 ? 5.379   56.961  29.993  1.00 29.59 ? 147 PHE A CB  1 
ATOM   1128  C CG  . PHE A 1 151 ? 4.075   57.059  29.254  1.00 30.06 ? 147 PHE A CG  1 
ATOM   1129  C CD1 . PHE A 1 151 ? 2.858   57.014  29.941  1.00 29.80 ? 147 PHE A CD1 1 
ATOM   1130  C CD2 . PHE A 1 151 ? 4.059   57.207  27.864  1.00 30.23 ? 147 PHE A CD2 1 
ATOM   1131  C CE1 . PHE A 1 151 ? 1.649   57.104  29.255  1.00 29.08 ? 147 PHE A CE1 1 
ATOM   1132  C CE2 . PHE A 1 151 ? 2.858   57.297  27.171  1.00 29.36 ? 147 PHE A CE2 1 
ATOM   1133  C CZ  . PHE A 1 151 ? 1.650   57.248  27.871  1.00 29.52 ? 147 PHE A CZ  1 
ATOM   1134  N N   . PHE A 1 152 ? 4.980   54.140  29.019  1.00 28.90 ? 148 PHE A N   1 
ATOM   1135  C CA  . PHE A 1 152 ? 5.235   53.111  28.015  1.00 28.52 ? 148 PHE A CA  1 
ATOM   1136  C C   . PHE A 1 152 ? 6.482   53.487  27.214  1.00 28.57 ? 148 PHE A C   1 
ATOM   1137  O O   . PHE A 1 152 ? 6.627   54.633  26.809  1.00 28.86 ? 148 PHE A O   1 
ATOM   1138  C CB  . PHE A 1 152 ? 4.026   52.959  27.077  1.00 28.29 ? 148 PHE A CB  1 
ATOM   1139  C CG  . PHE A 1 152 ? 2.765   52.493  27.765  1.00 27.34 ? 148 PHE A CG  1 
ATOM   1140  C CD1 . PHE A 1 152 ? 2.576   51.146  28.067  1.00 25.95 ? 148 PHE A CD1 1 
ATOM   1141  C CD2 . PHE A 1 152 ? 1.762   53.401  28.102  1.00 27.02 ? 148 PHE A CD2 1 
ATOM   1142  C CE1 . PHE A 1 152 ? 1.419   50.708  28.701  1.00 24.94 ? 148 PHE A CE1 1 
ATOM   1143  C CE2 . PHE A 1 152 ? 0.595   52.972  28.734  1.00 26.35 ? 148 PHE A CE2 1 
ATOM   1144  C CZ  . PHE A 1 152 ? 0.426   51.619  29.035  1.00 26.05 ? 148 PHE A CZ  1 
ATOM   1145  N N   . ARG A 1 153 ? 7.369   52.521  26.991  1.00 28.74 ? 149 ARG A N   1 
ATOM   1146  C CA  . ARG A 1 153 ? 8.678   52.775  26.363  1.00 29.17 ? 149 ARG A CA  1 
ATOM   1147  C C   . ARG A 1 153 ? 8.606   53.130  24.877  1.00 29.07 ? 149 ARG A C   1 
ATOM   1148  O O   . ARG A 1 153 ? 9.430   53.898  24.387  1.00 29.35 ? 149 ARG A O   1 
ATOM   1149  C CB  . ARG A 1 153 ? 9.619   51.570  26.540  1.00 29.38 ? 149 ARG A CB  1 
ATOM   1150  C CG  . ARG A 1 153 ? 9.890   51.135  27.985  1.00 30.05 ? 149 ARG A CG  1 
ATOM   1151  C CD  . ARG A 1 153 ? 11.254  51.577  28.482  1.00 32.10 ? 149 ARG A CD  1 
ATOM   1152  N NE  . ARG A 1 153 ? 11.164  52.671  29.450  1.00 34.26 ? 149 ARG A NE  1 
ATOM   1153  C CZ  . ARG A 1 153 ? 11.357  52.534  30.764  1.00 33.57 ? 149 ARG A CZ  1 
ATOM   1154  N NH1 . ARG A 1 153 ? 11.661  51.348  31.286  1.00 31.60 ? 149 ARG A NH1 1 
ATOM   1155  N NH2 . ARG A 1 153 ? 11.242  53.591  31.557  1.00 33.29 ? 149 ARG A NH2 1 
ATOM   1156  N N   . ASN A 1 154 ? 7.630   52.574  24.164  1.00 29.05 ? 150 ASN A N   1 
ATOM   1157  C CA  . ASN A 1 154 ? 7.588   52.681  22.702  1.00 29.08 ? 150 ASN A CA  1 
ATOM   1158  C C   . ASN A 1 154 ? 6.781   53.857  22.170  1.00 29.23 ? 150 ASN A C   1 
ATOM   1159  O O   . ASN A 1 154 ? 6.791   54.137  20.965  1.00 29.09 ? 150 ASN A O   1 
ATOM   1160  C CB  . ASN A 1 154 ? 7.088   51.373  22.089  1.00 29.17 ? 150 ASN A CB  1 
ATOM   1161  C CG  . ASN A 1 154 ? 7.938   50.183  22.488  1.00 29.23 ? 150 ASN A CG  1 
ATOM   1162  O OD1 . ASN A 1 154 ? 9.096   50.335  22.879  1.00 29.52 ? 150 ASN A OD1 1 
ATOM   1163  N ND2 . ASN A 1 154 ? 7.369   48.993  22.390  1.00 29.31 ? 150 ASN A ND2 1 
ATOM   1164  N N   . VAL A 1 155 ? 6.089   54.545  23.074  1.00 29.42 ? 151 VAL A N   1 
ATOM   1165  C CA  . VAL A 1 155 ? 5.229   55.665  22.703  1.00 29.66 ? 151 VAL A CA  1 
ATOM   1166  C C   . VAL A 1 155 ? 5.533   56.889  23.572  1.00 29.85 ? 151 VAL A C   1 
ATOM   1167  O O   . VAL A 1 155 ? 5.986   56.750  24.712  1.00 30.36 ? 151 VAL A O   1 
ATOM   1168  C CB  . VAL A 1 155 ? 3.711   55.285  22.766  1.00 29.56 ? 151 VAL A CB  1 
ATOM   1169  C CG1 . VAL A 1 155 ? 3.382   54.198  21.757  1.00 29.21 ? 151 VAL A CG1 1 
ATOM   1170  C CG2 . VAL A 1 155 ? 3.307   54.843  24.164  1.00 29.44 ? 151 VAL A CG2 1 
ATOM   1171  N N   . VAL A 1 156 ? 5.289   58.079  23.032  1.00 29.68 ? 152 VAL A N   1 
ATOM   1172  C CA  . VAL A 1 156 ? 5.647   59.320  23.715  1.00 29.69 ? 152 VAL A CA  1 
ATOM   1173  C C   . VAL A 1 156 ? 4.417   60.178  24.041  1.00 29.86 ? 152 VAL A C   1 
ATOM   1174  O O   . VAL A 1 156 ? 3.684   60.599  23.146  1.00 29.78 ? 152 VAL A O   1 
ATOM   1175  C CB  . VAL A 1 156 ? 6.659   60.148  22.883  1.00 29.66 ? 152 VAL A CB  1 
ATOM   1176  C CG1 . VAL A 1 156 ? 7.148   61.351  23.671  1.00 29.20 ? 152 VAL A CG1 1 
ATOM   1177  C CG2 . VAL A 1 156 ? 7.833   59.285  22.454  1.00 29.51 ? 152 VAL A CG2 1 
ATOM   1178  N N   . TRP A 1 157 ? 4.207   60.430  25.330  1.00 29.92 ? 153 TRP A N   1 
ATOM   1179  C CA  . TRP A 1 157 ? 3.121   61.279  25.790  1.00 30.03 ? 153 TRP A CA  1 
ATOM   1180  C C   . TRP A 1 157 ? 3.587   62.729  25.748  1.00 30.55 ? 153 TRP A C   1 
ATOM   1181  O O   . TRP A 1 157 ? 4.341   63.174  26.619  1.00 30.54 ? 153 TRP A O   1 
ATOM   1182  C CB  . TRP A 1 157 ? 2.705   60.868  27.201  1.00 29.72 ? 153 TRP A CB  1 
ATOM   1183  C CG  . TRP A 1 157 ? 1.524   61.589  27.785  1.00 28.99 ? 153 TRP A CG  1 
ATOM   1184  C CD1 . TRP A 1 157 ? 0.685   62.470  27.154  1.00 29.06 ? 153 TRP A CD1 1 
ATOM   1185  C CD2 . TRP A 1 157 ? 1.031   61.454  29.116  1.00 28.64 ? 153 TRP A CD2 1 
ATOM   1186  N NE1 . TRP A 1 157 ? -0.293  62.898  28.019  1.00 28.03 ? 153 TRP A NE1 1 
ATOM   1187  C CE2 . TRP A 1 157 ? -0.105  62.288  29.230  1.00 28.80 ? 153 TRP A CE2 1 
ATOM   1188  C CE3 . TRP A 1 157 ? 1.440   60.708  30.231  1.00 28.92 ? 153 TRP A CE3 1 
ATOM   1189  C CZ2 . TRP A 1 157 ? -0.835  62.401  30.417  1.00 29.09 ? 153 TRP A CZ2 1 
ATOM   1190  C CZ3 . TRP A 1 157 ? 0.713   60.818  31.409  1.00 29.63 ? 153 TRP A CZ3 1 
ATOM   1191  C CH2 . TRP A 1 157 ? -0.412  61.661  31.492  1.00 29.73 ? 153 TRP A CH2 1 
ATOM   1192  N N   . LEU A 1 158 ? 3.143   63.450  24.721  1.00 30.96 ? 154 LEU A N   1 
ATOM   1193  C CA  . LEU A 1 158 ? 3.589   64.818  24.480  1.00 31.56 ? 154 LEU A CA  1 
ATOM   1194  C C   . LEU A 1 158 ? 2.790   65.829  25.291  1.00 32.08 ? 154 LEU A C   1 
ATOM   1195  O O   . LEU A 1 158 ? 1.561   65.740  25.393  1.00 31.92 ? 154 LEU A O   1 
ATOM   1196  C CB  . LEU A 1 158 ? 3.535   65.171  22.989  1.00 31.41 ? 154 LEU A CB  1 
ATOM   1197  C CG  . LEU A 1 158 ? 4.429   64.384  22.022  1.00 31.52 ? 154 LEU A CG  1 
ATOM   1198  C CD1 . LEU A 1 158 ? 4.049   64.678  20.577  1.00 31.40 ? 154 LEU A CD1 1 
ATOM   1199  C CD2 . LEU A 1 158 ? 5.913   64.667  22.253  1.00 31.42 ? 154 LEU A CD2 1 
ATOM   1200  N N   . ILE A 1 159 ? 3.515   66.785  25.868  1.00 32.63 ? 155 ILE A N   1 
ATOM   1201  C CA  . ILE A 1 159 ? 2.930   67.837  26.688  1.00 33.23 ? 155 ILE A CA  1 
ATOM   1202  C C   . ILE A 1 159 ? 3.187   69.191  26.017  1.00 33.69 ? 155 ILE A C   1 
ATOM   1203  O O   . ILE A 1 159 ? 4.059   69.305  25.152  1.00 33.64 ? 155 ILE A O   1 
ATOM   1204  C CB  . ILE A 1 159 ? 3.516   67.796  28.143  1.00 33.20 ? 155 ILE A CB  1 
ATOM   1205  C CG1 . ILE A 1 159 ? 3.448   66.373  28.729  1.00 33.12 ? 155 ILE A CG1 1 
ATOM   1206  C CG2 . ILE A 1 159 ? 2.830   68.814  29.073  1.00 32.84 ? 155 ILE A CG2 1 
ATOM   1207  C CD1 . ILE A 1 159 ? 2.038   65.760  28.811  1.00 32.40 ? 155 ILE A CD1 1 
ATOM   1208  N N   . LYS A 1 160 ? 2.416   70.206  26.397  1.00 34.52 ? 156 LYS A N   1 
ATOM   1209  C CA  . LYS A 1 160 ? 2.701   71.578  25.973  1.00 35.60 ? 156 LYS A CA  1 
ATOM   1210  C C   . LYS A 1 160 ? 4.065   72.046  26.499  1.00 36.27 ? 156 LYS A C   1 
ATOM   1211  O O   . LYS A 1 160 ? 4.531   71.581  27.540  1.00 36.49 ? 156 LYS A O   1 
ATOM   1212  C CB  . LYS A 1 160 ? 1.596   72.535  26.430  1.00 35.58 ? 156 LYS A CB  1 
ATOM   1213  C CG  . LYS A 1 160 ? 1.609   72.845  27.919  1.00 35.43 ? 156 LYS A CG  1 
ATOM   1214  C CD  . LYS A 1 160 ? 0.337   73.530  28.351  1.00 35.71 ? 156 LYS A CD  1 
ATOM   1215  C CE  . LYS A 1 160 ? 0.472   74.092  29.754  1.00 35.40 ? 156 LYS A CE  1 
ATOM   1216  N NZ  . LYS A 1 160 ? -0.779  74.788  30.132  1.00 36.45 ? 156 LYS A NZ  1 
ATOM   1217  N N   . LYS A 1 161 ? 4.703   72.942  25.752  1.00 37.08 ? 157 LYS A N   1 
ATOM   1218  C CA  . LYS A 1 161 ? 5.946   73.584  26.169  1.00 37.95 ? 157 LYS A CA  1 
ATOM   1219  C C   . LYS A 1 161 ? 5.737   75.096  26.125  1.00 38.28 ? 157 LYS A C   1 
ATOM   1220  O O   . LYS A 1 161 ? 5.192   75.622  25.143  1.00 38.44 ? 157 LYS A O   1 
ATOM   1221  C CB  . LYS A 1 161 ? 7.106   73.188  25.250  1.00 37.98 ? 157 LYS A CB  1 
ATOM   1222  C CG  . LYS A 1 161 ? 8.440   73.781  25.673  1.00 39.15 ? 157 LYS A CG  1 
ATOM   1223  C CD  . LYS A 1 161 ? 9.365   74.049  24.493  1.00 40.99 ? 157 LYS A CD  1 
ATOM   1224  C CE  . LYS A 1 161 ? 10.481  73.025  24.407  1.00 41.82 ? 157 LYS A CE  1 
ATOM   1225  N NZ  . LYS A 1 161 ? 11.627  73.553  23.610  1.00 42.24 ? 157 LYS A NZ  1 
ATOM   1226  N N   . ASN A 1 162 ? 6.158   75.785  27.189  1.00 38.49 ? 158 ASN A N   1 
ATOM   1227  C CA  . ASN A 1 162 ? 5.977   77.239  27.320  1.00 38.76 ? 158 ASN A CA  1 
ATOM   1228  C C   . ASN A 1 162 ? 4.529   77.677  27.092  1.00 38.78 ? 158 ASN A C   1 
ATOM   1229  O O   . ASN A 1 162 ? 4.264   78.602  26.313  1.00 38.83 ? 158 ASN A O   1 
ATOM   1230  C CB  . ASN A 1 162 ? 6.922   78.006  26.376  1.00 38.82 ? 158 ASN A CB  1 
ATOM   1231  C CG  . ASN A 1 162 ? 8.390   77.745  26.669  1.00 39.25 ? 158 ASN A CG  1 
ATOM   1232  O OD1 . ASN A 1 162 ? 8.814   77.702  27.828  1.00 39.70 ? 158 ASN A OD1 1 
ATOM   1233  N ND2 . ASN A 1 162 ? 9.176   77.575  25.614  1.00 39.41 ? 158 ASN A ND2 1 
ATOM   1234  N N   . SER A 1 163 ? 3.604   77.001  27.775  1.00 38.67 ? 159 SER A N   1 
ATOM   1235  C CA  . SER A 1 163 ? 2.163   77.213  27.601  1.00 38.88 ? 159 SER A CA  1 
ATOM   1236  C C   . SER A 1 163 ? 1.703   77.274  26.134  1.00 38.70 ? 159 SER A C   1 
ATOM   1237  O O   . SER A 1 163 ? 0.968   78.181  25.737  1.00 38.84 ? 159 SER A O   1 
ATOM   1238  C CB  . SER A 1 163 ? 1.693   78.446  28.385  1.00 38.91 ? 159 SER A CB  1 
ATOM   1239  O OG  . SER A 1 163 ? 1.097   78.060  29.617  1.00 40.13 ? 159 SER A OG  1 
ATOM   1240  N N   . ALA A 1 164 ? 2.137   76.299  25.337  1.00 38.51 ? 160 ALA A N   1 
ATOM   1241  C CA  . ALA A 1 164 ? 1.772   76.239  23.919  1.00 38.04 ? 160 ALA A CA  1 
ATOM   1242  C C   . ALA A 1 164 ? 1.882   74.828  23.347  1.00 37.77 ? 160 ALA A C   1 
ATOM   1243  O O   . ALA A 1 164 ? 2.835   74.095  23.640  1.00 37.83 ? 160 ALA A O   1 
ATOM   1244  C CB  . ALA A 1 164 ? 2.625   77.214  23.100  1.00 37.97 ? 160 ALA A CB  1 
ATOM   1245  N N   . TYR A 1 165 ? 0.899   74.459  22.529  1.00 37.36 ? 161 TYR A N   1 
ATOM   1246  C CA  . TYR A 1 165 ? 0.923   73.189  21.810  1.00 36.72 ? 161 TYR A CA  1 
ATOM   1247  C C   . TYR A 1 165 ? 0.644   73.458  20.336  1.00 36.35 ? 161 TYR A C   1 
ATOM   1248  O O   . TYR A 1 165 ? -0.509  73.407  19.892  1.00 36.08 ? 161 TYR A O   1 
ATOM   1249  C CB  . TYR A 1 165 ? -0.093  72.210  22.402  1.00 36.69 ? 161 TYR A CB  1 
ATOM   1250  C CG  . TYR A 1 165 ? 0.121   70.740  22.067  1.00 36.62 ? 161 TYR A CG  1 
ATOM   1251  C CD1 . TYR A 1 165 ? 0.444   69.819  23.064  1.00 36.16 ? 161 TYR A CD1 1 
ATOM   1252  C CD2 . TYR A 1 165 ? -0.036  70.265  20.763  1.00 36.98 ? 161 TYR A CD2 1 
ATOM   1253  C CE1 . TYR A 1 165 ? 0.620   68.472  22.772  1.00 36.43 ? 161 TYR A CE1 1 
ATOM   1254  C CE2 . TYR A 1 165 ? 0.139   68.922  20.458  1.00 36.84 ? 161 TYR A CE2 1 
ATOM   1255  C CZ  . TYR A 1 165 ? 0.464   68.032  21.463  1.00 36.98 ? 161 TYR A CZ  1 
ATOM   1256  O OH  . TYR A 1 165 ? 0.632   66.703  21.152  1.00 36.80 ? 161 TYR A OH  1 
ATOM   1257  N N   . PRO A 1 166 ? 1.710   73.755  19.569  1.00 36.10 ? 162 PRO A N   1 
ATOM   1258  C CA  . PRO A 1 166 ? 1.583   74.003  18.134  1.00 35.78 ? 162 PRO A CA  1 
ATOM   1259  C C   . PRO A 1 166 ? 1.095   72.749  17.413  1.00 35.50 ? 162 PRO A C   1 
ATOM   1260  O O   . PRO A 1 166 ? 1.343   71.631  17.884  1.00 35.41 ? 162 PRO A O   1 
ATOM   1261  C CB  . PRO A 1 166 ? 3.019   74.327  17.696  1.00 35.84 ? 162 PRO A CB  1 
ATOM   1262  C CG  . PRO A 1 166 ? 3.812   74.509  18.954  1.00 35.88 ? 162 PRO A CG  1 
ATOM   1263  C CD  . PRO A 1 166 ? 3.119   73.718  20.002  1.00 36.07 ? 162 PRO A CD  1 
ATOM   1264  N N   . THR A 1 167 ? 0.408   72.937  16.288  1.00 35.12 ? 163 THR A N   1 
ATOM   1265  C CA  . THR A 1 167 ? -0.084  71.812  15.494  1.00 34.83 ? 163 THR A CA  1 
ATOM   1266  C C   . THR A 1 167 ? 1.091   70.979  14.986  1.00 34.69 ? 163 THR A C   1 
ATOM   1267  O O   . THR A 1 167 ? 2.048   71.512  14.426  1.00 34.63 ? 163 THR A O   1 
ATOM   1268  C CB  . THR A 1 167 ? -0.976  72.259  14.301  1.00 34.74 ? 163 THR A CB  1 
ATOM   1269  O OG1 . THR A 1 167 ? -1.884  73.282  14.725  1.00 34.65 ? 163 THR A OG1 1 
ATOM   1270  C CG2 . THR A 1 167 ? -1.783  71.081  13.762  1.00 34.51 ? 163 THR A CG2 1 
ATOM   1271  N N   . ILE A 1 168 ? 1.008   69.672  15.210  1.00 34.52 ? 164 ILE A N   1 
ATOM   1272  C CA  . ILE A 1 168 ? 2.035   68.733  14.785  1.00 34.40 ? 164 ILE A CA  1 
ATOM   1273  C C   . ILE A 1 168 ? 1.735   68.236  13.372  1.00 34.56 ? 164 ILE A C   1 
ATOM   1274  O O   . ILE A 1 168 ? 0.601   67.881  13.064  1.00 34.66 ? 164 ILE A O   1 
ATOM   1275  C CB  . ILE A 1 168 ? 2.131   67.546  15.778  1.00 34.25 ? 164 ILE A CB  1 
ATOM   1276  C CG1 . ILE A 1 168 ? 2.659   68.050  17.123  1.00 34.03 ? 164 ILE A CG1 1 
ATOM   1277  C CG2 . ILE A 1 168 ? 3.004   66.413  15.216  1.00 33.73 ? 164 ILE A CG2 1 
ATOM   1278  C CD1 . ILE A 1 168 ? 2.480   67.103  18.280  1.00 34.43 ? 164 ILE A CD1 1 
ATOM   1279  N N   . LYS A 1 169 ? 2.751   68.239  12.518  1.00 34.68 ? 165 LYS A N   1 
ATOM   1280  C CA  . LYS A 1 169 ? 2.658   67.642  11.192  1.00 35.00 ? 165 LYS A CA  1 
ATOM   1281  C C   . LYS A 1 169 ? 3.899   66.797  10.956  1.00 35.40 ? 165 LYS A C   1 
ATOM   1282  O O   . LYS A 1 169 ? 4.969   67.312  10.616  1.00 35.45 ? 165 LYS A O   1 
ATOM   1283  C CB  . LYS A 1 169 ? 2.513   68.709  10.103  1.00 34.82 ? 165 LYS A CB  1 
ATOM   1284  C CG  . LYS A 1 169 ? 1.125   69.298  10.004  1.00 35.10 ? 165 LYS A CG  1 
ATOM   1285  C CD  . LYS A 1 169 ? 1.132   70.622  9.266   1.00 35.36 ? 165 LYS A CD  1 
ATOM   1286  C CE  . LYS A 1 169 ? -0.279  71.151  9.109   1.00 36.21 ? 165 LYS A CE  1 
ATOM   1287  N NZ  . LYS A 1 169 ? -0.281  72.591  8.746   1.00 37.31 ? 165 LYS A NZ  1 
ATOM   1288  N N   . ARG A 1 170 ? 3.748   65.496  11.169  1.00 35.91 ? 166 ARG A N   1 
ATOM   1289  C CA  . ARG A 1 170 ? 4.832   64.546  10.991  1.00 36.67 ? 166 ARG A CA  1 
ATOM   1290  C C   . ARG A 1 170 ? 4.354   63.409  10.114  1.00 36.88 ? 166 ARG A C   1 
ATOM   1291  O O   . ARG A 1 170 ? 3.168   63.054  10.124  1.00 36.92 ? 166 ARG A O   1 
ATOM   1292  C CB  . ARG A 1 170 ? 5.309   63.996  12.338  1.00 36.58 ? 166 ARG A CB  1 
ATOM   1293  C CG  . ARG A 1 170 ? 5.859   65.050  13.303  1.00 38.14 ? 166 ARG A CG  1 
ATOM   1294  C CD  . ARG A 1 170 ? 7.182   65.670  12.837  1.00 39.78 ? 166 ARG A CD  1 
ATOM   1295  N NE  . ARG A 1 170 ? 8.278   64.701  12.808  1.00 40.80 ? 166 ARG A NE  1 
ATOM   1296  C CZ  . ARG A 1 170 ? 9.046   64.393  13.849  1.00 41.53 ? 166 ARG A CZ  1 
ATOM   1297  N NH1 . ARG A 1 170 ? 8.855   64.973  15.028  1.00 42.11 ? 166 ARG A NH1 1 
ATOM   1298  N NH2 . ARG A 1 170 ? 10.015  63.498  13.709  1.00 42.46 ? 166 ARG A NH2 1 
ATOM   1299  N N   . SER A 1 171 ? 5.280   62.844  9.350   1.00 37.25 ? 167 SER A N   1 
ATOM   1300  C CA  . SER A 1 171 ? 4.965   61.719  8.491   1.00 37.66 ? 167 SER A CA  1 
ATOM   1301  C C   . SER A 1 171 ? 6.133   60.750  8.406   1.00 37.92 ? 167 SER A C   1 
ATOM   1302  O O   . SER A 1 171 ? 7.279   61.128  8.644   1.00 37.82 ? 167 SER A O   1 
ATOM   1303  C CB  . SER A 1 171 ? 4.552   62.202  7.097   1.00 37.72 ? 167 SER A CB  1 
ATOM   1304  O OG  . SER A 1 171 ? 5.615   62.865  6.441   1.00 37.99 ? 167 SER A OG  1 
ATOM   1305  N N   . TYR A 1 172 ? 5.832   59.497  8.079   1.00 38.46 ? 168 TYR A N   1 
ATOM   1306  C CA  . TYR A 1 172 ? 6.866   58.492  7.884   1.00 38.88 ? 168 TYR A CA  1 
ATOM   1307  C C   . TYR A 1 172 ? 6.552   57.568  6.711   1.00 39.46 ? 168 TYR A C   1 
ATOM   1308  O O   . TYR A 1 172 ? 5.484   56.955  6.658   1.00 39.74 ? 168 TYR A O   1 
ATOM   1309  C CB  . TYR A 1 172 ? 7.086   57.679  9.162   1.00 38.72 ? 168 TYR A CB  1 
ATOM   1310  C CG  . TYR A 1 172 ? 7.946   56.461  8.937   1.00 38.38 ? 168 TYR A CG  1 
ATOM   1311  C CD1 . TYR A 1 172 ? 9.335   56.567  8.878   1.00 38.04 ? 168 TYR A CD1 1 
ATOM   1312  C CD2 . TYR A 1 172 ? 7.372   55.207  8.761   1.00 37.49 ? 168 TYR A CD2 1 
ATOM   1313  C CE1 . TYR A 1 172 ? 10.127  55.448  8.653   1.00 38.25 ? 168 TYR A CE1 1 
ATOM   1314  C CE2 . TYR A 1 172 ? 8.149   54.094  8.532   1.00 37.56 ? 168 TYR A CE2 1 
ATOM   1315  C CZ  . TYR A 1 172 ? 9.524   54.216  8.482   1.00 37.89 ? 168 TYR A CZ  1 
ATOM   1316  O OH  . TYR A 1 172 ? 10.293  53.099  8.264   1.00 38.51 ? 168 TYR A OH  1 
ATOM   1317  N N   . ASN A 1 173 ? 7.503   57.478  5.785   1.00 40.03 ? 169 ASN A N   1 
ATOM   1318  C CA  . ASN A 1 173 ? 7.444   56.553  4.661   1.00 40.58 ? 169 ASN A CA  1 
ATOM   1319  C C   . ASN A 1 173 ? 8.105   55.245  5.074   1.00 40.50 ? 169 ASN A C   1 
ATOM   1320  O O   . ASN A 1 173 ? 9.242   55.248  5.547   1.00 40.66 ? 169 ASN A O   1 
ATOM   1321  C CB  . ASN A 1 173 ? 8.212   57.138  3.469   1.00 40.98 ? 169 ASN A CB  1 
ATOM   1322  C CG  . ASN A 1 173 ? 7.422   57.101  2.176   1.00 42.60 ? 169 ASN A CG  1 
ATOM   1323  O OD1 . ASN A 1 173 ? 7.704   56.311  1.266   1.00 46.21 ? 169 ASN A OD1 1 
ATOM   1324  N ND2 . ASN A 1 173 ? 6.435   57.981  2.077   1.00 44.28 ? 169 ASN A ND2 1 
ATOM   1325  N N   . ASN A 1 174 ? 7.402   54.129  4.906   1.00 40.48 ? 170 ASN A N   1 
ATOM   1326  C CA  . ASN A 1 174 ? 8.007   52.815  5.121   1.00 40.33 ? 170 ASN A CA  1 
ATOM   1327  C C   . ASN A 1 174 ? 8.795   52.361  3.892   1.00 40.23 ? 170 ASN A C   1 
ATOM   1328  O O   . ASN A 1 174 ? 8.220   51.834  2.945   1.00 40.25 ? 170 ASN A O   1 
ATOM   1329  C CB  . ASN A 1 174 ? 6.945   51.772  5.497   1.00 40.28 ? 170 ASN A CB  1 
ATOM   1330  C CG  . ASN A 1 174 ? 7.536   50.384  5.717   1.00 40.29 ? 170 ASN A CG  1 
ATOM   1331  O OD1 . ASN A 1 174 ? 8.743   50.232  5.893   1.00 40.74 ? 170 ASN A OD1 1 
ATOM   1332  N ND2 . ASN A 1 174 ? 6.684   49.369  5.707   1.00 40.03 ? 170 ASN A ND2 1 
ATOM   1333  N N   . THR A 1 175 ? 10.108  52.574  3.908   1.00 40.22 ? 171 THR A N   1 
ATOM   1334  C CA  . THR A 1 175 ? 10.971  52.132  2.803   1.00 40.32 ? 171 THR A CA  1 
ATOM   1335  C C   . THR A 1 175 ? 11.694  50.809  3.107   1.00 40.21 ? 171 THR A C   1 
ATOM   1336  O O   . THR A 1 175 ? 12.520  50.346  2.322   1.00 40.09 ? 171 THR A O   1 
ATOM   1337  C CB  . THR A 1 175 ? 11.976  53.228  2.348   1.00 40.29 ? 171 THR A CB  1 
ATOM   1338  O OG1 . THR A 1 175 ? 12.785  53.643  3.452   1.00 40.47 ? 171 THR A OG1 1 
ATOM   1339  C CG2 . THR A 1 175 ? 11.238  54.433  1.787   1.00 40.56 ? 171 THR A CG2 1 
ATOM   1340  N N   . ASN A 1 176 ? 11.362  50.205  4.246   1.00 40.29 ? 172 ASN A N   1 
ATOM   1341  C CA  . ASN A 1 176 ? 11.786  48.845  4.560   1.00 40.28 ? 172 ASN A CA  1 
ATOM   1342  C C   . ASN A 1 176 ? 11.086  47.856  3.628   1.00 40.44 ? 172 ASN A C   1 
ATOM   1343  O O   . ASN A 1 176 ? 10.100  48.201  2.969   1.00 40.58 ? 172 ASN A O   1 
ATOM   1344  C CB  . ASN A 1 176 ? 11.474  48.506  6.024   1.00 40.16 ? 172 ASN A CB  1 
ATOM   1345  C CG  . ASN A 1 176 ? 12.112  49.477  7.003   1.00 39.88 ? 172 ASN A CG  1 
ATOM   1346  O OD1 . ASN A 1 176 ? 13.325  49.466  7.207   1.00 40.07 ? 172 ASN A OD1 1 
ATOM   1347  N ND2 . ASN A 1 176 ? 11.291  50.313  7.627   1.00 39.80 ? 172 ASN A ND2 1 
ATOM   1348  N N   . GLN A 1 177 ? 11.598  46.633  3.571   1.00 40.71 ? 173 GLN A N   1 
ATOM   1349  C CA  . GLN A 1 177 ? 11.032  45.595  2.713   1.00 41.07 ? 173 GLN A CA  1 
ATOM   1350  C C   . GLN A 1 177 ? 9.830   44.913  3.375   1.00 40.83 ? 173 GLN A C   1 
ATOM   1351  O O   . GLN A 1 177 ? 9.023   44.273  2.697   1.00 40.83 ? 173 GLN A O   1 
ATOM   1352  C CB  . GLN A 1 177 ? 12.104  44.562  2.330   1.00 41.37 ? 173 GLN A CB  1 
ATOM   1353  C CG  . GLN A 1 177 ? 13.127  45.050  1.288   1.00 42.75 ? 173 GLN A CG  1 
ATOM   1354  C CD  . GLN A 1 177 ? 12.642  44.878  -0.156  1.00 45.42 ? 173 GLN A CD  1 
ATOM   1355  O OE1 . GLN A 1 177 ? 12.321  45.857  -0.843  1.00 46.36 ? 173 GLN A OE1 1 
ATOM   1356  N NE2 . GLN A 1 177 ? 12.584  43.627  -0.618  1.00 45.48 ? 173 GLN A NE2 1 
ATOM   1357  N N   . GLU A 1 178 ? 9.707   45.071  4.691   1.00 40.46 ? 174 GLU A N   1 
ATOM   1358  C CA  . GLU A 1 178 ? 8.670   44.384  5.467   1.00 40.10 ? 174 GLU A CA  1 
ATOM   1359  C C   . GLU A 1 178 ? 7.472   45.268  5.819   1.00 39.34 ? 174 GLU A C   1 
ATOM   1360  O O   . GLU A 1 178 ? 7.575   46.499  5.837   1.00 39.16 ? 174 GLU A O   1 
ATOM   1361  C CB  . GLU A 1 178 ? 9.261   43.799  6.754   1.00 40.35 ? 174 GLU A CB  1 
ATOM   1362  C CG  . GLU A 1 178 ? 10.235  42.636  6.552   1.00 42.06 ? 174 GLU A CG  1 
ATOM   1363  C CD  . GLU A 1 178 ? 11.690  43.082  6.408   1.00 44.15 ? 174 GLU A CD  1 
ATOM   1364  O OE1 . GLU A 1 178 ? 11.978  44.298  6.530   1.00 45.04 ? 174 GLU A OE1 1 
ATOM   1365  O OE2 . GLU A 1 178 ? 12.551  42.206  6.174   1.00 44.82 ? 174 GLU A OE2 1 
ATOM   1366  N N   . ASP A 1 179 ? 6.337   44.622  6.095   1.00 38.55 ? 175 ASP A N   1 
ATOM   1367  C CA  . ASP A 1 179 ? 5.181   45.289  6.700   1.00 37.58 ? 175 ASP A CA  1 
ATOM   1368  C C   . ASP A 1 179 ? 5.581   45.825  8.069   1.00 36.61 ? 175 ASP A C   1 
ATOM   1369  O O   . ASP A 1 179 ? 6.392   45.222  8.780   1.00 36.35 ? 175 ASP A O   1 
ATOM   1370  C CB  . ASP A 1 179 ? 3.999   44.328  6.872   1.00 37.81 ? 175 ASP A CB  1 
ATOM   1371  C CG  . ASP A 1 179 ? 3.334   43.947  5.552   1.00 39.02 ? 175 ASP A CG  1 
ATOM   1372  O OD1 . ASP A 1 179 ? 3.929   44.145  4.471   1.00 40.76 ? 175 ASP A OD1 1 
ATOM   1373  O OD2 . ASP A 1 179 ? 2.202   43.423  5.601   1.00 40.43 ? 175 ASP A OD2 1 
ATOM   1374  N N   . LEU A 1 180 ? 5.002   46.961  8.431   1.00 35.38 ? 176 LEU A N   1 
ATOM   1375  C CA  . LEU A 1 180 ? 5.325   47.606  9.682   1.00 34.31 ? 176 LEU A CA  1 
ATOM   1376  C C   . LEU A 1 180 ? 4.079   47.713  10.559  1.00 33.40 ? 176 LEU A C   1 
ATOM   1377  O O   . LEU A 1 180 ? 3.036   48.197  10.109  1.00 33.16 ? 176 LEU A O   1 
ATOM   1378  C CB  . LEU A 1 180 ? 5.895   48.994  9.392   1.00 34.45 ? 176 LEU A CB  1 
ATOM   1379  C CG  . LEU A 1 180 ? 6.956   49.610  10.296  1.00 34.24 ? 176 LEU A CG  1 
ATOM   1380  C CD1 . LEU A 1 180 ? 8.267   48.869  10.161  1.00 35.02 ? 176 LEU A CD1 1 
ATOM   1381  C CD2 . LEU A 1 180 ? 7.139   51.059  9.898   1.00 34.12 ? 176 LEU A CD2 1 
ATOM   1382  N N   . LEU A 1 181 ? 4.187   47.249  11.801  1.00 32.18 ? 177 LEU A N   1 
ATOM   1383  C CA  . LEU A 1 181 ? 3.142   47.491  12.789  1.00 31.21 ? 177 LEU A CA  1 
ATOM   1384  C C   . LEU A 1 181 ? 3.436   48.778  13.559  1.00 30.67 ? 177 LEU A C   1 
ATOM   1385  O O   . LEU A 1 181 ? 4.417   48.859  14.310  1.00 30.53 ? 177 LEU A O   1 
ATOM   1386  C CB  . LEU A 1 181 ? 2.986   46.304  13.741  1.00 31.16 ? 177 LEU A CB  1 
ATOM   1387  C CG  . LEU A 1 181 ? 2.012   46.490  14.905  1.00 30.73 ? 177 LEU A CG  1 
ATOM   1388  C CD1 . LEU A 1 181 ? 0.574   46.462  14.416  1.00 30.94 ? 177 LEU A CD1 1 
ATOM   1389  C CD2 . LEU A 1 181 ? 2.241   45.435  15.977  1.00 29.80 ? 177 LEU A CD2 1 
ATOM   1390  N N   . VAL A 1 182 ? 2.574   49.772  13.355  1.00 29.92 ? 178 VAL A N   1 
ATOM   1391  C CA  . VAL A 1 182 ? 2.720   51.106  13.932  1.00 29.12 ? 178 VAL A CA  1 
ATOM   1392  C C   . VAL A 1 182 ? 1.644   51.331  14.993  1.00 28.72 ? 178 VAL A C   1 
ATOM   1393  O O   . VAL A 1 182 ? 0.466   51.051  14.757  1.00 28.62 ? 178 VAL A O   1 
ATOM   1394  C CB  . VAL A 1 182 ? 2.616   52.195  12.840  1.00 28.98 ? 178 VAL A CB  1 
ATOM   1395  C CG1 . VAL A 1 182 ? 2.791   53.583  13.434  1.00 29.18 ? 178 VAL A CG1 1 
ATOM   1396  C CG2 . VAL A 1 182 ? 3.644   51.957  11.752  1.00 29.15 ? 178 VAL A CG2 1 
ATOM   1397  N N   . LEU A 1 183 ? 2.061   51.840  16.153  1.00 28.39 ? 179 LEU A N   1 
ATOM   1398  C CA  . LEU A 1 183 ? 1.172   52.060  17.298  1.00 27.92 ? 179 LEU A CA  1 
ATOM   1399  C C   . LEU A 1 183 ? 1.149   53.524  17.753  1.00 27.31 ? 179 LEU A C   1 
ATOM   1400  O O   . LEU A 1 183 ? 2.164   54.215  17.711  1.00 27.27 ? 179 LEU A O   1 
ATOM   1401  C CB  . LEU A 1 183 ? 1.593   51.167  18.468  1.00 28.12 ? 179 LEU A CB  1 
ATOM   1402  C CG  . LEU A 1 183 ? 1.685   49.654  18.233  1.00 28.45 ? 179 LEU A CG  1 
ATOM   1403  C CD1 . LEU A 1 183 ? 2.707   49.041  19.180  1.00 29.67 ? 179 LEU A CD1 1 
ATOM   1404  C CD2 . LEU A 1 183 ? 0.335   48.977  18.400  1.00 28.86 ? 179 LEU A CD2 1 
ATOM   1405  N N   . TRP A 1 184 ? -0.021  53.984  18.182  1.00 26.57 ? 180 TRP A N   1 
ATOM   1406  C CA  . TRP A 1 184 ? -0.196  55.340  18.700  1.00 25.87 ? 180 TRP A CA  1 
ATOM   1407  C C   . TRP A 1 184 ? -1.417  55.387  19.605  1.00 25.72 ? 180 TRP A C   1 
ATOM   1408  O O   . TRP A 1 184 ? -2.132  54.395  19.740  1.00 25.67 ? 180 TRP A O   1 
ATOM   1409  C CB  . TRP A 1 184 ? -0.326  56.366  17.570  1.00 25.83 ? 180 TRP A CB  1 
ATOM   1410  C CG  . TRP A 1 184 ? -1.600  56.255  16.766  1.00 25.25 ? 180 TRP A CG  1 
ATOM   1411  C CD1 . TRP A 1 184 ? -2.767  56.948  16.966  1.00 24.01 ? 180 TRP A CD1 1 
ATOM   1412  C CD2 . TRP A 1 184 ? -1.821  55.416  15.627  1.00 24.30 ? 180 TRP A CD2 1 
ATOM   1413  N NE1 . TRP A 1 184 ? -3.700  56.582  16.026  1.00 23.34 ? 180 TRP A NE1 1 
ATOM   1414  C CE2 . TRP A 1 184 ? -3.147  55.646  15.190  1.00 24.34 ? 180 TRP A CE2 1 
ATOM   1415  C CE3 . TRP A 1 184 ? -1.029  54.491  14.933  1.00 24.25 ? 180 TRP A CE3 1 
ATOM   1416  C CZ2 . TRP A 1 184 ? -3.703  54.979  14.087  1.00 23.67 ? 180 TRP A CZ2 1 
ATOM   1417  C CZ3 . TRP A 1 184 ? -1.586  53.825  13.830  1.00 25.24 ? 180 TRP A CZ3 1 
ATOM   1418  C CH2 . TRP A 1 184 ? -2.912  54.077  13.425  1.00 23.63 ? 180 TRP A CH2 1 
ATOM   1419  N N   . GLY A 1 185 ? -1.653  56.537  20.229  1.00 25.55 ? 181 GLY A N   1 
ATOM   1420  C CA  . GLY A 1 185 ? -2.736  56.653  21.188  1.00 25.15 ? 181 GLY A CA  1 
ATOM   1421  C C   . GLY A 1 185 ? -3.291  58.050  21.348  1.00 25.18 ? 181 GLY A C   1 
ATOM   1422  O O   . GLY A 1 185 ? -2.774  59.020  20.782  1.00 24.72 ? 181 GLY A O   1 
ATOM   1423  N N   . ILE A 1 186 ? -4.349  58.133  22.145  1.00 25.22 ? 182 ILE A N   1 
ATOM   1424  C CA  . ILE A 1 186 ? -4.990  59.387  22.490  1.00 25.68 ? 182 ILE A CA  1 
ATOM   1425  C C   . ILE A 1 186 ? -5.279  59.380  23.990  1.00 26.04 ? 182 ILE A C   1 
ATOM   1426  O O   . ILE A 1 186 ? -5.660  58.348  24.553  1.00 25.81 ? 182 ILE A O   1 
ATOM   1427  C CB  . ILE A 1 186 ? -6.303  59.601  21.676  1.00 25.71 ? 182 ILE A CB  1 
ATOM   1428  C CG1 . ILE A 1 186 ? -7.001  60.909  22.078  1.00 25.68 ? 182 ILE A CG1 1 
ATOM   1429  C CG2 . ILE A 1 186 ? -7.241  58.403  21.833  1.00 25.54 ? 182 ILE A CG2 1 
ATOM   1430  C CD1 . ILE A 1 186 ? -8.117  61.357  21.117  1.00 27.09 ? 182 ILE A CD1 1 
ATOM   1431  N N   . HIS A 1 187 ? -5.091  60.528  24.632  1.00 26.44 ? 183 HIS A N   1 
ATOM   1432  C CA  . HIS A 1 187 ? -5.400  60.657  26.045  1.00 27.26 ? 183 HIS A CA  1 
ATOM   1433  C C   . HIS A 1 187 ? -6.751  61.342  26.247  1.00 27.88 ? 183 HIS A C   1 
ATOM   1434  O O   . HIS A 1 187 ? -6.998  62.406  25.685  1.00 27.70 ? 183 HIS A O   1 
ATOM   1435  C CB  . HIS A 1 187 ? -4.286  61.427  26.764  1.00 27.26 ? 183 HIS A CB  1 
ATOM   1436  C CG  . HIS A 1 187 ? -4.555  61.667  28.214  1.00 26.75 ? 183 HIS A CG  1 
ATOM   1437  N ND1 . HIS A 1 187 ? -4.627  62.930  28.756  1.00 27.19 ? 183 HIS A ND1 1 
ATOM   1438  C CD2 . HIS A 1 187 ? -4.776  60.806  29.234  1.00 27.02 ? 183 HIS A CD2 1 
ATOM   1439  C CE1 . HIS A 1 187 ? -4.871  62.838  30.051  1.00 27.38 ? 183 HIS A CE1 1 
ATOM   1440  N NE2 . HIS A 1 187 ? -4.965  61.559  30.367  1.00 27.46 ? 183 HIS A NE2 1 
ATOM   1441  N N   . HIS A 1 188 ? -7.617  60.702  27.033  1.00 28.81 ? 184 HIS A N   1 
ATOM   1442  C CA  . HIS A 1 188 ? -8.873  61.293  27.478  1.00 29.90 ? 184 HIS A CA  1 
ATOM   1443  C C   . HIS A 1 188 ? -8.711  61.806  28.916  1.00 30.84 ? 184 HIS A C   1 
ATOM   1444  O O   . HIS A 1 188 ? -8.616  61.009  29.860  1.00 30.66 ? 184 HIS A O   1 
ATOM   1445  C CB  . HIS A 1 188 ? -10.023 60.279  27.428  1.00 29.77 ? 184 HIS A CB  1 
ATOM   1446  C CG  . HIS A 1 188 ? -10.160 59.567  26.117  1.00 30.34 ? 184 HIS A CG  1 
ATOM   1447  N ND1 . HIS A 1 188 ? -10.649 60.179  24.983  1.00 29.76 ? 184 HIS A ND1 1 
ATOM   1448  C CD2 . HIS A 1 188 ? -9.891  58.286  25.767  1.00 30.16 ? 184 HIS A CD2 1 
ATOM   1449  C CE1 . HIS A 1 188 ? -10.665 59.310  23.989  1.00 29.87 ? 184 HIS A CE1 1 
ATOM   1450  N NE2 . HIS A 1 188 ? -10.209 58.155  24.438  1.00 30.47 ? 184 HIS A NE2 1 
ATOM   1451  N N   . PRO A 1 189 ? -8.679  63.141  29.091  1.00 31.78 ? 185 PRO A N   1 
ATOM   1452  C CA  . PRO A 1 189 ? -8.578  63.733  30.428  1.00 32.56 ? 185 PRO A CA  1 
ATOM   1453  C C   . PRO A 1 189 ? -9.901  63.619  31.184  1.00 33.62 ? 185 PRO A C   1 
ATOM   1454  O O   . PRO A 1 189 ? -10.919 63.245  30.593  1.00 33.68 ? 185 PRO A O   1 
ATOM   1455  C CB  . PRO A 1 189 ? -8.253  65.204  30.143  1.00 32.62 ? 185 PRO A CB  1 
ATOM   1456  C CG  . PRO A 1 189 ? -8.005  65.295  28.649  1.00 31.99 ? 185 PRO A CG  1 
ATOM   1457  C CD  . PRO A 1 189 ? -8.752  64.169  28.042  1.00 31.60 ? 185 PRO A CD  1 
ATOM   1458  N N   . ASN A 1 190 ? -9.893  63.933  32.479  1.00 34.78 ? 186 ASN A N   1 
ATOM   1459  C CA  . ASN A 1 190 ? -11.117 63.843  33.281  1.00 35.87 ? 186 ASN A CA  1 
ATOM   1460  C C   . ASN A 1 190 ? -11.948 65.127  33.372  1.00 36.20 ? 186 ASN A C   1 
ATOM   1461  O O   . ASN A 1 190 ? -13.115 65.076  33.761  1.00 36.39 ? 186 ASN A O   1 
ATOM   1462  C CB  . ASN A 1 190 ? -10.839 63.256  34.672  1.00 36.14 ? 186 ASN A CB  1 
ATOM   1463  C CG  . ASN A 1 190 ? -9.701  63.958  35.390  1.00 37.47 ? 186 ASN A CG  1 
ATOM   1464  O OD1 . ASN A 1 190 ? -8.654  63.356  35.643  1.00 38.99 ? 186 ASN A OD1 1 
ATOM   1465  N ND2 . ASN A 1 190 ? -9.898  65.233  35.726  1.00 38.03 ? 186 ASN A ND2 1 
ATOM   1466  N N   . ASP A 1 191 ? -11.351 66.267  33.022  1.00 36.76 ? 187 ASP A N   1 
ATOM   1467  C CA  . ASP A 1 191 ? -12.080 67.543  32.960  1.00 37.43 ? 187 ASP A CA  1 
ATOM   1468  C C   . ASP A 1 191 ? -11.415 68.572  32.047  1.00 37.78 ? 187 ASP A C   1 
ATOM   1469  O O   . ASP A 1 191 ? -10.298 68.365  31.574  1.00 37.89 ? 187 ASP A O   1 
ATOM   1470  C CB  . ASP A 1 191 ? -12.356 68.133  34.358  1.00 37.57 ? 187 ASP A CB  1 
ATOM   1471  C CG  . ASP A 1 191 ? -11.102 68.258  35.215  1.00 38.45 ? 187 ASP A CG  1 
ATOM   1472  O OD1 . ASP A 1 191 ? -10.094 68.833  34.749  1.00 39.11 ? 187 ASP A OD1 1 
ATOM   1473  O OD2 . ASP A 1 191 ? -11.135 67.784  36.372  1.00 39.24 ? 187 ASP A OD2 1 
ATOM   1474  N N   . ALA A 1 192 ? -12.123 69.673  31.805  1.00 38.36 ? 188 ALA A N   1 
ATOM   1475  C CA  . ALA A 1 192 ? -11.674 70.742  30.914  1.00 38.78 ? 188 ALA A CA  1 
ATOM   1476  C C   . ALA A 1 192 ? -10.461 71.490  31.462  1.00 39.25 ? 188 ALA A C   1 
ATOM   1477  O O   . ALA A 1 192 ? -9.692  72.084  30.698  1.00 39.37 ? 188 ALA A O   1 
ATOM   1478  C CB  . ALA A 1 192 ? -12.816 71.710  30.653  1.00 38.88 ? 188 ALA A CB  1 
ATOM   1479  N N   . ALA A 1 193 ? -10.308 71.465  32.786  1.00 39.62 ? 189 ALA A N   1 
ATOM   1480  C CA  . ALA A 1 193 ? -9.154  72.049  33.461  1.00 39.89 ? 189 ALA A CA  1 
ATOM   1481  C C   . ALA A 1 193 ? -7.879  71.284  33.120  1.00 40.07 ? 189 ALA A C   1 
ATOM   1482  O O   . ALA A 1 193 ? -6.856  71.882  32.771  1.00 40.35 ? 189 ALA A O   1 
ATOM   1483  C CB  . ALA A 1 193 ? -9.381  72.059  34.966  1.00 40.04 ? 189 ALA A CB  1 
ATOM   1484  N N   . GLU A 1 194 ? -7.958  69.959  33.221  1.00 40.26 ? 190 GLU A N   1 
ATOM   1485  C CA  . GLU A 1 194 ? -6.850  69.052  32.911  1.00 40.45 ? 190 GLU A CA  1 
ATOM   1486  C C   . GLU A 1 194 ? -6.438  69.149  31.439  1.00 40.26 ? 190 GLU A C   1 
ATOM   1487  O O   . GLU A 1 194 ? -5.249  69.040  31.112  1.00 40.31 ? 190 GLU A O   1 
ATOM   1488  C CB  . GLU A 1 194 ? -7.251  67.619  33.276  1.00 40.70 ? 190 GLU A CB  1 
ATOM   1489  C CG  . GLU A 1 194 ? -6.182  66.558  33.081  1.00 42.25 ? 190 GLU A CG  1 
ATOM   1490  C CD  . GLU A 1 194 ? -6.548  65.240  33.745  1.00 44.77 ? 190 GLU A CD  1 
ATOM   1491  O OE1 . GLU A 1 194 ? -6.853  65.251  34.959  1.00 46.02 ? 190 GLU A OE1 1 
ATOM   1492  O OE2 . GLU A 1 194 ? -6.522  64.189  33.064  1.00 46.34 ? 190 GLU A OE2 1 
ATOM   1493  N N   . GLN A 1 195 ? -7.424  69.361  30.565  1.00 40.06 ? 191 GLN A N   1 
ATOM   1494  C CA  . GLN A 1 195 ? -7.184  69.562  29.131  1.00 39.88 ? 191 GLN A CA  1 
ATOM   1495  C C   . GLN A 1 195 ? -6.250  70.745  28.865  1.00 39.97 ? 191 GLN A C   1 
ATOM   1496  O O   . GLN A 1 195 ? -5.308  70.620  28.085  1.00 39.74 ? 191 GLN A O   1 
ATOM   1497  C CB  . GLN A 1 195 ? -8.516  69.735  28.381  1.00 39.80 ? 191 GLN A CB  1 
ATOM   1498  C CG  . GLN A 1 195 ? -8.400  70.042  26.879  1.00 39.01 ? 191 GLN A CG  1 
ATOM   1499  C CD  . GLN A 1 195 ? -7.770  68.912  26.079  1.00 38.40 ? 191 GLN A CD  1 
ATOM   1500  O OE1 . GLN A 1 195 ? -8.078  67.737  26.288  1.00 38.54 ? 191 GLN A OE1 1 
ATOM   1501  N NE2 . GLN A 1 195 ? -6.887  69.266  25.150  1.00 37.40 ? 191 GLN A NE2 1 
ATOM   1502  N N   . THR A 1 196 ? -6.516  71.875  29.526  1.00 40.33 ? 192 THR A N   1 
ATOM   1503  C CA  . THR A 1 196 ? -5.741  73.116  29.356  1.00 40.67 ? 192 THR A CA  1 
ATOM   1504  C C   . THR A 1 196 ? -4.343  73.006  29.961  1.00 40.61 ? 192 THR A C   1 
ATOM   1505  O O   . THR A 1 196 ? -3.366  73.501  29.393  1.00 40.56 ? 192 THR A O   1 
ATOM   1506  C CB  . THR A 1 196 ? -6.446  74.320  30.025  1.00 40.84 ? 192 THR A CB  1 
ATOM   1507  O OG1 . THR A 1 196 ? -7.866  74.153  29.962  1.00 41.77 ? 192 THR A OG1 1 
ATOM   1508  C CG2 . THR A 1 196 ? -6.060  75.632  29.346  1.00 41.09 ? 192 THR A CG2 1 
ATOM   1509  N N   . LYS A 1 197 ? -4.264  72.358  31.121  1.00 40.61 ? 193 LYS A N   1 
ATOM   1510  C CA  . LYS A 1 197 ? -3.014  72.200  31.858  1.00 40.66 ? 193 LYS A CA  1 
ATOM   1511  C C   . LYS A 1 197 ? -2.028  71.306  31.103  1.00 40.39 ? 193 LYS A C   1 
ATOM   1512  O O   . LYS A 1 197 ? -0.815  71.521  31.153  1.00 40.75 ? 193 LYS A O   1 
ATOM   1513  C CB  . LYS A 1 197 ? -3.314  71.653  33.264  1.00 40.89 ? 193 LYS A CB  1 
ATOM   1514  C CG  . LYS A 1 197 ? -2.132  71.051  34.024  1.00 41.80 ? 193 LYS A CG  1 
ATOM   1515  C CD  . LYS A 1 197 ? -2.605  70.414  35.333  1.00 43.44 ? 193 LYS A CD  1 
ATOM   1516  C CE  . LYS A 1 197 ? -2.066  68.993  35.516  1.00 44.54 ? 193 LYS A CE  1 
ATOM   1517  N NZ  . LYS A 1 197 ? -0.575  68.924  35.595  1.00 45.29 ? 193 LYS A NZ  1 
ATOM   1518  N N   . LEU A 1 198 ? -2.553  70.311  30.396  1.00 39.88 ? 194 LEU A N   1 
ATOM   1519  C CA  . LEU A 1 198 ? -1.711  69.381  29.648  1.00 39.17 ? 194 LEU A CA  1 
ATOM   1520  C C   . LEU A 1 198 ? -1.431  69.822  28.212  1.00 38.59 ? 194 LEU A C   1 
ATOM   1521  O O   . LEU A 1 198 ? -0.337  69.588  27.697  1.00 38.39 ? 194 LEU A O   1 
ATOM   1522  C CB  . LEU A 1 198 ? -2.318  67.974  29.674  1.00 39.22 ? 194 LEU A CB  1 
ATOM   1523  C CG  . LEU A 1 198 ? -1.810  66.920  30.678  1.00 39.44 ? 194 LEU A CG  1 
ATOM   1524  C CD1 . LEU A 1 198 ? -1.373  67.489  32.041  1.00 38.84 ? 194 LEU A CD1 1 
ATOM   1525  C CD2 . LEU A 1 198 ? -2.867  65.836  30.862  1.00 39.48 ? 194 LEU A CD2 1 
ATOM   1526  N N   . TYR A 1 199 ? -2.407  70.467  27.573  1.00 38.03 ? 195 TYR A N   1 
ATOM   1527  C CA  . TYR A 1 199 ? -2.324  70.729  26.129  1.00 37.56 ? 195 TYR A CA  1 
ATOM   1528  C C   . TYR A 1 199 ? -2.646  72.159  25.670  1.00 37.90 ? 195 TYR A C   1 
ATOM   1529  O O   . TYR A 1 199 ? -2.458  72.468  24.491  1.00 38.13 ? 195 TYR A O   1 
ATOM   1530  C CB  . TYR A 1 199 ? -3.186  69.717  25.348  1.00 37.04 ? 195 TYR A CB  1 
ATOM   1531  C CG  . TYR A 1 199 ? -3.089  68.300  25.869  1.00 34.88 ? 195 TYR A CG  1 
ATOM   1532  C CD1 . TYR A 1 199 ? -1.922  67.557  25.707  1.00 33.81 ? 195 TYR A CD1 1 
ATOM   1533  C CD2 . TYR A 1 199 ? -4.159  67.709  26.533  1.00 32.83 ? 195 TYR A CD2 1 
ATOM   1534  C CE1 . TYR A 1 199 ? -1.821  66.263  26.194  1.00 32.84 ? 195 TYR A CE1 1 
ATOM   1535  C CE2 . TYR A 1 199 ? -4.071  66.414  27.014  1.00 32.40 ? 195 TYR A CE2 1 
ATOM   1536  C CZ  . TYR A 1 199 ? -2.897  65.699  26.843  1.00 32.22 ? 195 TYR A CZ  1 
ATOM   1537  O OH  . TYR A 1 199 ? -2.793  64.418  27.319  1.00 31.63 ? 195 TYR A OH  1 
ATOM   1538  N N   . GLN A 1 200 ? -3.130  73.012  26.580  1.00 37.93 ? 196 GLN A N   1 
ATOM   1539  C CA  . GLN A 1 200 ? -3.451  74.428  26.283  1.00 38.06 ? 196 GLN A CA  1 
ATOM   1540  C C   . GLN A 1 200 ? -4.720  74.624  25.445  1.00 37.90 ? 196 GLN A C   1 
ATOM   1541  O O   . GLN A 1 200 ? -5.659  75.293  25.878  1.00 37.82 ? 196 GLN A O   1 
ATOM   1542  C CB  . GLN A 1 200 ? -2.261  75.161  25.633  1.00 38.24 ? 196 GLN A CB  1 
ATOM   1543  C CG  . GLN A 1 200 ? -2.504  76.650  25.343  1.00 38.81 ? 196 GLN A CG  1 
ATOM   1544  C CD  . GLN A 1 200 ? -2.445  77.515  26.598  1.00 40.24 ? 196 GLN A CD  1 
ATOM   1545  O OE1 . GLN A 1 200 ? -3.419  78.182  26.956  1.00 40.58 ? 196 GLN A OE1 1 
ATOM   1546  N NE2 . GLN A 1 200 ? -1.303  77.494  27.276  1.00 40.29 ? 196 GLN A NE2 1 
ATOM   1547  N N   . ASN A 1 201 ? -4.734  74.044  24.246  1.00 37.82 ? 197 ASN A N   1 
ATOM   1548  C CA  . ASN A 1 201 ? -5.887  74.126  23.343  1.00 37.63 ? 197 ASN A CA  1 
ATOM   1549  C C   . ASN A 1 201 ? -7.121  73.425  23.928  1.00 37.41 ? 197 ASN A C   1 
ATOM   1550  O O   . ASN A 1 201 ? -7.014  72.308  24.433  1.00 37.61 ? 197 ASN A O   1 
ATOM   1551  C CB  . ASN A 1 201 ? -5.525  73.549  21.969  1.00 37.44 ? 197 ASN A CB  1 
ATOM   1552  C CG  . ASN A 1 201 ? -4.203  74.092  21.432  1.00 37.31 ? 197 ASN A CG  1 
ATOM   1553  O OD1 . ASN A 1 201 ? -3.909  75.284  21.550  1.00 36.92 ? 197 ASN A OD1 1 
ATOM   1554  N ND2 . ASN A 1 201 ? -3.400  73.215  20.839  1.00 37.00 ? 197 ASN A ND2 1 
ATOM   1555  N N   . PRO A 1 202 ? -8.292  74.089  23.884  1.00 37.19 ? 198 PRO A N   1 
ATOM   1556  C CA  . PRO A 1 202 ? -9.491  73.483  24.478  1.00 36.94 ? 198 PRO A CA  1 
ATOM   1557  C C   . PRO A 1 202 ? -10.153 72.416  23.600  1.00 36.68 ? 198 PRO A C   1 
ATOM   1558  O O   . PRO A 1 202 ? -10.715 71.455  24.127  1.00 36.68 ? 198 PRO A O   1 
ATOM   1559  C CB  . PRO A 1 202 ? -10.430 74.677  24.672  1.00 36.99 ? 198 PRO A CB  1 
ATOM   1560  C CG  . PRO A 1 202 ? -10.006 75.672  23.643  1.00 37.01 ? 198 PRO A CG  1 
ATOM   1561  C CD  . PRO A 1 202 ? -8.551  75.442  23.350  1.00 37.06 ? 198 PRO A CD  1 
ATOM   1562  N N   . THR A 1 203 ? -10.082 72.590  22.280  1.00 36.26 ? 199 THR A N   1 
ATOM   1563  C CA  . THR A 1 203 ? -10.744 71.697  21.326  1.00 35.82 ? 199 THR A CA  1 
ATOM   1564  C C   . THR A 1 203 ? -9.708  71.036  20.412  1.00 35.20 ? 199 THR A C   1 
ATOM   1565  O O   . THR A 1 203 ? -9.077  71.697  19.589  1.00 35.41 ? 199 THR A O   1 
ATOM   1566  C CB  . THR A 1 203 ? -11.833 72.466  20.539  1.00 35.99 ? 199 THR A CB  1 
ATOM   1567  O OG1 . THR A 1 203 ? -12.941 72.716  21.414  1.00 36.59 ? 199 THR A OG1 1 
ATOM   1568  C CG2 . THR A 1 203 ? -12.326 71.684  19.335  1.00 36.13 ? 199 THR A CG2 1 
ATOM   1569  N N   . THR A 1 204 ? -9.517  69.730  20.580  1.00 34.41 ? 200 THR A N   1 
ATOM   1570  C CA  . THR A 1 204 ? -8.389  69.049  19.936  1.00 33.62 ? 200 THR A CA  1 
ATOM   1571  C C   . THR A 1 204 ? -8.785  67.834  19.103  1.00 33.09 ? 200 THR A C   1 
ATOM   1572  O O   . THR A 1 204 ? -9.899  67.324  19.213  1.00 32.96 ? 200 THR A O   1 
ATOM   1573  C CB  . THR A 1 204 ? -7.286  68.626  20.960  1.00 33.41 ? 200 THR A CB  1 
ATOM   1574  O OG1 . THR A 1 204 ? -7.804  67.645  21.866  1.00 33.09 ? 200 THR A OG1 1 
ATOM   1575  C CG2 . THR A 1 204 ? -6.773  69.825  21.742  1.00 33.39 ? 200 THR A CG2 1 
ATOM   1576  N N   . TYR A 1 205 ? -7.840  67.382  18.282  1.00 32.49 ? 201 TYR A N   1 
ATOM   1577  C CA  . TYR A 1 205 ? -8.004  66.197  17.452  1.00 32.05 ? 201 TYR A CA  1 
ATOM   1578  C C   . TYR A 1 205 ? -6.644  65.542  17.196  1.00 31.71 ? 201 TYR A C   1 
ATOM   1579  O O   . TYR A 1 205 ? -5.602  66.187  17.321  1.00 31.57 ? 201 TYR A O   1 
ATOM   1580  C CB  . TYR A 1 205 ? -8.653  66.579  16.110  1.00 31.97 ? 201 TYR A CB  1 
ATOM   1581  C CG  . TYR A 1 205 ? -7.780  67.478  15.253  1.00 31.69 ? 201 TYR A CG  1 
ATOM   1582  C CD1 . TYR A 1 205 ? -6.930  66.943  14.282  1.00 31.25 ? 201 TYR A CD1 1 
ATOM   1583  C CD2 . TYR A 1 205 ? -7.793  68.864  15.426  1.00 32.05 ? 201 TYR A CD2 1 
ATOM   1584  C CE1 . TYR A 1 205 ? -6.121  67.764  13.500  1.00 32.00 ? 201 TYR A CE1 1 
ATOM   1585  C CE2 . TYR A 1 205 ? -6.985  69.697  14.654  1.00 32.50 ? 201 TYR A CE2 1 
ATOM   1586  C CZ  . TYR A 1 205 ? -6.154  69.140  13.691  1.00 32.90 ? 201 TYR A CZ  1 
ATOM   1587  O OH  . TYR A 1 205 ? -5.356  69.962  12.929  1.00 33.67 ? 201 TYR A OH  1 
ATOM   1588  N N   . ILE A 1 206 ? -6.669  64.258  16.845  1.00 31.29 ? 202 ILE A N   1 
ATOM   1589  C CA  . ILE A 1 206 ? -5.538  63.590  16.211  1.00 30.90 ? 202 ILE A CA  1 
ATOM   1590  C C   . ILE A 1 206 ? -6.061  63.022  14.900  1.00 30.80 ? 202 ILE A C   1 
ATOM   1591  O O   . ILE A 1 206 ? -7.066  62.318  14.892  1.00 30.62 ? 202 ILE A O   1 
ATOM   1592  C CB  . ILE A 1 206 ? -4.972  62.418  17.062  1.00 30.77 ? 202 ILE A CB  1 
ATOM   1593  C CG1 . ILE A 1 206 ? -4.293  62.923  18.332  1.00 30.82 ? 202 ILE A CG1 1 
ATOM   1594  C CG2 . ILE A 1 206 ? -3.956  61.609  16.271  1.00 30.83 ? 202 ILE A CG2 1 
ATOM   1595  C CD1 . ILE A 1 206 ? -5.120  62.779  19.569  1.00 31.76 ? 202 ILE A CD1 1 
ATOM   1596  N N   . SER A 1 207 ? -5.393  63.332  13.795  1.00 30.72 ? 203 SER A N   1 
ATOM   1597  C CA  . SER A 1 207 ? -5.750  62.729  12.516  1.00 30.85 ? 203 SER A CA  1 
ATOM   1598  C C   . SER A 1 207 ? -4.617  61.852  11.989  1.00 31.08 ? 203 SER A C   1 
ATOM   1599  O O   . SER A 1 207 ? -3.441  62.193  12.124  1.00 30.97 ? 203 SER A O   1 
ATOM   1600  C CB  . SER A 1 207 ? -6.154  63.791  11.486  1.00 30.58 ? 203 SER A CB  1 
ATOM   1601  O OG  . SER A 1 207 ? -5.031  64.476  10.967  1.00 30.50 ? 203 SER A OG  1 
ATOM   1602  N N   . VAL A 1 208 ? -4.989  60.719  11.401  1.00 31.17 ? 204 VAL A N   1 
ATOM   1603  C CA  . VAL A 1 208 ? -4.033  59.781  10.829  1.00 31.37 ? 204 VAL A CA  1 
ATOM   1604  C C   . VAL A 1 208 ? -4.535  59.297  9.474   1.00 31.59 ? 204 VAL A C   1 
ATOM   1605  O O   . VAL A 1 208 ? -5.691  58.881  9.346   1.00 31.72 ? 204 VAL A O   1 
ATOM   1606  C CB  . VAL A 1 208 ? -3.829  58.539  11.724  1.00 31.37 ? 204 VAL A CB  1 
ATOM   1607  C CG1 . VAL A 1 208 ? -2.610  57.750  11.265  1.00 31.18 ? 204 VAL A CG1 1 
ATOM   1608  C CG2 . VAL A 1 208 ? -3.687  58.930  13.202  1.00 31.72 ? 204 VAL A CG2 1 
ATOM   1609  N N   . GLY A 1 209 ? -3.663  59.340  8.471   1.00 31.60 ? 205 GLY A N   1 
ATOM   1610  C CA  . GLY A 1 209 ? -4.010  58.868  7.141   1.00 31.82 ? 205 GLY A CA  1 
ATOM   1611  C C   . GLY A 1 209 ? -2.883  58.134  6.448   1.00 32.02 ? 205 GLY A C   1 
ATOM   1612  O O   . GLY A 1 209 ? -1.790  58.678  6.290   1.00 32.48 ? 205 GLY A O   1 
ATOM   1613  N N   . THR A 1 210 ? -3.147  56.886  6.063   1.00 31.96 ? 206 THR A N   1 
ATOM   1614  C CA  . THR A 1 210 ? -2.298  56.154  5.128   1.00 31.93 ? 206 THR A CA  1 
ATOM   1615  C C   . THR A 1 210 ? -3.063  56.036  3.803   1.00 32.10 ? 206 THR A C   1 
ATOM   1616  O O   . THR A 1 210 ? -4.095  56.690  3.616   1.00 31.97 ? 206 THR A O   1 
ATOM   1617  C CB  . THR A 1 210 ? -1.916  54.749  5.652   1.00 31.96 ? 206 THR A CB  1 
ATOM   1618  O OG1 . THR A 1 210 ? -3.063  53.890  5.631   1.00 31.81 ? 206 THR A OG1 1 
ATOM   1619  C CG2 . THR A 1 210 ? -1.360  54.822  7.065   1.00 32.02 ? 206 THR A CG2 1 
ATOM   1620  N N   . SER A 1 211 ? -2.575  55.214  2.879   1.00 32.24 ? 207 SER A N   1 
ATOM   1621  C CA  . SER A 1 211 ? -3.290  55.051  1.615   1.00 32.46 ? 207 SER A CA  1 
ATOM   1622  C C   . SER A 1 211 ? -4.588  54.252  1.790   1.00 32.26 ? 207 SER A C   1 
ATOM   1623  O O   . SER A 1 211 ? -5.499  54.372  0.973   1.00 32.46 ? 207 SER A O   1 
ATOM   1624  C CB  . SER A 1 211 ? -2.393  54.481  0.510   1.00 32.40 ? 207 SER A CB  1 
ATOM   1625  O OG  . SER A 1 211 ? -2.218  53.087  0.652   1.00 33.59 ? 207 SER A OG  1 
ATOM   1626  N N   . THR A 1 212 ? -4.682  53.472  2.870   1.00 32.04 ? 208 THR A N   1 
ATOM   1627  C CA  . THR A 1 212 ? -5.926  52.758  3.203   1.00 31.79 ? 208 THR A CA  1 
ATOM   1628  C C   . THR A 1 212 ? -6.658  53.285  4.452   1.00 31.61 ? 208 THR A C   1 
ATOM   1629  O O   . THR A 1 212 ? -7.886  53.179  4.543   1.00 31.81 ? 208 THR A O   1 
ATOM   1630  C CB  . THR A 1 212 ? -5.711  51.221  3.333   1.00 31.93 ? 208 THR A CB  1 
ATOM   1631  O OG1 . THR A 1 212 ? -4.680  50.948  4.290   1.00 32.08 ? 208 THR A OG1 1 
ATOM   1632  C CG2 . THR A 1 212 ? -5.334  50.603  1.987   1.00 31.58 ? 208 THR A CG2 1 
ATOM   1633  N N   . LEU A 1 213 ? -5.915  53.854  5.402   1.00 31.12 ? 209 LEU A N   1 
ATOM   1634  C CA  . LEU A 1 213 ? -6.494  54.317  6.671   1.00 30.39 ? 209 LEU A CA  1 
ATOM   1635  C C   . LEU A 1 213 ? -6.926  55.789  6.650   1.00 30.22 ? 209 LEU A C   1 
ATOM   1636  O O   . LEU A 1 213 ? -6.222  56.654  6.113   1.00 29.76 ? 209 LEU A O   1 
ATOM   1637  C CB  . LEU A 1 213 ? -5.527  54.048  7.841   1.00 30.27 ? 209 LEU A CB  1 
ATOM   1638  C CG  . LEU A 1 213 ? -5.909  54.440  9.282   1.00 29.78 ? 209 LEU A CG  1 
ATOM   1639  C CD1 . LEU A 1 213 ? -7.073  53.617  9.826   1.00 28.20 ? 209 LEU A CD1 1 
ATOM   1640  C CD2 . LEU A 1 213 ? -4.708  54.329  10.221  1.00 29.42 ? 209 LEU A CD2 1 
ATOM   1641  N N   . ASN A 1 214 ? -8.093  56.052  7.238   1.00 30.14 ? 210 ASN A N   1 
ATOM   1642  C CA  . ASN A 1 214 ? -8.604  57.412  7.417   1.00 30.44 ? 210 ASN A CA  1 
ATOM   1643  C C   . ASN A 1 214 ? -9.260  57.558  8.783   1.00 30.69 ? 210 ASN A C   1 
ATOM   1644  O O   . ASN A 1 214 ? -10.353 57.033  9.005   1.00 30.76 ? 210 ASN A O   1 
ATOM   1645  C CB  . ASN A 1 214 ? -9.606  57.779  6.313   1.00 30.37 ? 210 ASN A CB  1 
ATOM   1646  C CG  . ASN A 1 214 ? -10.044 59.241  6.371   1.00 30.53 ? 210 ASN A CG  1 
ATOM   1647  O OD1 . ASN A 1 214 ? -9.224  60.146  6.509   1.00 30.60 ? 210 ASN A OD1 1 
ATOM   1648  N ND2 . ASN A 1 214 ? -11.345 59.472  6.253   1.00 31.13 ? 210 ASN A ND2 1 
ATOM   1649  N N   . GLN A 1 215 ? -8.588  58.244  9.705   1.00 30.92 ? 211 GLN A N   1 
ATOM   1650  C CA  . GLN A 1 215 ? -9.192  58.509  11.009  1.00 31.46 ? 211 GLN A CA  1 
ATOM   1651  C C   . GLN A 1 215 ? -8.889  59.886  11.583  1.00 31.38 ? 211 GLN A C   1 
ATOM   1652  O O   . GLN A 1 215 ? -7.813  60.449  11.377  1.00 31.64 ? 211 GLN A O   1 
ATOM   1653  C CB  . GLN A 1 215 ? -8.885  57.390  12.026  1.00 31.47 ? 211 GLN A CB  1 
ATOM   1654  C CG  . GLN A 1 215 ? -7.551  57.488  12.750  1.00 32.63 ? 211 GLN A CG  1 
ATOM   1655  C CD  . GLN A 1 215 ? -7.365  56.425  13.844  1.00 34.27 ? 211 GLN A CD  1 
ATOM   1656  O OE1 . GLN A 1 215 ? -6.540  56.596  14.739  1.00 35.22 ? 211 GLN A OE1 1 
ATOM   1657  N NE2 . GLN A 1 215 ? -8.122  55.332  13.770  1.00 33.37 ? 211 GLN A NE2 1 
ATOM   1658  N N   . ARG A 1 216 ? -9.875  60.432  12.280  1.00 31.45 ? 212 ARG A N   1 
ATOM   1659  C CA  . ARG A 1 216 ? -9.689  61.627  13.072  1.00 31.65 ? 212 ARG A CA  1 
ATOM   1660  C C   . ARG A 1 216 ? -10.286 61.367  14.441  1.00 31.68 ? 212 ARG A C   1 
ATOM   1661  O O   . ARG A 1 216 ? -11.497 61.195  14.580  1.00 31.50 ? 212 ARG A O   1 
ATOM   1662  C CB  . ARG A 1 216 ? -10.352 62.826  12.411  1.00 31.68 ? 212 ARG A CB  1 
ATOM   1663  C CG  . ARG A 1 216 ? -9.929  64.173  12.976  1.00 32.06 ? 212 ARG A CG  1 
ATOM   1664  C CD  . ARG A 1 216 ? -10.561 65.258  12.143  1.00 32.50 ? 212 ARG A CD  1 
ATOM   1665  N NE  . ARG A 1 216 ? -10.305 66.617  12.611  1.00 33.49 ? 212 ARG A NE  1 
ATOM   1666  C CZ  . ARG A 1 216 ? -9.497  67.483  12.001  1.00 34.15 ? 212 ARG A CZ  1 
ATOM   1667  N NH1 . ARG A 1 216 ? -8.835  67.139  10.902  1.00 33.81 ? 212 ARG A NH1 1 
ATOM   1668  N NH2 . ARG A 1 216 ? -9.350  68.704  12.496  1.00 35.18 ? 212 ARG A NH2 1 
ATOM   1669  N N   . LEU A 1 217 ? -9.418  61.316  15.443  1.00 31.99 ? 213 LEU A N   1 
ATOM   1670  C CA  . LEU A 1 217 ? -9.827  61.069  16.819  1.00 32.47 ? 213 LEU A CA  1 
ATOM   1671  C C   . LEU A 1 217 ? -10.033 62.367  17.583  1.00 32.66 ? 213 LEU A C   1 
ATOM   1672  O O   . LEU A 1 217 ? -9.284  63.325  17.397  1.00 32.54 ? 213 LEU A O   1 
ATOM   1673  C CB  . LEU A 1 217 ? -8.780  60.219  17.533  1.00 32.38 ? 213 LEU A CB  1 
ATOM   1674  C CG  . LEU A 1 217 ? -8.356  58.940  16.820  1.00 32.87 ? 213 LEU A CG  1 
ATOM   1675  C CD1 . LEU A 1 217 ? -7.094  58.384  17.460  1.00 32.98 ? 213 LEU A CD1 1 
ATOM   1676  C CD2 . LEU A 1 217 ? -9.492  57.911  16.816  1.00 33.35 ? 213 LEU A CD2 1 
ATOM   1677  N N   . VAL A 1 218 ? -11.051 62.378  18.440  1.00 33.35 ? 214 VAL A N   1 
ATOM   1678  C CA  . VAL A 1 218 ? -11.336 63.499  19.343  1.00 34.15 ? 214 VAL A CA  1 
ATOM   1679  C C   . VAL A 1 218 ? -11.484 62.969  20.777  1.00 34.53 ? 214 VAL A C   1 
ATOM   1680  O O   . VAL A 1 218 ? -12.197 61.991  21.005  1.00 34.50 ? 214 VAL A O   1 
ATOM   1681  C CB  . VAL A 1 218 ? -12.596 64.301  18.876  1.00 34.31 ? 214 VAL A CB  1 
ATOM   1682  C CG1 . VAL A 1 218 ? -13.278 65.030  20.029  1.00 34.65 ? 214 VAL A CG1 1 
ATOM   1683  C CG2 . VAL A 1 218 ? -12.224 65.289  17.771  1.00 34.49 ? 214 VAL A CG2 1 
ATOM   1684  N N   . PRO A 1 219 ? -10.797 63.605  21.748  1.00 35.13 ? 215 PRO A N   1 
ATOM   1685  C CA  . PRO A 1 219 ? -10.852 63.100  23.125  1.00 35.31 ? 215 PRO A CA  1 
ATOM   1686  C C   . PRO A 1 219 ? -12.249 63.218  23.722  1.00 35.55 ? 215 PRO A C   1 
ATOM   1687  O O   . PRO A 1 219 ? -12.955 64.193  23.458  1.00 35.69 ? 215 PRO A O   1 
ATOM   1688  C CB  . PRO A 1 219 ? -9.868  64.001  23.876  1.00 35.29 ? 215 PRO A CB  1 
ATOM   1689  C CG  . PRO A 1 219 ? -9.769  65.237  23.049  1.00 35.27 ? 215 PRO A CG  1 
ATOM   1690  C CD  . PRO A 1 219 ? -9.932  64.796  21.632  1.00 35.13 ? 215 PRO A CD  1 
ATOM   1691  N N   . GLU A 1 220 ? -12.633 62.220  24.510  1.00 35.68 ? 216 GLU A N   1 
ATOM   1692  C CA  . GLU A 1 220 ? -13.939 62.183  25.150  1.00 36.02 ? 216 GLU A CA  1 
ATOM   1693  C C   . GLU A 1 220 ? -13.809 62.336  26.665  1.00 35.74 ? 216 GLU A C   1 
ATOM   1694  O O   . GLU A 1 220 ? -13.502 61.372  27.373  1.00 35.89 ? 216 GLU A O   1 
ATOM   1695  C CB  . GLU A 1 220 ? -14.688 60.894  24.772  1.00 36.39 ? 216 GLU A CB  1 
ATOM   1696  C CG  . GLU A 1 220 ? -15.091 60.840  23.287  1.00 38.44 ? 216 GLU A CG  1 
ATOM   1697  C CD  . GLU A 1 220 ? -15.972 59.647  22.918  1.00 41.07 ? 216 GLU A CD  1 
ATOM   1698  O OE1 . GLU A 1 220 ? -16.596 59.035  23.817  1.00 41.84 ? 216 GLU A OE1 1 
ATOM   1699  O OE2 . GLU A 1 220 ? -16.048 59.330  21.708  1.00 42.60 ? 216 GLU A OE2 1 
ATOM   1700  N N   . ILE A 1 221 ? -14.032 63.561  27.147  1.00 35.28 ? 217 ILE A N   1 
ATOM   1701  C CA  . ILE A 1 221 ? -13.924 63.883  28.570  1.00 34.89 ? 217 ILE A CA  1 
ATOM   1702  C C   . ILE A 1 221 ? -15.132 63.365  29.360  1.00 34.81 ? 217 ILE A C   1 
ATOM   1703  O O   . ILE A 1 221 ? -16.283 63.517  28.935  1.00 34.89 ? 217 ILE A O   1 
ATOM   1704  C CB  . ILE A 1 221 ? -13.733 65.413  28.798  1.00 34.87 ? 217 ILE A CB  1 
ATOM   1705  C CG1 . ILE A 1 221 ? -12.371 65.868  28.266  1.00 34.79 ? 217 ILE A CG1 1 
ATOM   1706  C CG2 . ILE A 1 221 ? -13.870 65.776  30.275  1.00 34.69 ? 217 ILE A CG2 1 
ATOM   1707  C CD1 . ILE A 1 221 ? -12.201 67.370  28.188  1.00 35.01 ? 217 ILE A CD1 1 
ATOM   1708  N N   . ALA A 1 222 ? -14.849 62.746  30.503  1.00 34.47 ? 218 ALA A N   1 
ATOM   1709  C CA  . ALA A 1 222 ? -15.872 62.260  31.424  1.00 34.39 ? 218 ALA A CA  1 
ATOM   1710  C C   . ALA A 1 222 ? -15.291 62.157  32.830  1.00 34.42 ? 218 ALA A C   1 
ATOM   1711  O O   . ALA A 1 222 ? -14.080 62.276  33.012  1.00 34.34 ? 218 ALA A O   1 
ATOM   1712  C CB  . ALA A 1 222 ? -16.417 60.910  30.967  1.00 34.27 ? 218 ALA A CB  1 
ATOM   1713  N N   . THR A 1 223 ? -16.160 61.944  33.817  1.00 34.54 ? 219 THR A N   1 
ATOM   1714  C CA  . THR A 1 223 ? -15.745 61.803  35.209  1.00 34.80 ? 219 THR A CA  1 
ATOM   1715  C C   . THR A 1 223 ? -15.670 60.322  35.533  1.00 34.88 ? 219 THR A C   1 
ATOM   1716  O O   . THR A 1 223 ? -16.668 59.605  35.438  1.00 35.13 ? 219 THR A O   1 
ATOM   1717  C CB  . THR A 1 223 ? -16.711 62.530  36.186  1.00 34.67 ? 219 THR A CB  1 
ATOM   1718  O OG1 . THR A 1 223 ? -16.823 63.905  35.810  1.00 35.23 ? 219 THR A OG1 1 
ATOM   1719  C CG2 . THR A 1 223 ? -16.201 62.460  37.620  1.00 34.70 ? 219 THR A CG2 1 
ATOM   1720  N N   . ARG A 1 224 ? -14.481 59.870  35.916  1.00 34.84 ? 220 ARG A N   1 
ATOM   1721  C CA  . ARG A 1 224 ? -14.234 58.446  36.091  1.00 34.62 ? 220 ARG A CA  1 
ATOM   1722  C C   . ARG A 1 224 ? -13.614 58.133  37.444  1.00 34.65 ? 220 ARG A C   1 
ATOM   1723  O O   . ARG A 1 224 ? -12.894 58.963  38.006  1.00 34.41 ? 220 ARG A O   1 
ATOM   1724  C CB  . ARG A 1 224 ? -13.318 57.930  34.981  1.00 34.63 ? 220 ARG A CB  1 
ATOM   1725  C CG  . ARG A 1 224 ? -13.707 58.404  33.597  1.00 34.62 ? 220 ARG A CG  1 
ATOM   1726  C CD  . ARG A 1 224 ? -12.716 57.966  32.545  1.00 34.51 ? 220 ARG A CD  1 
ATOM   1727  N NE  . ARG A 1 224 ? -12.814 58.821  31.367  1.00 34.83 ? 220 ARG A NE  1 
ATOM   1728  C CZ  . ARG A 1 224 ? -12.085 59.914  31.166  1.00 34.97 ? 220 ARG A CZ  1 
ATOM   1729  N NH1 . ARG A 1 224 ? -11.178 60.290  32.059  1.00 35.21 ? 220 ARG A NH1 1 
ATOM   1730  N NH2 . ARG A 1 224 ? -12.262 60.630  30.066  1.00 34.65 ? 220 ARG A NH2 1 
ATOM   1731  N N   . PRO A 1 225 ? -13.904 56.929  37.976  1.00 34.74 ? 221 PRO A N   1 
ATOM   1732  C CA  . PRO A 1 225 ? -13.210 56.390  39.140  1.00 34.82 ? 221 PRO A CA  1 
ATOM   1733  C C   . PRO A 1 225 ? -11.720 56.243  38.859  1.00 35.06 ? 221 PRO A C   1 
ATOM   1734  O O   . PRO A 1 225 ? -11.302 56.181  37.695  1.00 35.01 ? 221 PRO A O   1 
ATOM   1735  C CB  . PRO A 1 225 ? -13.826 54.999  39.305  1.00 34.81 ? 221 PRO A CB  1 
ATOM   1736  C CG  . PRO A 1 225 ? -15.153 55.091  38.664  1.00 34.94 ? 221 PRO A CG  1 
ATOM   1737  C CD  . PRO A 1 225 ? -15.015 56.062  37.544  1.00 34.65 ? 221 PRO A CD  1 
ATOM   1738  N N   . LYS A 1 226 ? -10.926 56.180  39.922  1.00 35.09 ? 222 LYS A N   1 
ATOM   1739  C CA  . LYS A 1 226 ? -9.503  55.968  39.769  1.00 34.95 ? 222 LYS A CA  1 
ATOM   1740  C C   . LYS A 1 226 ? -9.218  54.497  39.501  1.00 34.92 ? 222 LYS A C   1 
ATOM   1741  O O   . LYS A 1 226 ? -9.822  53.613  40.115  1.00 35.01 ? 222 LYS A O   1 
ATOM   1742  C CB  . LYS A 1 226 ? -8.746  56.470  40.996  1.00 35.04 ? 222 LYS A CB  1 
ATOM   1743  C CG  . LYS A 1 226 ? -8.706  57.983  41.092  1.00 35.52 ? 222 LYS A CG  1 
ATOM   1744  C CD  . LYS A 1 226 ? -7.867  58.448  42.260  1.00 36.56 ? 222 LYS A CD  1 
ATOM   1745  C CE  . LYS A 1 226 ? -7.855  59.955  42.334  1.00 37.65 ? 222 LYS A CE  1 
ATOM   1746  N NZ  . LYS A 1 226 ? -6.883  60.419  43.355  1.00 39.68 ? 222 LYS A NZ  1 
ATOM   1747  N N   . VAL A 1 227 ? -8.330  54.255  38.541  1.00 34.74 ? 223 VAL A N   1 
ATOM   1748  C CA  . VAL A 1 227 ? -7.798  52.927  38.251  1.00 34.55 ? 223 VAL A CA  1 
ATOM   1749  C C   . VAL A 1 227 ? -6.291  53.128  38.212  1.00 34.66 ? 223 VAL A C   1 
ATOM   1750  O O   . VAL A 1 227 ? -5.792  53.943  37.427  1.00 34.53 ? 223 VAL A O   1 
ATOM   1751  C CB  . VAL A 1 227 ? -8.314  52.367  36.893  1.00 34.63 ? 223 VAL A CB  1 
ATOM   1752  C CG1 . VAL A 1 227 ? -7.764  50.963  36.620  1.00 34.21 ? 223 VAL A CG1 1 
ATOM   1753  C CG2 . VAL A 1 227 ? -9.836  52.351  36.853  1.00 34.47 ? 223 VAL A CG2 1 
ATOM   1754  N N   . ASN A 1 228 ? -5.574  52.412  39.082  1.00 34.70 ? 224 ASN A N   1 
ATOM   1755  C CA  . ASN A 1 228 ? -4.136  52.629  39.301  1.00 34.51 ? 224 ASN A CA  1 
ATOM   1756  C C   . ASN A 1 228 ? -3.811  54.103  39.596  1.00 34.19 ? 224 ASN A C   1 
ATOM   1757  O O   . ASN A 1 228 ? -2.800  54.639  39.131  1.00 34.13 ? 224 ASN A O   1 
ATOM   1758  C CB  . ASN A 1 228 ? -3.304  52.105  38.116  1.00 34.63 ? 224 ASN A CB  1 
ATOM   1759  C CG  . ASN A 1 228 ? -3.551  50.627  37.819  1.00 35.61 ? 224 ASN A CG  1 
ATOM   1760  O OD1 . ASN A 1 228 ? -3.969  49.859  38.690  1.00 36.26 ? 224 ASN A OD1 1 
ATOM   1761  N ND2 . ASN A 1 228 ? -3.276  50.221  36.579  1.00 36.25 ? 224 ASN A ND2 1 
ATOM   1762  N N   . GLY A 1 229 ? -4.694  54.747  40.357  1.00 33.82 ? 225 GLY A N   1 
ATOM   1763  C CA  . GLY A 1 229 ? -4.531  56.142  40.763  1.00 33.52 ? 225 GLY A CA  1 
ATOM   1764  C C   . GLY A 1 229 ? -4.883  57.204  39.734  1.00 33.53 ? 225 GLY A C   1 
ATOM   1765  O O   . GLY A 1 229 ? -4.618  58.385  39.956  1.00 33.64 ? 225 GLY A O   1 
ATOM   1766  N N   . GLN A 1 230 ? -5.481  56.802  38.610  1.00 33.37 ? 226 GLN A N   1 
ATOM   1767  C CA  . GLN A 1 230 ? -5.761  57.738  37.511  1.00 33.04 ? 226 GLN A CA  1 
ATOM   1768  C C   . GLN A 1 230 ? -7.215  57.724  37.065  1.00 32.63 ? 226 GLN A C   1 
ATOM   1769  O O   . GLN A 1 230 ? -7.784  56.663  36.799  1.00 32.74 ? 226 GLN A O   1 
ATOM   1770  C CB  . GLN A 1 230 ? -4.866  57.464  36.296  1.00 33.11 ? 226 GLN A CB  1 
ATOM   1771  C CG  . GLN A 1 230 ? -3.371  57.451  36.570  1.00 34.23 ? 226 GLN A CG  1 
ATOM   1772  C CD  . GLN A 1 230 ? -2.858  58.731  37.216  1.00 35.89 ? 226 GLN A CD  1 
ATOM   1773  O OE1 . GLN A 1 230 ? -3.128  59.844  36.742  1.00 36.49 ? 226 GLN A OE1 1 
ATOM   1774  N NE2 . GLN A 1 230 ? -2.103  58.575  38.301  1.00 35.80 ? 226 GLN A NE2 1 
ATOM   1775  N N   . SER A 1 231 ? -7.802  58.914  36.986  1.00 32.15 ? 227 SER A N   1 
ATOM   1776  C CA  . SER A 1 231 ? -9.154  59.096  36.475  1.00 31.75 ? 227 SER A CA  1 
ATOM   1777  C C   . SER A 1 231 ? -9.152  59.247  34.960  1.00 31.35 ? 227 SER A C   1 
ATOM   1778  O O   . SER A 1 231 ? -10.168 59.012  34.301  1.00 31.54 ? 227 SER A O   1 
ATOM   1779  C CB  . SER A 1 231 ? -9.801  60.325  37.110  1.00 31.79 ? 227 SER A CB  1 
ATOM   1780  O OG  . SER A 1 231 ? -10.376 59.985  38.351  1.00 32.14 ? 227 SER A OG  1 
ATOM   1781  N N   . GLY A 1 232 ? -8.008  59.657  34.421  1.00 30.78 ? 228 GLY A N   1 
ATOM   1782  C CA  . GLY A 1 232 ? -7.818  59.770  32.984  1.00 30.07 ? 228 GLY A CA  1 
ATOM   1783  C C   . GLY A 1 232 ? -7.726  58.405  32.328  1.00 29.65 ? 228 GLY A C   1 
ATOM   1784  O O   . GLY A 1 232 ? -7.537  57.385  33.000  1.00 29.28 ? 228 GLY A O   1 
ATOM   1785  N N   . ARG A 1 233 ? -7.878  58.389  31.008  1.00 29.18 ? 229 ARG A N   1 
ATOM   1786  C CA  . ARG A 1 233 ? -7.808  57.151  30.240  1.00 28.92 ? 229 ARG A CA  1 
ATOM   1787  C C   . ARG A 1 233 ? -7.005  57.357  28.972  1.00 28.97 ? 229 ARG A C   1 
ATOM   1788  O O   . ARG A 1 233 ? -6.922  58.465  28.441  1.00 28.95 ? 229 ARG A O   1 
ATOM   1789  C CB  . ARG A 1 233 ? -9.207  56.631  29.886  1.00 28.45 ? 229 ARG A CB  1 
ATOM   1790  C CG  . ARG A 1 233 ? -10.104 56.308  31.069  1.00 28.01 ? 229 ARG A CG  1 
ATOM   1791  C CD  . ARG A 1 233 ? -9.729  55.002  31.747  1.00 27.95 ? 229 ARG A CD  1 
ATOM   1792  N NE  . ARG A 1 233 ? -10.627 54.694  32.857  1.00 27.86 ? 229 ARG A NE  1 
ATOM   1793  C CZ  . ARG A 1 233 ? -10.456 55.109  34.113  1.00 28.61 ? 229 ARG A CZ  1 
ATOM   1794  N NH1 . ARG A 1 233 ? -9.413  55.860  34.448  1.00 27.83 ? 229 ARG A NH1 1 
ATOM   1795  N NH2 . ARG A 1 233 ? -11.341 54.772  35.039  1.00 29.14 ? 229 ARG A NH2 1 
ATOM   1796  N N   . MET A 1 234 ? -6.408  56.277  28.497  1.00 29.23 ? 230 MET A N   1 
ATOM   1797  C CA  . MET A 1 234 ? -5.734  56.287  27.218  1.00 29.59 ? 230 MET A CA  1 
ATOM   1798  C C   . MET A 1 234 ? -6.255  55.185  26.319  1.00 29.28 ? 230 MET A C   1 
ATOM   1799  O O   . MET A 1 234 ? -6.456  54.058  26.755  1.00 29.32 ? 230 MET A O   1 
ATOM   1800  C CB  . MET A 1 234 ? -4.233  56.165  27.412  1.00 29.91 ? 230 MET A CB  1 
ATOM   1801  C CG  . MET A 1 234 ? -3.592  57.478  27.751  1.00 31.51 ? 230 MET A CG  1 
ATOM   1802  S SD  . MET A 1 234 ? -1.894  57.255  28.262  1.00 36.58 ? 230 MET A SD  1 
ATOM   1803  C CE  . MET A 1 234 ? -1.495  58.941  28.737  1.00 34.46 ? 230 MET A CE  1 
ATOM   1804  N N   . GLU A 1 235 ? -6.478  55.532  25.061  1.00 29.23 ? 231 GLU A N   1 
ATOM   1805  C CA  . GLU A 1 235 ? -6.968  54.595  24.064  1.00 29.10 ? 231 GLU A CA  1 
ATOM   1806  C C   . GLU A 1 235 ? -5.883  54.430  23.011  1.00 28.89 ? 231 GLU A C   1 
ATOM   1807  O O   . GLU A 1 235 ? -5.376  55.414  22.481  1.00 28.89 ? 231 GLU A O   1 
ATOM   1808  C CB  . GLU A 1 235 ? -8.252  55.147  23.447  1.00 29.28 ? 231 GLU A CB  1 
ATOM   1809  C CG  . GLU A 1 235 ? -9.126  54.138  22.707  1.00 29.64 ? 231 GLU A CG  1 
ATOM   1810  C CD  . GLU A 1 235 ? -10.528 54.677  22.418  1.00 30.05 ? 231 GLU A CD  1 
ATOM   1811  O OE1 . GLU A 1 235 ? -10.715 55.921  22.361  1.00 29.77 ? 231 GLU A OE1 1 
ATOM   1812  O OE2 . GLU A 1 235 ? -11.449 53.846  22.257  1.00 30.45 ? 231 GLU A OE2 1 
ATOM   1813  N N   . PHE A 1 236 ? -5.512  53.188  22.723  1.00 28.73 ? 232 PHE A N   1 
ATOM   1814  C CA  . PHE A 1 236 ? -4.468  52.922  21.739  1.00 28.77 ? 232 PHE A CA  1 
ATOM   1815  C C   . PHE A 1 236 ? -4.990  52.338  20.436  1.00 28.84 ? 232 PHE A C   1 
ATOM   1816  O O   . PHE A 1 236 ? -5.956  51.570  20.426  1.00 28.83 ? 232 PHE A O   1 
ATOM   1817  C CB  . PHE A 1 236 ? -3.379  52.029  22.334  1.00 28.73 ? 232 PHE A CB  1 
ATOM   1818  C CG  . PHE A 1 236 ? -2.617  52.686  23.436  1.00 28.86 ? 232 PHE A CG  1 
ATOM   1819  C CD1 . PHE A 1 236 ? -1.569  53.558  23.145  1.00 28.67 ? 232 PHE A CD1 1 
ATOM   1820  C CD2 . PHE A 1 236 ? -2.965  52.462  24.763  1.00 29.04 ? 232 PHE A CD2 1 
ATOM   1821  C CE1 . PHE A 1 236 ? -0.869  54.186  24.163  1.00 29.17 ? 232 PHE A CE1 1 
ATOM   1822  C CE2 . PHE A 1 236 ? -2.272  53.084  25.794  1.00 29.70 ? 232 PHE A CE2 1 
ATOM   1823  C CZ  . PHE A 1 236 ? -1.222  53.951  25.494  1.00 30.19 ? 232 PHE A CZ  1 
ATOM   1824  N N   . PHE A 1 237 ? -4.327  52.707  19.344  1.00 28.77 ? 233 PHE A N   1 
ATOM   1825  C CA  . PHE A 1 237 ? -4.701  52.279  18.005  1.00 28.85 ? 233 PHE A CA  1 
ATOM   1826  C C   . PHE A 1 237 ? -3.491  51.716  17.272  1.00 29.08 ? 233 PHE A C   1 
ATOM   1827  O O   . PHE A 1 237 ? -2.345  51.922  17.689  1.00 29.09 ? 233 PHE A O   1 
ATOM   1828  C CB  . PHE A 1 237 ? -5.297  53.454  17.222  1.00 28.78 ? 233 PHE A CB  1 
ATOM   1829  C CG  . PHE A 1 237 ? -6.564  53.994  17.815  1.00 28.66 ? 233 PHE A CG  1 
ATOM   1830  C CD1 . PHE A 1 237 ? -7.800  53.597  17.317  1.00 28.36 ? 233 PHE A CD1 1 
ATOM   1831  C CD2 . PHE A 1 237 ? -6.525  54.893  18.883  1.00 29.08 ? 233 PHE A CD2 1 
ATOM   1832  C CE1 . PHE A 1 237 ? -8.978  54.083  17.863  1.00 28.36 ? 233 PHE A CE1 1 
ATOM   1833  C CE2 . PHE A 1 237 ? -7.701  55.385  19.443  1.00 28.80 ? 233 PHE A CE2 1 
ATOM   1834  C CZ  . PHE A 1 237 ? -8.929  54.981  18.929  1.00 29.43 ? 233 PHE A CZ  1 
ATOM   1835  N N   . TRP A 1 238 ? -3.751  50.998  16.182  1.00 29.16 ? 234 TRP A N   1 
ATOM   1836  C CA  . TRP A 1 238 ? -2.690  50.408  15.381  1.00 29.21 ? 234 TRP A CA  1 
ATOM   1837  C C   . TRP A 1 238 ? -3.100  50.259  13.920  1.00 29.78 ? 234 TRP A C   1 
ATOM   1838  O O   . TRP A 1 238 ? -4.286  50.222  13.599  1.00 29.77 ? 234 TRP A O   1 
ATOM   1839  C CB  . TRP A 1 238 ? -2.282  49.052  15.957  1.00 28.74 ? 234 TRP A CB  1 
ATOM   1840  C CG  . TRP A 1 238 ? -3.382  48.041  15.960  1.00 28.00 ? 234 TRP A CG  1 
ATOM   1841  C CD1 . TRP A 1 238 ? -4.332  47.870  16.922  1.00 27.48 ? 234 TRP A CD1 1 
ATOM   1842  C CD2 . TRP A 1 238 ? -3.650  47.059  14.953  1.00 27.08 ? 234 TRP A CD2 1 
ATOM   1843  N NE1 . TRP A 1 238 ? -5.175  46.842  16.583  1.00 26.93 ? 234 TRP A NE1 1 
ATOM   1844  C CE2 . TRP A 1 238 ? -4.782  46.326  15.377  1.00 27.25 ? 234 TRP A CE2 1 
ATOM   1845  C CE3 . TRP A 1 238 ? -3.045  46.726  13.733  1.00 26.50 ? 234 TRP A CE3 1 
ATOM   1846  C CZ2 . TRP A 1 238 ? -5.323  45.273  14.626  1.00 27.14 ? 234 TRP A CZ2 1 
ATOM   1847  C CZ3 . TRP A 1 238 ? -3.581  45.682  12.985  1.00 26.74 ? 234 TRP A CZ3 1 
ATOM   1848  C CH2 . TRP A 1 238 ? -4.712  44.968  13.435  1.00 27.08 ? 234 TRP A CH2 1 
ATOM   1849  N N   . THR A 1 239 ? -2.106  50.186  13.041  1.00 30.56 ? 235 THR A N   1 
ATOM   1850  C CA  . THR A 1 239 ? -2.324  49.819  11.646  1.00 31.14 ? 235 THR A CA  1 
ATOM   1851  C C   . THR A 1 239 ? -1.082  49.134  11.082  1.00 31.71 ? 235 THR A C   1 
ATOM   1852  O O   . THR A 1 239 ? 0.020   49.251  11.639  1.00 31.76 ? 235 THR A O   1 
ATOM   1853  C CB  . THR A 1 239 ? -2.701  51.035  10.764  1.00 31.22 ? 235 THR A CB  1 
ATOM   1854  O OG1 . THR A 1 239 ? -3.219  50.573  9.506   1.00 31.78 ? 235 THR A OG1 1 
ATOM   1855  C CG2 . THR A 1 239 ? -1.496  51.935  10.518  1.00 30.93 ? 235 THR A CG2 1 
ATOM   1856  N N   . ILE A 1 240 ? -1.272  48.410  9.982   1.00 32.08 ? 236 ILE A N   1 
ATOM   1857  C CA  . ILE A 1 240 ? -0.163  47.814  9.261   1.00 32.22 ? 236 ILE A CA  1 
ATOM   1858  C C   . ILE A 1 240 ? 0.223   48.780  8.161   1.00 32.54 ? 236 ILE A C   1 
ATOM   1859  O O   . ILE A 1 240 ? -0.614  49.180  7.358   1.00 32.70 ? 236 ILE A O   1 
ATOM   1860  C CB  . ILE A 1 240 ? -0.531  46.427  8.669   1.00 32.25 ? 236 ILE A CB  1 
ATOM   1861  C CG1 . ILE A 1 240 ? -0.947  45.441  9.776   1.00 32.26 ? 236 ILE A CG1 1 
ATOM   1862  C CG2 . ILE A 1 240 ? 0.614   45.870  7.819   1.00 32.07 ? 236 ILE A CG2 1 
ATOM   1863  C CD1 . ILE A 1 240 ? 0.124   45.170  10.856  1.00 32.73 ? 236 ILE A CD1 1 
ATOM   1864  N N   . LEU A 1 241 ? 1.489   49.176  8.143   1.00 33.00 ? 237 LEU A N   1 
ATOM   1865  C CA  . LEU A 1 241 ? 1.982   50.076  7.115   1.00 33.42 ? 237 LEU A CA  1 
ATOM   1866  C C   . LEU A 1 241 ? 2.726   49.288  6.036   1.00 33.80 ? 237 LEU A C   1 
ATOM   1867  O O   . LEU A 1 241 ? 3.804   48.741  6.280   1.00 33.79 ? 237 LEU A O   1 
ATOM   1868  C CB  . LEU A 1 241 ? 2.867   51.162  7.734   1.00 33.33 ? 237 LEU A CB  1 
ATOM   1869  C CG  . LEU A 1 241 ? 3.208   52.392  6.888   1.00 33.54 ? 237 LEU A CG  1 
ATOM   1870  C CD1 . LEU A 1 241 ? 1.954   53.127  6.431   1.00 33.49 ? 237 LEU A CD1 1 
ATOM   1871  C CD2 . LEU A 1 241 ? 4.126   53.329  7.663   1.00 33.44 ? 237 LEU A CD2 1 
ATOM   1872  N N   . LYS A 1 242 ? 2.127   49.230  4.850   1.00 34.31 ? 238 LYS A N   1 
ATOM   1873  C CA  . LYS A 1 242 ? 2.689   48.507  3.706   1.00 34.91 ? 238 LYS A CA  1 
ATOM   1874  C C   . LYS A 1 242 ? 4.016   49.084  3.236   1.00 35.01 ? 238 LYS A C   1 
ATOM   1875  O O   . LYS A 1 242 ? 4.259   50.279  3.404   1.00 35.14 ? 238 LYS A O   1 
ATOM   1876  C CB  . LYS A 1 242 ? 1.705   48.515  2.533   1.00 35.01 ? 238 LYS A CB  1 
ATOM   1877  C CG  . LYS A 1 242 ? 1.035   47.183  2.263   1.00 35.85 ? 238 LYS A CG  1 
ATOM   1878  C CD  . LYS A 1 242 ? -0.084  46.898  3.244   1.00 37.25 ? 238 LYS A CD  1 
ATOM   1879  C CE  . LYS A 1 242 ? -0.953  45.752  2.750   1.00 38.52 ? 238 LYS A CE  1 
ATOM   1880  N NZ  . LYS A 1 242 ? -1.657  46.108  1.475   1.00 39.63 ? 238 LYS A NZ  1 
ATOM   1881  N N   . PRO A 1 243 ? 4.878   48.237  2.640   1.00 35.29 ? 239 PRO A N   1 
ATOM   1882  C CA  . PRO A 1 243 ? 6.096   48.757  2.032   1.00 35.41 ? 239 PRO A CA  1 
ATOM   1883  C C   . PRO A 1 243 ? 5.755   49.848  1.027   1.00 35.72 ? 239 PRO A C   1 
ATOM   1884  O O   . PRO A 1 243 ? 4.847   49.673  0.206   1.00 36.07 ? 239 PRO A O   1 
ATOM   1885  C CB  . PRO A 1 243 ? 6.686   47.533  1.328   1.00 35.43 ? 239 PRO A CB  1 
ATOM   1886  C CG  . PRO A 1 243 ? 6.189   46.376  2.123   1.00 35.34 ? 239 PRO A CG  1 
ATOM   1887  C CD  . PRO A 1 243 ? 4.808   46.762  2.560   1.00 35.19 ? 239 PRO A CD  1 
ATOM   1888  N N   . ASN A 1 244 ? 6.460   50.974  1.135   1.00 35.96 ? 240 ASN A N   1 
ATOM   1889  C CA  . ASN A 1 244 ? 6.275   52.167  0.287   1.00 36.09 ? 240 ASN A CA  1 
ATOM   1890  C C   . ASN A 1 244 ? 4.995   52.985  0.517   1.00 35.67 ? 240 ASN A C   1 
ATOM   1891  O O   . ASN A 1 244 ? 4.699   53.911  -0.240  1.00 35.37 ? 240 ASN A O   1 
ATOM   1892  C CB  . ASN A 1 244 ? 6.498   51.845  -1.200  1.00 36.46 ? 240 ASN A CB  1 
ATOM   1893  C CG  . ASN A 1 244 ? 7.853   51.208  -1.453  1.00 38.10 ? 240 ASN A CG  1 
ATOM   1894  O OD1 . ASN A 1 244 ? 7.939   50.063  -1.912  1.00 40.14 ? 240 ASN A OD1 1 
ATOM   1895  N ND2 . ASN A 1 244 ? 8.923   51.934  -1.125  1.00 38.84 ? 240 ASN A ND2 1 
ATOM   1896  N N   . ASP A 1 245 ? 4.253   52.655  1.570   1.00 35.55 ? 241 ASP A N   1 
ATOM   1897  C CA  . ASP A 1 245 ? 3.164   53.520  2.020   1.00 35.56 ? 241 ASP A CA  1 
ATOM   1898  C C   . ASP A 1 245 ? 3.647   54.418  3.167   1.00 35.32 ? 241 ASP A C   1 
ATOM   1899  O O   . ASP A 1 245 ? 4.607   54.082  3.871   1.00 35.39 ? 241 ASP A O   1 
ATOM   1900  C CB  . ASP A 1 245 ? 1.926   52.710  2.427   1.00 35.64 ? 241 ASP A CB  1 
ATOM   1901  C CG  . ASP A 1 245 ? 0.651   53.560  2.466   1.00 36.26 ? 241 ASP A CG  1 
ATOM   1902  O OD1 . ASP A 1 245 ? 0.597   54.598  1.766   1.00 35.98 ? 241 ASP A OD1 1 
ATOM   1903  O OD2 . ASP A 1 245 ? -0.302  53.189  3.192   1.00 36.50 ? 241 ASP A OD2 1 
ATOM   1904  N N   . ALA A 1 246 ? 2.985   55.560  3.338   1.00 34.98 ? 242 ALA A N   1 
ATOM   1905  C CA  . ALA A 1 246 ? 3.352   56.534  4.366   1.00 34.61 ? 242 ALA A CA  1 
ATOM   1906  C C   . ALA A 1 246 ? 2.224   56.755  5.361   1.00 34.33 ? 242 ALA A C   1 
ATOM   1907  O O   . ALA A 1 246 ? 1.048   56.707  4.995   1.00 34.09 ? 242 ALA A O   1 
ATOM   1908  C CB  . ALA A 1 246 ? 3.747   57.862  3.722   1.00 34.57 ? 242 ALA A CB  1 
ATOM   1909  N N   . ILE A 1 247 ? 2.595   57.004  6.614   1.00 34.16 ? 243 ILE A N   1 
ATOM   1910  C CA  . ILE A 1 247 ? 1.630   57.377  7.649   1.00 34.07 ? 243 ILE A CA  1 
ATOM   1911  C C   . ILE A 1 247 ? 1.797   58.857  8.022   1.00 34.25 ? 243 ILE A C   1 
ATOM   1912  O O   . ILE A 1 247 ? 2.905   59.306  8.325   1.00 34.56 ? 243 ILE A O   1 
ATOM   1913  C CB  . ILE A 1 247 ? 1.716   56.435  8.887   1.00 33.88 ? 243 ILE A CB  1 
ATOM   1914  C CG1 . ILE A 1 247 ? 0.499   56.618  9.795   1.00 33.58 ? 243 ILE A CG1 1 
ATOM   1915  C CG2 . ILE A 1 247 ? 3.043   56.615  9.655   1.00 34.04 ? 243 ILE A CG2 1 
ATOM   1916  C CD1 . ILE A 1 247 ? 0.195   55.422  10.683  1.00 32.39 ? 243 ILE A CD1 1 
ATOM   1917  N N   . ASN A 1 248 ? 0.700   59.611  7.965   1.00 34.15 ? 244 ASN A N   1 
ATOM   1918  C CA  . ASN A 1 248 ? 0.714   61.054  8.239   1.00 33.81 ? 244 ASN A CA  1 
ATOM   1919  C C   . ASN A 1 248 ? -0.053  61.375  9.519   1.00 33.44 ? 244 ASN A C   1 
ATOM   1920  O O   . ASN A 1 248 ? -1.252  61.105  9.606   1.00 33.58 ? 244 ASN A O   1 
ATOM   1921  C CB  . ASN A 1 248 ? 0.085   61.837  7.075   1.00 33.78 ? 244 ASN A CB  1 
ATOM   1922  C CG  . ASN A 1 248 ? 0.854   61.692  5.772   1.00 34.44 ? 244 ASN A CG  1 
ATOM   1923  O OD1 . ASN A 1 248 ? 1.876   62.341  5.570   1.00 35.36 ? 244 ASN A OD1 1 
ATOM   1924  N ND2 . ASN A 1 248 ? 0.343   60.860  4.866   1.00 34.99 ? 244 ASN A ND2 1 
ATOM   1925  N N   . PHE A 1 249 ? 0.630   61.964  10.500  1.00 32.81 ? 245 PHE A N   1 
ATOM   1926  C CA  . PHE A 1 249 ? -0.016  62.379  11.747  1.00 32.13 ? 245 PHE A CA  1 
ATOM   1927  C C   . PHE A 1 249 ? -0.188  63.894  11.817  1.00 32.17 ? 245 PHE A C   1 
ATOM   1928  O O   . PHE A 1 249 ? 0.709   64.653  11.441  1.00 31.96 ? 245 PHE A O   1 
ATOM   1929  C CB  . PHE A 1 249 ? 0.788   61.921  12.967  1.00 31.84 ? 245 PHE A CB  1 
ATOM   1930  C CG  . PHE A 1 249 ? 0.868   60.434  13.127  1.00 30.87 ? 245 PHE A CG  1 
ATOM   1931  C CD1 . PHE A 1 249 ? -0.157  59.732  13.744  1.00 29.81 ? 245 PHE A CD1 1 
ATOM   1932  C CD2 . PHE A 1 249 ? 1.978   59.734  12.677  1.00 29.77 ? 245 PHE A CD2 1 
ATOM   1933  C CE1 . PHE A 1 249 ? -0.074  58.361  13.904  1.00 29.45 ? 245 PHE A CE1 1 
ATOM   1934  C CE2 . PHE A 1 249 ? 2.062   58.360  12.832  1.00 28.40 ? 245 PHE A CE2 1 
ATOM   1935  C CZ  . PHE A 1 249 ? 1.040   57.677  13.446  1.00 28.58 ? 245 PHE A CZ  1 
ATOM   1936  N N   . GLU A 1 250 ? -1.345  64.320  12.311  1.00 31.97 ? 246 GLU A N   1 
ATOM   1937  C CA  . GLU A 1 250 ? -1.582  65.719  12.631  1.00 31.98 ? 246 GLU A CA  1 
ATOM   1938  C C   . GLU A 1 250 ? -2.361  65.802  13.945  1.00 31.78 ? 246 GLU A C   1 
ATOM   1939  O O   . GLU A 1 250 ? -3.291  65.019  14.165  1.00 31.66 ? 246 GLU A O   1 
ATOM   1940  C CB  . GLU A 1 250 ? -2.323  66.427  11.491  1.00 32.03 ? 246 GLU A CB  1 
ATOM   1941  C CG  . GLU A 1 250 ? -2.395  67.939  11.654  1.00 32.78 ? 246 GLU A CG  1 
ATOM   1942  C CD  . GLU A 1 250 ? -3.063  68.639  10.484  1.00 34.01 ? 246 GLU A CD  1 
ATOM   1943  O OE1 . GLU A 1 250 ? -4.163  69.201  10.682  1.00 32.35 ? 246 GLU A OE1 1 
ATOM   1944  O OE2 . GLU A 1 250 ? -2.482  68.628  9.371   1.00 34.98 ? 246 GLU A OE2 1 
ATOM   1945  N N   . SER A 1 251 ? -1.963  66.733  14.817  1.00 31.58 ? 247 SER A N   1 
ATOM   1946  C CA  . SER A 1 251 ? -2.590  66.895  16.137  1.00 31.43 ? 247 SER A CA  1 
ATOM   1947  C C   . SER A 1 251 ? -2.324  68.252  16.783  1.00 31.41 ? 247 SER A C   1 
ATOM   1948  O O   . SER A 1 251 ? -1.278  68.868  16.559  1.00 31.51 ? 247 SER A O   1 
ATOM   1949  C CB  . SER A 1 251 ? -2.130  65.789  17.096  1.00 31.37 ? 247 SER A CB  1 
ATOM   1950  O OG  . SER A 1 251 ? -2.914  65.785  18.282  1.00 31.29 ? 247 SER A OG  1 
ATOM   1951  N N   . ASN A 1 252 ? -3.275  68.706  17.595  1.00 31.36 ? 248 ASN A N   1 
ATOM   1952  C CA  . ASN A 1 252 ? -3.073  69.881  18.444  1.00 31.45 ? 248 ASN A CA  1 
ATOM   1953  C C   . ASN A 1 252 ? -3.308  69.580  19.928  1.00 31.40 ? 248 ASN A C   1 
ATOM   1954  O O   . ASN A 1 252 ? -3.706  70.456  20.692  1.00 31.49 ? 248 ASN A O   1 
ATOM   1955  C CB  . ASN A 1 252 ? -3.939  71.057  17.975  1.00 31.32 ? 248 ASN A CB  1 
ATOM   1956  C CG  . ASN A 1 252 ? -5.427  70.774  18.087  1.00 31.67 ? 248 ASN A CG  1 
ATOM   1957  O OD1 . ASN A 1 252 ? -5.859  69.618  18.058  1.00 31.60 ? 248 ASN A OD1 1 
ATOM   1958  N ND2 . ASN A 1 252 ? -6.221  71.835  18.208  1.00 31.52 ? 248 ASN A ND2 1 
ATOM   1959  N N   . GLY A 1 253 ? -3.055  68.335  20.324  1.00 31.29 ? 249 GLY A N   1 
ATOM   1960  C CA  . GLY A 1 253 ? -3.195  67.919  21.720  1.00 31.10 ? 249 GLY A CA  1 
ATOM   1961  C C   . GLY A 1 253 ? -3.623  66.470  21.883  1.00 31.05 ? 249 GLY A C   1 
ATOM   1962  O O   . GLY A 1 253 ? -4.111  65.848  20.934  1.00 31.10 ? 249 GLY A O   1 
ATOM   1963  N N   . ASN A 1 254 ? -3.425  65.939  23.091  1.00 30.63 ? 250 ASN A N   1 
ATOM   1964  C CA  . ASN A 1 254 ? -3.892  64.602  23.483  1.00 30.25 ? 250 ASN A CA  1 
ATOM   1965  C C   . ASN A 1 254 ? -3.236  63.435  22.733  1.00 30.17 ? 250 ASN A C   1 
ATOM   1966  O O   . ASN A 1 254 ? -3.610  62.279  22.921  1.00 30.18 ? 250 ASN A O   1 
ATOM   1967  C CB  . ASN A 1 254 ? -5.424  64.512  23.405  1.00 29.97 ? 250 ASN A CB  1 
ATOM   1968  C CG  . ASN A 1 254 ? -6.114  65.603  24.203  1.00 29.93 ? 250 ASN A CG  1 
ATOM   1969  O OD1 . ASN A 1 254 ? -6.047  66.783  23.851  1.00 29.28 ? 250 ASN A OD1 1 
ATOM   1970  N ND2 . ASN A 1 254 ? -6.791  65.212  25.280  1.00 29.05 ? 250 ASN A ND2 1 
ATOM   1971  N N   . PHE A 1 255 ? -2.241  63.749  21.911  1.00 29.95 ? 251 PHE A N   1 
ATOM   1972  C CA  . PHE A 1 255 ? -1.559  62.770  21.072  1.00 29.73 ? 251 PHE A CA  1 
ATOM   1973  C C   . PHE A 1 255 ? -0.549  61.932  21.861  1.00 29.98 ? 251 PHE A C   1 
ATOM   1974  O O   . PHE A 1 255 ? 0.288   62.468  22.594  1.00 30.13 ? 251 PHE A O   1 
ATOM   1975  C CB  . PHE A 1 255 ? -0.878  63.506  19.907  1.00 29.41 ? 251 PHE A CB  1 
ATOM   1976  C CG  . PHE A 1 255 ? -0.298  62.603  18.845  1.00 29.05 ? 251 PHE A CG  1 
ATOM   1977  C CD1 . PHE A 1 255 ? -0.859  61.360  18.559  1.00 28.51 ? 251 PHE A CD1 1 
ATOM   1978  C CD2 . PHE A 1 255 ? 0.792   63.029  18.090  1.00 28.40 ? 251 PHE A CD2 1 
ATOM   1979  C CE1 . PHE A 1 255 ? -0.319  60.542  17.564  1.00 27.97 ? 251 PHE A CE1 1 
ATOM   1980  C CE2 . PHE A 1 255 ? 1.329   62.225  17.093  1.00 27.89 ? 251 PHE A CE2 1 
ATOM   1981  C CZ  . PHE A 1 255 ? 0.772   60.979  16.830  1.00 27.73 ? 251 PHE A CZ  1 
ATOM   1982  N N   . ILE A 1 256 ? -0.646  60.611  21.723  1.00 30.07 ? 252 ILE A N   1 
ATOM   1983  C CA  . ILE A 1 256 ? 0.389   59.710  22.223  1.00 29.97 ? 252 ILE A CA  1 
ATOM   1984  C C   . ILE A 1 256 ? 1.139   59.154  21.017  1.00 30.27 ? 252 ILE A C   1 
ATOM   1985  O O   . ILE A 1 256 ? 0.717   58.172  20.394  1.00 30.27 ? 252 ILE A O   1 
ATOM   1986  C CB  . ILE A 1 256 ? -0.175  58.569  23.105  1.00 29.87 ? 252 ILE A CB  1 
ATOM   1987  C CG1 . ILE A 1 256 ? -1.242  59.092  24.082  1.00 29.27 ? 252 ILE A CG1 1 
ATOM   1988  C CG2 . ILE A 1 256 ? 0.968   57.835  23.828  1.00 29.73 ? 252 ILE A CG2 1 
ATOM   1989  C CD1 . ILE A 1 256 ? -0.732  60.077  25.145  1.00 28.78 ? 252 ILE A CD1 1 
ATOM   1990  N N   . ALA A 1 257 ? 2.256   59.804  20.703  1.00 30.59 ? 253 ALA A N   1 
ATOM   1991  C CA  . ALA A 1 257 ? 2.976   59.599  19.455  1.00 30.87 ? 253 ALA A CA  1 
ATOM   1992  C C   . ALA A 1 257 ? 3.815   58.335  19.444  1.00 31.21 ? 253 ALA A C   1 
ATOM   1993  O O   . ALA A 1 257 ? 4.384   57.957  20.473  1.00 31.24 ? 253 ALA A O   1 
ATOM   1994  C CB  . ALA A 1 257 ? 3.853   60.808  19.154  1.00 30.87 ? 253 ALA A CB  1 
ATOM   1995  N N   . PRO A 1 258 ? 3.920   57.689  18.266  1.00 31.61 ? 254 PRO A N   1 
ATOM   1996  C CA  . PRO A 1 258 ? 4.820   56.549  18.172  1.00 31.96 ? 254 PRO A CA  1 
ATOM   1997  C C   . PRO A 1 258 ? 6.249   57.020  18.393  1.00 32.49 ? 254 PRO A C   1 
ATOM   1998  O O   . PRO A 1 258 ? 6.546   58.200  18.191  1.00 32.41 ? 254 PRO A O   1 
ATOM   1999  C CB  . PRO A 1 258 ? 4.677   56.095  16.714  1.00 31.72 ? 254 PRO A CB  1 
ATOM   2000  C CG  . PRO A 1 258 ? 3.561   56.889  16.131  1.00 31.64 ? 254 PRO A CG  1 
ATOM   2001  C CD  . PRO A 1 258 ? 3.412   58.106  16.945  1.00 31.47 ? 254 PRO A CD  1 
ATOM   2002  N N   . GLU A 1 259 ? 7.110   56.114  18.834  1.00 33.06 ? 255 GLU A N   1 
ATOM   2003  C CA  . GLU A 1 259 ? 8.544   56.315  18.718  1.00 33.83 ? 255 GLU A CA  1 
ATOM   2004  C C   . GLU A 1 259 ? 9.138   55.106  18.001  1.00 34.08 ? 255 GLU A C   1 
ATOM   2005  O O   . GLU A 1 259 ? 9.867   55.262  17.019  1.00 34.29 ? 255 GLU A O   1 
ATOM   2006  C CB  . GLU A 1 259 ? 9.227   56.556  20.078  1.00 33.77 ? 255 GLU A CB  1 
ATOM   2007  C CG  . GLU A 1 259 ? 10.760  56.483  19.969  1.00 35.10 ? 255 GLU A CG  1 
ATOM   2008  C CD  . GLU A 1 259 ? 11.526  57.133  21.115  1.00 36.52 ? 255 GLU A CD  1 
ATOM   2009  O OE1 . GLU A 1 259 ? 11.061  57.095  22.281  1.00 37.43 ? 255 GLU A OE1 1 
ATOM   2010  O OE2 . GLU A 1 259 ? 12.624  57.665  20.832  1.00 36.12 ? 255 GLU A OE2 1 
ATOM   2011  N N   . TYR A 1 260 ? 8.811   53.912  18.496  1.00 34.31 ? 256 TYR A N   1 
ATOM   2012  C CA  . TYR A 1 260 ? 9.261   52.658  17.899  1.00 34.79 ? 256 TYR A CA  1 
ATOM   2013  C C   . TYR A 1 260 ? 8.105   51.918  17.223  1.00 34.69 ? 256 TYR A C   1 
ATOM   2014  O O   . TYR A 1 260 ? 6.977   51.924  17.716  1.00 34.69 ? 256 TYR A O   1 
ATOM   2015  C CB  . TYR A 1 260 ? 9.893   51.743  18.956  1.00 34.98 ? 256 TYR A CB  1 
ATOM   2016  C CG  . TYR A 1 260 ? 11.149  52.285  19.606  1.00 36.13 ? 256 TYR A CG  1 
ATOM   2017  C CD1 . TYR A 1 260 ? 12.414  52.024  19.065  1.00 36.76 ? 256 TYR A CD1 1 
ATOM   2018  C CD2 . TYR A 1 260 ? 11.075  53.041  20.778  1.00 37.31 ? 256 TYR A CD2 1 
ATOM   2019  C CE1 . TYR A 1 260 ? 13.573  52.517  19.671  1.00 37.31 ? 256 TYR A CE1 1 
ATOM   2020  C CE2 . TYR A 1 260 ? 12.222  53.539  21.390  1.00 38.01 ? 256 TYR A CE2 1 
ATOM   2021  C CZ  . TYR A 1 260 ? 13.466  53.276  20.833  1.00 38.08 ? 256 TYR A CZ  1 
ATOM   2022  O OH  . TYR A 1 260 ? 14.591  53.778  21.451  1.00 38.28 ? 256 TYR A OH  1 
ATOM   2023  N N   . ALA A 1 261 ? 8.401   51.290  16.089  1.00 34.60 ? 257 ALA A N   1 
ATOM   2024  C CA  . ALA A 1 261 ? 7.460   50.416  15.404  1.00 34.58 ? 257 ALA A CA  1 
ATOM   2025  C C   . ALA A 1 261 ? 8.092   49.027  15.256  1.00 34.77 ? 257 ALA A C   1 
ATOM   2026  O O   . ALA A 1 261 ? 9.261   48.833  15.604  1.00 34.74 ? 257 ALA A O   1 
ATOM   2027  C CB  . ALA A 1 261 ? 7.091   50.996  14.051  1.00 34.40 ? 257 ALA A CB  1 
ATOM   2028  N N   . TYR A 1 262 ? 7.323   48.062  14.755  1.00 34.93 ? 258 TYR A N   1 
ATOM   2029  C CA  . TYR A 1 262 ? 7.824   46.697  14.576  1.00 35.07 ? 258 TYR A CA  1 
ATOM   2030  C C   . TYR A 1 262 ? 7.790   46.237  13.119  1.00 35.47 ? 258 TYR A C   1 
ATOM   2031  O O   . TYR A 1 262 ? 6.745   46.300  12.460  1.00 35.26 ? 258 TYR A O   1 
ATOM   2032  C CB  . TYR A 1 262 ? 7.019   45.713  15.418  1.00 34.74 ? 258 TYR A CB  1 
ATOM   2033  C CG  . TYR A 1 262 ? 7.102   45.918  16.904  1.00 34.06 ? 258 TYR A CG  1 
ATOM   2034  C CD1 . TYR A 1 262 ? 8.060   45.253  17.665  1.00 33.49 ? 258 TYR A CD1 1 
ATOM   2035  C CD2 . TYR A 1 262 ? 6.203   46.752  17.560  1.00 33.65 ? 258 TYR A CD2 1 
ATOM   2036  C CE1 . TYR A 1 262 ? 8.130   45.424  19.037  1.00 32.59 ? 258 TYR A CE1 1 
ATOM   2037  C CE2 . TYR A 1 262 ? 6.266   46.929  18.936  1.00 33.00 ? 258 TYR A CE2 1 
ATOM   2038  C CZ  . TYR A 1 262 ? 7.231   46.261  19.663  1.00 32.73 ? 258 TYR A CZ  1 
ATOM   2039  O OH  . TYR A 1 262 ? 7.296   46.429  21.023  1.00 34.19 ? 258 TYR A OH  1 
ATOM   2040  N N   . LYS A 1 263 ? 8.938   45.775  12.631  1.00 36.14 ? 259 LYS A N   1 
ATOM   2041  C CA  . LYS A 1 263 ? 9.019   45.096  11.342  1.00 36.91 ? 259 LYS A CA  1 
ATOM   2042  C C   . LYS A 1 263 ? 8.543   43.662  11.514  1.00 37.22 ? 259 LYS A C   1 
ATOM   2043  O O   . LYS A 1 263 ? 9.046   42.933  12.374  1.00 37.21 ? 259 LYS A O   1 
ATOM   2044  C CB  . LYS A 1 263 ? 10.455  45.089  10.814  1.00 37.02 ? 259 LYS A CB  1 
ATOM   2045  C CG  . LYS A 1 263 ? 10.883  46.357  10.107  1.00 37.71 ? 259 LYS A CG  1 
ATOM   2046  C CD  . LYS A 1 263 ? 12.405  46.553  10.141  1.00 39.22 ? 259 LYS A CD  1 
ATOM   2047  C CE  . LYS A 1 263 ? 13.161  45.485  9.352   1.00 40.22 ? 259 LYS A CE  1 
ATOM   2048  N NZ  . LYS A 1 263 ? 14.622  45.781  9.252   1.00 40.72 ? 259 LYS A NZ  1 
ATOM   2049  N N   . ILE A 1 264 ? 7.558   43.277  10.707  1.00 37.81 ? 260 ILE A N   1 
ATOM   2050  C CA  . ILE A 1 264 ? 7.094   41.893  10.632  1.00 38.24 ? 260 ILE A CA  1 
ATOM   2051  C C   . ILE A 1 264 ? 8.049   41.158  9.684   1.00 38.63 ? 260 ILE A C   1 
ATOM   2052  O O   . ILE A 1 264 ? 7.814   41.098  8.475   1.00 38.53 ? 260 ILE A O   1 
ATOM   2053  C CB  . ILE A 1 264 ? 5.617   41.822  10.135  1.00 38.19 ? 260 ILE A CB  1 
ATOM   2054  C CG1 . ILE A 1 264 ? 4.707   42.674  11.032  1.00 38.28 ? 260 ILE A CG1 1 
ATOM   2055  C CG2 . ILE A 1 264 ? 5.119   40.377  10.069  1.00 37.82 ? 260 ILE A CG2 1 
ATOM   2056  C CD1 . ILE A 1 264 ? 3.333   42.974  10.446  1.00 37.58 ? 260 ILE A CD1 1 
ATOM   2057  N N   . VAL A 1 265 ? 9.143   40.628  10.228  1.00 39.21 ? 261 VAL A N   1 
ATOM   2058  C CA  . VAL A 1 265 ? 10.188  40.037  9.378   1.00 40.01 ? 261 VAL A CA  1 
ATOM   2059  C C   . VAL A 1 265 ? 9.920   38.590  8.959   1.00 40.37 ? 261 VAL A C   1 
ATOM   2060  O O   . VAL A 1 265 ? 10.469  38.124  7.961   1.00 40.59 ? 261 VAL A O   1 
ATOM   2061  C CB  . VAL A 1 265 ? 11.659  40.264  9.925   1.00 40.16 ? 261 VAL A CB  1 
ATOM   2062  C CG1 . VAL A 1 265 ? 11.676  40.564  11.418  1.00 40.53 ? 261 VAL A CG1 1 
ATOM   2063  C CG2 . VAL A 1 265 ? 12.598  39.092  9.569   1.00 39.86 ? 261 VAL A CG2 1 
ATOM   2064  N N   . LYS A 1 266 ? 9.053   37.898  9.696   1.00 40.90 ? 262 LYS A N   1 
ATOM   2065  C CA  . LYS A 1 266 ? 8.777   36.488  9.436   1.00 41.30 ? 262 LYS A CA  1 
ATOM   2066  C C   . LYS A 1 266 ? 7.317   36.127  9.711   1.00 41.44 ? 262 LYS A C   1 
ATOM   2067  O O   . LYS A 1 266 ? 6.858   36.184  10.849  1.00 41.56 ? 262 LYS A O   1 
ATOM   2068  C CB  . LYS A 1 266 ? 9.722   35.619  10.274  1.00 41.32 ? 262 LYS A CB  1 
ATOM   2069  C CG  . LYS A 1 266 ? 9.464   34.126  10.223  1.00 42.71 ? 262 LYS A CG  1 
ATOM   2070  C CD  . LYS A 1 266 ? 10.392  33.414  9.257   1.00 45.04 ? 262 LYS A CD  1 
ATOM   2071  C CE  . LYS A 1 266 ? 10.488  31.933  9.605   1.00 45.97 ? 262 LYS A CE  1 
ATOM   2072  N NZ  . LYS A 1 266 ? 11.369  31.204  8.649   1.00 47.89 ? 262 LYS A NZ  1 
ATOM   2073  N N   . LYS A 1 267 ? 6.596   35.748  8.660   1.00 41.85 ? 263 LYS A N   1 
ATOM   2074  C CA  . LYS A 1 267 ? 5.225   35.257  8.793   1.00 42.26 ? 263 LYS A CA  1 
ATOM   2075  C C   . LYS A 1 267 ? 5.186   33.740  8.648   1.00 42.36 ? 263 LYS A C   1 
ATOM   2076  O O   . LYS A 1 267 ? 5.877   33.177  7.804   1.00 42.66 ? 263 LYS A O   1 
ATOM   2077  C CB  . LYS A 1 267 ? 4.325   35.890  7.734   1.00 42.42 ? 263 LYS A CB  1 
ATOM   2078  C CG  . LYS A 1 267 ? 4.080   37.380  7.905   1.00 43.37 ? 263 LYS A CG  1 
ATOM   2079  C CD  . LYS A 1 267 ? 3.505   38.002  6.637   1.00 45.23 ? 263 LYS A CD  1 
ATOM   2080  C CE  . LYS A 1 267 ? 4.604   38.364  5.638   1.00 47.19 ? 263 LYS A CE  1 
ATOM   2081  N NZ  . LYS A 1 267 ? 5.330   37.170  5.092   1.00 47.89 ? 263 LYS A NZ  1 
ATOM   2082  N N   . GLY A 1 268 ? 4.377   33.078  9.468   1.00 42.48 ? 264 GLY A N   1 
ATOM   2083  C CA  . GLY A 1 268 ? 4.223   31.629  9.380   1.00 42.67 ? 264 GLY A CA  1 
ATOM   2084  C C   . GLY A 1 268 ? 3.218   31.091  10.377  1.00 42.96 ? 264 GLY A C   1 
ATOM   2085  O O   . GLY A 1 268 ? 2.440   31.853  10.954  1.00 43.07 ? 264 GLY A O   1 
ATOM   2086  N N   . ASP A 1 269 A 3.228   29.773  10.568  1.00 43.20 ? 264 ASP A N   1 
ATOM   2087  C CA  . ASP A 1 269 A 2.389   29.132  11.577  1.00 43.41 ? 264 ASP A CA  1 
ATOM   2088  C C   . ASP A 1 269 A 2.903   29.470  12.962  1.00 43.13 ? 264 ASP A C   1 
ATOM   2089  O O   . ASP A 1 269 A 4.076   29.238  13.279  1.00 43.24 ? 264 ASP A O   1 
ATOM   2090  C CB  . ASP A 1 269 A 2.355   27.609  11.392  1.00 43.81 ? 264 ASP A CB  1 
ATOM   2091  C CG  . ASP A 1 269 A 1.333   27.157  10.348  1.00 45.24 ? 264 ASP A CG  1 
ATOM   2092  O OD1 . ASP A 1 269 A 1.469   26.018  9.840   1.00 46.46 ? 264 ASP A OD1 1 
ATOM   2093  O OD2 . ASP A 1 269 A 0.392   27.929  10.041  1.00 46.43 ? 264 ASP A OD2 1 
ATOM   2094  N N   . SER A 1 270 ? 2.022   30.046  13.773  1.00 42.70 ? 265 SER A N   1 
ATOM   2095  C CA  . SER A 1 270 ? 2.322   30.346  15.164  1.00 42.26 ? 265 SER A CA  1 
ATOM   2096  C C   . SER A 1 270 ? 1.035   30.277  15.965  1.00 41.88 ? 265 SER A C   1 
ATOM   2097  O O   . SER A 1 270 ? -0.025  29.999  15.412  1.00 42.05 ? 265 SER A O   1 
ATOM   2098  C CB  . SER A 1 270 ? 2.981   31.723  15.302  1.00 42.32 ? 265 SER A CB  1 
ATOM   2099  O OG  . SER A 1 270 ? 3.503   31.909  16.609  1.00 42.26 ? 265 SER A OG  1 
ATOM   2100  N N   . ALA A 1 271 ? 1.135   30.522  17.266  1.00 41.43 ? 266 ALA A N   1 
ATOM   2101  C CA  . ALA A 1 271 ? -0.009  30.465  18.159  1.00 41.09 ? 266 ALA A CA  1 
ATOM   2102  C C   . ALA A 1 271 ? 0.218   31.319  19.398  1.00 40.90 ? 266 ALA A C   1 
ATOM   2103  O O   . ALA A 1 271 ? 1.357   31.503  19.830  1.00 41.01 ? 266 ALA A O   1 
ATOM   2104  C CB  . ALA A 1 271 ? -0.288  29.021  18.562  1.00 41.06 ? 266 ALA A CB  1 
ATOM   2105  N N   . ILE A 1 272 ? -0.874  31.851  19.946  1.00 40.74 ? 267 ILE A N   1 
ATOM   2106  C CA  . ILE A 1 272 ? -0.878  32.443  21.283  1.00 40.51 ? 267 ILE A CA  1 
ATOM   2107  C C   . ILE A 1 272 ? -1.479  31.407  22.230  1.00 40.36 ? 267 ILE A C   1 
ATOM   2108  O O   . ILE A 1 272 ? -2.701  31.267  22.329  1.00 40.26 ? 267 ILE A O   1 
ATOM   2109  C CB  . ILE A 1 272 ? -1.713  33.751  21.378  1.00 40.58 ? 267 ILE A CB  1 
ATOM   2110  C CG1 . ILE A 1 272 ? -1.414  34.707  20.211  1.00 40.28 ? 267 ILE A CG1 1 
ATOM   2111  C CG2 . ILE A 1 272 ? -1.524  34.407  22.760  1.00 40.60 ? 267 ILE A CG2 1 
ATOM   2112  C CD1 . ILE A 1 272 ? -0.507  35.859  20.539  1.00 39.62 ? 267 ILE A CD1 1 
ATOM   2113  N N   . MET A 1 273 ? -0.605  30.687  22.917  1.00 40.31 ? 268 MET A N   1 
ATOM   2114  C CA  . MET A 1 273 ? -1.004  29.633  23.830  1.00 40.41 ? 268 MET A CA  1 
ATOM   2115  C C   . MET A 1 273 ? -1.322  30.196  25.211  1.00 40.29 ? 268 MET A C   1 
ATOM   2116  O O   . MET A 1 273 ? -0.570  31.007  25.753  1.00 40.29 ? 268 MET A O   1 
ATOM   2117  C CB  . MET A 1 273 ? 0.117   28.610  23.918  1.00 40.60 ? 268 MET A CB  1 
ATOM   2118  C CG  . MET A 1 273 ? -0.259  27.306  24.568  1.00 41.92 ? 268 MET A CG  1 
ATOM   2119  S SD  . MET A 1 273 ? 0.994   26.055  24.238  1.00 44.09 ? 268 MET A SD  1 
ATOM   2120  C CE  . MET A 1 273 ? 0.714   25.727  22.493  1.00 43.30 ? 268 MET A CE  1 
ATOM   2121  N N   . LYS A 1 274 ? -2.444  29.759  25.774  1.00 40.32 ? 269 LYS A N   1 
ATOM   2122  C CA  . LYS A 1 274 ? -2.859  30.184  27.108  1.00 40.42 ? 269 LYS A CA  1 
ATOM   2123  C C   . LYS A 1 274 ? -2.479  29.124  28.132  1.00 40.31 ? 269 LYS A C   1 
ATOM   2124  O O   . LYS A 1 274 ? -2.991  28.002  28.101  1.00 40.19 ? 269 LYS A O   1 
ATOM   2125  C CB  . LYS A 1 274 ? -4.367  30.478  27.153  1.00 40.61 ? 269 LYS A CB  1 
ATOM   2126  C CG  . LYS A 1 274 ? -4.860  31.479  26.095  1.00 41.18 ? 269 LYS A CG  1 
ATOM   2127  C CD  . LYS A 1 274 ? -4.220  32.866  26.247  1.00 42.58 ? 269 LYS A CD  1 
ATOM   2128  C CE  . LYS A 1 274 ? -4.855  33.669  27.379  1.00 43.58 ? 269 LYS A CE  1 
ATOM   2129  N NZ  . LYS A 1 274 ? -4.155  34.964  27.599  1.00 43.84 ? 269 LYS A NZ  1 
ATOM   2130  N N   . SER A 1 275 ? -1.565  29.491  29.028  1.00 40.27 ? 270 SER A N   1 
ATOM   2131  C CA  . SER A 1 275 ? -0.994  28.562  30.000  1.00 40.26 ? 270 SER A CA  1 
ATOM   2132  C C   . SER A 1 275 ? -0.347  29.290  31.178  1.00 40.32 ? 270 SER A C   1 
ATOM   2133  O O   . SER A 1 275 ? 0.230   30.367  31.017  1.00 39.84 ? 270 SER A O   1 
ATOM   2134  C CB  . SER A 1 275 ? 0.037   27.657  29.324  1.00 40.16 ? 270 SER A CB  1 
ATOM   2135  O OG  . SER A 1 275 ? 0.724   26.874  30.278  1.00 40.25 ? 270 SER A OG  1 
ATOM   2136  N N   . GLU A 1 276 ? -0.450  28.683  32.358  1.00 40.70 ? 271 GLU A N   1 
ATOM   2137  C CA  . GLU A 1 276 ? 0.144   29.232  33.575  1.00 41.31 ? 271 GLU A CA  1 
ATOM   2138  C C   . GLU A 1 276 ? 1.543   28.659  33.840  1.00 41.48 ? 271 GLU A C   1 
ATOM   2139  O O   . GLU A 1 276 ? 2.203   29.045  34.804  1.00 41.61 ? 271 GLU A O   1 
ATOM   2140  C CB  . GLU A 1 276 ? -0.772  29.007  34.785  1.00 41.33 ? 271 GLU A CB  1 
ATOM   2141  C CG  . GLU A 1 276 ? -2.183  29.601  34.659  1.00 42.43 ? 271 GLU A CG  1 
ATOM   2142  C CD  . GLU A 1 276 ? -2.198  31.095  34.342  1.00 43.97 ? 271 GLU A CD  1 
ATOM   2143  O OE1 . GLU A 1 276 ? -1.590  31.884  35.101  1.00 44.66 ? 271 GLU A OE1 1 
ATOM   2144  O OE2 . GLU A 1 276 ? -2.830  31.478  33.331  1.00 44.03 ? 271 GLU A OE2 1 
ATOM   2145  N N   . LEU A 1 277 ? 1.979   27.740  32.977  1.00 41.63 ? 272 LEU A N   1 
ATOM   2146  C CA  . LEU A 1 277 ? 3.328   27.172  33.020  1.00 41.69 ? 272 LEU A CA  1 
ATOM   2147  C C   . LEU A 1 277 ? 4.373   28.140  32.476  1.00 41.78 ? 272 LEU A C   1 
ATOM   2148  O O   . LEU A 1 277 ? 4.033   29.180  31.908  1.00 41.82 ? 272 LEU A O   1 
ATOM   2149  C CB  . LEU A 1 277 ? 3.379   25.877  32.205  1.00 41.62 ? 272 LEU A CB  1 
ATOM   2150  C CG  . LEU A 1 277 ? 3.241   24.498  32.859  1.00 41.98 ? 272 LEU A CG  1 
ATOM   2151  C CD1 . LEU A 1 277 ? 2.268   24.469  34.041  1.00 41.63 ? 272 LEU A CD1 1 
ATOM   2152  C CD2 . LEU A 1 277 ? 2.845   23.471  31.788  1.00 41.79 ? 272 LEU A CD2 1 
ATOM   2153  N N   . GLU A 1 278 ? 5.643   27.781  32.653  1.00 42.07 ? 273 GLU A N   1 
ATOM   2154  C CA  . GLU A 1 278 ? 6.770   28.517  32.067  1.00 42.24 ? 273 GLU A CA  1 
ATOM   2155  C C   . GLU A 1 278 ? 7.832   27.569  31.481  1.00 41.89 ? 273 GLU A C   1 
ATOM   2156  O O   . GLU A 1 278 ? 7.639   26.351  31.460  1.00 41.60 ? 273 GLU A O   1 
ATOM   2157  C CB  . GLU A 1 278 ? 7.370   29.503  33.080  1.00 42.55 ? 273 GLU A CB  1 
ATOM   2158  C CG  . GLU A 1 278 ? 6.699   30.879  33.047  1.00 43.67 ? 273 GLU A CG  1 
ATOM   2159  C CD  . GLU A 1 278 ? 6.962   31.720  34.286  1.00 45.59 ? 273 GLU A CD  1 
ATOM   2160  O OE1 . GLU A 1 278 ? 5.987   32.298  34.815  1.00 46.01 ? 273 GLU A OE1 1 
ATOM   2161  O OE2 . GLU A 1 278 ? 8.132   31.811  34.730  1.00 46.42 ? 273 GLU A OE2 1 
ATOM   2162  N N   . TYR A 1 279 ? 8.941   28.141  31.010  1.00 41.63 ? 274 TYR A N   1 
ATOM   2163  C CA  . TYR A 1 279 ? 9.950   27.422  30.227  1.00 41.38 ? 274 TYR A CA  1 
ATOM   2164  C C   . TYR A 1 279 ? 10.556  26.213  30.942  1.00 41.60 ? 274 TYR A C   1 
ATOM   2165  O O   . TYR A 1 279 ? 10.949  26.296  32.109  1.00 41.63 ? 274 TYR A O   1 
ATOM   2166  C CB  . TYR A 1 279 ? 11.047  28.390  29.787  1.00 41.15 ? 274 TYR A CB  1 
ATOM   2167  C CG  . TYR A 1 279 ? 11.904  27.910  28.636  1.00 40.89 ? 274 TYR A CG  1 
ATOM   2168  C CD1 . TYR A 1 279 ? 11.329  27.403  27.468  1.00 40.53 ? 274 TYR A CD1 1 
ATOM   2169  C CD2 . TYR A 1 279 ? 13.295  28.000  28.700  1.00 40.58 ? 274 TYR A CD2 1 
ATOM   2170  C CE1 . TYR A 1 279 ? 12.120  26.976  26.406  1.00 40.19 ? 274 TYR A CE1 1 
ATOM   2171  C CE2 . TYR A 1 279 ? 14.092  27.582  27.645  1.00 40.10 ? 274 TYR A CE2 1 
ATOM   2172  C CZ  . TYR A 1 279 ? 13.501  27.072  26.501  1.00 40.05 ? 274 TYR A CZ  1 
ATOM   2173  O OH  . TYR A 1 279 ? 14.295  26.656  25.458  1.00 38.90 ? 274 TYR A OH  1 
ATOM   2174  N N   . GLY A 1 280 ? 10.625  25.089  30.230  1.00 41.65 ? 275 GLY A N   1 
ATOM   2175  C CA  . GLY A 1 280 ? 11.121  23.842  30.803  1.00 41.70 ? 275 GLY A CA  1 
ATOM   2176  C C   . GLY A 1 280 ? 12.486  23.395  30.313  1.00 41.75 ? 275 GLY A C   1 
ATOM   2177  O O   . GLY A 1 280 ? 12.989  22.365  30.763  1.00 41.73 ? 275 GLY A O   1 
ATOM   2178  N N   . ASN A 1 281 ? 13.081  24.163  29.397  1.00 41.83 ? 276 ASN A N   1 
ATOM   2179  C CA  . ASN A 1 281 ? 14.418  23.870  28.847  1.00 42.05 ? 276 ASN A CA  1 
ATOM   2180  C C   . ASN A 1 281 ? 14.501  22.541  28.086  1.00 42.10 ? 276 ASN A C   1 
ATOM   2181  O O   . ASN A 1 281 ? 15.398  21.733  28.316  1.00 42.18 ? 276 ASN A O   1 
ATOM   2182  C CB  . ASN A 1 281 ? 15.495  23.930  29.947  1.00 41.98 ? 276 ASN A CB  1 
ATOM   2183  C CG  . ASN A 1 281 ? 15.585  25.293  30.606  1.00 41.94 ? 276 ASN A CG  1 
ATOM   2184  O OD1 . ASN A 1 281 ? 15.158  25.473  31.743  1.00 42.26 ? 276 ASN A OD1 1 
ATOM   2185  N ND2 . ASN A 1 281 ? 16.134  26.262  29.889  1.00 42.08 ? 276 ASN A ND2 1 
ATOM   2186  N N   . CYS A 1 282 ? 13.563  22.338  27.170  1.00 42.30 ? 277 CYS A N   1 
ATOM   2187  C CA  . CYS A 1 282 ? 13.432  21.082  26.442  1.00 42.55 ? 277 CYS A CA  1 
ATOM   2188  C C   . CYS A 1 282 ? 13.184  21.347  24.965  1.00 42.48 ? 277 CYS A C   1 
ATOM   2189  O O   . CYS A 1 282 ? 13.056  22.501  24.543  1.00 42.57 ? 277 CYS A O   1 
ATOM   2190  C CB  . CYS A 1 282 ? 12.279  20.253  27.026  1.00 42.53 ? 277 CYS A CB  1 
ATOM   2191  S SG  . CYS A 1 282 ? 10.828  21.251  27.568  1.00 44.13 ? 277 CYS A SG  1 
ATOM   2192  N N   . ASN A 1 283 ? 13.124  20.273  24.185  1.00 42.46 ? 278 ASN A N   1 
ATOM   2193  C CA  . ASN A 1 283 ? 12.768  20.350  22.774  1.00 42.44 ? 278 ASN A CA  1 
ATOM   2194  C C   . ASN A 1 283 ? 11.654  19.345  22.482  1.00 42.34 ? 278 ASN A C   1 
ATOM   2195  O O   . ASN A 1 283 ? 11.589  18.283  23.111  1.00 42.40 ? 278 ASN A O   1 
ATOM   2196  C CB  . ASN A 1 283 ? 13.997  20.077  21.896  1.00 42.46 ? 278 ASN A CB  1 
ATOM   2197  C CG  . ASN A 1 283 ? 13.861  20.648  20.483  1.00 43.10 ? 278 ASN A CG  1 
ATOM   2198  O OD1 . ASN A 1 283 ? 13.004  21.493  20.214  1.00 44.18 ? 278 ASN A OD1 1 
ATOM   2199  N ND2 . ASN A 1 283 ? 14.719  20.190  19.577  1.00 43.38 ? 278 ASN A ND2 1 
ATOM   2200  N N   . THR A 1 284 ? 10.770  19.689  21.547  1.00 42.14 ? 279 THR A N   1 
ATOM   2201  C CA  . THR A 1 284 ? 9.667   18.799  21.156  1.00 41.90 ? 279 THR A CA  1 
ATOM   2202  C C   . THR A 1 284 ? 9.193   19.025  19.720  1.00 41.79 ? 279 THR A C   1 
ATOM   2203  O O   . THR A 1 284 ? 9.546   20.028  19.087  1.00 41.63 ? 279 THR A O   1 
ATOM   2204  C CB  . THR A 1 284 ? 8.454   18.928  22.110  1.00 41.98 ? 279 THR A CB  1 
ATOM   2205  O OG1 . THR A 1 284 ? 7.509   17.891  21.822  1.00 42.30 ? 279 THR A OG1 1 
ATOM   2206  C CG2 . THR A 1 284 ? 7.768   20.298  21.966  1.00 41.57 ? 279 THR A CG2 1 
ATOM   2207  N N   . LYS A 1 285 ? 8.394   18.084  19.220  1.00 41.64 ? 280 LYS A N   1 
ATOM   2208  C CA  . LYS A 1 285 ? 7.702   18.255  17.942  1.00 41.74 ? 280 LYS A CA  1 
ATOM   2209  C C   . LYS A 1 285 ? 6.220   18.589  18.125  1.00 41.22 ? 280 LYS A C   1 
ATOM   2210  O O   . LYS A 1 285 ? 5.563   19.045  17.187  1.00 41.15 ? 280 LYS A O   1 
ATOM   2211  C CB  . LYS A 1 285 ? 7.871   17.023  17.041  1.00 42.05 ? 280 LYS A CB  1 
ATOM   2212  C CG  . LYS A 1 285 ? 9.212   16.968  16.302  1.00 43.29 ? 280 LYS A CG  1 
ATOM   2213  C CD  . LYS A 1 285 ? 9.022   16.757  14.791  1.00 45.24 ? 280 LYS A CD  1 
ATOM   2214  C CE  . LYS A 1 285 ? 8.698   15.303  14.428  1.00 46.47 ? 280 LYS A CE  1 
ATOM   2215  N NZ  . LYS A 1 285 ? 9.920   14.452  14.292  1.00 47.40 ? 280 LYS A NZ  1 
ATOM   2216  N N   . CYS A 1 286 ? 5.709   18.368  19.337  1.00 40.86 ? 281 CYS A N   1 
ATOM   2217  C CA  . CYS A 1 286 ? 4.298   18.598  19.658  1.00 40.46 ? 281 CYS A CA  1 
ATOM   2218  C C   . CYS A 1 286 ? 4.124   19.216  21.044  1.00 39.96 ? 281 CYS A C   1 
ATOM   2219  O O   . CYS A 1 286 ? 4.552   18.642  22.046  1.00 39.83 ? 281 CYS A O   1 
ATOM   2220  C CB  . CYS A 1 286 ? 3.510   17.286  19.570  1.00 40.68 ? 281 CYS A CB  1 
ATOM   2221  S SG  . CYS A 1 286 ? 1.748   17.445  19.965  1.00 41.52 ? 281 CYS A SG  1 
ATOM   2222  N N   . GLN A 1 287 ? 3.470   20.374  21.088  1.00 39.55 ? 282 GLN A N   1 
ATOM   2223  C CA  . GLN A 1 287 ? 3.292   21.132  22.327  1.00 39.06 ? 282 GLN A CA  1 
ATOM   2224  C C   . GLN A 1 287 ? 1.823   21.401  22.658  1.00 39.02 ? 282 GLN A C   1 
ATOM   2225  O O   . GLN A 1 287 ? 1.052   21.817  21.792  1.00 38.94 ? 282 GLN A O   1 
ATOM   2226  C CB  . GLN A 1 287 ? 4.051   22.461  22.237  1.00 38.90 ? 282 GLN A CB  1 
ATOM   2227  C CG  . GLN A 1 287 ? 4.057   23.280  23.524  1.00 38.50 ? 282 GLN A CG  1 
ATOM   2228  C CD  . GLN A 1 287 ? 4.846   22.611  24.640  1.00 37.72 ? 282 GLN A CD  1 
ATOM   2229  O OE1 . GLN A 1 287 ? 6.058   22.438  24.544  1.00 36.78 ? 282 GLN A OE1 1 
ATOM   2230  N NE2 . GLN A 1 287 ? 4.155   22.232  25.702  1.00 38.04 ? 282 GLN A NE2 1 
ATOM   2231  N N   . THR A 1 288 ? 1.447   21.156  23.912  1.00 39.01 ? 283 THR A N   1 
ATOM   2232  C CA  . THR A 1 288 ? 0.140   21.566  24.435  1.00 39.30 ? 283 THR A CA  1 
ATOM   2233  C C   . THR A 1 288 ? 0.355   22.559  25.585  1.00 39.55 ? 283 THR A C   1 
ATOM   2234  O O   . THR A 1 288 ? 1.467   22.650  26.107  1.00 39.55 ? 283 THR A O   1 
ATOM   2235  C CB  . THR A 1 288 ? -0.711  20.370  24.943  1.00 39.19 ? 283 THR A CB  1 
ATOM   2236  O OG1 . THR A 1 288 ? -0.349  20.051  26.295  1.00 39.10 ? 283 THR A OG1 1 
ATOM   2237  C CG2 . THR A 1 288 ? -0.548  19.149  24.055  1.00 38.87 ? 283 THR A CG2 1 
ATOM   2238  N N   . PRO A 1 289 ? -0.704  23.300  25.989  1.00 39.79 ? 284 PRO A N   1 
ATOM   2239  C CA  . PRO A 1 289 ? -0.607  24.221  27.134  1.00 39.96 ? 284 PRO A CA  1 
ATOM   2240  C C   . PRO A 1 289 ? -0.354  23.510  28.469  1.00 40.18 ? 284 PRO A C   1 
ATOM   2241  O O   . PRO A 1 289 ? -0.038  24.164  29.462  1.00 40.06 ? 284 PRO A O   1 
ATOM   2242  C CB  . PRO A 1 289 ? -1.983  24.898  27.160  1.00 39.88 ? 284 PRO A CB  1 
ATOM   2243  C CG  . PRO A 1 289 ? -2.556  24.676  25.803  1.00 39.76 ? 284 PRO A CG  1 
ATOM   2244  C CD  . PRO A 1 289 ? -2.040  23.356  25.366  1.00 39.69 ? 284 PRO A CD  1 
ATOM   2245  N N   . MET A 1 290 ? -0.498  22.186  28.477  1.00 40.56 ? 285 MET A N   1 
ATOM   2246  C CA  . MET A 1 290 ? -0.288  21.369  29.669  1.00 41.17 ? 285 MET A CA  1 
ATOM   2247  C C   . MET A 1 290 ? 1.075   20.683  29.685  1.00 40.79 ? 285 MET A C   1 
ATOM   2248  O O   . MET A 1 290 ? 1.507   20.185  30.719  1.00 40.76 ? 285 MET A O   1 
ATOM   2249  C CB  . MET A 1 290 ? -1.379  20.306  29.777  1.00 41.69 ? 285 MET A CB  1 
ATOM   2250  C CG  . MET A 1 290 ? -2.659  20.788  30.423  1.00 44.18 ? 285 MET A CG  1 
ATOM   2251  S SD  . MET A 1 290 ? -3.830  19.425  30.562  1.00 50.05 ? 285 MET A SD  1 
ATOM   2252  C CE  . MET A 1 290 ? -4.664  19.855  32.098  1.00 49.89 ? 285 MET A CE  1 
ATOM   2253  N N   . GLY A 1 291 ? 1.743   20.656  28.538  1.00 40.65 ? 286 GLY A N   1 
ATOM   2254  C CA  . GLY A 1 291 ? 3.029   19.981  28.403  1.00 40.45 ? 286 GLY A CA  1 
ATOM   2255  C C   . GLY A 1 291 ? 3.232   19.431  27.007  1.00 40.45 ? 286 GLY A C   1 
ATOM   2256  O O   . GLY A 1 291 ? 2.334   19.514  26.161  1.00 40.32 ? 286 GLY A O   1 
ATOM   2257  N N   . ALA A 1 292 ? 4.413   18.863  26.772  1.00 40.40 ? 287 ALA A N   1 
ATOM   2258  C CA  . ALA A 1 292 ? 4.793   18.348  25.460  1.00 40.41 ? 287 ALA A CA  1 
ATOM   2259  C C   . ALA A 1 292 ? 4.511   16.857  25.315  1.00 40.45 ? 287 ALA A C   1 
ATOM   2260  O O   . ALA A 1 292 ? 4.440   16.133  26.306  1.00 40.26 ? 287 ALA A O   1 
ATOM   2261  C CB  . ALA A 1 292 ? 6.261   18.638  25.185  1.00 40.49 ? 287 ALA A CB  1 
ATOM   2262  N N   . ILE A 1 293 ? 4.367   16.414  24.067  1.00 40.65 ? 288 ILE A N   1 
ATOM   2263  C CA  . ILE A 1 293 ? 4.105   15.015  23.740  1.00 40.96 ? 288 ILE A CA  1 
ATOM   2264  C C   . ILE A 1 293 ? 5.257   14.431  22.923  1.00 41.34 ? 288 ILE A C   1 
ATOM   2265  O O   . ILE A 1 293 ? 5.722   15.049  21.962  1.00 41.44 ? 288 ILE A O   1 
ATOM   2266  C CB  . ILE A 1 293 ? 2.782   14.869  22.945  1.00 41.00 ? 288 ILE A CB  1 
ATOM   2267  C CG1 . ILE A 1 293 ? 1.581   15.201  23.837  1.00 41.11 ? 288 ILE A CG1 1 
ATOM   2268  C CG2 . ILE A 1 293 ? 2.641   13.465  22.353  1.00 40.83 ? 288 ILE A CG2 1 
ATOM   2269  C CD1 . ILE A 1 293 ? 0.347   15.639  23.062  1.00 41.14 ? 288 ILE A CD1 1 
ATOM   2270  N N   . ASN A 1 294 ? 5.721   13.247  23.323  1.00 41.72 ? 289 ASN A N   1 
ATOM   2271  C CA  . ASN A 1 294 ? 6.685   12.476  22.542  1.00 42.14 ? 289 ASN A CA  1 
ATOM   2272  C C   . ASN A 1 294 ? 6.088   11.099  22.273  1.00 42.18 ? 289 ASN A C   1 
ATOM   2273  O O   . ASN A 1 294 ? 6.100   10.220  23.138  1.00 42.00 ? 289 ASN A O   1 
ATOM   2274  C CB  . ASN A 1 294 ? 8.030   12.368  23.277  1.00 42.37 ? 289 ASN A CB  1 
ATOM   2275  C CG  . ASN A 1 294 ? 9.169   11.885  22.372  1.00 43.10 ? 289 ASN A CG  1 
ATOM   2276  O OD1 . ASN A 1 294 ? 10.101  11.223  22.834  1.00 44.79 ? 289 ASN A OD1 1 
ATOM   2277  N ND2 . ASN A 1 294 ? 9.098   12.218  21.086  1.00 43.24 ? 289 ASN A ND2 1 
ATOM   2278  N N   . SER A 1 295 ? 5.536   10.923  21.077  1.00 42.41 ? 290 SER A N   1 
ATOM   2279  C CA  . SER A 1 295 ? 4.718   9.747   20.797  1.00 42.60 ? 290 SER A CA  1 
ATOM   2280  C C   . SER A 1 295 ? 4.689   9.345   19.333  1.00 42.59 ? 290 SER A C   1 
ATOM   2281  O O   . SER A 1 295 ? 4.669   10.187  18.435  1.00 42.48 ? 290 SER A O   1 
ATOM   2282  C CB  . SER A 1 295 ? 3.286   9.969   21.289  1.00 42.64 ? 290 SER A CB  1 
ATOM   2283  O OG  . SER A 1 295 ? 2.674   8.742   21.645  1.00 42.97 ? 290 SER A OG  1 
ATOM   2284  N N   . SER A 1 296 ? 4.681   8.035   19.120  1.00 42.77 ? 291 SER A N   1 
ATOM   2285  C CA  . SER A 1 296 ? 4.539   7.437   17.798  1.00 42.82 ? 291 SER A CA  1 
ATOM   2286  C C   . SER A 1 296 ? 3.071   7.076   17.567  1.00 42.57 ? 291 SER A C   1 
ATOM   2287  O O   . SER A 1 296 ? 2.700   6.568   16.511  1.00 42.49 ? 291 SER A O   1 
ATOM   2288  C CB  . SER A 1 296 ? 5.439   6.197   17.703  1.00 42.89 ? 291 SER A CB  1 
ATOM   2289  O OG  . SER A 1 296 ? 4.748   5.087   17.154  1.00 43.48 ? 291 SER A OG  1 
ATOM   2290  N N   . MET A 1 297 ? 2.254   7.371   18.576  1.00 42.43 ? 292 MET A N   1 
ATOM   2291  C CA  . MET A 1 297 ? 0.834   7.046   18.623  1.00 42.19 ? 292 MET A CA  1 
ATOM   2292  C C   . MET A 1 297 ? 0.059   7.919   17.635  1.00 41.78 ? 292 MET A C   1 
ATOM   2293  O O   . MET A 1 297 ? 0.486   9.037   17.342  1.00 41.83 ? 292 MET A O   1 
ATOM   2294  C CB  . MET A 1 297 ? 0.330   7.310   20.042  1.00 42.40 ? 292 MET A CB  1 
ATOM   2295  C CG  . MET A 1 297 ? -0.496  6.208   20.673  1.00 43.29 ? 292 MET A CG  1 
ATOM   2296  S SD  . MET A 1 297 ? 0.384   4.661   20.938  1.00 45.41 ? 292 MET A SD  1 
ATOM   2297  C CE  . MET A 1 297 ? -0.315  4.132   22.502  1.00 44.27 ? 292 MET A CE  1 
ATOM   2298  N N   . PRO A 1 298 ? -1.075  7.411   17.104  1.00 41.33 ? 293 PRO A N   1 
ATOM   2299  C CA  . PRO A 1 298 ? -1.896  8.229   16.201  1.00 40.74 ? 293 PRO A CA  1 
ATOM   2300  C C   . PRO A 1 298 ? -2.900  9.154   16.905  1.00 40.14 ? 293 PRO A C   1 
ATOM   2301  O O   . PRO A 1 298 ? -3.344  10.134  16.305  1.00 40.28 ? 293 PRO A O   1 
ATOM   2302  C CB  . PRO A 1 298 ? -2.631  7.184   15.356  1.00 40.78 ? 293 PRO A CB  1 
ATOM   2303  C CG  . PRO A 1 298 ? -2.736  6.000   16.235  1.00 40.98 ? 293 PRO A CG  1 
ATOM   2304  C CD  . PRO A 1 298 ? -1.521  6.002   17.126  1.00 41.18 ? 293 PRO A CD  1 
ATOM   2305  N N   . PHE A 1 299 ? -3.255  8.843   18.151  1.00 39.29 ? 294 PHE A N   1 
ATOM   2306  C CA  . PHE A 1 299 ? -4.190  9.661   18.929  1.00 38.57 ? 294 PHE A CA  1 
ATOM   2307  C C   . PHE A 1 299 ? -3.637  10.062  20.305  1.00 38.09 ? 294 PHE A C   1 
ATOM   2308  O O   . PHE A 1 299 ? -2.788  9.365   20.875  1.00 37.86 ? 294 PHE A O   1 
ATOM   2309  C CB  . PHE A 1 299 ? -5.511  8.919   19.151  1.00 38.73 ? 294 PHE A CB  1 
ATOM   2310  C CG  . PHE A 1 299 ? -6.264  8.603   17.894  1.00 39.07 ? 294 PHE A CG  1 
ATOM   2311  C CD1 . PHE A 1 299 ? -7.062  9.568   17.282  1.00 39.11 ? 294 PHE A CD1 1 
ATOM   2312  C CD2 . PHE A 1 299 ? -6.201  7.330   17.337  1.00 39.49 ? 294 PHE A CD2 1 
ATOM   2313  C CE1 . PHE A 1 299 ? -7.765  9.277   16.126  1.00 39.43 ? 294 PHE A CE1 1 
ATOM   2314  C CE2 . PHE A 1 299 ? -6.903  7.027   16.181  1.00 39.95 ? 294 PHE A CE2 1 
ATOM   2315  C CZ  . PHE A 1 299 ? -7.688  8.005   15.573  1.00 40.00 ? 294 PHE A CZ  1 
ATOM   2316  N N   . HIS A 1 300 ? -4.139  11.181  20.831  1.00 37.24 ? 295 HIS A N   1 
ATOM   2317  C CA  . HIS A 1 300 ? -3.867  11.601  22.205  1.00 36.59 ? 295 HIS A CA  1 
ATOM   2318  C C   . HIS A 1 300 ? -5.110  12.246  22.817  1.00 36.18 ? 295 HIS A C   1 
ATOM   2319  O O   . HIS A 1 300 ? -6.028  12.631  22.100  1.00 36.11 ? 295 HIS A O   1 
ATOM   2320  C CB  . HIS A 1 300 ? -2.680  12.571  22.262  1.00 36.61 ? 295 HIS A CB  1 
ATOM   2321  C CG  . HIS A 1 300 ? -3.029  13.983  21.899  1.00 36.23 ? 295 HIS A CG  1 
ATOM   2322  N ND1 . HIS A 1 300 ? -2.991  14.452  20.602  1.00 35.15 ? 295 HIS A ND1 1 
ATOM   2323  C CD2 . HIS A 1 300 ? -3.423  15.028  22.666  1.00 35.64 ? 295 HIS A CD2 1 
ATOM   2324  C CE1 . HIS A 1 300 ? -3.345  15.725  20.587  1.00 35.01 ? 295 HIS A CE1 1 
ATOM   2325  N NE2 . HIS A 1 300 ? -3.614  16.098  21.826  1.00 35.53 ? 295 HIS A NE2 1 
ATOM   2326  N N   . ASN A 1 301 ? -5.131  12.368  24.138  1.00 35.75 ? 296 ASN A N   1 
ATOM   2327  C CA  . ASN A 1 301 ? -6.250  12.998  24.832  1.00 35.64 ? 296 ASN A CA  1 
ATOM   2328  C C   . ASN A 1 301 ? -5.803  14.088  25.809  1.00 35.52 ? 296 ASN A C   1 
ATOM   2329  O O   . ASN A 1 301 ? -6.503  14.391  26.772  1.00 35.53 ? 296 ASN A O   1 
ATOM   2330  C CB  . ASN A 1 301 ? -7.087  11.940  25.562  1.00 35.62 ? 296 ASN A CB  1 
ATOM   2331  C CG  . ASN A 1 301 ? -6.314  11.240  26.669  1.00 35.85 ? 296 ASN A CG  1 
ATOM   2332  O OD1 . ASN A 1 301 ? -5.085  11.272  26.696  1.00 36.53 ? 296 ASN A OD1 1 
ATOM   2333  N ND2 . ASN A 1 301 ? -7.033  10.604  27.587  1.00 35.40 ? 296 ASN A ND2 1 
ATOM   2334  N N   . ILE A 1 302 ? -4.638  14.674  25.551  1.00 35.43 ? 297 ILE A N   1 
ATOM   2335  C CA  . ILE A 1 302 ? -4.025  15.623  26.477  1.00 35.37 ? 297 ILE A CA  1 
ATOM   2336  C C   . ILE A 1 302 ? -4.792  16.945  26.531  1.00 35.53 ? 297 ILE A C   1 
ATOM   2337  O O   . ILE A 1 302 ? -5.261  17.348  27.594  1.00 35.76 ? 297 ILE A O   1 
ATOM   2338  C CB  . ILE A 1 302 ? -2.522  15.874  26.134  1.00 35.25 ? 297 ILE A CB  1 
ATOM   2339  C CG1 . ILE A 1 302 ? -1.745  14.551  26.015  1.00 35.02 ? 297 ILE A CG1 1 
ATOM   2340  C CG2 . ILE A 1 302 ? -1.872  16.822  27.147  1.00 35.02 ? 297 ILE A CG2 1 
ATOM   2341  C CD1 . ILE A 1 302 ? -1.782  13.658  27.248  1.00 34.83 ? 297 ILE A CD1 1 
ATOM   2342  N N   . HIS A 1 303 ? -4.913  17.601  25.378  1.00 35.53 ? 298 HIS A N   1 
ATOM   2343  C CA  . HIS A 1 303 ? -5.523  18.924  25.257  1.00 35.61 ? 298 HIS A CA  1 
ATOM   2344  C C   . HIS A 1 303 ? -5.784  19.188  23.776  1.00 35.64 ? 298 HIS A C   1 
ATOM   2345  O O   . HIS A 1 303 ? -4.972  18.805  22.928  1.00 35.49 ? 298 HIS A O   1 
ATOM   2346  C CB  . HIS A 1 303 ? -4.594  20.006  25.829  1.00 35.57 ? 298 HIS A CB  1 
ATOM   2347  C CG  . HIS A 1 303 ? -5.273  21.316  26.087  1.00 35.93 ? 298 HIS A CG  1 
ATOM   2348  N ND1 . HIS A 1 303 ? -5.557  22.218  25.083  1.00 36.22 ? 298 HIS A ND1 1 
ATOM   2349  C CD2 . HIS A 1 303 ? -5.725  21.877  27.234  1.00 35.79 ? 298 HIS A CD2 1 
ATOM   2350  C CE1 . HIS A 1 303 ? -6.156  23.277  25.601  1.00 35.94 ? 298 HIS A CE1 1 
ATOM   2351  N NE2 . HIS A 1 303 ? -6.271  23.095  26.904  1.00 36.04 ? 298 HIS A NE2 1 
ATOM   2352  N N   . PRO A 1 304 ? -6.924  19.826  23.452  1.00 35.84 ? 299 PRO A N   1 
ATOM   2353  C CA  . PRO A 1 304 ? -7.275  20.073  22.045  1.00 35.79 ? 299 PRO A CA  1 
ATOM   2354  C C   . PRO A 1 304 ? -6.386  21.084  21.309  1.00 35.99 ? 299 PRO A C   1 
ATOM   2355  O O   . PRO A 1 304 ? -6.185  20.952  20.099  1.00 35.78 ? 299 PRO A O   1 
ATOM   2356  C CB  . PRO A 1 304 ? -8.716  20.583  22.127  1.00 35.78 ? 299 PRO A CB  1 
ATOM   2357  C CG  . PRO A 1 304 ? -8.899  21.031  23.545  1.00 35.75 ? 299 PRO A CG  1 
ATOM   2358  C CD  . PRO A 1 304 ? -8.045  20.133  24.361  1.00 35.79 ? 299 PRO A CD  1 
ATOM   2359  N N   . LEU A 1 305 ? -5.862  22.077  22.028  1.00 36.36 ? 300 LEU A N   1 
ATOM   2360  C CA  . LEU A 1 305 ? -5.088  23.162  21.409  1.00 36.66 ? 300 LEU A CA  1 
ATOM   2361  C C   . LEU A 1 305 ? -3.588  22.877  21.338  1.00 36.82 ? 300 LEU A C   1 
ATOM   2362  O O   . LEU A 1 305 ? -2.830  23.251  22.231  1.00 37.11 ? 300 LEU A O   1 
ATOM   2363  C CB  . LEU A 1 305 ? -5.338  24.487  22.137  1.00 36.75 ? 300 LEU A CB  1 
ATOM   2364  C CG  . LEU A 1 305 ? -6.768  25.028  22.226  1.00 37.22 ? 300 LEU A CG  1 
ATOM   2365  C CD1 . LEU A 1 305 ? -6.772  26.362  22.968  1.00 36.56 ? 300 LEU A CD1 1 
ATOM   2366  C CD2 . LEU A 1 305 ? -7.409  25.165  20.838  1.00 37.41 ? 300 LEU A CD2 1 
ATOM   2367  N N   . THR A 1 306 ? -3.160  22.228  20.262  1.00 36.90 ? 301 THR A N   1 
ATOM   2368  C CA  . THR A 1 306 ? -1.755  21.871  20.100  1.00 36.87 ? 301 THR A CA  1 
ATOM   2369  C C   . THR A 1 306 ? -1.095  22.646  18.959  1.00 36.94 ? 301 THR A C   1 
ATOM   2370  O O   . THR A 1 306 ? -1.776  23.284  18.163  1.00 37.02 ? 301 THR A O   1 
ATOM   2371  C CB  . THR A 1 306 ? -1.586  20.352  19.865  1.00 36.88 ? 301 THR A CB  1 
ATOM   2372  O OG1 . THR A 1 306 ? -2.138  19.994  18.594  1.00 36.63 ? 301 THR A OG1 1 
ATOM   2373  C CG2 . THR A 1 306 ? -2.279  19.560  20.956  1.00 36.69 ? 301 THR A CG2 1 
ATOM   2374  N N   . ILE A 1 307 ? 0.234   22.605  18.907  1.00 37.20 ? 302 ILE A N   1 
ATOM   2375  C CA  . ILE A 1 307 ? 0.992   23.124  17.769  1.00 37.53 ? 302 ILE A CA  1 
ATOM   2376  C C   . ILE A 1 307 ? 2.140   22.174  17.412  1.00 37.89 ? 302 ILE A C   1 
ATOM   2377  O O   . ILE A 1 307 ? 2.758   21.573  18.297  1.00 37.66 ? 302 ILE A O   1 
ATOM   2378  C CB  . ILE A 1 307 ? 1.509   24.584  17.994  1.00 37.61 ? 302 ILE A CB  1 
ATOM   2379  C CG1 . ILE A 1 307 ? 2.214   25.105  16.729  1.00 37.30 ? 302 ILE A CG1 1 
ATOM   2380  C CG2 . ILE A 1 307 ? 2.427   24.675  19.237  1.00 37.80 ? 302 ILE A CG2 1 
ATOM   2381  C CD1 . ILE A 1 307 ? 2.253   26.606  16.578  1.00 37.35 ? 302 ILE A CD1 1 
ATOM   2382  N N   . GLY A 1 308 ? 2.408   22.052  16.114  1.00 38.43 ? 303 GLY A N   1 
ATOM   2383  C CA  . GLY A 1 308 ? 3.453   21.172  15.600  1.00 39.50 ? 303 GLY A CA  1 
ATOM   2384  C C   . GLY A 1 308 ? 2.886   19.869  15.065  1.00 40.15 ? 303 GLY A C   1 
ATOM   2385  O O   . GLY A 1 308 ? 1.678   19.752  14.868  1.00 40.15 ? 303 GLY A O   1 
ATOM   2386  N N   . GLU A 1 309 ? 3.763   18.892  14.835  1.00 41.04 ? 304 GLU A N   1 
ATOM   2387  C CA  . GLU A 1 309 ? 3.367   17.571  14.331  1.00 41.79 ? 304 GLU A CA  1 
ATOM   2388  C C   . GLU A 1 309 ? 2.809   16.714  15.466  1.00 41.78 ? 304 GLU A C   1 
ATOM   2389  O O   . GLU A 1 309 ? 3.552   16.023  16.169  1.00 41.94 ? 304 GLU A O   1 
ATOM   2390  C CB  . GLU A 1 309 ? 4.553   16.875  13.662  1.00 42.08 ? 304 GLU A CB  1 
ATOM   2391  C CG  . GLU A 1 309 ? 4.192   15.612  12.876  1.00 44.32 ? 304 GLU A CG  1 
ATOM   2392  C CD  . GLU A 1 309 ? 5.415   14.923  12.273  1.00 46.95 ? 304 GLU A CD  1 
ATOM   2393  O OE1 . GLU A 1 309 ? 6.413   15.618  11.973  1.00 47.50 ? 304 GLU A OE1 1 
ATOM   2394  O OE2 . GLU A 1 309 ? 5.375   13.682  12.099  1.00 48.48 ? 304 GLU A OE2 1 
ATOM   2395  N N   . CYS A 1 310 ? 1.493   16.768  15.635  1.00 41.79 ? 305 CYS A N   1 
ATOM   2396  C CA  . CYS A 1 310 ? 0.830   16.146  16.772  1.00 41.89 ? 305 CYS A CA  1 
ATOM   2397  C C   . CYS A 1 310 ? -0.066  14.982  16.363  1.00 41.73 ? 305 CYS A C   1 
ATOM   2398  O O   . CYS A 1 310 ? -0.530  14.927  15.225  1.00 41.62 ? 305 CYS A O   1 
ATOM   2399  C CB  . CYS A 1 310 ? 0.004   17.196  17.516  1.00 41.91 ? 305 CYS A CB  1 
ATOM   2400  S SG  . CYS A 1 310 ? 1.007   18.448  18.352  1.00 43.16 ? 305 CYS A SG  1 
ATOM   2401  N N   . PRO A 1 311 ? -0.304  14.036  17.292  1.00 41.69 ? 306 PRO A N   1 
ATOM   2402  C CA  . PRO A 1 311 ? -1.359  13.050  17.057  1.00 41.53 ? 306 PRO A CA  1 
ATOM   2403  C C   . PRO A 1 311 ? -2.730  13.727  17.085  1.00 41.32 ? 306 PRO A C   1 
ATOM   2404  O O   . PRO A 1 311 ? -2.862  14.836  17.610  1.00 41.26 ? 306 PRO A O   1 
ATOM   2405  C CB  . PRO A 1 311 ? -1.215  12.077  18.237  1.00 41.53 ? 306 PRO A CB  1 
ATOM   2406  C CG  . PRO A 1 311 ? -0.403  12.793  19.257  1.00 41.80 ? 306 PRO A CG  1 
ATOM   2407  C CD  . PRO A 1 311 ? 0.465   13.754  18.519  1.00 41.68 ? 306 PRO A CD  1 
ATOM   2408  N N   . LYS A 1 312 ? -3.737  13.070  16.519  1.00 40.95 ? 307 LYS A N   1 
ATOM   2409  C CA  . LYS A 1 312 ? -5.088  13.629  16.504  1.00 40.64 ? 307 LYS A CA  1 
ATOM   2410  C C   . LYS A 1 312 ? -5.719  13.548  17.889  1.00 39.86 ? 307 LYS A C   1 
ATOM   2411  O O   . LYS A 1 312 ? -5.573  12.549  18.585  1.00 39.79 ? 307 LYS A O   1 
ATOM   2412  C CB  . LYS A 1 312 ? -5.962  12.918  15.461  1.00 40.96 ? 307 LYS A CB  1 
ATOM   2413  C CG  . LYS A 1 312 ? -5.349  12.854  14.064  1.00 42.05 ? 307 LYS A CG  1 
ATOM   2414  C CD  . LYS A 1 312 ? -5.200  14.238  13.434  1.00 44.15 ? 307 LYS A CD  1 
ATOM   2415  C CE  . LYS A 1 312 ? -4.314  14.195  12.197  1.00 45.14 ? 307 LYS A CE  1 
ATOM   2416  N NZ  . LYS A 1 312 ? -2.902  13.840  12.547  1.00 45.88 ? 307 LYS A NZ  1 
ATOM   2417  N N   . TYR A 1 313 ? -6.408  14.612  18.286  1.00 39.19 ? 308 TYR A N   1 
ATOM   2418  C CA  . TYR A 1 313 ? -7.015  14.683  19.610  1.00 38.65 ? 308 TYR A CA  1 
ATOM   2419  C C   . TYR A 1 313 ? -8.402  14.053  19.662  1.00 38.64 ? 308 TYR A C   1 
ATOM   2420  O O   . TYR A 1 313 ? -9.235  14.304  18.793  1.00 38.67 ? 308 TYR A O   1 
ATOM   2421  C CB  . TYR A 1 313 ? -7.086  16.135  20.090  1.00 38.35 ? 308 TYR A CB  1 
ATOM   2422  C CG  . TYR A 1 313 ? -7.829  16.301  21.393  1.00 37.35 ? 308 TYR A CG  1 
ATOM   2423  C CD1 . TYR A 1 313 ? -7.190  16.086  22.617  1.00 36.55 ? 308 TYR A CD1 1 
ATOM   2424  C CD2 . TYR A 1 313 ? -9.172  16.659  21.406  1.00 36.50 ? 308 TYR A CD2 1 
ATOM   2425  C CE1 . TYR A 1 313 ? -7.875  16.231  23.823  1.00 35.97 ? 308 TYR A CE1 1 
ATOM   2426  C CE2 . TYR A 1 313 ? -9.866  16.804  22.609  1.00 36.51 ? 308 TYR A CE2 1 
ATOM   2427  C CZ  . TYR A 1 313 ? -9.211  16.592  23.810  1.00 35.76 ? 308 TYR A CZ  1 
ATOM   2428  O OH  . TYR A 1 313 ? -9.896  16.740  24.991  1.00 35.82 ? 308 TYR A OH  1 
ATOM   2429  N N   . VAL A 1 314 ? -8.628  13.233  20.688  1.00 38.78 ? 309 VAL A N   1 
ATOM   2430  C CA  . VAL A 1 314 ? -9.952  12.682  21.019  1.00 38.98 ? 309 VAL A CA  1 
ATOM   2431  C C   . VAL A 1 314 ? -10.191 12.785  22.528  1.00 39.23 ? 309 VAL A C   1 
ATOM   2432  O O   . VAL A 1 314 ? -9.242  12.883  23.301  1.00 39.34 ? 309 VAL A O   1 
ATOM   2433  C CB  . VAL A 1 314 ? -10.130 11.207  20.553  1.00 38.97 ? 309 VAL A CB  1 
ATOM   2434  C CG1 . VAL A 1 314 ? -10.051 11.093  19.030  1.00 38.62 ? 309 VAL A CG1 1 
ATOM   2435  C CG2 . VAL A 1 314 ? -9.110  10.286  21.220  1.00 38.98 ? 309 VAL A CG2 1 
ATOM   2436  N N   . LYS A 1 315 ? -11.454 12.763  22.943  1.00 39.60 ? 310 LYS A N   1 
ATOM   2437  C CA  . LYS A 1 315 ? -11.808 12.924  24.356  1.00 40.06 ? 310 LYS A CA  1 
ATOM   2438  C C   . LYS A 1 315 ? -11.779 11.619  25.157  1.00 40.59 ? 310 LYS A C   1 
ATOM   2439  O O   . LYS A 1 315 ? -12.040 11.622  26.363  1.00 40.84 ? 310 LYS A O   1 
ATOM   2440  C CB  . LYS A 1 315 ? -13.185 13.573  24.489  1.00 40.01 ? 310 LYS A CB  1 
ATOM   2441  C CG  . LYS A 1 315 ? -13.219 15.071  24.276  1.00 39.93 ? 310 LYS A CG  1 
ATOM   2442  C CD  . LYS A 1 315 ? -14.598 15.601  24.624  1.00 40.52 ? 310 LYS A CD  1 
ATOM   2443  C CE  . LYS A 1 315 ? -14.721 17.091  24.377  1.00 41.02 ? 310 LYS A CE  1 
ATOM   2444  N NZ  . LYS A 1 315 ? -16.135 17.532  24.518  1.00 41.40 ? 310 LYS A NZ  1 
ATOM   2445  N N   . SER A 1 316 ? -11.452 10.517  24.485  1.00 41.11 ? 311 SER A N   1 
ATOM   2446  C CA  . SER A 1 316 ? -11.459 9.172   25.070  1.00 41.63 ? 311 SER A CA  1 
ATOM   2447  C C   . SER A 1 316 ? -10.470 8.972   26.225  1.00 42.14 ? 311 SER A C   1 
ATOM   2448  O O   . SER A 1 316 ? -9.474  9.687   26.339  1.00 42.10 ? 311 SER A O   1 
ATOM   2449  C CB  . SER A 1 316 ? -11.160 8.142   23.976  1.00 41.61 ? 311 SER A CB  1 
ATOM   2450  O OG  . SER A 1 316 ? -11.690 8.560   22.728  1.00 41.60 ? 311 SER A OG  1 
ATOM   2451  N N   . ASN A 1 317 ? -10.757 7.985   27.071  1.00 42.88 ? 312 ASN A N   1 
ATOM   2452  C CA  . ASN A 1 317 ? -9.844  7.555   28.129  1.00 43.68 ? 312 ASN A CA  1 
ATOM   2453  C C   . ASN A 1 317 ? -8.979  6.384   27.680  1.00 43.94 ? 312 ASN A C   1 
ATOM   2454  O O   . ASN A 1 317 ? -7.804  6.283   28.041  1.00 44.24 ? 312 ASN A O   1 
ATOM   2455  C CB  . ASN A 1 317 ? -10.627 7.131   29.371  1.00 43.90 ? 312 ASN A CB  1 
ATOM   2456  C CG  . ASN A 1 317 ? -11.370 8.280   30.024  1.00 45.06 ? 312 ASN A CG  1 
ATOM   2457  O OD1 . ASN A 1 317 ? -12.374 8.064   30.705  1.00 46.13 ? 312 ASN A OD1 1 
ATOM   2458  N ND2 . ASN A 1 317 ? -10.878 9.507   29.835  1.00 46.11 ? 312 ASN A ND2 1 
ATOM   2459  N N   . ARG A 1 318 ? -9.589  5.497   26.901  1.00 44.10 ? 313 ARG A N   1 
ATOM   2460  C CA  . ARG A 1 318 ? -8.954  4.281   26.426  1.00 44.23 ? 313 ARG A CA  1 
ATOM   2461  C C   . ARG A 1 318 ? -9.325  4.075   24.971  1.00 43.69 ? 313 ARG A C   1 
ATOM   2462  O O   . ARG A 1 318 ? -10.495 4.176   24.601  1.00 43.62 ? 313 ARG A O   1 
ATOM   2463  C CB  . ARG A 1 318 ? -9.441  3.079   27.238  1.00 44.65 ? 313 ARG A CB  1 
ATOM   2464  C CG  . ARG A 1 318 ? -8.797  2.906   28.613  1.00 46.58 ? 313 ARG A CG  1 
ATOM   2465  C CD  . ARG A 1 318 ? -9.721  2.181   29.599  1.00 49.58 ? 313 ARG A CD  1 
ATOM   2466  N NE  . ARG A 1 318 ? -10.361 0.987   29.033  1.00 52.14 ? 313 ARG A NE  1 
ATOM   2467  C CZ  . ARG A 1 318 ? -11.623 0.930   28.600  1.00 53.27 ? 313 ARG A CZ  1 
ATOM   2468  N NH1 . ARG A 1 318 ? -12.410 2.002   28.657  1.00 53.41 ? 313 ARG A NH1 1 
ATOM   2469  N NH2 . ARG A 1 318 ? -12.101 -0.206  28.102  1.00 53.92 ? 313 ARG A NH2 1 
ATOM   2470  N N   . LEU A 1 319 ? -8.326  3.792   24.145  1.00 43.24 ? 314 LEU A N   1 
ATOM   2471  C CA  . LEU A 1 319 ? -8.570  3.456   22.755  1.00 42.88 ? 314 LEU A CA  1 
ATOM   2472  C C   . LEU A 1 319 ? -7.668  2.291   22.378  1.00 42.67 ? 314 LEU A C   1 
ATOM   2473  O O   . LEU A 1 319 ? -6.519  2.488   21.982  1.00 42.69 ? 314 LEU A O   1 
ATOM   2474  C CB  . LEU A 1 319 ? -8.334  4.674   21.857  1.00 42.85 ? 314 LEU A CB  1 
ATOM   2475  C CG  . LEU A 1 319 ? -9.178  4.815   20.588  1.00 42.72 ? 314 LEU A CG  1 
ATOM   2476  C CD1 . LEU A 1 319 ? -10.668 4.901   20.918  1.00 42.50 ? 314 LEU A CD1 1 
ATOM   2477  C CD2 . LEU A 1 319 ? -8.736  6.038   19.802  1.00 42.12 ? 314 LEU A CD2 1 
ATOM   2478  N N   . VAL A 1 320 ? -8.189  1.075   22.530  1.00 42.42 ? 315 VAL A N   1 
ATOM   2479  C CA  . VAL A 1 320 ? -7.393  -0.133  22.296  1.00 42.38 ? 315 VAL A CA  1 
ATOM   2480  C C   . VAL A 1 320 ? -7.969  -1.027  21.191  1.00 42.36 ? 315 VAL A C   1 
ATOM   2481  O O   . VAL A 1 320 ? -9.140  -1.425  21.227  1.00 42.15 ? 315 VAL A O   1 
ATOM   2482  C CB  . VAL A 1 320 ? -7.085  -0.922  23.624  1.00 42.32 ? 315 VAL A CB  1 
ATOM   2483  C CG1 . VAL A 1 320 ? -8.349  -1.172  24.448  1.00 42.58 ? 315 VAL A CG1 1 
ATOM   2484  C CG2 . VAL A 1 320 ? -6.357  -2.224  23.333  1.00 41.87 ? 315 VAL A CG2 1 
ATOM   2485  N N   . LEU A 1 321 ? -7.113  -1.337  20.219  1.00 42.41 ? 316 LEU A N   1 
ATOM   2486  C CA  . LEU A 1 321 ? -7.495  -2.056  19.011  1.00 42.55 ? 316 LEU A CA  1 
ATOM   2487  C C   . LEU A 1 321 ? -7.064  -3.526  19.062  1.00 42.64 ? 316 LEU A C   1 
ATOM   2488  O O   . LEU A 1 321 ? -5.913  -3.834  19.376  1.00 42.71 ? 316 LEU A O   1 
ATOM   2489  C CB  . LEU A 1 321 ? -6.863  -1.357  17.807  1.00 42.53 ? 316 LEU A CB  1 
ATOM   2490  C CG  . LEU A 1 321 ? -7.469  -1.426  16.407  1.00 42.88 ? 316 LEU A CG  1 
ATOM   2491  C CD1 . LEU A 1 321 ? -8.970  -1.166  16.406  1.00 43.32 ? 316 LEU A CD1 1 
ATOM   2492  C CD2 . LEU A 1 321 ? -6.755  -0.417  15.514  1.00 43.04 ? 316 LEU A CD2 1 
ATOM   2493  N N   . ALA A 1 322 ? -7.995  -4.427  18.756  1.00 42.69 ? 317 ALA A N   1 
ATOM   2494  C CA  . ALA A 1 322 ? -7.716  -5.864  18.730  1.00 42.76 ? 317 ALA A CA  1 
ATOM   2495  C C   . ALA A 1 322 ? -6.933  -6.261  17.482  1.00 42.94 ? 317 ALA A C   1 
ATOM   2496  O O   . ALA A 1 322 ? -7.334  -5.930  16.360  1.00 42.94 ? 317 ALA A O   1 
ATOM   2497  C CB  . ALA A 1 322 ? -9.010  -6.653  18.808  1.00 42.70 ? 317 ALA A CB  1 
ATOM   2498  N N   . THR A 1 323 ? -5.815  -6.960  17.683  1.00 42.98 ? 318 THR A N   1 
ATOM   2499  C CA  . THR A 1 323 ? -5.036  -7.525  16.574  1.00 43.17 ? 318 THR A CA  1 
ATOM   2500  C C   . THR A 1 323 ? -5.113  -9.051  16.575  1.00 43.34 ? 318 THR A C   1 
ATOM   2501  O O   . THR A 1 323 ? -5.310  -9.673  15.528  1.00 43.19 ? 318 THR A O   1 
ATOM   2502  C CB  . THR A 1 323 ? -3.548  -7.092  16.607  1.00 43.19 ? 318 THR A CB  1 
ATOM   2503  O OG1 . THR A 1 323 ? -2.967  -7.461  17.863  1.00 43.07 ? 318 THR A OG1 1 
ATOM   2504  C CG2 . THR A 1 323 ? -3.407  -5.584  16.400  1.00 42.99 ? 318 THR A CG2 1 
ATOM   2505  N N   . GLY A 1 324 ? -4.951  -9.642  17.757  1.00 43.57 ? 319 GLY A N   1 
ATOM   2506  C CA  . GLY A 1 324 ? -5.041  -11.087 17.930  1.00 43.97 ? 319 GLY A CA  1 
ATOM   2507  C C   . GLY A 1 324 ? -6.469  -11.555 18.132  1.00 44.33 ? 319 GLY A C   1 
ATOM   2508  O O   . GLY A 1 324 ? -7.420  -10.838 17.807  1.00 44.57 ? 319 GLY A O   1 
ATOM   2509  N N   . LEU A 1 325 ? -6.619  -12.756 18.682  1.00 44.42 ? 320 LEU A N   1 
ATOM   2510  C CA  . LEU A 1 325 ? -7.929  -13.386 18.825  1.00 44.50 ? 320 LEU A CA  1 
ATOM   2511  C C   . LEU A 1 325 ? -8.346  -13.528 20.282  1.00 44.70 ? 320 LEU A C   1 
ATOM   2512  O O   . LEU A 1 325 ? -7.594  -13.161 21.182  1.00 44.52 ? 320 LEU A O   1 
ATOM   2513  C CB  . LEU A 1 325 ? -7.946  -14.743 18.115  1.00 44.44 ? 320 LEU A CB  1 
ATOM   2514  C CG  . LEU A 1 325 ? -6.730  -15.656 18.270  1.00 44.42 ? 320 LEU A CG  1 
ATOM   2515  C CD1 . LEU A 1 325 ? -6.999  -16.722 19.308  1.00 43.93 ? 320 LEU A CD1 1 
ATOM   2516  C CD2 . LEU A 1 325 ? -6.399  -16.288 16.933  1.00 44.73 ? 320 LEU A CD2 1 
ATOM   2517  N N   . ARG A 1 326 ? -9.553  -14.047 20.498  1.00 45.05 ? 321 ARG A N   1 
ATOM   2518  C CA  . ARG A 1 326 ? -10.081 -14.268 21.839  1.00 45.63 ? 321 ARG A CA  1 
ATOM   2519  C C   . ARG A 1 326 ? -9.188  -15.219 22.633  1.00 46.12 ? 321 ARG A C   1 
ATOM   2520  O O   . ARG A 1 326 ? -8.780  -16.268 22.132  1.00 46.08 ? 321 ARG A O   1 
ATOM   2521  C CB  . ARG A 1 326 ? -11.502 -14.818 21.765  1.00 45.53 ? 321 ARG A CB  1 
ATOM   2522  C CG  . ARG A 1 326 ? -12.267 -14.713 23.066  1.00 45.61 ? 321 ARG A CG  1 
ATOM   2523  C CD  . ARG A 1 326 ? -13.652 -15.317 22.937  1.00 46.49 ? 321 ARG A CD  1 
ATOM   2524  N NE  . ARG A 1 326 ? -14.459 -15.057 24.126  1.00 46.69 ? 321 ARG A NE  1 
ATOM   2525  C CZ  . ARG A 1 326 ? -15.344 -14.070 24.235  1.00 46.57 ? 321 ARG A CZ  1 
ATOM   2526  N NH1 . ARG A 1 326 ? -15.561 -13.236 23.221  1.00 45.46 ? 321 ARG A NH1 1 
ATOM   2527  N NH2 . ARG A 1 326 ? -16.019 -13.923 25.365  1.00 47.18 ? 321 ARG A NH2 1 
ATOM   2528  N N   . ASN A 1 327 ? -8.882  -14.840 23.870  1.00 46.72 ? 322 ASN A N   1 
ATOM   2529  C CA  . ASN A 1 327 ? -7.990  -15.633 24.705  1.00 47.38 ? 322 ASN A CA  1 
ATOM   2530  C C   . ASN A 1 327 ? -8.733  -16.598 25.632  1.00 47.85 ? 322 ASN A C   1 
ATOM   2531  O O   . ASN A 1 327 ? -9.875  -16.345 26.028  1.00 47.84 ? 322 ASN A O   1 
ATOM   2532  C CB  . ASN A 1 327 ? -7.056  -14.722 25.505  1.00 47.34 ? 322 ASN A CB  1 
ATOM   2533  C CG  . ASN A 1 327 ? -5.757  -15.412 25.900  1.00 47.49 ? 322 ASN A CG  1 
ATOM   2534  O OD1 . ASN A 1 327 ? -5.310  -16.356 25.241  1.00 46.78 ? 322 ASN A OD1 1 
ATOM   2535  N ND2 . ASN A 1 327 ? -5.139  -14.933 26.977  1.00 47.16 ? 322 ASN A ND2 1 
ATOM   2536  N N   . THR A 1 328 ? -8.069  -17.708 25.954  1.00 48.46 ? 323 THR A N   1 
ATOM   2537  C CA  . THR A 1 328 ? -8.583  -18.729 26.872  1.00 48.84 ? 323 THR A CA  1 
ATOM   2538  C C   . THR A 1 328 ? -8.123  -18.434 28.303  1.00 49.00 ? 323 THR A C   1 
ATOM   2539  O O   . THR A 1 328 ? -8.914  -18.488 29.247  1.00 49.31 ? 323 THR A O   1 
ATOM   2540  C CB  . THR A 1 328 ? -8.084  -20.129 26.463  1.00 48.94 ? 323 THR A CB  1 
ATOM   2541  O OG1 . THR A 1 328 ? -8.204  -20.283 25.040  1.00 49.22 ? 323 THR A OG1 1 
ATOM   2542  C CG2 . THR A 1 328 ? -8.872  -21.232 27.179  1.00 48.87 ? 323 THR A CG2 1 
ATOM   2543  N N   . GLY B 2 1   ? -18.900 -17.503 19.079  1.00 40.63 ? 1   GLY B N   1 
ATOM   2544  C CA  . GLY B 2 1   ? -18.759 -16.412 18.072  1.00 40.55 ? 1   GLY B CA  1 
ATOM   2545  C C   . GLY B 2 1   ? -19.457 -16.749 16.770  1.00 40.54 ? 1   GLY B C   1 
ATOM   2546  O O   . GLY B 2 1   ? -19.888 -17.888 16.561  1.00 40.47 ? 1   GLY B O   1 
ATOM   2547  N N   . LEU B 2 2   ? -19.550 -15.756 15.887  1.00 40.50 ? 2   LEU B N   1 
ATOM   2548  C CA  . LEU B 2 2   ? -20.296 -15.874 14.630  1.00 40.50 ? 2   LEU B CA  1 
ATOM   2549  C C   . LEU B 2 2   ? -20.085 -17.176 13.853  1.00 40.59 ? 2   LEU B C   1 
ATOM   2550  O O   . LEU B 2 2   ? -21.024 -17.703 13.260  1.00 40.44 ? 2   LEU B O   1 
ATOM   2551  C CB  . LEU B 2 2   ? -20.014 -14.672 13.724  1.00 40.54 ? 2   LEU B CB  1 
ATOM   2552  C CG  . LEU B 2 2   ? -21.149 -13.680 13.447  1.00 40.42 ? 2   LEU B CG  1 
ATOM   2553  C CD1 . LEU B 2 2   ? -21.940 -13.327 14.698  1.00 40.46 ? 2   LEU B CD1 1 
ATOM   2554  C CD2 . LEU B 2 2   ? -20.601 -12.430 12.781  1.00 40.20 ? 2   LEU B CD2 1 
ATOM   2555  N N   . PHE B 2 3   ? -18.859 -17.694 13.869  1.00 40.75 ? 3   PHE B N   1 
ATOM   2556  C CA  . PHE B 2 3   ? -18.529 -18.880 13.079  1.00 40.85 ? 3   PHE B CA  1 
ATOM   2557  C C   . PHE B 2 3   ? -18.401 -20.181 13.883  1.00 41.06 ? 3   PHE B C   1 
ATOM   2558  O O   . PHE B 2 3   ? -18.065 -21.232 13.332  1.00 40.91 ? 3   PHE B O   1 
ATOM   2559  C CB  . PHE B 2 3   ? -17.321 -18.586 12.191  1.00 40.66 ? 3   PHE B CB  1 
ATOM   2560  C CG  . PHE B 2 3   ? -17.598 -17.517 11.175  1.00 40.75 ? 3   PHE B CG  1 
ATOM   2561  C CD1 . PHE B 2 3   ? -18.129 -17.846 9.930   1.00 40.51 ? 3   PHE B CD1 1 
ATOM   2562  C CD2 . PHE B 2 3   ? -17.388 -16.173 11.483  1.00 40.42 ? 3   PHE B CD2 1 
ATOM   2563  C CE1 . PHE B 2 3   ? -18.418 -16.858 8.995   1.00 40.29 ? 3   PHE B CE1 1 
ATOM   2564  C CE2 . PHE B 2 3   ? -17.676 -15.178 10.555  1.00 40.41 ? 3   PHE B CE2 1 
ATOM   2565  C CZ  . PHE B 2 3   ? -18.193 -15.523 9.309   1.00 40.68 ? 3   PHE B CZ  1 
ATOM   2566  N N   . GLY B 2 4   ? -18.698 -20.094 15.180  1.00 41.33 ? 4   GLY B N   1 
ATOM   2567  C CA  . GLY B 2 4   ? -18.870 -21.258 16.047  1.00 41.67 ? 4   GLY B CA  1 
ATOM   2568  C C   . GLY B 2 4   ? -17.665 -22.158 16.238  1.00 42.11 ? 4   GLY B C   1 
ATOM   2569  O O   . GLY B 2 4   ? -17.814 -23.289 16.702  1.00 42.17 ? 4   GLY B O   1 
ATOM   2570  N N   . ALA B 2 5   ? -16.478 -21.658 15.890  1.00 42.43 ? 5   ALA B N   1 
ATOM   2571  C CA  . ALA B 2 5   ? -15.236 -22.427 15.990  1.00 42.83 ? 5   ALA B CA  1 
ATOM   2572  C C   . ALA B 2 5   ? -14.402 -22.075 17.230  1.00 43.17 ? 5   ALA B C   1 
ATOM   2573  O O   . ALA B 2 5   ? -14.205 -22.930 18.096  1.00 43.34 ? 5   ALA B O   1 
ATOM   2574  C CB  . ALA B 2 5   ? -14.411 -22.293 14.711  1.00 42.72 ? 5   ALA B CB  1 
ATOM   2575  N N   . ILE B 2 6   ? -13.917 -20.833 17.315  1.00 43.54 ? 6   ILE B N   1 
ATOM   2576  C CA  . ILE B 2 6   ? -13.161 -20.375 18.492  1.00 43.84 ? 6   ILE B CA  1 
ATOM   2577  C C   . ILE B 2 6   ? -14.089 -20.321 19.703  1.00 44.12 ? 6   ILE B C   1 
ATOM   2578  O O   . ILE B 2 6   ? -15.114 -19.633 19.677  1.00 44.31 ? 6   ILE B O   1 
ATOM   2579  C CB  . ILE B 2 6   ? -12.467 -18.999 18.260  1.00 43.84 ? 6   ILE B CB  1 
ATOM   2580  C CG1 . ILE B 2 6   ? -11.260 -19.157 17.328  1.00 43.67 ? 6   ILE B CG1 1 
ATOM   2581  C CG2 . ILE B 2 6   ? -12.031 -18.363 19.595  1.00 43.66 ? 6   ILE B CG2 1 
ATOM   2582  C CD1 . ILE B 2 6   ? -10.608 -17.841 16.900  1.00 42.95 ? 6   ILE B CD1 1 
ATOM   2583  N N   . ALA B 2 7   ? -13.722 -21.059 20.752  1.00 44.42 ? 7   ALA B N   1 
ATOM   2584  C CA  . ALA B 2 7   ? -14.565 -21.252 21.943  1.00 44.79 ? 7   ALA B CA  1 
ATOM   2585  C C   . ALA B 2 7   ? -15.945 -21.827 21.587  1.00 45.07 ? 7   ALA B C   1 
ATOM   2586  O O   . ALA B 2 7   ? -16.926 -21.637 22.309  1.00 45.02 ? 7   ALA B O   1 
ATOM   2587  C CB  . ALA B 2 7   ? -14.683 -19.952 22.764  1.00 44.57 ? 7   ALA B CB  1 
ATOM   2588  N N   . GLY B 2 8   ? -15.995 -22.539 20.465  1.00 45.53 ? 8   GLY B N   1 
ATOM   2589  C CA  . GLY B 2 8   ? -17.201 -23.213 20.006  1.00 45.94 ? 8   GLY B CA  1 
ATOM   2590  C C   . GLY B 2 8   ? -16.961 -24.706 20.052  1.00 46.32 ? 8   GLY B C   1 
ATOM   2591  O O   . GLY B 2 8   ? -16.781 -25.272 21.134  1.00 46.45 ? 8   GLY B O   1 
ATOM   2592  N N   . PHE B 2 9   ? -16.934 -25.345 18.882  1.00 46.59 ? 9   PHE B N   1 
ATOM   2593  C CA  . PHE B 2 9   ? -16.673 -26.785 18.813  1.00 46.74 ? 9   PHE B CA  1 
ATOM   2594  C C   . PHE B 2 9   ? -15.217 -27.140 19.147  1.00 46.91 ? 9   PHE B C   1 
ATOM   2595  O O   . PHE B 2 9   ? -14.918 -28.281 19.494  1.00 46.99 ? 9   PHE B O   1 
ATOM   2596  C CB  . PHE B 2 9   ? -17.157 -27.407 17.487  1.00 46.66 ? 9   PHE B CB  1 
ATOM   2597  C CG  . PHE B 2 9   ? -16.363 -27.005 16.269  1.00 46.34 ? 9   PHE B CG  1 
ATOM   2598  C CD1 . PHE B 2 9   ? -15.253 -27.742 15.869  1.00 46.22 ? 9   PHE B CD1 1 
ATOM   2599  C CD2 . PHE B 2 9   ? -16.763 -25.928 15.488  1.00 46.79 ? 9   PHE B CD2 1 
ATOM   2600  C CE1 . PHE B 2 9   ? -14.525 -27.386 14.731  1.00 45.96 ? 9   PHE B CE1 1 
ATOM   2601  C CE2 . PHE B 2 9   ? -16.047 -25.564 14.340  1.00 46.34 ? 9   PHE B CE2 1 
ATOM   2602  C CZ  . PHE B 2 9   ? -14.924 -26.294 13.967  1.00 46.38 ? 9   PHE B CZ  1 
ATOM   2603  N N   . ILE B 2 10  ? -14.332 -26.151 19.040  1.00 47.17 ? 10  ILE B N   1 
ATOM   2604  C CA  . ILE B 2 10  ? -12.976 -26.245 19.569  1.00 47.44 ? 10  ILE B CA  1 
ATOM   2605  C C   . ILE B 2 10  ? -12.940 -25.464 20.884  1.00 47.91 ? 10  ILE B C   1 
ATOM   2606  O O   . ILE B 2 10  ? -12.788 -24.242 20.886  1.00 48.14 ? 10  ILE B O   1 
ATOM   2607  C CB  . ILE B 2 10  ? -11.929 -25.700 18.574  1.00 47.19 ? 10  ILE B CB  1 
ATOM   2608  C CG1 . ILE B 2 10  ? -12.112 -26.357 17.204  1.00 46.76 ? 10  ILE B CG1 1 
ATOM   2609  C CG2 . ILE B 2 10  ? -10.513 -25.929 19.110  1.00 47.38 ? 10  ILE B CG2 1 
ATOM   2610  C CD1 . ILE B 2 10  ? -11.253 -25.788 16.106  1.00 46.12 ? 10  ILE B CD1 1 
ATOM   2611  N N   . GLU B 2 11  ? -13.086 -26.188 21.994  1.00 48.42 ? 11  GLU B N   1 
ATOM   2612  C CA  . GLU B 2 11  ? -13.326 -25.594 23.319  1.00 48.96 ? 11  GLU B CA  1 
ATOM   2613  C C   . GLU B 2 11  ? -12.297 -24.560 23.795  1.00 48.76 ? 11  GLU B C   1 
ATOM   2614  O O   . GLU B 2 11  ? -12.666 -23.580 24.444  1.00 48.78 ? 11  GLU B O   1 
ATOM   2615  C CB  . GLU B 2 11  ? -13.513 -26.691 24.377  1.00 49.21 ? 11  GLU B CB  1 
ATOM   2616  C CG  . GLU B 2 11  ? -14.899 -27.356 24.348  1.00 51.16 ? 11  GLU B CG  1 
ATOM   2617  C CD  . GLU B 2 11  ? -15.023 -28.583 25.265  1.00 53.64 ? 11  GLU B CD  1 
ATOM   2618  O OE1 . GLU B 2 11  ? -16.126 -29.181 25.314  1.00 54.08 ? 11  GLU B OE1 1 
ATOM   2619  O OE2 . GLU B 2 11  ? -14.028 -28.950 25.936  1.00 54.45 ? 11  GLU B OE2 1 
ATOM   2620  N N   . GLY B 2 12  ? -11.023 -24.768 23.471  1.00 48.60 ? 12  GLY B N   1 
ATOM   2621  C CA  . GLY B 2 12  ? -9.972  -23.860 23.925  1.00 48.53 ? 12  GLY B CA  1 
ATOM   2622  C C   . GLY B 2 12  ? -8.817  -23.665 22.964  1.00 48.56 ? 12  GLY B C   1 
ATOM   2623  O O   . GLY B 2 12  ? -8.753  -24.297 21.910  1.00 48.43 ? 12  GLY B O   1 
ATOM   2624  N N   . GLY B 2 13  ? -7.905  -22.773 23.338  1.00 48.78 ? 13  GLY B N   1 
ATOM   2625  C CA  . GLY B 2 13  ? -6.688  -22.529 22.567  1.00 49.17 ? 13  GLY B CA  1 
ATOM   2626  C C   . GLY B 2 13  ? -5.510  -23.319 23.110  1.00 49.46 ? 13  GLY B C   1 
ATOM   2627  O O   . GLY B 2 13  ? -5.577  -23.860 24.216  1.00 49.34 ? 13  GLY B O   1 
ATOM   2628  N N   . TRP B 2 14  ? -4.431  -23.380 22.332  1.00 49.83 ? 14  TRP B N   1 
ATOM   2629  C CA  . TRP B 2 14  ? -3.227  -24.115 22.727  1.00 50.29 ? 14  TRP B CA  1 
ATOM   2630  C C   . TRP B 2 14  ? -2.069  -23.202 23.127  1.00 50.91 ? 14  TRP B C   1 
ATOM   2631  O O   . TRP B 2 14  ? -1.581  -22.408 22.320  1.00 50.86 ? 14  TRP B O   1 
ATOM   2632  C CB  . TRP B 2 14  ? -2.764  -25.062 21.612  1.00 50.00 ? 14  TRP B CB  1 
ATOM   2633  C CG  . TRP B 2 14  ? -3.772  -26.099 21.200  1.00 48.76 ? 14  TRP B CG  1 
ATOM   2634  C CD1 . TRP B 2 14  ? -4.744  -26.662 21.979  1.00 47.89 ? 14  TRP B CD1 1 
ATOM   2635  C CD2 . TRP B 2 14  ? -3.886  -26.713 19.912  1.00 47.49 ? 14  TRP B CD2 1 
ATOM   2636  N NE1 . TRP B 2 14  ? -5.464  -27.579 21.252  1.00 47.29 ? 14  TRP B NE1 1 
ATOM   2637  C CE2 . TRP B 2 14  ? -4.957  -27.632 19.980  1.00 47.22 ? 14  TRP B CE2 1 
ATOM   2638  C CE3 . TRP B 2 14  ? -3.190  -26.572 18.705  1.00 46.76 ? 14  TRP B CE3 1 
ATOM   2639  C CZ2 . TRP B 2 14  ? -5.349  -28.408 18.886  1.00 46.44 ? 14  TRP B CZ2 1 
ATOM   2640  C CZ3 . TRP B 2 14  ? -3.577  -27.346 17.619  1.00 46.33 ? 14  TRP B CZ3 1 
ATOM   2641  C CH2 . TRP B 2 14  ? -4.648  -28.252 17.717  1.00 45.94 ? 14  TRP B CH2 1 
ATOM   2642  N N   . GLN B 2 15  ? -1.632  -23.337 24.378  1.00 51.83 ? 15  GLN B N   1 
ATOM   2643  C CA  . GLN B 2 15  ? -0.442  -22.643 24.880  1.00 52.63 ? 15  GLN B CA  1 
ATOM   2644  C C   . GLN B 2 15  ? 0.816   -23.090 24.132  1.00 52.99 ? 15  GLN B C   1 
ATOM   2645  O O   . GLN B 2 15  ? 1.737   -22.298 23.925  1.00 53.00 ? 15  GLN B O   1 
ATOM   2646  C CB  . GLN B 2 15  ? -0.271  -22.894 26.380  1.00 52.68 ? 15  GLN B CB  1 
ATOM   2647  C CG  . GLN B 2 15  ? -1.440  -22.420 27.237  1.00 53.59 ? 15  GLN B CG  1 
ATOM   2648  C CD  . GLN B 2 15  ? -1.392  -20.929 27.529  1.00 54.74 ? 15  GLN B CD  1 
ATOM   2649  O OE1 . GLN B 2 15  ? -0.411  -20.421 28.072  1.00 55.34 ? 15  GLN B OE1 1 
ATOM   2650  N NE2 . GLN B 2 15  ? -2.460  -20.224 27.179  1.00 55.23 ? 15  GLN B NE2 1 
ATOM   2651  N N   . GLY B 2 16  ? 0.830   -24.355 23.712  1.00 53.48 ? 16  GLY B N   1 
ATOM   2652  C CA  . GLY B 2 16  ? 1.980   -24.956 23.040  1.00 54.26 ? 16  GLY B CA  1 
ATOM   2653  C C   . GLY B 2 16  ? 2.264   -24.496 21.619  1.00 54.90 ? 16  GLY B C   1 
ATOM   2654  O O   . GLY B 2 16  ? 3.300   -24.851 21.047  1.00 54.93 ? 16  GLY B O   1 
ATOM   2655  N N   . MET B 2 17  ? 1.352   -23.715 21.041  1.00 55.54 ? 17  MET B N   1 
ATOM   2656  C CA  . MET B 2 17  ? 1.557   -23.170 19.699  1.00 56.17 ? 17  MET B CA  1 
ATOM   2657  C C   . MET B 2 17  ? 2.037   -21.721 19.753  1.00 56.45 ? 17  MET B C   1 
ATOM   2658  O O   . MET B 2 17  ? 1.246   -20.786 19.625  1.00 56.72 ? 17  MET B O   1 
ATOM   2659  C CB  . MET B 2 17  ? 0.284   -23.286 18.859  1.00 56.25 ? 17  MET B CB  1 
ATOM   2660  C CG  . MET B 2 17  ? 0.472   -22.876 17.399  1.00 56.71 ? 17  MET B CG  1 
ATOM   2661  S SD  . MET B 2 17  ? -0.974  -23.215 16.389  1.00 57.23 ? 17  MET B SD  1 
ATOM   2662  C CE  . MET B 2 17  ? -1.004  -25.003 16.473  1.00 57.86 ? 17  MET B CE  1 
ATOM   2663  N N   . VAL B 2 18  ? 3.341   -21.549 19.948  1.00 56.76 ? 18  VAL B N   1 
ATOM   2664  C CA  . VAL B 2 18  ? 3.963   -20.226 20.005  1.00 56.94 ? 18  VAL B CA  1 
ATOM   2665  C C   . VAL B 2 18  ? 4.317   -19.778 18.583  1.00 56.89 ? 18  VAL B C   1 
ATOM   2666  O O   . VAL B 2 18  ? 4.742   -18.644 18.353  1.00 56.81 ? 18  VAL B O   1 
ATOM   2667  C CB  . VAL B 2 18  ? 5.233   -20.246 20.897  1.00 57.05 ? 18  VAL B CB  1 
ATOM   2668  C CG1 . VAL B 2 18  ? 5.638   -18.826 21.309  1.00 57.46 ? 18  VAL B CG1 1 
ATOM   2669  C CG2 . VAL B 2 18  ? 5.005   -21.109 22.139  1.00 57.12 ? 18  VAL B CG2 1 
ATOM   2670  N N   . ASP B 2 19  ? 4.101   -20.687 17.637  1.00 56.88 ? 19  ASP B N   1 
ATOM   2671  C CA  . ASP B 2 19  ? 4.541   -20.549 16.253  1.00 56.90 ? 19  ASP B CA  1 
ATOM   2672  C C   . ASP B 2 19  ? 3.704   -19.542 15.438  1.00 56.55 ? 19  ASP B C   1 
ATOM   2673  O O   . ASP B 2 19  ? 4.216   -18.904 14.514  1.00 56.55 ? 19  ASP B O   1 
ATOM   2674  C CB  . ASP B 2 19  ? 4.500   -21.936 15.591  1.00 57.16 ? 19  ASP B CB  1 
ATOM   2675  C CG  . ASP B 2 19  ? 5.813   -22.318 14.916  1.00 58.10 ? 19  ASP B CG  1 
ATOM   2676  O OD1 . ASP B 2 19  ? 6.894   -21.918 15.407  1.00 58.85 ? 19  ASP B OD1 1 
ATOM   2677  O OD2 . ASP B 2 19  ? 5.763   -23.048 13.899  1.00 59.02 ? 19  ASP B OD2 1 
ATOM   2678  N N   . GLY B 2 20  ? 2.422   -19.408 15.779  1.00 56.08 ? 20  GLY B N   1 
ATOM   2679  C CA  . GLY B 2 20  ? 1.506   -18.529 15.044  1.00 55.34 ? 20  GLY B CA  1 
ATOM   2680  C C   . GLY B 2 20  ? 0.110   -18.478 15.637  1.00 54.76 ? 20  GLY B C   1 
ATOM   2681  O O   . GLY B 2 20  ? -0.098  -18.879 16.780  1.00 54.68 ? 20  GLY B O   1 
ATOM   2682  N N   . TRP B 2 21  ? -0.849  -17.980 14.857  1.00 54.36 ? 21  TRP B N   1 
ATOM   2683  C CA  . TRP B 2 21  ? -2.241  -17.862 15.315  1.00 53.88 ? 21  TRP B CA  1 
ATOM   2684  C C   . TRP B 2 21  ? -3.052  -19.149 15.155  1.00 53.91 ? 21  TRP B C   1 
ATOM   2685  O O   . TRP B 2 21  ? -3.789  -19.536 16.064  1.00 53.79 ? 21  TRP B O   1 
ATOM   2686  C CB  . TRP B 2 21  ? -2.968  -16.701 14.622  1.00 53.52 ? 21  TRP B CB  1 
ATOM   2687  C CG  . TRP B 2 21  ? -2.762  -15.355 15.263  1.00 52.17 ? 21  TRP B CG  1 
ATOM   2688  C CD1 . TRP B 2 21  ? -2.587  -15.095 16.592  1.00 51.46 ? 21  TRP B CD1 1 
ATOM   2689  C CD2 . TRP B 2 21  ? -2.752  -14.083 14.603  1.00 50.77 ? 21  TRP B CD2 1 
ATOM   2690  N NE1 . TRP B 2 21  ? -2.447  -13.743 16.797  1.00 50.94 ? 21  TRP B NE1 1 
ATOM   2691  C CE2 . TRP B 2 21  ? -2.546  -13.099 15.593  1.00 50.46 ? 21  TRP B CE2 1 
ATOM   2692  C CE3 . TRP B 2 21  ? -2.890  -13.679 13.268  1.00 50.57 ? 21  TRP B CE3 1 
ATOM   2693  C CZ2 . TRP B 2 21  ? -2.475  -11.736 15.292  1.00 50.14 ? 21  TRP B CZ2 1 
ATOM   2694  C CZ3 . TRP B 2 21  ? -2.820  -12.324 12.968  1.00 49.98 ? 21  TRP B CZ3 1 
ATOM   2695  C CH2 . TRP B 2 21  ? -2.617  -11.369 13.978  1.00 49.91 ? 21  TRP B CH2 1 
ATOM   2696  N N   . TYR B 2 22  ? -2.925  -19.793 13.996  1.00 53.97 ? 22  TYR B N   1 
ATOM   2697  C CA  . TYR B 2 22  ? -3.664  -21.026 13.709  1.00 54.26 ? 22  TYR B CA  1 
ATOM   2698  C C   . TYR B 2 22  ? -2.721  -22.137 13.258  1.00 54.64 ? 22  TYR B C   1 
ATOM   2699  O O   . TYR B 2 22  ? -1.673  -21.869 12.663  1.00 54.65 ? 22  TYR B O   1 
ATOM   2700  C CB  . TYR B 2 22  ? -4.731  -20.799 12.628  1.00 54.05 ? 22  TYR B CB  1 
ATOM   2701  C CG  . TYR B 2 22  ? -5.304  -19.397 12.556  1.00 53.50 ? 22  TYR B CG  1 
ATOM   2702  C CD1 . TYR B 2 22  ? -6.191  -18.927 13.528  1.00 53.13 ? 22  TYR B CD1 1 
ATOM   2703  C CD2 . TYR B 2 22  ? -4.968  -18.545 11.505  1.00 52.96 ? 22  TYR B CD2 1 
ATOM   2704  C CE1 . TYR B 2 22  ? -6.719  -17.637 13.460  1.00 52.42 ? 22  TYR B CE1 1 
ATOM   2705  C CE2 . TYR B 2 22  ? -5.490  -17.260 11.426  1.00 52.47 ? 22  TYR B CE2 1 
ATOM   2706  C CZ  . TYR B 2 22  ? -6.363  -16.812 12.404  1.00 52.33 ? 22  TYR B CZ  1 
ATOM   2707  O OH  . TYR B 2 22  ? -6.880  -15.543 12.317  1.00 51.74 ? 22  TYR B OH  1 
ATOM   2708  N N   . GLY B 2 23  ? -3.102  -23.384 13.533  1.00 55.06 ? 23  GLY B N   1 
ATOM   2709  C CA  . GLY B 2 23  ? -2.311  -24.530 13.097  1.00 55.63 ? 23  GLY B CA  1 
ATOM   2710  C C   . GLY B 2 23  ? -2.810  -25.904 13.506  1.00 56.14 ? 23  GLY B C   1 
ATOM   2711  O O   . GLY B 2 23  ? -4.005  -26.110 13.751  1.00 56.09 ? 23  GLY B O   1 
ATOM   2712  N N   . TYR B 2 24  ? -1.869  -26.841 13.590  1.00 56.70 ? 24  TYR B N   1 
ATOM   2713  C CA  . TYR B 2 24  ? -2.172  -28.258 13.756  1.00 57.21 ? 24  TYR B CA  1 
ATOM   2714  C C   . TYR B 2 24  ? -1.492  -28.886 14.968  1.00 57.84 ? 24  TYR B C   1 
ATOM   2715  O O   . TYR B 2 24  ? -0.542  -28.337 15.524  1.00 57.87 ? 24  TYR B O   1 
ATOM   2716  C CB  . TYR B 2 24  ? -1.742  -29.036 12.513  1.00 56.95 ? 24  TYR B CB  1 
ATOM   2717  C CG  . TYR B 2 24  ? -2.133  -28.411 11.195  1.00 56.39 ? 24  TYR B CG  1 
ATOM   2718  C CD1 . TYR B 2 24  ? -3.353  -28.711 10.599  1.00 55.71 ? 24  TYR B CD1 1 
ATOM   2719  C CD2 . TYR B 2 24  ? -1.273  -27.536 10.534  1.00 55.73 ? 24  TYR B CD2 1 
ATOM   2720  C CE1 . TYR B 2 24  ? -3.714  -28.149 9.387   1.00 55.20 ? 24  TYR B CE1 1 
ATOM   2721  C CE2 . TYR B 2 24  ? -1.624  -26.972 9.320   1.00 55.24 ? 24  TYR B CE2 1 
ATOM   2722  C CZ  . TYR B 2 24  ? -2.847  -27.284 8.752   1.00 55.29 ? 24  TYR B CZ  1 
ATOM   2723  O OH  . TYR B 2 24  ? -3.208  -26.729 7.546   1.00 55.31 ? 24  TYR B OH  1 
ATOM   2724  N N   . HIS B 2 25  ? -1.997  -30.050 15.359  1.00 58.81 ? 25  HIS B N   1 
ATOM   2725  C CA  . HIS B 2 25  ? -1.354  -30.909 16.343  1.00 59.76 ? 25  HIS B CA  1 
ATOM   2726  C C   . HIS B 2 25  ? -1.495  -32.352 15.867  1.00 60.33 ? 25  HIS B C   1 
ATOM   2727  O O   . HIS B 2 25  ? -2.607  -32.809 15.585  1.00 60.36 ? 25  HIS B O   1 
ATOM   2728  C CB  . HIS B 2 25  ? -1.993  -30.723 17.719  1.00 59.75 ? 25  HIS B CB  1 
ATOM   2729  C CG  . HIS B 2 25  ? -1.489  -31.678 18.756  1.00 60.43 ? 25  HIS B CG  1 
ATOM   2730  N ND1 . HIS B 2 25  ? -0.221  -31.597 19.290  1.00 60.82 ? 25  HIS B ND1 1 
ATOM   2731  C CD2 . HIS B 2 25  ? -2.087  -32.731 19.362  1.00 60.83 ? 25  HIS B CD2 1 
ATOM   2732  C CE1 . HIS B 2 25  ? -0.057  -32.560 20.179  1.00 61.07 ? 25  HIS B CE1 1 
ATOM   2733  N NE2 . HIS B 2 25  ? -1.175  -33.262 20.242  1.00 61.31 ? 25  HIS B NE2 1 
ATOM   2734  N N   . HIS B 2 26  ? -0.371  -33.059 15.762  1.00 61.16 ? 26  HIS B N   1 
ATOM   2735  C CA  . HIS B 2 26  ? -0.383  -34.429 15.239  1.00 61.92 ? 26  HIS B CA  1 
ATOM   2736  C C   . HIS B 2 26  ? 0.092   -35.480 16.238  1.00 62.29 ? 26  HIS B C   1 
ATOM   2737  O O   . HIS B 2 26  ? 1.036   -35.247 16.989  1.00 62.30 ? 26  HIS B O   1 
ATOM   2738  C CB  . HIS B 2 26  ? 0.412   -34.534 13.927  1.00 62.03 ? 26  HIS B CB  1 
ATOM   2739  C CG  . HIS B 2 26  ? 1.876   -34.237 14.063  1.00 62.86 ? 26  HIS B CG  1 
ATOM   2740  N ND1 . HIS B 2 26  ? 2.717   -34.971 14.872  1.00 63.70 ? 26  HIS B ND1 1 
ATOM   2741  C CD2 . HIS B 2 26  ? 2.654   -33.305 13.461  1.00 63.69 ? 26  HIS B CD2 1 
ATOM   2742  C CE1 . HIS B 2 26  ? 3.945   -34.490 14.780  1.00 64.15 ? 26  HIS B CE1 1 
ATOM   2743  N NE2 . HIS B 2 26  ? 3.935   -33.481 13.928  1.00 64.00 ? 26  HIS B NE2 1 
ATOM   2744  N N   . SER B 2 27  ? -0.580  -36.631 16.233  1.00 62.78 ? 27  SER B N   1 
ATOM   2745  C CA  . SER B 2 27  ? -0.162  -37.797 17.011  1.00 63.19 ? 27  SER B CA  1 
ATOM   2746  C C   . SER B 2 27  ? -0.058  -39.028 16.115  1.00 63.52 ? 27  SER B C   1 
ATOM   2747  O O   . SER B 2 27  ? -1.030  -39.411 15.455  1.00 63.55 ? 27  SER B O   1 
ATOM   2748  C CB  . SER B 2 27  ? -1.136  -38.073 18.161  1.00 63.15 ? 27  SER B CB  1 
ATOM   2749  O OG  . SER B 2 27  ? -0.891  -37.223 19.268  1.00 63.30 ? 27  SER B OG  1 
ATOM   2750  N N   . ASN B 2 28  ? 1.128   -39.632 16.083  1.00 63.95 ? 28  ASN B N   1 
ATOM   2751  C CA  . ASN B 2 28  ? 1.333   -40.913 15.399  1.00 64.28 ? 28  ASN B CA  1 
ATOM   2752  C C   . ASN B 2 28  ? 2.450   -41.764 16.024  1.00 64.62 ? 28  ASN B C   1 
ATOM   2753  O O   . ASN B 2 28  ? 2.922   -41.466 17.129  1.00 64.57 ? 28  ASN B O   1 
ATOM   2754  C CB  . ASN B 2 28  ? 1.521   -40.724 13.876  1.00 64.14 ? 28  ASN B CB  1 
ATOM   2755  C CG  . ASN B 2 28  ? 2.803   -39.983 13.506  1.00 63.92 ? 28  ASN B CG  1 
ATOM   2756  O OD1 . ASN B 2 28  ? 3.094   -39.805 12.321  1.00 63.62 ? 28  ASN B OD1 1 
ATOM   2757  N ND2 . ASN B 2 28  ? 3.570   -39.551 14.504  1.00 63.54 ? 28  ASN B ND2 1 
ATOM   2758  N N   . GLU B 2 29  ? 2.852   -42.818 15.314  1.00 65.01 ? 29  GLU B N   1 
ATOM   2759  C CA  . GLU B 2 29  ? 3.896   -43.740 15.769  1.00 65.38 ? 29  GLU B CA  1 
ATOM   2760  C C   . GLU B 2 29  ? 5.219   -43.014 16.049  1.00 65.39 ? 29  GLU B C   1 
ATOM   2761  O O   . GLU B 2 29  ? 5.862   -43.260 17.073  1.00 65.39 ? 29  GLU B O   1 
ATOM   2762  C CB  . GLU B 2 29  ? 4.108   -44.851 14.733  1.00 65.51 ? 29  GLU B CB  1 
ATOM   2763  C CG  . GLU B 2 29  ? 4.388   -46.229 15.330  1.00 66.37 ? 29  GLU B CG  1 
ATOM   2764  C CD  . GLU B 2 29  ? 3.117   -46.964 15.747  1.00 67.64 ? 29  GLU B CD  1 
ATOM   2765  O OE1 . GLU B 2 29  ? 2.274   -47.259 14.868  1.00 67.95 ? 29  GLU B OE1 1 
ATOM   2766  O OE2 . GLU B 2 29  ? 2.966   -47.254 16.955  1.00 68.01 ? 29  GLU B OE2 1 
ATOM   2767  N N   . GLN B 2 30  ? 5.598   -42.112 15.143  1.00 65.33 ? 30  GLN B N   1 
ATOM   2768  C CA  . GLN B 2 30  ? 6.843   -41.345 15.243  1.00 65.25 ? 30  GLN B CA  1 
ATOM   2769  C C   . GLN B 2 30  ? 6.870   -40.351 16.408  1.00 65.25 ? 30  GLN B C   1 
ATOM   2770  O O   . GLN B 2 30  ? 7.944   -40.027 16.920  1.00 65.40 ? 30  GLN B O   1 
ATOM   2771  C CB  . GLN B 2 30  ? 7.120   -40.613 13.925  1.00 65.35 ? 30  GLN B CB  1 
ATOM   2772  C CG  . GLN B 2 30  ? 7.583   -41.516 12.782  1.00 65.18 ? 30  GLN B CG  1 
ATOM   2773  C CD  . GLN B 2 30  ? 7.019   -41.093 11.440  1.00 65.11 ? 30  GLN B CD  1 
ATOM   2774  O OE1 . GLN B 2 30  ? 5.803   -41.053 11.255  1.00 65.36 ? 30  GLN B OE1 1 
ATOM   2775  N NE2 . GLN B 2 30  ? 7.898   -40.784 10.492  1.00 64.96 ? 30  GLN B NE2 1 
ATOM   2776  N N   . GLY B 2 31  ? 5.696   -39.868 16.816  1.00 65.15 ? 31  GLY B N   1 
ATOM   2777  C CA  . GLY B 2 31  ? 5.580   -38.927 17.934  1.00 64.92 ? 31  GLY B CA  1 
ATOM   2778  C C   . GLY B 2 31  ? 4.501   -37.869 17.746  1.00 64.87 ? 31  GLY B C   1 
ATOM   2779  O O   . GLY B 2 31  ? 3.716   -37.928 16.794  1.00 64.86 ? 31  GLY B O   1 
ATOM   2780  N N   . SER B 2 32  ? 4.470   -36.897 18.657  1.00 64.64 ? 32  SER B N   1 
ATOM   2781  C CA  . SER B 2 32  ? 3.471   -35.828 18.635  1.00 64.37 ? 32  SER B CA  1 
ATOM   2782  C C   . SER B 2 32  ? 4.105   -34.432 18.603  1.00 64.16 ? 32  SER B C   1 
ATOM   2783  O O   . SER B 2 32  ? 5.311   -34.288 18.822  1.00 64.08 ? 32  SER B O   1 
ATOM   2784  C CB  . SER B 2 32  ? 2.516   -35.965 19.829  1.00 64.43 ? 32  SER B CB  1 
ATOM   2785  O OG  . SER B 2 32  ? 3.193   -35.785 21.062  1.00 64.61 ? 32  SER B OG  1 
ATOM   2786  N N   . GLY B 2 33  ? 3.292   -33.410 18.321  1.00 63.89 ? 33  GLY B N   1 
ATOM   2787  C CA  . GLY B 2 33  ? 3.769   -32.023 18.319  1.00 63.55 ? 33  GLY B CA  1 
ATOM   2788  C C   . GLY B 2 33  ? 2.867   -30.990 17.660  1.00 63.28 ? 33  GLY B C   1 
ATOM   2789  O O   . GLY B 2 33  ? 1.949   -31.332 16.908  1.00 63.39 ? 33  GLY B O   1 
ATOM   2790  N N   . TYR B 2 34  ? 3.146   -29.718 17.947  1.00 62.91 ? 34  TYR B N   1 
ATOM   2791  C CA  . TYR B 2 34  ? 2.395   -28.592 17.395  1.00 62.40 ? 34  TYR B CA  1 
ATOM   2792  C C   . TYR B 2 34  ? 3.112   -27.980 16.202  1.00 62.29 ? 34  TYR B C   1 
ATOM   2793  O O   . TYR B 2 34  ? 4.340   -28.002 16.126  1.00 62.20 ? 34  TYR B O   1 
ATOM   2794  C CB  . TYR B 2 34  ? 2.218   -27.494 18.443  1.00 62.30 ? 34  TYR B CB  1 
ATOM   2795  C CG  . TYR B 2 34  ? 1.402   -27.865 19.658  1.00 61.68 ? 34  TYR B CG  1 
ATOM   2796  C CD1 . TYR B 2 34  ? 0.010   -27.822 19.626  1.00 61.15 ? 34  TYR B CD1 1 
ATOM   2797  C CD2 . TYR B 2 34  ? 2.023   -28.225 20.853  1.00 61.19 ? 34  TYR B CD2 1 
ATOM   2798  C CE1 . TYR B 2 34  ? -0.745  -28.150 20.750  1.00 60.82 ? 34  TYR B CE1 1 
ATOM   2799  C CE2 . TYR B 2 34  ? 1.276   -28.551 21.983  1.00 60.83 ? 34  TYR B CE2 1 
ATOM   2800  C CZ  . TYR B 2 34  ? -0.105  -28.510 21.923  1.00 60.40 ? 34  TYR B CZ  1 
ATOM   2801  O OH  . TYR B 2 34  ? -0.845  -28.830 23.033  1.00 59.75 ? 34  TYR B OH  1 
ATOM   2802  N N   . ALA B 2 35  ? 2.331   -27.417 15.283  1.00 62.10 ? 35  ALA B N   1 
ATOM   2803  C CA  . ALA B 2 35  ? 2.861   -26.670 14.145  1.00 61.97 ? 35  ALA B CA  1 
ATOM   2804  C C   . ALA B 2 35  ? 1.829   -25.650 13.669  1.00 61.89 ? 35  ALA B C   1 
ATOM   2805  O O   . ALA B 2 35  ? 0.636   -25.950 13.610  1.00 61.87 ? 35  ALA B O   1 
ATOM   2806  C CB  . ALA B 2 35  ? 3.243   -27.616 13.010  1.00 61.91 ? 35  ALA B CB  1 
ATOM   2807  N N   . ALA B 2 36  ? 2.289   -24.448 13.336  1.00 61.68 ? 36  ALA B N   1 
ATOM   2808  C CA  . ALA B 2 36  ? 1.400   -23.406 12.832  1.00 61.56 ? 36  ALA B CA  1 
ATOM   2809  C C   . ALA B 2 36  ? 1.235   -23.509 11.321  1.00 61.54 ? 36  ALA B C   1 
ATOM   2810  O O   . ALA B 2 36  ? 2.181   -23.854 10.611  1.00 61.62 ? 36  ALA B O   1 
ATOM   2811  C CB  . ALA B 2 36  ? 1.918   -22.037 13.212  1.00 61.46 ? 36  ALA B CB  1 
ATOM   2812  N N   . ASP B 2 37  ? 0.033   -23.212 10.833  1.00 61.41 ? 37  ASP B N   1 
ATOM   2813  C CA  . ASP B 2 37  ? -0.201  -23.149 9.398   1.00 61.43 ? 37  ASP B CA  1 
ATOM   2814  C C   . ASP B 2 37  ? 0.328   -21.824 8.859   1.00 61.46 ? 37  ASP B C   1 
ATOM   2815  O O   . ASP B 2 37  ? -0.212  -20.759 9.162   1.00 61.47 ? 37  ASP B O   1 
ATOM   2816  C CB  . ASP B 2 37  ? -1.685  -23.316 9.072   1.00 61.43 ? 37  ASP B CB  1 
ATOM   2817  C CG  . ASP B 2 37  ? -1.929  -23.580 7.599   1.00 61.54 ? 37  ASP B CG  1 
ATOM   2818  O OD1 . ASP B 2 37  ? -1.540  -24.662 7.107   1.00 61.34 ? 37  ASP B OD1 1 
ATOM   2819  O OD2 . ASP B 2 37  ? -2.509  -22.704 6.928   1.00 61.98 ? 37  ASP B OD2 1 
ATOM   2820  N N   . LYS B 2 38  ? 1.393   -21.906 8.066   1.00 61.49 ? 38  LYS B N   1 
ATOM   2821  C CA  . LYS B 2 38  ? 2.100   -20.729 7.564   1.00 61.52 ? 38  LYS B CA  1 
ATOM   2822  C C   . LYS B 2 38  ? 1.203   -19.829 6.711   1.00 61.30 ? 38  LYS B C   1 
ATOM   2823  O O   . LYS B 2 38  ? 1.127   -18.619 6.945   1.00 61.33 ? 38  LYS B O   1 
ATOM   2824  C CB  . LYS B 2 38  ? 3.337   -21.158 6.765   1.00 61.72 ? 38  LYS B CB  1 
ATOM   2825  C CG  . LYS B 2 38  ? 4.390   -20.069 6.567   1.00 62.52 ? 38  LYS B CG  1 
ATOM   2826  C CD  . LYS B 2 38  ? 5.489   -20.128 7.628   1.00 63.34 ? 38  LYS B CD  1 
ATOM   2827  C CE  . LYS B 2 38  ? 6.648   -19.200 7.264   1.00 63.91 ? 38  LYS B CE  1 
ATOM   2828  N NZ  . LYS B 2 38  ? 7.895   -19.539 8.006   1.00 63.82 ? 38  LYS B NZ  1 
ATOM   2829  N N   . GLU B 2 39  ? 0.523   -20.427 5.734   1.00 60.95 ? 39  GLU B N   1 
ATOM   2830  C CA  . GLU B 2 39  ? -0.334  -19.689 4.808   1.00 60.58 ? 39  GLU B CA  1 
ATOM   2831  C C   . GLU B 2 39  ? -1.519  -19.030 5.520   1.00 60.06 ? 39  GLU B C   1 
ATOM   2832  O O   . GLU B 2 39  ? -1.845  -17.873 5.251   1.00 60.11 ? 39  GLU B O   1 
ATOM   2833  C CB  . GLU B 2 39  ? -0.825  -20.613 3.688   1.00 60.78 ? 39  GLU B CB  1 
ATOM   2834  C CG  . GLU B 2 39  ? -1.382  -19.890 2.460   1.00 61.63 ? 39  GLU B CG  1 
ATOM   2835  C CD  . GLU B 2 39  ? -1.673  -20.829 1.292   1.00 62.94 ? 39  GLU B CD  1 
ATOM   2836  O OE1 . GLU B 2 39  ? -1.745  -22.060 1.504   1.00 63.15 ? 39  GLU B OE1 1 
ATOM   2837  O OE2 . GLU B 2 39  ? -1.834  -20.332 0.154   1.00 63.80 ? 39  GLU B OE2 1 
ATOM   2838  N N   . SER B 2 40  ? -2.144  -19.767 6.434   1.00 59.36 ? 40  SER B N   1 
ATOM   2839  C CA  . SER B 2 40  ? -3.308  -19.281 7.170   1.00 58.65 ? 40  SER B CA  1 
ATOM   2840  C C   . SER B 2 40  ? -2.977  -18.102 8.092   1.00 58.17 ? 40  SER B C   1 
ATOM   2841  O O   . SER B 2 40  ? -3.747  -17.144 8.188   1.00 58.06 ? 40  SER B O   1 
ATOM   2842  C CB  . SER B 2 40  ? -3.938  -20.420 7.971   1.00 58.56 ? 40  SER B CB  1 
ATOM   2843  O OG  . SER B 2 40  ? -5.175  -20.029 8.529   1.00 58.69 ? 40  SER B OG  1 
ATOM   2844  N N   . THR B 2 41  ? -1.830  -18.181 8.762   1.00 57.54 ? 41  THR B N   1 
ATOM   2845  C CA  . THR B 2 41  ? -1.397  -17.141 9.691   1.00 57.01 ? 41  THR B CA  1 
ATOM   2846  C C   . THR B 2 41  ? -0.970  -15.868 8.961   1.00 56.70 ? 41  THR B C   1 
ATOM   2847  O O   . THR B 2 41  ? -1.296  -14.763 9.398   1.00 56.55 ? 41  THR B O   1 
ATOM   2848  C CB  . THR B 2 41  ? -0.265  -17.648 10.617  1.00 57.03 ? 41  THR B CB  1 
ATOM   2849  O OG1 . THR B 2 41  ? -0.773  -18.696 11.453  1.00 56.94 ? 41  THR B OG1 1 
ATOM   2850  C CG2 . THR B 2 41  ? 0.273   -16.530 11.504  1.00 56.82 ? 41  THR B CG2 1 
ATOM   2851  N N   . GLN B 2 42  ? -0.260  -16.030 7.846   1.00 56.30 ? 42  GLN B N   1 
ATOM   2852  C CA  . GLN B 2 42  ? 0.247   -14.894 7.079   1.00 55.98 ? 42  GLN B CA  1 
ATOM   2853  C C   . GLN B 2 42  ? -0.876  -14.056 6.455   1.00 55.63 ? 42  GLN B C   1 
ATOM   2854  O O   . GLN B 2 42  ? -0.801  -12.822 6.436   1.00 55.56 ? 42  GLN B O   1 
ATOM   2855  C CB  . GLN B 2 42  ? 1.252   -15.357 6.013   1.00 56.15 ? 42  GLN B CB  1 
ATOM   2856  C CG  . GLN B 2 42  ? 2.075   -14.232 5.359   1.00 56.53 ? 42  GLN B CG  1 
ATOM   2857  C CD  . GLN B 2 42  ? 2.777   -13.329 6.369   1.00 56.77 ? 42  GLN B CD  1 
ATOM   2858  O OE1 . GLN B 2 42  ? 3.341   -13.797 7.360   1.00 56.98 ? 42  GLN B OE1 1 
ATOM   2859  N NE2 . GLN B 2 42  ? 2.743   -12.025 6.117   1.00 57.01 ? 42  GLN B NE2 1 
ATOM   2860  N N   . LYS B 2 43  ? -1.914  -14.725 5.958   1.00 55.11 ? 43  LYS B N   1 
ATOM   2861  C CA  . LYS B 2 43  ? -3.073  -14.025 5.409   1.00 54.59 ? 43  LYS B CA  1 
ATOM   2862  C C   . LYS B 2 43  ? -3.763  -13.180 6.468   1.00 54.05 ? 43  LYS B C   1 
ATOM   2863  O O   . LYS B 2 43  ? -4.162  -12.045 6.198   1.00 54.01 ? 43  LYS B O   1 
ATOM   2864  C CB  . LYS B 2 43  ? -4.065  -15.000 4.776   1.00 54.68 ? 43  LYS B CB  1 
ATOM   2865  C CG  . LYS B 2 43  ? -3.911  -15.118 3.275   1.00 55.29 ? 43  LYS B CG  1 
ATOM   2866  C CD  . LYS B 2 43  ? -5.233  -15.489 2.609   1.00 56.18 ? 43  LYS B CD  1 
ATOM   2867  C CE  . LYS B 2 43  ? -5.231  -15.130 1.125   1.00 56.36 ? 43  LYS B CE  1 
ATOM   2868  N NZ  . LYS B 2 43  ? -4.143  -15.819 0.366   1.00 56.64 ? 43  LYS B NZ  1 
ATOM   2869  N N   . ALA B 2 44  ? -3.882  -13.733 7.673   1.00 53.40 ? 44  ALA B N   1 
ATOM   2870  C CA  . ALA B 2 44  ? -4.515  -13.035 8.792   1.00 53.02 ? 44  ALA B CA  1 
ATOM   2871  C C   . ALA B 2 44  ? -3.662  -11.883 9.341   1.00 52.70 ? 44  ALA B C   1 
ATOM   2872  O O   . ALA B 2 44  ? -4.199  -10.915 9.881   1.00 52.55 ? 44  ALA B O   1 
ATOM   2873  C CB  . ALA B 2 44  ? -4.873  -14.014 9.893   1.00 52.92 ? 44  ALA B CB  1 
ATOM   2874  N N   . ILE B 2 45  ? -2.342  -11.993 9.201   1.00 52.39 ? 45  ILE B N   1 
ATOM   2875  C CA  . ILE B 2 45  ? -1.432  -10.904 9.564   1.00 52.08 ? 45  ILE B CA  1 
ATOM   2876  C C   . ILE B 2 45  ? -1.602  -9.729  8.594   1.00 51.83 ? 45  ILE B C   1 
ATOM   2877  O O   . ILE B 2 45  ? -1.799  -8.590  9.025   1.00 51.79 ? 45  ILE B O   1 
ATOM   2878  C CB  . ILE B 2 45  ? 0.049   -11.374 9.625   1.00 52.09 ? 45  ILE B CB  1 
ATOM   2879  C CG1 . ILE B 2 45  ? 0.277   -12.265 10.849  1.00 51.80 ? 45  ILE B CG1 1 
ATOM   2880  C CG2 . ILE B 2 45  ? 1.008   -10.179 9.668   1.00 52.22 ? 45  ILE B CG2 1 
ATOM   2881  C CD1 . ILE B 2 45  ? 1.587   -13.043 10.815  1.00 51.86 ? 45  ILE B CD1 1 
ATOM   2882  N N   . ASP B 2 46  ? -1.543  -10.019 7.293   1.00 51.42 ? 46  ASP B N   1 
ATOM   2883  C CA  . ASP B 2 46  ? -1.740  -9.015  6.249   1.00 51.11 ? 46  ASP B CA  1 
ATOM   2884  C C   . ASP B 2 46  ? -3.062  -8.269  6.414   1.00 50.69 ? 46  ASP B C   1 
ATOM   2885  O O   . ASP B 2 46  ? -3.105  -7.041  6.314   1.00 50.75 ? 46  ASP B O   1 
ATOM   2886  C CB  . ASP B 2 46  ? -1.695  -9.661  4.863   1.00 51.33 ? 46  ASP B CB  1 
ATOM   2887  C CG  . ASP B 2 46  ? -0.315  -10.187 4.496   1.00 52.11 ? 46  ASP B CG  1 
ATOM   2888  O OD1 . ASP B 2 46  ? -0.216  -10.889 3.467   1.00 52.90 ? 46  ASP B OD1 1 
ATOM   2889  O OD2 . ASP B 2 46  ? 0.668   -9.906  5.220   1.00 52.82 ? 46  ASP B OD2 1 
ATOM   2890  N N   . GLY B 2 47  ? -4.130  -9.019  6.673   1.00 50.07 ? 47  GLY B N   1 
ATOM   2891  C CA  . GLY B 2 47  ? -5.463  -8.453  6.853   1.00 49.25 ? 47  GLY B CA  1 
ATOM   2892  C C   . GLY B 2 47  ? -5.554  -7.507  8.035   1.00 48.84 ? 47  GLY B C   1 
ATOM   2893  O O   . GLY B 2 47  ? -6.072  -6.394  7.905   1.00 48.86 ? 47  GLY B O   1 
ATOM   2894  N N   . VAL B 2 48  ? -5.043  -7.947  9.184   1.00 48.28 ? 48  VAL B N   1 
ATOM   2895  C CA  . VAL B 2 48  ? -5.045  -7.129  10.400  1.00 47.70 ? 48  VAL B CA  1 
ATOM   2896  C C   . VAL B 2 48  ? -4.172  -5.889  10.234  1.00 47.42 ? 48  VAL B C   1 
ATOM   2897  O O   . VAL B 2 48  ? -4.604  -4.782  10.561  1.00 47.55 ? 48  VAL B O   1 
ATOM   2898  C CB  . VAL B 2 48  ? -4.622  -7.939  11.656  1.00 47.64 ? 48  VAL B CB  1 
ATOM   2899  C CG1 . VAL B 2 48  ? -4.344  -7.018  12.838  1.00 47.40 ? 48  VAL B CG1 1 
ATOM   2900  C CG2 . VAL B 2 48  ? -5.698  -8.945  12.022  1.00 47.44 ? 48  VAL B CG2 1 
ATOM   2901  N N   . THR B 2 49  ? -2.957  -6.072  9.719   1.00 47.00 ? 49  THR B N   1 
ATOM   2902  C CA  . THR B 2 49  ? -2.042  -4.954  9.489   1.00 46.59 ? 49  THR B CA  1 
ATOM   2903  C C   . THR B 2 49  ? -2.725  -3.883  8.636   1.00 46.20 ? 49  THR B C   1 
ATOM   2904  O O   . THR B 2 49  ? -2.792  -2.718  9.042   1.00 46.16 ? 49  THR B O   1 
ATOM   2905  C CB  . THR B 2 49  ? -0.701  -5.413  8.850   1.00 46.71 ? 49  THR B CB  1 
ATOM   2906  O OG1 . THR B 2 49  ? -0.066  -6.372  9.702   1.00 46.55 ? 49  THR B OG1 1 
ATOM   2907  C CG2 . THR B 2 49  ? 0.247   -4.232  8.654   1.00 46.84 ? 49  THR B CG2 1 
ATOM   2908  N N   . ASN B 2 50  ? -3.257  -4.290  7.481   1.00 45.65 ? 50  ASN B N   1 
ATOM   2909  C CA  . ASN B 2 50  ? -3.985  -3.381  6.584   1.00 45.21 ? 50  ASN B CA  1 
ATOM   2910  C C   . ASN B 2 50  ? -5.124  -2.626  7.269   1.00 44.78 ? 50  ASN B C   1 
ATOM   2911  O O   . ASN B 2 50  ? -5.306  -1.427  7.032   1.00 44.79 ? 50  ASN B O   1 
ATOM   2912  C CB  . ASN B 2 50  ? -4.525  -4.127  5.356   1.00 45.32 ? 50  ASN B CB  1 
ATOM   2913  C CG  . ASN B 2 50  ? -3.423  -4.615  4.423   1.00 45.54 ? 50  ASN B CG  1 
ATOM   2914  O OD1 . ASN B 2 50  ? -2.264  -4.202  4.523   1.00 45.99 ? 50  ASN B OD1 1 
ATOM   2915  N ND2 . ASN B 2 50  ? -3.787  -5.501  3.508   1.00 45.63 ? 50  ASN B ND2 1 
ATOM   2916  N N   . LYS B 2 51  ? -5.878  -3.334  8.112   1.00 44.11 ? 51  LYS B N   1 
ATOM   2917  C CA  . LYS B 2 51  ? -6.986  -2.748  8.865   1.00 43.65 ? 51  LYS B CA  1 
ATOM   2918  C C   . LYS B 2 51  ? -6.514  -1.617  9.783   1.00 43.58 ? 51  LYS B C   1 
ATOM   2919  O O   . LYS B 2 51  ? -7.088  -0.522  9.772   1.00 43.42 ? 51  LYS B O   1 
ATOM   2920  C CB  . LYS B 2 51  ? -7.724  -3.823  9.673   1.00 43.53 ? 51  LYS B CB  1 
ATOM   2921  C CG  . LYS B 2 51  ? -8.810  -3.280  10.605  1.00 42.76 ? 51  LYS B CG  1 
ATOM   2922  C CD  . LYS B 2 51  ? -9.468  -4.369  11.447  1.00 42.00 ? 51  LYS B CD  1 
ATOM   2923  C CE  . LYS B 2 51  ? -10.317 -5.313  10.610  1.00 40.51 ? 51  LYS B CE  1 
ATOM   2924  N NZ  . LYS B 2 51  ? -11.365 -5.952  11.437  1.00 40.45 ? 51  LYS B NZ  1 
ATOM   2925  N N   . VAL B 2 52  ? -5.469  -1.890  10.564  1.00 43.43 ? 52  VAL B N   1 
ATOM   2926  C CA  . VAL B 2 52  ? -4.880  -0.900  11.472  1.00 43.26 ? 52  VAL B CA  1 
ATOM   2927  C C   . VAL B 2 52  ? -4.437  0.355   10.707  1.00 43.37 ? 52  VAL B C   1 
ATOM   2928  O O   . VAL B 2 52  ? -4.716  1.479   11.140  1.00 43.14 ? 52  VAL B O   1 
ATOM   2929  C CB  . VAL B 2 52  ? -3.705  -1.500  12.290  1.00 43.16 ? 52  VAL B CB  1 
ATOM   2930  C CG1 . VAL B 2 52  ? -3.098  -0.458  13.222  1.00 43.08 ? 52  VAL B CG1 1 
ATOM   2931  C CG2 . VAL B 2 52  ? -4.176  -2.706  13.092  1.00 42.97 ? 52  VAL B CG2 1 
ATOM   2932  N N   . ASN B 2 53  ? -3.777  0.152   9.565   1.00 43.55 ? 53  ASN B N   1 
ATOM   2933  C CA  . ASN B 2 53  ? -3.333  1.255   8.704   1.00 43.91 ? 53  ASN B CA  1 
ATOM   2934  C C   . ASN B 2 53  ? -4.475  2.051   8.064   1.00 44.15 ? 53  ASN B C   1 
ATOM   2935  O O   . ASN B 2 53  ? -4.404  3.277   7.983   1.00 44.30 ? 53  ASN B O   1 
ATOM   2936  C CB  . ASN B 2 53  ? -2.360  0.751   7.632   1.00 43.80 ? 53  ASN B CB  1 
ATOM   2937  C CG  . ASN B 2 53  ? -1.019  0.326   8.211   1.00 44.26 ? 53  ASN B CG  1 
ATOM   2938  O OD1 . ASN B 2 53  ? -0.665  0.685   9.339   1.00 44.56 ? 53  ASN B OD1 1 
ATOM   2939  N ND2 . ASN B 2 53  ? -0.266  -0.446  7.441   1.00 44.50 ? 53  ASN B ND2 1 
ATOM   2940  N N   . SER B 2 54  ? -5.519  1.349   7.621   1.00 44.43 ? 54  SER B N   1 
ATOM   2941  C CA  . SER B 2 54  ? -6.716  1.987   7.071   1.00 44.65 ? 54  SER B CA  1 
ATOM   2942  C C   . SER B 2 54  ? -7.389  2.872   8.112   1.00 44.91 ? 54  SER B C   1 
ATOM   2943  O O   . SER B 2 54  ? -7.834  3.972   7.798   1.00 44.91 ? 54  SER B O   1 
ATOM   2944  C CB  . SER B 2 54  ? -7.711  0.940   6.567   1.00 44.49 ? 54  SER B CB  1 
ATOM   2945  O OG  . SER B 2 54  ? -7.266  0.363   5.358   1.00 44.48 ? 54  SER B OG  1 
ATOM   2946  N N   . ILE B 2 55  ? -7.450  2.378   9.346   1.00 45.32 ? 55  ILE B N   1 
ATOM   2947  C CA  . ILE B 2 55  ? -8.035  3.112   10.465  1.00 45.79 ? 55  ILE B CA  1 
ATOM   2948  C C   . ILE B 2 55  ? -7.271  4.410   10.746  1.00 46.28 ? 55  ILE B C   1 
ATOM   2949  O O   . ILE B 2 55  ? -7.880  5.472   10.869  1.00 46.30 ? 55  ILE B O   1 
ATOM   2950  C CB  . ILE B 2 55  ? -8.127  2.221   11.731  1.00 45.71 ? 55  ILE B CB  1 
ATOM   2951  C CG1 . ILE B 2 55  ? -9.221  1.162   11.550  1.00 45.36 ? 55  ILE B CG1 1 
ATOM   2952  C CG2 . ILE B 2 55  ? -8.383  3.060   12.987  1.00 45.78 ? 55  ILE B CG2 1 
ATOM   2953  C CD1 . ILE B 2 55  ? -9.258  0.096   12.634  1.00 45.11 ? 55  ILE B CD1 1 
ATOM   2954  N N   . ILE B 2 56  ? -5.945  4.319   10.825  1.00 46.97 ? 56  ILE B N   1 
ATOM   2955  C CA  . ILE B 2 56  ? -5.096  5.490   11.067  1.00 47.60 ? 56  ILE B CA  1 
ATOM   2956  C C   . ILE B 2 56  ? -5.134  6.467   9.885   1.00 48.15 ? 56  ILE B C   1 
ATOM   2957  O O   . ILE B 2 56  ? -5.364  7.661   10.082  1.00 48.32 ? 56  ILE B O   1 
ATOM   2958  C CB  . ILE B 2 56  ? -3.634  5.095   11.429  1.00 47.48 ? 56  ILE B CB  1 
ATOM   2959  C CG1 . ILE B 2 56  ? -3.610  4.264   12.719  1.00 47.31 ? 56  ILE B CG1 1 
ATOM   2960  C CG2 . ILE B 2 56  ? -2.750  6.339   11.579  1.00 47.45 ? 56  ILE B CG2 1 
ATOM   2961  C CD1 . ILE B 2 56  ? -2.284  3.558   12.996  1.00 46.60 ? 56  ILE B CD1 1 
ATOM   2962  N N   . ASP B 2 57  ? -4.929  5.956   8.670   1.00 48.85 ? 57  ASP B N   1 
ATOM   2963  C CA  . ASP B 2 57  ? -4.980  6.776   7.450   1.00 49.58 ? 57  ASP B CA  1 
ATOM   2964  C C   . ASP B 2 57  ? -6.251  7.612   7.314   1.00 49.64 ? 57  ASP B C   1 
ATOM   2965  O O   . ASP B 2 57  ? -6.188  8.780   6.932   1.00 49.70 ? 57  ASP B O   1 
ATOM   2966  C CB  . ASP B 2 57  ? -4.810  5.910   6.196   1.00 49.76 ? 57  ASP B CB  1 
ATOM   2967  C CG  . ASP B 2 57  ? -3.354  5.670   5.840   1.00 51.13 ? 57  ASP B CG  1 
ATOM   2968  O OD1 . ASP B 2 57  ? -2.468  6.314   6.453   1.00 53.04 ? 57  ASP B OD1 1 
ATOM   2969  O OD2 . ASP B 2 57  ? -3.092  4.841   4.937   1.00 51.94 ? 57  ASP B OD2 1 
ATOM   2970  N N   . LYS B 2 58  ? -7.393  7.010   7.634   1.00 49.81 ? 58  LYS B N   1 
ATOM   2971  C CA  . LYS B 2 58  ? -8.693  7.657   7.471   1.00 50.17 ? 58  LYS B CA  1 
ATOM   2972  C C   . LYS B 2 58  ? -8.914  8.795   8.474   1.00 50.45 ? 58  LYS B C   1 
ATOM   2973  O O   . LYS B 2 58  ? -9.760  9.671   8.259   1.00 50.26 ? 58  LYS B O   1 
ATOM   2974  C CB  . LYS B 2 58  ? -9.811  6.614   7.568   1.00 50.09 ? 58  LYS B CB  1 
ATOM   2975  C CG  . LYS B 2 58  ? -11.034 6.879   6.682   1.00 50.67 ? 58  LYS B CG  1 
ATOM   2976  C CD  . LYS B 2 58  ? -10.677 7.173   5.219   1.00 51.12 ? 58  LYS B CD  1 
ATOM   2977  C CE  . LYS B 2 58  ? -10.156 5.949   4.481   1.00 51.31 ? 58  LYS B CE  1 
ATOM   2978  N NZ  . LYS B 2 58  ? -9.559  6.336   3.168   1.00 51.33 ? 58  LYS B NZ  1 
ATOM   2979  N N   . MET B 2 59  ? -8.131  8.780   9.552   1.00 50.84 ? 59  MET B N   1 
ATOM   2980  C CA  . MET B 2 59  ? -8.215  9.784   10.612  1.00 51.14 ? 59  MET B CA  1 
ATOM   2981  C C   . MET B 2 59  ? -7.190  10.908  10.453  1.00 51.29 ? 59  MET B C   1 
ATOM   2982  O O   . MET B 2 59  ? -7.195  11.867  11.226  1.00 51.37 ? 59  MET B O   1 
ATOM   2983  C CB  . MET B 2 59  ? -8.037  9.121   11.980  1.00 51.23 ? 59  MET B CB  1 
ATOM   2984  C CG  . MET B 2 59  ? -9.086  8.077   12.308  1.00 51.48 ? 59  MET B CG  1 
ATOM   2985  S SD  . MET B 2 59  ? -10.700 8.781   12.664  1.00 51.45 ? 59  MET B SD  1 
ATOM   2986  C CE  . MET B 2 59  ? -11.647 7.290   12.932  1.00 52.30 ? 59  MET B CE  1 
ATOM   2987  N N   . ASN B 2 60  ? -6.317  10.796  9.455   1.00 51.44 ? 60  ASN B N   1 
ATOM   2988  C CA  . ASN B 2 60  ? -5.267  11.794  9.250   1.00 51.76 ? 60  ASN B CA  1 
ATOM   2989  C C   . ASN B 2 60  ? -5.822  13.164  8.841   1.00 51.64 ? 60  ASN B C   1 
ATOM   2990  O O   . ASN B 2 60  ? -5.124  14.177  8.912   1.00 51.89 ? 60  ASN B O   1 
ATOM   2991  C CB  . ASN B 2 60  ? -4.236  11.302  8.229   1.00 51.86 ? 60  ASN B CB  1 
ATOM   2992  C CG  . ASN B 2 60  ? -4.599  11.677  6.804   1.00 52.90 ? 60  ASN B CG  1 
ATOM   2993  O OD1 . ASN B 2 60  ? -3.907  12.478  6.168   1.00 54.45 ? 60  ASN B OD1 1 
ATOM   2994  N ND2 . ASN B 2 60  ? -5.701  11.120  6.301   1.00 53.24 ? 60  ASN B ND2 1 
ATOM   2995  N N   . THR B 2 61  ? -7.076  13.184  8.410   1.00 51.42 ? 61  THR B N   1 
ATOM   2996  C CA  . THR B 2 61  ? -7.715  14.421  7.981   1.00 51.35 ? 61  THR B CA  1 
ATOM   2997  C C   . THR B 2 61  ? -8.754  14.898  9.013   1.00 51.05 ? 61  THR B C   1 
ATOM   2998  O O   . THR B 2 61  ? -9.853  15.344  8.670   1.00 51.14 ? 61  THR B O   1 
ATOM   2999  C CB  . THR B 2 61  ? -8.293  14.294  6.542   1.00 51.35 ? 61  THR B CB  1 
ATOM   3000  O OG1 . THR B 2 61  ? -8.735  15.578  6.090   1.00 51.60 ? 61  THR B OG1 1 
ATOM   3001  C CG2 . THR B 2 61  ? -9.452  13.278  6.475   1.00 51.48 ? 61  THR B CG2 1 
ATOM   3002  N N   . GLN B 2 62  ? -8.368  14.812  10.283  1.00 50.53 ? 62  GLN B N   1 
ATOM   3003  C CA  . GLN B 2 62  ? -9.227  15.184  11.399  1.00 49.93 ? 62  GLN B CA  1 
ATOM   3004  C C   . GLN B 2 62  ? -9.226  16.699  11.619  1.00 49.26 ? 62  GLN B C   1 
ATOM   3005  O O   . GLN B 2 62  ? -8.359  17.411  11.103  1.00 49.28 ? 62  GLN B O   1 
ATOM   3006  C CB  . GLN B 2 62  ? -8.757  14.475  12.668  1.00 50.07 ? 62  GLN B CB  1 
ATOM   3007  C CG  . GLN B 2 62  ? -9.875  14.061  13.598  1.00 50.89 ? 62  GLN B CG  1 
ATOM   3008  C CD  . GLN B 2 62  ? -9.430  13.913  15.040  1.00 52.00 ? 62  GLN B CD  1 
ATOM   3009  O OE1 . GLN B 2 62  ? -9.300  12.799  15.547  1.00 52.14 ? 62  GLN B OE1 1 
ATOM   3010  N NE2 . GLN B 2 62  ? -9.192  15.041  15.708  1.00 52.22 ? 62  GLN B NE2 1 
ATOM   3011  N N   . PHE B 2 63  ? -10.203 17.174  12.390  1.00 48.27 ? 63  PHE B N   1 
ATOM   3012  C CA  . PHE B 2 63  ? -10.347 18.588  12.724  1.00 47.36 ? 63  PHE B CA  1 
ATOM   3013  C C   . PHE B 2 63  ? -9.250  19.061  13.680  1.00 47.11 ? 63  PHE B C   1 
ATOM   3014  O O   . PHE B 2 63  ? -8.907  18.369  14.637  1.00 47.09 ? 63  PHE B O   1 
ATOM   3015  C CB  . PHE B 2 63  ? -11.730 18.833  13.343  1.00 47.06 ? 63  PHE B CB  1 
ATOM   3016  C CG  . PHE B 2 63  ? -11.974 20.256  13.750  1.00 46.04 ? 63  PHE B CG  1 
ATOM   3017  C CD1 . PHE B 2 63  ? -12.542 21.159  12.857  1.00 45.39 ? 63  PHE B CD1 1 
ATOM   3018  C CD2 . PHE B 2 63  ? -11.644 20.694  15.032  1.00 45.14 ? 63  PHE B CD2 1 
ATOM   3019  C CE1 . PHE B 2 63  ? -12.770 22.480  13.229  1.00 44.98 ? 63  PHE B CE1 1 
ATOM   3020  C CE2 . PHE B 2 63  ? -11.863 22.011  15.412  1.00 44.82 ? 63  PHE B CE2 1 
ATOM   3021  C CZ  . PHE B 2 63  ? -12.428 22.908  14.511  1.00 44.95 ? 63  PHE B CZ  1 
ATOM   3022  N N   . GLU B 2 64  ? -8.724  20.255  13.421  1.00 46.82 ? 64  GLU B N   1 
ATOM   3023  C CA  . GLU B 2 64  ? -7.691  20.852  14.266  1.00 46.56 ? 64  GLU B CA  1 
ATOM   3024  C C   . GLU B 2 64  ? -8.190  22.132  14.932  1.00 45.96 ? 64  GLU B C   1 
ATOM   3025  O O   . GLU B 2 64  ? -8.400  23.153  14.267  1.00 45.83 ? 64  GLU B O   1 
ATOM   3026  C CB  . GLU B 2 64  ? -6.425  21.136  13.449  1.00 46.84 ? 64  GLU B CB  1 
ATOM   3027  C CG  . GLU B 2 64  ? -5.698  19.882  12.963  1.00 48.19 ? 64  GLU B CG  1 
ATOM   3028  C CD  . GLU B 2 64  ? -4.773  20.157  11.788  1.00 50.09 ? 64  GLU B CD  1 
ATOM   3029  O OE1 . GLU B 2 64  ? -4.029  21.166  11.824  1.00 50.90 ? 64  GLU B OE1 1 
ATOM   3030  O OE2 . GLU B 2 64  ? -4.788  19.357  10.827  1.00 50.53 ? 64  GLU B OE2 1 
ATOM   3031  N N   . ALA B 2 65  ? -8.380  22.064  16.247  1.00 45.24 ? 65  ALA B N   1 
ATOM   3032  C CA  . ALA B 2 65  ? -8.832  23.211  17.030  1.00 44.56 ? 65  ALA B CA  1 
ATOM   3033  C C   . ALA B 2 65  ? -7.771  24.308  17.070  1.00 44.07 ? 65  ALA B C   1 
ATOM   3034  O O   . ALA B 2 65  ? -6.587  24.027  17.233  1.00 44.12 ? 65  ALA B O   1 
ATOM   3035  C CB  . ALA B 2 65  ? -9.203  22.773  18.440  1.00 44.50 ? 65  ALA B CB  1 
ATOM   3036  N N   . VAL B 2 66  ? -8.204  25.553  16.903  1.00 43.46 ? 66  VAL B N   1 
ATOM   3037  C CA  . VAL B 2 66  ? -7.318  26.712  16.991  1.00 42.91 ? 66  VAL B CA  1 
ATOM   3038  C C   . VAL B 2 66  ? -7.909  27.692  17.999  1.00 42.58 ? 66  VAL B C   1 
ATOM   3039  O O   . VAL B 2 66  ? -9.107  28.000  17.944  1.00 42.88 ? 66  VAL B O   1 
ATOM   3040  C CB  . VAL B 2 66  ? -7.134  27.413  15.618  1.00 43.02 ? 66  VAL B CB  1 
ATOM   3041  C CG1 . VAL B 2 66  ? -6.325  28.705  15.762  1.00 42.88 ? 66  VAL B CG1 1 
ATOM   3042  C CG2 . VAL B 2 66  ? -6.467  26.480  14.611  1.00 43.03 ? 66  VAL B CG2 1 
ATOM   3043  N N   . GLY B 2 67  ? -7.072  28.168  18.922  1.00 41.81 ? 67  GLY B N   1 
ATOM   3044  C CA  . GLY B 2 67  ? -7.504  29.101  19.956  1.00 40.72 ? 67  GLY B CA  1 
ATOM   3045  C C   . GLY B 2 67  ? -7.866  30.453  19.374  1.00 40.14 ? 67  GLY B C   1 
ATOM   3046  O O   . GLY B 2 67  ? -7.150  30.992  18.521  1.00 40.28 ? 67  GLY B O   1 
ATOM   3047  N N   . ARG B 2 68  ? -8.992  30.996  19.821  1.00 39.23 ? 68  ARG B N   1 
ATOM   3048  C CA  . ARG B 2 68  ? -9.422  32.327  19.400  1.00 38.26 ? 68  ARG B CA  1 
ATOM   3049  C C   . ARG B 2 68  ? -9.838  33.151  20.602  1.00 37.38 ? 68  ARG B C   1 
ATOM   3050  O O   . ARG B 2 68  ? -10.277 32.604  21.611  1.00 37.29 ? 68  ARG B O   1 
ATOM   3051  C CB  . ARG B 2 68  ? -10.561 32.233  18.381  1.00 38.44 ? 68  ARG B CB  1 
ATOM   3052  C CG  . ARG B 2 68  ? -10.105 31.695  17.051  1.00 38.63 ? 68  ARG B CG  1 
ATOM   3053  C CD  . ARG B 2 68  ? -11.185 31.719  16.008  1.00 40.12 ? 68  ARG B CD  1 
ATOM   3054  N NE  . ARG B 2 68  ? -10.747 30.956  14.846  1.00 40.59 ? 68  ARG B NE  1 
ATOM   3055  C CZ  . ARG B 2 68  ? -11.051 29.682  14.633  1.00 41.36 ? 68  ARG B CZ  1 
ATOM   3056  N NH1 . ARG B 2 68  ? -11.821 29.025  15.492  1.00 41.36 ? 68  ARG B NH1 1 
ATOM   3057  N NH2 . ARG B 2 68  ? -10.593 29.067  13.549  1.00 42.36 ? 68  ARG B NH2 1 
ATOM   3058  N N   . GLU B 2 69  ? -9.688  34.466  20.494  1.00 36.44 ? 69  GLU B N   1 
ATOM   3059  C CA  . GLU B 2 69  ? -10.024 35.359  21.596  1.00 35.68 ? 69  GLU B CA  1 
ATOM   3060  C C   . GLU B 2 69  ? -11.053 36.422  21.225  1.00 34.63 ? 69  GLU B C   1 
ATOM   3061  O O   . GLU B 2 69  ? -11.092 36.892  20.095  1.00 34.38 ? 69  GLU B O   1 
ATOM   3062  C CB  . GLU B 2 69  ? -8.762  35.994  22.169  1.00 35.91 ? 69  GLU B CB  1 
ATOM   3063  C CG  . GLU B 2 69  ? -7.998  35.061  23.094  1.00 37.56 ? 69  GLU B CG  1 
ATOM   3064  C CD  . GLU B 2 69  ? -6.622  35.588  23.448  1.00 39.75 ? 69  GLU B CD  1 
ATOM   3065  O OE1 . GLU B 2 69  ? -6.430  35.994  24.616  1.00 40.47 ? 69  GLU B OE1 1 
ATOM   3066  O OE2 . GLU B 2 69  ? -5.740  35.603  22.557  1.00 40.11 ? 69  GLU B OE2 1 
ATOM   3067  N N   . PHE B 2 70  ? -11.879 36.785  22.202  1.00 33.82 ? 70  PHE B N   1 
ATOM   3068  C CA  . PHE B 2 70  ? -12.981 37.728  22.019  1.00 33.05 ? 70  PHE B CA  1 
ATOM   3069  C C   . PHE B 2 70  ? -13.112 38.668  23.217  1.00 32.82 ? 70  PHE B C   1 
ATOM   3070  O O   . PHE B 2 70  ? -12.802 38.281  24.340  1.00 32.58 ? 70  PHE B O   1 
ATOM   3071  C CB  . PHE B 2 70  ? -14.289 36.958  21.808  1.00 32.76 ? 70  PHE B CB  1 
ATOM   3072  C CG  . PHE B 2 70  ? -14.211 35.937  20.713  1.00 31.70 ? 70  PHE B CG  1 
ATOM   3073  C CD1 . PHE B 2 70  ? -14.443 36.300  19.390  1.00 30.61 ? 70  PHE B CD1 1 
ATOM   3074  C CD2 . PHE B 2 70  ? -13.876 34.618  20.997  1.00 30.74 ? 70  PHE B CD2 1 
ATOM   3075  C CE1 . PHE B 2 70  ? -14.356 35.363  18.371  1.00 29.91 ? 70  PHE B CE1 1 
ATOM   3076  C CE2 . PHE B 2 70  ? -13.788 33.678  19.982  1.00 30.45 ? 70  PHE B CE2 1 
ATOM   3077  C CZ  . PHE B 2 70  ? -14.031 34.055  18.666  1.00 29.67 ? 70  PHE B CZ  1 
ATOM   3078  N N   . ASN B 2 71  ? -13.553 39.903  22.976  1.00 32.61 ? 71  ASN B N   1 
ATOM   3079  C CA  . ASN B 2 71  ? -13.800 40.837  24.072  1.00 32.33 ? 71  ASN B CA  1 
ATOM   3080  C C   . ASN B 2 71  ? -15.179 40.604  24.689  1.00 32.37 ? 71  ASN B C   1 
ATOM   3081  O O   . ASN B 2 71  ? -15.929 39.738  24.221  1.00 32.16 ? 71  ASN B O   1 
ATOM   3082  C CB  . ASN B 2 71  ? -13.564 42.302  23.659  1.00 32.32 ? 71  ASN B CB  1 
ATOM   3083  C CG  . ASN B 2 71  ? -14.557 42.809  22.622  1.00 32.23 ? 71  ASN B CG  1 
ATOM   3084  O OD1 . ASN B 2 71  ? -15.774 42.683  22.769  1.00 32.02 ? 71  ASN B OD1 1 
ATOM   3085  N ND2 . ASN B 2 71  ? -14.030 43.426  21.580  1.00 32.53 ? 71  ASN B ND2 1 
ATOM   3086  N N   . ASN B 2 72  ? -15.514 41.354  25.737  1.00 32.29 ? 72  ASN B N   1 
ATOM   3087  C CA  . ASN B 2 72  ? -16.735 41.057  26.486  1.00 32.64 ? 72  ASN B CA  1 
ATOM   3088  C C   . ASN B 2 72  ? -18.028 41.644  25.894  1.00 32.18 ? 72  ASN B C   1 
ATOM   3089  O O   . ASN B 2 72  ? -19.097 41.545  26.501  1.00 32.10 ? 72  ASN B O   1 
ATOM   3090  C CB  . ASN B 2 72  ? -16.575 41.390  27.972  1.00 32.91 ? 72  ASN B CB  1 
ATOM   3091  C CG  . ASN B 2 72  ? -16.702 42.862  28.255  1.00 34.78 ? 72  ASN B CG  1 
ATOM   3092  O OD1 . ASN B 2 72  ? -16.135 43.702  27.548  1.00 36.91 ? 72  ASN B OD1 1 
ATOM   3093  N ND2 . ASN B 2 72  ? -17.448 43.191  29.304  1.00 37.19 ? 72  ASN B ND2 1 
ATOM   3094  N N   . LEU B 2 73  ? -17.920 42.243  24.709  1.00 31.78 ? 73  LEU B N   1 
ATOM   3095  C CA  . LEU B 2 73  ? -19.090 42.607  23.916  1.00 31.29 ? 73  LEU B CA  1 
ATOM   3096  C C   . LEU B 2 73  ? -19.177 41.715  22.679  1.00 30.99 ? 73  LEU B C   1 
ATOM   3097  O O   . LEU B 2 73  ? -19.867 42.041  21.711  1.00 31.34 ? 73  LEU B O   1 
ATOM   3098  C CB  . LEU B 2 73  ? -19.059 44.091  23.529  1.00 31.34 ? 73  LEU B CB  1 
ATOM   3099  C CG  . LEU B 2 73  ? -19.462 45.110  24.611  1.00 31.42 ? 73  LEU B CG  1 
ATOM   3100  C CD1 . LEU B 2 73  ? -19.083 46.534  24.192  1.00 30.68 ? 73  LEU B CD1 1 
ATOM   3101  C CD2 . LEU B 2 73  ? -20.957 45.019  24.965  1.00 30.89 ? 73  LEU B CD2 1 
ATOM   3102  N N   . GLU B 2 74  ? -18.466 40.588  22.725  1.00 30.29 ? 74  GLU B N   1 
ATOM   3103  C CA  . GLU B 2 74  ? -18.455 39.614  21.641  1.00 29.68 ? 74  GLU B CA  1 
ATOM   3104  C C   . GLU B 2 74  ? -18.776 38.224  22.186  1.00 29.30 ? 74  GLU B C   1 
ATOM   3105  O O   . GLU B 2 74  ? -18.211 37.233  21.743  1.00 28.93 ? 74  GLU B O   1 
ATOM   3106  C CB  . GLU B 2 74  ? -17.090 39.581  20.947  1.00 29.69 ? 74  GLU B CB  1 
ATOM   3107  C CG  . GLU B 2 74  ? -16.732 40.792  20.097  1.00 29.27 ? 74  GLU B CG  1 
ATOM   3108  C CD  . GLU B 2 74  ? -15.311 40.701  19.521  1.00 29.55 ? 74  GLU B CD  1 
ATOM   3109  O OE1 . GLU B 2 74  ? -14.395 40.226  20.237  1.00 29.71 ? 74  GLU B OE1 1 
ATOM   3110  O OE2 . GLU B 2 74  ? -15.106 41.096  18.349  1.00 27.87 ? 74  GLU B OE2 1 
ATOM   3111  N N   . ARG B 2 75  ? -19.694 38.159  23.141  1.00 29.25 ? 75  ARG B N   1 
ATOM   3112  C CA  . ARG B 2 75  ? -19.982 36.915  23.853  1.00 29.38 ? 75  ARG B CA  1 
ATOM   3113  C C   . ARG B 2 75  ? -20.774 35.919  23.022  1.00 28.84 ? 75  ARG B C   1 
ATOM   3114  O O   . ARG B 2 75  ? -20.650 34.708  23.218  1.00 28.76 ? 75  ARG B O   1 
ATOM   3115  C CB  . ARG B 2 75  ? -20.689 37.204  25.181  1.00 29.99 ? 75  ARG B CB  1 
ATOM   3116  C CG  . ARG B 2 75  ? -19.784 37.855  26.234  1.00 31.56 ? 75  ARG B CG  1 
ATOM   3117  C CD  . ARG B 2 75  ? -19.123 36.805  27.102  1.00 36.42 ? 75  ARG B CD  1 
ATOM   3118  N NE  . ARG B 2 75  ? -17.839 37.245  27.657  1.00 39.87 ? 75  ARG B NE  1 
ATOM   3119  C CZ  . ARG B 2 75  ? -17.693 37.934  28.786  1.00 40.80 ? 75  ARG B CZ  1 
ATOM   3120  N NH1 . ARG B 2 75  ? -18.755 38.292  29.502  1.00 41.46 ? 75  ARG B NH1 1 
ATOM   3121  N NH2 . ARG B 2 75  ? -16.476 38.271  29.196  1.00 42.48 ? 75  ARG B NH2 1 
ATOM   3122  N N   . ARG B 2 76  ? -21.571 36.432  22.087  1.00 28.47 ? 76  ARG B N   1 
ATOM   3123  C CA  . ARG B 2 76  ? -22.326 35.589  21.163  1.00 27.74 ? 76  ARG B CA  1 
ATOM   3124  C C   . ARG B 2 76  ? -21.408 34.796  20.233  1.00 27.78 ? 76  ARG B C   1 
ATOM   3125  O O   . ARG B 2 76  ? -21.566 33.582  20.116  1.00 27.52 ? 76  ARG B O   1 
ATOM   3126  C CB  . ARG B 2 76  ? -23.352 36.405  20.376  1.00 27.45 ? 76  ARG B CB  1 
ATOM   3127  C CG  . ARG B 2 76  ? -24.563 36.816  21.209  1.00 26.51 ? 76  ARG B CG  1 
ATOM   3128  C CD  . ARG B 2 76  ? -25.400 37.906  20.550  1.00 24.76 ? 76  ARG B CD  1 
ATOM   3129  N NE  . ARG B 2 76  ? -24.600 39.056  20.118  1.00 23.91 ? 76  ARG B NE  1 
ATOM   3130  C CZ  . ARG B 2 76  ? -24.674 39.612  18.912  1.00 23.20 ? 76  ARG B CZ  1 
ATOM   3131  N NH1 . ARG B 2 76  ? -25.534 39.143  18.009  1.00 23.44 ? 76  ARG B NH1 1 
ATOM   3132  N NH2 . ARG B 2 76  ? -23.900 40.646  18.612  1.00 20.70 ? 76  ARG B NH2 1 
ATOM   3133  N N   . ILE B 2 77  ? -20.445 35.464  19.595  1.00 27.85 ? 77  ILE B N   1 
ATOM   3134  C CA  . ILE B 2 77  ? -19.500 34.751  18.721  1.00 28.37 ? 77  ILE B CA  1 
ATOM   3135  C C   . ILE B 2 77  ? -18.508 33.858  19.475  1.00 28.45 ? 77  ILE B C   1 
ATOM   3136  O O   . ILE B 2 77  ? -18.146 32.784  18.975  1.00 28.43 ? 77  ILE B O   1 
ATOM   3137  C CB  . ILE B 2 77  ? -18.770 35.658  17.690  1.00 28.35 ? 77  ILE B CB  1 
ATOM   3138  C CG1 . ILE B 2 77  ? -18.209 36.919  18.354  1.00 29.01 ? 77  ILE B CG1 1 
ATOM   3139  C CG2 . ILE B 2 77  ? -19.706 35.992  16.525  1.00 29.08 ? 77  ILE B CG2 1 
ATOM   3140  C CD1 . ILE B 2 77  ? -17.501 37.882  17.385  1.00 29.34 ? 77  ILE B CD1 1 
ATOM   3141  N N   . GLU B 2 78  ? -18.092 34.291  20.669  1.00 28.35 ? 78  GLU B N   1 
ATOM   3142  C CA  . GLU B 2 78  ? -17.276 33.462  21.559  1.00 28.64 ? 78  GLU B CA  1 
ATOM   3143  C C   . GLU B 2 78  ? -17.980 32.135  21.841  1.00 28.84 ? 78  GLU B C   1 
ATOM   3144  O O   . GLU B 2 78  ? -17.382 31.065  21.722  1.00 28.84 ? 78  GLU B O   1 
ATOM   3145  C CB  . GLU B 2 78  ? -16.975 34.192  22.876  1.00 28.64 ? 78  GLU B CB  1 
ATOM   3146  C CG  . GLU B 2 78  ? -16.301 33.318  23.941  1.00 29.57 ? 78  GLU B CG  1 
ATOM   3147  C CD  . GLU B 2 78  ? -15.897 34.095  25.180  1.00 32.59 ? 78  GLU B CD  1 
ATOM   3148  O OE1 . GLU B 2 78  ? -16.785 34.462  25.989  1.00 34.20 ? 78  GLU B OE1 1 
ATOM   3149  O OE2 . GLU B 2 78  ? -14.681 34.336  25.355  1.00 33.68 ? 78  GLU B OE2 1 
ATOM   3150  N N   . ASN B 2 79  ? -19.252 32.227  22.215  1.00 29.02 ? 79  ASN B N   1 
ATOM   3151  C CA  . ASN B 2 79  ? -20.090 31.070  22.471  1.00 29.60 ? 79  ASN B CA  1 
ATOM   3152  C C   . ASN B 2 79  ? -20.233 30.173  21.248  1.00 29.58 ? 79  ASN B C   1 
ATOM   3153  O O   . ASN B 2 79  ? -20.156 28.944  21.356  1.00 29.30 ? 79  ASN B O   1 
ATOM   3154  C CB  . ASN B 2 79  ? -21.466 31.533  22.940  1.00 30.06 ? 79  ASN B CB  1 
ATOM   3155  C CG  . ASN B 2 79  ? -22.335 30.395  23.395  1.00 31.98 ? 79  ASN B CG  1 
ATOM   3156  O OD1 . ASN B 2 79  ? -23.334 30.053  22.742  1.00 34.09 ? 79  ASN B OD1 1 
ATOM   3157  N ND2 . ASN B 2 79  ? -21.961 29.784  24.521  1.00 33.81 ? 79  ASN B ND2 1 
ATOM   3158  N N   . LEU B 2 80  ? -20.431 30.798  20.086  1.00 29.78 ? 80  LEU B N   1 
ATOM   3159  C CA  . LEU B 2 80  ? -20.539 30.082  18.813  1.00 29.93 ? 80  LEU B CA  1 
ATOM   3160  C C   . LEU B 2 80  ? -19.230 29.369  18.462  1.00 30.03 ? 80  LEU B C   1 
ATOM   3161  O O   . LEU B 2 80  ? -19.248 28.223  18.010  1.00 29.82 ? 80  LEU B O   1 
ATOM   3162  C CB  . LEU B 2 80  ? -21.017 31.035  17.700  1.00 29.97 ? 80  LEU B CB  1 
ATOM   3163  C CG  . LEU B 2 80  ? -20.729 30.944  16.188  1.00 29.79 ? 80  LEU B CG  1 
ATOM   3164  C CD1 . LEU B 2 80  ? -20.890 29.567  15.592  1.00 29.36 ? 80  LEU B CD1 1 
ATOM   3165  C CD2 . LEU B 2 80  ? -21.637 31.930  15.455  1.00 30.46 ? 80  LEU B CD2 1 
ATOM   3166  N N   . ASN B 2 81  ? -18.105 30.043  18.697  1.00 30.33 ? 81  ASN B N   1 
ATOM   3167  C CA  . ASN B 2 81  ? -16.784 29.449  18.494  1.00 30.83 ? 81  ASN B CA  1 
ATOM   3168  C C   . ASN B 2 81  ? -16.571 28.205  19.360  1.00 31.25 ? 81  ASN B C   1 
ATOM   3169  O O   . ASN B 2 81  ? -16.071 27.181  18.888  1.00 31.21 ? 81  ASN B O   1 
ATOM   3170  C CB  . ASN B 2 81  ? -15.690 30.484  18.760  1.00 30.77 ? 81  ASN B CB  1 
ATOM   3171  C CG  . ASN B 2 81  ? -14.294 29.938  18.520  1.00 30.78 ? 81  ASN B CG  1 
ATOM   3172  O OD1 . ASN B 2 81  ? -13.862 29.772  17.381  1.00 30.94 ? 81  ASN B OD1 1 
ATOM   3173  N ND2 . ASN B 2 81  ? -13.577 29.669  19.601  1.00 30.64 ? 81  ASN B ND2 1 
ATOM   3174  N N   . LYS B 2 82  ? -16.975 28.301  20.621  1.00 31.95 ? 82  LYS B N   1 
ATOM   3175  C CA  . LYS B 2 82  ? -16.823 27.219  21.577  1.00 32.71 ? 82  LYS B CA  1 
ATOM   3176  C C   . LYS B 2 82  ? -17.663 26.020  21.149  1.00 33.09 ? 82  LYS B C   1 
ATOM   3177  O O   . LYS B 2 82  ? -17.148 24.914  21.027  1.00 33.33 ? 82  LYS B O   1 
ATOM   3178  C CB  . LYS B 2 82  ? -17.226 27.698  22.973  1.00 32.71 ? 82  LYS B CB  1 
ATOM   3179  C CG  . LYS B 2 82  ? -16.806 26.777  24.106  1.00 34.38 ? 82  LYS B CG  1 
ATOM   3180  C CD  . LYS B 2 82  ? -17.495 27.162  25.422  1.00 37.11 ? 82  LYS B CD  1 
ATOM   3181  C CE  . LYS B 2 82  ? -16.799 26.540  26.632  1.00 37.78 ? 82  LYS B CE  1 
ATOM   3182  N NZ  . LYS B 2 82  ? -16.815 25.046  26.602  1.00 38.51 ? 82  LYS B NZ  1 
ATOM   3183  N N   . LYS B 2 83  ? -18.951 26.257  20.904  1.00 33.73 ? 83  LYS B N   1 
ATOM   3184  C CA  . LYS B 2 83  ? -19.898 25.207  20.531  1.00 34.16 ? 83  LYS B CA  1 
ATOM   3185  C C   . LYS B 2 83  ? -19.486 24.473  19.274  1.00 34.29 ? 83  LYS B C   1 
ATOM   3186  O O   . LYS B 2 83  ? -19.672 23.260  19.176  1.00 34.53 ? 83  LYS B O   1 
ATOM   3187  C CB  . LYS B 2 83  ? -21.311 25.775  20.337  1.00 34.30 ? 83  LYS B CB  1 
ATOM   3188  C CG  . LYS B 2 83  ? -22.015 26.205  21.617  1.00 35.25 ? 83  LYS B CG  1 
ATOM   3189  C CD  . LYS B 2 83  ? -22.375 25.026  22.510  1.00 37.86 ? 83  LYS B CD  1 
ATOM   3190  C CE  . LYS B 2 83  ? -23.350 25.442  23.612  1.00 39.96 ? 83  LYS B CE  1 
ATOM   3191  N NZ  . LYS B 2 83  ? -22.878 26.590  24.456  1.00 40.57 ? 83  LYS B NZ  1 
ATOM   3192  N N   . MET B 2 84  ? -18.927 25.202  18.315  1.00 34.49 ? 84  MET B N   1 
ATOM   3193  C CA  . MET B 2 84  ? -18.538 24.587  17.060  1.00 34.94 ? 84  MET B CA  1 
ATOM   3194  C C   . MET B 2 84  ? -17.275 23.730  17.199  1.00 35.03 ? 84  MET B C   1 
ATOM   3195  O O   . MET B 2 84  ? -17.219 22.627  16.655  1.00 35.18 ? 84  MET B O   1 
ATOM   3196  C CB  . MET B 2 84  ? -18.414 25.620  15.939  1.00 34.95 ? 84  MET B CB  1 
ATOM   3197  C CG  . MET B 2 84  ? -17.037 26.160  15.714  1.00 36.25 ? 84  MET B CG  1 
ATOM   3198  S SD  . MET B 2 84  ? -16.620 25.936  13.988  1.00 39.46 ? 84  MET B SD  1 
ATOM   3199  C CE  . MET B 2 84  ? -14.844 25.692  14.084  1.00 36.47 ? 84  MET B CE  1 
ATOM   3200  N N   . GLU B 2 85  ? -16.279 24.229  17.934  1.00 35.19 ? 85  GLU B N   1 
ATOM   3201  C CA  . GLU B 2 85  ? -15.045 23.476  18.157  1.00 35.48 ? 85  GLU B CA  1 
ATOM   3202  C C   . GLU B 2 85  ? -15.297 22.229  19.002  1.00 35.17 ? 85  GLU B C   1 
ATOM   3203  O O   . GLU B 2 85  ? -14.791 21.152  18.676  1.00 35.14 ? 85  GLU B O   1 
ATOM   3204  C CB  . GLU B 2 85  ? -13.935 24.349  18.759  1.00 35.78 ? 85  GLU B CB  1 
ATOM   3205  C CG  . GLU B 2 85  ? -13.366 25.383  17.771  1.00 37.49 ? 85  GLU B CG  1 
ATOM   3206  C CD  . GLU B 2 85  ? -11.936 25.821  18.087  1.00 39.80 ? 85  GLU B CD  1 
ATOM   3207  O OE1 . GLU B 2 85  ? -11.646 26.171  19.262  1.00 40.68 ? 85  GLU B OE1 1 
ATOM   3208  O OE2 . GLU B 2 85  ? -11.105 25.827  17.148  1.00 39.60 ? 85  GLU B OE2 1 
ATOM   3209  N N   . ASP B 2 86  ? -16.093 22.366  20.062  1.00 34.69 ? 86  ASP B N   1 
ATOM   3210  C CA  . ASP B 2 86  ? -16.493 21.207  20.869  1.00 34.56 ? 86  ASP B CA  1 
ATOM   3211  C C   . ASP B 2 86  ? -17.308 20.221  20.043  1.00 33.99 ? 86  ASP B C   1 
ATOM   3212  O O   . ASP B 2 86  ? -17.188 19.009  20.221  1.00 33.76 ? 86  ASP B O   1 
ATOM   3213  C CB  . ASP B 2 86  ? -17.295 21.628  22.101  1.00 34.84 ? 86  ASP B CB  1 
ATOM   3214  C CG  . ASP B 2 86  ? -16.424 22.192  23.216  1.00 36.03 ? 86  ASP B CG  1 
ATOM   3215  O OD1 . ASP B 2 86  ? -15.175 22.128  23.130  1.00 36.61 ? 86  ASP B OD1 1 
ATOM   3216  O OD2 . ASP B 2 86  ? -17.007 22.707  24.194  1.00 38.02 ? 86  ASP B OD2 1 
ATOM   3217  N N   . GLY B 2 87  ? -18.129 20.757  19.142  1.00 33.49 ? 87  GLY B N   1 
ATOM   3218  C CA  . GLY B 2 87  ? -18.926 19.957  18.218  1.00 32.81 ? 87  GLY B CA  1 
ATOM   3219  C C   . GLY B 2 87  ? -18.089 19.019  17.366  1.00 32.44 ? 87  GLY B C   1 
ATOM   3220  O O   . GLY B 2 87  ? -18.387 17.826  17.275  1.00 32.52 ? 87  GLY B O   1 
ATOM   3221  N N   . PHE B 2 88  ? -17.038 19.551  16.748  1.00 31.84 ? 88  PHE B N   1 
ATOM   3222  C CA  . PHE B 2 88  ? -16.160 18.736  15.917  1.00 31.49 ? 88  PHE B CA  1 
ATOM   3223  C C   . PHE B 2 88  ? -15.314 17.756  16.726  1.00 31.36 ? 88  PHE B C   1 
ATOM   3224  O O   . PHE B 2 88  ? -15.100 16.624  16.297  1.00 31.46 ? 88  PHE B O   1 
ATOM   3225  C CB  . PHE B 2 88  ? -15.288 19.601  15.004  1.00 31.36 ? 88  PHE B CB  1 
ATOM   3226  C CG  . PHE B 2 88  ? -16.018 20.130  13.800  1.00 31.18 ? 88  PHE B CG  1 
ATOM   3227  C CD1 . PHE B 2 88  ? -16.523 19.261  12.842  1.00 30.99 ? 88  PHE B CD1 1 
ATOM   3228  C CD2 . PHE B 2 88  ? -16.201 21.496  13.626  1.00 30.93 ? 88  PHE B CD2 1 
ATOM   3229  C CE1 . PHE B 2 88  ? -17.206 19.743  11.729  1.00 31.73 ? 88  PHE B CE1 1 
ATOM   3230  C CE2 . PHE B 2 88  ? -16.879 21.989  12.518  1.00 31.44 ? 88  PHE B CE2 1 
ATOM   3231  C CZ  . PHE B 2 88  ? -17.385 21.111  11.565  1.00 31.47 ? 88  PHE B CZ  1 
ATOM   3232  N N   . LEU B 2 89  ? -14.845 18.190  17.891  1.00 31.11 ? 89  LEU B N   1 
ATOM   3233  C CA  . LEU B 2 89  ? -14.161 17.301  18.823  1.00 30.99 ? 89  LEU B CA  1 
ATOM   3234  C C   . LEU B 2 89  ? -15.038 16.090  19.159  1.00 30.88 ? 89  LEU B C   1 
ATOM   3235  O O   . LEU B 2 89  ? -14.586 14.951  19.045  1.00 30.79 ? 89  LEU B O   1 
ATOM   3236  C CB  . LEU B 2 89  ? -13.751 18.056  20.093  1.00 30.89 ? 89  LEU B CB  1 
ATOM   3237  C CG  . LEU B 2 89  ? -12.330 18.641  20.224  1.00 31.74 ? 89  LEU B CG  1 
ATOM   3238  C CD1 . LEU B 2 89  ? -11.644 18.982  18.890  1.00 31.47 ? 89  LEU B CD1 1 
ATOM   3239  C CD2 . LEU B 2 89  ? -12.324 19.855  21.165  1.00 30.97 ? 89  LEU B CD2 1 
ATOM   3240  N N   . ASP B 2 90  ? -16.293 16.344  19.537  1.00 30.52 ? 90  ASP B N   1 
ATOM   3241  C CA  . ASP B 2 90  ? -17.244 15.281  19.855  1.00 30.31 ? 90  ASP B CA  1 
ATOM   3242  C C   . ASP B 2 90  ? -17.508 14.345  18.659  1.00 30.00 ? 90  ASP B C   1 
ATOM   3243  O O   . ASP B 2 90  ? -17.519 13.118  18.820  1.00 29.92 ? 90  ASP B O   1 
ATOM   3244  C CB  . ASP B 2 90  ? -18.559 15.867  20.399  1.00 30.56 ? 90  ASP B CB  1 
ATOM   3245  C CG  . ASP B 2 90  ? -18.379 16.631  21.729  1.00 31.78 ? 90  ASP B CG  1 
ATOM   3246  O OD1 . ASP B 2 90  ? -17.449 16.314  22.513  1.00 32.62 ? 90  ASP B OD1 1 
ATOM   3247  O OD2 . ASP B 2 90  ? -19.183 17.558  21.995  1.00 32.22 ? 90  ASP B OD2 1 
ATOM   3248  N N   . VAL B 2 91  ? -17.695 14.920  17.468  1.00 29.51 ? 91  VAL B N   1 
ATOM   3249  C CA  . VAL B 2 91  ? -17.960 14.146  16.251  1.00 29.08 ? 91  VAL B CA  1 
ATOM   3250  C C   . VAL B 2 91  ? -16.807 13.179  15.937  1.00 29.31 ? 91  VAL B C   1 
ATOM   3251  O O   . VAL B 2 91  ? -17.032 11.996  15.634  1.00 29.43 ? 91  VAL B O   1 
ATOM   3252  C CB  . VAL B 2 91  ? -18.269 15.073  15.033  1.00 29.02 ? 91  VAL B CB  1 
ATOM   3253  C CG1 . VAL B 2 91  ? -18.156 14.321  13.703  1.00 28.13 ? 91  VAL B CG1 1 
ATOM   3254  C CG2 . VAL B 2 91  ? -19.649 15.694  15.171  1.00 28.67 ? 91  VAL B CG2 1 
ATOM   3255  N N   . TRP B 2 92  ? -15.579 13.681  16.028  1.00 29.24 ? 92  TRP B N   1 
ATOM   3256  C CA  . TRP B 2 92  ? -14.402 12.869  15.741  1.00 29.34 ? 92  TRP B CA  1 
ATOM   3257  C C   . TRP B 2 92  ? -14.067 11.875  16.853  1.00 29.47 ? 92  TRP B C   1 
ATOM   3258  O O   . TRP B 2 92  ? -13.556 10.790  16.577  1.00 29.77 ? 92  TRP B O   1 
ATOM   3259  C CB  . TRP B 2 92  ? -13.202 13.748  15.397  1.00 29.16 ? 92  TRP B CB  1 
ATOM   3260  C CG  . TRP B 2 92  ? -13.302 14.338  14.032  1.00 28.84 ? 92  TRP B CG  1 
ATOM   3261  C CD1 . TRP B 2 92  ? -13.664 15.611  13.721  1.00 28.69 ? 92  TRP B CD1 1 
ATOM   3262  C CD2 . TRP B 2 92  ? -13.041 13.675  12.784  1.00 28.19 ? 92  TRP B CD2 1 
ATOM   3263  N NE1 . TRP B 2 92  ? -13.643 15.789  12.358  1.00 29.47 ? 92  TRP B NE1 1 
ATOM   3264  C CE2 . TRP B 2 92  ? -13.265 14.616  11.759  1.00 28.49 ? 92  TRP B CE2 1 
ATOM   3265  C CE3 . TRP B 2 92  ? -12.642 12.378  12.435  1.00 28.71 ? 92  TRP B CE3 1 
ATOM   3266  C CZ2 . TRP B 2 92  ? -13.101 14.306  10.403  1.00 28.29 ? 92  TRP B CZ2 1 
ATOM   3267  C CZ3 . TRP B 2 92  ? -12.474 12.069  11.084  1.00 28.65 ? 92  TRP B CZ3 1 
ATOM   3268  C CH2 . TRP B 2 92  ? -12.704 13.032  10.086  1.00 28.38 ? 92  TRP B CH2 1 
ATOM   3269  N N   . THR B 2 93  ? -14.362 12.239  18.097  1.00 29.59 ? 93  THR B N   1 
ATOM   3270  C CA  . THR B 2 93  ? -14.265 11.296  19.210  1.00 29.91 ? 93  THR B CA  1 
ATOM   3271  C C   . THR B 2 93  ? -15.240 10.127  18.988  1.00 30.08 ? 93  THR B C   1 
ATOM   3272  O O   . THR B 2 93  ? -14.879 8.971   19.190  1.00 30.13 ? 93  THR B O   1 
ATOM   3273  C CB  . THR B 2 93  ? -14.522 11.993  20.563  1.00 29.81 ? 93  THR B CB  1 
ATOM   3274  O OG1 . THR B 2 93  ? -13.532 13.007  20.761  1.00 30.55 ? 93  THR B OG1 1 
ATOM   3275  C CG2 . THR B 2 93  ? -14.456 11.014  21.724  1.00 29.57 ? 93  THR B CG2 1 
ATOM   3276  N N   . TYR B 2 94  ? -16.458 10.437  18.548  1.00 30.23 ? 94  TYR B N   1 
ATOM   3277  C CA  . TYR B 2 94  ? -17.451 9.411   18.216  1.00 30.34 ? 94  TYR B CA  1 
ATOM   3278  C C   . TYR B 2 94  ? -16.967 8.507   17.082  1.00 30.39 ? 94  TYR B C   1 
ATOM   3279  O O   . TYR B 2 94  ? -16.994 7.285   17.212  1.00 30.57 ? 94  TYR B O   1 
ATOM   3280  C CB  . TYR B 2 94  ? -18.802 10.055  17.875  1.00 30.42 ? 94  TYR B CB  1 
ATOM   3281  C CG  . TYR B 2 94  ? -19.833 9.115   17.275  1.00 30.51 ? 94  TYR B CG  1 
ATOM   3282  C CD1 . TYR B 2 94  ? -20.709 8.386   18.089  1.00 30.39 ? 94  TYR B CD1 1 
ATOM   3283  C CD2 . TYR B 2 94  ? -19.949 8.976   15.887  1.00 30.49 ? 94  TYR B CD2 1 
ATOM   3284  C CE1 . TYR B 2 94  ? -21.663 7.525   17.534  1.00 30.46 ? 94  TYR B CE1 1 
ATOM   3285  C CE2 . TYR B 2 94  ? -20.891 8.120   15.324  1.00 30.96 ? 94  TYR B CE2 1 
ATOM   3286  C CZ  . TYR B 2 94  ? -21.744 7.398   16.150  1.00 31.03 ? 94  TYR B CZ  1 
ATOM   3287  O OH  . TYR B 2 94  ? -22.676 6.562   15.575  1.00 31.73 ? 94  TYR B OH  1 
ATOM   3288  N N   . ASN B 2 95  ? -16.510 9.110   15.987  1.00 30.29 ? 95  ASN B N   1 
ATOM   3289  C CA  . ASN B 2 95  ? -16.003 8.358   14.844  1.00 30.32 ? 95  ASN B CA  1 
ATOM   3290  C C   . ASN B 2 95  ? -14.886 7.392   15.210  1.00 30.54 ? 95  ASN B C   1 
ATOM   3291  O O   . ASN B 2 95  ? -14.860 6.262   14.727  1.00 30.54 ? 95  ASN B O   1 
ATOM   3292  C CB  . ASN B 2 95  ? -15.496 9.298   13.751  1.00 30.33 ? 95  ASN B CB  1 
ATOM   3293  C CG  . ASN B 2 95  ? -16.614 9.987   12.979  1.00 30.44 ? 95  ASN B CG  1 
ATOM   3294  O OD1 . ASN B 2 95  ? -16.344 10.882  12.180  1.00 32.30 ? 95  ASN B OD1 1 
ATOM   3295  N ND2 . ASN B 2 95  ? -17.861 9.578   13.202  1.00 29.26 ? 95  ASN B ND2 1 
ATOM   3296  N N   . ALA B 2 96  ? -13.960 7.846   16.053  1.00 30.78 ? 96  ALA B N   1 
ATOM   3297  C CA  . ALA B 2 96  ? -12.830 7.028   16.481  1.00 30.93 ? 96  ALA B CA  1 
ATOM   3298  C C   . ALA B 2 96  ? -13.291 5.886   17.379  1.00 31.05 ? 96  ALA B C   1 
ATOM   3299  O O   . ALA B 2 96  ? -12.952 4.727   17.141  1.00 30.65 ? 96  ALA B O   1 
ATOM   3300  C CB  . ALA B 2 96  ? -11.783 7.886   17.185  1.00 31.02 ? 96  ALA B CB  1 
ATOM   3301  N N   . GLU B 2 97  ? -14.082 6.219   18.395  1.00 31.44 ? 97  GLU B N   1 
ATOM   3302  C CA  . GLU B 2 97  ? -14.564 5.228   19.352  1.00 32.10 ? 97  GLU B CA  1 
ATOM   3303  C C   . GLU B 2 97  ? -15.427 4.163   18.683  1.00 32.25 ? 97  GLU B C   1 
ATOM   3304  O O   . GLU B 2 97  ? -15.264 2.972   18.950  1.00 32.67 ? 97  GLU B O   1 
ATOM   3305  C CB  . GLU B 2 97  ? -15.313 5.895   20.508  1.00 32.21 ? 97  GLU B CB  1 
ATOM   3306  C CG  . GLU B 2 97  ? -14.394 6.638   21.483  1.00 33.43 ? 97  GLU B CG  1 
ATOM   3307  C CD  . GLU B 2 97  ? -15.121 7.194   22.706  1.00 35.08 ? 97  GLU B CD  1 
ATOM   3308  O OE1 . GLU B 2 97  ? -16.361 7.018   22.816  1.00 35.87 ? 97  GLU B OE1 1 
ATOM   3309  O OE2 . GLU B 2 97  ? -14.446 7.808   23.562  1.00 34.58 ? 97  GLU B OE2 1 
ATOM   3310  N N   . LEU B 2 98  ? -16.321 4.589   17.796  1.00 32.30 ? 98  LEU B N   1 
ATOM   3311  C CA  . LEU B 2 98  ? -17.210 3.663   17.111  1.00 32.03 ? 98  LEU B CA  1 
ATOM   3312  C C   . LEU B 2 98  ? -16.463 2.772   16.119  1.00 31.79 ? 98  LEU B C   1 
ATOM   3313  O O   . LEU B 2 98  ? -16.710 1.568   16.060  1.00 31.70 ? 98  LEU B O   1 
ATOM   3314  C CB  . LEU B 2 98  ? -18.346 4.416   16.418  1.00 32.15 ? 98  LEU B CB  1 
ATOM   3315  C CG  . LEU B 2 98  ? -19.442 3.557   15.786  1.00 32.91 ? 98  LEU B CG  1 
ATOM   3316  C CD1 . LEU B 2 98  ? -20.341 2.901   16.848  1.00 32.49 ? 98  LEU B CD1 1 
ATOM   3317  C CD2 . LEU B 2 98  ? -20.257 4.380   14.796  1.00 33.04 ? 98  LEU B CD2 1 
ATOM   3318  N N   . LEU B 2 99  ? -15.550 3.358   15.351  1.00 31.63 ? 99  LEU B N   1 
ATOM   3319  C CA  . LEU B 2 99  ? -14.777 2.585   14.379  1.00 31.79 ? 99  LEU B CA  1 
ATOM   3320  C C   . LEU B 2 99  ? -13.966 1.473   15.062  1.00 31.90 ? 99  LEU B C   1 
ATOM   3321  O O   . LEU B 2 99  ? -13.963 0.331   14.603  1.00 31.87 ? 99  LEU B O   1 
ATOM   3322  C CB  . LEU B 2 99  ? -13.878 3.493   13.529  1.00 31.63 ? 99  LEU B CB  1 
ATOM   3323  C CG  . LEU B 2 99  ? -13.119 2.835   12.368  1.00 32.44 ? 99  LEU B CG  1 
ATOM   3324  C CD1 . LEU B 2 99  ? -14.046 2.012   11.481  1.00 33.22 ? 99  LEU B CD1 1 
ATOM   3325  C CD2 . LEU B 2 99  ? -12.342 3.853   11.537  1.00 32.91 ? 99  LEU B CD2 1 
ATOM   3326  N N   . VAL B 2 100 ? -13.306 1.813   16.167  1.00 31.94 ? 100 VAL B N   1 
ATOM   3327  C CA  . VAL B 2 100 ? -12.542 0.847   16.955  1.00 31.99 ? 100 VAL B CA  1 
ATOM   3328  C C   . VAL B 2 100 ? -13.441 -0.289  17.442  1.00 32.24 ? 100 VAL B C   1 
ATOM   3329  O O   . VAL B 2 100 ? -13.153 -1.460  17.210  1.00 31.73 ? 100 VAL B O   1 
ATOM   3330  C CB  . VAL B 2 100 ? -11.808 1.537   18.133  1.00 31.76 ? 100 VAL B CB  1 
ATOM   3331  C CG1 . VAL B 2 100 ? -11.421 0.535   19.225  1.00 31.30 ? 100 VAL B CG1 1 
ATOM   3332  C CG2 . VAL B 2 100 ? -10.589 2.279   17.615  1.00 31.28 ? 100 VAL B CG2 1 
ATOM   3333  N N   . LEU B 2 101 ? -14.539 0.081   18.090  1.00 32.77 ? 101 LEU B N   1 
ATOM   3334  C CA  . LEU B 2 101 ? -15.523 -0.870  18.589  1.00 33.49 ? 101 LEU B CA  1 
ATOM   3335  C C   . LEU B 2 101 ? -15.977 -1.851  17.491  1.00 33.87 ? 101 LEU B C   1 
ATOM   3336  O O   . LEU B 2 101 ? -15.814 -3.066  17.641  1.00 33.89 ? 101 LEU B O   1 
ATOM   3337  C CB  . LEU B 2 101 ? -16.713 -0.099  19.165  1.00 33.53 ? 101 LEU B CB  1 
ATOM   3338  C CG  . LEU B 2 101 ? -17.188 -0.388  20.589  1.00 34.38 ? 101 LEU B CG  1 
ATOM   3339  C CD1 . LEU B 2 101 ? -16.040 -0.310  21.594  1.00 34.89 ? 101 LEU B CD1 1 
ATOM   3340  C CD2 . LEU B 2 101 ? -18.294 0.588   20.970  1.00 34.50 ? 101 LEU B CD2 1 
ATOM   3341  N N   . MET B 2 102 ? -16.502 -1.314  16.384  1.00 34.22 ? 102 MET B N   1 
ATOM   3342  C CA  . MET B 2 102 ? -17.066 -2.120  15.288  1.00 34.55 ? 102 MET B CA  1 
ATOM   3343  C C   . MET B 2 102 ? -16.058 -3.066  14.656  1.00 34.50 ? 102 MET B C   1 
ATOM   3344  O O   . MET B 2 102 ? -16.379 -4.222  14.366  1.00 34.50 ? 102 MET B O   1 
ATOM   3345  C CB  . MET B 2 102 ? -17.684 -1.230  14.197  1.00 34.68 ? 102 MET B CB  1 
ATOM   3346  C CG  . MET B 2 102 ? -19.011 -0.593  14.579  1.00 36.08 ? 102 MET B CG  1 
ATOM   3347  S SD  . MET B 2 102 ? -19.928 0.097   13.175  1.00 40.49 ? 102 MET B SD  1 
ATOM   3348  C CE  . MET B 2 102 ? -18.895 1.477   12.675  1.00 40.05 ? 102 MET B CE  1 
ATOM   3349  N N   . GLU B 2 103 ? -14.843 -2.567  14.438  1.00 34.67 ? 103 GLU B N   1 
ATOM   3350  C CA  . GLU B 2 103 ? -13.790 -3.354  13.800  1.00 34.82 ? 103 GLU B CA  1 
ATOM   3351  C C   . GLU B 2 103 ? -13.141 -4.373  14.732  1.00 34.61 ? 103 GLU B C   1 
ATOM   3352  O O   . GLU B 2 103 ? -12.627 -5.390  14.259  1.00 34.54 ? 103 GLU B O   1 
ATOM   3353  C CB  . GLU B 2 103 ? -12.728 -2.459  13.164  1.00 34.77 ? 103 GLU B CB  1 
ATOM   3354  C CG  . GLU B 2 103 ? -13.220 -1.663  11.963  1.00 36.03 ? 103 GLU B CG  1 
ATOM   3355  C CD  . GLU B 2 103 ? -13.761 -2.523  10.817  1.00 37.38 ? 103 GLU B CD  1 
ATOM   3356  O OE1 . GLU B 2 103 ? -13.171 -3.583  10.504  1.00 36.11 ? 103 GLU B OE1 1 
ATOM   3357  O OE2 . GLU B 2 103 ? -14.782 -2.111  10.213  1.00 39.11 ? 103 GLU B OE2 1 
ATOM   3358  N N   . ASN B 2 104 ? -13.157 -4.102  16.039  1.00 34.63 ? 104 ASN B N   1 
ATOM   3359  C CA  . ASN B 2 104 ? -12.753 -5.102  17.031  1.00 34.74 ? 104 ASN B CA  1 
ATOM   3360  C C   . ASN B 2 104 ? -13.602 -6.358  16.856  1.00 35.00 ? 104 ASN B C   1 
ATOM   3361  O O   . ASN B 2 104 ? -13.072 -7.453  16.694  1.00 34.91 ? 104 ASN B O   1 
ATOM   3362  C CB  . ASN B 2 104 ? -12.890 -4.582  18.467  1.00 34.49 ? 104 ASN B CB  1 
ATOM   3363  C CG  . ASN B 2 104 ? -11.762 -3.633  18.880  1.00 34.16 ? 104 ASN B CG  1 
ATOM   3364  O OD1 . ASN B 2 104 ? -10.772 -3.453  18.164  1.00 33.19 ? 104 ASN B OD1 1 
ATOM   3365  N ND2 . ASN B 2 104 ? -11.920 -3.015  20.053  1.00 32.80 ? 104 ASN B ND2 1 
ATOM   3366  N N   . GLU B 2 105 ? -14.922 -6.180  16.854  1.00 35.60 ? 105 GLU B N   1 
ATOM   3367  C CA  . GLU B 2 105 ? -15.863 -7.284  16.654  1.00 36.25 ? 105 GLU B CA  1 
ATOM   3368  C C   . GLU B 2 105 ? -15.634 -8.033  15.338  1.00 36.28 ? 105 GLU B C   1 
ATOM   3369  O O   . GLU B 2 105 ? -15.746 -9.261  15.290  1.00 36.42 ? 105 GLU B O   1 
ATOM   3370  C CB  . GLU B 2 105 ? -17.304 -6.789  16.724  1.00 36.35 ? 105 GLU B CB  1 
ATOM   3371  C CG  . GLU B 2 105 ? -18.312 -7.906  16.926  1.00 37.44 ? 105 GLU B CG  1 
ATOM   3372  C CD  . GLU B 2 105 ? -19.731 -7.396  16.973  1.00 39.16 ? 105 GLU B CD  1 
ATOM   3373  O OE1 . GLU B 2 105 ? -20.300 -7.119  15.891  1.00 39.64 ? 105 GLU B OE1 1 
ATOM   3374  O OE2 . GLU B 2 105 ? -20.272 -7.273  18.095  1.00 39.77 ? 105 GLU B OE2 1 
ATOM   3375  N N   . ARG B 2 106 ? -15.308 -7.296  14.281  1.00 36.18 ? 106 ARG B N   1 
ATOM   3376  C CA  . ARG B 2 106 ? -14.992 -7.914  13.000  1.00 36.38 ? 106 ARG B CA  1 
ATOM   3377  C C   . ARG B 2 106 ? -13.661 -8.672  13.025  1.00 36.14 ? 106 ARG B C   1 
ATOM   3378  O O   . ARG B 2 106 ? -13.517 -9.702  12.367  1.00 36.27 ? 106 ARG B O   1 
ATOM   3379  C CB  . ARG B 2 106 ? -15.022 -6.882  11.872  1.00 36.59 ? 106 ARG B CB  1 
ATOM   3380  C CG  . ARG B 2 106 ? -16.426 -6.561  11.393  1.00 37.74 ? 106 ARG B CG  1 
ATOM   3381  C CD  . ARG B 2 106 ? -16.411 -5.843  10.059  1.00 41.33 ? 106 ARG B CD  1 
ATOM   3382  N NE  . ARG B 2 106 ? -17.314 -6.487  9.097   1.00 44.24 ? 106 ARG B NE  1 
ATOM   3383  C CZ  . ARG B 2 106 ? -16.931 -7.376  8.182   1.00 44.51 ? 106 ARG B CZ  1 
ATOM   3384  N NH1 . ARG B 2 106 ? -15.657 -7.733  8.082   1.00 44.84 ? 106 ARG B NH1 1 
ATOM   3385  N NH2 . ARG B 2 106 ? -17.823 -7.907  7.358   1.00 45.38 ? 106 ARG B NH2 1 
ATOM   3386  N N   . THR B 2 107 ? -12.700 -8.163  13.792  1.00 35.89 ? 107 THR B N   1 
ATOM   3387  C CA  . THR B 2 107 ? -11.404 -8.815  13.951  1.00 35.39 ? 107 THR B CA  1 
ATOM   3388  C C   . THR B 2 107 ? -11.569 -10.146 14.693  1.00 34.97 ? 107 THR B C   1 
ATOM   3389  O O   . THR B 2 107 ? -11.008 -11.165 14.283  1.00 34.67 ? 107 THR B O   1 
ATOM   3390  C CB  . THR B 2 107 ? -10.397 -7.876  14.654  1.00 35.58 ? 107 THR B CB  1 
ATOM   3391  O OG1 . THR B 2 107 ? -10.180 -6.729  13.826  1.00 35.66 ? 107 THR B OG1 1 
ATOM   3392  C CG2 . THR B 2 107 ? -9.046  -8.566  14.914  1.00 35.59 ? 107 THR B CG2 1 
ATOM   3393  N N   . LEU B 2 108 ? -12.362 -10.136 15.759  1.00 34.55 ? 108 LEU B N   1 
ATOM   3394  C CA  . LEU B 2 108 ? -12.667 -11.358 16.503  1.00 34.49 ? 108 LEU B CA  1 
ATOM   3395  C C   . LEU B 2 108 ? -13.366 -12.398 15.631  1.00 34.44 ? 108 LEU B C   1 
ATOM   3396  O O   . LEU B 2 108 ? -12.971 -13.564 15.626  1.00 34.59 ? 108 LEU B O   1 
ATOM   3397  C CB  . LEU B 2 108 ? -13.483 -11.042 17.761  1.00 34.36 ? 108 LEU B CB  1 
ATOM   3398  C CG  . LEU B 2 108 ? -12.728 -10.754 19.072  1.00 34.45 ? 108 LEU B CG  1 
ATOM   3399  C CD1 . LEU B 2 108 ? -11.418 -10.006 18.867  1.00 34.59 ? 108 LEU B CD1 1 
ATOM   3400  C CD2 . LEU B 2 108 ? -13.616 -9.996  20.051  1.00 35.10 ? 108 LEU B CD2 1 
ATOM   3401  N N   . ASP B 2 109 ? -14.376 -11.963 14.875  1.00 34.31 ? 109 ASP B N   1 
ATOM   3402  C CA  . ASP B 2 109 ? -15.088 -12.831 13.925  1.00 33.89 ? 109 ASP B CA  1 
ATOM   3403  C C   . ASP B 2 109 ? -14.199 -13.316 12.778  1.00 33.39 ? 109 ASP B C   1 
ATOM   3404  O O   . ASP B 2 109 ? -14.380 -14.423 12.274  1.00 33.36 ? 109 ASP B O   1 
ATOM   3405  C CB  . ASP B 2 109 ? -16.320 -12.121 13.354  1.00 34.04 ? 109 ASP B CB  1 
ATOM   3406  C CG  . ASP B 2 109 ? -17.376 -11.826 14.408  1.00 34.72 ? 109 ASP B CG  1 
ATOM   3407  O OD1 . ASP B 2 109 ? -17.499 -12.612 15.373  1.00 36.43 ? 109 ASP B OD1 1 
ATOM   3408  O OD2 . ASP B 2 109 ? -18.093 -10.805 14.269  1.00 34.56 ? 109 ASP B OD2 1 
ATOM   3409  N N   . PHE B 2 110 ? -13.252 -12.478 12.365  1.00 32.77 ? 110 PHE B N   1 
ATOM   3410  C CA  . PHE B 2 110 ? -12.308 -12.816 11.295  1.00 32.35 ? 110 PHE B CA  1 
ATOM   3411  C C   . PHE B 2 110 ? -11.415 -14.009 11.672  1.00 32.55 ? 110 PHE B C   1 
ATOM   3412  O O   . PHE B 2 110 ? -11.214 -14.921 10.864  1.00 32.50 ? 110 PHE B O   1 
ATOM   3413  C CB  . PHE B 2 110 ? -11.474 -11.581 10.936  1.00 31.91 ? 110 PHE B CB  1 
ATOM   3414  C CG  . PHE B 2 110 ? -10.391 -11.827 9.923   1.00 30.80 ? 110 PHE B CG  1 
ATOM   3415  C CD1 . PHE B 2 110 ? -10.700 -12.219 8.624   1.00 29.70 ? 110 PHE B CD1 1 
ATOM   3416  C CD2 . PHE B 2 110 ? -9.054  -11.626 10.263  1.00 29.62 ? 110 PHE B CD2 1 
ATOM   3417  C CE1 . PHE B 2 110 ? -9.696  -12.428 7.687   1.00 28.80 ? 110 PHE B CE1 1 
ATOM   3418  C CE2 . PHE B 2 110 ? -8.044  -11.829 9.333   1.00 28.96 ? 110 PHE B CE2 1 
ATOM   3419  C CZ  . PHE B 2 110 ? -8.364  -12.227 8.042   1.00 28.95 ? 110 PHE B CZ  1 
ATOM   3420  N N   . HIS B 2 111 ? -10.900 -13.996 12.902  1.00 32.59 ? 111 HIS B N   1 
ATOM   3421  C CA  . HIS B 2 111 ? -10.104 -15.105 13.427  1.00 32.67 ? 111 HIS B CA  1 
ATOM   3422  C C   . HIS B 2 111 ? -10.939 -16.374 13.587  1.00 33.06 ? 111 HIS B C   1 
ATOM   3423  O O   . HIS B 2 111 ? -10.458 -17.475 13.312  1.00 32.86 ? 111 HIS B O   1 
ATOM   3424  C CB  . HIS B 2 111 ? -9.453  -14.735 14.764  1.00 32.33 ? 111 HIS B CB  1 
ATOM   3425  C CG  . HIS B 2 111 ? -8.398  -13.676 14.655  1.00 31.50 ? 111 HIS B CG  1 
ATOM   3426  N ND1 . HIS B 2 111 ? -7.318  -13.782 13.805  1.00 30.51 ? 111 HIS B ND1 1 
ATOM   3427  C CD2 . HIS B 2 111 ? -8.250  -12.498 15.305  1.00 30.24 ? 111 HIS B CD2 1 
ATOM   3428  C CE1 . HIS B 2 111 ? -6.559  -12.708 13.922  1.00 29.81 ? 111 HIS B CE1 1 
ATOM   3429  N NE2 . HIS B 2 111 ? -7.102  -11.913 14.827  1.00 30.30 ? 111 HIS B NE2 1 
ATOM   3430  N N   . ASP B 2 112 ? -12.184 -16.210 14.034  1.00 33.55 ? 112 ASP B N   1 
ATOM   3431  C CA  . ASP B 2 112 ? -13.111 -17.327 14.188  1.00 34.27 ? 112 ASP B CA  1 
ATOM   3432  C C   . ASP B 2 112 ? -13.327 -18.019 12.842  1.00 34.72 ? 112 ASP B C   1 
ATOM   3433  O O   . ASP B 2 112 ? -13.284 -19.245 12.754  1.00 35.03 ? 112 ASP B O   1 
ATOM   3434  C CB  . ASP B 2 112 ? -14.439 -16.841 14.779  1.00 34.28 ? 112 ASP B CB  1 
ATOM   3435  C CG  . ASP B 2 112 ? -15.259 -17.965 15.403  1.00 35.11 ? 112 ASP B CG  1 
ATOM   3436  O OD1 . ASP B 2 112 ? -14.876 -19.146 15.269  1.00 35.99 ? 112 ASP B OD1 1 
ATOM   3437  O OD2 . ASP B 2 112 ? -16.297 -17.667 16.034  1.00 35.46 ? 112 ASP B OD2 1 
ATOM   3438  N N   . SER B 2 113 ? -13.521 -17.214 11.797  1.00 35.24 ? 113 SER B N   1 
ATOM   3439  C CA  . SER B 2 113 ? -13.734 -17.689 10.428  1.00 35.57 ? 113 SER B CA  1 
ATOM   3440  C C   . SER B 2 113 ? -12.518 -18.408 9.822   1.00 36.01 ? 113 SER B C   1 
ATOM   3441  O O   . SER B 2 113 ? -12.671 -19.339 9.029   1.00 36.12 ? 113 SER B O   1 
ATOM   3442  C CB  . SER B 2 113 ? -14.162 -16.512 9.537   1.00 35.42 ? 113 SER B CB  1 
ATOM   3443  O OG  . SER B 2 113 ? -13.926 -16.771 8.165   1.00 34.96 ? 113 SER B OG  1 
ATOM   3444  N N   . ASN B 2 114 ? -11.320 -17.958 10.179  1.00 36.47 ? 114 ASN B N   1 
ATOM   3445  C CA  . ASN B 2 114 ? -10.090 -18.567 9.685   1.00 37.19 ? 114 ASN B CA  1 
ATOM   3446  C C   . ASN B 2 114 ? -9.844  -19.967 10.258  1.00 37.62 ? 114 ASN B C   1 
ATOM   3447  O O   . ASN B 2 114 ? -9.279  -20.828 9.587   1.00 37.58 ? 114 ASN B O   1 
ATOM   3448  C CB  . ASN B 2 114 ? -8.889  -17.662 9.973   1.00 37.17 ? 114 ASN B CB  1 
ATOM   3449  C CG  . ASN B 2 114 ? -8.819  -16.456 9.044   1.00 37.79 ? 114 ASN B CG  1 
ATOM   3450  O OD1 . ASN B 2 114 ? -8.245  -15.423 9.398   1.00 38.16 ? 114 ASN B OD1 1 
ATOM   3451  N ND2 . ASN B 2 114 ? -9.400  -16.581 7.851   1.00 37.75 ? 114 ASN B ND2 1 
ATOM   3452  N N   . VAL B 2 115 ? -10.265 -20.178 11.503  1.00 38.18 ? 115 VAL B N   1 
ATOM   3453  C CA  . VAL B 2 115 ? -10.136 -21.472 12.159  1.00 38.77 ? 115 VAL B CA  1 
ATOM   3454  C C   . VAL B 2 115 ? -11.149 -22.434 11.539  1.00 39.33 ? 115 VAL B C   1 
ATOM   3455  O O   . VAL B 2 115 ? -10.820 -23.578 11.220  1.00 39.38 ? 115 VAL B O   1 
ATOM   3456  C CB  . VAL B 2 115 ? -10.341 -21.360 13.699  1.00 38.67 ? 115 VAL B CB  1 
ATOM   3457  C CG1 . VAL B 2 115 ? -10.212 -22.714 14.368  1.00 38.12 ? 115 VAL B CG1 1 
ATOM   3458  C CG2 . VAL B 2 115 ? -9.339  -20.389 14.302  1.00 38.55 ? 115 VAL B CG2 1 
ATOM   3459  N N   . LYS B 2 116 ? -12.373 -21.940 11.361  1.00 39.92 ? 116 LYS B N   1 
ATOM   3460  C CA  . LYS B 2 116 ? -13.447 -22.674 10.704  1.00 40.58 ? 116 LYS B CA  1 
ATOM   3461  C C   . LYS B 2 116 ? -13.038 -23.110 9.292   1.00 41.08 ? 116 LYS B C   1 
ATOM   3462  O O   . LYS B 2 116 ? -13.244 -24.268 8.914   1.00 41.14 ? 116 LYS B O   1 
ATOM   3463  C CB  . LYS B 2 116 ? -14.711 -21.811 10.677  1.00 40.65 ? 116 LYS B CB  1 
ATOM   3464  C CG  . LYS B 2 116 ? -16.035 -22.560 10.564  1.00 41.16 ? 116 LYS B CG  1 
ATOM   3465  C CD  . LYS B 2 116 ? -16.561 -22.550 9.131   1.00 42.36 ? 116 LYS B CD  1 
ATOM   3466  C CE  . LYS B 2 116 ? -18.088 -22.448 9.077   1.00 43.40 ? 116 LYS B CE  1 
ATOM   3467  N NZ  . LYS B 2 116 ? -18.798 -23.585 9.742   1.00 43.75 ? 116 LYS B NZ  1 
ATOM   3468  N N   . ASN B 2 117 ? -12.440 -22.197 8.525   1.00 41.61 ? 117 ASN B N   1 
ATOM   3469  C CA  . ASN B 2 117 ? -11.993 -22.521 7.164   1.00 42.29 ? 117 ASN B CA  1 
ATOM   3470  C C   . ASN B 2 117 ? -10.804 -23.473 7.110   1.00 42.94 ? 117 ASN B C   1 
ATOM   3471  O O   . ASN B 2 117 ? -10.653 -24.222 6.142   1.00 43.11 ? 117 ASN B O   1 
ATOM   3472  C CB  . ASN B 2 117 ? -11.694 -21.257 6.352   1.00 42.06 ? 117 ASN B CB  1 
ATOM   3473  C CG  . ASN B 2 117 ? -12.946 -20.467 6.014   1.00 41.89 ? 117 ASN B CG  1 
ATOM   3474  O OD1 . ASN B 2 117 ? -14.069 -20.965 6.123   1.00 40.45 ? 117 ASN B OD1 1 
ATOM   3475  N ND2 . ASN B 2 117 ? -12.756 -19.219 5.606   1.00 42.23 ? 117 ASN B ND2 1 
ATOM   3476  N N   . LEU B 2 118 ? -9.960  -23.435 8.138   1.00 43.71 ? 118 LEU B N   1 
ATOM   3477  C CA  . LEU B 2 118 ? -8.816  -24.332 8.216   1.00 44.57 ? 118 LEU B CA  1 
ATOM   3478  C C   . LEU B 2 118 ? -9.290  -25.755 8.496   1.00 45.30 ? 118 LEU B C   1 
ATOM   3479  O O   . LEU B 2 118 ? -8.819  -26.708 7.876   1.00 45.30 ? 118 LEU B O   1 
ATOM   3480  C CB  . LEU B 2 118 ? -7.827  -23.874 9.294   1.00 44.58 ? 118 LEU B CB  1 
ATOM   3481  C CG  . LEU B 2 118 ? -6.485  -24.615 9.384   1.00 44.51 ? 118 LEU B CG  1 
ATOM   3482  C CD1 . LEU B 2 118 ? -5.618  -24.352 8.158   1.00 44.40 ? 118 LEU B CD1 1 
ATOM   3483  C CD2 . LEU B 2 118 ? -5.741  -24.230 10.656  1.00 44.90 ? 118 LEU B CD2 1 
ATOM   3484  N N   . TYR B 2 119 ? -10.229 -25.880 9.429   1.00 46.19 ? 119 TYR B N   1 
ATOM   3485  C CA  . TYR B 2 119 ? -10.811 -27.162 9.793   1.00 47.22 ? 119 TYR B CA  1 
ATOM   3486  C C   . TYR B 2 119 ? -11.519 -27.813 8.604   1.00 47.99 ? 119 TYR B C   1 
ATOM   3487  O O   . TYR B 2 119 ? -11.413 -29.026 8.405   1.00 48.21 ? 119 TYR B O   1 
ATOM   3488  C CB  . TYR B 2 119 ? -11.769 -26.979 10.973  1.00 47.29 ? 119 TYR B CB  1 
ATOM   3489  C CG  . TYR B 2 119 ? -12.526 -28.224 11.390  1.00 47.80 ? 119 TYR B CG  1 
ATOM   3490  C CD1 . TYR B 2 119 ? -11.971 -29.134 12.286  1.00 48.07 ? 119 TYR B CD1 1 
ATOM   3491  C CD2 . TYR B 2 119 ? -13.810 -28.478 10.900  1.00 48.17 ? 119 TYR B CD2 1 
ATOM   3492  C CE1 . TYR B 2 119 ? -12.669 -30.270 12.676  1.00 48.63 ? 119 TYR B CE1 1 
ATOM   3493  C CE2 . TYR B 2 119 ? -14.513 -29.608 11.282  1.00 48.46 ? 119 TYR B CE2 1 
ATOM   3494  C CZ  . TYR B 2 119 ? -13.938 -30.500 12.170  1.00 49.03 ? 119 TYR B CZ  1 
ATOM   3495  O OH  . TYR B 2 119 ? -14.633 -31.623 12.553  1.00 49.74 ? 119 TYR B OH  1 
ATOM   3496  N N   . ASP B 2 120 ? -12.229 -27.003 7.818   1.00 48.82 ? 120 ASP B N   1 
ATOM   3497  C CA  . ASP B 2 120 ? -12.923 -27.483 6.621   1.00 49.52 ? 120 ASP B CA  1 
ATOM   3498  C C   . ASP B 2 120 ? -11.966 -27.870 5.503   1.00 50.05 ? 120 ASP B C   1 
ATOM   3499  O O   . ASP B 2 120 ? -12.251 -28.784 4.733   1.00 50.26 ? 120 ASP B O   1 
ATOM   3500  C CB  . ASP B 2 120 ? -13.922 -26.442 6.114   1.00 49.45 ? 120 ASP B CB  1 
ATOM   3501  C CG  . ASP B 2 120 ? -15.146 -26.326 6.998   1.00 49.60 ? 120 ASP B CG  1 
ATOM   3502  O OD1 . ASP B 2 120 ? -15.361 -27.206 7.862   1.00 49.89 ? 120 ASP B OD1 1 
ATOM   3503  O OD2 . ASP B 2 120 ? -15.899 -25.346 6.829   1.00 50.10 ? 120 ASP B OD2 1 
ATOM   3504  N N   . LYS B 2 121 ? -10.840 -27.169 5.412   1.00 50.82 ? 121 LYS B N   1 
ATOM   3505  C CA  . LYS B 2 121 ? -9.813  -27.483 4.420   1.00 51.63 ? 121 LYS B CA  1 
ATOM   3506  C C   . LYS B 2 121 ? -9.286  -28.903 4.641   1.00 52.11 ? 121 LYS B C   1 
ATOM   3507  O O   . LYS B 2 121 ? -9.027  -29.631 3.682   1.00 52.20 ? 121 LYS B O   1 
ATOM   3508  C CB  . LYS B 2 121 ? -8.672  -26.462 4.484   1.00 51.60 ? 121 LYS B CB  1 
ATOM   3509  C CG  . LYS B 2 121 ? -7.632  -26.579 3.375   1.00 52.11 ? 121 LYS B CG  1 
ATOM   3510  C CD  . LYS B 2 121 ? -6.545  -25.520 3.534   1.00 53.13 ? 121 LYS B CD  1 
ATOM   3511  C CE  . LYS B 2 121 ? -5.445  -25.660 2.481   1.00 54.00 ? 121 LYS B CE  1 
ATOM   3512  N NZ  . LYS B 2 121 ? -4.567  -26.847 2.716   1.00 53.99 ? 121 LYS B NZ  1 
ATOM   3513  N N   . VAL B 2 122 ? -9.153  -29.287 5.909   1.00 52.61 ? 122 VAL B N   1 
ATOM   3514  C CA  . VAL B 2 122 ? -8.683  -30.618 6.278   1.00 53.26 ? 122 VAL B CA  1 
ATOM   3515  C C   . VAL B 2 122 ? -9.773  -31.670 6.055   1.00 53.81 ? 122 VAL B C   1 
ATOM   3516  O O   . VAL B 2 122 ? -9.505  -32.734 5.496   1.00 53.81 ? 122 VAL B O   1 
ATOM   3517  C CB  . VAL B 2 122 ? -8.165  -30.649 7.742   1.00 53.24 ? 122 VAL B CB  1 
ATOM   3518  C CG1 . VAL B 2 122 ? -7.867  -32.073 8.197   1.00 53.16 ? 122 VAL B CG1 1 
ATOM   3519  C CG2 . VAL B 2 122 ? -6.920  -29.782 7.878   1.00 53.13 ? 122 VAL B CG2 1 
ATOM   3520  N N   . ARG B 2 123 ? -10.996 -31.353 6.481   1.00 54.54 ? 123 ARG B N   1 
ATOM   3521  C CA  . ARG B 2 123 ? -12.140 -32.264 6.385   1.00 55.22 ? 123 ARG B CA  1 
ATOM   3522  C C   . ARG B 2 123 ? -12.453 -32.682 4.949   1.00 55.71 ? 123 ARG B C   1 
ATOM   3523  O O   . ARG B 2 123 ? -12.743 -33.848 4.685   1.00 55.92 ? 123 ARG B O   1 
ATOM   3524  C CB  . ARG B 2 123 ? -13.373 -31.638 7.047   1.00 55.20 ? 123 ARG B CB  1 
ATOM   3525  C CG  . ARG B 2 123 ? -14.682 -32.369 6.787   1.00 55.48 ? 123 ARG B CG  1 
ATOM   3526  C CD  . ARG B 2 123 ? -15.845 -31.682 7.473   1.00 56.41 ? 123 ARG B CD  1 
ATOM   3527  N NE  . ARG B 2 123 ? -16.985 -31.545 6.569   1.00 57.48 ? 123 ARG B NE  1 
ATOM   3528  C CZ  . ARG B 2 123 ? -17.341 -30.410 5.969   1.00 57.64 ? 123 ARG B CZ  1 
ATOM   3529  N NH1 . ARG B 2 123 ? -16.658 -29.292 6.180   1.00 57.07 ? 123 ARG B NH1 1 
ATOM   3530  N NH2 . ARG B 2 123 ? -18.393 -30.392 5.159   1.00 58.34 ? 123 ARG B NH2 1 
ATOM   3531  N N   . LEU B 2 124 ? -12.393 -31.724 4.029   1.00 56.45 ? 124 LEU B N   1 
ATOM   3532  C CA  . LEU B 2 124 ? -12.689 -31.977 2.621   1.00 57.04 ? 124 LEU B CA  1 
ATOM   3533  C C   . LEU B 2 124 ? -11.554 -32.721 1.923   1.00 57.31 ? 124 LEU B C   1 
ATOM   3534  O O   . LEU B 2 124 ? -11.773 -33.432 0.941   1.00 57.40 ? 124 LEU B O   1 
ATOM   3535  C CB  . LEU B 2 124 ? -13.008 -30.666 1.898   1.00 57.14 ? 124 LEU B CB  1 
ATOM   3536  C CG  . LEU B 2 124 ? -14.480 -30.234 1.861   1.00 57.72 ? 124 LEU B CG  1 
ATOM   3537  C CD1 . LEU B 2 124 ? -15.046 -29.895 3.241   1.00 58.14 ? 124 LEU B CD1 1 
ATOM   3538  C CD2 . LEU B 2 124 ? -14.649 -29.050 0.926   1.00 58.20 ? 124 LEU B CD2 1 
ATOM   3539  N N   . GLN B 2 125 ? -10.347 -32.555 2.449   1.00 57.75 ? 125 GLN B N   1 
ATOM   3540  C CA  . GLN B 2 125 ? -9.159  -33.218 1.933   1.00 58.25 ? 125 GLN B CA  1 
ATOM   3541  C C   . GLN B 2 125 ? -9.133  -34.700 2.316   1.00 58.56 ? 125 GLN B C   1 
ATOM   3542  O O   . GLN B 2 125 ? -8.729  -35.551 1.517   1.00 58.58 ? 125 GLN B O   1 
ATOM   3543  C CB  . GLN B 2 125 ? -7.923  -32.519 2.485   1.00 58.28 ? 125 GLN B CB  1 
ATOM   3544  C CG  . GLN B 2 125 ? -6.717  -32.522 1.580   1.00 58.75 ? 125 GLN B CG  1 
ATOM   3545  C CD  . GLN B 2 125 ? -5.819  -31.336 1.856   1.00 59.39 ? 125 GLN B CD  1 
ATOM   3546  O OE1 . GLN B 2 125 ? -6.202  -30.191 1.618   1.00 60.56 ? 125 GLN B OE1 1 
ATOM   3547  N NE2 . GLN B 2 125 ? -4.622  -31.599 2.364   1.00 58.96 ? 125 GLN B NE2 1 
ATOM   3548  N N   . LEU B 2 126 ? -9.573  -34.996 3.537   1.00 58.91 ? 126 LEU B N   1 
ATOM   3549  C CA  . LEU B 2 126 ? -9.512  -36.349 4.086   1.00 59.21 ? 126 LEU B CA  1 
ATOM   3550  C C   . LEU B 2 126 ? -10.705 -37.223 3.717   1.00 59.48 ? 126 LEU B C   1 
ATOM   3551  O O   . LEU B 2 126 ? -10.582 -38.448 3.685   1.00 59.53 ? 126 LEU B O   1 
ATOM   3552  C CB  . LEU B 2 126 ? -9.365  -36.310 5.609   1.00 59.15 ? 126 LEU B CB  1 
ATOM   3553  C CG  . LEU B 2 126 ? -8.099  -35.701 6.206   1.00 59.04 ? 126 LEU B CG  1 
ATOM   3554  C CD1 . LEU B 2 126 ? -8.131  -35.856 7.712   1.00 59.06 ? 126 LEU B CD1 1 
ATOM   3555  C CD2 . LEU B 2 126 ? -6.848  -36.338 5.627   1.00 59.04 ? 126 LEU B CD2 1 
ATOM   3556  N N   . ARG B 2 127 ? -11.851 -36.594 3.452   1.00 59.77 ? 127 ARG B N   1 
ATOM   3557  C CA  . ARG B 2 127 ? -13.090 -37.310 3.122   1.00 60.13 ? 127 ARG B CA  1 
ATOM   3558  C C   . ARG B 2 127 ? -13.414 -38.362 4.192   1.00 60.21 ? 127 ARG B C   1 
ATOM   3559  O O   . ARG B 2 127 ? -13.355 -38.064 5.384   1.00 60.22 ? 127 ARG B O   1 
ATOM   3560  C CB  . ARG B 2 127 ? -13.003 -37.936 1.719   1.00 60.20 ? 127 ARG B CB  1 
ATOM   3561  C CG  . ARG B 2 127 ? -13.039 -36.935 0.570   1.00 60.48 ? 127 ARG B CG  1 
ATOM   3562  C CD  . ARG B 2 127 ? -14.434 -36.829 -0.037  1.00 61.21 ? 127 ARG B CD  1 
ATOM   3563  N NE  . ARG B 2 127 ? -14.756 -37.991 -0.866  1.00 61.58 ? 127 ARG B NE  1 
ATOM   3564  C CZ  . ARG B 2 127 ? -14.501 -38.087 -2.171  1.00 62.01 ? 127 ARG B CZ  1 
ATOM   3565  N NH1 . ARG B 2 127 ? -13.918 -37.085 -2.822  1.00 61.91 ? 127 ARG B NH1 1 
ATOM   3566  N NH2 . ARG B 2 127 ? -14.832 -39.191 -2.829  1.00 62.00 ? 127 ARG B NH2 1 
ATOM   3567  N N   . ASP B 2 128 ? -13.738 -39.584 3.771   1.00 60.42 ? 128 ASP B N   1 
ATOM   3568  C CA  . ASP B 2 128 ? -14.031 -40.668 4.716   1.00 60.50 ? 128 ASP B CA  1 
ATOM   3569  C C   . ASP B 2 128 ? -12.800 -41.475 5.169   1.00 60.45 ? 128 ASP B C   1 
ATOM   3570  O O   . ASP B 2 128 ? -12.930 -42.410 5.962   1.00 60.53 ? 128 ASP B O   1 
ATOM   3571  C CB  . ASP B 2 128 ? -15.166 -41.580 4.205   1.00 60.65 ? 128 ASP B CB  1 
ATOM   3572  C CG  . ASP B 2 128 ? -14.880 -42.205 2.837   1.00 60.93 ? 128 ASP B CG  1 
ATOM   3573  O OD1 . ASP B 2 128 ? -13.821 -41.937 2.229   1.00 61.38 ? 128 ASP B OD1 1 
ATOM   3574  O OD2 . ASP B 2 128 ? -15.741 -42.981 2.366   1.00 61.11 ? 128 ASP B OD2 1 
ATOM   3575  N N   . ASN B 2 129 ? -11.614 -41.092 4.689   1.00 60.36 ? 129 ASN B N   1 
ATOM   3576  C CA  . ASN B 2 129 ? -10.347 -41.693 5.132   1.00 60.25 ? 129 ASN B CA  1 
ATOM   3577  C C   . ASN B 2 129 ? -9.987  -41.382 6.589   1.00 60.27 ? 129 ASN B C   1 
ATOM   3578  O O   . ASN B 2 129 ? -8.921  -41.778 7.068   1.00 60.38 ? 129 ASN B O   1 
ATOM   3579  C CB  . ASN B 2 129 ? -9.191  -41.259 4.222   1.00 60.21 ? 129 ASN B CB  1 
ATOM   3580  C CG  . ASN B 2 129 ? -9.152  -42.018 2.905   1.00 60.30 ? 129 ASN B CG  1 
ATOM   3581  O OD1 . ASN B 2 129 ? -8.214  -41.861 2.120   1.00 60.31 ? 129 ASN B OD1 1 
ATOM   3582  N ND2 . ASN B 2 129 ? -10.165 -42.843 2.654   1.00 60.45 ? 129 ASN B ND2 1 
ATOM   3583  N N   . ALA B 2 130 ? -10.870 -40.666 7.281   1.00 60.25 ? 130 ALA B N   1 
ATOM   3584  C CA  . ALA B 2 130 ? -10.674 -40.316 8.685   1.00 60.17 ? 130 ALA B CA  1 
ATOM   3585  C C   . ALA B 2 130 ? -12.011 -40.149 9.396   1.00 60.21 ? 130 ALA B C   1 
ATOM   3586  O O   . ALA B 2 130 ? -13.050 -39.988 8.752   1.00 60.20 ? 130 ALA B O   1 
ATOM   3587  C CB  . ALA B 2 130 ? -9.840  -39.048 8.812   1.00 60.13 ? 130 ALA B CB  1 
ATOM   3588  N N   . LYS B 2 131 ? -11.969 -40.192 10.726  1.00 60.31 ? 131 LYS B N   1 
ATOM   3589  C CA  . LYS B 2 131 ? -13.158 -40.087 11.567  1.00 60.34 ? 131 LYS B CA  1 
ATOM   3590  C C   . LYS B 2 131 ? -13.249 -38.694 12.181  1.00 60.22 ? 131 LYS B C   1 
ATOM   3591  O O   . LYS B 2 131 ? -12.248 -38.145 12.642  1.00 60.24 ? 131 LYS B O   1 
ATOM   3592  C CB  . LYS B 2 131 ? -13.113 -41.145 12.672  1.00 60.45 ? 131 LYS B CB  1 
ATOM   3593  C CG  . LYS B 2 131 ? -14.451 -41.426 13.339  1.00 61.03 ? 131 LYS B CG  1 
ATOM   3594  C CD  . LYS B 2 131 ? -14.313 -42.471 14.442  1.00 62.09 ? 131 LYS B CD  1 
ATOM   3595  C CE  . LYS B 2 131 ? -15.662 -43.103 14.769  1.00 62.68 ? 131 LYS B CE  1 
ATOM   3596  N NZ  . LYS B 2 131 ? -15.609 -43.916 16.013  1.00 63.12 ? 131 LYS B NZ  1 
ATOM   3597  N N   . GLU B 2 132 ? -14.455 -38.136 12.189  1.00 60.09 ? 132 GLU B N   1 
ATOM   3598  C CA  . GLU B 2 132 ? -14.687 -36.795 12.717  1.00 59.92 ? 132 GLU B CA  1 
ATOM   3599  C C   . GLU B 2 132 ? -15.136 -36.860 14.176  1.00 59.77 ? 132 GLU B C   1 
ATOM   3600  O O   . GLU B 2 132 ? -16.282 -37.218 14.470  1.00 59.72 ? 132 GLU B O   1 
ATOM   3601  C CB  . GLU B 2 132 ? -15.719 -36.065 11.855  1.00 59.92 ? 132 GLU B CB  1 
ATOM   3602  C CG  . GLU B 2 132 ? -15.837 -34.579 12.136  1.00 60.23 ? 132 GLU B CG  1 
ATOM   3603  C CD  . GLU B 2 132 ? -16.643 -33.836 11.082  1.00 60.90 ? 132 GLU B CD  1 
ATOM   3604  O OE1 . GLU B 2 132 ? -16.795 -34.360 9.953   1.00 60.48 ? 132 GLU B OE1 1 
ATOM   3605  O OE2 . GLU B 2 132 ? -17.120 -32.718 11.383  1.00 61.08 ? 132 GLU B OE2 1 
ATOM   3606  N N   . LEU B 2 133 ? -14.228 -36.514 15.085  1.00 59.58 ? 133 LEU B N   1 
ATOM   3607  C CA  . LEU B 2 133 ? -14.500 -36.624 16.521  1.00 59.47 ? 133 LEU B CA  1 
ATOM   3608  C C   . LEU B 2 133 ? -15.485 -35.568 17.025  1.00 59.39 ? 133 LEU B C   1 
ATOM   3609  O O   . LEU B 2 133 ? -16.179 -35.783 18.020  1.00 59.41 ? 133 LEU B O   1 
ATOM   3610  C CB  . LEU B 2 133 ? -13.201 -36.601 17.344  1.00 59.43 ? 133 LEU B CB  1 
ATOM   3611  C CG  . LEU B 2 133 ? -12.220 -37.790 17.342  1.00 59.44 ? 133 LEU B CG  1 
ATOM   3612  C CD1 . LEU B 2 133 ? -12.923 -39.145 17.233  1.00 59.71 ? 133 LEU B CD1 1 
ATOM   3613  C CD2 . LEU B 2 133 ? -11.176 -37.662 16.251  1.00 59.30 ? 133 LEU B CD2 1 
ATOM   3614  N N   . GLY B 2 134 ? -15.545 -34.434 16.329  1.00 59.29 ? 134 GLY B N   1 
ATOM   3615  C CA  . GLY B 2 134 ? -16.473 -33.360 16.669  1.00 59.15 ? 134 GLY B CA  1 
ATOM   3616  C C   . GLY B 2 134 ? -15.922 -32.394 17.698  1.00 59.10 ? 134 GLY B C   1 
ATOM   3617  O O   . GLY B 2 134 ? -16.684 -31.722 18.394  1.00 59.21 ? 134 GLY B O   1 
ATOM   3618  N N   . ASN B 2 135 ? -14.596 -32.325 17.792  1.00 58.98 ? 135 ASN B N   1 
ATOM   3619  C CA  . ASN B 2 135 ? -13.926 -31.421 18.724  1.00 58.87 ? 135 ASN B CA  1 
ATOM   3620  C C   . ASN B 2 135 ? -12.745 -30.695 18.080  1.00 58.79 ? 135 ASN B C   1 
ATOM   3621  O O   . ASN B 2 135 ? -12.002 -29.977 18.751  1.00 58.80 ? 135 ASN B O   1 
ATOM   3622  C CB  . ASN B 2 135 ? -13.473 -32.181 19.977  1.00 58.86 ? 135 ASN B CB  1 
ATOM   3623  C CG  . ASN B 2 135 ? -12.413 -33.236 19.679  1.00 58.98 ? 135 ASN B CG  1 
ATOM   3624  O OD1 . ASN B 2 135 ? -12.287 -33.716 18.550  1.00 59.11 ? 135 ASN B OD1 1 
ATOM   3625  N ND2 . ASN B 2 135 ? -11.648 -33.604 20.700  1.00 59.04 ? 135 ASN B ND2 1 
ATOM   3626  N N   . GLY B 2 136 ? -12.583 -30.888 16.775  1.00 58.75 ? 136 GLY B N   1 
ATOM   3627  C CA  . GLY B 2 136 ? -11.482 -30.287 16.030  1.00 58.76 ? 136 GLY B CA  1 
ATOM   3628  C C   . GLY B 2 136 ? -10.459 -31.303 15.557  1.00 58.82 ? 136 GLY B C   1 
ATOM   3629  O O   . GLY B 2 136 ? -9.521  -30.955 14.837  1.00 58.62 ? 136 GLY B O   1 
ATOM   3630  N N   . CYS B 2 137 ? -10.648 -32.561 15.952  1.00 59.05 ? 137 CYS B N   1 
ATOM   3631  C CA  . CYS B 2 137 ? -9.684  -33.620 15.653  1.00 59.31 ? 137 CYS B CA  1 
ATOM   3632  C C   . CYS B 2 137 ? -10.189 -34.653 14.650  1.00 59.82 ? 137 CYS B C   1 
ATOM   3633  O O   . CYS B 2 137 ? -11.391 -34.916 14.557  1.00 59.85 ? 137 CYS B O   1 
ATOM   3634  C CB  . CYS B 2 137 ? -9.237  -34.307 16.940  1.00 59.04 ? 137 CYS B CB  1 
ATOM   3635  S SG  . CYS B 2 137 ? -8.326  -33.210 18.043  1.00 58.28 ? 137 CYS B SG  1 
ATOM   3636  N N   . PHE B 2 138 ? -9.251  -35.229 13.901  1.00 60.46 ? 138 PHE B N   1 
ATOM   3637  C CA  . PHE B 2 138 ? -9.548  -36.289 12.943  1.00 61.21 ? 138 PHE B CA  1 
ATOM   3638  C C   . PHE B 2 138 ? -8.732  -37.544 13.243  1.00 61.73 ? 138 PHE B C   1 
ATOM   3639  O O   . PHE B 2 138 ? -7.499  -37.506 13.241  1.00 61.66 ? 138 PHE B O   1 
ATOM   3640  C CB  . PHE B 2 138 ? -9.257  -35.827 11.511  1.00 61.17 ? 138 PHE B CB  1 
ATOM   3641  C CG  . PHE B 2 138 ? -10.104 -34.675 11.055  1.00 61.24 ? 138 PHE B CG  1 
ATOM   3642  C CD1 . PHE B 2 138 ? -11.331 -34.900 10.439  1.00 61.20 ? 138 PHE B CD1 1 
ATOM   3643  C CD2 . PHE B 2 138 ? -9.667  -33.363 11.226  1.00 60.83 ? 138 PHE B CD2 1 
ATOM   3644  C CE1 . PHE B 2 138 ? -12.116 -33.835 10.007  1.00 61.45 ? 138 PHE B CE1 1 
ATOM   3645  C CE2 . PHE B 2 138 ? -10.442 -32.296 10.800  1.00 61.07 ? 138 PHE B CE2 1 
ATOM   3646  C CZ  . PHE B 2 138 ? -11.668 -32.529 10.188  1.00 61.34 ? 138 PHE B CZ  1 
ATOM   3647  N N   . GLU B 2 139 ? -9.428  -38.651 13.499  1.00 62.55 ? 139 GLU B N   1 
ATOM   3648  C CA  . GLU B 2 139 ? -8.783  -39.949 13.694  1.00 63.30 ? 139 GLU B CA  1 
ATOM   3649  C C   . GLU B 2 139 ? -8.755  -40.682 12.358  1.00 63.72 ? 139 GLU B C   1 
ATOM   3650  O O   . GLU B 2 139 ? -9.805  -40.950 11.774  1.00 63.73 ? 139 GLU B O   1 
ATOM   3651  C CB  . GLU B 2 139 ? -9.529  -40.772 14.748  1.00 63.22 ? 139 GLU B CB  1 
ATOM   3652  C CG  . GLU B 2 139 ? -8.688  -41.856 15.409  1.00 63.88 ? 139 GLU B CG  1 
ATOM   3653  C CD  . GLU B 2 139 ? -9.423  -42.573 16.537  1.00 64.73 ? 139 GLU B CD  1 
ATOM   3654  O OE1 . GLU B 2 139 ? -10.448 -43.238 16.264  1.00 64.97 ? 139 GLU B OE1 1 
ATOM   3655  O OE2 . GLU B 2 139 ? -8.967  -42.478 17.699  1.00 64.69 ? 139 GLU B OE2 1 
ATOM   3656  N N   . PHE B 2 140 ? -7.551  -40.993 11.881  1.00 64.38 ? 140 PHE B N   1 
ATOM   3657  C CA  . PHE B 2 140 ? -7.353  -41.632 10.576  1.00 65.16 ? 140 PHE B CA  1 
ATOM   3658  C C   . PHE B 2 140 ? -7.755  -43.109 10.556  1.00 65.75 ? 140 PHE B C   1 
ATOM   3659  O O   . PHE B 2 140 ? -7.505  -43.845 11.518  1.00 65.72 ? 140 PHE B O   1 
ATOM   3660  C CB  . PHE B 2 140 ? -5.889  -41.512 10.148  1.00 65.12 ? 140 PHE B CB  1 
ATOM   3661  C CG  . PHE B 2 140 ? -5.478  -40.123 9.751   1.00 65.38 ? 140 PHE B CG  1 
ATOM   3662  C CD1 . PHE B 2 140 ? -5.450  -39.750 8.409   1.00 65.73 ? 140 PHE B CD1 1 
ATOM   3663  C CD2 . PHE B 2 140 ? -5.101  -39.191 10.713  1.00 65.45 ? 140 PHE B CD2 1 
ATOM   3664  C CE1 . PHE B 2 140 ? -5.063  -38.467 8.031   1.00 65.64 ? 140 PHE B CE1 1 
ATOM   3665  C CE2 . PHE B 2 140 ? -4.716  -37.907 10.350  1.00 65.60 ? 140 PHE B CE2 1 
ATOM   3666  C CZ  . PHE B 2 140 ? -4.695  -37.543 9.005   1.00 65.88 ? 140 PHE B CZ  1 
ATOM   3667  N N   . TYR B 2 141 ? -8.365  -43.536 9.450   1.00 66.49 ? 141 TYR B N   1 
ATOM   3668  C CA  . TYR B 2 141 ? -8.699  -44.950 9.236   1.00 67.29 ? 141 TYR B CA  1 
ATOM   3669  C C   . TYR B 2 141 ? -7.553  -45.726 8.569   1.00 67.95 ? 141 TYR B C   1 
ATOM   3670  O O   . TYR B 2 141 ? -7.765  -46.788 7.979   1.00 68.01 ? 141 TYR B O   1 
ATOM   3671  C CB  . TYR B 2 141 ? -9.993  -45.099 8.426   1.00 67.11 ? 141 TYR B CB  1 
ATOM   3672  C CG  . TYR B 2 141 ? -11.273 -44.903 9.218   1.00 66.90 ? 141 TYR B CG  1 
ATOM   3673  C CD1 . TYR B 2 141 ? -11.600 -45.749 10.280  1.00 66.82 ? 141 TYR B CD1 1 
ATOM   3674  C CD2 . TYR B 2 141 ? -12.171 -43.888 8.884   1.00 66.66 ? 141 TYR B CD2 1 
ATOM   3675  C CE1 . TYR B 2 141 ? -12.780 -45.577 11.004  1.00 66.86 ? 141 TYR B CE1 1 
ATOM   3676  C CE2 . TYR B 2 141 ? -13.354 -43.708 9.599   1.00 66.75 ? 141 TYR B CE2 1 
ATOM   3677  C CZ  . TYR B 2 141 ? -13.651 -44.555 10.656  1.00 66.87 ? 141 TYR B CZ  1 
ATOM   3678  O OH  . TYR B 2 141 ? -14.819 -44.379 11.364  1.00 66.93 ? 141 TYR B OH  1 
ATOM   3679  N N   . HIS B 2 142 ? -6.344  -45.175 8.669   1.00 68.85 ? 142 HIS B N   1 
ATOM   3680  C CA  . HIS B 2 142 ? -5.117  -45.816 8.197   1.00 69.73 ? 142 HIS B CA  1 
ATOM   3681  C C   . HIS B 2 142 ? -3.930  -45.221 8.945   1.00 70.33 ? 142 HIS B C   1 
ATOM   3682  O O   . HIS B 2 142 ? -4.053  -44.160 9.558   1.00 70.43 ? 142 HIS B O   1 
ATOM   3683  C CB  . HIS B 2 142 ? -4.940  -45.630 6.683   1.00 69.74 ? 142 HIS B CB  1 
ATOM   3684  C CG  . HIS B 2 142 ? -4.815  -44.201 6.255   1.00 69.96 ? 142 HIS B CG  1 
ATOM   3685  N ND1 . HIS B 2 142 ? -3.609  -43.533 6.232   1.00 70.14 ? 142 HIS B ND1 1 
ATOM   3686  C CD2 . HIS B 2 142 ? -5.745  -43.312 5.833   1.00 69.99 ? 142 HIS B CD2 1 
ATOM   3687  C CE1 . HIS B 2 142 ? -3.802  -42.294 5.816   1.00 69.93 ? 142 HIS B CE1 1 
ATOM   3688  N NE2 . HIS B 2 142 ? -5.089  -42.135 5.565   1.00 69.95 ? 142 HIS B NE2 1 
ATOM   3689  N N   . LYS B 2 143 ? -2.786  -45.898 8.901   1.00 71.16 ? 143 LYS B N   1 
ATOM   3690  C CA  . LYS B 2 143 ? -1.579  -45.356 9.517   1.00 71.93 ? 143 LYS B CA  1 
ATOM   3691  C C   . LYS B 2 143 ? -0.994  -44.244 8.654   1.00 72.40 ? 143 LYS B C   1 
ATOM   3692  O O   . LYS B 2 143 ? -0.696  -44.446 7.474   1.00 72.41 ? 143 LYS B O   1 
ATOM   3693  C CB  . LYS B 2 143 ? -0.549  -46.452 9.813   1.00 71.94 ? 143 LYS B CB  1 
ATOM   3694  C CG  . LYS B 2 143 ? -0.800  -47.178 11.136  1.00 72.30 ? 143 LYS B CG  1 
ATOM   3695  C CD  . LYS B 2 143 ? 0.455   -47.866 11.673  1.00 73.04 ? 143 LYS B CD  1 
ATOM   3696  C CE  . LYS B 2 143 ? 0.645   -49.263 11.082  1.00 73.37 ? 143 LYS B CE  1 
ATOM   3697  N NZ  . LYS B 2 143 ? 1.829   -49.958 11.660  1.00 73.24 ? 143 LYS B NZ  1 
ATOM   3698  N N   . CYS B 2 144 ? -0.869  -43.062 9.255   1.00 73.06 ? 144 CYS B N   1 
ATOM   3699  C CA  . CYS B 2 144 ? -0.365  -41.871 8.577   1.00 73.68 ? 144 CYS B CA  1 
ATOM   3700  C C   . CYS B 2 144 ? 0.933   -41.401 9.237   1.00 73.84 ? 144 CYS B C   1 
ATOM   3701  O O   . CYS B 2 144 ? 0.934   -40.906 10.366  1.00 73.83 ? 144 CYS B O   1 
ATOM   3702  C CB  . CYS B 2 144 ? -1.438  -40.768 8.568   1.00 73.80 ? 144 CYS B CB  1 
ATOM   3703  S SG  . CYS B 2 144 ? -0.965  -39.154 7.859   1.00 74.67 ? 144 CYS B SG  1 
ATOM   3704  N N   . ASP B 2 145 ? 2.037   -41.590 8.520   1.00 74.20 ? 145 ASP B N   1 
ATOM   3705  C CA  . ASP B 2 145 ? 3.368   -41.209 8.989   1.00 74.57 ? 145 ASP B CA  1 
ATOM   3706  C C   . ASP B 2 145 ? 3.587   -39.699 8.886   1.00 74.71 ? 145 ASP B C   1 
ATOM   3707  O O   . ASP B 2 145 ? 2.776   -38.994 8.292   1.00 74.75 ? 145 ASP B O   1 
ATOM   3708  C CB  . ASP B 2 145 ? 4.445   -41.965 8.198   1.00 74.60 ? 145 ASP B CB  1 
ATOM   3709  C CG  . ASP B 2 145 ? 4.262   -41.850 6.688   1.00 74.84 ? 145 ASP B CG  1 
ATOM   3710  O OD1 . ASP B 2 145 ? 5.261   -41.588 5.985   1.00 75.24 ? 145 ASP B OD1 1 
ATOM   3711  O OD2 . ASP B 2 145 ? 3.125   -42.024 6.201   1.00 74.91 ? 145 ASP B OD2 1 
ATOM   3712  N N   . ASN B 2 146 ? 4.688   -39.214 9.461   1.00 74.94 ? 146 ASN B N   1 
ATOM   3713  C CA  . ASN B 2 146 ? 5.019   -37.781 9.456   1.00 75.20 ? 146 ASN B CA  1 
ATOM   3714  C C   . ASN B 2 146 ? 5.065   -37.146 8.064   1.00 75.38 ? 146 ASN B C   1 
ATOM   3715  O O   . ASN B 2 146 ? 4.775   -35.958 7.910   1.00 75.44 ? 146 ASN B O   1 
ATOM   3716  C CB  . ASN B 2 146 ? 6.339   -37.522 10.195  1.00 75.11 ? 146 ASN B CB  1 
ATOM   3717  C CG  . ASN B 2 146 ? 6.205   -37.638 11.708  1.00 75.05 ? 146 ASN B CG  1 
ATOM   3718  O OD1 . ASN B 2 146 ? 7.195   -37.540 12.433  1.00 75.13 ? 146 ASN B OD1 1 
ATOM   3719  N ND2 . ASN B 2 146 ? 4.983   -37.844 12.192  1.00 74.75 ? 146 ASN B ND2 1 
ATOM   3720  N N   . GLU B 2 147 ? 5.428   -37.943 7.062   1.00 75.66 ? 147 GLU B N   1 
ATOM   3721  C CA  . GLU B 2 147 ? 5.446   -37.491 5.672   1.00 75.94 ? 147 GLU B CA  1 
ATOM   3722  C C   . GLU B 2 147 ? 4.015   -37.319 5.161   1.00 76.01 ? 147 GLU B C   1 
ATOM   3723  O O   . GLU B 2 147 ? 3.737   -36.428 4.360   1.00 75.99 ? 147 GLU B O   1 
ATOM   3724  C CB  . GLU B 2 147 ? 6.210   -38.484 4.781   1.00 75.99 ? 147 GLU B CB  1 
ATOM   3725  C CG  . GLU B 2 147 ? 7.396   -39.209 5.449   1.00 76.35 ? 147 GLU B CG  1 
ATOM   3726  C CD  . GLU B 2 147 ? 8.591   -38.310 5.755   1.00 76.73 ? 147 GLU B CD  1 
ATOM   3727  O OE1 . GLU B 2 147 ? 8.845   -37.344 5.001   1.00 76.91 ? 147 GLU B OE1 1 
ATOM   3728  O OE2 . GLU B 2 147 ? 9.289   -38.586 6.753   1.00 76.69 ? 147 GLU B OE2 1 
ATOM   3729  N N   . CYS B 2 148 ? 3.118   -38.181 5.636   1.00 76.22 ? 148 CYS B N   1 
ATOM   3730  C CA  . CYS B 2 148 ? 1.692   -38.105 5.316   1.00 76.45 ? 148 CYS B CA  1 
ATOM   3731  C C   . CYS B 2 148 ? 1.010   -36.974 6.094   1.00 76.74 ? 148 CYS B C   1 
ATOM   3732  O O   . CYS B 2 148 ? 0.045   -36.373 5.613   1.00 76.76 ? 148 CYS B O   1 
ATOM   3733  C CB  . CYS B 2 148 ? 1.021   -39.463 5.585   1.00 76.34 ? 148 CYS B CB  1 
ATOM   3734  S SG  . CYS B 2 148 ? -0.780  -39.478 5.851   1.00 76.00 ? 148 CYS B SG  1 
ATOM   3735  N N   . MET B 2 149 ? 1.521   -36.683 7.289   1.00 77.04 ? 149 MET B N   1 
ATOM   3736  C CA  . MET B 2 149 ? 0.972   -35.614 8.126   1.00 77.37 ? 149 MET B CA  1 
ATOM   3737  C C   . MET B 2 149 ? 1.385   -34.223 7.646   1.00 77.63 ? 149 MET B C   1 
ATOM   3738  O O   . MET B 2 149 ? 0.701   -33.240 7.932   1.00 77.74 ? 149 MET B O   1 
ATOM   3739  C CB  . MET B 2 149 ? 1.352   -35.801 9.600   1.00 77.35 ? 149 MET B CB  1 
ATOM   3740  C CG  . MET B 2 149 ? 0.942   -37.146 10.177  1.00 77.51 ? 149 MET B CG  1 
ATOM   3741  S SD  . MET B 2 149 ? -0.165  -37.036 11.592  1.00 77.83 ? 149 MET B SD  1 
ATOM   3742  C CE  . MET B 2 149 ? -1.640  -36.415 10.804  1.00 77.37 ? 149 MET B CE  1 
ATOM   3743  N N   . GLU B 2 150 ? 2.503   -34.140 6.929   1.00 77.85 ? 150 GLU B N   1 
ATOM   3744  C CA  . GLU B 2 150 ? 2.928   -32.875 6.330   1.00 78.08 ? 150 GLU B CA  1 
ATOM   3745  C C   . GLU B 2 150 ? 2.191   -32.597 5.019   1.00 78.08 ? 150 GLU B C   1 
ATOM   3746  O O   . GLU B 2 150 ? 2.095   -31.448 4.589   1.00 78.12 ? 150 GLU B O   1 
ATOM   3747  C CB  . GLU B 2 150 ? 4.447   -32.838 6.119   1.00 78.14 ? 150 GLU B CB  1 
ATOM   3748  C CG  . GLU B 2 150 ? 5.258   -32.497 7.375   1.00 78.42 ? 150 GLU B CG  1 
ATOM   3749  C CD  . GLU B 2 150 ? 5.186   -31.020 7.775   1.00 78.83 ? 150 GLU B CD  1 
ATOM   3750  O OE1 . GLU B 2 150 ? 4.809   -30.171 6.937   1.00 78.80 ? 150 GLU B OE1 1 
ATOM   3751  O OE2 . GLU B 2 150 ? 5.521   -30.707 8.939   1.00 78.99 ? 150 GLU B OE2 1 
ATOM   3752  N N   . SER B 2 151 ? 1.664   -33.652 4.400   1.00 78.18 ? 151 SER B N   1 
ATOM   3753  C CA  . SER B 2 151 ? 0.933   -33.533 3.138   1.00 78.24 ? 151 SER B CA  1 
ATOM   3754  C C   . SER B 2 151 ? -0.448  -32.892 3.319   1.00 78.38 ? 151 SER B C   1 
ATOM   3755  O O   . SER B 2 151 ? -0.995  -32.312 2.377   1.00 78.35 ? 151 SER B O   1 
ATOM   3756  C CB  . SER B 2 151 ? 0.820   -34.895 2.440   1.00 78.20 ? 151 SER B CB  1 
ATOM   3757  O OG  . SER B 2 151 ? 0.057   -35.814 3.201   1.00 77.97 ? 151 SER B OG  1 
ATOM   3758  N N   . VAL B 2 152 ? -1.000  -33.001 4.528   1.00 78.54 ? 152 VAL B N   1 
ATOM   3759  C CA  . VAL B 2 152 ? -2.281  -32.366 4.862   1.00 78.74 ? 152 VAL B CA  1 
ATOM   3760  C C   . VAL B 2 152 ? -2.117  -30.904 5.279   1.00 78.87 ? 152 VAL B C   1 
ATOM   3761  O O   . VAL B 2 152 ? -3.040  -30.102 5.128   1.00 78.87 ? 152 VAL B O   1 
ATOM   3762  C CB  . VAL B 2 152 ? -3.075  -33.141 5.947   1.00 78.68 ? 152 VAL B CB  1 
ATOM   3763  C CG1 . VAL B 2 152 ? -3.798  -34.319 5.332   1.00 78.82 ? 152 VAL B CG1 1 
ATOM   3764  C CG2 . VAL B 2 152 ? -2.168  -33.604 7.067   1.00 78.79 ? 152 VAL B CG2 1 
ATOM   3765  N N   . LYS B 2 153 ? -0.942  -30.573 5.806   1.00 79.16 ? 153 LYS B N   1 
ATOM   3766  C CA  . LYS B 2 153 ? -0.598  -29.193 6.142   1.00 79.39 ? 153 LYS B CA  1 
ATOM   3767  C C   . LYS B 2 153 ? -0.243  -28.413 4.877   1.00 79.71 ? 153 LYS B C   1 
ATOM   3768  O O   . LYS B 2 153 ? -0.495  -27.210 4.792   1.00 79.76 ? 153 LYS B O   1 
ATOM   3769  C CB  . LYS B 2 153 ? 0.580   -29.147 7.117   1.00 79.32 ? 153 LYS B CB  1 
ATOM   3770  C CG  . LYS B 2 153 ? 0.381   -29.927 8.407   1.00 78.94 ? 153 LYS B CG  1 
ATOM   3771  C CD  . LYS B 2 153 ? 1.616   -29.815 9.284   1.00 78.72 ? 153 LYS B CD  1 
ATOM   3772  C CE  . LYS B 2 153 ? 1.559   -30.768 10.462  1.00 78.55 ? 153 LYS B CE  1 
ATOM   3773  N NZ  . LYS B 2 153 ? 2.828   -30.743 11.238  1.00 78.16 ? 153 LYS B NZ  1 
ATOM   3774  N N   . ASN B 2 154 ? 0.344   -29.114 3.905   1.00 80.08 ? 154 ASN B N   1 
ATOM   3775  C CA  . ASN B 2 154 ? 0.779   -28.530 2.632   1.00 80.38 ? 154 ASN B CA  1 
ATOM   3776  C C   . ASN B 2 154 ? -0.366  -28.425 1.619   1.00 80.53 ? 154 ASN B C   1 
ATOM   3777  O O   . ASN B 2 154 ? -0.268  -27.685 0.638   1.00 80.56 ? 154 ASN B O   1 
ATOM   3778  C CB  . ASN B 2 154 ? 1.939   -29.355 2.043   1.00 80.46 ? 154 ASN B CB  1 
ATOM   3779  C CG  . ASN B 2 154 ? 2.931   -28.514 1.229   1.00 80.75 ? 154 ASN B CG  1 
ATOM   3780  O OD1 . ASN B 2 154 ? 3.976   -29.015 0.802   1.00 80.58 ? 154 ASN B OD1 1 
ATOM   3781  N ND2 . ASN B 2 154 ? 2.612   -27.240 1.016   1.00 81.04 ? 154 ASN B ND2 1 
ATOM   3782  N N   . GLY B 2 155 ? -1.445  -29.166 1.860   1.00 80.72 ? 155 GLY B N   1 
ATOM   3783  C CA  . GLY B 2 155 ? -2.613  -29.139 0.980   1.00 80.97 ? 155 GLY B CA  1 
ATOM   3784  C C   . GLY B 2 155 ? -2.683  -30.292 -0.005  1.00 81.16 ? 155 GLY B C   1 
ATOM   3785  O O   . GLY B 2 155 ? -3.770  -30.781 -0.311  1.00 81.20 ? 155 GLY B O   1 
ATOM   3786  N N   . THR B 2 156 ? -1.526  -30.722 -0.506  1.00 81.39 ? 156 THR B N   1 
ATOM   3787  C CA  . THR B 2 156 ? -1.452  -31.816 -1.482  1.00 81.58 ? 156 THR B CA  1 
ATOM   3788  C C   . THR B 2 156 ? -1.467  -33.191 -0.808  1.00 81.71 ? 156 THR B C   1 
ATOM   3789  O O   . THR B 2 156 ? -0.429  -33.851 -0.687  1.00 81.72 ? 156 THR B O   1 
ATOM   3790  C CB  . THR B 2 156 ? -0.210  -31.694 -2.407  1.00 81.63 ? 156 THR B CB  1 
ATOM   3791  O OG1 . THR B 2 156 ? 0.947   -31.366 -1.625  1.00 81.69 ? 156 THR B OG1 1 
ATOM   3792  C CG2 . THR B 2 156 ? -0.428  -30.626 -3.481  1.00 81.57 ? 156 THR B CG2 1 
ATOM   3793  N N   . TYR B 2 157 ? -2.653  -33.610 -0.370  1.00 81.83 ? 157 TYR B N   1 
ATOM   3794  C CA  . TYR B 2 157 ? -2.849  -34.923 0.241   1.00 81.88 ? 157 TYR B CA  1 
ATOM   3795  C C   . TYR B 2 157 ? -3.510  -35.879 -0.744  1.00 82.03 ? 157 TYR B C   1 
ATOM   3796  O O   . TYR B 2 157 ? -4.517  -35.544 -1.374  1.00 82.03 ? 157 TYR B O   1 
ATOM   3797  C CB  . TYR B 2 157 ? -3.682  -34.807 1.521   1.00 81.85 ? 157 TYR B CB  1 
ATOM   3798  C CG  . TYR B 2 157 ? -4.181  -36.125 2.081   1.00 81.64 ? 157 TYR B CG  1 
ATOM   3799  C CD1 . TYR B 2 157 ? -3.352  -36.939 2.852   1.00 81.65 ? 157 TYR B CD1 1 
ATOM   3800  C CD2 . TYR B 2 157 ? -5.490  -36.550 1.848   1.00 81.42 ? 157 TYR B CD2 1 
ATOM   3801  C CE1 . TYR B 2 157 ? -3.811  -38.148 3.371   1.00 81.60 ? 157 TYR B CE1 1 
ATOM   3802  C CE2 . TYR B 2 157 ? -5.959  -37.754 2.360   1.00 81.35 ? 157 TYR B CE2 1 
ATOM   3803  C CZ  . TYR B 2 157 ? -5.116  -38.548 3.122   1.00 81.50 ? 157 TYR B CZ  1 
ATOM   3804  O OH  . TYR B 2 157 ? -5.578  -39.739 3.633   1.00 81.36 ? 157 TYR B OH  1 
ATOM   3805  N N   . ASP B 2 158 ? -2.938  -37.075 -0.852  1.00 82.18 ? 158 ASP B N   1 
ATOM   3806  C CA  . ASP B 2 158 ? -3.373  -38.075 -1.819  1.00 82.32 ? 158 ASP B CA  1 
ATOM   3807  C C   . ASP B 2 158 ? -4.487  -38.959 -1.247  1.00 82.48 ? 158 ASP B C   1 
ATOM   3808  O O   . ASP B 2 158 ? -4.248  -39.777 -0.354  1.00 82.47 ? 158 ASP B O   1 
ATOM   3809  C CB  . ASP B 2 158 ? -2.171  -38.922 -2.254  1.00 82.25 ? 158 ASP B CB  1 
ATOM   3810  C CG  . ASP B 2 158 ? -2.277  -39.412 -3.687  1.00 82.14 ? 158 ASP B CG  1 
ATOM   3811  O OD1 . ASP B 2 158 ? -3.386  -39.776 -4.133  1.00 82.14 ? 158 ASP B OD1 1 
ATOM   3812  O OD2 . ASP B 2 158 ? -1.233  -39.441 -4.368  1.00 82.04 ? 158 ASP B OD2 1 
ATOM   3813  N N   . TYR B 2 159 ? -5.704  -38.776 -1.761  1.00 82.71 ? 159 TYR B N   1 
ATOM   3814  C CA  . TYR B 2 159 ? -6.860  -39.586 -1.358  1.00 82.89 ? 159 TYR B CA  1 
ATOM   3815  C C   . TYR B 2 159 ? -6.927  -40.946 -2.073  1.00 83.07 ? 159 TYR B C   1 
ATOM   3816  O O   . TYR B 2 159 ? -7.131  -41.965 -1.408  1.00 83.11 ? 159 TYR B O   1 
ATOM   3817  C CB  . TYR B 2 159 ? -8.174  -38.806 -1.517  1.00 82.88 ? 159 TYR B CB  1 
ATOM   3818  C CG  . TYR B 2 159 ? -9.424  -39.603 -1.189  1.00 83.02 ? 159 TYR B CG  1 
ATOM   3819  C CD1 . TYR B 2 159 ? -9.798  -39.838 0.134   1.00 83.02 ? 159 TYR B CD1 1 
ATOM   3820  C CD2 . TYR B 2 159 ? -10.239 -40.113 -2.204  1.00 83.14 ? 159 TYR B CD2 1 
ATOM   3821  C CE1 . TYR B 2 159 ? -10.947 -40.569 0.441   1.00 83.13 ? 159 TYR B CE1 1 
ATOM   3822  C CE2 . TYR B 2 159 ? -11.393 -40.845 -1.907  1.00 83.16 ? 159 TYR B CE2 1 
ATOM   3823  C CZ  . TYR B 2 159 ? -11.738 -41.068 -0.581  1.00 83.19 ? 159 TYR B CZ  1 
ATOM   3824  O OH  . TYR B 2 159 ? -12.872 -41.785 -0.272  1.00 82.93 ? 159 TYR B OH  1 
ATOM   3825  N N   . PRO B 2 160 ? -6.766  -40.975 -3.421  1.00 83.24 ? 160 PRO B N   1 
ATOM   3826  C CA  . PRO B 2 160 ? -6.677  -42.276 -4.107  1.00 83.31 ? 160 PRO B CA  1 
ATOM   3827  C C   . PRO B 2 160 ? -5.362  -43.025 -3.832  1.00 83.36 ? 160 PRO B C   1 
ATOM   3828  O O   . PRO B 2 160 ? -4.929  -43.847 -4.645  1.00 83.42 ? 160 PRO B O   1 
ATOM   3829  C CB  . PRO B 2 160 ? -6.794  -41.900 -5.593  1.00 83.29 ? 160 PRO B CB  1 
ATOM   3830  C CG  . PRO B 2 160 ? -7.436  -40.558 -5.601  1.00 83.32 ? 160 PRO B CG  1 
ATOM   3831  C CD  . PRO B 2 160 ? -6.877  -39.873 -4.395  1.00 83.24 ? 160 PRO B CD  1 
ATOM   3832  N N   . GLN B 2 161 ? -4.745  -42.729 -2.691  1.00 83.40 ? 161 GLN B N   1 
ATOM   3833  C CA  . GLN B 2 161 ? -3.565  -43.436 -2.208  1.00 83.46 ? 161 GLN B CA  1 
ATOM   3834  C C   . GLN B 2 161 ? -4.003  -44.397 -1.110  1.00 83.46 ? 161 GLN B C   1 
ATOM   3835  O O   . GLN B 2 161 ? -3.775  -45.604 -1.196  1.00 83.46 ? 161 GLN B O   1 
ATOM   3836  C CB  . GLN B 2 161 ? -2.556  -42.438 -1.639  1.00 83.46 ? 161 GLN B CB  1 
ATOM   3837  C CG  . GLN B 2 161 ? -1.229  -43.033 -1.200  1.00 83.66 ? 161 GLN B CG  1 
ATOM   3838  C CD  . GLN B 2 161 ? -0.118  -42.763 -2.193  1.00 84.07 ? 161 GLN B CD  1 
ATOM   3839  O OE1 . GLN B 2 161 ? 0.314   -43.661 -2.915  1.00 84.15 ? 161 GLN B OE1 1 
ATOM   3840  N NE2 . GLN B 2 161 ? 0.346   -41.516 -2.241  1.00 83.98 ? 161 GLN B NE2 1 
ATOM   3841  N N   . TYR B 2 162 ? -4.649  -43.838 -0.088  1.00 83.48 ? 162 TYR B N   1 
ATOM   3842  C CA  . TYR B 2 162 ? -5.040  -44.571 1.111   1.00 83.49 ? 162 TYR B CA  1 
ATOM   3843  C C   . TYR B 2 162 ? -6.502  -45.021 1.052   1.00 83.47 ? 162 TYR B C   1 
ATOM   3844  O O   . TYR B 2 162 ? -7.098  -45.360 2.080   1.00 83.40 ? 162 TYR B O   1 
ATOM   3845  C CB  . TYR B 2 162 ? -4.797  -43.712 2.361   1.00 83.52 ? 162 TYR B CB  1 
ATOM   3846  C CG  . TYR B 2 162 ? -3.394  -43.142 2.482   1.00 83.57 ? 162 TYR B CG  1 
ATOM   3847  C CD1 . TYR B 2 162 ? -2.381  -43.856 3.124   1.00 83.66 ? 162 TYR B CD1 1 
ATOM   3848  C CD2 . TYR B 2 162 ? -3.084  -41.882 1.964   1.00 83.50 ? 162 TYR B CD2 1 
ATOM   3849  C CE1 . TYR B 2 162 ? -1.093  -43.332 3.243   1.00 83.68 ? 162 TYR B CE1 1 
ATOM   3850  C CE2 . TYR B 2 162 ? -1.800  -41.353 2.074   1.00 83.48 ? 162 TYR B CE2 1 
ATOM   3851  C CZ  . TYR B 2 162 ? -0.811  -42.082 2.715   1.00 83.63 ? 162 TYR B CZ  1 
ATOM   3852  O OH  . TYR B 2 162 ? 0.458   -41.561 2.828   1.00 83.63 ? 162 TYR B OH  1 
ATOM   3853  N N   . SER B 2 163 ? -7.067  -45.028 -0.155  1.00 83.52 ? 163 SER B N   1 
ATOM   3854  C CA  . SER B 2 163 ? -8.443  -45.477 -0.382  1.00 83.65 ? 163 SER B CA  1 
ATOM   3855  C C   . SER B 2 163 ? -8.662  -46.928 0.046   1.00 83.71 ? 163 SER B C   1 
ATOM   3856  O O   . SER B 2 163 ? -9.728  -47.271 0.560   1.00 83.70 ? 163 SER B O   1 
ATOM   3857  C CB  . SER B 2 163 ? -8.829  -45.307 -1.855  1.00 83.68 ? 163 SER B CB  1 
ATOM   3858  O OG  . SER B 2 163 ? -8.884  -43.940 -2.218  1.00 83.64 ? 163 SER B OG  1 
ATOM   3859  N N   . GLU B 2 164 ? -7.645  -47.764 -0.168  1.00 83.79 ? 164 GLU B N   1 
ATOM   3860  C CA  . GLU B 2 164 ? -7.688  -49.192 0.171   1.00 83.81 ? 164 GLU B CA  1 
ATOM   3861  C C   . GLU B 2 164 ? -7.775  -49.475 1.680   1.00 83.70 ? 164 GLU B C   1 
ATOM   3862  O O   . GLU B 2 164 ? -8.749  -50.069 2.144   1.00 83.64 ? 164 GLU B O   1 
ATOM   3863  C CB  . GLU B 2 164 ? -6.498  -49.944 -0.457  1.00 83.90 ? 164 GLU B CB  1 
ATOM   3864  C CG  . GLU B 2 164 ? -5.116  -49.314 -0.211  1.00 84.11 ? 164 GLU B CG  1 
ATOM   3865  C CD  . GLU B 2 164 ? -3.965  -50.285 -0.444  1.00 84.52 ? 164 GLU B CD  1 
ATOM   3866  O OE1 . GLU B 2 164 ? -3.896  -50.893 -1.536  1.00 84.48 ? 164 GLU B OE1 1 
ATOM   3867  O OE2 . GLU B 2 164 ? -3.121  -50.433 0.468   1.00 84.52 ? 164 GLU B OE2 1 
ATOM   3868  N N   . GLU B 2 165 ? -6.761  -49.041 2.430   1.00 83.63 ? 165 GLU B N   1 
ATOM   3869  C CA  . GLU B 2 165 ? -6.655  -49.314 3.866   1.00 83.61 ? 165 GLU B CA  1 
ATOM   3870  C C   . GLU B 2 165 ? -7.893  -48.869 4.639   1.00 83.76 ? 165 GLU B C   1 
ATOM   3871  O O   . GLU B 2 165 ? -8.368  -49.583 5.523   1.00 83.84 ? 165 GLU B O   1 
ATOM   3872  C CB  . GLU B 2 165 ? -5.416  -48.633 4.458   1.00 83.54 ? 165 GLU B CB  1 
ATOM   3873  C CG  . GLU B 2 165 ? -4.090  -49.035 3.827   1.00 83.30 ? 165 GLU B CG  1 
ATOM   3874  C CD  . GLU B 2 165 ? -2.888  -48.489 4.585   1.00 82.98 ? 165 GLU B CD  1 
ATOM   3875  O OE1 . GLU B 2 165 ? -1.990  -47.912 3.935   1.00 82.99 ? 165 GLU B OE1 1 
ATOM   3876  O OE2 . GLU B 2 165 ? -2.839  -48.632 5.827   1.00 82.47 ? 165 GLU B OE2 1 
ATOM   3877  N N   . ALA B 2 166 ? -8.407  -47.691 4.292   1.00 83.88 ? 166 ALA B N   1 
ATOM   3878  C CA  . ALA B 2 166 ? -9.556  -47.097 4.971   1.00 84.00 ? 166 ALA B CA  1 
ATOM   3879  C C   . ALA B 2 166 ? -10.876 -47.774 4.610   1.00 84.12 ? 166 ALA B C   1 
ATOM   3880  O O   . ALA B 2 166 ? -11.803 -47.807 5.421   1.00 84.13 ? 166 ALA B O   1 
ATOM   3881  C CB  . ALA B 2 166 ? -9.627  -45.611 4.670   1.00 84.01 ? 166 ALA B CB  1 
ATOM   3882  N N   . ARG B 2 167 ? -10.950 -48.305 3.391   1.00 84.34 ? 167 ARG B N   1 
ATOM   3883  C CA  . ARG B 2 167 ? -12.154 -48.959 2.875   1.00 84.57 ? 167 ARG B CA  1 
ATOM   3884  C C   . ARG B 2 167 ? -12.569 -50.162 3.725   1.00 84.69 ? 167 ARG B C   1 
ATOM   3885  O O   . ARG B 2 167 ? -13.715 -50.242 4.174   1.00 84.74 ? 167 ARG B O   1 
ATOM   3886  C CB  . ARG B 2 167 ? -11.931 -49.394 1.421   1.00 84.62 ? 167 ARG B CB  1 
ATOM   3887  C CG  . ARG B 2 167 ? -13.188 -49.785 0.644   1.00 84.77 ? 167 ARG B CG  1 
ATOM   3888  C CD  . ARG B 2 167 ? -12.839 -50.651 -0.571  1.00 85.00 ? 167 ARG B CD  1 
ATOM   3889  N NE  . ARG B 2 167 ? -11.823 -50.035 -1.428  1.00 85.14 ? 167 ARG B NE  1 
ATOM   3890  C CZ  . ARG B 2 167 ? -11.102 -50.680 -2.344  1.00 85.12 ? 167 ARG B CZ  1 
ATOM   3891  N NH1 . ARG B 2 167 ? -11.265 -51.983 -2.545  1.00 85.01 ? 167 ARG B NH1 1 
ATOM   3892  N NH2 . ARG B 2 167 ? -10.206 -50.016 -3.062  1.00 85.20 ? 167 ARG B NH2 1 
ATOM   3893  N N   . LEU B 2 168 ? -11.628 -51.078 3.954   1.00 84.80 ? 168 LEU B N   1 
ATOM   3894  C CA  . LEU B 2 168 ? -11.920 -52.358 4.612   1.00 84.91 ? 168 LEU B CA  1 
ATOM   3895  C C   . LEU B 2 168 ? -12.094 -52.279 6.136   1.00 84.92 ? 168 LEU B C   1 
ATOM   3896  O O   . LEU B 2 168 ? -12.687 -53.178 6.741   1.00 84.93 ? 168 LEU B O   1 
ATOM   3897  C CB  . LEU B 2 168 ? -10.870 -53.420 4.238   1.00 84.93 ? 168 LEU B CB  1 
ATOM   3898  C CG  . LEU B 2 168 ? -11.010 -54.115 2.875   1.00 84.88 ? 168 LEU B CG  1 
ATOM   3899  C CD1 . LEU B 2 168 ? -10.259 -53.370 1.775   1.00 84.59 ? 168 LEU B CD1 1 
ATOM   3900  C CD2 . LEU B 2 168 ? -10.526 -55.557 2.956   1.00 84.88 ? 168 LEU B CD2 1 
ATOM   3901  N N   . ASN B 2 169 ? -11.589 -51.205 6.743   1.00 84.91 ? 169 ASN B N   1 
ATOM   3902  C CA  . ASN B 2 169 ? -11.698 -50.993 8.191   1.00 84.91 ? 169 ASN B CA  1 
ATOM   3903  C C   . ASN B 2 169 ? -13.123 -50.737 8.690   1.00 84.92 ? 169 ASN B C   1 
ATOM   3904  O O   . ASN B 2 169 ? -13.512 -51.225 9.755   1.00 84.95 ? 169 ASN B O   1 
ATOM   3905  C CB  . ASN B 2 169 ? -10.771 -49.861 8.641   1.00 84.88 ? 169 ASN B CB  1 
ATOM   3906  C CG  . ASN B 2 169 ? -9.339  -50.321 8.832   1.00 84.89 ? 169 ASN B CG  1 
ATOM   3907  O OD1 . ASN B 2 169 ? -9.078  -51.303 9.525   1.00 85.15 ? 169 ASN B OD1 1 
ATOM   3908  N ND2 . ASN B 2 169 ? -8.400  -49.604 8.226   1.00 84.74 ? 169 ASN B ND2 1 
ATOM   3909  N N   . ARG B 2 170 ? -13.893 -49.974 7.914   1.00 84.92 ? 170 ARG B N   1 
ATOM   3910  C CA  . ARG B 2 170 ? -15.275 -49.638 8.267   1.00 84.83 ? 170 ARG B CA  1 
ATOM   3911  C C   . ARG B 2 170 ? -16.225 -50.818 8.056   1.00 84.84 ? 170 ARG B C   1 
ATOM   3912  O O   . ARG B 2 170 ? -15.886 -51.797 7.390   1.00 84.77 ? 170 ARG B O   1 
ATOM   3913  C CB  . ARG B 2 170 ? -15.760 -48.421 7.467   1.00 84.80 ? 170 ARG B CB  1 
ATOM   3914  C CG  . ARG B 2 170 ? -14.919 -47.158 7.657   1.00 84.51 ? 170 ARG B CG  1 
ATOM   3915  C CD  . ARG B 2 170 ? -15.585 -45.915 7.056   1.00 83.97 ? 170 ARG B CD  1 
ATOM   3916  N NE  . ARG B 2 170 ? -15.807 -46.021 5.611   1.00 83.63 ? 170 ARG B NE  1 
ATOM   3917  C CZ  . ARG B 2 170 ? -14.895 -45.755 4.676   1.00 83.30 ? 170 ARG B CZ  1 
ATOM   3918  N NH1 . ARG B 2 170 ? -13.669 -45.368 5.010   1.00 83.24 ? 170 ARG B NH1 1 
ATOM   3919  N NH2 . ARG B 2 170 ? -15.210 -45.884 3.396   1.00 83.14 ? 170 ARG B NH2 1 
ATOM   3920  N N   . GLY C 1 8   ? -21.323 -41.634 -12.710 1.00 57.37 ? 10  GLY C N   1 
ATOM   3921  C CA  . GLY C 1 8   ? -21.745 -41.111 -14.043 1.00 57.32 ? 10  GLY C CA  1 
ATOM   3922  C C   . GLY C 1 8   ? -22.281 -39.690 -13.987 1.00 57.18 ? 10  GLY C C   1 
ATOM   3923  O O   . GLY C 1 8   ? -21.586 -38.748 -14.367 1.00 57.22 ? 10  GLY C O   1 
ATOM   3924  N N   . ASP C 1 9   ? -23.517 -39.545 -13.508 1.00 56.94 ? 11  ASP C N   1 
ATOM   3925  C CA  . ASP C 1 9   ? -24.208 -38.252 -13.454 1.00 56.69 ? 11  ASP C CA  1 
ATOM   3926  C C   . ASP C 1 9   ? -23.639 -37.304 -12.397 1.00 56.53 ? 11  ASP C C   1 
ATOM   3927  O O   . ASP C 1 9   ? -23.289 -37.725 -11.288 1.00 56.55 ? 11  ASP C O   1 
ATOM   3928  C CB  . ASP C 1 9   ? -25.712 -38.456 -13.231 1.00 56.75 ? 11  ASP C CB  1 
ATOM   3929  C CG  . ASP C 1 9   ? -26.394 -39.154 -14.404 1.00 56.92 ? 11  ASP C CG  1 
ATOM   3930  O OD1 . ASP C 1 9   ? -25.689 -39.757 -15.243 1.00 56.83 ? 11  ASP C OD1 1 
ATOM   3931  O OD2 . ASP C 1 9   ? -27.641 -39.103 -14.486 1.00 57.24 ? 11  ASP C OD2 1 
ATOM   3932  N N   . GLN C 1 10  ? -23.562 -36.020 -12.752 1.00 56.17 ? 12  GLN C N   1 
ATOM   3933  C CA  . GLN C 1 10  ? -22.942 -35.001 -11.900 1.00 55.69 ? 12  GLN C CA  1 
ATOM   3934  C C   . GLN C 1 10  ? -23.691 -33.674 -11.873 1.00 55.12 ? 12  GLN C C   1 
ATOM   3935  O O   . GLN C 1 10  ? -24.262 -33.248 -12.881 1.00 55.13 ? 12  GLN C O   1 
ATOM   3936  C CB  . GLN C 1 10  ? -21.502 -34.737 -12.346 1.00 55.85 ? 12  GLN C CB  1 
ATOM   3937  C CG  . GLN C 1 10  ? -20.455 -35.589 -11.652 1.00 56.26 ? 12  GLN C CG  1 
ATOM   3938  C CD  . GLN C 1 10  ? -19.035 -35.188 -12.019 1.00 56.99 ? 12  GLN C CD  1 
ATOM   3939  O OE1 . GLN C 1 10  ? -18.128 -36.018 -12.010 1.00 57.57 ? 12  GLN C OE1 1 
ATOM   3940  N NE2 . GLN C 1 10  ? -18.837 -33.912 -12.342 1.00 57.10 ? 12  GLN C NE2 1 
ATOM   3941  N N   . ILE C 1 11  ? -23.679 -33.036 -10.704 1.00 54.34 ? 13  ILE C N   1 
ATOM   3942  C CA  . ILE C 1 11  ? -24.114 -31.650 -10.550 1.00 53.67 ? 13  ILE C CA  1 
ATOM   3943  C C   . ILE C 1 11  ? -23.041 -30.859 -9.789  1.00 53.22 ? 13  ILE C C   1 
ATOM   3944  O O   . ILE C 1 11  ? -22.494 -31.338 -8.791  1.00 53.04 ? 13  ILE C O   1 
ATOM   3945  C CB  . ILE C 1 11  ? -25.521 -31.530 -9.880  1.00 53.61 ? 13  ILE C CB  1 
ATOM   3946  C CG1 . ILE C 1 11  ? -26.107 -30.128 -10.104 1.00 53.43 ? 13  ILE C CG1 1 
ATOM   3947  C CG2 . ILE C 1 11  ? -25.473 -31.902 -8.389  1.00 53.60 ? 13  ILE C CG2 1 
ATOM   3948  C CD1 . ILE C 1 11  ? -27.609 -30.028 -9.886  1.00 53.15 ? 13  ILE C CD1 1 
ATOM   3949  N N   . CYS C 1 12  ? -22.731 -29.665 -10.287 1.00 52.64 ? 14  CYS C N   1 
ATOM   3950  C CA  . CYS C 1 12  ? -21.725 -28.803 -9.675  1.00 52.20 ? 14  CYS C CA  1 
ATOM   3951  C C   . CYS C 1 12  ? -22.289 -27.427 -9.359  1.00 51.46 ? 14  CYS C C   1 
ATOM   3952  O O   . CYS C 1 12  ? -23.074 -26.878 -10.130 1.00 51.39 ? 14  CYS C O   1 
ATOM   3953  C CB  . CYS C 1 12  ? -20.511 -28.666 -10.591 1.00 52.43 ? 14  CYS C CB  1 
ATOM   3954  S SG  . CYS C 1 12  ? -19.613 -30.209 -10.855 1.00 53.80 ? 14  CYS C SG  1 
ATOM   3955  N N   . ILE C 1 13  ? -21.887 -26.880 -8.216  1.00 50.63 ? 15  ILE C N   1 
ATOM   3956  C CA  . ILE C 1 13  ? -22.294 -25.540 -7.803  1.00 49.69 ? 15  ILE C CA  1 
ATOM   3957  C C   . ILE C 1 13  ? -21.103 -24.597 -7.930  1.00 49.12 ? 15  ILE C C   1 
ATOM   3958  O O   . ILE C 1 13  ? -20.007 -24.904 -7.466  1.00 49.11 ? 15  ILE C O   1 
ATOM   3959  C CB  . ILE C 1 13  ? -22.859 -25.526 -6.356  1.00 49.64 ? 15  ILE C CB  1 
ATOM   3960  C CG1 . ILE C 1 13  ? -24.251 -26.163 -6.313  1.00 49.73 ? 15  ILE C CG1 1 
ATOM   3961  C CG2 . ILE C 1 13  ? -22.939 -24.107 -5.801  1.00 49.34 ? 15  ILE C CG2 1 
ATOM   3962  C CD1 . ILE C 1 13  ? -24.247 -27.661 -6.060  1.00 49.76 ? 15  ILE C CD1 1 
ATOM   3963  N N   . GLY C 1 14  ? -21.327 -23.456 -8.571  1.00 48.46 ? 16  GLY C N   1 
ATOM   3964  C CA  . GLY C 1 14  ? -20.276 -22.469 -8.772  1.00 47.84 ? 16  GLY C CA  1 
ATOM   3965  C C   . GLY C 1 14  ? -20.800 -21.061 -8.972  1.00 47.28 ? 16  GLY C C   1 
ATOM   3966  O O   . GLY C 1 14  ? -22.002 -20.803 -8.846  1.00 47.10 ? 16  GLY C O   1 
ATOM   3967  N N   . TYR C 1 15  ? -19.886 -20.153 -9.299  1.00 46.81 ? 17  TYR C N   1 
ATOM   3968  C CA  . TYR C 1 15  ? -20.205 -18.734 -9.398  1.00 46.27 ? 17  TYR C CA  1 
ATOM   3969  C C   . TYR C 1 15  ? -19.691 -18.090 -10.688 1.00 46.21 ? 17  TYR C C   1 
ATOM   3970  O O   . TYR C 1 15  ? -18.916 -18.693 -11.430 1.00 45.84 ? 17  TYR C O   1 
ATOM   3971  C CB  . TYR C 1 15  ? -19.712 -17.979 -8.150  1.00 45.97 ? 17  TYR C CB  1 
ATOM   3972  C CG  . TYR C 1 15  ? -18.269 -18.228 -7.762  1.00 44.97 ? 17  TYR C CG  1 
ATOM   3973  C CD1 . TYR C 1 15  ? -17.280 -17.285 -8.041  1.00 44.62 ? 17  TYR C CD1 1 
ATOM   3974  C CD2 . TYR C 1 15  ? -17.895 -19.395 -7.094  1.00 44.13 ? 17  TYR C CD2 1 
ATOM   3975  C CE1 . TYR C 1 15  ? -15.951 -17.502 -7.676  1.00 44.20 ? 17  TYR C CE1 1 
ATOM   3976  C CE2 . TYR C 1 15  ? -16.572 -19.623 -6.727  1.00 43.78 ? 17  TYR C CE2 1 
ATOM   3977  C CZ  . TYR C 1 15  ? -15.606 -18.673 -7.021  1.00 44.02 ? 17  TYR C CZ  1 
ATOM   3978  O OH  . TYR C 1 15  ? -14.297 -18.897 -6.664  1.00 43.91 ? 17  TYR C OH  1 
ATOM   3979  N N   . HIS C 1 16  ? -20.147 -16.865 -10.940 1.00 46.29 ? 18  HIS C N   1 
ATOM   3980  C CA  . HIS C 1 16  ? -19.803 -16.104 -12.137 1.00 46.34 ? 18  HIS C CA  1 
ATOM   3981  C C   . HIS C 1 16  ? -18.347 -15.646 -12.139 1.00 46.30 ? 18  HIS C C   1 
ATOM   3982  O O   . HIS C 1 16  ? -17.738 -15.439 -11.086 1.00 46.14 ? 18  HIS C O   1 
ATOM   3983  C CB  . HIS C 1 16  ? -20.736 -14.891 -12.252 1.00 46.48 ? 18  HIS C CB  1 
ATOM   3984  C CG  . HIS C 1 16  ? -20.535 -14.076 -13.494 1.00 47.59 ? 18  HIS C CG  1 
ATOM   3985  N ND1 . HIS C 1 16  ? -21.258 -14.288 -14.649 1.00 48.39 ? 18  HIS C ND1 1 
ATOM   3986  C CD2 . HIS C 1 16  ? -19.701 -13.041 -13.757 1.00 48.15 ? 18  HIS C CD2 1 
ATOM   3987  C CE1 . HIS C 1 16  ? -20.874 -13.423 -15.572 1.00 48.91 ? 18  HIS C CE1 1 
ATOM   3988  N NE2 . HIS C 1 16  ? -19.930 -12.655 -15.057 1.00 48.67 ? 18  HIS C NE2 1 
ATOM   3989  N N   . ALA C 1 17  ? -17.799 -15.514 -13.342 1.00 46.48 ? 19  ALA C N   1 
ATOM   3990  C CA  . ALA C 1 17  ? -16.528 -14.834 -13.579 1.00 46.68 ? 19  ALA C CA  1 
ATOM   3991  C C   . ALA C 1 17  ? -16.617 -14.154 -14.939 1.00 46.92 ? 19  ALA C C   1 
ATOM   3992  O O   . ALA C 1 17  ? -17.408 -14.572 -15.793 1.00 46.86 ? 19  ALA C O   1 
ATOM   3993  C CB  . ALA C 1 17  ? -15.371 -15.815 -13.540 1.00 46.56 ? 19  ALA C CB  1 
ATOM   3994  N N   . ASN C 1 18  A -15.826 -13.097 -15.130 1.00 47.22 ? 19  ASN C N   1 
ATOM   3995  C CA  . ASN C 1 18  A -15.791 -12.366 -16.400 1.00 47.44 ? 19  ASN C CA  1 
ATOM   3996  C C   . ASN C 1 18  A -14.438 -11.712 -16.672 1.00 47.89 ? 19  ASN C C   1 
ATOM   3997  O O   . ASN C 1 18  A -13.508 -11.849 -15.876 1.00 47.97 ? 19  ASN C O   1 
ATOM   3998  C CB  . ASN C 1 18  A -16.946 -11.352 -16.504 1.00 47.31 ? 19  ASN C CB  1 
ATOM   3999  C CG  . ASN C 1 18  A -16.925 -10.298 -15.398 1.00 47.02 ? 19  ASN C CG  1 
ATOM   4000  O OD1 . ASN C 1 18  A -15.871 -9.942  -14.865 1.00 46.94 ? 19  ASN C OD1 1 
ATOM   4001  N ND2 . ASN C 1 18  A -18.103 -9.781  -15.063 1.00 45.85 ? 19  ASN C ND2 1 
ATOM   4002  N N   . ASN C 1 19  ? -14.344 -10.999 -17.795 1.00 48.48 ? 20  ASN C N   1 
ATOM   4003  C CA  . ASN C 1 19  ? -13.089 -10.399 -18.260 1.00 49.03 ? 20  ASN C CA  1 
ATOM   4004  C C   . ASN C 1 19  ? -12.671 -9.114  -17.519 1.00 49.19 ? 20  ASN C C   1 
ATOM   4005  O O   . ASN C 1 19  ? -11.548 -8.631  -17.708 1.00 49.33 ? 20  ASN C O   1 
ATOM   4006  C CB  . ASN C 1 19  ? -13.160 -10.114 -19.776 1.00 49.24 ? 20  ASN C CB  1 
ATOM   4007  C CG  . ASN C 1 19  ? -13.273 -11.386 -20.629 1.00 49.96 ? 20  ASN C CG  1 
ATOM   4008  O OD1 . ASN C 1 19  ? -12.730 -12.440 -20.288 1.00 50.77 ? 20  ASN C OD1 1 
ATOM   4009  N ND2 . ASN C 1 19  ? -13.968 -11.274 -21.762 1.00 50.16 ? 20  ASN C ND2 1 
ATOM   4010  N N   . SER C 1 20  ? -13.559 -8.575  -16.680 1.00 49.24 ? 21  SER C N   1 
ATOM   4011  C CA  . SER C 1 20  ? -13.387 -7.225  -16.117 1.00 49.29 ? 21  SER C CA  1 
ATOM   4012  C C   . SER C 1 20  ? -12.166 -7.042  -15.200 1.00 49.32 ? 21  SER C C   1 
ATOM   4013  O O   . SER C 1 20  ? -11.698 -7.991  -14.561 1.00 49.15 ? 21  SER C O   1 
ATOM   4014  C CB  . SER C 1 20  ? -14.669 -6.745  -15.421 1.00 49.28 ? 21  SER C CB  1 
ATOM   4015  O OG  . SER C 1 20  ? -14.592 -6.898  -14.016 1.00 49.46 ? 21  SER C OG  1 
ATOM   4016  N N   . THR C 1 21  ? -11.670 -5.804  -15.154 1.00 49.35 ? 22  THR C N   1 
ATOM   4017  C CA  . THR C 1 21  ? -10.473 -5.438  -14.394 1.00 49.29 ? 22  THR C CA  1 
ATOM   4018  C C   . THR C 1 21  ? -10.768 -4.353  -13.353 1.00 49.18 ? 22  THR C C   1 
ATOM   4019  O O   . THR C 1 21  ? -9.863  -3.896  -12.649 1.00 49.32 ? 22  THR C O   1 
ATOM   4020  C CB  . THR C 1 21  ? -9.345  -4.941  -15.330 1.00 49.38 ? 22  THR C CB  1 
ATOM   4021  O OG1 . THR C 1 21  ? -9.841  -3.874  -16.148 1.00 49.70 ? 22  THR C OG1 1 
ATOM   4022  C CG2 . THR C 1 21  ? -8.833  -6.068  -16.226 1.00 49.45 ? 22  THR C CG2 1 
ATOM   4023  N N   . GLU C 1 22  ? -12.036 -3.951  -13.262 1.00 49.00 ? 23  GLU C N   1 
ATOM   4024  C CA  . GLU C 1 22  ? -12.497 -2.945  -12.298 1.00 48.88 ? 23  GLU C CA  1 
ATOM   4025  C C   . GLU C 1 22  ? -12.078 -3.329  -10.879 1.00 48.26 ? 23  GLU C C   1 
ATOM   4026  O O   . GLU C 1 22  ? -12.020 -4.516  -10.552 1.00 48.31 ? 23  GLU C O   1 
ATOM   4027  C CB  . GLU C 1 22  ? -14.019 -2.808  -12.372 1.00 49.08 ? 23  GLU C CB  1 
ATOM   4028  C CG  . GLU C 1 22  ? -14.519 -1.375  -12.295 1.00 50.91 ? 23  GLU C CG  1 
ATOM   4029  C CD  . GLU C 1 22  ? -14.470 -0.672  -13.641 1.00 53.15 ? 23  GLU C CD  1 
ATOM   4030  O OE1 . GLU C 1 22  ? -15.331 -0.974  -14.496 1.00 53.66 ? 23  GLU C OE1 1 
ATOM   4031  O OE2 . GLU C 1 22  ? -13.576 0.183   -13.844 1.00 54.18 ? 23  GLU C OE2 1 
ATOM   4032  N N   . GLN C 1 23  ? -11.787 -2.330  -10.044 1.00 47.44 ? 24  GLN C N   1 
ATOM   4033  C CA  . GLN C 1 23  ? -11.188 -2.581  -8.729  1.00 46.60 ? 24  GLN C CA  1 
ATOM   4034  C C   . GLN C 1 23  ? -11.774 -1.748  -7.596  1.00 46.07 ? 24  GLN C C   1 
ATOM   4035  O O   . GLN C 1 23  ? -11.983 -0.543  -7.750  1.00 46.06 ? 24  GLN C O   1 
ATOM   4036  C CB  . GLN C 1 23  ? -9.677  -2.369  -8.787  1.00 46.59 ? 24  GLN C CB  1 
ATOM   4037  C CG  . GLN C 1 23  ? -8.923  -3.488  -9.491  1.00 46.99 ? 24  GLN C CG  1 
ATOM   4038  C CD  . GLN C 1 23  ? -7.438  -3.214  -9.625  1.00 47.09 ? 24  GLN C CD  1 
ATOM   4039  O OE1 . GLN C 1 23  ? -7.010  -2.065  -9.730  1.00 46.79 ? 24  GLN C OE1 1 
ATOM   4040  N NE2 . GLN C 1 23  ? -6.641  -4.277  -9.626  1.00 47.70 ? 24  GLN C NE2 1 
ATOM   4041  N N   . VAL C 1 24  ? -12.021 -2.400  -6.458  1.00 45.25 ? 25  VAL C N   1 
ATOM   4042  C CA  . VAL C 1 24  ? -12.500 -1.729  -5.241  1.00 44.57 ? 25  VAL C CA  1 
ATOM   4043  C C   . VAL C 1 24  ? -11.565 -1.960  -4.047  1.00 44.12 ? 25  VAL C C   1 
ATOM   4044  O O   . VAL C 1 24  ? -10.674 -2.810  -4.101  1.00 43.87 ? 25  VAL C O   1 
ATOM   4045  C CB  . VAL C 1 24  ? -13.946 -2.159  -4.850  1.00 44.47 ? 25  VAL C CB  1 
ATOM   4046  C CG1 . VAL C 1 24  ? -14.912 -1.940  -6.002  1.00 44.48 ? 25  VAL C CG1 1 
ATOM   4047  C CG2 . VAL C 1 24  ? -13.982 -3.611  -4.385  1.00 44.57 ? 25  VAL C CG2 1 
ATOM   4048  N N   . ASP C 1 25  ? -11.779 -1.197  -2.976  1.00 43.71 ? 26  ASP C N   1 
ATOM   4049  C CA  . ASP C 1 25  ? -11.029 -1.362  -1.729  1.00 43.33 ? 26  ASP C CA  1 
ATOM   4050  C C   . ASP C 1 25  ? -11.931 -1.803  -0.580  1.00 42.86 ? 26  ASP C C   1 
ATOM   4051  O O   . ASP C 1 25  ? -13.124 -1.501  -0.555  1.00 42.43 ? 26  ASP C O   1 
ATOM   4052  C CB  . ASP C 1 25  ? -10.307 -0.063  -1.337  1.00 43.35 ? 26  ASP C CB  1 
ATOM   4053  C CG  . ASP C 1 25  ? -9.307  0.404   -2.385  1.00 44.21 ? 26  ASP C CG  1 
ATOM   4054  O OD1 . ASP C 1 25  ? -8.958  -0.384  -3.292  1.00 45.30 ? 26  ASP C OD1 1 
ATOM   4055  O OD2 . ASP C 1 25  ? -8.862  1.571   -2.300  1.00 45.16 ? 26  ASP C OD2 1 
ATOM   4056  N N   . THR C 1 26  ? -11.336 -2.528  0.362   1.00 42.66 ? 27  THR C N   1 
ATOM   4057  C CA  . THR C 1 26  ? -11.977 -2.894  1.623   1.00 42.54 ? 27  THR C CA  1 
ATOM   4058  C C   . THR C 1 26  ? -11.084 -2.386  2.765   1.00 42.70 ? 27  THR C C   1 
ATOM   4059  O O   . THR C 1 26  ? -9.999  -1.860  2.511   1.00 42.65 ? 27  THR C O   1 
ATOM   4060  C CB  . THR C 1 26  ? -12.196 -4.428  1.741   1.00 42.42 ? 27  THR C CB  1 
ATOM   4061  O OG1 . THR C 1 26  ? -10.931 -5.102  1.744   1.00 42.37 ? 27  THR C OG1 1 
ATOM   4062  C CG2 . THR C 1 26  ? -13.036 -4.955  0.583   1.00 41.89 ? 27  THR C CG2 1 
ATOM   4063  N N   . ILE C 1 27  ? -11.520 -2.564  4.003   1.00 42.88 ? 28  ILE C N   1 
ATOM   4064  C CA  . ILE C 1 27  ? -10.703 -2.157  5.133   1.00 42.98 ? 28  ILE C CA  1 
ATOM   4065  C C   . ILE C 1 27  ? -9.446  -3.009  5.219   1.00 42.96 ? 28  ILE C C   1 
ATOM   4066  O O   . ILE C 1 27  ? -8.375  -2.508  5.533   1.00 43.16 ? 28  ILE C O   1 
ATOM   4067  C CB  . ILE C 1 27  ? -11.480 -2.221  6.456   1.00 43.06 ? 28  ILE C CB  1 
ATOM   4068  C CG1 . ILE C 1 27  ? -11.984 -0.830  6.834   1.00 43.29 ? 28  ILE C CG1 1 
ATOM   4069  C CG2 . ILE C 1 27  ? -10.605 -2.767  7.558   1.00 42.97 ? 28  ILE C CG2 1 
ATOM   4070  C CD1 . ILE C 1 27  ? -13.060 -0.837  7.882   1.00 44.21 ? 28  ILE C CD1 1 
ATOM   4071  N N   . MET C 1 28  ? -9.687  -4.244  4.591   1.00 47.45 ? 31  MET C N   1 
ATOM   4072  C CA  . MET C 1 28  ? -8.667  -5.221  4.952   1.00 47.28 ? 31  MET C CA  1 
ATOM   4073  C C   . MET C 1 28  ? -7.820  -5.606  3.743   1.00 47.23 ? 31  MET C C   1 
ATOM   4074  O O   . MET C 1 28  ? -6.784  -6.256  3.881   1.00 47.20 ? 31  MET C O   1 
ATOM   4075  C CB  . MET C 1 28  ? -9.311  -6.468  5.561   1.00 47.40 ? 31  MET C CB  1 
ATOM   4076  C CG  . MET C 1 28  ? -9.468  -6.410  7.072   1.00 47.54 ? 31  MET C CG  1 
ATOM   4077  S SD  . MET C 1 28  ? -9.534  -8.045  7.828   1.00 48.79 ? 31  MET C SD  1 
ATOM   4078  C CE  . MET C 1 28  ? -10.879 -8.789  6.908   1.00 48.36 ? 31  MET C CE  1 
ATOM   4079  N N   . GLU C 1 29  ? -8.268  -5.200  2.560   1.00 47.17 ? 32  GLU C N   1 
ATOM   4080  C CA  . GLU C 1 29  ? -7.553  -5.502  1.325   1.00 47.31 ? 32  GLU C CA  1 
ATOM   4081  C C   . GLU C 1 29  ? -7.815  -4.442  0.261   1.00 47.23 ? 32  GLU C C   1 
ATOM   4082  O O   . GLU C 1 29  ? -8.965  -4.156  -0.074  1.00 47.00 ? 32  GLU C O   1 
ATOM   4083  C CB  . GLU C 1 29  ? -7.951  -6.883  0.800   1.00 47.32 ? 32  GLU C CB  1 
ATOM   4084  C CG  . GLU C 1 29  ? -7.005  -7.444  -0.250  1.00 48.16 ? 32  GLU C CG  1 
ATOM   4085  C CD  . GLU C 1 29  ? -7.539  -8.704  -0.902  1.00 49.26 ? 32  GLU C CD  1 
ATOM   4086  O OE1 . GLU C 1 29  ? -8.383  -9.384  -0.281  1.00 49.85 ? 32  GLU C OE1 1 
ATOM   4087  O OE2 . GLU C 1 29  ? -7.115  -9.014  -2.035  1.00 49.64 ? 32  GLU C OE2 1 
ATOM   4088  N N   . LYS C 1 30  ? -6.742  -3.862  -0.266  1.00 47.24 ? 33  LYS C N   1 
ATOM   4089  C CA  . LYS C 1 30  ? -6.853  -2.834  -1.294  1.00 47.30 ? 33  LYS C CA  1 
ATOM   4090  C C   . LYS C 1 30  ? -6.760  -3.489  -2.668  1.00 47.13 ? 33  LYS C C   1 
ATOM   4091  O O   . LYS C 1 30  ? -6.256  -4.607  -2.788  1.00 47.12 ? 33  LYS C O   1 
ATOM   4092  C CB  . LYS C 1 30  ? -5.752  -1.778  -1.116  1.00 47.22 ? 33  LYS C CB  1 
ATOM   4093  C CG  . LYS C 1 30  ? -5.690  -1.149  0.282   1.00 47.42 ? 33  LYS C CG  1 
ATOM   4094  C CD  . LYS C 1 30  ? -6.796  -0.113  0.501   1.00 47.54 ? 33  LYS C CD  1 
ATOM   4095  C CE  . LYS C 1 30  ? -6.862  0.358   1.953   1.00 47.29 ? 33  LYS C CE  1 
ATOM   4096  N NZ  . LYS C 1 30  ? -7.562  -0.618  2.836   1.00 46.39 ? 33  LYS C NZ  1 
ATOM   4097  N N   . ASN C 1 31  ? -7.227  -2.788  -3.695  1.00 47.04 ? 34  ASN C N   1 
ATOM   4098  C CA  . ASN C 1 31  ? -7.106  -3.259  -5.071  1.00 47.23 ? 34  ASN C CA  1 
ATOM   4099  C C   . ASN C 1 31  ? -7.646  -4.669  -5.302  1.00 46.38 ? 34  ASN C C   1 
ATOM   4100  O O   . ASN C 1 31  ? -6.946  -5.533  -5.830  1.00 46.49 ? 34  ASN C O   1 
ATOM   4101  C CB  . ASN C 1 31  ? -5.650  -3.177  -5.536  1.00 47.96 ? 34  ASN C CB  1 
ATOM   4102  C CG  . ASN C 1 31  ? -5.367  -1.928  -6.346  1.00 50.49 ? 34  ASN C CG  1 
ATOM   4103  O OD1 . ASN C 1 31  ? -5.582  -1.897  -7.558  1.00 56.35 ? 34  ASN C OD1 1 
ATOM   4104  N ND2 . ASN C 1 31  ? -4.881  -0.887  -5.679  1.00 53.03 ? 34  ASN C ND2 1 
ATOM   4105  N N   . VAL C 1 32  ? -8.896  -4.893  -4.910  1.00 45.21 ? 35  VAL C N   1 
ATOM   4106  C CA  . VAL C 1 32  ? -9.570  -6.167  -5.167  1.00 44.13 ? 35  VAL C CA  1 
ATOM   4107  C C   . VAL C 1 32  ? -10.338 -6.104  -6.485  1.00 43.60 ? 35  VAL C C   1 
ATOM   4108  O O   . VAL C 1 32  ? -11.194 -5.233  -6.664  1.00 43.60 ? 35  VAL C O   1 
ATOM   4109  C CB  . VAL C 1 32  ? -10.555 -6.530  -4.024  1.00 44.15 ? 35  VAL C CB  1 
ATOM   4110  C CG1 . VAL C 1 32  ? -11.331 -7.808  -4.348  1.00 44.01 ? 35  VAL C CG1 1 
ATOM   4111  C CG2 . VAL C 1 32  ? -9.821  -6.676  -2.706  1.00 43.76 ? 35  VAL C CG2 1 
ATOM   4112  N N   . THR C 1 33  A -10.033 -7.020  -7.404  1.00 42.67 ? 35  THR C N   1 
ATOM   4113  C CA  . THR C 1 33  A -10.761 -7.098  -8.669  1.00 41.94 ? 35  THR C CA  1 
ATOM   4114  C C   . THR C 1 33  A -12.118 -7.761  -8.441  1.00 41.56 ? 35  THR C C   1 
ATOM   4115  O O   . THR C 1 33  A -12.217 -8.778  -7.746  1.00 41.55 ? 35  THR C O   1 
ATOM   4116  C CB  . THR C 1 33  A -9.968  -7.848  -9.772  1.00 41.90 ? 35  THR C CB  1 
ATOM   4117  O OG1 . THR C 1 33  A -8.669  -7.262  -9.913  1.00 42.18 ? 35  THR C OG1 1 
ATOM   4118  C CG2 . THR C 1 33  A -10.683 -7.759  -11.119 1.00 41.45 ? 35  THR C CG2 1 
ATOM   4119  N N   . VAL C 1 34  ? -13.156 -7.158  -9.016  1.00 40.87 ? 36  VAL C N   1 
ATOM   4120  C CA  . VAL C 1 34  ? -14.524 -7.656  -8.910  1.00 40.26 ? 36  VAL C CA  1 
ATOM   4121  C C   . VAL C 1 34  ? -15.170 -7.744  -10.293 1.00 40.06 ? 36  VAL C C   1 
ATOM   4122  O O   . VAL C 1 34  ? -14.685 -7.139  -11.251 1.00 39.99 ? 36  VAL C O   1 
ATOM   4123  C CB  . VAL C 1 34  ? -15.390 -6.779  -7.969  1.00 40.32 ? 36  VAL C CB  1 
ATOM   4124  C CG1 . VAL C 1 34  ? -14.920 -6.908  -6.523  1.00 39.82 ? 36  VAL C CG1 1 
ATOM   4125  C CG2 . VAL C 1 34  ? -15.389 -5.314  -8.422  1.00 40.08 ? 36  VAL C CG2 1 
ATOM   4126  N N   . THR C 1 35  ? -16.261 -8.500  -10.387 1.00 39.83 ? 37  THR C N   1 
ATOM   4127  C CA  . THR C 1 35  ? -16.917 -8.768  -11.668 1.00 39.58 ? 37  THR C CA  1 
ATOM   4128  C C   . THR C 1 35  ? -17.780 -7.593  -12.106 1.00 39.81 ? 37  THR C C   1 
ATOM   4129  O O   . THR C 1 35  ? -17.915 -7.324  -13.298 1.00 39.91 ? 37  THR C O   1 
ATOM   4130  C CB  . THR C 1 35  ? -17.792 -10.051 -11.622 1.00 39.49 ? 37  THR C CB  1 
ATOM   4131  O OG1 . THR C 1 35  ? -18.902 -9.851  -10.740 1.00 38.96 ? 37  THR C OG1 1 
ATOM   4132  C CG2 . THR C 1 35  ? -16.979 -11.263 -11.162 1.00 39.13 ? 37  THR C CG2 1 
ATOM   4133  N N   . HIS C 1 36  ? -18.381 -6.913  -11.132 1.00 39.93 ? 38  HIS C N   1 
ATOM   4134  C CA  . HIS C 1 36  ? -19.197 -5.731  -11.387 1.00 40.01 ? 38  HIS C CA  1 
ATOM   4135  C C   . HIS C 1 36  ? -18.956 -4.694  -10.293 1.00 39.97 ? 38  HIS C C   1 
ATOM   4136  O O   . HIS C 1 36  ? -18.960 -5.022  -9.099  1.00 40.10 ? 38  HIS C O   1 
ATOM   4137  C CB  . HIS C 1 36  ? -20.687 -6.095  -11.451 1.00 40.06 ? 38  HIS C CB  1 
ATOM   4138  C CG  . HIS C 1 36  ? -21.031 -7.068  -12.536 1.00 40.71 ? 38  HIS C CG  1 
ATOM   4139  N ND1 . HIS C 1 36  ? -20.851 -8.429  -12.401 1.00 41.08 ? 38  HIS C ND1 1 
ATOM   4140  C CD2 . HIS C 1 36  ? -21.545 -6.878  -13.774 1.00 40.90 ? 38  HIS C CD2 1 
ATOM   4141  C CE1 . HIS C 1 36  ? -21.236 -9.034  -13.510 1.00 41.41 ? 38  HIS C CE1 1 
ATOM   4142  N NE2 . HIS C 1 36  ? -21.664 -8.116  -14.358 1.00 41.40 ? 38  HIS C NE2 1 
ATOM   4143  N N   . ALA C 1 37  ? -18.746 -3.446  -10.706 1.00 39.59 ? 39  ALA C N   1 
ATOM   4144  C CA  . ALA C 1 37  ? -18.577 -2.335  -9.770  1.00 39.14 ? 39  ALA C CA  1 
ATOM   4145  C C   . ALA C 1 37  ? -19.315 -1.093  -10.262 1.00 38.82 ? 39  ALA C C   1 
ATOM   4146  O O   . ALA C 1 37  ? -19.609 -0.969  -11.456 1.00 38.94 ? 39  ALA C O   1 
ATOM   4147  C CB  . ALA C 1 37  ? -17.104 -2.037  -9.564  1.00 39.07 ? 39  ALA C CB  1 
ATOM   4148  N N   . GLN C 1 38  ? -19.624 -0.186  -9.337  1.00 38.26 ? 40  GLN C N   1 
ATOM   4149  C CA  . GLN C 1 38  ? -20.290 1.073   -9.678  1.00 37.61 ? 40  GLN C CA  1 
ATOM   4150  C C   . GLN C 1 38  ? -19.526 2.289   -9.155  1.00 37.18 ? 40  GLN C C   1 
ATOM   4151  O O   . GLN C 1 38  ? -19.322 2.449   -7.940  1.00 36.74 ? 40  GLN C O   1 
ATOM   4152  C CB  . GLN C 1 38  ? -21.737 1.089   -9.175  1.00 37.64 ? 40  GLN C CB  1 
ATOM   4153  C CG  . GLN C 1 38  ? -22.602 2.163   -9.827  1.00 37.83 ? 40  GLN C CG  1 
ATOM   4154  C CD  . GLN C 1 38  ? -24.042 2.126   -9.360  1.00 38.32 ? 40  GLN C CD  1 
ATOM   4155  O OE1 . GLN C 1 38  ? -24.642 1.057   -9.237  1.00 38.91 ? 40  GLN C OE1 1 
ATOM   4156  N NE2 . GLN C 1 38  ? -24.611 3.299   -9.105  1.00 38.22 ? 40  GLN C NE2 1 
ATOM   4157  N N   . ASP C 1 39  ? -19.091 3.127   -10.096 1.00 36.75 ? 41  ASP C N   1 
ATOM   4158  C CA  . ASP C 1 39  ? -18.478 4.412   -9.787  1.00 36.05 ? 41  ASP C CA  1 
ATOM   4159  C C   . ASP C 1 39  ? -19.598 5.341   -9.364  1.00 35.48 ? 41  ASP C C   1 
ATOM   4160  O O   . ASP C 1 39  ? -20.671 5.343   -9.966  1.00 35.37 ? 41  ASP C O   1 
ATOM   4161  C CB  . ASP C 1 39  ? -17.751 4.971   -11.016 1.00 36.18 ? 41  ASP C CB  1 
ATOM   4162  C CG  . ASP C 1 39  ? -16.771 6.097   -10.674 1.00 36.72 ? 41  ASP C CG  1 
ATOM   4163  O OD1 . ASP C 1 39  ? -16.901 6.734   -9.604  1.00 38.07 ? 41  ASP C OD1 1 
ATOM   4164  O OD2 . ASP C 1 39  ? -15.857 6.349   -11.490 1.00 36.59 ? 41  ASP C OD2 1 
ATOM   4165  N N   . ILE C 1 40  ? -19.357 6.116   -8.314  1.00 35.04 ? 42  ILE C N   1 
ATOM   4166  C CA  . ILE C 1 40  ? -20.369 7.043   -7.817  1.00 34.69 ? 42  ILE C CA  1 
ATOM   4167  C C   . ILE C 1 40  ? -19.831 8.473   -7.704  1.00 34.74 ? 42  ILE C C   1 
ATOM   4168  O O   . ILE C 1 40  ? -20.450 9.333   -7.073  1.00 34.69 ? 42  ILE C O   1 
ATOM   4169  C CB  . ILE C 1 40  ? -21.004 6.553   -6.475  1.00 34.65 ? 42  ILE C CB  1 
ATOM   4170  C CG1 . ILE C 1 40  ? -19.931 6.246   -5.419  1.00 33.67 ? 42  ILE C CG1 1 
ATOM   4171  C CG2 . ILE C 1 40  ? -21.904 5.332   -6.717  1.00 34.48 ? 42  ILE C CG2 1 
ATOM   4172  C CD1 . ILE C 1 40  ? -20.492 6.029   -4.016  1.00 31.83 ? 42  ILE C CD1 1 
ATOM   4173  N N   . LEU C 1 41  ? -18.691 8.722   -8.349  1.00 34.66 ? 43  LEU C N   1 
ATOM   4174  C CA  . LEU C 1 41  ? -17.994 10.006  -8.229  1.00 34.74 ? 43  LEU C CA  1 
ATOM   4175  C C   . LEU C 1 41  ? -17.735 10.694  -9.576  1.00 34.83 ? 43  LEU C C   1 
ATOM   4176  O O   . LEU C 1 41  ? -17.049 10.136  -10.434 1.00 34.68 ? 43  LEU C O   1 
ATOM   4177  C CB  . LEU C 1 41  ? -16.674 9.822   -7.458  1.00 34.22 ? 43  LEU C CB  1 
ATOM   4178  C CG  . LEU C 1 41  ? -15.822 11.070  -7.204  1.00 33.97 ? 43  LEU C CG  1 
ATOM   4179  C CD1 . LEU C 1 41  ? -16.571 12.082  -6.361  1.00 33.09 ? 43  LEU C CD1 1 
ATOM   4180  C CD2 . LEU C 1 41  ? -14.491 10.712  -6.549  1.00 33.40 ? 43  LEU C CD2 1 
ATOM   4181  N N   . GLU C 1 42  ? -18.288 11.899  -9.740  1.00 35.22 ? 44  GLU C N   1 
ATOM   4182  C CA  . GLU C 1 42  ? -17.974 12.782  -10.875 1.00 35.72 ? 44  GLU C CA  1 
ATOM   4183  C C   . GLU C 1 42  ? -16.660 13.513  -10.694 1.00 35.88 ? 44  GLU C C   1 
ATOM   4184  O O   . GLU C 1 42  ? -16.427 14.131  -9.653  1.00 35.85 ? 44  GLU C O   1 
ATOM   4185  C CB  . GLU C 1 42  ? -19.043 13.857  -11.062 1.00 35.79 ? 44  GLU C CB  1 
ATOM   4186  C CG  . GLU C 1 42  ? -20.083 13.574  -12.118 1.00 36.89 ? 44  GLU C CG  1 
ATOM   4187  C CD  . GLU C 1 42  ? -19.527 13.196  -13.487 1.00 37.63 ? 44  GLU C CD  1 
ATOM   4188  O OE1 . GLU C 1 42  ? -18.550 13.816  -13.963 1.00 37.29 ? 44  GLU C OE1 1 
ATOM   4189  O OE2 . GLU C 1 42  ? -20.097 12.265  -14.093 1.00 38.74 ? 44  GLU C OE2 1 
ATOM   4190  N N   . LYS C 1 43  ? -15.824 13.462  -11.728 1.00 36.24 ? 45  LYS C N   1 
ATOM   4191  C CA  . LYS C 1 43  ? -14.558 14.197  -11.756 1.00 36.59 ? 45  LYS C CA  1 
ATOM   4192  C C   . LYS C 1 43  ? -14.541 15.186  -12.920 1.00 36.52 ? 45  LYS C C   1 
ATOM   4193  O O   . LYS C 1 43  ? -13.578 15.927  -13.092 1.00 37.02 ? 45  LYS C O   1 
ATOM   4194  C CB  . LYS C 1 43  ? -13.369 13.233  -11.870 1.00 36.67 ? 45  LYS C CB  1 
ATOM   4195  C CG  . LYS C 1 43  ? -13.382 12.076  -10.873 1.00 37.62 ? 45  LYS C CG  1 
ATOM   4196  C CD  . LYS C 1 43  ? -12.384 10.981  -11.261 1.00 38.77 ? 45  LYS C CD  1 
ATOM   4197  C CE  . LYS C 1 43  ? -12.673 9.671   -10.528 1.00 39.38 ? 45  LYS C CE  1 
ATOM   4198  N NZ  . LYS C 1 43  ? -14.040 9.132   -10.826 1.00 39.56 ? 45  LYS C NZ  1 
ATOM   4199  N N   . THR C 1 44  ? -15.623 15.209  -13.695 1.00 36.37 ? 46  THR C N   1 
ATOM   4200  C CA  . THR C 1 44  ? -15.686 15.959  -14.951 1.00 36.27 ? 46  THR C CA  1 
ATOM   4201  C C   . THR C 1 44  ? -16.628 17.170  -14.898 1.00 36.05 ? 46  THR C C   1 
ATOM   4202  O O   . THR C 1 44  ? -17.789 17.049  -14.516 1.00 35.79 ? 46  THR C O   1 
ATOM   4203  C CB  . THR C 1 44  ? -16.095 15.019  -16.131 1.00 36.36 ? 46  THR C CB  1 
ATOM   4204  O OG1 . THR C 1 44  ? -15.090 14.018  -16.313 1.00 36.04 ? 46  THR C OG1 1 
ATOM   4205  C CG2 . THR C 1 44  ? -16.262 15.790  -17.442 1.00 36.83 ? 46  THR C CG2 1 
ATOM   4206  N N   . HIS C 1 45  ? -16.099 18.330  -15.285 1.00 36.06 ? 47  HIS C N   1 
ATOM   4207  C CA  . HIS C 1 45  ? -16.892 19.534  -15.536 1.00 36.29 ? 47  HIS C CA  1 
ATOM   4208  C C   . HIS C 1 45  ? -16.574 20.052  -16.950 1.00 36.50 ? 47  HIS C C   1 
ATOM   4209  O O   . HIS C 1 45  ? -15.590 19.624  -17.557 1.00 36.57 ? 47  HIS C O   1 
ATOM   4210  C CB  . HIS C 1 45  ? -16.595 20.605  -14.480 1.00 36.13 ? 47  HIS C CB  1 
ATOM   4211  C CG  . HIS C 1 45  ? -15.174 21.073  -14.480 1.00 36.34 ? 47  HIS C CG  1 
ATOM   4212  N ND1 . HIS C 1 45  ? -14.743 22.142  -15.235 1.00 36.47 ? 47  HIS C ND1 1 
ATOM   4213  C CD2 . HIS C 1 45  ? -14.082 20.609  -13.827 1.00 36.92 ? 47  HIS C CD2 1 
ATOM   4214  C CE1 . HIS C 1 45  ? -13.447 22.320  -15.044 1.00 36.80 ? 47  HIS C CE1 1 
ATOM   4215  N NE2 . HIS C 1 45  ? -13.021 21.403  -14.194 1.00 36.87 ? 47  HIS C NE2 1 
ATOM   4216  N N   . ASN C 1 46  ? -17.388 20.968  -17.473 1.00 36.64 ? 48  ASN C N   1 
ATOM   4217  C CA  . ASN C 1 46  ? -17.213 21.441  -18.854 1.00 36.77 ? 48  ASN C CA  1 
ATOM   4218  C C   . ASN C 1 46  ? -16.326 22.682  -19.023 1.00 37.09 ? 48  ASN C C   1 
ATOM   4219  O O   . ASN C 1 46  ? -16.108 23.144  -20.147 1.00 37.27 ? 48  ASN C O   1 
ATOM   4220  C CB  . ASN C 1 46  ? -18.570 21.633  -19.551 1.00 36.63 ? 48  ASN C CB  1 
ATOM   4221  C CG  . ASN C 1 46  ? -19.352 22.821  -19.014 1.00 36.20 ? 48  ASN C CG  1 
ATOM   4222  O OD1 . ASN C 1 46  ? -18.824 23.651  -18.277 1.00 36.30 ? 48  ASN C OD1 1 
ATOM   4223  N ND2 . ASN C 1 46  ? -20.621 22.909  -19.390 1.00 35.36 ? 48  ASN C ND2 1 
ATOM   4224  N N   . GLY C 1 47  ? -15.834 23.224  -17.911 1.00 37.21 ? 49  GLY C N   1 
ATOM   4225  C CA  . GLY C 1 47  ? -14.934 24.384  -17.932 1.00 37.52 ? 49  GLY C CA  1 
ATOM   4226  C C   . GLY C 1 47  ? -15.566 25.719  -18.312 1.00 37.76 ? 49  GLY C C   1 
ATOM   4227  O O   . GLY C 1 47  ? -14.854 26.671  -18.636 1.00 37.63 ? 49  GLY C O   1 
ATOM   4228  N N   . LYS C 1 48  ? -16.896 25.795  -18.243 1.00 37.90 ? 50  LYS C N   1 
ATOM   4229  C CA  . LYS C 1 48  ? -17.649 26.949  -18.734 1.00 38.24 ? 50  LYS C CA  1 
ATOM   4230  C C   . LYS C 1 48  ? -18.644 27.498  -17.710 1.00 38.23 ? 50  LYS C C   1 
ATOM   4231  O O   . LYS C 1 48  ? -19.113 26.768  -16.833 1.00 38.22 ? 50  LYS C O   1 
ATOM   4232  C CB  . LYS C 1 48  ? -18.418 26.561  -20.000 1.00 38.37 ? 50  LYS C CB  1 
ATOM   4233  C CG  . LYS C 1 48  ? -17.566 26.356  -21.242 1.00 39.42 ? 50  LYS C CG  1 
ATOM   4234  C CD  . LYS C 1 48  ? -18.185 25.283  -22.141 1.00 41.17 ? 50  LYS C CD  1 
ATOM   4235  C CE  . LYS C 1 48  ? -17.909 25.547  -23.613 1.00 42.66 ? 50  LYS C CE  1 
ATOM   4236  N NZ  . LYS C 1 48  ? -18.776 26.646  -24.151 1.00 43.68 ? 50  LYS C NZ  1 
ATOM   4237  N N   . LEU C 1 49  ? -18.976 28.781  -17.848 1.00 38.21 ? 51  LEU C N   1 
ATOM   4238  C CA  . LEU C 1 49  ? -20.034 29.405  -17.054 1.00 38.41 ? 51  LEU C CA  1 
ATOM   4239  C C   . LEU C 1 49  ? -21.344 29.450  -17.834 1.00 38.58 ? 51  LEU C C   1 
ATOM   4240  O O   . LEU C 1 49  ? -21.461 30.170  -18.824 1.00 38.47 ? 51  LEU C O   1 
ATOM   4241  C CB  . LEU C 1 49  ? -19.630 30.813  -16.616 1.00 38.30 ? 51  LEU C CB  1 
ATOM   4242  C CG  . LEU C 1 49  ? -18.324 30.985  -15.840 1.00 38.70 ? 51  LEU C CG  1 
ATOM   4243  C CD1 . LEU C 1 49  ? -18.138 32.450  -15.493 1.00 38.91 ? 51  LEU C CD1 1 
ATOM   4244  C CD2 . LEU C 1 49  ? -18.257 30.114  -14.578 1.00 38.34 ? 51  LEU C CD2 1 
ATOM   4245  N N   . CYS C 1 50  ? -22.331 28.692  -17.366 1.00 39.02 ? 52  CYS C N   1 
ATOM   4246  C CA  . CYS C 1 50  ? -23.557 28.459  -18.126 1.00 39.49 ? 52  CYS C CA  1 
ATOM   4247  C C   . CYS C 1 50  ? -24.781 29.094  -17.500 1.00 39.35 ? 52  CYS C C   1 
ATOM   4248  O O   . CYS C 1 50  ? -24.712 29.658  -16.408 1.00 39.57 ? 52  CYS C O   1 
ATOM   4249  C CB  . CYS C 1 50  ? -23.803 26.958  -18.275 1.00 39.73 ? 52  CYS C CB  1 
ATOM   4250  S SG  . CYS C 1 50  ? -22.429 26.041  -18.979 1.00 41.55 ? 52  CYS C SG  1 
ATOM   4251  N N   . ASP C 1 51  ? -25.902 28.996  -18.209 1.00 39.33 ? 53  ASP C N   1 
ATOM   4252  C CA  . ASP C 1 51  ? -27.198 29.377  -17.675 1.00 39.48 ? 53  ASP C CA  1 
ATOM   4253  C C   . ASP C 1 51  ? -27.649 28.335  -16.662 1.00 39.47 ? 53  ASP C C   1 
ATOM   4254  O O   . ASP C 1 51  ? -27.266 27.167  -16.747 1.00 39.57 ? 53  ASP C O   1 
ATOM   4255  C CB  . ASP C 1 51  ? -28.240 29.478  -18.795 1.00 39.66 ? 53  ASP C CB  1 
ATOM   4256  C CG  . ASP C 1 51  ? -27.921 30.571  -19.818 1.00 40.34 ? 53  ASP C CG  1 
ATOM   4257  O OD1 . ASP C 1 51  ? -28.698 30.707  -20.784 1.00 40.99 ? 53  ASP C OD1 1 
ATOM   4258  O OD2 . ASP C 1 51  ? -26.906 31.289  -19.672 1.00 41.01 ? 53  ASP C OD2 1 
ATOM   4259  N N   . LEU C 1 52  A -28.464 28.764  -15.706 1.00 39.43 ? 53  LEU C N   1 
ATOM   4260  C CA  . LEU C 1 52  A -29.046 27.865  -14.728 1.00 39.42 ? 53  LEU C CA  1 
ATOM   4261  C C   . LEU C 1 52  A -30.548 27.786  -14.976 1.00 39.58 ? 53  LEU C C   1 
ATOM   4262  O O   . LEU C 1 52  A -31.263 28.771  -14.780 1.00 39.60 ? 53  LEU C O   1 
ATOM   4263  C CB  . LEU C 1 52  A -28.751 28.365  -13.310 1.00 39.39 ? 53  LEU C CB  1 
ATOM   4264  C CG  . LEU C 1 52  A -28.898 27.380  -12.150 1.00 38.92 ? 53  LEU C CG  1 
ATOM   4265  C CD1 . LEU C 1 52  A -27.663 26.497  -12.034 1.00 38.76 ? 53  LEU C CD1 1 
ATOM   4266  C CD2 . LEU C 1 52  A -29.136 28.137  -10.859 1.00 38.86 ? 53  LEU C CD2 1 
ATOM   4267  N N   . ASP C 1 53  ? -31.010 26.610  -15.409 1.00 39.75 ? 54  ASP C N   1 
ATOM   4268  C CA  . ASP C 1 53  ? -32.403 26.375  -15.837 1.00 39.86 ? 54  ASP C CA  1 
ATOM   4269  C C   . ASP C 1 53  ? -32.900 27.410  -16.860 1.00 39.35 ? 54  ASP C C   1 
ATOM   4270  O O   . ASP C 1 53  ? -34.059 27.837  -16.822 1.00 39.14 ? 54  ASP C O   1 
ATOM   4271  C CB  . ASP C 1 53  ? -33.364 26.284  -14.636 1.00 40.25 ? 54  ASP C CB  1 
ATOM   4272  C CG  . ASP C 1 53  ? -32.893 25.302  -13.572 1.00 42.25 ? 54  ASP C CG  1 
ATOM   4273  O OD1 . ASP C 1 53  ? -32.636 24.118  -13.902 1.00 44.65 ? 54  ASP C OD1 1 
ATOM   4274  O OD2 . ASP C 1 53  ? -32.789 25.712  -12.393 1.00 44.15 ? 54  ASP C OD2 1 
ATOM   4275  N N   . GLY C 1 54  ? -32.015 27.808  -17.769 1.00 38.88 ? 55  GLY C N   1 
ATOM   4276  C CA  . GLY C 1 54  ? -32.354 28.791  -18.792 1.00 38.51 ? 55  GLY C CA  1 
ATOM   4277  C C   . GLY C 1 54  ? -32.231 30.245  -18.366 1.00 38.24 ? 55  GLY C C   1 
ATOM   4278  O O   . GLY C 1 54  ? -32.416 31.141  -19.188 1.00 38.54 ? 55  GLY C O   1 
ATOM   4279  N N   . VAL C 1 55  ? -31.927 30.490  -17.091 1.00 37.81 ? 56  VAL C N   1 
ATOM   4280  C CA  . VAL C 1 55  ? -31.717 31.859  -16.598 1.00 37.38 ? 56  VAL C CA  1 
ATOM   4281  C C   . VAL C 1 55  ? -30.232 32.226  -16.662 1.00 37.09 ? 56  VAL C C   1 
ATOM   4282  O O   . VAL C 1 55  ? -29.386 31.530  -16.091 1.00 37.05 ? 56  VAL C O   1 
ATOM   4283  C CB  . VAL C 1 55  ? -32.257 32.074  -15.153 1.00 37.35 ? 56  VAL C CB  1 
ATOM   4284  C CG1 . VAL C 1 55  ? -32.177 33.552  -14.768 1.00 37.23 ? 56  VAL C CG1 1 
ATOM   4285  C CG2 . VAL C 1 55  ? -33.687 31.579  -15.023 1.00 37.07 ? 56  VAL C CG2 1 
ATOM   4286  N N   . LYS C 1 56  ? -29.927 33.319  -17.358 1.00 36.64 ? 57  LYS C N   1 
ATOM   4287  C CA  . LYS C 1 56  ? -28.542 33.737  -17.560 1.00 36.47 ? 57  LYS C CA  1 
ATOM   4288  C C   . LYS C 1 56  ? -27.924 34.357  -16.298 1.00 36.13 ? 57  LYS C C   1 
ATOM   4289  O O   . LYS C 1 56  ? -28.594 35.092  -15.575 1.00 35.88 ? 57  LYS C O   1 
ATOM   4290  C CB  . LYS C 1 56  ? -28.432 34.717  -18.732 1.00 36.46 ? 57  LYS C CB  1 
ATOM   4291  C CG  . LYS C 1 56  ? -27.028 34.770  -19.320 1.00 37.33 ? 57  LYS C CG  1 
ATOM   4292  C CD  . LYS C 1 56  ? -26.635 36.143  -19.844 1.00 38.23 ? 57  LYS C CD  1 
ATOM   4293  C CE  . LYS C 1 56  ? -25.145 36.170  -20.141 1.00 38.24 ? 57  LYS C CE  1 
ATOM   4294  N NZ  . LYS C 1 56  ? -24.702 37.467  -20.699 1.00 39.09 ? 57  LYS C NZ  1 
ATOM   4295  N N   . PRO C 1 57  ? -26.642 34.047  -16.025 1.00 35.81 ? 58  PRO C N   1 
ATOM   4296  C CA  . PRO C 1 57  ? -25.922 34.717  -14.945 1.00 35.72 ? 58  PRO C CA  1 
ATOM   4297  C C   . PRO C 1 57  ? -25.584 36.173  -15.260 1.00 35.64 ? 58  PRO C C   1 
ATOM   4298  O O   . PRO C 1 57  ? -25.596 36.578  -16.423 1.00 35.70 ? 58  PRO C O   1 
ATOM   4299  C CB  . PRO C 1 57  ? -24.628 33.904  -14.830 1.00 35.67 ? 58  PRO C CB  1 
ATOM   4300  C CG  . PRO C 1 57  ? -24.484 33.218  -16.139 1.00 35.48 ? 58  PRO C CG  1 
ATOM   4301  C CD  . PRO C 1 57  ? -25.871 32.916  -16.573 1.00 35.73 ? 58  PRO C CD  1 
ATOM   4302  N N   . LEU C 1 58  ? -25.296 36.947  -14.220 1.00 35.58 ? 59  LEU C N   1 
ATOM   4303  C CA  . LEU C 1 58  ? -24.786 38.297  -14.388 1.00 35.54 ? 59  LEU C CA  1 
ATOM   4304  C C   . LEU C 1 58  ? -23.276 38.228  -14.311 1.00 35.59 ? 59  LEU C C   1 
ATOM   4305  O O   . LEU C 1 58  ? -22.715 37.936  -13.254 1.00 35.78 ? 59  LEU C O   1 
ATOM   4306  C CB  . LEU C 1 58  ? -25.347 39.242  -13.316 1.00 35.54 ? 59  LEU C CB  1 
ATOM   4307  C CG  . LEU C 1 58  ? -24.777 40.670  -13.220 1.00 35.79 ? 59  LEU C CG  1 
ATOM   4308  C CD1 . LEU C 1 58  ? -24.871 41.424  -14.552 1.00 35.14 ? 59  LEU C CD1 1 
ATOM   4309  C CD2 . LEU C 1 58  ? -25.451 41.464  -12.111 1.00 34.86 ? 59  LEU C CD2 1 
ATOM   4310  N N   . ILE C 1 59  ? -22.625 38.478  -15.443 1.00 35.69 ? 60  ILE C N   1 
ATOM   4311  C CA  . ILE C 1 59  ? -21.170 38.401  -15.536 1.00 35.68 ? 60  ILE C CA  1 
ATOM   4312  C C   . ILE C 1 59  ? -20.594 39.815  -15.594 1.00 35.84 ? 60  ILE C C   1 
ATOM   4313  O O   . ILE C 1 59  ? -20.775 40.544  -16.576 1.00 36.00 ? 60  ILE C O   1 
ATOM   4314  C CB  . ILE C 1 59  ? -20.718 37.478  -16.708 1.00 35.65 ? 60  ILE C CB  1 
ATOM   4315  C CG1 . ILE C 1 59  ? -21.033 36.020  -16.351 1.00 35.67 ? 60  ILE C CG1 1 
ATOM   4316  C CG2 . ILE C 1 59  ? -19.222 37.633  -16.997 1.00 35.08 ? 60  ILE C CG2 1 
ATOM   4317  C CD1 . ILE C 1 59  ? -21.274 35.108  -17.529 1.00 36.30 ? 60  ILE C CD1 1 
ATOM   4318  N N   . LEU C 1 60  ? -19.919 40.195  -14.513 1.00 35.93 ? 61  LEU C N   1 
ATOM   4319  C CA  . LEU C 1 60  ? -19.538 41.581  -14.278 1.00 36.23 ? 61  LEU C CA  1 
ATOM   4320  C C   . LEU C 1 60  ? -18.245 41.984  -14.979 1.00 36.68 ? 61  LEU C C   1 
ATOM   4321  O O   . LEU C 1 60  ? -17.836 43.145  -14.906 1.00 36.79 ? 61  LEU C O   1 
ATOM   4322  C CB  . LEU C 1 60  ? -19.454 41.869  -12.774 1.00 36.14 ? 61  LEU C CB  1 
ATOM   4323  C CG  . LEU C 1 60  ? -20.753 41.845  -11.963 1.00 35.98 ? 61  LEU C CG  1 
ATOM   4324  C CD1 . LEU C 1 60  ? -20.447 41.979  -10.483 1.00 35.52 ? 61  LEU C CD1 1 
ATOM   4325  C CD2 . LEU C 1 60  ? -21.722 42.942  -12.412 1.00 35.94 ? 61  LEU C CD2 1 
ATOM   4326  N N   . ARG C 1 61  ? -17.635 41.034  -15.680 1.00 37.22 ? 62  ARG C N   1 
ATOM   4327  C CA  . ARG C 1 61  ? -16.439 41.304  -16.469 1.00 37.79 ? 62  ARG C CA  1 
ATOM   4328  C C   . ARG C 1 61  ? -15.387 41.998  -15.613 1.00 37.66 ? 62  ARG C C   1 
ATOM   4329  O O   . ARG C 1 61  ? -14.882 41.424  -14.648 1.00 37.88 ? 62  ARG C O   1 
ATOM   4330  C CB  . ARG C 1 61  ? -16.783 42.165  -17.686 1.00 38.08 ? 62  ARG C CB  1 
ATOM   4331  C CG  . ARG C 1 61  ? -18.104 41.806  -18.347 1.00 40.12 ? 62  ARG C CG  1 
ATOM   4332  C CD  . ARG C 1 61  ? -17.883 41.057  -19.651 1.00 43.83 ? 62  ARG C CD  1 
ATOM   4333  N NE  . ARG C 1 61  ? -18.320 41.834  -20.808 1.00 46.51 ? 62  ARG C NE  1 
ATOM   4334  C CZ  . ARG C 1 61  ? -17.495 42.423  -21.667 1.00 48.05 ? 62  ARG C CZ  1 
ATOM   4335  N NH1 . ARG C 1 61  ? -16.183 42.325  -21.503 1.00 48.76 ? 62  ARG C NH1 1 
ATOM   4336  N NH2 . ARG C 1 61  ? -17.982 43.110  -22.692 1.00 49.43 ? 62  ARG C NH2 1 
ATOM   4337  N N   . ASP C 1 62  ? -15.058 43.234  -15.973 1.00 37.29 ? 63  ASP C N   1 
ATOM   4338  C CA  . ASP C 1 62  ? -14.035 43.982  -15.246 1.00 37.13 ? 63  ASP C CA  1 
ATOM   4339  C C   . ASP C 1 62  ? -14.570 44.874  -14.118 1.00 36.65 ? 63  ASP C C   1 
ATOM   4340  O O   . ASP C 1 62  ? -13.806 45.614  -13.484 1.00 36.46 ? 63  ASP C O   1 
ATOM   4341  C CB  . ASP C 1 62  ? -13.183 44.786  -16.235 1.00 37.42 ? 63  ASP C CB  1 
ATOM   4342  C CG  . ASP C 1 62  ? -12.286 43.894  -17.098 1.00 39.14 ? 63  ASP C CG  1 
ATOM   4343  O OD1 . ASP C 1 62  ? -11.659 42.951  -16.547 1.00 39.97 ? 63  ASP C OD1 1 
ATOM   4344  O OD2 . ASP C 1 62  ? -12.204 44.140  -18.330 1.00 39.67 ? 63  ASP C OD2 1 
ATOM   4345  N N   . CYS C 1 63  ? -15.875 44.793  -13.862 1.00 35.90 ? 64  CYS C N   1 
ATOM   4346  C CA  . CYS C 1 63  ? -16.496 45.585  -12.803 1.00 35.47 ? 64  CYS C CA  1 
ATOM   4347  C C   . CYS C 1 63  ? -16.688 44.786  -11.519 1.00 34.57 ? 64  CYS C C   1 
ATOM   4348  O O   . CYS C 1 63  ? -16.970 43.590  -11.552 1.00 34.46 ? 64  CYS C O   1 
ATOM   4349  C CB  . CYS C 1 63  ? -17.827 46.182  -13.271 1.00 35.46 ? 64  CYS C CB  1 
ATOM   4350  S SG  . CYS C 1 63  ? -17.657 47.385  -14.614 1.00 37.95 ? 64  CYS C SG  1 
ATOM   4351  N N   . SER C 1 64  ? -16.515 45.455  -10.388 1.00 33.80 ? 65  SER C N   1 
ATOM   4352  C CA  . SER C 1 64  ? -16.791 44.849  -9.098  1.00 33.17 ? 65  SER C CA  1 
ATOM   4353  C C   . SER C 1 64  ? -18.240 45.154  -8.729  1.00 32.77 ? 65  SER C C   1 
ATOM   4354  O O   . SER C 1 64  ? -18.899 45.949  -9.405  1.00 32.74 ? 65  SER C O   1 
ATOM   4355  C CB  . SER C 1 64  ? -15.836 45.387  -8.035  1.00 32.97 ? 65  SER C CB  1 
ATOM   4356  O OG  . SER C 1 64  ? -16.206 46.693  -7.641  1.00 32.96 ? 65  SER C OG  1 
ATOM   4357  N N   . VAL C 1 65  ? -18.731 44.528  -7.664  1.00 32.07 ? 66  VAL C N   1 
ATOM   4358  C CA  . VAL C 1 65  ? -20.094 44.762  -7.209  1.00 31.71 ? 66  VAL C CA  1 
ATOM   4359  C C   . VAL C 1 65  ? -20.280 46.247  -6.898  1.00 31.56 ? 66  VAL C C   1 
ATOM   4360  O O   . VAL C 1 65  ? -21.296 46.847  -7.272  1.00 31.67 ? 66  VAL C O   1 
ATOM   4361  C CB  . VAL C 1 65  ? -20.451 43.866  -5.996  1.00 31.72 ? 66  VAL C CB  1 
ATOM   4362  C CG1 . VAL C 1 65  ? -21.759 44.302  -5.339  1.00 31.51 ? 66  VAL C CG1 1 
ATOM   4363  C CG2 . VAL C 1 65  ? -20.545 42.412  -6.432  1.00 32.05 ? 66  VAL C CG2 1 
ATOM   4364  N N   . ALA C 1 66  ? -19.282 46.833  -6.240  1.00 31.17 ? 67  ALA C N   1 
ATOM   4365  C CA  . ALA C 1 66  ? -19.291 48.254  -5.896  1.00 30.74 ? 67  ALA C CA  1 
ATOM   4366  C C   . ALA C 1 66  ? -19.326 49.141  -7.138  1.00 30.26 ? 67  ALA C C   1 
ATOM   4367  O O   . ALA C 1 66  ? -20.105 50.087  -7.198  1.00 30.22 ? 67  ALA C O   1 
ATOM   4368  C CB  . ALA C 1 66  ? -18.094 48.603  -5.028  1.00 30.72 ? 67  ALA C CB  1 
ATOM   4369  N N   . GLY C 1 67  ? -18.482 48.827  -8.117  1.00 29.93 ? 68  GLY C N   1 
ATOM   4370  C CA  . GLY C 1 67  ? -18.445 49.553  -9.386  1.00 29.44 ? 68  GLY C CA  1 
ATOM   4371  C C   . GLY C 1 67  ? -19.810 49.573  -10.043 1.00 29.38 ? 68  GLY C C   1 
ATOM   4372  O O   . GLY C 1 67  ? -20.273 50.621  -10.497 1.00 29.22 ? 68  GLY C O   1 
ATOM   4373  N N   . TRP C 1 68  ? -20.463 48.412  -10.061 1.00 29.19 ? 69  TRP C N   1 
ATOM   4374  C CA  . TRP C 1 68  ? -21.784 48.256  -10.655 1.00 29.25 ? 69  TRP C CA  1 
ATOM   4375  C C   . TRP C 1 68  ? -22.868 49.029  -9.897  1.00 29.49 ? 69  TRP C C   1 
ATOM   4376  O O   . TRP C 1 68  ? -23.618 49.794  -10.500 1.00 29.68 ? 69  TRP C O   1 
ATOM   4377  C CB  . TRP C 1 68  ? -22.127 46.761  -10.800 1.00 29.08 ? 69  TRP C CB  1 
ATOM   4378  C CG  . TRP C 1 68  ? -23.598 46.417  -10.917 1.00 28.92 ? 69  TRP C CG  1 
ATOM   4379  C CD1 . TRP C 1 68  ? -24.527 47.011  -11.724 1.00 28.57 ? 69  TRP C CD1 1 
ATOM   4380  C CD2 . TRP C 1 68  ? -24.291 45.374  -10.216 1.00 29.02 ? 69  TRP C CD2 1 
ATOM   4381  N NE1 . TRP C 1 68  ? -25.756 46.413  -11.559 1.00 28.38 ? 69  TRP C NE1 1 
ATOM   4382  C CE2 . TRP C 1 68  ? -25.636 45.402  -10.643 1.00 28.81 ? 69  TRP C CE2 1 
ATOM   4383  C CE3 . TRP C 1 68  ? -23.904 44.417  -9.268  1.00 28.97 ? 69  TRP C CE3 1 
ATOM   4384  C CZ2 . TRP C 1 68  ? -26.597 44.514  -10.151 1.00 29.09 ? 69  TRP C CZ2 1 
ATOM   4385  C CZ3 . TRP C 1 68  ? -24.858 43.532  -8.787  1.00 28.70 ? 69  TRP C CZ3 1 
ATOM   4386  C CH2 . TRP C 1 68  ? -26.188 43.590  -9.225  1.00 28.64 ? 69  TRP C CH2 1 
ATOM   4387  N N   . LEU C 1 69  ? -22.941 48.839  -8.585  1.00 29.79 ? 70  LEU C N   1 
ATOM   4388  C CA  . LEU C 1 69  ? -24.010 49.435  -7.784  1.00 30.20 ? 70  LEU C CA  1 
ATOM   4389  C C   . LEU C 1 69  ? -23.929 50.957  -7.671  1.00 30.49 ? 70  LEU C C   1 
ATOM   4390  O O   . LEU C 1 69  ? -24.956 51.631  -7.653  1.00 30.81 ? 70  LEU C O   1 
ATOM   4391  C CB  . LEU C 1 69  ? -24.065 48.797  -6.392  1.00 30.22 ? 70  LEU C CB  1 
ATOM   4392  C CG  . LEU C 1 69  ? -24.584 47.362  -6.317  1.00 30.46 ? 70  LEU C CG  1 
ATOM   4393  C CD1 . LEU C 1 69  ? -24.536 46.853  -4.889  1.00 29.79 ? 70  LEU C CD1 1 
ATOM   4394  C CD2 . LEU C 1 69  ? -26.008 47.258  -6.885  1.00 30.96 ? 70  LEU C CD2 1 
ATOM   4395  N N   . LEU C 1 70  ? -22.712 51.487  -7.603  1.00 30.80 ? 71  LEU C N   1 
ATOM   4396  C CA  . LEU C 1 70  ? -22.488 52.924  -7.478  1.00 31.08 ? 71  LEU C CA  1 
ATOM   4397  C C   . LEU C 1 70  ? -22.531 53.666  -8.817  1.00 31.78 ? 71  LEU C C   1 
ATOM   4398  O O   . LEU C 1 70  ? -22.863 54.856  -8.861  1.00 31.85 ? 71  LEU C O   1 
ATOM   4399  C CB  . LEU C 1 70  ? -21.158 53.188  -6.771  1.00 30.95 ? 71  LEU C CB  1 
ATOM   4400  C CG  . LEU C 1 70  ? -21.114 53.504  -5.264  1.00 30.33 ? 71  LEU C CG  1 
ATOM   4401  C CD1 . LEU C 1 70  ? -22.284 52.948  -4.477  1.00 30.51 ? 71  LEU C CD1 1 
ATOM   4402  C CD2 . LEU C 1 70  ? -19.811 53.021  -4.673  1.00 29.00 ? 71  LEU C CD2 1 
ATOM   4403  N N   . GLY C 1 71  ? -22.183 52.967  -9.897  1.00 32.29 ? 72  GLY C N   1 
ATOM   4404  C CA  . GLY C 1 71  ? -22.236 53.533  -11.235 1.00 32.91 ? 72  GLY C CA  1 
ATOM   4405  C C   . GLY C 1 71  ? -20.913 54.102  -11.697 1.00 33.68 ? 72  GLY C C   1 
ATOM   4406  O O   . GLY C 1 71  ? -20.860 55.202  -12.257 1.00 33.73 ? 72  GLY C O   1 
ATOM   4407  N N   . ASN C 1 72  ? -19.839 53.354  -11.455 1.00 34.37 ? 73  ASN C N   1 
ATOM   4408  C CA  . ASN C 1 72  ? -18.520 53.698  -11.966 1.00 35.15 ? 73  ASN C CA  1 
ATOM   4409  C C   . ASN C 1 72  ? -18.644 53.953  -13.470 1.00 35.81 ? 73  ASN C C   1 
ATOM   4410  O O   . ASN C 1 72  ? -19.154 53.102  -14.198 1.00 35.67 ? 73  ASN C O   1 
ATOM   4411  C CB  . ASN C 1 72  ? -17.535 52.562  -11.661 1.00 35.11 ? 73  ASN C CB  1 
ATOM   4412  C CG  . ASN C 1 72  ? -16.114 52.853  -12.119 1.00 35.45 ? 73  ASN C CG  1 
ATOM   4413  O OD1 . ASN C 1 72  ? -15.879 53.285  -13.249 1.00 36.25 ? 73  ASN C OD1 1 
ATOM   4414  N ND2 . ASN C 1 72  ? -15.150 52.568  -11.249 1.00 35.19 ? 73  ASN C ND2 1 
ATOM   4415  N N   . PRO C 1 73  ? -18.197 55.140  -13.935 1.00 36.60 ? 74  PRO C N   1 
ATOM   4416  C CA  . PRO C 1 73  ? -18.366 55.565  -15.328 1.00 37.03 ? 74  PRO C CA  1 
ATOM   4417  C C   . PRO C 1 73  ? -17.966 54.506  -16.350 1.00 37.44 ? 74  PRO C C   1 
ATOM   4418  O O   . PRO C 1 73  ? -18.402 54.574  -17.491 1.00 37.42 ? 74  PRO C O   1 
ATOM   4419  C CB  . PRO C 1 73  ? -17.425 56.770  -15.443 1.00 37.02 ? 74  PRO C CB  1 
ATOM   4420  C CG  . PRO C 1 73  ? -17.328 57.305  -14.083 1.00 36.77 ? 74  PRO C CG  1 
ATOM   4421  C CD  . PRO C 1 73  ? -17.450 56.142  -13.148 1.00 36.61 ? 74  PRO C CD  1 
ATOM   4422  N N   . MET C 1 74  ? -17.137 53.549  -15.943 1.00 38.10 ? 75  MET C N   1 
ATOM   4423  C CA  . MET C 1 74  ? -16.650 52.505  -16.848 1.00 38.71 ? 75  MET C CA  1 
ATOM   4424  C C   . MET C 1 74  ? -17.543 51.258  -16.861 1.00 38.39 ? 75  MET C C   1 
ATOM   4425  O O   . MET C 1 74  ? -17.259 50.300  -17.584 1.00 38.43 ? 75  MET C O   1 
ATOM   4426  C CB  . MET C 1 74  ? -15.194 52.137  -16.509 1.00 39.25 ? 75  MET C CB  1 
ATOM   4427  C CG  . MET C 1 74  ? -14.165 53.246  -16.819 1.00 41.58 ? 75  MET C CG  1 
ATOM   4428  S SD  . MET C 1 74  ? -14.224 53.850  -18.536 1.00 46.74 ? 75  MET C SD  1 
ATOM   4429  C CE  . MET C 1 74  ? -13.111 52.705  -19.357 1.00 46.44 ? 75  MET C CE  1 
ATOM   4430  N N   . CYS C 1 75  ? -18.625 51.290  -16.082 1.00 38.03 ? 76  CYS C N   1 
ATOM   4431  C CA  . CYS C 1 75  ? -19.520 50.141  -15.914 1.00 37.92 ? 76  CYS C CA  1 
ATOM   4432  C C   . CYS C 1 75  ? -20.946 50.379  -16.444 1.00 37.70 ? 76  CYS C C   1 
ATOM   4433  O O   . CYS C 1 75  ? -21.923 49.917  -15.845 1.00 37.18 ? 76  CYS C O   1 
ATOM   4434  C CB  . CYS C 1 75  ? -19.576 49.734  -14.435 1.00 37.97 ? 76  CYS C CB  1 
ATOM   4435  S SG  . CYS C 1 75  ? -18.002 49.205  -13.731 1.00 38.52 ? 76  CYS C SG  1 
ATOM   4436  N N   . ASP C 1 76  ? -21.059 51.080  -17.572 1.00 37.77 ? 77  ASP C N   1 
ATOM   4437  C CA  . ASP C 1 76  ? -22.371 51.436  -18.135 1.00 38.00 ? 77  ASP C CA  1 
ATOM   4438  C C   . ASP C 1 76  ? -23.087 50.249  -18.764 1.00 37.73 ? 77  ASP C C   1 
ATOM   4439  O O   . ASP C 1 76  ? -24.306 50.266  -18.917 1.00 37.84 ? 77  ASP C O   1 
ATOM   4440  C CB  . ASP C 1 76  ? -22.260 52.578  -19.145 1.00 38.11 ? 77  ASP C CB  1 
ATOM   4441  C CG  . ASP C 1 76  ? -21.199 53.581  -18.765 1.00 39.42 ? 77  ASP C CG  1 
ATOM   4442  O OD1 . ASP C 1 76  ? -20.003 53.197  -18.852 1.00 41.04 ? 77  ASP C OD1 1 
ATOM   4443  O OD2 . ASP C 1 76  ? -21.551 54.727  -18.382 1.00 38.06 ? 77  ASP C OD2 1 
ATOM   4444  N N   . GLU C 1 77  ? -22.323 49.219  -19.114 1.00 37.57 ? 78  GLU C N   1 
ATOM   4445  C CA  . GLU C 1 77  ? -22.883 47.956  -19.574 1.00 37.49 ? 78  GLU C CA  1 
ATOM   4446  C C   . GLU C 1 77  ? -23.917 47.417  -18.580 1.00 37.03 ? 78  GLU C C   1 
ATOM   4447  O O   . GLU C 1 77  ? -24.799 46.646  -18.958 1.00 36.88 ? 78  GLU C O   1 
ATOM   4448  C CB  . GLU C 1 77  ? -21.765 46.929  -19.776 1.00 37.70 ? 78  GLU C CB  1 
ATOM   4449  C CG  . GLU C 1 77  ? -22.168 45.734  -20.627 1.00 39.21 ? 78  GLU C CG  1 
ATOM   4450  C CD  . GLU C 1 77  ? -21.279 44.519  -20.409 1.00 41.51 ? 78  GLU C CD  1 
ATOM   4451  O OE1 . GLU C 1 77  ? -20.049 44.690  -20.241 1.00 42.51 ? 78  GLU C OE1 1 
ATOM   4452  O OE2 . GLU C 1 77  ? -21.815 43.386  -20.418 1.00 42.23 ? 78  GLU C OE2 1 
ATOM   4453  N N   . PHE C 1 78  ? -23.809 47.847  -17.320 1.00 36.43 ? 79  PHE C N   1 
ATOM   4454  C CA  . PHE C 1 78  ? -24.639 47.323  -16.237 1.00 35.87 ? 79  PHE C CA  1 
ATOM   4455  C C   . PHE C 1 78  ? -25.589 48.339  -15.600 1.00 35.87 ? 79  PHE C C   1 
ATOM   4456  O O   . PHE C 1 78  ? -26.172 48.066  -14.548 1.00 35.61 ? 79  PHE C O   1 
ATOM   4457  C CB  . PHE C 1 78  ? -23.761 46.666  -15.158 1.00 35.61 ? 79  PHE C CB  1 
ATOM   4458  C CG  . PHE C 1 78  ? -22.785 45.659  -15.697 1.00 34.52 ? 79  PHE C CG  1 
ATOM   4459  C CD1 . PHE C 1 78  ? -23.227 44.432  -16.182 1.00 33.39 ? 79  PHE C CD1 1 
ATOM   4460  C CD2 . PHE C 1 78  ? -21.423 45.938  -15.716 1.00 33.83 ? 79  PHE C CD2 1 
ATOM   4461  C CE1 . PHE C 1 78  ? -22.327 43.500  -16.675 1.00 33.53 ? 79  PHE C CE1 1 
ATOM   4462  C CE2 . PHE C 1 78  ? -20.509 45.011  -16.211 1.00 33.47 ? 79  PHE C CE2 1 
ATOM   4463  C CZ  . PHE C 1 78  ? -20.962 43.793  -16.698 1.00 33.53 ? 79  PHE C CZ  1 
ATOM   4464  N N   . ILE C 1 79  ? -25.759 49.496  -16.243 1.00 36.15 ? 80  ILE C N   1 
ATOM   4465  C CA  . ILE C 1 79  ? -26.723 50.514  -15.786 1.00 36.44 ? 80  ILE C CA  1 
ATOM   4466  C C   . ILE C 1 79  ? -28.152 49.959  -15.702 1.00 36.43 ? 80  ILE C C   1 
ATOM   4467  O O   . ILE C 1 79  ? -28.931 50.354  -14.835 1.00 36.25 ? 80  ILE C O   1 
ATOM   4468  C CB  . ILE C 1 79  ? -26.651 51.811  -16.647 1.00 36.62 ? 80  ILE C CB  1 
ATOM   4469  C CG1 . ILE C 1 79  ? -25.996 52.946  -15.861 1.00 37.09 ? 80  ILE C CG1 1 
ATOM   4470  C CG2 . ILE C 1 79  ? -28.017 52.304  -17.044 1.00 37.16 ? 80  ILE C CG2 1 
ATOM   4471  C CD1 . ILE C 1 79  ? -24.544 53.154  -16.174 1.00 38.24 ? 80  ILE C CD1 1 
ATOM   4472  N N   . ASN C 1 80  ? -28.475 49.035  -16.604 1.00 36.59 ? 81  ASN C N   1 
ATOM   4473  C CA  . ASN C 1 80  ? -29.756 48.345  -16.597 1.00 36.83 ? 81  ASN C CA  1 
ATOM   4474  C C   . ASN C 1 80  ? -29.545 46.863  -16.840 1.00 36.55 ? 81  ASN C C   1 
ATOM   4475  O O   . ASN C 1 80  ? -29.091 46.455  -17.911 1.00 36.92 ? 81  ASN C O   1 
ATOM   4476  C CB  . ASN C 1 80  ? -30.691 48.924  -17.656 1.00 37.08 ? 81  ASN C CB  1 
ATOM   4477  C CG  . ASN C 1 80  ? -31.240 50.273  -17.263 1.00 38.14 ? 81  ASN C CG  1 
ATOM   4478  O OD1 . ASN C 1 80  ? -31.959 50.399  -16.263 1.00 39.13 ? 81  ASN C OD1 1 
ATOM   4479  N ND2 . ASN C 1 80  ? -30.915 51.296  -18.052 1.00 38.63 ? 81  ASN C ND2 1 
ATOM   4480  N N   . VAL C 1 81  ? -29.893 46.065  -15.839 1.00 35.89 ? 82  VAL C N   1 
ATOM   4481  C CA  . VAL C 1 81  ? -29.537 44.660  -15.807 1.00 35.15 ? 82  VAL C CA  1 
ATOM   4482  C C   . VAL C 1 81  ? -30.795 43.797  -15.650 1.00 34.67 ? 82  VAL C C   1 
ATOM   4483  O O   . VAL C 1 81  ? -31.662 44.116  -14.835 1.00 34.67 ? 82  VAL C O   1 
ATOM   4484  C CB  . VAL C 1 81  ? -28.461 44.428  -14.698 1.00 35.16 ? 82  VAL C CB  1 
ATOM   4485  C CG1 . VAL C 1 81  ? -28.729 43.191  -13.856 1.00 35.10 ? 82  VAL C CG1 1 
ATOM   4486  C CG2 . VAL C 1 81  ? -27.072 44.396  -15.316 1.00 35.02 ? 82  VAL C CG2 1 
ATOM   4487  N N   . PRO C 1 82  A -30.918 42.727  -16.462 1.00 34.10 ? 82  PRO C N   1 
ATOM   4488  C CA  . PRO C 1 82  A -32.075 41.836  -16.348 1.00 33.83 ? 82  PRO C CA  1 
ATOM   4489  C C   . PRO C 1 82  A -31.913 40.820  -15.220 1.00 33.74 ? 82  PRO C C   1 
ATOM   4490  O O   . PRO C 1 82  A -30.850 40.748  -14.599 1.00 33.86 ? 82  PRO C O   1 
ATOM   4491  C CB  . PRO C 1 82  A -32.103 41.123  -17.703 1.00 33.79 ? 82  PRO C CB  1 
ATOM   4492  C CG  . PRO C 1 82  A -30.680 41.122  -18.164 1.00 33.83 ? 82  PRO C CG  1 
ATOM   4493  C CD  . PRO C 1 82  A -30.046 42.367  -17.597 1.00 34.13 ? 82  PRO C CD  1 
ATOM   4494  N N   . GLU C 1 83  ? -32.965 40.045  -14.968 1.00 33.51 ? 83  GLU C N   1 
ATOM   4495  C CA  . GLU C 1 83  ? -32.946 38.981  -13.968 1.00 33.17 ? 83  GLU C CA  1 
ATOM   4496  C C   . GLU C 1 83  ? -31.757 38.047  -14.193 1.00 32.65 ? 83  GLU C C   1 
ATOM   4497  O O   . GLU C 1 83  ? -31.450 37.675  -15.331 1.00 32.47 ? 83  GLU C O   1 
ATOM   4498  C CB  . GLU C 1 83  ? -34.262 38.195  -13.999 1.00 33.30 ? 83  GLU C CB  1 
ATOM   4499  C CG  . GLU C 1 83  ? -34.408 37.161  -12.884 1.00 34.66 ? 83  GLU C CG  1 
ATOM   4500  C CD  . GLU C 1 83  ? -35.784 36.498  -12.842 1.00 36.91 ? 83  GLU C CD  1 
ATOM   4501  O OE1 . GLU C 1 83  ? -36.763 37.097  -13.347 1.00 38.12 ? 83  GLU C OE1 1 
ATOM   4502  O OE2 . GLU C 1 83  ? -35.888 35.377  -12.290 1.00 36.91 ? 83  GLU C OE2 1 
ATOM   4503  N N   . TRP C 1 84  ? -31.086 37.689  -13.099 1.00 31.97 ? 84  TRP C N   1 
ATOM   4504  C CA  . TRP C 1 84  ? -29.931 36.802  -13.155 1.00 31.09 ? 84  TRP C CA  1 
ATOM   4505  C C   . TRP C 1 84  ? -30.171 35.539  -12.345 1.00 31.00 ? 84  TRP C C   1 
ATOM   4506  O O   . TRP C 1 84  ? -31.055 35.499  -11.485 1.00 31.13 ? 84  TRP C O   1 
ATOM   4507  C CB  . TRP C 1 84  ? -28.671 37.520  -12.660 1.00 30.88 ? 84  TRP C CB  1 
ATOM   4508  C CG  . TRP C 1 84  ? -28.721 37.920  -11.215 1.00 30.15 ? 84  TRP C CG  1 
ATOM   4509  C CD1 . TRP C 1 84  ? -28.500 37.114  -10.130 1.00 29.66 ? 84  TRP C CD1 1 
ATOM   4510  C CD2 . TRP C 1 84  ? -29.006 39.223  -10.693 1.00 29.06 ? 84  TRP C CD2 1 
ATOM   4511  N NE1 . TRP C 1 84  ? -28.635 37.833  -8.971  1.00 29.63 ? 84  TRP C NE1 1 
ATOM   4512  C CE2 . TRP C 1 84  ? -28.939 39.132  -9.285  1.00 29.02 ? 84  TRP C CE2 1 
ATOM   4513  C CE3 . TRP C 1 84  ? -29.305 40.460  -11.276 1.00 28.12 ? 84  TRP C CE3 1 
ATOM   4514  C CZ2 . TRP C 1 84  ? -29.163 40.229  -8.452  1.00 27.76 ? 84  TRP C CZ2 1 
ATOM   4515  C CZ3 . TRP C 1 84  ? -29.523 41.548  -10.448 1.00 27.48 ? 84  TRP C CZ3 1 
ATOM   4516  C CH2 . TRP C 1 84  ? -29.455 41.423  -9.050  1.00 27.28 ? 84  TRP C CH2 1 
ATOM   4517  N N   . SER C 1 85  ? -29.383 34.509  -12.635 1.00 30.87 ? 85  SER C N   1 
ATOM   4518  C CA  . SER C 1 85  ? -29.390 33.275  -11.861 1.00 30.77 ? 85  SER C CA  1 
ATOM   4519  C C   . SER C 1 85  ? -28.370 33.400  -10.739 1.00 30.88 ? 85  SER C C   1 
ATOM   4520  O O   . SER C 1 85  ? -28.701 33.225  -9.569  1.00 30.91 ? 85  SER C O   1 
ATOM   4521  C CB  . SER C 1 85  ? -29.069 32.070  -12.752 1.00 30.80 ? 85  SER C CB  1 
ATOM   4522  O OG  . SER C 1 85  ? -27.893 32.292  -13.518 1.00 30.36 ? 85  SER C OG  1 
ATOM   4523  N N   . TYR C 1 86  ? -27.130 33.711  -11.111 1.00 30.95 ? 86  TYR C N   1 
ATOM   4524  C CA  . TYR C 1 86  ? -26.055 33.934  -10.159 1.00 30.99 ? 86  TYR C CA  1 
ATOM   4525  C C   . TYR C 1 86  ? -25.155 35.047  -10.678 1.00 31.43 ? 86  TYR C C   1 
ATOM   4526  O O   . TYR C 1 86  ? -25.241 35.422  -11.848 1.00 31.78 ? 86  TYR C O   1 
ATOM   4527  C CB  . TYR C 1 86  ? -25.267 32.642  -9.902  1.00 30.78 ? 86  TYR C CB  1 
ATOM   4528  C CG  . TYR C 1 86  ? -24.615 32.037  -11.125 1.00 30.01 ? 86  TYR C CG  1 
ATOM   4529  C CD1 . TYR C 1 86  ? -23.277 32.285  -11.416 1.00 28.96 ? 86  TYR C CD1 1 
ATOM   4530  C CD2 . TYR C 1 86  ? -25.332 31.202  -11.987 1.00 29.09 ? 86  TYR C CD2 1 
ATOM   4531  C CE1 . TYR C 1 86  ? -22.677 31.736  -12.541 1.00 28.24 ? 86  TYR C CE1 1 
ATOM   4532  C CE2 . TYR C 1 86  ? -24.736 30.649  -13.116 1.00 27.83 ? 86  TYR C CE2 1 
ATOM   4533  C CZ  . TYR C 1 86  ? -23.408 30.919  -13.383 1.00 27.73 ? 86  TYR C CZ  1 
ATOM   4534  O OH  . TYR C 1 86  ? -22.798 30.377  -14.491 1.00 27.24 ? 86  TYR C OH  1 
ATOM   4535  N N   . ILE C 1 87  ? -24.300 35.576  -9.807  1.00 31.59 ? 87  ILE C N   1 
ATOM   4536  C CA  . ILE C 1 87  ? -23.417 36.680  -10.154 1.00 31.85 ? 87  ILE C CA  1 
ATOM   4537  C C   . ILE C 1 87  ? -21.962 36.201  -10.217 1.00 32.10 ? 87  ILE C C   1 
ATOM   4538  O O   . ILE C 1 87  ? -21.523 35.425  -9.368  1.00 32.05 ? 87  ILE C O   1 
ATOM   4539  C CB  . ILE C 1 87  ? -23.575 37.846  -9.142  1.00 31.99 ? 87  ILE C CB  1 
ATOM   4540  C CG1 . ILE C 1 87  ? -25.046 38.273  -9.061  1.00 32.56 ? 87  ILE C CG1 1 
ATOM   4541  C CG2 . ILE C 1 87  ? -22.688 39.042  -9.523  1.00 31.72 ? 87  ILE C CG2 1 
ATOM   4542  C CD1 . ILE C 1 87  ? -25.374 39.261  -7.955  1.00 33.14 ? 87  ILE C CD1 1 
ATOM   4543  N N   . VAL C 1 88  ? -21.227 36.655  -11.232 1.00 32.29 ? 88  VAL C N   1 
ATOM   4544  C CA  . VAL C 1 88  ? -19.821 36.287  -11.395 1.00 32.58 ? 88  VAL C CA  1 
ATOM   4545  C C   . VAL C 1 88  ? -18.923 37.524  -11.320 1.00 33.04 ? 88  VAL C C   1 
ATOM   4546  O O   . VAL C 1 88  ? -19.005 38.413  -12.172 1.00 33.03 ? 88  VAL C O   1 
ATOM   4547  C CB  . VAL C 1 88  ? -19.559 35.523  -12.725 1.00 32.48 ? 88  VAL C CB  1 
ATOM   4548  C CG1 . VAL C 1 88  ? -18.090 35.170  -12.860 1.00 32.04 ? 88  VAL C CG1 1 
ATOM   4549  C CG2 . VAL C 1 88  ? -20.400 34.262  -12.801 1.00 32.15 ? 88  VAL C CG2 1 
ATOM   4550  N N   . GLU C 1 89  ? -18.073 37.563  -10.294 1.00 33.47 ? 89  GLU C N   1 
ATOM   4551  C CA  . GLU C 1 89  ? -17.126 38.654  -10.092 1.00 34.12 ? 89  GLU C CA  1 
ATOM   4552  C C   . GLU C 1 89  ? -15.705 38.109  -10.095 1.00 34.65 ? 89  GLU C C   1 
ATOM   4553  O O   . GLU C 1 89  ? -15.427 37.073  -9.480  1.00 34.75 ? 89  GLU C O   1 
ATOM   4554  C CB  . GLU C 1 89  ? -17.414 39.374  -8.769  1.00 34.05 ? 89  GLU C CB  1 
ATOM   4555  C CG  . GLU C 1 89  ? -16.511 40.583  -8.465  1.00 34.67 ? 89  GLU C CG  1 
ATOM   4556  C CD  . GLU C 1 89  ? -16.668 41.106  -7.036  1.00 35.55 ? 89  GLU C CD  1 
ATOM   4557  O OE1 . GLU C 1 89  ? -16.417 40.341  -6.071  1.00 36.54 ? 89  GLU C OE1 1 
ATOM   4558  O OE2 . GLU C 1 89  ? -17.033 42.290  -6.874  1.00 34.73 ? 89  GLU C OE2 1 
ATOM   4559  N N   . LYS C 1 90  ? -14.805 38.808  -10.788 1.00 35.36 ? 90  LYS C N   1 
ATOM   4560  C CA  . LYS C 1 90  ? -13.384 38.449  -10.787 1.00 35.96 ? 90  LYS C CA  1 
ATOM   4561  C C   . LYS C 1 90  ? -12.761 38.613  -9.406  1.00 36.17 ? 90  LYS C C   1 
ATOM   4562  O O   . LYS C 1 90  ? -13.313 39.305  -8.549  1.00 36.30 ? 90  LYS C O   1 
ATOM   4563  C CB  . LYS C 1 90  ? -12.616 39.269  -11.821 1.00 36.00 ? 90  LYS C CB  1 
ATOM   4564  C CG  . LYS C 1 90  ? -12.669 38.684  -13.220 1.00 36.65 ? 90  LYS C CG  1 
ATOM   4565  C CD  . LYS C 1 90  ? -12.067 39.644  -14.240 1.00 37.53 ? 90  LYS C CD  1 
ATOM   4566  C CE  . LYS C 1 90  ? -11.982 39.023  -15.629 1.00 38.14 ? 90  LYS C CE  1 
ATOM   4567  N NZ  . LYS C 1 90  ? -13.252 38.370  -16.047 1.00 38.84 ? 90  LYS C NZ  1 
ATOM   4568  N N   . ALA C 1 91  ? -11.623 37.958  -9.195  1.00 36.75 ? 91  ALA C N   1 
ATOM   4569  C CA  . ALA C 1 91  ? -10.867 38.076  -7.946  1.00 37.28 ? 91  ALA C CA  1 
ATOM   4570  C C   . ALA C 1 91  ? -10.447 39.525  -7.674  1.00 37.64 ? 91  ALA C C   1 
ATOM   4571  O O   . ALA C 1 91  ? -10.635 40.027  -6.564  1.00 37.81 ? 91  ALA C O   1 
ATOM   4572  C CB  . ALA C 1 91  ? -9.651  37.149  -7.958  1.00 37.21 ? 91  ALA C CB  1 
ATOM   4573  N N   . SER C 1 92  ? -9.898  40.197  -8.686  1.00 38.00 ? 92  SER C N   1 
ATOM   4574  C CA  . SER C 1 92  ? -9.534  41.612  -8.549  1.00 38.71 ? 92  SER C CA  1 
ATOM   4575  C C   . SER C 1 92  ? -9.934  42.458  -9.765  1.00 38.65 ? 92  SER C C   1 
ATOM   4576  O O   . SER C 1 92  ? -9.124  42.675  -10.665 1.00 39.01 ? 92  SER C O   1 
ATOM   4577  C CB  . SER C 1 92  ? -8.042  41.761  -8.241  1.00 38.75 ? 92  SER C CB  1 
ATOM   4578  O OG  . SER C 1 92  ? -7.726  41.117  -7.018  1.00 39.73 ? 92  SER C OG  1 
ATOM   4579  N N   . PRO C 1 93  ? -11.190 42.942  -9.789  1.00 38.57 ? 93  PRO C N   1 
ATOM   4580  C CA  . PRO C 1 93  ? -11.675 43.735  -10.917 1.00 38.60 ? 93  PRO C CA  1 
ATOM   4581  C C   . PRO C 1 93  ? -10.990 45.095  -10.966 1.00 38.62 ? 93  PRO C C   1 
ATOM   4582  O O   . PRO C 1 93  ? -10.619 45.634  -9.920  1.00 38.74 ? 93  PRO C O   1 
ATOM   4583  C CB  . PRO C 1 93  ? -13.174 43.910  -10.617 1.00 38.53 ? 93  PRO C CB  1 
ATOM   4584  C CG  . PRO C 1 93  ? -13.475 42.988  -9.479  1.00 38.55 ? 93  PRO C CG  1 
ATOM   4585  C CD  . PRO C 1 93  ? -12.203 42.834  -8.725  1.00 38.43 ? 93  PRO C CD  1 
ATOM   4586  N N   . ALA C 1 94  ? -10.816 45.631  -12.173 1.00 38.56 ? 94  ALA C N   1 
ATOM   4587  C CA  . ALA C 1 94  ? -10.178 46.936  -12.371 1.00 38.48 ? 94  ALA C CA  1 
ATOM   4588  C C   . ALA C 1 94  ? -11.112 48.082  -11.996 1.00 38.51 ? 94  ALA C C   1 
ATOM   4589  O O   . ALA C 1 94  ? -10.685 49.097  -11.445 1.00 38.57 ? 94  ALA C O   1 
ATOM   4590  C CB  . ALA C 1 94  ? -9.722  47.086  -13.814 1.00 38.46 ? 94  ALA C CB  1 
ATOM   4591  N N   . ASN C 1 95  ? -12.393 47.909  -12.294 1.00 38.59 ? 95  ASN C N   1 
ATOM   4592  C CA  . ASN C 1 95  ? -13.364 48.975  -12.136 1.00 38.47 ? 95  ASN C CA  1 
ATOM   4593  C C   . ASN C 1 95  ? -14.154 48.843  -10.845 1.00 38.55 ? 95  ASN C C   1 
ATOM   4594  O O   . ASN C 1 95  ? -15.226 48.237  -10.808 1.00 38.70 ? 95  ASN C O   1 
ATOM   4595  C CB  . ASN C 1 95  ? -14.254 49.043  -13.370 1.00 38.37 ? 95  ASN C CB  1 
ATOM   4596  C CG  . ASN C 1 95  ? -13.454 49.291  -14.635 1.00 38.66 ? 95  ASN C CG  1 
ATOM   4597  O OD1 . ASN C 1 95  ? -12.670 50.241  -14.712 1.00 38.34 ? 95  ASN C OD1 1 
ATOM   4598  N ND2 . ASN C 1 95  ? -13.637 48.431  -15.631 1.00 39.43 ? 95  ASN C ND2 1 
ATOM   4599  N N   . ASP C 1 96  ? -13.567 49.349  -9.673  1.00 38.30 ? 96  ASP C N   1 
ATOM   4600  C CA  . ASP C 1 96  ? -14.190 49.328  -8.355  1.00 38.30 ? 96  ASP C CA  1 
ATOM   4601  C C   . ASP C 1 96  ? -14.683 50.583  -7.647  1.00 38.29 ? 96  ASP C C   1 
ATOM   4602  O O   . ASP C 1 96  ? -15.879 50.876  -7.646  1.00 38.32 ? 96  ASP C O   1 
ATOM   4603  C CB  . ASP C 1 96  ? -13.255 48.689  -7.328  1.00 38.35 ? 96  ASP C CB  1 
ATOM   4604  C CG  . ASP C 1 96  ? -13.945 48.408  -6.007  1.00 38.94 ? 96  ASP C CG  1 
ATOM   4605  O OD1 . ASP C 1 96  ? -15.084 47.896  -6.027  1.00 38.78 ? 96  ASP C OD1 1 
ATOM   4606  O OD2 . ASP C 1 96  ? -13.348 48.699  -4.950  1.00 39.83 ? 96  ASP C OD2 1 
ATOM   4607  N N   . LEU C 1 97  A -13.833 51.244  -6.914  1.00 38.48 ? 96  LEU C N   1 
ATOM   4608  C CA  . LEU C 1 97  A -14.078 52.594  -6.426  1.00 38.55 ? 96  LEU C CA  1 
ATOM   4609  C C   . LEU C 1 97  A -13.131 53.521  -7.185  1.00 38.60 ? 96  LEU C C   1 
ATOM   4610  O O   . LEU C 1 97  A -11.974 53.698  -6.788  1.00 38.83 ? 96  LEU C O   1 
ATOM   4611  C CB  . LEU C 1 97  A -13.851 52.698  -4.915  1.00 38.58 ? 96  LEU C CB  1 
ATOM   4612  C CG  . LEU C 1 97  A -15.020 52.685  -3.911  1.00 38.98 ? 96  LEU C CG  1 
ATOM   4613  C CD1 . LEU C 1 97  A -16.208 51.837  -4.334  1.00 38.25 ? 96  LEU C CD1 1 
ATOM   4614  C CD2 . LEU C 1 97  A -14.524 52.254  -2.533  1.00 38.62 ? 96  LEU C CD2 1 
ATOM   4615  N N   . CYS C 1 98  ? -13.628 54.126  -8.261  1.00 38.46 ? 97  CYS C N   1 
ATOM   4616  C CA  . CYS C 1 98  ? -12.792 55.011  -9.083  1.00 38.40 ? 97  CYS C CA  1 
ATOM   4617  C C   . CYS C 1 98  ? -12.243 56.175  -8.251  1.00 37.61 ? 97  CYS C C   1 
ATOM   4618  O O   . CYS C 1 98  ? -11.033 56.410  -8.237  1.00 37.84 ? 97  CYS C O   1 
ATOM   4619  C CB  . CYS C 1 98  ? -13.509 55.478  -10.368 1.00 38.64 ? 97  CYS C CB  1 
ATOM   4620  S SG  . CYS C 1 98  ? -15.120 56.295  -10.170 1.00 40.71 ? 97  CYS C SG  1 
ATOM   4621  N N   . TYR C 1 99  ? -13.118 56.879  -7.541  1.00 36.58 ? 98  TYR C N   1 
ATOM   4622  C CA  . TYR C 1 99  ? -12.655 57.798  -6.504  1.00 35.98 ? 98  TYR C CA  1 
ATOM   4623  C C   . TYR C 1 99  ? -12.376 56.988  -5.231  1.00 35.46 ? 98  TYR C C   1 
ATOM   4624  O O   . TYR C 1 99  ? -13.258 56.281  -4.738  1.00 35.51 ? 98  TYR C O   1 
ATOM   4625  C CB  . TYR C 1 99  ? -13.671 58.910  -6.249  1.00 35.69 ? 98  TYR C CB  1 
ATOM   4626  C CG  . TYR C 1 99  ? -13.118 60.104  -5.494  1.00 35.32 ? 98  TYR C CG  1 
ATOM   4627  C CD1 . TYR C 1 99  ? -12.730 61.263  -6.168  1.00 34.53 ? 98  TYR C CD1 1 
ATOM   4628  C CD2 . TYR C 1 99  ? -12.995 60.079  -4.104  1.00 35.12 ? 98  TYR C CD2 1 
ATOM   4629  C CE1 . TYR C 1 99  ? -12.232 62.364  -5.477  1.00 34.20 ? 98  TYR C CE1 1 
ATOM   4630  C CE2 . TYR C 1 99  ? -12.497 61.168  -3.405  1.00 34.40 ? 98  TYR C CE2 1 
ATOM   4631  C CZ  . TYR C 1 99  ? -12.118 62.307  -4.095  1.00 34.49 ? 98  TYR C CZ  1 
ATOM   4632  O OH  . TYR C 1 99  ? -11.640 63.386  -3.395  1.00 33.51 ? 98  TYR C OH  1 
ATOM   4633  N N   . PRO C 1 100 ? -11.145 57.082  -4.698  1.00 35.13 ? 99  PRO C N   1 
ATOM   4634  C CA  . PRO C 1 100 ? -10.713 56.176  -3.628  1.00 34.82 ? 99  PRO C CA  1 
ATOM   4635  C C   . PRO C 1 100 ? -11.500 56.361  -2.339  1.00 34.42 ? 99  PRO C C   1 
ATOM   4636  O O   . PRO C 1 100 ? -12.012 57.451  -2.075  1.00 34.34 ? 99  PRO C O   1 
ATOM   4637  C CB  . PRO C 1 100 ? -9.243  56.553  -3.421  1.00 34.90 ? 99  PRO C CB  1 
ATOM   4638  C CG  . PRO C 1 100 ? -9.160  57.973  -3.854  1.00 34.92 ? 99  PRO C CG  1 
ATOM   4639  C CD  . PRO C 1 100 ? -10.119 58.097  -5.003  1.00 35.09 ? 99  PRO C CD  1 
ATOM   4640  N N   . GLY C 1 101 ? -11.595 55.291  -1.556  1.00 34.14 ? 100 GLY C N   1 
ATOM   4641  C CA  . GLY C 1 101 ? -12.330 55.307  -0.299  1.00 34.01 ? 100 GLY C CA  1 
ATOM   4642  C C   . GLY C 1 101 ? -12.837 53.934  0.096   1.00 34.13 ? 100 GLY C C   1 
ATOM   4643  O O   . GLY C 1 101 ? -12.191 52.924  -0.190  1.00 33.93 ? 100 GLY C O   1 
ATOM   4644  N N   . ASP C 1 102 ? -14.006 53.901  0.739   1.00 34.23 ? 101 ASP C N   1 
ATOM   4645  C CA  . ASP C 1 102 ? -14.569 52.671  1.299   1.00 34.38 ? 101 ASP C CA  1 
ATOM   4646  C C   . ASP C 1 102 ? -16.063 52.527  1.070   1.00 34.05 ? 101 ASP C C   1 
ATOM   4647  O O   . ASP C 1 102 ? -16.793 53.520  0.996   1.00 34.10 ? 101 ASP C O   1 
ATOM   4648  C CB  . ASP C 1 102 ? -14.314 52.603  2.804   1.00 34.78 ? 101 ASP C CB  1 
ATOM   4649  C CG  . ASP C 1 102 ? -12.856 52.418  3.136   1.00 36.44 ? 101 ASP C CG  1 
ATOM   4650  O OD1 . ASP C 1 102 ? -12.405 51.250  3.197   1.00 37.22 ? 101 ASP C OD1 1 
ATOM   4651  O OD2 . ASP C 1 102 ? -12.168 53.448  3.337   1.00 38.51 ? 101 ASP C OD2 1 
ATOM   4652  N N   . PHE C 1 103 ? -16.501 51.273  0.980   1.00 33.47 ? 102 PHE C N   1 
ATOM   4653  C CA  . PHE C 1 103 ? -17.908 50.932  0.975   1.00 33.04 ? 102 PHE C CA  1 
ATOM   4654  C C   . PHE C 1 103 ? -18.250 50.346  2.340   1.00 32.86 ? 102 PHE C C   1 
ATOM   4655  O O   . PHE C 1 103 ? -17.840 49.235  2.655   1.00 33.06 ? 102 PHE C O   1 
ATOM   4656  C CB  . PHE C 1 103 ? -18.191 49.901  -0.119  1.00 33.00 ? 102 PHE C CB  1 
ATOM   4657  C CG  . PHE C 1 103 ? -19.566 49.996  -0.703  1.00 32.79 ? 102 PHE C CG  1 
ATOM   4658  C CD1 . PHE C 1 103 ? -19.738 50.038  -2.078  1.00 32.53 ? 102 PHE C CD1 1 
ATOM   4659  C CD2 . PHE C 1 103 ? -20.693 50.051  0.116   1.00 33.12 ? 102 PHE C CD2 1 
ATOM   4660  C CE1 . PHE C 1 103 ? -21.006 50.124  -2.634  1.00 32.35 ? 102 PHE C CE1 1 
ATOM   4661  C CE2 . PHE C 1 103 ? -21.968 50.153  -0.430  1.00 33.35 ? 102 PHE C CE2 1 
ATOM   4662  C CZ  . PHE C 1 103 ? -22.124 50.187  -1.810  1.00 32.85 ? 102 PHE C CZ  1 
ATOM   4663  N N   . ASN C 1 104 ? -18.988 51.095  3.153   1.00 32.61 ? 103 ASN C N   1 
ATOM   4664  C CA  . ASN C 1 104 ? -19.369 50.636  4.488   1.00 32.38 ? 103 ASN C CA  1 
ATOM   4665  C C   . ASN C 1 104 ? -20.302 49.434  4.403   1.00 32.36 ? 103 ASN C C   1 
ATOM   4666  O O   . ASN C 1 104 ? -21.229 49.427  3.588   1.00 32.66 ? 103 ASN C O   1 
ATOM   4667  C CB  . ASN C 1 104 ? -20.043 51.764  5.262   1.00 32.32 ? 103 ASN C CB  1 
ATOM   4668  C CG  . ASN C 1 104 ? -20.205 51.453  6.732   1.00 32.36 ? 103 ASN C CG  1 
ATOM   4669  O OD1 . ASN C 1 104 ? -19.226 51.433  7.480   1.00 33.25 ? 103 ASN C OD1 1 
ATOM   4670  N ND2 . ASN C 1 104 ? -21.449 51.241  7.167   1.00 31.18 ? 103 ASN C ND2 1 
ATOM   4671  N N   . ASN C 1 105 ? -20.054 48.425  5.239   1.00 32.04 ? 104 ASN C N   1 
ATOM   4672  C CA  . ASN C 1 105 ? -20.833 47.176  5.233   1.00 31.57 ? 104 ASN C CA  1 
ATOM   4673  C C   . ASN C 1 105 ? -20.882 46.483  3.871   1.00 30.89 ? 104 ASN C C   1 
ATOM   4674  O O   . ASN C 1 105 ? -21.921 45.949  3.474   1.00 30.70 ? 104 ASN C O   1 
ATOM   4675  C CB  . ASN C 1 105 ? -22.259 47.412  5.743   1.00 31.86 ? 104 ASN C CB  1 
ATOM   4676  C CG  . ASN C 1 105 ? -22.376 47.256  7.235   1.00 32.70 ? 104 ASN C CG  1 
ATOM   4677  O OD1 . ASN C 1 105 ? -21.767 47.998  7.999   1.00 33.36 ? 104 ASN C OD1 1 
ATOM   4678  N ND2 . ASN C 1 105 ? -23.173 46.287  7.662   1.00 34.78 ? 104 ASN C ND2 1 
ATOM   4679  N N   . TYR C 1 106 ? -19.753 46.488  3.169   1.00 30.07 ? 105 TYR C N   1 
ATOM   4680  C CA  . TYR C 1 106 ? -19.672 45.921  1.824   1.00 29.27 ? 105 TYR C CA  1 
ATOM   4681  C C   . TYR C 1 106 ? -19.949 44.417  1.800   1.00 29.32 ? 105 TYR C C   1 
ATOM   4682  O O   . TYR C 1 106 ? -20.715 43.939  0.959   1.00 29.22 ? 105 TYR C O   1 
ATOM   4683  C CB  . TYR C 1 106 ? -18.306 46.230  1.214   1.00 28.77 ? 105 TYR C CB  1 
ATOM   4684  C CG  . TYR C 1 106 ? -18.161 45.897  -0.255  1.00 28.42 ? 105 TYR C CG  1 
ATOM   4685  C CD1 . TYR C 1 106 ? -19.078 46.373  -1.204  1.00 27.54 ? 105 TYR C CD1 1 
ATOM   4686  C CD2 . TYR C 1 106 ? -17.084 45.136  -0.705  1.00 27.13 ? 105 TYR C CD2 1 
ATOM   4687  C CE1 . TYR C 1 106 ? -18.929 46.079  -2.558  1.00 26.45 ? 105 TYR C CE1 1 
ATOM   4688  C CE2 . TYR C 1 106 ? -16.925 44.843  -2.049  1.00 26.79 ? 105 TYR C CE2 1 
ATOM   4689  C CZ  . TYR C 1 106 ? -17.847 45.316  -2.971  1.00 26.80 ? 105 TYR C CZ  1 
ATOM   4690  O OH  . TYR C 1 106 ? -17.678 45.015  -4.301  1.00 26.58 ? 105 TYR C OH  1 
ATOM   4691  N N   . GLU C 1 107 ? -19.341 43.681  2.734   1.00 28.97 ? 106 GLU C N   1 
ATOM   4692  C CA  . GLU C 1 107 ? -19.462 42.221  2.774   1.00 28.85 ? 106 GLU C CA  1 
ATOM   4693  C C   . GLU C 1 107 ? -20.891 41.823  3.127   1.00 28.62 ? 106 GLU C C   1 
ATOM   4694  O O   . GLU C 1 107 ? -21.440 40.854  2.601   1.00 28.30 ? 106 GLU C O   1 
ATOM   4695  C CB  . GLU C 1 107 ? -18.455 41.603  3.764   1.00 28.76 ? 106 GLU C CB  1 
ATOM   4696  C CG  . GLU C 1 107 ? -16.974 41.819  3.403   1.00 28.82 ? 106 GLU C CG  1 
ATOM   4697  C CD  . GLU C 1 107 ? -16.513 43.272  3.552   1.00 29.05 ? 106 GLU C CD  1 
ATOM   4698  O OE1 . GLU C 1 107 ? -17.031 43.987  4.437   1.00 29.08 ? 106 GLU C OE1 1 
ATOM   4699  O OE2 . GLU C 1 107 ? -15.632 43.699  2.780   1.00 29.39 ? 106 GLU C OE2 1 
ATOM   4700  N N   . GLU C 1 108 ? -21.483 42.601  4.018   1.00 28.77 ? 107 GLU C N   1 
ATOM   4701  C CA  . GLU C 1 108 ? -22.871 42.441  4.403   1.00 29.04 ? 107 GLU C CA  1 
ATOM   4702  C C   . GLU C 1 108 ? -23.811 42.748  3.226   1.00 29.26 ? 107 GLU C C   1 
ATOM   4703  O O   . GLU C 1 108 ? -24.903 42.175  3.128   1.00 29.63 ? 107 GLU C O   1 
ATOM   4704  C CB  . GLU C 1 108 ? -23.151 43.346  5.605   1.00 28.95 ? 107 GLU C CB  1 
ATOM   4705  C CG  . GLU C 1 108 ? -24.362 42.974  6.437   1.00 29.47 ? 107 GLU C CG  1 
ATOM   4706  C CD  . GLU C 1 108 ? -24.196 41.720  7.299   1.00 28.91 ? 107 GLU C CD  1 
ATOM   4707  O OE1 . GLU C 1 108 ? -23.091 41.135  7.418   1.00 27.84 ? 107 GLU C OE1 1 
ATOM   4708  O OE2 . GLU C 1 108 ? -25.221 41.321  7.873   1.00 28.59 ? 107 GLU C OE2 1 
ATOM   4709  N N   . LEU C 1 109 ? -23.377 43.627  2.320   1.00 29.27 ? 108 LEU C N   1 
ATOM   4710  C CA  . LEU C 1 109 ? -24.166 43.956  1.130   1.00 29.16 ? 108 LEU C CA  1 
ATOM   4711  C C   . LEU C 1 109 ? -24.110 42.834  0.102   1.00 29.18 ? 108 LEU C C   1 
ATOM   4712  O O   . LEU C 1 109 ? -25.137 42.457  -0.469  1.00 29.14 ? 108 LEU C O   1 
ATOM   4713  C CB  . LEU C 1 109 ? -23.725 45.295  0.505   1.00 29.19 ? 108 LEU C CB  1 
ATOM   4714  C CG  . LEU C 1 109 ? -24.453 45.781  -0.763  1.00 29.03 ? 108 LEU C CG  1 
ATOM   4715  C CD1 . LEU C 1 109 ? -25.973 45.775  -0.602  1.00 28.10 ? 108 LEU C CD1 1 
ATOM   4716  C CD2 . LEU C 1 109 ? -23.981 47.163  -1.166  1.00 29.35 ? 108 LEU C CD2 1 
ATOM   4717  N N   . LYS C 1 110 ? -22.907 42.313  -0.135  1.00 29.13 ? 109 LYS C N   1 
ATOM   4718  C CA  . LYS C 1 110 ? -22.719 41.156  -1.003  1.00 29.14 ? 109 LYS C CA  1 
ATOM   4719  C C   . LYS C 1 110 ? -23.576 39.966  -0.566  1.00 29.30 ? 109 LYS C C   1 
ATOM   4720  O O   . LYS C 1 110 ? -24.121 39.249  -1.408  1.00 29.20 ? 109 LYS C O   1 
ATOM   4721  C CB  . LYS C 1 110 ? -21.249 40.759  -1.059  1.00 29.03 ? 109 LYS C CB  1 
ATOM   4722  C CG  . LYS C 1 110 ? -20.401 41.658  -1.944  1.00 29.65 ? 109 LYS C CG  1 
ATOM   4723  C CD  . LYS C 1 110 ? -18.982 41.131  -2.022  1.00 30.54 ? 109 LYS C CD  1 
ATOM   4724  C CE  . LYS C 1 110 ? -18.239 41.732  -3.182  1.00 31.44 ? 109 LYS C CE  1 
ATOM   4725  N NZ  . LYS C 1 110 ? -16.944 41.040  -3.429  1.00 33.08 ? 109 LYS C NZ  1 
ATOM   4726  N N   . HIS C 1 111 ? -23.705 39.770  0.748   1.00 29.45 ? 110 HIS C N   1 
ATOM   4727  C CA  . HIS C 1 111 ? -24.533 38.692  1.281   1.00 29.61 ? 110 HIS C CA  1 
ATOM   4728  C C   . HIS C 1 111 ? -26.010 38.886  0.948   1.00 30.17 ? 110 HIS C C   1 
ATOM   4729  O O   . HIS C 1 111 ? -26.731 37.916  0.720   1.00 30.32 ? 110 HIS C O   1 
ATOM   4730  C CB  . HIS C 1 111 ? -24.361 38.539  2.793   1.00 29.24 ? 110 HIS C CB  1 
ATOM   4731  C CG  . HIS C 1 111 ? -25.161 37.413  3.367   1.00 28.05 ? 110 HIS C CG  1 
ATOM   4732  N ND1 . HIS C 1 111 ? -26.445 37.578  3.838   1.00 27.24 ? 110 HIS C ND1 1 
ATOM   4733  C CD2 . HIS C 1 111 ? -24.875 36.096  3.505   1.00 26.78 ? 110 HIS C CD2 1 
ATOM   4734  C CE1 . HIS C 1 111 ? -26.910 36.415  4.260   1.00 26.58 ? 110 HIS C CE1 1 
ATOM   4735  N NE2 . HIS C 1 111 ? -25.975 35.501  4.070   1.00 26.70 ? 110 HIS C NE2 1 
ATOM   4736  N N   . LEU C 1 112 ? -26.457 40.137  0.940   1.00 30.76 ? 111 LEU C N   1 
ATOM   4737  C CA  . LEU C 1 112 ? -27.822 40.458  0.551   1.00 31.40 ? 111 LEU C CA  1 
ATOM   4738  C C   . LEU C 1 112 ? -28.053 40.161  -0.933  1.00 31.93 ? 111 LEU C C   1 
ATOM   4739  O O   . LEU C 1 112 ? -29.107 39.647  -1.318  1.00 31.94 ? 111 LEU C O   1 
ATOM   4740  C CB  . LEU C 1 112 ? -28.125 41.921  0.863   1.00 31.24 ? 111 LEU C CB  1 
ATOM   4741  C CG  . LEU C 1 112 ? -29.590 42.344  0.756   1.00 32.05 ? 111 LEU C CG  1 
ATOM   4742  C CD1 . LEU C 1 112 ? -30.001 43.121  2.000   1.00 32.54 ? 111 LEU C CD1 1 
ATOM   4743  C CD2 . LEU C 1 112 ? -29.840 43.146  -0.525  1.00 31.24 ? 111 LEU C CD2 1 
ATOM   4744  N N   . LEU C 1 113 ? -27.051 40.469  -1.750  1.00 32.50 ? 112 LEU C N   1 
ATOM   4745  C CA  . LEU C 1 113 ? -27.102 40.252  -3.188  1.00 33.24 ? 112 LEU C CA  1 
ATOM   4746  C C   . LEU C 1 113 ? -27.226 38.769  -3.545  1.00 33.80 ? 112 LEU C C   1 
ATOM   4747  O O   . LEU C 1 113 ? -27.881 38.415  -4.535  1.00 33.74 ? 112 LEU C O   1 
ATOM   4748  C CB  . LEU C 1 113 ? -25.836 40.807  -3.822  1.00 33.36 ? 112 LEU C CB  1 
ATOM   4749  C CG  . LEU C 1 113 ? -25.983 41.789  -4.972  1.00 33.76 ? 112 LEU C CG  1 
ATOM   4750  C CD1 . LEU C 1 113 ? -26.526 43.101  -4.452  1.00 34.55 ? 112 LEU C CD1 1 
ATOM   4751  C CD2 . LEU C 1 113 ? -24.623 42.004  -5.585  1.00 34.91 ? 112 LEU C CD2 1 
ATOM   4752  N N   . SER C 1 114 ? -26.600 37.917  -2.732  1.00 34.21 ? 113 SER C N   1 
ATOM   4753  C CA  . SER C 1 114 ? -26.629 36.466  -2.926  1.00 34.76 ? 113 SER C CA  1 
ATOM   4754  C C   . SER C 1 114 ? -28.006 35.877  -2.626  1.00 35.10 ? 113 SER C C   1 
ATOM   4755  O O   . SER C 1 114 ? -28.248 34.698  -2.871  1.00 35.22 ? 113 SER C O   1 
ATOM   4756  C CB  . SER C 1 114 ? -25.566 35.786  -2.059  1.00 34.57 ? 113 SER C CB  1 
ATOM   4757  O OG  . SER C 1 114 ? -25.997 35.684  -0.710  1.00 35.11 ? 113 SER C OG  1 
ATOM   4758  N N   . ARG C 1 115 ? -28.893 36.703  -2.076  1.00 35.57 ? 114 ARG C N   1 
ATOM   4759  C CA  . ARG C 1 115 ? -30.272 36.313  -1.812  1.00 36.13 ? 114 ARG C CA  1 
ATOM   4760  C C   . ARG C 1 115 ? -31.224 37.078  -2.744  1.00 36.03 ? 114 ARG C C   1 
ATOM   4761  O O   . ARG C 1 115 ? -32.412 37.219  -2.451  1.00 36.13 ? 114 ARG C O   1 
ATOM   4762  C CB  . ARG C 1 115 ? -30.644 36.575  -0.342  1.00 36.50 ? 114 ARG C CB  1 
ATOM   4763  C CG  . ARG C 1 115 ? -29.591 36.192  0.727   1.00 37.97 ? 114 ARG C CG  1 
ATOM   4764  C CD  . ARG C 1 115 ? -29.440 34.679  0.974   1.00 40.98 ? 114 ARG C CD  1 
ATOM   4765  N NE  . ARG C 1 115 ? -30.699 33.945  0.842   1.00 43.42 ? 114 ARG C NE  1 
ATOM   4766  C CZ  . ARG C 1 115 ? -30.871 32.859  0.086   1.00 44.76 ? 114 ARG C CZ  1 
ATOM   4767  N NH1 . ARG C 1 115 ? -29.858 32.334  -0.602  1.00 44.69 ? 114 ARG C NH1 1 
ATOM   4768  N NH2 . ARG C 1 115 ? -32.064 32.280  0.035   1.00 45.53 ? 114 ARG C NH2 1 
ATOM   4769  N N   . THR C 1 116 ? -30.689 37.563  -3.866  1.00 36.04 ? 115 THR C N   1 
ATOM   4770  C CA  . THR C 1 116 ? -31.425 38.400  -4.820  1.00 35.92 ? 115 THR C CA  1 
ATOM   4771  C C   . THR C 1 116 ? -31.240 37.878  -6.243  1.00 35.96 ? 115 THR C C   1 
ATOM   4772  O O   . THR C 1 116 ? -30.171 37.385  -6.590  1.00 35.91 ? 115 THR C O   1 
ATOM   4773  C CB  . THR C 1 116 ? -30.931 39.875  -4.773  1.00 35.75 ? 115 THR C CB  1 
ATOM   4774  O OG1 . THR C 1 116 ? -31.004 40.373  -3.435  1.00 35.93 ? 115 THR C OG1 1 
ATOM   4775  C CG2 . THR C 1 116 ? -31.775 40.767  -5.657  1.00 35.67 ? 115 THR C CG2 1 
ATOM   4776  N N   . ASN C 1 117 ? -32.278 37.998  -7.064  1.00 36.16 ? 116 ASN C N   1 
ATOM   4777  C CA  . ASN C 1 117 ? -32.184 37.644  -8.478  1.00 36.32 ? 116 ASN C CA  1 
ATOM   4778  C C   . ASN C 1 117 ? -32.484 38.799  -9.446  1.00 36.47 ? 116 ASN C C   1 
ATOM   4779  O O   . ASN C 1 117 ? -32.165 38.713  -10.637 1.00 36.35 ? 116 ASN C O   1 
ATOM   4780  C CB  . ASN C 1 117 ? -33.094 36.453  -8.787  1.00 36.31 ? 116 ASN C CB  1 
ATOM   4781  C CG  . ASN C 1 117 ? -32.614 35.164  -8.146  1.00 36.50 ? 116 ASN C CG  1 
ATOM   4782  O OD1 . ASN C 1 117 ? -33.302 34.591  -7.302  1.00 37.42 ? 116 ASN C OD1 1 
ATOM   4783  N ND2 . ASN C 1 117 ? -31.433 34.698  -8.546  1.00 35.85 ? 116 ASN C ND2 1 
ATOM   4784  N N   . HIS C 1 118 ? -33.088 39.875  -8.944  1.00 36.71 ? 117 HIS C N   1 
ATOM   4785  C CA  . HIS C 1 118 ? -33.565 40.942  -9.827  1.00 37.28 ? 117 HIS C CA  1 
ATOM   4786  C C   . HIS C 1 118 ? -33.586 42.325  -9.175  1.00 37.38 ? 117 HIS C C   1 
ATOM   4787  O O   . HIS C 1 118 ? -34.320 42.571  -8.219  1.00 37.49 ? 117 HIS C O   1 
ATOM   4788  C CB  . HIS C 1 118 ? -34.952 40.572  -10.390 1.00 37.21 ? 117 HIS C CB  1 
ATOM   4789  C CG  . HIS C 1 118 ? -35.356 41.348  -11.608 1.00 37.91 ? 117 HIS C CG  1 
ATOM   4790  N ND1 . HIS C 1 118 ? -34.486 42.159  -12.308 1.00 38.22 ? 117 HIS C ND1 1 
ATOM   4791  C CD2 . HIS C 1 118 ? -36.538 41.407  -12.270 1.00 38.14 ? 117 HIS C CD2 1 
ATOM   4792  C CE1 . HIS C 1 118 ? -35.121 42.700  -13.334 1.00 38.21 ? 117 HIS C CE1 1 
ATOM   4793  N NE2 . HIS C 1 118 ? -36.367 42.259  -13.333 1.00 38.15 ? 117 HIS C NE2 1 
ATOM   4794  N N   . PHE C 1 119 ? -32.764 43.215  -9.719  1.00 37.75 ? 118 PHE C N   1 
ATOM   4795  C CA  . PHE C 1 119 ? -32.723 44.623  -9.342  1.00 38.18 ? 118 PHE C CA  1 
ATOM   4796  C C   . PHE C 1 119 ? -33.286 45.471  -10.481 1.00 38.33 ? 118 PHE C C   1 
ATOM   4797  O O   . PHE C 1 119 ? -32.902 45.283  -11.642 1.00 38.28 ? 118 PHE C O   1 
ATOM   4798  C CB  . PHE C 1 119 ? -31.274 45.053  -9.091  1.00 38.32 ? 118 PHE C CB  1 
ATOM   4799  C CG  . PHE C 1 119 ? -30.805 44.878  -7.671  1.00 38.72 ? 118 PHE C CG  1 
ATOM   4800  C CD1 . PHE C 1 119 ? -31.593 44.246  -6.718  1.00 39.37 ? 118 PHE C CD1 1 
ATOM   4801  C CD2 . PHE C 1 119 ? -29.542 45.325  -7.298  1.00 39.09 ? 118 PHE C CD2 1 
ATOM   4802  C CE1 . PHE C 1 119 ? -31.137 44.086  -5.402  1.00 39.84 ? 118 PHE C CE1 1 
ATOM   4803  C CE2 . PHE C 1 119 ? -29.080 45.168  -5.994  1.00 39.34 ? 118 PHE C CE2 1 
ATOM   4804  C CZ  . PHE C 1 119 ? -29.878 44.546  -5.044  1.00 39.43 ? 118 PHE C CZ  1 
ATOM   4805  N N   . GLU C 1 120 ? -34.188 46.396  -10.152 1.00 38.31 ? 119 GLU C N   1 
ATOM   4806  C CA  . GLU C 1 120 ? -34.672 47.380  -11.121 1.00 38.48 ? 119 GLU C CA  1 
ATOM   4807  C C   . GLU C 1 120 ? -34.418 48.808  -10.625 1.00 38.34 ? 119 GLU C C   1 
ATOM   4808  O O   . GLU C 1 120 ? -34.848 49.194  -9.540  1.00 38.10 ? 119 GLU C O   1 
ATOM   4809  C CB  . GLU C 1 120 ? -36.156 47.168  -11.449 1.00 38.61 ? 119 GLU C CB  1 
ATOM   4810  C CG  . GLU C 1 120 ? -36.653 47.994  -12.644 1.00 39.84 ? 119 GLU C CG  1 
ATOM   4811  C CD  . GLU C 1 120 ? -38.171 47.992  -12.788 1.00 41.61 ? 119 GLU C CD  1 
ATOM   4812  O OE1 . GLU C 1 120 ? -38.773 46.896  -12.854 1.00 42.67 ? 119 GLU C OE1 1 
ATOM   4813  O OE2 . GLU C 1 120 ? -38.764 49.092  -12.845 1.00 41.94 ? 119 GLU C OE2 1 
ATOM   4814  N N   . LYS C 1 121 ? -33.726 49.582  -11.453 1.00 38.31 ? 120 LYS C N   1 
ATOM   4815  C CA  . LYS C 1 121 ? -33.287 50.929  -11.118 1.00 38.33 ? 120 LYS C CA  1 
ATOM   4816  C C   . LYS C 1 121 ? -34.413 51.948  -11.203 1.00 38.23 ? 120 LYS C C   1 
ATOM   4817  O O   . LYS C 1 121 ? -35.160 51.971  -12.180 1.00 38.44 ? 120 LYS C O   1 
ATOM   4818  C CB  . LYS C 1 121 ? -32.184 51.326  -12.088 1.00 38.49 ? 120 LYS C CB  1 
ATOM   4819  C CG  . LYS C 1 121 ? -31.187 52.318  -11.557 1.00 38.75 ? 120 LYS C CG  1 
ATOM   4820  C CD  . LYS C 1 121 ? -29.804 51.801  -11.869 1.00 39.25 ? 120 LYS C CD  1 
ATOM   4821  C CE  . LYS C 1 121 ? -28.905 52.885  -12.378 1.00 39.13 ? 120 LYS C CE  1 
ATOM   4822  N NZ  . LYS C 1 121 ? -27.544 52.337  -12.569 1.00 39.57 ? 120 LYS C NZ  1 
ATOM   4823  N N   . ILE C 1 122 ? -34.543 52.783  -10.174 1.00 38.10 ? 121 ILE C N   1 
ATOM   4824  C CA  . ILE C 1 122 ? -35.454 53.929  -10.236 1.00 37.92 ? 121 ILE C CA  1 
ATOM   4825  C C   . ILE C 1 122 ? -34.844 55.209  -9.649  1.00 37.67 ? 121 ILE C C   1 
ATOM   4826  O O   . ILE C 1 122 ? -33.908 55.161  -8.845  1.00 37.50 ? 121 ILE C O   1 
ATOM   4827  C CB  . ILE C 1 122 ? -36.864 53.649  -9.607  1.00 38.08 ? 121 ILE C CB  1 
ATOM   4828  C CG1 . ILE C 1 122 ? -36.846 53.775  -8.083  1.00 38.24 ? 121 ILE C CG1 1 
ATOM   4829  C CG2 . ILE C 1 122 ? -37.444 52.300  -10.074 1.00 38.13 ? 121 ILE C CG2 1 
ATOM   4830  C CD1 . ILE C 1 122 ? -38.209 54.138  -7.510  1.00 39.02 ? 121 ILE C CD1 1 
ATOM   4831  N N   . GLN C 1 123 ? -35.395 56.345  -10.067 1.00 37.50 ? 122 GLN C N   1 
ATOM   4832  C CA  . GLN C 1 123 ? -34.922 57.660  -9.662  1.00 37.13 ? 122 GLN C CA  1 
ATOM   4833  C C   . GLN C 1 123 ? -35.667 58.099  -8.416  1.00 36.97 ? 122 GLN C C   1 
ATOM   4834  O O   . GLN C 1 123 ? -36.900 58.154  -8.408  1.00 37.00 ? 122 GLN C O   1 
ATOM   4835  C CB  . GLN C 1 123 ? -35.155 58.658  -10.790 1.00 37.07 ? 122 GLN C CB  1 
ATOM   4836  C CG  . GLN C 1 123 ? -34.497 60.010  -10.586 1.00 37.53 ? 122 GLN C CG  1 
ATOM   4837  C CD  . GLN C 1 123 ? -34.931 61.027  -11.626 1.00 37.61 ? 122 GLN C CD  1 
ATOM   4838  O OE1 . GLN C 1 123 ? -36.107 61.381  -11.709 1.00 38.07 ? 122 GLN C OE1 1 
ATOM   4839  N NE2 . GLN C 1 123 ? -33.983 61.509  -12.417 1.00 37.19 ? 122 GLN C NE2 1 
ATOM   4840  N N   . ILE C 1 124 ? -34.922 58.409  -7.363  1.00 36.51 ? 123 ILE C N   1 
ATOM   4841  C CA  . ILE C 1 124 ? -35.544 58.798  -6.104  1.00 36.31 ? 123 ILE C CA  1 
ATOM   4842  C C   . ILE C 1 124 ? -35.403 60.294  -5.815  1.00 36.16 ? 123 ILE C C   1 
ATOM   4843  O O   . ILE C 1 124 ? -36.276 60.894  -5.191  1.00 36.17 ? 123 ILE C O   1 
ATOM   4844  C CB  . ILE C 1 124 ? -35.072 57.912  -4.911  1.00 36.50 ? 123 ILE C CB  1 
ATOM   4845  C CG1 . ILE C 1 124 ? -33.563 58.033  -4.674  1.00 36.34 ? 123 ILE C CG1 1 
ATOM   4846  C CG2 . ILE C 1 124 ? -35.464 56.445  -5.146  1.00 36.30 ? 123 ILE C CG2 1 
ATOM   4847  C CD1 . ILE C 1 124 ? -33.134 57.626  -3.284  1.00 36.42 ? 123 ILE C CD1 1 
ATOM   4848  N N   . ILE C 1 125 ? -34.306 60.888  -6.273  1.00 36.02 ? 124 ILE C N   1 
ATOM   4849  C CA  . ILE C 1 125 ? -34.120 62.338  -6.209  1.00 36.01 ? 124 ILE C CA  1 
ATOM   4850  C C   . ILE C 1 125 ? -33.542 62.812  -7.536  1.00 36.00 ? 124 ILE C C   1 
ATOM   4851  O O   . ILE C 1 125 ? -32.414 62.450  -7.876  1.00 36.14 ? 124 ILE C O   1 
ATOM   4852  C CB  . ILE C 1 125 ? -33.167 62.778  -5.075  1.00 35.95 ? 124 ILE C CB  1 
ATOM   4853  C CG1 . ILE C 1 125 ? -33.674 62.311  -3.705  1.00 36.17 ? 124 ILE C CG1 1 
ATOM   4854  C CG2 . ILE C 1 125 ? -33.006 64.294  -5.091  1.00 35.89 ? 124 ILE C CG2 1 
ATOM   4855  C CD1 . ILE C 1 125 ? -32.629 62.388  -2.600  1.00 36.74 ? 124 ILE C CD1 1 
ATOM   4856  N N   . PRO C 1 126 ? -34.313 63.616  -8.294  1.00 35.94 ? 125 PRO C N   1 
ATOM   4857  C CA  . PRO C 1 126 ? -33.823 64.104  -9.584  1.00 35.90 ? 125 PRO C CA  1 
ATOM   4858  C C   . PRO C 1 126 ? -32.624 65.034  -9.411  1.00 35.96 ? 125 PRO C C   1 
ATOM   4859  O O   . PRO C 1 126 ? -32.601 65.851  -8.494  1.00 35.72 ? 125 PRO C O   1 
ATOM   4860  C CB  . PRO C 1 126 ? -35.026 64.869  -10.157 1.00 35.74 ? 125 PRO C CB  1 
ATOM   4861  C CG  . PRO C 1 126 ? -36.209 64.343  -9.410  1.00 35.90 ? 125 PRO C CG  1 
ATOM   4862  C CD  . PRO C 1 126 ? -35.696 64.055  -8.033  1.00 35.88 ? 125 PRO C CD  1 
ATOM   4863  N N   . LYS C 1 127 A -31.639 64.893  -10.292 1.00 36.26 ? 125 LYS C N   1 
ATOM   4864  C CA  . LYS C 1 127 A -30.419 65.687  -10.246 1.00 36.83 ? 125 LYS C CA  1 
ATOM   4865  C C   . LYS C 1 127 A -30.685 67.187  -10.411 1.00 37.17 ? 125 LYS C C   1 
ATOM   4866  O O   . LYS C 1 127 A -29.910 68.015  -9.927  1.00 37.37 ? 125 LYS C O   1 
ATOM   4867  C CB  . LYS C 1 127 A -29.460 65.200  -11.326 1.00 36.94 ? 125 LYS C CB  1 
ATOM   4868  C CG  . LYS C 1 127 A -28.004 65.549  -11.103 1.00 37.84 ? 125 LYS C CG  1 
ATOM   4869  C CD  . LYS C 1 127 A -27.127 64.719  -12.026 1.00 39.15 ? 125 LYS C CD  1 
ATOM   4870  C CE  . LYS C 1 127 A -25.816 65.417  -12.319 1.00 39.72 ? 125 LYS C CE  1 
ATOM   4871  N NZ  . LYS C 1 127 A -24.937 64.546  -13.139 1.00 40.82 ? 125 LYS C NZ  1 
ATOM   4872  N N   . SER C 1 128 B -31.785 67.524  -11.085 1.00 37.41 ? 125 SER C N   1 
ATOM   4873  C CA  . SER C 1 128 B -32.164 68.915  -11.333 1.00 37.51 ? 125 SER C CA  1 
ATOM   4874  C C   . SER C 1 128 B -32.904 69.567  -10.154 1.00 37.39 ? 125 SER C C   1 
ATOM   4875  O O   . SER C 1 128 B -33.236 70.754  -10.207 1.00 37.55 ? 125 SER C O   1 
ATOM   4876  C CB  . SER C 1 128 B -33.003 69.021  -12.617 1.00 37.68 ? 125 SER C CB  1 
ATOM   4877  O OG  . SER C 1 128 B -34.319 68.528  -12.414 1.00 38.05 ? 125 SER C OG  1 
ATOM   4878  N N   . SER C 1 129 ? -33.151 68.804  -9.092  1.00 37.11 ? 126 SER C N   1 
ATOM   4879  C CA  . SER C 1 129 ? -33.872 69.324  -7.924  1.00 37.09 ? 126 SER C CA  1 
ATOM   4880  C C   . SER C 1 129 ? -32.979 70.069  -6.918  1.00 36.94 ? 126 SER C C   1 
ATOM   4881  O O   . SER C 1 129 ? -33.440 70.474  -5.855  1.00 36.75 ? 126 SER C O   1 
ATOM   4882  C CB  . SER C 1 129 ? -34.639 68.197  -7.224  1.00 37.10 ? 126 SER C CB  1 
ATOM   4883  O OG  . SER C 1 129 ? -33.750 67.318  -6.555  1.00 37.90 ? 126 SER C OG  1 
ATOM   4884  N N   . TRP C 1 130 ? -31.708 70.257  -7.260  1.00 37.00 ? 127 TRP C N   1 
ATOM   4885  C CA  . TRP C 1 130 ? -30.769 70.947  -6.379  1.00 36.97 ? 127 TRP C CA  1 
ATOM   4886  C C   . TRP C 1 130 ? -30.595 72.403  -6.801  1.00 37.29 ? 127 TRP C C   1 
ATOM   4887  O O   . TRP C 1 130 ? -29.601 72.761  -7.448  1.00 37.31 ? 127 TRP C O   1 
ATOM   4888  C CB  . TRP C 1 130 ? -29.418 70.226  -6.379  1.00 36.77 ? 127 TRP C CB  1 
ATOM   4889  C CG  . TRP C 1 130 ? -29.505 68.790  -5.973  1.00 36.06 ? 127 TRP C CG  1 
ATOM   4890  C CD1 . TRP C 1 130 ? -29.334 67.694  -6.775  1.00 35.56 ? 127 TRP C CD1 1 
ATOM   4891  C CD2 . TRP C 1 130 ? -29.786 68.289  -4.663  1.00 35.00 ? 127 TRP C CD2 1 
ATOM   4892  N NE1 . TRP C 1 130 ? -29.490 66.545  -6.042  1.00 35.02 ? 127 TRP C NE1 1 
ATOM   4893  C CE2 . TRP C 1 130 ? -29.768 66.881  -4.743  1.00 34.74 ? 127 TRP C CE2 1 
ATOM   4894  C CE3 . TRP C 1 130 ? -30.053 68.895  -3.430  1.00 34.30 ? 127 TRP C CE3 1 
ATOM   4895  C CZ2 . TRP C 1 130 ? -30.013 66.069  -3.637  1.00 34.39 ? 127 TRP C CZ2 1 
ATOM   4896  C CZ3 . TRP C 1 130 ? -30.292 68.088  -2.332  1.00 34.36 ? 127 TRP C CZ3 1 
ATOM   4897  C CH2 . TRP C 1 130 ? -30.268 66.690  -2.442  1.00 34.14 ? 127 TRP C CH2 1 
ATOM   4898  N N   . SER C 1 131 ? -31.562 73.243  -6.437  1.00 37.47 ? 128 SER C N   1 
ATOM   4899  C CA  . SER C 1 131 ? -31.533 74.654  -6.837  1.00 37.85 ? 128 SER C CA  1 
ATOM   4900  C C   . SER C 1 131 ? -30.551 75.495  -6.021  1.00 37.82 ? 128 SER C C   1 
ATOM   4901  O O   . SER C 1 131 ? -29.964 76.445  -6.543  1.00 38.24 ? 128 SER C O   1 
ATOM   4902  C CB  . SER C 1 131 ? -32.933 75.270  -6.820  1.00 37.85 ? 128 SER C CB  1 
ATOM   4903  O OG  . SER C 1 131 ? -33.614 74.966  -5.621  1.00 38.71 ? 128 SER C OG  1 
ATOM   4904  N N   . ASN C 1 132 ? -30.354 75.136  -4.755  1.00 37.70 ? 129 ASN C N   1 
ATOM   4905  C CA  . ASN C 1 132 ? -29.410 75.849  -3.894  1.00 37.51 ? 129 ASN C CA  1 
ATOM   4906  C C   . ASN C 1 132 ? -27.982 75.293  -3.932  1.00 37.17 ? 129 ASN C C   1 
ATOM   4907  O O   . ASN C 1 132 ? -27.107 75.765  -3.198  1.00 36.90 ? 129 ASN C O   1 
ATOM   4908  C CB  . ASN C 1 132 ? -29.918 75.871  -2.451  1.00 37.75 ? 129 ASN C CB  1 
ATOM   4909  C CG  . ASN C 1 132 ? -31.273 76.547  -2.307  1.00 38.97 ? 129 ASN C CG  1 
ATOM   4910  O OD1 . ASN C 1 132 ? -32.027 76.243  -1.379  1.00 40.53 ? 129 ASN C OD1 1 
ATOM   4911  N ND2 . ASN C 1 132 ? -31.589 77.470  -3.218  1.00 39.60 ? 129 ASN C ND2 1 
ATOM   4912  N N   . HIS C 1 133 ? -27.746 74.295  -4.786  1.00 36.78 ? 130 HIS C N   1 
ATOM   4913  C CA  . HIS C 1 133 ? -26.466 73.587  -4.803  1.00 36.32 ? 130 HIS C CA  1 
ATOM   4914  C C   . HIS C 1 133 ? -25.943 73.310  -6.214  1.00 36.48 ? 130 HIS C C   1 
ATOM   4915  O O   . HIS C 1 133 ? -26.725 73.084  -7.140  1.00 36.97 ? 130 HIS C O   1 
ATOM   4916  C CB  . HIS C 1 133 ? -26.585 72.279  -4.008  1.00 36.06 ? 130 HIS C CB  1 
ATOM   4917  C CG  . HIS C 1 133 ? -26.981 72.477  -2.577  1.00 34.88 ? 130 HIS C CG  1 
ATOM   4918  N ND1 . HIS C 1 133 ? -28.297 72.548  -2.171  1.00 33.72 ? 130 HIS C ND1 1 
ATOM   4919  C CD2 . HIS C 1 133 ? -26.233 72.637  -1.459  1.00 34.16 ? 130 HIS C CD2 1 
ATOM   4920  C CE1 . HIS C 1 133 ? -28.345 72.739  -0.865  1.00 33.15 ? 130 HIS C CE1 1 
ATOM   4921  N NE2 . HIS C 1 133 ? -27.106 72.792  -0.408  1.00 34.30 ? 130 HIS C NE2 1 
ATOM   4922  N N   . ASP C 1 134 ? -24.621 73.331  -6.371  1.00 36.36 ? 131 ASP C N   1 
ATOM   4923  C CA  . ASP C 1 134 ? -23.981 72.968  -7.636  1.00 36.44 ? 131 ASP C CA  1 
ATOM   4924  C C   . ASP C 1 134 ? -23.967 71.442  -7.810  1.00 36.66 ? 131 ASP C C   1 
ATOM   4925  O O   . ASP C 1 134 ? -23.252 70.727  -7.096  1.00 36.60 ? 131 ASP C O   1 
ATOM   4926  C CB  . ASP C 1 134 ? -22.558 73.537  -7.704  1.00 36.23 ? 131 ASP C CB  1 
ATOM   4927  C CG  . ASP C 1 134 ? -21.877 73.300  -9.052  1.00 36.56 ? 131 ASP C CG  1 
ATOM   4928  O OD1 . ASP C 1 134 ? -22.342 72.462  -9.856  1.00 36.81 ? 131 ASP C OD1 1 
ATOM   4929  O OD2 . ASP C 1 134 ? -20.849 73.959  -9.309  1.00 36.92 ? 131 ASP C OD2 1 
ATOM   4930  N N   . ALA C 1 135 ? -24.760 70.961  -8.767  1.00 36.69 ? 132 ALA C N   1 
ATOM   4931  C CA  . ALA C 1 135 ? -24.857 69.536  -9.074  1.00 36.73 ? 132 ALA C CA  1 
ATOM   4932  C C   . ALA C 1 135 ? -24.118 69.166  -10.360 1.00 37.02 ? 132 ALA C C   1 
ATOM   4933  O O   . ALA C 1 135 ? -24.245 68.039  -10.850 1.00 37.39 ? 132 ALA C O   1 
ATOM   4934  C CB  . ALA C 1 135 ? -26.318 69.112  -9.156  1.00 36.51 ? 132 ALA C CB  1 
ATOM   4935  N N   . SER C 1 136 ? -23.331 70.095  -10.895 1.00 37.14 ? 133 SER C N   1 
ATOM   4936  C CA  . SER C 1 136 ? -22.650 69.855  -12.166 1.00 37.47 ? 133 SER C CA  1 
ATOM   4937  C C   . SER C 1 136 ? -21.126 69.777  -12.098 1.00 37.58 ? 133 SER C C   1 
ATOM   4938  O O   . SER C 1 136 ? -20.509 69.150  -12.960 1.00 37.75 ? 133 SER C O   1 
ATOM   4939  C CB  . SER C 1 136 ? -23.089 70.865  -13.240 1.00 37.63 ? 133 SER C CB  1 
ATOM   4940  O OG  . SER C 1 136 ? -22.966 72.200  -12.783 1.00 38.31 ? 133 SER C OG  1 
ATOM   4941  N N   . SER C 1 137 A -20.515 70.406  -11.095 1.00 37.66 ? 133 SER C N   1 
ATOM   4942  C CA  . SER C 1 137 A -19.050 70.491  -11.068 1.00 37.85 ? 133 SER C CA  1 
ATOM   4943  C C   . SER C 1 137 A -18.379 69.461  -10.155 1.00 37.85 ? 133 SER C C   1 
ATOM   4944  O O   . SER C 1 137 A -17.158 69.466  -9.998  1.00 37.83 ? 133 SER C O   1 
ATOM   4945  C CB  . SER C 1 137 A -18.566 71.925  -10.787 1.00 37.81 ? 133 SER C CB  1 
ATOM   4946  O OG  . SER C 1 137 A -18.803 72.315  -9.447  1.00 38.35 ? 133 SER C OG  1 
ATOM   4947  N N   . GLY C 1 138 ? -19.177 68.561  -9.586  1.00 38.02 ? 134 GLY C N   1 
ATOM   4948  C CA  . GLY C 1 138 ? -18.656 67.468  -8.760  1.00 38.00 ? 134 GLY C CA  1 
ATOM   4949  C C   . GLY C 1 138 ? -18.187 66.296  -9.604  1.00 38.07 ? 134 GLY C C   1 
ATOM   4950  O O   . GLY C 1 138 ? -18.770 65.212  -9.562  1.00 37.68 ? 134 GLY C O   1 
ATOM   4951  N N   . VAL C 1 139 ? -17.136 66.525  -10.384 1.00 38.46 ? 135 VAL C N   1 
ATOM   4952  C CA  . VAL C 1 139 ? -16.542 65.486  -11.230 1.00 38.92 ? 135 VAL C CA  1 
ATOM   4953  C C   . VAL C 1 139 ? -15.034 65.397  -10.989 1.00 39.38 ? 135 VAL C C   1 
ATOM   4954  O O   . VAL C 1 139 ? -14.402 66.373  -10.570 1.00 39.44 ? 135 VAL C O   1 
ATOM   4955  C CB  . VAL C 1 139 ? -16.836 65.702  -12.746 1.00 39.00 ? 135 VAL C CB  1 
ATOM   4956  C CG1 . VAL C 1 139 ? -18.332 65.578  -13.040 1.00 38.49 ? 135 VAL C CG1 1 
ATOM   4957  C CG2 . VAL C 1 139 ? -16.269 67.039  -13.253 1.00 38.88 ? 135 VAL C CG2 1 
ATOM   4958  N N   . SER C 1 140 ? -14.460 64.230  -11.253 1.00 39.91 ? 136 SER C N   1 
ATOM   4959  C CA  . SER C 1 140 ? -13.050 64.005  -10.953 1.00 40.57 ? 136 SER C CA  1 
ATOM   4960  C C   . SER C 1 140 ? -12.305 63.333  -12.095 1.00 40.94 ? 136 SER C C   1 
ATOM   4961  O O   . SER C 1 140 ? -12.886 62.553  -12.855 1.00 40.89 ? 136 SER C O   1 
ATOM   4962  C CB  . SER C 1 140 ? -12.904 63.177  -9.668  1.00 40.58 ? 136 SER C CB  1 
ATOM   4963  O OG  . SER C 1 140 ? -11.542 62.934  -9.365  1.00 40.42 ? 136 SER C OG  1 
ATOM   4964  N N   . SER C 1 141 ? -11.014 63.642  -12.199 1.00 41.50 ? 137 SER C N   1 
ATOM   4965  C CA  . SER C 1 141 ? -10.117 62.938  -13.113 1.00 42.03 ? 137 SER C CA  1 
ATOM   4966  C C   . SER C 1 141 ? -9.902  61.489  -12.667 1.00 42.34 ? 137 SER C C   1 
ATOM   4967  O O   . SER C 1 141 ? -9.460  60.657  -13.459 1.00 42.55 ? 137 SER C O   1 
ATOM   4968  C CB  . SER C 1 141 ? -8.775  63.673  -13.247 1.00 42.08 ? 137 SER C CB  1 
ATOM   4969  O OG  . SER C 1 141 ? -8.138  63.848  -11.992 1.00 41.85 ? 137 SER C OG  1 
ATOM   4970  N N   . ALA C 1 142 ? -10.226 61.196  -11.407 1.00 42.68 ? 138 ALA C N   1 
ATOM   4971  C CA  . ALA C 1 142 ? -10.158 59.829  -10.871 1.00 43.17 ? 138 ALA C CA  1 
ATOM   4972  C C   . ALA C 1 142 ? -11.283 58.935  -11.391 1.00 43.43 ? 138 ALA C C   1 
ATOM   4973  O O   . ALA C 1 142 ? -11.166 57.710  -11.372 1.00 43.45 ? 138 ALA C O   1 
ATOM   4974  C CB  . ALA C 1 142 ? -10.161 59.844  -9.351  1.00 42.98 ? 138 ALA C CB  1 
ATOM   4975  N N   . CYS C 1 143 ? -12.374 59.550  -11.837 1.00 43.90 ? 139 CYS C N   1 
ATOM   4976  C CA  . CYS C 1 143 ? -13.484 58.818  -12.437 1.00 44.44 ? 139 CYS C CA  1 
ATOM   4977  C C   . CYS C 1 143 ? -13.746 59.312  -13.854 1.00 44.96 ? 139 CYS C C   1 
ATOM   4978  O O   . CYS C 1 143 ? -14.766 59.959  -14.095 1.00 44.86 ? 139 CYS C O   1 
ATOM   4979  C CB  . CYS C 1 143 ? -14.755 58.971  -11.596 1.00 44.11 ? 139 CYS C CB  1 
ATOM   4980  S SG  . CYS C 1 143 ? -14.661 58.287  -9.940  1.00 44.17 ? 139 CYS C SG  1 
ATOM   4981  N N   . PRO C 1 144 ? -12.841 58.999  -14.803 1.00 45.67 ? 140 PRO C N   1 
ATOM   4982  C CA  . PRO C 1 144 ? -13.000 59.526  -16.160 1.00 46.35 ? 140 PRO C CA  1 
ATOM   4983  C C   . PRO C 1 144 ? -13.979 58.696  -16.987 1.00 47.02 ? 140 PRO C C   1 
ATOM   4984  O O   . PRO C 1 144 ? -14.150 57.507  -16.722 1.00 47.30 ? 140 PRO C O   1 
ATOM   4985  C CB  . PRO C 1 144 ? -11.589 59.419  -16.737 1.00 46.31 ? 140 PRO C CB  1 
ATOM   4986  C CG  . PRO C 1 144 ? -10.976 58.236  -16.028 1.00 45.93 ? 140 PRO C CG  1 
ATOM   4987  C CD  . PRO C 1 144 ? -11.718 58.044  -14.718 1.00 45.80 ? 140 PRO C CD  1 
ATOM   4988  N N   . TYR C 1 145 ? -14.626 59.310  -17.971 1.00 47.86 ? 141 TYR C N   1 
ATOM   4989  C CA  . TYR C 1 145 ? -15.529 58.550  -18.836 1.00 48.76 ? 141 TYR C CA  1 
ATOM   4990  C C   . TYR C 1 145 ? -14.880 58.221  -20.192 1.00 49.28 ? 141 TYR C C   1 
ATOM   4991  O O   . TYR C 1 145 ? -14.565 57.053  -20.477 1.00 49.31 ? 141 TYR C O   1 
ATOM   4992  C CB  . TYR C 1 145 ? -16.897 59.234  -18.983 1.00 48.79 ? 141 TYR C CB  1 
ATOM   4993  C CG  . TYR C 1 145 ? -17.823 58.484  -19.905 1.00 49.12 ? 141 TYR C CG  1 
ATOM   4994  C CD1 . TYR C 1 145 ? -18.005 57.106  -19.772 1.00 49.57 ? 141 TYR C CD1 1 
ATOM   4995  C CD2 . TYR C 1 145 ? -18.506 59.142  -20.922 1.00 49.85 ? 141 TYR C CD2 1 
ATOM   4996  C CE1 . TYR C 1 145 ? -18.842 56.405  -20.627 1.00 49.88 ? 141 TYR C CE1 1 
ATOM   4997  C CE2 . TYR C 1 145 ? -19.354 58.447  -21.783 1.00 50.00 ? 141 TYR C CE2 1 
ATOM   4998  C CZ  . TYR C 1 145 ? -19.513 57.083  -21.628 1.00 49.84 ? 141 TYR C CZ  1 
ATOM   4999  O OH  . TYR C 1 145 ? -20.346 56.394  -22.476 1.00 50.86 ? 141 TYR C OH  1 
ATOM   5000  N N   . HIS C 1 146 ? -14.689 59.243  -21.023 1.00 49.66 ? 142 HIS C N   1 
ATOM   5001  C CA  . HIS C 1 146 ? -13.799 59.103  -22.158 1.00 50.17 ? 142 HIS C CA  1 
ATOM   5002  C C   . HIS C 1 146 ? -12.338 59.413  -21.784 1.00 50.06 ? 142 HIS C C   1 
ATOM   5003  O O   . HIS C 1 146 ? -11.519 58.496  -21.623 1.00 50.11 ? 142 HIS C O   1 
ATOM   5004  C CB  . HIS C 1 146 ? -14.136 60.141  -23.255 1.00 50.60 ? 142 HIS C CB  1 
ATOM   5005  C CG  . HIS C 1 146 ? -15.524 60.013  -23.810 1.00 51.98 ? 142 HIS C CG  1 
ATOM   5006  N ND1 . HIS C 1 146 ? -15.942 58.917  -24.537 1.00 53.61 ? 142 HIS C ND1 1 
ATOM   5007  C CD2 . HIS C 1 146 ? -16.582 60.861  -23.769 1.00 53.32 ? 142 HIS C CD2 1 
ATOM   5008  C CE1 . HIS C 1 146 ? -17.202 59.086  -24.903 1.00 53.89 ? 142 HIS C CE1 1 
ATOM   5009  N NE2 . HIS C 1 146 ? -17.614 60.258  -24.452 1.00 53.85 ? 142 HIS C NE2 1 
ATOM   5010  N N   . GLY C 1 147 ? -12.031 60.696  -21.630 1.00 49.80 ? 143 GLY C N   1 
ATOM   5011  C CA  . GLY C 1 147 ? -10.810 61.122  -20.981 1.00 49.15 ? 143 GLY C CA  1 
ATOM   5012  C C   . GLY C 1 147 ? -11.293 62.418  -20.334 1.00 48.77 ? 143 GLY C C   1 
ATOM   5013  O O   . GLY C 1 147 ? -10.522 63.359  -20.119 1.00 48.93 ? 143 GLY C O   1 
ATOM   5014  N N   . LYS C 1 148 ? -12.594 62.445  -20.045 1.00 47.94 ? 144 LYS C N   1 
ATOM   5015  C CA  . LYS C 1 148 ? -13.248 63.611  -19.480 1.00 47.07 ? 144 LYS C CA  1 
ATOM   5016  C C   . LYS C 1 148 ? -13.586 63.339  -18.015 1.00 46.03 ? 144 LYS C C   1 
ATOM   5017  O O   . LYS C 1 148 ? -14.011 62.235  -17.666 1.00 45.97 ? 144 LYS C O   1 
ATOM   5018  C CB  . LYS C 1 148 ? -14.526 63.922  -20.266 1.00 47.42 ? 144 LYS C CB  1 
ATOM   5019  C CG  . LYS C 1 148 ? -14.640 65.360  -20.768 1.00 48.72 ? 144 LYS C CG  1 
ATOM   5020  C CD  . LYS C 1 148 ? -14.692 66.395  -19.636 1.00 50.86 ? 144 LYS C CD  1 
ATOM   5021  C CE  . LYS C 1 148 ? -14.621 67.820  -20.196 1.00 51.59 ? 144 LYS C CE  1 
ATOM   5022  N NZ  . LYS C 1 148 ? -14.665 68.855  -19.125 1.00 52.35 ? 144 LYS C NZ  1 
ATOM   5023  N N   . SER C 1 149 ? -13.394 64.350  -17.168 1.00 44.59 ? 145 SER C N   1 
ATOM   5024  C CA  . SER C 1 149 ? -13.707 64.246  -15.746 1.00 43.04 ? 145 SER C CA  1 
ATOM   5025  C C   . SER C 1 149 ? -15.194 63.964  -15.523 1.00 41.97 ? 145 SER C C   1 
ATOM   5026  O O   . SER C 1 149 ? -16.055 64.707  -15.993 1.00 41.81 ? 145 SER C O   1 
ATOM   5027  C CB  . SER C 1 149 ? -13.287 65.518  -15.006 1.00 43.15 ? 145 SER C CB  1 
ATOM   5028  O OG  . SER C 1 149 ? -11.878 65.607  -14.907 1.00 43.19 ? 145 SER C OG  1 
ATOM   5029  N N   . SER C 1 150 ? -15.478 62.876  -14.810 1.00 40.50 ? 146 SER C N   1 
ATOM   5030  C CA  . SER C 1 150 ? -16.850 62.444  -14.551 1.00 38.89 ? 146 SER C CA  1 
ATOM   5031  C C   . SER C 1 150 ? -17.003 61.941  -13.105 1.00 37.95 ? 146 SER C C   1 
ATOM   5032  O O   . SER C 1 150 ? -16.188 62.275  -12.238 1.00 37.70 ? 146 SER C O   1 
ATOM   5033  C CB  . SER C 1 150 ? -17.273 61.383  -15.578 1.00 38.84 ? 146 SER C CB  1 
ATOM   5034  O OG  . SER C 1 150 ? -18.662 61.124  -15.515 1.00 37.97 ? 146 SER C OG  1 
ATOM   5035  N N   . PHE C 1 151 ? -18.044 61.148  -12.855 1.00 36.70 ? 147 PHE C N   1 
ATOM   5036  C CA  . PHE C 1 151 ? -18.366 60.667  -11.520 1.00 35.60 ? 147 PHE C CA  1 
ATOM   5037  C C   . PHE C 1 151 ? -19.302 59.465  -11.567 1.00 35.17 ? 147 PHE C C   1 
ATOM   5038  O O   . PHE C 1 151 ? -19.789 59.090  -12.633 1.00 35.03 ? 147 PHE C O   1 
ATOM   5039  C CB  . PHE C 1 151 ? -19.019 61.789  -10.708 1.00 35.51 ? 147 PHE C CB  1 
ATOM   5040  C CG  . PHE C 1 151 ? -18.973 61.570  -9.226  1.00 34.80 ? 147 PHE C CG  1 
ATOM   5041  C CD1 . PHE C 1 151 ? -17.754 61.483  -8.559  1.00 33.70 ? 147 PHE C CD1 1 
ATOM   5042  C CD2 . PHE C 1 151 ? -20.150 61.461  -8.493  1.00 34.17 ? 147 PHE C CD2 1 
ATOM   5043  C CE1 . PHE C 1 151 ? -17.704 61.284  -7.185  1.00 33.87 ? 147 PHE C CE1 1 
ATOM   5044  C CE2 . PHE C 1 151 ? -20.115 61.258  -7.115  1.00 34.08 ? 147 PHE C CE2 1 
ATOM   5045  C CZ  . PHE C 1 151 ? -18.890 61.171  -6.460  1.00 34.28 ? 147 PHE C CZ  1 
ATOM   5046  N N   . PHE C 1 152 ? -19.545 58.865  -10.400 1.00 34.66 ? 148 PHE C N   1 
ATOM   5047  C CA  . PHE C 1 152 ? -20.549 57.819  -10.235 1.00 34.04 ? 148 PHE C CA  1 
ATOM   5048  C C   . PHE C 1 152 ? -21.893 58.307  -10.767 1.00 33.66 ? 148 PHE C C   1 
ATOM   5049  O O   . PHE C 1 152 ? -22.222 59.484  -10.639 1.00 33.83 ? 148 PHE C O   1 
ATOM   5050  C CB  . PHE C 1 152 ? -20.682 57.430  -8.759  1.00 34.08 ? 148 PHE C CB  1 
ATOM   5051  C CG  . PHE C 1 152 ? -19.422 56.861  -8.155  1.00 34.24 ? 148 PHE C CG  1 
ATOM   5052  C CD1 . PHE C 1 152 ? -19.025 55.548  -8.433  1.00 33.53 ? 148 PHE C CD1 1 
ATOM   5053  C CD2 . PHE C 1 152 ? -18.637 57.633  -7.291  1.00 34.24 ? 148 PHE C CD2 1 
ATOM   5054  C CE1 . PHE C 1 152 ? -17.862 55.016  -7.875  1.00 32.92 ? 148 PHE C CE1 1 
ATOM   5055  C CE2 . PHE C 1 152 ? -17.467 57.107  -6.723  1.00 33.92 ? 148 PHE C CE2 1 
ATOM   5056  C CZ  . PHE C 1 152 ? -17.082 55.795  -7.017  1.00 33.48 ? 148 PHE C CZ  1 
ATOM   5057  N N   . ARG C 1 153 ? -22.662 57.402  -11.364 1.00 33.21 ? 149 ARG C N   1 
ATOM   5058  C CA  . ARG C 1 153 ? -23.901 57.765  -12.055 1.00 32.80 ? 149 ARG C CA  1 
ATOM   5059  C C   . ARG C 1 153 ? -25.113 57.811  -11.128 1.00 32.46 ? 149 ARG C C   1 
ATOM   5060  O O   . ARG C 1 153 ? -26.013 58.623  -11.317 1.00 32.61 ? 149 ARG C O   1 
ATOM   5061  C CB  . ARG C 1 153 ? -24.176 56.792  -13.210 1.00 32.90 ? 149 ARG C CB  1 
ATOM   5062  C CG  . ARG C 1 153 ? -23.040 56.642  -14.230 1.00 32.98 ? 149 ARG C CG  1 
ATOM   5063  C CD  . ARG C 1 153 ? -23.131 57.696  -15.315 1.00 33.65 ? 149 ARG C CD  1 
ATOM   5064  N NE  . ARG C 1 153 ? -22.377 57.336  -16.514 1.00 33.86 ? 149 ARG C NE  1 
ATOM   5065  C CZ  . ARG C 1 153 ? -21.486 58.121  -17.112 1.00 34.13 ? 149 ARG C CZ  1 
ATOM   5066  N NH1 . ARG C 1 153 ? -21.220 59.329  -16.628 1.00 34.50 ? 149 ARG C NH1 1 
ATOM   5067  N NH2 . ARG C 1 153 ? -20.862 57.701  -18.205 1.00 34.01 ? 149 ARG C NH2 1 
ATOM   5068  N N   . ASN C 1 154 ? -25.126 56.942  -10.123 1.00 32.01 ? 150 ASN C N   1 
ATOM   5069  C CA  . ASN C 1 154 ? -26.296 56.764  -9.266  1.00 31.54 ? 150 ASN C CA  1 
ATOM   5070  C C   . ASN C 1 154 ? -26.310 57.693  -8.063  1.00 31.05 ? 150 ASN C C   1 
ATOM   5071  O O   . ASN C 1 154 ? -27.275 57.740  -7.298  1.00 30.94 ? 150 ASN C O   1 
ATOM   5072  C CB  . ASN C 1 154 ? -26.392 55.301  -8.820  1.00 31.63 ? 150 ASN C CB  1 
ATOM   5073  C CG  . ASN C 1 154 ? -26.525 54.352  -9.988  1.00 32.10 ? 150 ASN C CG  1 
ATOM   5074  O OD1 . ASN C 1 154 ? -26.874 54.764  -11.094 1.00 33.42 ? 150 ASN C OD1 1 
ATOM   5075  N ND2 . ASN C 1 154 ? -26.240 53.075  -9.754  1.00 33.20 ? 150 ASN C ND2 1 
ATOM   5076  N N   . VAL C 1 155 ? -25.240 58.458  -7.934  1.00 30.74 ? 151 VAL C N   1 
ATOM   5077  C CA  . VAL C 1 155 ? -24.984 59.254  -6.756  1.00 30.60 ? 151 VAL C CA  1 
ATOM   5078  C C   . VAL C 1 155 ? -24.414 60.611  -7.192  1.00 30.53 ? 151 VAL C C   1 
ATOM   5079  O O   . VAL C 1 155 ? -23.726 60.696  -8.220  1.00 30.52 ? 151 VAL C O   1 
ATOM   5080  C CB  . VAL C 1 155 ? -24.068 58.445  -5.796  1.00 30.70 ? 151 VAL C CB  1 
ATOM   5081  C CG1 . VAL C 1 155 ? -22.885 59.239  -5.317  1.00 30.62 ? 151 VAL C CG1 1 
ATOM   5082  C CG2 . VAL C 1 155 ? -24.881 57.868  -4.638  1.00 30.79 ? 151 VAL C CG2 1 
ATOM   5083  N N   . VAL C 1 156 ? -24.729 61.668  -6.440  1.00 30.32 ? 152 VAL C N   1 
ATOM   5084  C CA  . VAL C 1 156 ? -24.384 63.047  -6.837  1.00 30.24 ? 152 VAL C CA  1 
ATOM   5085  C C   . VAL C 1 156 ? -23.510 63.786  -5.811  1.00 30.34 ? 152 VAL C C   1 
ATOM   5086  O O   . VAL C 1 156 ? -23.872 63.924  -4.643  1.00 30.00 ? 152 VAL C O   1 
ATOM   5087  C CB  . VAL C 1 156 ? -25.660 63.894  -7.146  1.00 30.15 ? 152 VAL C CB  1 
ATOM   5088  C CG1 . VAL C 1 156 ? -25.289 65.322  -7.531  1.00 29.93 ? 152 VAL C CG1 1 
ATOM   5089  C CG2 . VAL C 1 156 ? -26.488 63.257  -8.254  1.00 30.08 ? 152 VAL C CG2 1 
ATOM   5090  N N   . TRP C 1 157 ? -22.368 64.277  -6.279  1.00 30.87 ? 153 TRP C N   1 
ATOM   5091  C CA  . TRP C 1 157 ? -21.432 65.041  -5.458  1.00 31.32 ? 153 TRP C CA  1 
ATOM   5092  C C   . TRP C 1 157 ? -21.767 66.535  -5.492  1.00 32.00 ? 153 TRP C C   1 
ATOM   5093  O O   . TRP C 1 157 ? -21.448 67.228  -6.459  1.00 32.24 ? 153 TRP C O   1 
ATOM   5094  C CB  . TRP C 1 157 ? -20.010 64.782  -5.953  1.00 31.02 ? 153 TRP C CB  1 
ATOM   5095  C CG  . TRP C 1 157 ? -18.896 65.393  -5.138  1.00 30.66 ? 153 TRP C CG  1 
ATOM   5096  C CD1 . TRP C 1 157 ? -18.990 66.001  -3.910  1.00 30.35 ? 153 TRP C CD1 1 
ATOM   5097  C CD2 . TRP C 1 157 ? -17.511 65.410  -5.485  1.00 29.48 ? 153 TRP C CD2 1 
ATOM   5098  N NE1 . TRP C 1 157 ? -17.749 66.411  -3.487  1.00 29.39 ? 153 TRP C NE1 1 
ATOM   5099  C CE2 . TRP C 1 157 ? -16.821 66.056  -4.431  1.00 29.60 ? 153 TRP C CE2 1 
ATOM   5100  C CE3 . TRP C 1 157 ? -16.781 64.942  -6.585  1.00 29.00 ? 153 TRP C CE3 1 
ATOM   5101  C CZ2 . TRP C 1 157 ? -15.437 66.253  -4.450  1.00 29.45 ? 153 TRP C CZ2 1 
ATOM   5102  C CZ3 . TRP C 1 157 ? -15.403 65.139  -6.607  1.00 29.85 ? 153 TRP C CZ3 1 
ATOM   5103  C CH2 . TRP C 1 157 ? -14.746 65.794  -5.545  1.00 29.47 ? 153 TRP C CH2 1 
ATOM   5104  N N   . LEU C 1 158 ? -22.408 67.015  -4.428  1.00 32.66 ? 154 LEU C N   1 
ATOM   5105  C CA  . LEU C 1 158 ? -22.863 68.400  -4.344  1.00 33.50 ? 154 LEU C CA  1 
ATOM   5106  C C   . LEU C 1 158 ? -21.766 69.341  -3.847  1.00 34.42 ? 154 LEU C C   1 
ATOM   5107  O O   . LEU C 1 158 ? -21.051 69.036  -2.882  1.00 34.52 ? 154 LEU C O   1 
ATOM   5108  C CB  . LEU C 1 158 ? -24.112 68.516  -3.453  1.00 33.37 ? 154 LEU C CB  1 
ATOM   5109  C CG  . LEU C 1 158 ? -25.369 67.705  -3.824  1.00 33.27 ? 154 LEU C CG  1 
ATOM   5110  C CD1 . LEU C 1 158 ? -26.407 67.768  -2.718  1.00 32.62 ? 154 LEU C CD1 1 
ATOM   5111  C CD2 . LEU C 1 158 ? -25.982 68.149  -5.148  1.00 32.39 ? 154 LEU C CD2 1 
ATOM   5112  N N   . ILE C 1 159 ? -21.651 70.485  -4.522  1.00 35.31 ? 155 ILE C N   1 
ATOM   5113  C CA  . ILE C 1 159 ? -20.649 71.516  -4.230  1.00 36.11 ? 155 ILE C CA  1 
ATOM   5114  C C   . ILE C 1 159 ? -21.381 72.813  -3.888  1.00 36.69 ? 155 ILE C C   1 
ATOM   5115  O O   . ILE C 1 159 ? -22.487 73.040  -4.369  1.00 36.97 ? 155 ILE C O   1 
ATOM   5116  C CB  . ILE C 1 159 ? -19.703 71.740  -5.457  1.00 36.19 ? 155 ILE C CB  1 
ATOM   5117  C CG1 . ILE C 1 159 ? -19.158 70.404  -5.993  1.00 36.34 ? 155 ILE C CG1 1 
ATOM   5118  C CG2 . ILE C 1 159 ? -18.562 72.726  -5.139  1.00 35.88 ? 155 ILE C CG2 1 
ATOM   5119  C CD1 . ILE C 1 159 ? -18.327 69.588  -4.988  1.00 36.61 ? 155 ILE C CD1 1 
ATOM   5120  N N   . LYS C 1 160 ? -20.783 73.656  -3.054  1.00 37.53 ? 156 LYS C N   1 
ATOM   5121  C CA  . LYS C 1 160 ? -21.408 74.931  -2.694  1.00 38.41 ? 156 LYS C CA  1 
ATOM   5122  C C   . LYS C 1 160 ? -21.806 75.759  -3.929  1.00 39.31 ? 156 LYS C C   1 
ATOM   5123  O O   . LYS C 1 160 ? -21.165 75.679  -4.990  1.00 39.31 ? 156 LYS C O   1 
ATOM   5124  C CB  . LYS C 1 160 ? -20.499 75.744  -1.769  1.00 38.21 ? 156 LYS C CB  1 
ATOM   5125  C CG  . LYS C 1 160 ? -19.276 76.349  -2.443  1.00 37.59 ? 156 LYS C CG  1 
ATOM   5126  C CD  . LYS C 1 160 ? -18.470 77.178  -1.460  1.00 36.86 ? 156 LYS C CD  1 
ATOM   5127  C CE  . LYS C 1 160 ? -17.374 77.961  -2.160  1.00 36.38 ? 156 LYS C CE  1 
ATOM   5128  N NZ  . LYS C 1 160 ? -16.458 78.566  -1.166  1.00 36.64 ? 156 LYS C NZ  1 
ATOM   5129  N N   . LYS C 1 161 ? -22.877 76.537  -3.786  1.00 40.07 ? 157 LYS C N   1 
ATOM   5130  C CA  . LYS C 1 161 ? -23.333 77.424  -4.852  1.00 40.92 ? 157 LYS C CA  1 
ATOM   5131  C C   . LYS C 1 161 ? -23.274 78.869  -4.361  1.00 41.16 ? 157 LYS C C   1 
ATOM   5132  O O   . LYS C 1 161 ? -23.709 79.160  -3.244  1.00 41.25 ? 157 LYS C O   1 
ATOM   5133  C CB  . LYS C 1 161 ? -24.760 77.058  -5.267  1.00 41.15 ? 157 LYS C CB  1 
ATOM   5134  C CG  . LYS C 1 161 ? -25.188 77.599  -6.621  1.00 41.84 ? 157 LYS C CG  1 
ATOM   5135  C CD  . LYS C 1 161 ? -26.649 77.269  -6.909  1.00 43.52 ? 157 LYS C CD  1 
ATOM   5136  C CE  . LYS C 1 161 ? -27.127 77.905  -8.210  1.00 44.48 ? 157 LYS C CE  1 
ATOM   5137  N NZ  . LYS C 1 161 ? -26.321 77.454  -9.389  1.00 45.18 ? 157 LYS C NZ  1 
ATOM   5138  N N   . ASN C 1 162 ? -22.730 79.759  -5.193  1.00 41.49 ? 158 ASN C N   1 
ATOM   5139  C CA  . ASN C 1 162 ? -22.589 81.187  -4.854  1.00 41.98 ? 158 ASN C CA  1 
ATOM   5140  C C   . ASN C 1 162 ? -21.978 81.420  -3.467  1.00 41.90 ? 158 ASN C C   1 
ATOM   5141  O O   . ASN C 1 162 ? -22.499 82.208  -2.672  1.00 41.97 ? 158 ASN C O   1 
ATOM   5142  C CB  . ASN C 1 162 ? -23.940 81.922  -4.972  1.00 42.14 ? 158 ASN C CB  1 
ATOM   5143  C CG  . ASN C 1 162 ? -24.430 82.037  -6.410  1.00 43.04 ? 158 ASN C CG  1 
ATOM   5144  O OD1 . ASN C 1 162 ? -23.635 82.161  -7.345  1.00 44.64 ? 158 ASN C OD1 1 
ATOM   5145  N ND2 . ASN C 1 162 ? -25.751 82.007  -6.591  1.00 42.98 ? 158 ASN C ND2 1 
ATOM   5146  N N   . SER C 1 163 ? -20.882 80.716  -3.185  1.00 41.87 ? 159 SER C N   1 
ATOM   5147  C CA  . SER C 1 163 ? -20.201 80.769  -1.878  1.00 41.80 ? 159 SER C CA  1 
ATOM   5148  C C   . SER C 1 163 ? -21.104 80.431  -0.679  1.00 41.54 ? 159 SER C C   1 
ATOM   5149  O O   . SER C 1 163 ? -20.897 80.935  0.430   1.00 41.69 ? 159 SER C O   1 
ATOM   5150  C CB  . SER C 1 163 ? -19.503 82.122  -1.672  1.00 41.87 ? 159 SER C CB  1 
ATOM   5151  O OG  . SER C 1 163 ? -18.334 82.218  -2.470  1.00 42.53 ? 159 SER C OG  1 
ATOM   5152  N N   . ALA C 1 164 ? -22.098 79.574  -0.908  1.00 41.04 ? 160 ALA C N   1 
ATOM   5153  C CA  . ALA C 1 164 ? -22.973 79.114  0.168   1.00 40.52 ? 160 ALA C CA  1 
ATOM   5154  C C   . ALA C 1 164 ? -23.419 77.659  -0.010  1.00 40.21 ? 160 ALA C C   1 
ATOM   5155  O O   . ALA C 1 164 ? -23.522 77.147  -1.132  1.00 40.31 ? 160 ALA C O   1 
ATOM   5156  C CB  . ALA C 1 164 ? -24.174 80.037  0.317   1.00 40.32 ? 160 ALA C CB  1 
ATOM   5157  N N   . TYR C 1 165 ? -23.660 77.001  1.120   1.00 39.68 ? 161 TYR C N   1 
ATOM   5158  C CA  . TYR C 1 165 ? -24.161 75.634  1.158   1.00 38.94 ? 161 TYR C CA  1 
ATOM   5159  C C   . TYR C 1 165 ? -25.268 75.589  2.204   1.00 38.95 ? 161 TYR C C   1 
ATOM   5160  O O   . TYR C 1 165 ? -25.007 75.313  3.381   1.00 38.95 ? 161 TYR C O   1 
ATOM   5161  C CB  . TYR C 1 165 ? -23.033 74.670  1.524   1.00 38.60 ? 161 TYR C CB  1 
ATOM   5162  C CG  . TYR C 1 165 ? -23.295 73.202  1.242   1.00 36.99 ? 161 TYR C CG  1 
ATOM   5163  C CD1 . TYR C 1 165 ? -22.494 72.497  0.343   1.00 35.43 ? 161 TYR C CD1 1 
ATOM   5164  C CD2 . TYR C 1 165 ? -24.323 72.513  1.888   1.00 35.38 ? 161 TYR C CD2 1 
ATOM   5165  C CE1 . TYR C 1 165 ? -22.714 71.146  0.091   1.00 34.38 ? 161 TYR C CE1 1 
ATOM   5166  C CE2 . TYR C 1 165 ? -24.551 71.170  1.641   1.00 34.48 ? 161 TYR C CE2 1 
ATOM   5167  C CZ  . TYR C 1 165 ? -23.744 70.493  0.746   1.00 33.90 ? 161 TYR C CZ  1 
ATOM   5168  O OH  . TYR C 1 165 ? -23.972 69.164  0.512   1.00 33.27 ? 161 TYR C OH  1 
ATOM   5169  N N   . PRO C 1 166 ? -26.510 75.889  1.783   1.00 38.90 ? 162 PRO C N   1 
ATOM   5170  C CA  . PRO C 1 166 ? -27.658 75.859  2.685   1.00 38.86 ? 162 PRO C CA  1 
ATOM   5171  C C   . PRO C 1 166 ? -27.971 74.432  3.118   1.00 38.89 ? 162 PRO C C   1 
ATOM   5172  O O   . PRO C 1 166 ? -27.554 73.477  2.458   1.00 38.80 ? 162 PRO C O   1 
ATOM   5173  C CB  . PRO C 1 166 ? -28.803 76.415  1.823   1.00 38.78 ? 162 PRO C CB  1 
ATOM   5174  C CG  . PRO C 1 166 ? -28.147 77.074  0.657   1.00 38.69 ? 162 PRO C CG  1 
ATOM   5175  C CD  . PRO C 1 166 ? -26.897 76.302  0.421   1.00 38.97 ? 162 PRO C CD  1 
ATOM   5176  N N   . THR C 1 167 ? -28.699 74.304  4.220   1.00 39.02 ? 163 THR C N   1 
ATOM   5177  C CA  . THR C 1 167 ? -29.031 73.006  4.792   1.00 39.16 ? 163 THR C CA  1 
ATOM   5178  C C   . THR C 1 167 ? -29.986 72.225  3.890   1.00 39.10 ? 163 THR C C   1 
ATOM   5179  O O   . THR C 1 167 ? -31.038 72.726  3.485   1.00 39.01 ? 163 THR C O   1 
ATOM   5180  C CB  . THR C 1 167 ? -29.621 73.157  6.211   1.00 39.14 ? 163 THR C CB  1 
ATOM   5181  O OG1 . THR C 1 167 ? -28.685 73.862  7.033   1.00 39.74 ? 163 THR C OG1 1 
ATOM   5182  C CG2 . THR C 1 167 ? -29.898 71.800  6.840   1.00 39.17 ? 163 THR C CG2 1 
ATOM   5183  N N   . ILE C 1 168 ? -29.581 70.999  3.570   1.00 39.02 ? 164 ILE C N   1 
ATOM   5184  C CA  . ILE C 1 168 ? -30.390 70.063  2.803   1.00 38.81 ? 164 ILE C CA  1 
ATOM   5185  C C   . ILE C 1 168 ? -31.346 69.331  3.748   1.00 39.03 ? 164 ILE C C   1 
ATOM   5186  O O   . ILE C 1 168 ? -30.943 68.869  4.817   1.00 38.90 ? 164 ILE C O   1 
ATOM   5187  C CB  . ILE C 1 168 ? -29.482 69.055  2.052   1.00 38.74 ? 164 ILE C CB  1 
ATOM   5188  C CG1 . ILE C 1 168 ? -28.644 69.796  1.005   1.00 38.47 ? 164 ILE C CG1 1 
ATOM   5189  C CG2 . ILE C 1 168 ? -30.297 67.927  1.414   1.00 38.04 ? 164 ILE C CG2 1 
ATOM   5190  C CD1 . ILE C 1 168 ? -27.413 69.058  0.543   1.00 38.55 ? 164 ILE C CD1 1 
ATOM   5191  N N   . LYS C 1 169 ? -32.617 69.271  3.362   1.00 39.20 ? 165 LYS C N   1 
ATOM   5192  C CA  . LYS C 1 169 ? -33.615 68.462  4.056   1.00 39.56 ? 165 LYS C CA  1 
ATOM   5193  C C   . LYS C 1 169 ? -34.503 67.822  3.005   1.00 39.57 ? 165 LYS C C   1 
ATOM   5194  O O   . LYS C 1 169 ? -35.324 68.501  2.376   1.00 39.73 ? 165 LYS C O   1 
ATOM   5195  C CB  . LYS C 1 169 ? -34.452 69.299  5.027   1.00 39.69 ? 165 LYS C CB  1 
ATOM   5196  C CG  . LYS C 1 169 ? -33.751 69.630  6.333   1.00 41.21 ? 165 LYS C CG  1 
ATOM   5197  C CD  . LYS C 1 169 ? -34.543 70.620  7.176   1.00 43.29 ? 165 LYS C CD  1 
ATOM   5198  C CE  . LYS C 1 169 ? -33.659 71.249  8.255   1.00 44.71 ? 165 LYS C CE  1 
ATOM   5199  N NZ  . LYS C 1 169 ? -34.384 72.282  9.069   1.00 45.60 ? 165 LYS C NZ  1 
ATOM   5200  N N   . ARG C 1 170 ? -34.307 66.523  2.792   1.00 39.38 ? 166 ARG C N   1 
ATOM   5201  C CA  . ARG C 1 170 ? -35.080 65.776  1.803   1.00 39.12 ? 166 ARG C CA  1 
ATOM   5202  C C   . ARG C 1 170 ? -35.740 64.551  2.416   1.00 38.80 ? 166 ARG C C   1 
ATOM   5203  O O   . ARG C 1 170 ? -35.253 63.982  3.395   1.00 38.68 ? 166 ARG C O   1 
ATOM   5204  C CB  . ARG C 1 170 ? -34.204 65.351  0.622   1.00 39.31 ? 166 ARG C CB  1 
ATOM   5205  C CG  . ARG C 1 170 ? -33.568 66.493  -0.164  1.00 40.10 ? 166 ARG C CG  1 
ATOM   5206  C CD  . ARG C 1 170 ? -34.604 67.437  -0.771  1.00 41.58 ? 166 ARG C CD  1 
ATOM   5207  N NE  . ARG C 1 170 ? -33.969 68.399  -1.666  1.00 42.42 ? 166 ARG C NE  1 
ATOM   5208  C CZ  . ARG C 1 170 ? -33.820 68.223  -2.977  1.00 42.78 ? 166 ARG C CZ  1 
ATOM   5209  N NH1 . ARG C 1 170 ? -34.276 67.124  -3.567  1.00 42.92 ? 166 ARG C NH1 1 
ATOM   5210  N NH2 . ARG C 1 170 ? -33.219 69.154  -3.701  1.00 42.47 ? 166 ARG C NH2 1 
ATOM   5211  N N   . SER C 1 171 ? -36.858 64.156  1.825   1.00 38.42 ? 167 SER C N   1 
ATOM   5212  C CA  . SER C 1 171 ? -37.606 63.001  2.269   1.00 37.95 ? 167 SER C CA  1 
ATOM   5213  C C   . SER C 1 171 ? -38.094 62.234  1.049   1.00 37.71 ? 167 SER C C   1 
ATOM   5214  O O   . SER C 1 171 ? -38.687 62.816  0.140   1.00 37.60 ? 167 SER C O   1 
ATOM   5215  C CB  . SER C 1 171 ? -38.787 63.441  3.128   1.00 37.83 ? 167 SER C CB  1 
ATOM   5216  O OG  . SER C 1 171 ? -39.438 62.319  3.693   1.00 38.39 ? 167 SER C OG  1 
ATOM   5217  N N   . TYR C 1 172 ? -37.817 60.934  1.018   1.00 37.39 ? 168 TYR C N   1 
ATOM   5218  C CA  . TYR C 1 172 ? -38.371 60.071  -0.018  1.00 37.01 ? 168 TYR C CA  1 
ATOM   5219  C C   . TYR C 1 172 ? -39.209 58.942  0.595   1.00 36.94 ? 168 TYR C C   1 
ATOM   5220  O O   . TYR C 1 172 ? -38.728 58.197  1.454   1.00 36.87 ? 168 TYR C O   1 
ATOM   5221  C CB  . TYR C 1 172 ? -37.275 59.523  -0.946  1.00 36.82 ? 168 TYR C CB  1 
ATOM   5222  C CG  . TYR C 1 172 ? -37.800 58.503  -1.939  1.00 36.71 ? 168 TYR C CG  1 
ATOM   5223  C CD1 . TYR C 1 172 ? -38.339 58.902  -3.163  1.00 36.22 ? 168 TYR C CD1 1 
ATOM   5224  C CD2 . TYR C 1 172 ? -37.783 57.140  -1.640  1.00 36.12 ? 168 TYR C CD2 1 
ATOM   5225  C CE1 . TYR C 1 172 ? -38.837 57.970  -4.067  1.00 35.73 ? 168 TYR C CE1 1 
ATOM   5226  C CE2 . TYR C 1 172 ? -38.282 56.199  -2.538  1.00 35.87 ? 168 TYR C CE2 1 
ATOM   5227  C CZ  . TYR C 1 172 ? -38.802 56.620  -3.748  1.00 35.89 ? 168 TYR C CZ  1 
ATOM   5228  O OH  . TYR C 1 172 ? -39.292 55.687  -4.633  1.00 35.75 ? 168 TYR C OH  1 
ATOM   5229  N N   . ASN C 1 173 ? -40.459 58.839  0.143   1.00 36.68 ? 169 ASN C N   1 
ATOM   5230  C CA  . ASN C 1 173 ? -41.384 57.795  0.562   1.00 36.75 ? 169 ASN C CA  1 
ATOM   5231  C C   . ASN C 1 173 ? -41.304 56.626  -0.419  1.00 36.53 ? 169 ASN C C   1 
ATOM   5232  O O   . ASN C 1 173 ? -41.410 56.826  -1.633  1.00 36.59 ? 169 ASN C O   1 
ATOM   5233  C CB  . ASN C 1 173 ? -42.819 58.336  0.570   1.00 36.88 ? 169 ASN C CB  1 
ATOM   5234  C CG  . ASN C 1 173 ? -43.552 58.062  1.875   1.00 37.81 ? 169 ASN C CG  1 
ATOM   5235  O OD1 . ASN C 1 173 ? -44.292 57.078  2.011   1.00 38.19 ? 169 ASN C OD1 1 
ATOM   5236  N ND2 . ASN C 1 173 ? -43.358 58.955  2.848   1.00 39.52 ? 169 ASN C ND2 1 
ATOM   5237  N N   . ASN C 1 174 ? -41.120 55.413  0.093   1.00 36.18 ? 170 ASN C N   1 
ATOM   5238  C CA  . ASN C 1 174 ? -41.111 54.231  -0.765  1.00 36.11 ? 170 ASN C CA  1 
ATOM   5239  C C   . ASN C 1 174 ? -42.537 53.772  -1.097  1.00 36.10 ? 170 ASN C C   1 
ATOM   5240  O O   . ASN C 1 174 ? -43.095 52.897  -0.426  1.00 36.04 ? 170 ASN C O   1 
ATOM   5241  C CB  . ASN C 1 174 ? -40.283 53.106  -0.132  1.00 35.95 ? 170 ASN C CB  1 
ATOM   5242  C CG  . ASN C 1 174 ? -40.153 51.882  -1.029  1.00 36.03 ? 170 ASN C CG  1 
ATOM   5243  O OD1 . ASN C 1 174 ? -40.396 51.937  -2.237  1.00 36.07 ? 170 ASN C OD1 1 
ATOM   5244  N ND2 . ASN C 1 174 ? -39.755 50.765  -0.433  1.00 36.14 ? 170 ASN C ND2 1 
ATOM   5245  N N   . THR C 1 175 ? -43.113 54.377  -2.134  1.00 36.13 ? 171 THR C N   1 
ATOM   5246  C CA  . THR C 1 175 ? -44.482 54.076  -2.581  1.00 36.33 ? 171 THR C CA  1 
ATOM   5247  C C   . THR C 1 175 ? -44.600 52.716  -3.279  1.00 36.50 ? 171 THR C C   1 
ATOM   5248  O O   . THR C 1 175 ? -45.702 52.195  -3.447  1.00 36.73 ? 171 THR C O   1 
ATOM   5249  C CB  . THR C 1 175 ? -45.043 55.178  -3.525  1.00 36.29 ? 171 THR C CB  1 
ATOM   5250  O OG1 . THR C 1 175 ? -44.122 55.412  -4.599  1.00 36.42 ? 171 THR C OG1 1 
ATOM   5251  C CG2 . THR C 1 175 ? -45.273 56.487  -2.774  1.00 36.20 ? 171 THR C CG2 1 
ATOM   5252  N N   . ASN C 1 176 ? -43.462 52.147  -3.671  1.00 36.68 ? 172 ASN C N   1 
ATOM   5253  C CA  . ASN C 1 176 ? -43.404 50.852  -4.352  1.00 36.70 ? 172 ASN C CA  1 
ATOM   5254  C C   . ASN C 1 176 ? -43.738 49.656  -3.449  1.00 37.02 ? 172 ASN C C   1 
ATOM   5255  O O   . ASN C 1 176 ? -43.805 49.786  -2.224  1.00 37.09 ? 172 ASN C O   1 
ATOM   5256  C CB  . ASN C 1 176 ? -42.023 50.669  -4.973  1.00 36.61 ? 172 ASN C CB  1 
ATOM   5257  C CG  . ASN C 1 176 ? -41.582 51.878  -5.767  1.00 36.60 ? 172 ASN C CG  1 
ATOM   5258  O OD1 . ASN C 1 176 ? -41.966 52.048  -6.924  1.00 36.80 ? 172 ASN C OD1 1 
ATOM   5259  N ND2 . ASN C 1 176 ? -40.766 52.726  -5.149  1.00 36.41 ? 172 ASN C ND2 1 
ATOM   5260  N N   . GLN C 1 177 ? -43.955 48.498  -4.067  1.00 37.33 ? 173 GLN C N   1 
ATOM   5261  C CA  . GLN C 1 177 ? -44.294 47.267  -3.349  1.00 37.76 ? 173 GLN C CA  1 
ATOM   5262  C C   . GLN C 1 177 ? -43.046 46.518  -2.882  1.00 37.61 ? 173 GLN C C   1 
ATOM   5263  O O   . GLN C 1 177 ? -43.123 45.644  -2.022  1.00 37.92 ? 173 GLN C O   1 
ATOM   5264  C CB  . GLN C 1 177 ? -45.131 46.341  -4.245  1.00 38.17 ? 173 GLN C CB  1 
ATOM   5265  C CG  . GLN C 1 177 ? -46.546 46.826  -4.533  1.00 39.53 ? 173 GLN C CG  1 
ATOM   5266  C CD  . GLN C 1 177 ? -47.477 46.633  -3.350  1.00 41.41 ? 173 GLN C CD  1 
ATOM   5267  O OE1 . GLN C 1 177 ? -47.710 47.562  -2.572  1.00 42.64 ? 173 GLN C OE1 1 
ATOM   5268  N NE2 . GLN C 1 177 ? -48.004 45.419  -3.198  1.00 41.72 ? 173 GLN C NE2 1 
ATOM   5269  N N   . GLU C 1 178 ? -41.905 46.866  -3.463  1.00 37.35 ? 174 GLU C N   1 
ATOM   5270  C CA  . GLU C 1 178 ? -40.649 46.170  -3.218  1.00 37.15 ? 174 GLU C CA  1 
ATOM   5271  C C   . GLU C 1 178 ? -39.766 46.912  -2.214  1.00 36.56 ? 174 GLU C C   1 
ATOM   5272  O O   . GLU C 1 178 ? -39.857 48.137  -2.080  1.00 36.38 ? 174 GLU C O   1 
ATOM   5273  C CB  . GLU C 1 178 ? -39.873 46.015  -4.535  1.00 37.39 ? 174 GLU C CB  1 
ATOM   5274  C CG  . GLU C 1 178 ? -40.548 45.135  -5.589  1.00 38.51 ? 174 GLU C CG  1 
ATOM   5275  C CD  . GLU C 1 178 ? -41.669 45.838  -6.352  1.00 39.57 ? 174 GLU C CD  1 
ATOM   5276  O OE1 . GLU C 1 178 ? -42.464 45.130  -7.004  1.00 40.06 ? 174 GLU C OE1 1 
ATOM   5277  O OE2 . GLU C 1 178 ? -41.765 47.086  -6.298  1.00 40.37 ? 174 GLU C OE2 1 
ATOM   5278  N N   . ASP C 1 179 ? -38.908 46.161  -1.521  1.00 35.75 ? 175 ASP C N   1 
ATOM   5279  C CA  . ASP C 1 179 ? -37.805 46.745  -0.757  1.00 34.96 ? 175 ASP C CA  1 
ATOM   5280  C C   . ASP C 1 179 ? -36.923 47.556  -1.701  1.00 34.24 ? 175 ASP C C   1 
ATOM   5281  O O   . ASP C 1 179 ? -36.817 47.238  -2.891  1.00 34.25 ? 175 ASP C O   1 
ATOM   5282  C CB  . ASP C 1 179 ? -36.951 45.660  -0.096  1.00 34.98 ? 175 ASP C CB  1 
ATOM   5283  C CG  . ASP C 1 179 ? -37.655 44.956  1.048   1.00 35.92 ? 175 ASP C CG  1 
ATOM   5284  O OD1 . ASP C 1 179 ? -38.661 45.475  1.578   1.00 37.24 ? 175 ASP C OD1 1 
ATOM   5285  O OD2 . ASP C 1 179 ? -37.179 43.866  1.434   1.00 37.23 ? 175 ASP C OD2 1 
ATOM   5286  N N   . LEU C 1 180 ? -36.282 48.587  -1.162  1.00 33.33 ? 176 LEU C N   1 
ATOM   5287  C CA  . LEU C 1 180 ? -35.434 49.465  -1.947  1.00 32.68 ? 176 LEU C CA  1 
ATOM   5288  C C   . LEU C 1 180 ? -34.013 49.520  -1.381  1.00 32.18 ? 176 LEU C C   1 
ATOM   5289  O O   . LEU C 1 180 ? -33.825 49.776  -0.191  1.00 32.10 ? 176 LEU C O   1 
ATOM   5290  C CB  . LEU C 1 180 ? -36.043 50.868  -1.954  1.00 32.77 ? 176 LEU C CB  1 
ATOM   5291  C CG  . LEU C 1 180 ? -36.022 51.670  -3.248  1.00 32.89 ? 176 LEU C CG  1 
ATOM   5292  C CD1 . LEU C 1 180 ? -37.128 51.193  -4.183  1.00 32.80 ? 176 LEU C CD1 1 
ATOM   5293  C CD2 . LEU C 1 180 ? -36.199 53.134  -2.924  1.00 33.60 ? 176 LEU C CD2 1 
ATOM   5294  N N   . LEU C 1 181 ? -33.021 49.264  -2.231  1.00 31.53 ? 177 LEU C N   1 
ATOM   5295  C CA  . LEU C 1 181 ? -31.623 49.480  -1.867  1.00 30.79 ? 177 LEU C CA  1 
ATOM   5296  C C   . LEU C 1 181 ? -31.250 50.935  -2.146  1.00 30.55 ? 177 LEU C C   1 
ATOM   5297  O O   . LEU C 1 181 ? -31.198 51.355  -3.304  1.00 30.43 ? 177 LEU C O   1 
ATOM   5298  C CB  . LEU C 1 181 ? -30.691 48.541  -2.644  1.00 30.50 ? 177 LEU C CB  1 
ATOM   5299  C CG  . LEU C 1 181 ? -29.176 48.694  -2.398  1.00 29.99 ? 177 LEU C CG  1 
ATOM   5300  C CD1 . LEU C 1 181 ? -28.782 48.345  -0.961  1.00 28.59 ? 177 LEU C CD1 1 
ATOM   5301  C CD2 . LEU C 1 181 ? -28.368 47.865  -3.382  1.00 29.17 ? 177 LEU C CD2 1 
ATOM   5302  N N   . VAL C 1 182 ? -30.999 51.697  -1.084  1.00 30.11 ? 178 VAL C N   1 
ATOM   5303  C CA  . VAL C 1 182 ? -30.665 53.121  -1.213  1.00 29.70 ? 178 VAL C CA  1 
ATOM   5304  C C   . VAL C 1 182 ? -29.195 53.340  -0.870  1.00 29.52 ? 178 VAL C C   1 
ATOM   5305  O O   . VAL C 1 182 ? -28.714 52.840  0.148   1.00 29.58 ? 178 VAL C O   1 
ATOM   5306  C CB  . VAL C 1 182 ? -31.553 54.014  -0.303  1.00 29.49 ? 178 VAL C CB  1 
ATOM   5307  C CG1 . VAL C 1 182 ? -31.362 55.484  -0.634  1.00 29.49 ? 178 VAL C CG1 1 
ATOM   5308  C CG2 . VAL C 1 182 ? -33.019 53.639  -0.433  1.00 29.14 ? 178 VAL C CG2 1 
ATOM   5309  N N   . LEU C 1 183 ? -28.496 54.092  -1.720  1.00 29.25 ? 179 LEU C N   1 
ATOM   5310  C CA  . LEU C 1 183 ? -27.081 54.394  -1.523  1.00 29.05 ? 179 LEU C CA  1 
ATOM   5311  C C   . LEU C 1 183 ? -26.808 55.897  -1.385  1.00 28.99 ? 179 LEU C C   1 
ATOM   5312  O O   . LEU C 1 183 ? -27.449 56.720  -2.042  1.00 28.76 ? 179 LEU C O   1 
ATOM   5313  C CB  . LEU C 1 183 ? -26.257 53.840  -2.681  1.00 29.15 ? 179 LEU C CB  1 
ATOM   5314  C CG  . LEU C 1 183 ? -26.651 52.486  -3.283  1.00 30.02 ? 179 LEU C CG  1 
ATOM   5315  C CD1 . LEU C 1 183 ? -26.034 52.348  -4.661  1.00 30.28 ? 179 LEU C CD1 1 
ATOM   5316  C CD2 . LEU C 1 183 ? -26.264 51.309  -2.383  1.00 29.96 ? 179 LEU C CD2 1 
ATOM   5317  N N   . TRP C 1 184 ? -25.851 56.240  -0.523  1.00 28.74 ? 180 TRP C N   1 
ATOM   5318  C CA  . TRP C 1 184 ? -25.372 57.613  -0.379  1.00 28.54 ? 180 TRP C CA  1 
ATOM   5319  C C   . TRP C 1 184 ? -23.922 57.615  0.096   1.00 28.76 ? 180 TRP C C   1 
ATOM   5320  O O   . TRP C 1 184 ? -23.333 56.550  0.335   1.00 28.70 ? 180 TRP C O   1 
ATOM   5321  C CB  . TRP C 1 184 ? -26.254 58.419  0.575   1.00 28.32 ? 180 TRP C CB  1 
ATOM   5322  C CG  . TRP C 1 184 ? -26.199 57.961  1.988   1.00 28.01 ? 180 TRP C CG  1 
ATOM   5323  C CD1 . TRP C 1 184 ? -25.435 58.484  2.990   1.00 27.19 ? 180 TRP C CD1 1 
ATOM   5324  C CD2 . TRP C 1 184 ? -26.946 56.890  2.570   1.00 28.28 ? 180 TRP C CD2 1 
ATOM   5325  N NE1 . TRP C 1 184 ? -25.654 57.805  4.157   1.00 26.61 ? 180 TRP C NE1 1 
ATOM   5326  C CE2 . TRP C 1 184 ? -26.577 56.819  3.933   1.00 27.69 ? 180 TRP C CE2 1 
ATOM   5327  C CE3 . TRP C 1 184 ? -27.894 55.981  2.074   1.00 28.30 ? 180 TRP C CE3 1 
ATOM   5328  C CZ2 . TRP C 1 184 ? -27.121 55.873  4.811   1.00 27.38 ? 180 TRP C CZ2 1 
ATOM   5329  C CZ3 . TRP C 1 184 ? -28.432 55.038  2.947   1.00 28.73 ? 180 TRP C CZ3 1 
ATOM   5330  C CH2 . TRP C 1 184 ? -28.040 54.993  4.303   1.00 27.98 ? 180 TRP C CH2 1 
ATOM   5331  N N   . GLY C 1 185 ? -23.345 58.805  0.231   1.00 28.41 ? 181 GLY C N   1 
ATOM   5332  C CA  . GLY C 1 185 ? -21.955 58.893  0.619   1.00 28.43 ? 181 GLY C CA  1 
ATOM   5333  C C   . GLY C 1 185 ? -21.538 60.151  1.343   1.00 28.38 ? 181 GLY C C   1 
ATOM   5334  O O   . GLY C 1 185 ? -22.297 61.116  1.459   1.00 28.47 ? 181 GLY C O   1 
ATOM   5335  N N   . ILE C 1 186 ? -20.309 60.116  1.838   1.00 28.22 ? 182 ILE C N   1 
ATOM   5336  C CA  . ILE C 1 186 ? -19.675 61.268  2.443   1.00 28.07 ? 182 ILE C CA  1 
ATOM   5337  C C   . ILE C 1 186 ? -18.306 61.449  1.793   1.00 28.19 ? 182 ILE C C   1 
ATOM   5338  O O   . ILE C 1 186 ? -17.627 60.471  1.474   1.00 27.86 ? 182 ILE C O   1 
ATOM   5339  C CB  . ILE C 1 186 ? -19.593 61.135  4.003   1.00 28.08 ? 182 ILE C CB  1 
ATOM   5340  C CG1 . ILE C 1 186 ? -18.926 62.362  4.634   1.00 27.87 ? 182 ILE C CG1 1 
ATOM   5341  C CG2 . ILE C 1 186 ? -18.903 59.832  4.429   1.00 27.79 ? 182 ILE C CG2 1 
ATOM   5342  C CD1 . ILE C 1 186 ? -19.258 62.558  6.107   1.00 28.10 ? 182 ILE C CD1 1 
ATOM   5343  N N   . HIS C 1 187 ? -17.928 62.702  1.559   1.00 28.42 ? 183 HIS C N   1 
ATOM   5344  C CA  . HIS C 1 187 ? -16.573 63.019  1.121   1.00 28.77 ? 183 HIS C CA  1 
ATOM   5345  C C   . HIS C 1 187 ? -15.696 63.438  2.304   1.00 28.88 ? 183 HIS C C   1 
ATOM   5346  O O   . HIS C 1 187 ? -16.102 64.265  3.125   1.00 28.89 ? 183 HIS C O   1 
ATOM   5347  C CB  . HIS C 1 187 ? -16.592 64.121  0.061   1.00 28.61 ? 183 HIS C CB  1 
ATOM   5348  C CG  . HIS C 1 187 ? -15.234 64.515  -0.426  1.00 28.32 ? 183 HIS C CG  1 
ATOM   5349  N ND1 . HIS C 1 187 ? -14.762 65.808  -0.351  1.00 29.19 ? 183 HIS C ND1 1 
ATOM   5350  C CD2 . HIS C 1 187 ? -14.244 63.785  -0.989  1.00 27.77 ? 183 HIS C CD2 1 
ATOM   5351  C CE1 . HIS C 1 187 ? -13.542 65.859  -0.857  1.00 28.74 ? 183 HIS C CE1 1 
ATOM   5352  N NE2 . HIS C 1 187 ? -13.206 64.645  -1.254  1.00 28.50 ? 183 HIS C NE2 1 
ATOM   5353  N N   . HIS C 1 188 ? -14.503 62.855  2.384   1.00 29.16 ? 184 HIS C N   1 
ATOM   5354  C CA  . HIS C 1 188 ? -13.497 63.270  3.367   1.00 29.49 ? 184 HIS C CA  1 
ATOM   5355  C C   . HIS C 1 188 ? -12.382 64.078  2.686   1.00 29.91 ? 184 HIS C C   1 
ATOM   5356  O O   . HIS C 1 188 ? -11.501 63.501  2.048   1.00 29.73 ? 184 HIS C O   1 
ATOM   5357  C CB  . HIS C 1 188 ? -12.895 62.060  4.091   1.00 29.20 ? 184 HIS C CB  1 
ATOM   5358  C CG  . HIS C 1 188 ? -13.904 61.165  4.741   1.00 28.66 ? 184 HIS C CG  1 
ATOM   5359  N ND1 . HIS C 1 188 ? -14.534 61.488  5.923   1.00 28.64 ? 184 HIS C ND1 1 
ATOM   5360  C CD2 . HIS C 1 188 ? -14.372 59.945  4.387   1.00 27.48 ? 184 HIS C CD2 1 
ATOM   5361  C CE1 . HIS C 1 188 ? -15.360 60.514  6.262   1.00 27.49 ? 184 HIS C CE1 1 
ATOM   5362  N NE2 . HIS C 1 188 ? -15.282 59.567  5.344   1.00 27.67 ? 184 HIS C NE2 1 
ATOM   5363  N N   . PRO C 1 189 ? -12.419 65.419  2.808   1.00 30.65 ? 185 PRO C N   1 
ATOM   5364  C CA  . PRO C 1 189 ? -11.365 66.261  2.219   1.00 31.44 ? 185 PRO C CA  1 
ATOM   5365  C C   . PRO C 1 189 ? -10.008 66.116  2.921   1.00 32.36 ? 185 PRO C C   1 
ATOM   5366  O O   . PRO C 1 189 ? -9.931  65.525  4.003   1.00 32.27 ? 185 PRO C O   1 
ATOM   5367  C CB  . PRO C 1 189 ? -11.914 67.685  2.375   1.00 31.23 ? 185 PRO C CB  1 
ATOM   5368  C CG  . PRO C 1 189 ? -12.938 67.604  3.425   1.00 30.87 ? 185 PRO C CG  1 
ATOM   5369  C CD  . PRO C 1 189 ? -13.509 66.221  3.386   1.00 30.68 ? 185 PRO C CD  1 
ATOM   5370  N N   . ASN C 1 190 ? -8.950  66.645  2.307   1.00 33.62 ? 186 ASN C N   1 
ATOM   5371  C CA  . ASN C 1 190 ? -7.597  66.515  2.869   1.00 34.90 ? 186 ASN C CA  1 
ATOM   5372  C C   . ASN C 1 190 ? -7.123  67.592  3.850   1.00 35.37 ? 186 ASN C C   1 
ATOM   5373  O O   . ASN C 1 190 ? -6.199  67.346  4.627   1.00 35.59 ? 186 ASN C O   1 
ATOM   5374  C CB  . ASN C 1 190 ? -6.538  66.260  1.787   1.00 35.26 ? 186 ASN C CB  1 
ATOM   5375  C CG  . ASN C 1 190 ? -6.884  66.882  0.455   1.00 36.60 ? 186 ASN C CG  1 
ATOM   5376  O OD1 . ASN C 1 190 ? -7.163  66.173  -0.512  1.00 37.21 ? 186 ASN C OD1 1 
ATOM   5377  N ND2 . ASN C 1 190 ? -6.848  68.211  0.388   1.00 38.49 ? 186 ASN C ND2 1 
ATOM   5378  N N   . ASP C 1 191 ? -7.749  68.769  3.827   1.00 35.96 ? 187 ASP C N   1 
ATOM   5379  C CA  . ASP C 1 191 ? -7.406  69.847  4.772   1.00 36.46 ? 187 ASP C CA  1 
ATOM   5380  C C   . ASP C 1 191 ? -8.553  70.836  4.966   1.00 36.45 ? 187 ASP C C   1 
ATOM   5381  O O   . ASP C 1 191 ? -9.448  70.921  4.127   1.00 36.73 ? 187 ASP C O   1 
ATOM   5382  C CB  . ASP C 1 191 ? -6.119  70.576  4.349   1.00 36.48 ? 187 ASP C CB  1 
ATOM   5383  C CG  . ASP C 1 191 ? -6.167  71.074  2.914   1.00 37.88 ? 187 ASP C CG  1 
ATOM   5384  O OD1 . ASP C 1 191 ? -5.385  70.567  2.079   1.00 39.64 ? 187 ASP C OD1 1 
ATOM   5385  O OD2 . ASP C 1 191 ? -6.988  71.967  2.612   1.00 39.21 ? 187 ASP C OD2 1 
ATOM   5386  N N   . ALA C 1 192 ? -8.510  71.578  6.073   1.00 36.52 ? 188 ALA C N   1 
ATOM   5387  C CA  . ALA C 1 192 ? -9.518  72.586  6.411   1.00 36.78 ? 188 ALA C CA  1 
ATOM   5388  C C   . ALA C 1 192 ? -9.826  73.559  5.273   1.00 37.09 ? 188 ALA C C   1 
ATOM   5389  O O   . ALA C 1 192 ? -10.973 73.997  5.113   1.00 37.02 ? 188 ALA C O   1 
ATOM   5390  C CB  . ALA C 1 192 ? -9.096  73.357  7.661   1.00 36.58 ? 188 ALA C CB  1 
ATOM   5391  N N   . ALA C 1 193 ? -8.796  73.894  4.496   1.00 37.44 ? 189 ALA C N   1 
ATOM   5392  C CA  . ALA C 1 193 ? -8.918  74.835  3.391   1.00 37.65 ? 189 ALA C CA  1 
ATOM   5393  C C   . ALA C 1 193 ? -9.799  74.271  2.282   1.00 38.00 ? 189 ALA C C   1 
ATOM   5394  O O   . ALA C 1 193 ? -10.539 75.018  1.630   1.00 38.27 ? 189 ALA C O   1 
ATOM   5395  C CB  . ALA C 1 193 ? -7.541  75.212  2.848   1.00 37.44 ? 189 ALA C CB  1 
ATOM   5396  N N   . GLU C 1 194 ? -9.722  72.957  2.076   1.00 38.10 ? 190 GLU C N   1 
ATOM   5397  C CA  . GLU C 1 194 ? -10.552 72.293  1.077   1.00 38.29 ? 190 GLU C CA  1 
ATOM   5398  C C   . GLU C 1 194 ? -12.026 72.286  1.504   1.00 38.06 ? 190 GLU C C   1 
ATOM   5399  O O   . GLU C 1 194 ? -12.907 72.530  0.675   1.00 37.98 ? 190 GLU C O   1 
ATOM   5400  C CB  . GLU C 1 194 ? -10.040 70.882  0.779   1.00 38.44 ? 190 GLU C CB  1 
ATOM   5401  C CG  . GLU C 1 194 ? -10.309 70.423  -0.652  1.00 40.13 ? 190 GLU C CG  1 
ATOM   5402  C CD  . GLU C 1 194 ? -9.654  69.088  -0.984  1.00 42.47 ? 190 GLU C CD  1 
ATOM   5403  O OE1 . GLU C 1 194 ? -10.085 68.044  -0.441  1.00 43.28 ? 190 GLU C OE1 1 
ATOM   5404  O OE2 . GLU C 1 194 ? -8.706  69.081  -1.797  1.00 43.68 ? 190 GLU C OE2 1 
ATOM   5405  N N   . GLN C 1 195 ? -12.281 72.021  2.789   1.00 37.82 ? 191 GLN C N   1 
ATOM   5406  C CA  . GLN C 1 195 ? -13.634 72.105  3.364   1.00 37.78 ? 191 GLN C CA  1 
ATOM   5407  C C   . GLN C 1 195 ? -14.390 73.340  2.888   1.00 37.97 ? 191 GLN C C   1 
ATOM   5408  O O   . GLN C 1 195 ? -15.446 73.227  2.259   1.00 37.70 ? 191 GLN C O   1 
ATOM   5409  C CB  . GLN C 1 195 ? -13.589 72.142  4.896   1.00 37.46 ? 191 GLN C CB  1 
ATOM   5410  C CG  . GLN C 1 195 ? -14.070 70.894  5.606   1.00 37.16 ? 191 GLN C CG  1 
ATOM   5411  C CD  . GLN C 1 195 ? -15.452 70.426  5.178   1.00 36.15 ? 191 GLN C CD  1 
ATOM   5412  O OE1 . GLN C 1 195 ? -15.585 69.358  4.598   1.00 36.00 ? 191 GLN C OE1 1 
ATOM   5413  N NE2 . GLN C 1 195 ? -16.480 71.212  5.476   1.00 35.64 ? 191 GLN C NE2 1 
ATOM   5414  N N   . THR C 1 196 ? -13.836 74.512  3.205   1.00 38.11 ? 192 THR C N   1 
ATOM   5415  C CA  . THR C 1 196 ? -14.464 75.790  2.879   1.00 38.40 ? 192 THR C CA  1 
ATOM   5416  C C   . THR C 1 196 ? -14.563 75.966  1.373   1.00 38.38 ? 192 THR C C   1 
ATOM   5417  O O   . THR C 1 196 ? -15.587 76.415  0.864   1.00 38.55 ? 192 THR C O   1 
ATOM   5418  C CB  . THR C 1 196 ? -13.703 76.988  3.494   1.00 38.46 ? 192 THR C CB  1 
ATOM   5419  O OG1 . THR C 1 196 ? -12.303 76.858  3.217   1.00 38.86 ? 192 THR C OG1 1 
ATOM   5420  C CG2 . THR C 1 196 ? -13.918 77.049  5.003   1.00 38.00 ? 192 THR C CG2 1 
ATOM   5421  N N   . LYS C 1 197 ? -13.498 75.589  0.670   1.00 38.42 ? 193 LYS C N   1 
ATOM   5422  C CA  . LYS C 1 197 ? -13.450 75.653  -0.787  1.00 38.53 ? 193 LYS C CA  1 
ATOM   5423  C C   . LYS C 1 197 ? -14.625 74.903  -1.418  1.00 38.21 ? 193 LYS C C   1 
ATOM   5424  O O   . LYS C 1 197 ? -15.276 75.424  -2.316  1.00 38.39 ? 193 LYS C O   1 
ATOM   5425  C CB  . LYS C 1 197 ? -12.103 75.106  -1.283  1.00 38.83 ? 193 LYS C CB  1 
ATOM   5426  C CG  . LYS C 1 197 ? -11.907 75.015  -2.795  1.00 40.30 ? 193 LYS C CG  1 
ATOM   5427  C CD  . LYS C 1 197 ? -10.551 74.360  -3.097  1.00 42.97 ? 193 LYS C CD  1 
ATOM   5428  C CE  . LYS C 1 197 ? -10.370 74.021  -4.576  1.00 44.36 ? 193 LYS C CE  1 
ATOM   5429  N NZ  . LYS C 1 197 ? -10.106 75.231  -5.408  1.00 45.37 ? 193 LYS C NZ  1 
ATOM   5430  N N   . LEU C 1 198 ? -14.911 73.697  -0.927  1.00 37.85 ? 194 LEU C N   1 
ATOM   5431  C CA  . LEU C 1 198 ? -15.938 72.848  -1.532  1.00 37.30 ? 194 LEU C CA  1 
ATOM   5432  C C   . LEU C 1 198 ? -17.332 73.043  -0.944  1.00 37.17 ? 194 LEU C C   1 
ATOM   5433  O O   . LEU C 1 198 ? -18.328 72.989  -1.673  1.00 37.05 ? 194 LEU C O   1 
ATOM   5434  C CB  . LEU C 1 198 ? -15.539 71.368  -1.457  1.00 37.29 ? 194 LEU C CB  1 
ATOM   5435  C CG  . LEU C 1 198 ? -14.367 70.835  -2.297  1.00 36.99 ? 194 LEU C CG  1 
ATOM   5436  C CD1 . LEU C 1 198 ? -14.142 69.369  -1.988  1.00 37.50 ? 194 LEU C CD1 1 
ATOM   5437  C CD2 . LEU C 1 198 ? -14.574 71.025  -3.799  1.00 36.58 ? 194 LEU C CD2 1 
ATOM   5438  N N   . TYR C 1 199 ? -17.400 73.278  0.366   1.00 37.07 ? 195 TYR C N   1 
ATOM   5439  C CA  . TYR C 1 199 ? -18.672 73.232  1.102   1.00 36.95 ? 195 TYR C CA  1 
ATOM   5440  C C   . TYR C 1 199 ? -18.979 74.462  1.967   1.00 37.22 ? 195 TYR C C   1 
ATOM   5441  O O   . TYR C 1 199 ? -20.021 74.508  2.626   1.00 37.14 ? 195 TYR C O   1 
ATOM   5442  C CB  . TYR C 1 199 ? -18.735 71.961  1.966   1.00 36.78 ? 195 TYR C CB  1 
ATOM   5443  C CG  . TYR C 1 199 ? -18.309 70.694  1.249   1.00 36.33 ? 195 TYR C CG  1 
ATOM   5444  C CD1 . TYR C 1 199 ? -17.128 70.033  1.602   1.00 35.37 ? 195 TYR C CD1 1 
ATOM   5445  C CD2 . TYR C 1 199 ? -19.080 70.161  0.213   1.00 35.95 ? 195 TYR C CD2 1 
ATOM   5446  C CE1 . TYR C 1 199 ? -16.726 68.871  0.944   1.00 35.02 ? 195 TYR C CE1 1 
ATOM   5447  C CE2 . TYR C 1 199 ? -18.688 69.001  -0.453  1.00 35.94 ? 195 TYR C CE2 1 
ATOM   5448  C CZ  . TYR C 1 199 ? -17.510 68.360  -0.084  1.00 35.51 ? 195 TYR C CZ  1 
ATOM   5449  O OH  . TYR C 1 199 ? -17.127 67.210  -0.743  1.00 34.54 ? 195 TYR C OH  1 
ATOM   5450  N N   . GLN C 1 200 ? -18.076 75.445  1.969   1.00 37.48 ? 196 GLN C N   1 
ATOM   5451  C CA  . GLN C 1 200 ? -18.234 76.690  2.737   1.00 37.80 ? 196 GLN C CA  1 
ATOM   5452  C C   . GLN C 1 200 ? -18.192 76.503  4.258   1.00 37.74 ? 196 GLN C C   1 
ATOM   5453  O O   . GLN C 1 200 ? -17.335 77.073  4.929   1.00 37.99 ? 196 GLN C O   1 
ATOM   5454  C CB  . GLN C 1 200 ? -19.502 77.462  2.311   1.00 37.99 ? 196 GLN C CB  1 
ATOM   5455  C CG  . GLN C 1 200 ? -19.550 78.932  2.757   1.00 38.71 ? 196 GLN C CG  1 
ATOM   5456  C CD  . GLN C 1 200 ? -18.433 79.784  2.152   1.00 40.21 ? 196 GLN C CD  1 
ATOM   5457  O OE1 . GLN C 1 200 ? -18.069 79.628  0.980   1.00 40.44 ? 196 GLN C OE1 1 
ATOM   5458  N NE2 . GLN C 1 200 ? -17.887 80.691  2.955   1.00 40.40 ? 196 GLN C NE2 1 
ATOM   5459  N N   . ASN C 1 201 ? -19.118 75.709  4.787   1.00 37.78 ? 197 ASN C N   1 
ATOM   5460  C CA  . ASN C 1 201 ? -19.242 75.486  6.228   1.00 37.77 ? 197 ASN C CA  1 
ATOM   5461  C C   . ASN C 1 201 ? -18.095 74.645  6.789   1.00 37.85 ? 197 ASN C C   1 
ATOM   5462  O O   . ASN C 1 201 ? -17.728 73.633  6.194   1.00 37.96 ? 197 ASN C O   1 
ATOM   5463  C CB  . ASN C 1 201 ? -20.588 74.829  6.550   1.00 37.67 ? 197 ASN C CB  1 
ATOM   5464  C CG  . ASN C 1 201 ? -21.766 75.546  5.898   1.00 37.50 ? 197 ASN C CG  1 
ATOM   5465  O OD1 . ASN C 1 201 ? -21.975 76.741  6.104   1.00 37.81 ? 197 ASN C OD1 1 
ATOM   5466  N ND2 . ASN C 1 201 ? -22.540 74.814  5.109   1.00 37.06 ? 197 ASN C ND2 1 
ATOM   5467  N N   . PRO C 1 202 ? -17.523 75.062  7.936   1.00 38.02 ? 198 PRO C N   1 
ATOM   5468  C CA  . PRO C 1 202 ? -16.378 74.341  8.509   1.00 37.96 ? 198 PRO C CA  1 
ATOM   5469  C C   . PRO C 1 202 ? -16.771 73.045  9.223   1.00 37.87 ? 198 PRO C C   1 
ATOM   5470  O O   . PRO C 1 202 ? -16.108 72.024  9.046   1.00 38.00 ? 198 PRO C O   1 
ATOM   5471  C CB  . PRO C 1 202 ? -15.781 75.349  9.511   1.00 37.88 ? 198 PRO C CB  1 
ATOM   5472  C CG  . PRO C 1 202 ? -16.549 76.634  9.313   1.00 37.95 ? 198 PRO C CG  1 
ATOM   5473  C CD  . PRO C 1 202 ? -17.862 76.253  8.732   1.00 37.88 ? 198 PRO C CD  1 
ATOM   5474  N N   . THR C 1 203 ? -17.836 73.095  10.017  1.00 37.85 ? 199 THR C N   1 
ATOM   5475  C CA  . THR C 1 203 ? -18.299 71.939  10.783  1.00 38.04 ? 199 THR C CA  1 
ATOM   5476  C C   . THR C 1 203 ? -19.582 71.362  10.183  1.00 37.92 ? 199 THR C C   1 
ATOM   5477  O O   . THR C 1 203 ? -20.692 71.824  10.475  1.00 37.96 ? 199 THR C O   1 
ATOM   5478  C CB  . THR C 1 203 ? -18.515 72.293  12.276  1.00 37.95 ? 199 THR C CB  1 
ATOM   5479  O OG1 . THR C 1 203 ? -17.352 72.964  12.775  1.00 38.96 ? 199 THR C OG1 1 
ATOM   5480  C CG2 . THR C 1 203 ? -18.760 71.040  13.103  1.00 37.44 ? 199 THR C CG2 1 
ATOM   5481  N N   . THR C 1 204 ? -19.420 70.349  9.342   1.00 37.79 ? 200 THR C N   1 
ATOM   5482  C CA  . THR C 1 204 ? -20.566 69.734  8.688   1.00 37.73 ? 200 THR C CA  1 
ATOM   5483  C C   . THR C 1 204 ? -20.952 68.378  9.290   1.00 37.75 ? 200 THR C C   1 
ATOM   5484  O O   . THR C 1 204 ? -20.217 67.801  10.102  1.00 37.75 ? 200 THR C O   1 
ATOM   5485  C CB  . THR C 1 204 ? -20.369 69.615  7.159   1.00 37.65 ? 200 THR C CB  1 
ATOM   5486  O OG1 . THR C 1 204 ? -19.480 68.534  6.869   1.00 37.58 ? 200 THR C OG1 1 
ATOM   5487  C CG2 . THR C 1 204 ? -19.819 70.913  6.574   1.00 37.50 ? 200 THR C CG2 1 
ATOM   5488  N N   . TYR C 1 205 ? -22.128 67.900  8.893   1.00 37.61 ? 201 TYR C N   1 
ATOM   5489  C CA  . TYR C 1 205 ? -22.643 66.605  9.299   1.00 37.60 ? 201 TYR C CA  1 
ATOM   5490  C C   . TYR C 1 205 ? -23.565 66.083  8.197   1.00 37.27 ? 201 TYR C C   1 
ATOM   5491  O O   . TYR C 1 205 ? -23.998 66.848  7.325   1.00 37.24 ? 201 TYR C O   1 
ATOM   5492  C CB  . TYR C 1 205 ? -23.425 66.740  10.607  1.00 37.89 ? 201 TYR C CB  1 
ATOM   5493  C CG  . TYR C 1 205 ? -24.663 67.600  10.476  1.00 39.51 ? 201 TYR C CG  1 
ATOM   5494  C CD1 . TYR C 1 205 ? -25.886 67.040  10.094  1.00 41.04 ? 201 TYR C CD1 1 
ATOM   5495  C CD2 . TYR C 1 205 ? -24.611 68.980  10.709  1.00 41.06 ? 201 TYR C CD2 1 
ATOM   5496  C CE1 . TYR C 1 205 ? -27.027 67.825  9.953   1.00 42.04 ? 201 TYR C CE1 1 
ATOM   5497  C CE2 . TYR C 1 205 ? -25.751 69.777  10.572  1.00 41.95 ? 201 TYR C CE2 1 
ATOM   5498  C CZ  . TYR C 1 205 ? -26.953 69.190  10.195  1.00 42.53 ? 201 TYR C CZ  1 
ATOM   5499  O OH  . TYR C 1 205 ? -28.088 69.957  10.061  1.00 44.17 ? 201 TYR C OH  1 
ATOM   5500  N N   . ILE C 1 206 ? -23.858 64.784  8.232   1.00 36.65 ? 202 ILE C N   1 
ATOM   5501  C CA  . ILE C 1 206 ? -24.926 64.207  7.411   1.00 36.00 ? 202 ILE C CA  1 
ATOM   5502  C C   . ILE C 1 206 ? -25.758 63.309  8.309   1.00 35.65 ? 202 ILE C C   1 
ATOM   5503  O O   . ILE C 1 206 ? -25.234 62.369  8.901   1.00 35.61 ? 202 ILE C O   1 
ATOM   5504  C CB  . ILE C 1 206 ? -24.394 63.373  6.219   1.00 35.93 ? 202 ILE C CB  1 
ATOM   5505  C CG1 . ILE C 1 206 ? -23.412 64.178  5.371   1.00 35.93 ? 202 ILE C CG1 1 
ATOM   5506  C CG2 . ILE C 1 206 ? -25.546 62.879  5.350   1.00 35.74 ? 202 ILE C CG2 1 
ATOM   5507  C CD1 . ILE C 1 206 ? -22.564 63.329  4.444   1.00 36.25 ? 202 ILE C CD1 1 
ATOM   5508  N N   . SER C 1 207 ? -27.047 63.618  8.421   1.00 35.13 ? 203 SER C N   1 
ATOM   5509  C CA  . SER C 1 207 ? -27.982 62.785  9.158   1.00 34.75 ? 203 SER C CA  1 
ATOM   5510  C C   . SER C 1 207 ? -28.913 62.041  8.216   1.00 34.55 ? 203 SER C C   1 
ATOM   5511  O O   . SER C 1 207 ? -29.562 62.650  7.362   1.00 34.88 ? 203 SER C O   1 
ATOM   5512  C CB  . SER C 1 207 ? -28.802 63.624  10.134  1.00 34.90 ? 203 SER C CB  1 
ATOM   5513  O OG  . SER C 1 207 ? -28.268 63.550  11.444  1.00 35.55 ? 203 SER C OG  1 
ATOM   5514  N N   . VAL C 1 208 ? -28.966 60.721  8.379   1.00 34.10 ? 204 VAL C N   1 
ATOM   5515  C CA  . VAL C 1 208 ? -29.872 59.862  7.617   1.00 33.67 ? 204 VAL C CA  1 
ATOM   5516  C C   . VAL C 1 208 ? -30.875 59.185  8.557   1.00 33.54 ? 204 VAL C C   1 
ATOM   5517  O O   . VAL C 1 208 ? -30.519 58.735  9.649   1.00 33.63 ? 204 VAL C O   1 
ATOM   5518  C CB  . VAL C 1 208 ? -29.100 58.804  6.801   1.00 33.71 ? 204 VAL C CB  1 
ATOM   5519  C CG1 . VAL C 1 208 ? -30.051 58.009  5.900   1.00 33.89 ? 204 VAL C CG1 1 
ATOM   5520  C CG2 . VAL C 1 208 ? -28.024 59.467  5.956   1.00 33.30 ? 204 VAL C CG2 1 
ATOM   5521  N N   . GLY C 1 209 ? -32.134 59.130  8.138   1.00 33.26 ? 205 GLY C N   1 
ATOM   5522  C CA  . GLY C 1 209 ? -33.179 58.552  8.973   1.00 32.80 ? 205 GLY C CA  1 
ATOM   5523  C C   . GLY C 1 209 ? -34.217 57.771  8.195   1.00 32.72 ? 205 GLY C C   1 
ATOM   5524  O O   . GLY C 1 209 ? -34.731 58.240  7.179   1.00 32.83 ? 205 GLY C O   1 
ATOM   5525  N N   . THR C 1 210 ? -34.499 56.560  8.660   1.00 32.43 ? 206 THR C N   1 
ATOM   5526  C CA  . THR C 1 210 ? -35.699 55.840  8.254   1.00 32.13 ? 206 THR C CA  1 
ATOM   5527  C C   . THR C 1 210 ? -36.464 55.594  9.540   1.00 32.21 ? 206 THR C C   1 
ATOM   5528  O O   . THR C 1 210 ? -36.225 56.280  10.533  1.00 32.22 ? 206 THR C O   1 
ATOM   5529  C CB  . THR C 1 210 ? -35.403 54.505  7.517   1.00 31.91 ? 206 THR C CB  1 
ATOM   5530  O OG1 . THR C 1 210 ? -34.815 53.567  8.423   1.00 31.71 ? 206 THR C OG1 1 
ATOM   5531  C CG2 . THR C 1 210 ? -34.479 54.719  6.333   1.00 31.34 ? 206 THR C CG2 1 
ATOM   5532  N N   . SER C 1 211 ? -37.373 54.629  9.541   1.00 32.31 ? 207 SER C N   1 
ATOM   5533  C CA  . SER C 1 211 ? -38.110 54.329  10.755  1.00 32.67 ? 207 SER C CA  1 
ATOM   5534  C C   . SER C 1 211 ? -37.309 53.416  11.691  1.00 32.68 ? 207 SER C C   1 
ATOM   5535  O O   . SER C 1 211 ? -37.686 53.239  12.846  1.00 32.79 ? 207 SER C O   1 
ATOM   5536  C CB  . SER C 1 211 ? -39.470 53.713  10.428  1.00 32.62 ? 207 SER C CB  1 
ATOM   5537  O OG  . SER C 1 211 ? -39.332 52.337  10.126  1.00 33.82 ? 207 SER C OG  1 
ATOM   5538  N N   . THR C 1 212 ? -36.219 52.837  11.183  1.00 32.70 ? 208 THR C N   1 
ATOM   5539  C CA  . THR C 1 212 ? -35.376 51.924  11.963  1.00 32.81 ? 208 THR C CA  1 
ATOM   5540  C C   . THR C 1 212 ? -33.912 52.351  11.953  1.00 32.93 ? 208 THR C C   1 
ATOM   5541  O O   . THR C 1 212 ? -33.175 52.062  12.896  1.00 33.12 ? 208 THR C O   1 
ATOM   5542  C CB  . THR C 1 212 ? -35.459 50.442  11.471  1.00 32.85 ? 208 THR C CB  1 
ATOM   5543  O OG1 . THR C 1 212 ? -34.880 50.329  10.168  1.00 32.74 ? 208 THR C OG1 1 
ATOM   5544  C CG2 . THR C 1 212 ? -36.903 49.930  11.434  1.00 32.85 ? 208 THR C CG2 1 
ATOM   5545  N N   . LEU C 1 213 ? -33.491 53.015  10.878  1.00 33.02 ? 209 LEU C N   1 
ATOM   5546  C CA  . LEU C 1 213 ? -32.135 53.532  10.775  1.00 33.12 ? 209 LEU C CA  1 
ATOM   5547  C C   . LEU C 1 213 ? -32.045 54.950  11.333  1.00 33.55 ? 209 LEU C C   1 
ATOM   5548  O O   . LEU C 1 213 ? -32.856 55.818  11.002  1.00 33.37 ? 209 LEU C O   1 
ATOM   5549  C CB  . LEU C 1 213 ? -31.639 53.500  9.327   1.00 32.90 ? 209 LEU C CB  1 
ATOM   5550  C CG  . LEU C 1 213 ? -30.225 54.034  9.034   1.00 32.85 ? 209 LEU C CG  1 
ATOM   5551  C CD1 . LEU C 1 213 ? -29.123 53.162  9.651   1.00 31.42 ? 209 LEU C CD1 1 
ATOM   5552  C CD2 . LEU C 1 213 ? -30.003 54.199  7.533   1.00 31.95 ? 209 LEU C CD2 1 
ATOM   5553  N N   . ASN C 1 214 ? -31.052 55.162  12.192  1.00 34.06 ? 210 ASN C N   1 
ATOM   5554  C CA  . ASN C 1 214 ? -30.732 56.479  12.719  1.00 34.53 ? 210 ASN C CA  1 
ATOM   5555  C C   . ASN C 1 214 ? -29.228 56.647  12.795  1.00 34.90 ? 210 ASN C C   1 
ATOM   5556  O O   . ASN C 1 214 ? -28.595 56.165  13.736  1.00 35.06 ? 210 ASN C O   1 
ATOM   5557  C CB  . ASN C 1 214 ? -31.355 56.674  14.101  1.00 34.56 ? 210 ASN C CB  1 
ATOM   5558  C CG  . ASN C 1 214 ? -31.097 58.060  14.672  1.00 34.91 ? 210 ASN C CG  1 
ATOM   5559  O OD1 . ASN C 1 214 ? -30.758 58.997  13.946  1.00 35.18 ? 210 ASN C OD1 1 
ATOM   5560  N ND2 . ASN C 1 214 ? -31.265 58.196  15.983  1.00 35.21 ? 210 ASN C ND2 1 
ATOM   5561  N N   . GLN C 1 215 ? -28.649 57.318  11.801  1.00 35.39 ? 211 GLN C N   1 
ATOM   5562  C CA  . GLN C 1 215 ? -27.206 57.536  11.811  1.00 36.06 ? 211 GLN C CA  1 
ATOM   5563  C C   . GLN C 1 215 ? -26.751 58.945  11.437  1.00 36.30 ? 211 GLN C C   1 
ATOM   5564  O O   . GLN C 1 215 ? -27.382 59.628  10.622  1.00 36.36 ? 211 GLN C O   1 
ATOM   5565  C CB  . GLN C 1 215 ? -26.479 56.480  10.972  1.00 36.25 ? 211 GLN C CB  1 
ATOM   5566  C CG  . GLN C 1 215 ? -26.539 56.663  9.469   1.00 37.07 ? 211 GLN C CG  1 
ATOM   5567  C CD  . GLN C 1 215 ? -25.648 55.676  8.721   1.00 38.73 ? 211 GLN C CD  1 
ATOM   5568  O OE1 . GLN C 1 215 ? -25.364 55.863  7.536   1.00 40.16 ? 211 GLN C OE1 1 
ATOM   5569  N NE2 . GLN C 1 215 ? -25.200 54.624  9.410   1.00 38.38 ? 211 GLN C NE2 1 
ATOM   5570  N N   . ARG C 1 216 ? -25.650 59.365  12.057  1.00 36.36 ? 212 ARG C N   1 
ATOM   5571  C CA  . ARG C 1 216 ? -25.000 60.622  11.724  1.00 36.46 ? 212 ARG C CA  1 
ATOM   5572  C C   . ARG C 1 216 ? -23.578 60.368  11.244  1.00 36.31 ? 212 ARG C C   1 
ATOM   5573  O O   . ARG C 1 216 ? -22.813 59.626  11.876  1.00 36.19 ? 212 ARG C O   1 
ATOM   5574  C CB  . ARG C 1 216 ? -24.982 61.560  12.930  1.00 36.66 ? 212 ARG C CB  1 
ATOM   5575  C CG  . ARG C 1 216 ? -24.700 63.020  12.592  1.00 37.98 ? 212 ARG C CG  1 
ATOM   5576  C CD  . ARG C 1 216 ? -24.663 63.834  13.872  1.00 41.42 ? 212 ARG C CD  1 
ATOM   5577  N NE  . ARG C 1 216 ? -24.917 65.267  13.701  1.00 43.02 ? 212 ARG C NE  1 
ATOM   5578  C CZ  . ARG C 1 216 ? -26.119 65.818  13.534  1.00 44.49 ? 212 ARG C CZ  1 
ATOM   5579  N NH1 . ARG C 1 216 ? -27.213 65.070  13.470  1.00 44.73 ? 212 ARG C NH1 1 
ATOM   5580  N NH2 . ARG C 1 216 ? -26.225 67.134  13.411  1.00 46.70 ? 212 ARG C NH2 1 
ATOM   5581  N N   . LEU C 1 217 ? -23.237 60.989  10.119  1.00 36.01 ? 213 LEU C N   1 
ATOM   5582  C CA  . LEU C 1 217 ? -21.880 60.955  9.590   1.00 35.81 ? 213 LEU C CA  1 
ATOM   5583  C C   . LEU C 1 217 ? -21.207 62.313  9.764   1.00 35.48 ? 213 LEU C C   1 
ATOM   5584  O O   . LEU C 1 217 ? -21.815 63.353  9.524   1.00 35.54 ? 213 LEU C O   1 
ATOM   5585  C CB  . LEU C 1 217 ? -21.888 60.564  8.108   1.00 35.81 ? 213 LEU C CB  1 
ATOM   5586  C CG  . LEU C 1 217 ? -22.699 59.333  7.694   1.00 36.09 ? 213 LEU C CG  1 
ATOM   5587  C CD1 . LEU C 1 217 ? -22.791 59.237  6.176   1.00 36.47 ? 213 LEU C CD1 1 
ATOM   5588  C CD2 . LEU C 1 217 ? -22.119 58.060  8.290   1.00 36.41 ? 213 LEU C CD2 1 
ATOM   5589  N N   . VAL C 1 218 ? -19.950 62.293  10.193  1.00 35.30 ? 214 VAL C N   1 
ATOM   5590  C CA  . VAL C 1 218 ? -19.138 63.506  10.300  1.00 35.05 ? 214 VAL C CA  1 
ATOM   5591  C C   . VAL C 1 218 ? -17.883 63.287  9.457   1.00 34.79 ? 214 VAL C C   1 
ATOM   5592  O O   . VAL C 1 218 ? -17.313 62.196  9.483   1.00 34.86 ? 214 VAL C O   1 
ATOM   5593  C CB  . VAL C 1 218 ? -18.765 63.817  11.779  1.00 35.08 ? 214 VAL C CB  1 
ATOM   5594  C CG1 . VAL C 1 218 ? -17.966 65.119  11.895  1.00 35.24 ? 214 VAL C CG1 1 
ATOM   5595  C CG2 . VAL C 1 218 ? -20.020 63.899  12.648  1.00 35.05 ? 214 VAL C CG2 1 
ATOM   5596  N N   . PRO C 1 219 ? -17.462 64.308  8.681   1.00 34.62 ? 215 PRO C N   1 
ATOM   5597  C CA  . PRO C 1 219 ? -16.229 64.171  7.892   1.00 34.50 ? 215 PRO C CA  1 
ATOM   5598  C C   . PRO C 1 219 ? -15.013 63.920  8.781   1.00 34.39 ? 215 PRO C C   1 
ATOM   5599  O O   . PRO C 1 219 ? -14.955 64.423  9.906   1.00 34.63 ? 215 PRO C O   1 
ATOM   5600  C CB  . PRO C 1 219 ? -16.085 65.537  7.217   1.00 34.32 ? 215 PRO C CB  1 
ATOM   5601  C CG  . PRO C 1 219 ? -17.417 66.128  7.248   1.00 34.20 ? 215 PRO C CG  1 
ATOM   5602  C CD  . PRO C 1 219 ? -18.113 65.610  8.457   1.00 34.31 ? 215 PRO C CD  1 
ATOM   5603  N N   . GLU C 1 220 ? -14.063 63.138  8.281   1.00 34.12 ? 216 GLU C N   1 
ATOM   5604  C CA  . GLU C 1 220 ? -12.816 62.896  8.992   1.00 33.96 ? 216 GLU C CA  1 
ATOM   5605  C C   . GLU C 1 220 ? -11.651 63.357  8.136   1.00 33.64 ? 216 GLU C C   1 
ATOM   5606  O O   . GLU C 1 220 ? -11.190 62.648  7.233   1.00 33.70 ? 216 GLU C O   1 
ATOM   5607  C CB  . GLU C 1 220 ? -12.677 61.423  9.395   1.00 34.25 ? 216 GLU C CB  1 
ATOM   5608  C CG  . GLU C 1 220 ? -13.571 61.019  10.571  1.00 35.12 ? 216 GLU C CG  1 
ATOM   5609  C CD  . GLU C 1 220 ? -13.423 59.558  10.964  1.00 37.01 ? 216 GLU C CD  1 
ATOM   5610  O OE1 . GLU C 1 220 ? -12.292 59.121  11.272  1.00 38.22 ? 216 GLU C OE1 1 
ATOM   5611  O OE2 . GLU C 1 220 ? -14.446 58.842  10.981  1.00 37.96 ? 216 GLU C OE2 1 
ATOM   5612  N N   . ILE C 1 221 ? -11.197 64.573  8.412   1.00 33.12 ? 217 ILE C N   1 
ATOM   5613  C CA  . ILE C 1 221 ? -10.118 65.171  7.641   1.00 32.73 ? 217 ILE C CA  1 
ATOM   5614  C C   . ILE C 1 221 ? -8.775  64.620  8.112   1.00 32.36 ? 217 ILE C C   1 
ATOM   5615  O O   . ILE C 1 221 ? -8.543  64.477  9.307   1.00 32.17 ? 217 ILE C O   1 
ATOM   5616  C CB  . ILE C 1 221 ? -10.178 66.712  7.699   1.00 32.73 ? 217 ILE C CB  1 
ATOM   5617  C CG1 . ILE C 1 221 ? -11.383 67.205  6.890   1.00 32.76 ? 217 ILE C CG1 1 
ATOM   5618  C CG2 . ILE C 1 221 ? -8.884  67.332  7.173   1.00 32.77 ? 217 ILE C CG2 1 
ATOM   5619  C CD1 . ILE C 1 221 ? -11.734 68.673  7.089   1.00 32.48 ? 217 ILE C CD1 1 
ATOM   5620  N N   . ALA C 1 222 ? -7.917  64.286  7.153   1.00 32.21 ? 218 ALA C N   1 
ATOM   5621  C CA  . ALA C 1 222 ? -6.605  63.710  7.427   1.00 32.24 ? 218 ALA C CA  1 
ATOM   5622  C C   . ALA C 1 222 ? -5.693  63.924  6.224   1.00 32.27 ? 218 ALA C C   1 
ATOM   5623  O O   . ALA C 1 222 ? -6.170  64.160  5.112   1.00 32.29 ? 218 ALA C O   1 
ATOM   5624  C CB  . ALA C 1 222 ? -6.731  62.217  7.751   1.00 32.18 ? 218 ALA C CB  1 
ATOM   5625  N N   . THR C 1 223 ? -4.385  63.854  6.456   1.00 32.08 ? 219 THR C N   1 
ATOM   5626  C CA  . THR C 1 223 ? -3.398  63.976  5.389   1.00 32.03 ? 219 THR C CA  1 
ATOM   5627  C C   . THR C 1 223 ? -3.069  62.580  4.883   1.00 32.00 ? 219 THR C C   1 
ATOM   5628  O O   . THR C 1 223 ? -2.718  61.699  5.666   1.00 32.03 ? 219 THR C O   1 
ATOM   5629  C CB  . THR C 1 223 ? -2.129  64.726  5.867   1.00 32.04 ? 219 THR C CB  1 
ATOM   5630  O OG1 . THR C 1 223 ? -2.506  66.025  6.324   1.00 32.05 ? 219 THR C OG1 1 
ATOM   5631  C CG2 . THR C 1 223 ? -1.109  64.885  4.738   1.00 31.71 ? 219 THR C CG2 1 
ATOM   5632  N N   . ARG C 1 224 ? -3.201  62.381  3.573   1.00 32.11 ? 220 ARG C N   1 
ATOM   5633  C CA  . ARG C 1 224 ? -3.193  61.038  2.985   1.00 31.95 ? 220 ARG C CA  1 
ATOM   5634  C C   . ARG C 1 224 ? -2.417  61.009  1.677   1.00 32.34 ? 220 ARG C C   1 
ATOM   5635  O O   . ARG C 1 224 ? -2.431  61.989  0.932   1.00 32.33 ? 220 ARG C O   1 
ATOM   5636  C CB  . ARG C 1 224 ? -4.627  60.557  2.719   1.00 31.59 ? 220 ARG C CB  1 
ATOM   5637  C CG  . ARG C 1 224 ? -5.619  60.770  3.856   1.00 30.89 ? 220 ARG C CG  1 
ATOM   5638  C CD  . ARG C 1 224 ? -7.017  60.306  3.464   1.00 30.59 ? 220 ARG C CD  1 
ATOM   5639  N NE  . ARG C 1 224 ? -8.064  60.926  4.274   1.00 29.89 ? 220 ARG C NE  1 
ATOM   5640  C CZ  . ARG C 1 224 ? -8.686  62.063  3.964   1.00 30.01 ? 220 ARG C CZ  1 
ATOM   5641  N NH1 . ARG C 1 224 ? -8.370  62.721  2.854   1.00 30.33 ? 220 ARG C NH1 1 
ATOM   5642  N NH2 . ARG C 1 224 ? -9.624  62.551  4.769   1.00 29.40 ? 220 ARG C NH2 1 
ATOM   5643  N N   . PRO C 1 225 ? -1.742  59.878  1.388   1.00 32.78 ? 221 PRO C N   1 
ATOM   5644  C CA  . PRO C 1 225 ? -1.099  59.681  0.090   1.00 33.33 ? 221 PRO C CA  1 
ATOM   5645  C C   . PRO C 1 225 ? -2.121  59.601  -1.040  1.00 34.09 ? 221 PRO C C   1 
ATOM   5646  O O   . PRO C 1 225 ? -3.287  59.262  -0.802  1.00 34.12 ? 221 PRO C O   1 
ATOM   5647  C CB  . PRO C 1 225 ? -0.401  58.324  0.244   1.00 33.13 ? 221 PRO C CB  1 
ATOM   5648  C CG  . PRO C 1 225 ? -0.268  58.119  1.700   1.00 32.90 ? 221 PRO C CG  1 
ATOM   5649  C CD  . PRO C 1 225 ? -1.476  58.753  2.301   1.00 32.73 ? 221 PRO C CD  1 
ATOM   5650  N N   . LYS C 1 226 ? -1.671  59.910  -2.253  1.00 34.89 ? 222 LYS C N   1 
ATOM   5651  C CA  . LYS C 1 226 ? -2.506  59.840  -3.447  1.00 35.72 ? 222 LYS C CA  1 
ATOM   5652  C C   . LYS C 1 226 ? -2.860  58.395  -3.780  1.00 36.14 ? 222 LYS C C   1 
ATOM   5653  O O   . LYS C 1 226 ? -1.979  57.540  -3.865  1.00 36.44 ? 222 LYS C O   1 
ATOM   5654  C CB  . LYS C 1 226 ? -1.783  60.457  -4.650  1.00 35.85 ? 222 LYS C CB  1 
ATOM   5655  C CG  . LYS C 1 226 ? -1.283  61.893  -4.469  1.00 36.81 ? 222 LYS C CG  1 
ATOM   5656  C CD  . LYS C 1 226 ? -2.344  62.922  -4.821  1.00 38.43 ? 222 LYS C CD  1 
ATOM   5657  C CE  . LYS C 1 226 ? -1.743  64.324  -4.947  1.00 40.09 ? 222 LYS C CE  1 
ATOM   5658  N NZ  . LYS C 1 226 ? -0.877  64.455  -6.158  1.00 40.81 ? 222 LYS C NZ  1 
ATOM   5659  N N   . VAL C 1 227 ? -4.154  58.130  -3.948  1.00 36.46 ? 223 VAL C N   1 
ATOM   5660  C CA  . VAL C 1 227 ? -4.633  56.896  -4.573  1.00 36.49 ? 223 VAL C CA  1 
ATOM   5661  C C   . VAL C 1 227 ? -5.476  57.324  -5.780  1.00 36.57 ? 223 VAL C C   1 
ATOM   5662  O O   . VAL C 1 227 ? -6.350  58.179  -5.646  1.00 36.40 ? 223 VAL C O   1 
ATOM   5663  C CB  . VAL C 1 227 ? -5.460  56.023  -3.592  1.00 36.69 ? 223 VAL C CB  1 
ATOM   5664  C CG1 . VAL C 1 227 ? -5.786  54.662  -4.218  1.00 36.11 ? 223 VAL C CG1 1 
ATOM   5665  C CG2 . VAL C 1 227 ? -4.713  55.834  -2.271  1.00 36.53 ? 223 VAL C CG2 1 
ATOM   5666  N N   . ASN C 1 228 ? -5.196  56.746  -6.951  1.00 36.69 ? 224 ASN C N   1 
ATOM   5667  C CA  . ASN C 1 228 ? -5.750  57.219  -8.235  1.00 36.83 ? 224 ASN C CA  1 
ATOM   5668  C C   . ASN C 1 228 ? -5.648  58.735  -8.391  1.00 36.76 ? 224 ASN C C   1 
ATOM   5669  O O   . ASN C 1 228 ? -6.585  59.384  -8.862  1.00 36.91 ? 224 ASN C O   1 
ATOM   5670  C CB  . ASN C 1 228 ? -7.211  56.780  -8.437  1.00 36.80 ? 224 ASN C CB  1 
ATOM   5671  C CG  . ASN C 1 228 ? -7.391  55.273  -8.390  1.00 37.20 ? 224 ASN C CG  1 
ATOM   5672  O OD1 . ASN C 1 228 ? -6.485  54.510  -8.729  1.00 37.77 ? 224 ASN C OD1 1 
ATOM   5673  N ND2 . ASN C 1 228 ? -8.574  54.838  -7.968  1.00 37.06 ? 224 ASN C ND2 1 
ATOM   5674  N N   . GLY C 1 229 ? -4.516  59.294  -7.973  1.00 36.69 ? 225 GLY C N   1 
ATOM   5675  C CA  . GLY C 1 229 ? -4.276  60.732  -8.072  1.00 36.47 ? 225 GLY C CA  1 
ATOM   5676  C C   . GLY C 1 229 ? -5.004  61.602  -7.060  1.00 36.41 ? 225 GLY C C   1 
ATOM   5677  O O   . GLY C 1 229 ? -4.930  62.824  -7.140  1.00 36.72 ? 225 GLY C O   1 
ATOM   5678  N N   . GLN C 1 230 ? -5.701  60.989  -6.104  1.00 36.32 ? 226 GLN C N   1 
ATOM   5679  C CA  . GLN C 1 230 ? -6.468  61.745  -5.104  1.00 36.16 ? 226 GLN C CA  1 
ATOM   5680  C C   . GLN C 1 230 ? -6.039  61.448  -3.672  1.00 35.90 ? 226 GLN C C   1 
ATOM   5681  O O   . GLN C 1 230 ? -5.829  60.288  -3.301  1.00 36.06 ? 226 GLN C O   1 
ATOM   5682  C CB  . GLN C 1 230 ? -7.972  61.484  -5.242  1.00 36.21 ? 226 GLN C CB  1 
ATOM   5683  C CG  . GLN C 1 230 ? -8.576  61.845  -6.600  1.00 37.62 ? 226 GLN C CG  1 
ATOM   5684  C CD  . GLN C 1 230 ? -8.341  63.298  -7.004  1.00 39.37 ? 226 GLN C CD  1 
ATOM   5685  O OE1 . GLN C 1 230 ? -8.238  64.190  -6.157  1.00 39.92 ? 226 GLN C OE1 1 
ATOM   5686  N NE2 . GLN C 1 230 ? -8.260  63.540  -8.310  1.00 39.75 ? 226 GLN C NE2 1 
ATOM   5687  N N   . SER C 1 231 ? -5.915  62.506  -2.876  1.00 35.40 ? 227 SER C N   1 
ATOM   5688  C CA  . SER C 1 231 ? -5.661  62.388  -1.443  1.00 35.06 ? 227 SER C CA  1 
ATOM   5689  C C   . SER C 1 231 ? -6.970  62.401  -0.651  1.00 34.56 ? 227 SER C C   1 
ATOM   5690  O O   . SER C 1 231 ? -7.009  62.002  0.521   1.00 34.66 ? 227 SER C O   1 
ATOM   5691  C CB  . SER C 1 231 ? -4.731  63.510  -0.968  1.00 35.18 ? 227 SER C CB  1 
ATOM   5692  O OG  . SER C 1 231 ? -3.445  63.371  -1.555  1.00 36.02 ? 227 SER C OG  1 
ATOM   5693  N N   . GLY C 1 232 ? -8.039  62.861  -1.297  1.00 33.89 ? 228 GLY C N   1 
ATOM   5694  C CA  . GLY C 1 232 ? -9.376  62.797  -0.721  1.00 33.23 ? 228 GLY C CA  1 
ATOM   5695  C C   . GLY C 1 232 ? -9.889  61.372  -0.689  1.00 32.90 ? 228 GLY C C   1 
ATOM   5696  O O   . GLY C 1 232 ? -9.345  60.486  -1.358  1.00 32.69 ? 228 GLY C O   1 
ATOM   5697  N N   . ARG C 1 233 ? -10.933 61.146  0.101   1.00 32.70 ? 229 ARG C N   1 
ATOM   5698  C CA  . ARG C 1 233 ? -11.552 59.828  0.201   1.00 32.55 ? 229 ARG C CA  1 
ATOM   5699  C C   . ARG C 1 233 ? -13.056 59.963  0.165   1.00 32.63 ? 229 ARG C C   1 
ATOM   5700  O O   . ARG C 1 233 ? -13.601 61.014  0.505   1.00 32.78 ? 229 ARG C O   1 
ATOM   5701  C CB  . ARG C 1 233 ? -11.153 59.118  1.501   1.00 32.39 ? 229 ARG C CB  1 
ATOM   5702  C CG  . ARG C 1 233 ? -9.684  58.797  1.652   1.00 31.95 ? 229 ARG C CG  1 
ATOM   5703  C CD  . ARG C 1 233 ? -9.222  57.675  0.749   1.00 30.98 ? 229 ARG C CD  1 
ATOM   5704  N NE  . ARG C 1 233 ? -7.799  57.416  0.944   1.00 31.76 ? 229 ARG C NE  1 
ATOM   5705  C CZ  . ARG C 1 233 ? -6.814  58.011  0.271   1.00 32.20 ? 229 ARG C CZ  1 
ATOM   5706  N NH1 . ARG C 1 233 ? -7.079  58.917  -0.664  1.00 31.60 ? 229 ARG C NH1 1 
ATOM   5707  N NH2 . ARG C 1 233 ? -5.551  57.697  0.536   1.00 32.05 ? 229 ARG C NH2 1 
ATOM   5708  N N   . MET C 1 234 ? -13.726 58.891  -0.240  1.00 32.69 ? 230 MET C N   1 
ATOM   5709  C CA  . MET C 1 234 ? -15.176 58.825  -0.162  1.00 32.46 ? 230 MET C CA  1 
ATOM   5710  C C   . MET C 1 234 ? -15.630 57.521  0.471   1.00 32.27 ? 230 MET C C   1 
ATOM   5711  O O   . MET C 1 234 ? -15.161 56.433  0.109   1.00 32.43 ? 230 MET C O   1 
ATOM   5712  C CB  . MET C 1 234 ? -15.800 58.994  -1.538  1.00 32.60 ? 230 MET C CB  1 
ATOM   5713  C CG  . MET C 1 234 ? -15.881 60.434  -1.977  1.00 33.64 ? 230 MET C CG  1 
ATOM   5714  S SD  . MET C 1 234 ? -16.652 60.624  -3.589  1.00 34.74 ? 230 MET C SD  1 
ATOM   5715  C CE  . MET C 1 234 ? -16.547 62.405  -3.760  1.00 34.92 ? 230 MET C CE  1 
ATOM   5716  N N   . GLU C 1 235 ? -16.551 57.648  1.418   1.00 31.68 ? 231 GLU C N   1 
ATOM   5717  C CA  . GLU C 1 235 ? -17.104 56.518  2.132   1.00 31.25 ? 231 GLU C CA  1 
ATOM   5718  C C   . GLU C 1 235 ? -18.581 56.395  1.770   1.00 30.66 ? 231 GLU C C   1 
ATOM   5719  O O   . GLU C 1 235 ? -19.351 57.358  1.890   1.00 30.25 ? 231 GLU C O   1 
ATOM   5720  C CB  . GLU C 1 235 ? -16.919 56.720  3.636   1.00 31.47 ? 231 GLU C CB  1 
ATOM   5721  C CG  . GLU C 1 235 ? -16.908 55.446  4.467   1.00 33.07 ? 231 GLU C CG  1 
ATOM   5722  C CD  . GLU C 1 235 ? -16.565 55.700  5.937   1.00 35.42 ? 231 GLU C CD  1 
ATOM   5723  O OE1 . GLU C 1 235 ? -16.523 54.716  6.713   1.00 35.59 ? 231 GLU C OE1 1 
ATOM   5724  O OE2 . GLU C 1 235 ? -16.341 56.878  6.318   1.00 35.81 ? 231 GLU C OE2 1 
ATOM   5725  N N   . PHE C 1 236 ? -18.976 55.211  1.319   1.00 29.92 ? 232 PHE C N   1 
ATOM   5726  C CA  . PHE C 1 236 ? -20.349 55.004  0.900   1.00 29.29 ? 232 PHE C CA  1 
ATOM   5727  C C   . PHE C 1 236 ? -21.139 54.159  1.881   1.00 29.11 ? 232 PHE C C   1 
ATOM   5728  O O   . PHE C 1 236 ? -20.606 53.235  2.493   1.00 28.95 ? 232 PHE C O   1 
ATOM   5729  C CB  . PHE C 1 236 ? -20.399 54.432  -0.511  1.00 29.21 ? 232 PHE C CB  1 
ATOM   5730  C CG  . PHE C 1 236 ? -19.823 55.353  -1.544  1.00 29.34 ? 232 PHE C CG  1 
ATOM   5731  C CD1 . PHE C 1 236 ? -18.537 55.154  -2.032  1.00 29.69 ? 232 PHE C CD1 1 
ATOM   5732  C CD2 . PHE C 1 236 ? -20.557 56.440  -2.012  1.00 28.41 ? 232 PHE C CD2 1 
ATOM   5733  C CE1 . PHE C 1 236 ? -17.999 56.015  -2.982  1.00 29.61 ? 232 PHE C CE1 1 
ATOM   5734  C CE2 . PHE C 1 236 ? -20.030 57.298  -2.953  1.00 28.29 ? 232 PHE C CE2 1 
ATOM   5735  C CZ  . PHE C 1 236 ? -18.748 57.089  -3.438  1.00 29.33 ? 232 PHE C CZ  1 
ATOM   5736  N N   . PHE C 1 237 ? -22.415 54.507  2.029   1.00 28.96 ? 233 PHE C N   1 
ATOM   5737  C CA  . PHE C 1 237 ? -23.315 53.840  2.957   1.00 28.95 ? 233 PHE C CA  1 
ATOM   5738  C C   . PHE C 1 237 ? -24.572 53.385  2.224   1.00 28.94 ? 233 PHE C C   1 
ATOM   5739  O O   . PHE C 1 237 ? -24.928 53.942  1.178   1.00 29.05 ? 233 PHE C O   1 
ATOM   5740  C CB  . PHE C 1 237 ? -23.653 54.770  4.128   1.00 28.84 ? 233 PHE C CB  1 
ATOM   5741  C CG  . PHE C 1 237 ? -22.449 55.157  4.959   1.00 29.71 ? 233 PHE C CG  1 
ATOM   5742  C CD1 . PHE C 1 237 ? -21.594 56.183  4.546   1.00 29.33 ? 233 PHE C CD1 1 
ATOM   5743  C CD2 . PHE C 1 237 ? -22.164 54.486  6.150   1.00 29.90 ? 233 PHE C CD2 1 
ATOM   5744  C CE1 . PHE C 1 237 ? -20.475 56.526  5.296   1.00 29.73 ? 233 PHE C CE1 1 
ATOM   5745  C CE2 . PHE C 1 237 ? -21.053 54.830  6.918   1.00 29.91 ? 233 PHE C CE2 1 
ATOM   5746  C CZ  . PHE C 1 237 ? -20.203 55.850  6.488   1.00 30.41 ? 233 PHE C CZ  1 
ATOM   5747  N N   . TRP C 1 238 ? -25.233 52.365  2.765   1.00 28.65 ? 234 TRP C N   1 
ATOM   5748  C CA  . TRP C 1 238 ? -26.464 51.852  2.175   1.00 28.49 ? 234 TRP C CA  1 
ATOM   5749  C C   . TRP C 1 238 ? -27.475 51.430  3.241   1.00 28.58 ? 234 TRP C C   1 
ATOM   5750  O O   . TRP C 1 238 ? -27.112 51.226  4.394   1.00 28.80 ? 234 TRP C O   1 
ATOM   5751  C CB  . TRP C 1 238 ? -26.147 50.678  1.248   1.00 28.41 ? 234 TRP C CB  1 
ATOM   5752  C CG  . TRP C 1 238 ? -25.572 49.491  1.968   1.00 27.65 ? 234 TRP C CG  1 
ATOM   5753  C CD1 . TRP C 1 238 ? -24.255 49.259  2.252   1.00 26.96 ? 234 TRP C CD1 1 
ATOM   5754  C CD2 . TRP C 1 238 ? -26.300 48.382  2.504   1.00 27.08 ? 234 TRP C CD2 1 
ATOM   5755  N NE1 . TRP C 1 238 ? -24.117 48.069  2.931   1.00 26.18 ? 234 TRP C NE1 1 
ATOM   5756  C CE2 . TRP C 1 238 ? -25.356 47.509  3.097   1.00 26.59 ? 234 TRP C CE2 1 
ATOM   5757  C CE3 . TRP C 1 238 ? -27.659 48.036  2.536   1.00 26.81 ? 234 TRP C CE3 1 
ATOM   5758  C CZ2 . TRP C 1 238 ? -25.728 46.313  3.714   1.00 25.85 ? 234 TRP C CZ2 1 
ATOM   5759  C CZ3 . TRP C 1 238 ? -28.027 46.846  3.150   1.00 27.05 ? 234 TRP C CZ3 1 
ATOM   5760  C CH2 . TRP C 1 238 ? -27.062 46.000  3.734   1.00 26.22 ? 234 TRP C CH2 1 
ATOM   5761  N N   . THR C 1 239 ? -28.742 51.316  2.844   1.00 28.52 ? 235 THR C N   1 
ATOM   5762  C CA  . THR C 1 239 ? -29.790 50.735  3.684   1.00 28.32 ? 235 THR C CA  1 
ATOM   5763  C C   . THR C 1 239 ? -30.908 50.147  2.826   1.00 28.61 ? 235 THR C C   1 
ATOM   5764  O O   . THR C 1 239 ? -31.028 50.470  1.642   1.00 28.79 ? 235 THR C O   1 
ATOM   5765  C CB  . THR C 1 239 ? -30.373 51.746  4.701   1.00 28.24 ? 235 THR C CB  1 
ATOM   5766  O OG1 . THR C 1 239 ? -31.189 51.050  5.647   1.00 28.13 ? 235 THR C OG1 1 
ATOM   5767  C CG2 . THR C 1 239 ? -31.219 52.819  4.018   1.00 28.48 ? 235 THR C CG2 1 
ATOM   5768  N N   . ILE C 1 240 ? -31.706 49.267  3.425   1.00 28.75 ? 236 ILE C N   1 
ATOM   5769  C CA  . ILE C 1 240 ? -32.889 48.740  2.779   1.00 28.89 ? 236 ILE C CA  1 
ATOM   5770  C C   . ILE C 1 240 ? -34.097 49.537  3.257   1.00 29.50 ? 236 ILE C C   1 
ATOM   5771  O O   . ILE C 1 240 ? -34.394 49.576  4.460   1.00 29.24 ? 236 ILE C O   1 
ATOM   5772  C CB  . ILE C 1 240 ? -33.070 47.220  3.057   1.00 29.03 ? 236 ILE C CB  1 
ATOM   5773  C CG1 . ILE C 1 240 ? -31.977 46.403  2.353   1.00 28.23 ? 236 ILE C CG1 1 
ATOM   5774  C CG2 . ILE C 1 240 ? -34.478 46.729  2.644   1.00 29.00 ? 236 ILE C CG2 1 
ATOM   5775  C CD1 . ILE C 1 240 ? -31.855 46.653  0.852   1.00 28.06 ? 236 ILE C CD1 1 
ATOM   5776  N N   . LEU C 1 241 ? -34.780 50.184  2.311   1.00 29.99 ? 237 LEU C N   1 
ATOM   5777  C CA  . LEU C 1 241 ? -35.991 50.940  2.615   1.00 30.43 ? 237 LEU C CA  1 
ATOM   5778  C C   . LEU C 1 241 ? -37.220 50.083  2.333   1.00 31.10 ? 237 LEU C C   1 
ATOM   5779  O O   . LEU C 1 241 ? -37.457 49.663  1.194   1.00 31.38 ? 237 LEU C O   1 
ATOM   5780  C CB  . LEU C 1 241 ? -36.032 52.260  1.829   1.00 30.20 ? 237 LEU C CB  1 
ATOM   5781  C CG  . LEU C 1 241 ? -37.141 53.286  2.114   1.00 29.43 ? 237 LEU C CG  1 
ATOM   5782  C CD1 . LEU C 1 241 ? -37.115 53.807  3.549   1.00 28.51 ? 237 LEU C CD1 1 
ATOM   5783  C CD2 . LEU C 1 241 ? -37.029 54.437  1.143   1.00 28.89 ? 237 LEU C CD2 1 
ATOM   5784  N N   . LYS C 1 242 ? -37.994 49.819  3.380   1.00 31.72 ? 238 LYS C N   1 
ATOM   5785  C CA  . LYS C 1 242 ? -39.165 48.945  3.275   1.00 32.43 ? 238 LYS C CA  1 
ATOM   5786  C C   . LYS C 1 242 ? -40.362 49.649  2.618   1.00 32.38 ? 238 LYS C C   1 
ATOM   5787  O O   . LYS C 1 242 ? -40.455 50.881  2.665   1.00 32.45 ? 238 LYS C O   1 
ATOM   5788  C CB  . LYS C 1 242 ? -39.538 48.388  4.657   1.00 32.67 ? 238 LYS C CB  1 
ATOM   5789  C CG  . LYS C 1 242 ? -38.558 47.334  5.157   1.00 34.01 ? 238 LYS C CG  1 
ATOM   5790  C CD  . LYS C 1 242 ? -39.148 46.500  6.272   1.00 36.86 ? 238 LYS C CD  1 
ATOM   5791  C CE  . LYS C 1 242 ? -38.239 45.327  6.597   1.00 39.74 ? 238 LYS C CE  1 
ATOM   5792  N NZ  . LYS C 1 242 ? -38.689 44.577  7.820   1.00 41.95 ? 238 LYS C NZ  1 
ATOM   5793  N N   . PRO C 1 243 ? -41.275 48.873  1.990   1.00 32.27 ? 239 PRO C N   1 
ATOM   5794  C CA  . PRO C 1 243 ? -42.447 49.490  1.370   1.00 32.13 ? 239 PRO C CA  1 
ATOM   5795  C C   . PRO C 1 243 ? -43.247 50.280  2.392   1.00 32.28 ? 239 PRO C C   1 
ATOM   5796  O O   . PRO C 1 243 ? -43.533 49.771  3.477   1.00 32.29 ? 239 PRO C O   1 
ATOM   5797  C CB  . PRO C 1 243 ? -43.250 48.289  0.863   1.00 32.04 ? 239 PRO C CB  1 
ATOM   5798  C CG  . PRO C 1 243 ? -42.226 47.229  0.639   1.00 32.16 ? 239 PRO C CG  1 
ATOM   5799  C CD  . PRO C 1 243 ? -41.255 47.414  1.775   1.00 32.09 ? 239 PRO C CD  1 
ATOM   5800  N N   . ASN C 1 244 ? -43.576 51.524  2.042   1.00 32.53 ? 240 ASN C N   1 
ATOM   5801  C CA  . ASN C 1 244 ? -44.301 52.452  2.922   1.00 32.83 ? 240 ASN C CA  1 
ATOM   5802  C C   . ASN C 1 244 ? -43.471 53.195  3.967   1.00 32.72 ? 240 ASN C C   1 
ATOM   5803  O O   . ASN C 1 244 ? -43.985 54.074  4.655   1.00 32.63 ? 240 ASN C O   1 
ATOM   5804  C CB  . ASN C 1 244 ? -45.501 51.782  3.586   1.00 33.12 ? 240 ASN C CB  1 
ATOM   5805  C CG  . ASN C 1 244 ? -46.802 52.383  3.146   1.00 34.26 ? 240 ASN C CG  1 
ATOM   5806  O OD1 . ASN C 1 244 ? -47.126 52.396  1.955   1.00 36.49 ? 240 ASN C OD1 1 
ATOM   5807  N ND2 . ASN C 1 244 ? -47.558 52.903  4.102   1.00 35.07 ? 240 ASN C ND2 1 
ATOM   5808  N N   . ASP C 1 245 ? -42.196 52.843  4.087   1.00 32.72 ? 241 ASP C N   1 
ATOM   5809  C CA  . ASP C 1 245 ? -41.295 53.586  4.953   1.00 32.66 ? 241 ASP C CA  1 
ATOM   5810  C C   . ASP C 1 245 ? -40.703 54.743  4.150   1.00 32.35 ? 241 ASP C C   1 
ATOM   5811  O O   . ASP C 1 245 ? -40.733 54.727  2.915   1.00 32.08 ? 241 ASP C O   1 
ATOM   5812  C CB  . ASP C 1 245 ? -40.199 52.674  5.520   1.00 32.79 ? 241 ASP C CB  1 
ATOM   5813  C CG  . ASP C 1 245 ? -39.590 53.210  6.817   1.00 33.95 ? 241 ASP C CG  1 
ATOM   5814  O OD1 . ASP C 1 245 ? -40.068 54.252  7.333   1.00 34.84 ? 241 ASP C OD1 1 
ATOM   5815  O OD2 . ASP C 1 245 ? -38.626 52.586  7.324   1.00 34.13 ? 241 ASP C OD2 1 
ATOM   5816  N N   . ALA C 1 246 ? -40.187 55.750  4.852   1.00 32.06 ? 242 ALA C N   1 
ATOM   5817  C CA  . ALA C 1 246 ? -39.552 56.890  4.202   1.00 32.07 ? 242 ALA C CA  1 
ATOM   5818  C C   . ALA C 1 246 ? -38.098 57.052  4.652   1.00 32.16 ? 242 ALA C C   1 
ATOM   5819  O O   . ALA C 1 246 ? -37.718 56.586  5.726   1.00 32.25 ? 242 ALA C O   1 
ATOM   5820  C CB  . ALA C 1 246 ? -40.343 58.165  4.468   1.00 31.85 ? 242 ALA C CB  1 
ATOM   5821  N N   . ILE C 1 247 ? -37.291 57.696  3.815   1.00 32.10 ? 243 ILE C N   1 
ATOM   5822  C CA  . ILE C 1 247 ? -35.922 58.030  4.175   1.00 32.03 ? 243 ILE C CA  1 
ATOM   5823  C C   . ILE C 1 247 ? -35.704 59.553  4.175   1.00 32.55 ? 243 ILE C C   1 
ATOM   5824  O O   . ILE C 1 247 ? -36.091 60.249  3.232   1.00 32.52 ? 243 ILE C O   1 
ATOM   5825  C CB  . ILE C 1 247 ? -34.880 57.260  3.301   1.00 31.81 ? 243 ILE C CB  1 
ATOM   5826  C CG1 . ILE C 1 247 ? -33.465 57.411  3.881   1.00 30.97 ? 243 ILE C CG1 1 
ATOM   5827  C CG2 . ILE C 1 247 ? -34.959 57.675  1.827   1.00 31.05 ? 243 ILE C CG2 1 
ATOM   5828  C CD1 . ILE C 1 247 ? -32.473 56.347  3.436   1.00 28.26 ? 243 ILE C CD1 1 
ATOM   5829  N N   . ASN C 1 248 ? -35.103 60.055  5.254   1.00 33.08 ? 244 ASN C N   1 
ATOM   5830  C CA  . ASN C 1 248 ? -34.828 61.485  5.420   1.00 33.46 ? 244 ASN C CA  1 
ATOM   5831  C C   . ASN C 1 248 ? -33.334 61.791  5.431   1.00 33.72 ? 244 ASN C C   1 
ATOM   5832  O O   . ASN C 1 248 ? -32.577 61.201  6.214   1.00 33.98 ? 244 ASN C O   1 
ATOM   5833  C CB  . ASN C 1 248 ? -35.460 62.015  6.712   1.00 33.47 ? 244 ASN C CB  1 
ATOM   5834  C CG  . ASN C 1 248 ? -36.987 62.078  6.655   1.00 33.87 ? 244 ASN C CG  1 
ATOM   5835  O OD1 . ASN C 1 248 ? -37.613 61.718  5.658   1.00 34.05 ? 244 ASN C OD1 1 
ATOM   5836  N ND2 . ASN C 1 248 ? -37.589 62.532  7.745   1.00 33.93 ? 244 ASN C ND2 1 
ATOM   5837  N N   . PHE C 1 249 ? -32.921 62.709  4.560   1.00 33.81 ? 245 PHE C N   1 
ATOM   5838  C CA  . PHE C 1 249 ? -31.540 63.179  4.508   1.00 33.99 ? 245 PHE C CA  1 
ATOM   5839  C C   . PHE C 1 249 ? -31.477 64.630  4.963   1.00 34.26 ? 245 PHE C C   1 
ATOM   5840  O O   . PHE C 1 249 ? -32.322 65.449  4.582   1.00 34.17 ? 245 PHE C O   1 
ATOM   5841  C CB  . PHE C 1 249 ? -30.956 63.053  3.094   1.00 34.04 ? 245 PHE C CB  1 
ATOM   5842  C CG  . PHE C 1 249 ? -30.832 61.634  2.607   1.00 34.21 ? 245 PHE C CG  1 
ATOM   5843  C CD1 . PHE C 1 249 ? -31.820 61.071  1.809   1.00 33.67 ? 245 PHE C CD1 1 
ATOM   5844  C CD2 . PHE C 1 249 ? -29.723 60.859  2.947   1.00 34.76 ? 245 PHE C CD2 1 
ATOM   5845  C CE1 . PHE C 1 249 ? -31.711 59.757  1.356   1.00 33.55 ? 245 PHE C CE1 1 
ATOM   5846  C CE2 . PHE C 1 249 ? -29.605 59.540  2.500   1.00 34.41 ? 245 PHE C CE2 1 
ATOM   5847  C CZ  . PHE C 1 249 ? -30.600 58.992  1.701   1.00 33.95 ? 245 PHE C CZ  1 
ATOM   5848  N N   . GLU C 1 250 ? -30.473 64.933  5.783   1.00 34.38 ? 246 GLU C N   1 
ATOM   5849  C CA  . GLU C 1 250 ? -30.261 66.273  6.302   1.00 34.44 ? 246 GLU C CA  1 
ATOM   5850  C C   . GLU C 1 250 ? -28.762 66.556  6.389   1.00 34.12 ? 246 GLU C C   1 
ATOM   5851  O O   . GLU C 1 250 ? -28.028 65.811  7.034   1.00 34.46 ? 246 GLU C O   1 
ATOM   5852  C CB  . GLU C 1 250 ? -30.923 66.410  7.667   1.00 34.56 ? 246 GLU C CB  1 
ATOM   5853  C CG  . GLU C 1 250 ? -31.123 67.846  8.117   1.00 35.86 ? 246 GLU C CG  1 
ATOM   5854  C CD  . GLU C 1 250 ? -31.993 67.958  9.356   1.00 37.13 ? 246 GLU C CD  1 
ATOM   5855  O OE1 . GLU C 1 250 ? -31.588 68.683  10.290  1.00 39.02 ? 246 GLU C OE1 1 
ATOM   5856  O OE2 . GLU C 1 250 ? -33.072 67.324  9.402   1.00 36.98 ? 246 GLU C OE2 1 
ATOM   5857  N N   . SER C 1 251 ? -28.308 67.621  5.730   1.00 33.58 ? 247 SER C N   1 
ATOM   5858  C CA  . SER C 1 251 ? -26.876 67.899  5.630   1.00 33.14 ? 247 SER C CA  1 
ATOM   5859  C C   . SER C 1 251 ? -26.550 69.353  5.306   1.00 33.00 ? 247 SER C C   1 
ATOM   5860  O O   . SER C 1 251 ? -27.276 70.012  4.558   1.00 33.00 ? 247 SER C O   1 
ATOM   5861  C CB  . SER C 1 251 ? -26.227 66.989  4.579   1.00 33.07 ? 247 SER C CB  1 
ATOM   5862  O OG  . SER C 1 251 ? -24.816 67.146  4.567   1.00 32.29 ? 247 SER C OG  1 
ATOM   5863  N N   . ASN C 1 252 ? -25.441 69.833  5.866   1.00 32.65 ? 248 ASN C N   1 
ATOM   5864  C CA  . ASN C 1 252 ? -24.903 71.149  5.545   1.00 32.41 ? 248 ASN C CA  1 
ATOM   5865  C C   . ASN C 1 252 ? -23.518 71.076  4.884   1.00 32.28 ? 248 ASN C C   1 
ATOM   5866  O O   . ASN C 1 252 ? -22.805 72.085  4.807   1.00 32.06 ? 248 ASN C O   1 
ATOM   5867  C CB  . ASN C 1 252 ? -24.869 72.035  6.792   1.00 32.30 ? 248 ASN C CB  1 
ATOM   5868  C CG  . ASN C 1 252 ? -23.885 71.538  7.836   1.00 33.16 ? 248 ASN C CG  1 
ATOM   5869  O OD1 . ASN C 1 252 ? -23.499 70.364  7.840   1.00 33.63 ? 248 ASN C OD1 1 
ATOM   5870  N ND2 . ASN C 1 252 ? -23.478 72.429  8.733   1.00 33.02 ? 248 ASN C ND2 1 
ATOM   5871  N N   . GLY C 1 253 ? -23.148 69.884  4.407   1.00 31.97 ? 249 GLY C N   1 
ATOM   5872  C CA  . GLY C 1 253 ? -21.910 69.700  3.641   1.00 31.76 ? 249 GLY C CA  1 
ATOM   5873  C C   . GLY C 1 253 ? -21.458 68.258  3.479   1.00 31.66 ? 249 GLY C C   1 
ATOM   5874  O O   . GLY C 1 253 ? -21.948 67.364  4.167   1.00 31.77 ? 249 GLY C O   1 
ATOM   5875  N N   . ASN C 1 254 ? -20.526 68.040  2.551   1.00 31.45 ? 250 ASN C N   1 
ATOM   5876  C CA  . ASN C 1 254 ? -19.862 66.740  2.347   1.00 31.30 ? 250 ASN C CA  1 
ATOM   5877  C C   . ASN C 1 254 ? -20.767 65.595  1.896   1.00 31.54 ? 250 ASN C C   1 
ATOM   5878  O O   . ASN C 1 254 ? -20.326 64.448  1.786   1.00 31.51 ? 250 ASN C O   1 
ATOM   5879  C CB  . ASN C 1 254 ? -19.067 66.333  3.591   1.00 31.04 ? 250 ASN C CB  1 
ATOM   5880  C CG  . ASN C 1 254 ? -18.052 67.370  3.983   1.00 30.12 ? 250 ASN C CG  1 
ATOM   5881  O OD1 . ASN C 1 254 ? -18.402 68.449  4.459   1.00 29.51 ? 250 ASN C OD1 1 
ATOM   5882  N ND2 . ASN C 1 254 ? -16.786 67.057  3.777   1.00 29.19 ? 250 ASN C ND2 1 
ATOM   5883  N N   . PHE C 1 255 ? -22.021 65.928  1.608   1.00 31.50 ? 251 PHE C N   1 
ATOM   5884  C CA  . PHE C 1 255 ? -23.029 64.947  1.253   1.00 31.38 ? 251 PHE C CA  1 
ATOM   5885  C C   . PHE C 1 255 ? -22.916 64.494  -0.203  1.00 31.32 ? 251 PHE C C   1 
ATOM   5886  O O   . PHE C 1 255 ? -22.836 65.301  -1.129  1.00 31.32 ? 251 PHE C O   1 
ATOM   5887  C CB  . PHE C 1 255 ? -24.418 65.514  1.567   1.00 31.41 ? 251 PHE C CB  1 
ATOM   5888  C CG  . PHE C 1 255 ? -25.557 64.577  1.280   1.00 30.95 ? 251 PHE C CG  1 
ATOM   5889  C CD1 . PHE C 1 255 ? -25.455 63.212  1.543   1.00 31.03 ? 251 PHE C CD1 1 
ATOM   5890  C CD2 . PHE C 1 255 ? -26.761 65.080  0.789   1.00 30.56 ? 251 PHE C CD2 1 
ATOM   5891  C CE1 . PHE C 1 255 ? -26.522 62.355  1.286   1.00 31.13 ? 251 PHE C CE1 1 
ATOM   5892  C CE2 . PHE C 1 255 ? -27.835 64.240  0.534   1.00 30.50 ? 251 PHE C CE2 1 
ATOM   5893  C CZ  . PHE C 1 255 ? -27.718 62.871  0.784   1.00 31.38 ? 251 PHE C CZ  1 
ATOM   5894  N N   . ILE C 1 256 ? -22.884 63.183  -0.387  1.00 31.23 ? 252 ILE C N   1 
ATOM   5895  C CA  . ILE C 1 256 ? -22.973 62.607  -1.709  1.00 30.95 ? 252 ILE C CA  1 
ATOM   5896  C C   . ILE C 1 256 ? -24.379 62.027  -1.834  1.00 31.00 ? 252 ILE C C   1 
ATOM   5897  O O   . ILE C 1 256 ? -24.687 60.953  -1.304  1.00 30.99 ? 252 ILE C O   1 
ATOM   5898  C CB  . ILE C 1 256 ? -21.864 61.582  -1.960  1.00 30.92 ? 252 ILE C CB  1 
ATOM   5899  C CG1 . ILE C 1 256 ? -20.502 62.217  -1.667  1.00 30.66 ? 252 ILE C CG1 1 
ATOM   5900  C CG2 . ILE C 1 256 ? -21.899 61.120  -3.395  1.00 30.55 ? 252 ILE C CG2 1 
ATOM   5901  C CD1 . ILE C 1 256 ? -19.374 61.236  -1.625  1.00 31.05 ? 252 ILE C CD1 1 
ATOM   5902  N N   . ALA C 1 257 ? -25.230 62.779  -2.523  1.00 30.76 ? 253 ALA C N   1 
ATOM   5903  C CA  . ALA C 1 257 ? -26.658 62.523  -2.548  1.00 30.77 ? 253 ALA C CA  1 
ATOM   5904  C C   . ALA C 1 257 ? -27.013 61.377  -3.469  1.00 30.58 ? 253 ALA C C   1 
ATOM   5905  O O   . ALA C 1 257 ? -26.359 61.175  -4.485  1.00 30.78 ? 253 ALA C O   1 
ATOM   5906  C CB  . ALA C 1 257 ? -27.407 63.783  -2.963  1.00 30.83 ? 253 ALA C CB  1 
ATOM   5907  N N   . PRO C 1 258 ? -28.055 60.618  -3.118  1.00 30.51 ? 254 PRO C N   1 
ATOM   5908  C CA  . PRO C 1 258 ? -28.514 59.616  -4.071  1.00 30.64 ? 254 PRO C CA  1 
ATOM   5909  C C   . PRO C 1 258 ? -29.225 60.282  -5.236  1.00 30.96 ? 254 PRO C C   1 
ATOM   5910  O O   . PRO C 1 258 ? -29.764 61.376  -5.079  1.00 30.74 ? 254 PRO C O   1 
ATOM   5911  C CB  . PRO C 1 258 ? -29.516 58.788  -3.263  1.00 30.49 ? 254 PRO C CB  1 
ATOM   5912  C CG  . PRO C 1 258 ? -29.925 59.646  -2.123  1.00 30.27 ? 254 PRO C CG  1 
ATOM   5913  C CD  . PRO C 1 258 ? -28.806 60.588  -1.848  1.00 30.22 ? 254 PRO C CD  1 
ATOM   5914  N N   . GLU C 1 259 ? -29.186 59.649  -6.402  1.00 31.64 ? 255 GLU C N   1 
ATOM   5915  C CA  . GLU C 1 259 ? -30.159 59.951  -7.449  1.00 32.32 ? 255 GLU C CA  1 
ATOM   5916  C C   . GLU C 1 259 ? -30.957 58.690  -7.752  1.00 32.42 ? 255 GLU C C   1 
ATOM   5917  O O   . GLU C 1 259 ? -32.187 58.713  -7.730  1.00 32.83 ? 255 GLU C O   1 
ATOM   5918  C CB  . GLU C 1 259 ? -29.512 60.518  -8.716  1.00 32.43 ? 255 GLU C CB  1 
ATOM   5919  C CG  . GLU C 1 259 ? -30.514 60.659  -9.862  1.00 34.16 ? 255 GLU C CG  1 
ATOM   5920  C CD  . GLU C 1 259 ? -30.122 61.677  -10.926 1.00 36.75 ? 255 GLU C CD  1 
ATOM   5921  O OE1 . GLU C 1 259 ? -28.908 61.841  -11.205 1.00 37.19 ? 255 GLU C OE1 1 
ATOM   5922  O OE2 . GLU C 1 259 ? -31.051 62.307  -11.495 1.00 37.23 ? 255 GLU C OE2 1 
ATOM   5923  N N   . TYR C 1 260 ? -30.249 57.590  -8.007  1.00 32.40 ? 256 TYR C N   1 
ATOM   5924  C CA  . TYR C 1 260 ? -30.883 56.314  -8.325  1.00 32.35 ? 256 TYR C CA  1 
ATOM   5925  C C   . TYR C 1 260 ? -30.750 55.300  -7.201  1.00 32.18 ? 256 TYR C C   1 
ATOM   5926  O O   . TYR C 1 260 ? -29.702 55.203  -6.560  1.00 32.44 ? 256 TYR C O   1 
ATOM   5927  C CB  . TYR C 1 260 ? -30.323 55.738  -9.629  1.00 32.36 ? 256 TYR C CB  1 
ATOM   5928  C CG  . TYR C 1 260 ? -30.594 56.615  -10.833 1.00 33.15 ? 256 TYR C CG  1 
ATOM   5929  C CD1 . TYR C 1 260 ? -29.626 57.507  -11.302 1.00 33.88 ? 256 TYR C CD1 1 
ATOM   5930  C CD2 . TYR C 1 260 ? -31.821 56.562  -11.497 1.00 33.36 ? 256 TYR C CD2 1 
ATOM   5931  C CE1 . TYR C 1 260 ? -29.869 58.321  -12.405 1.00 34.03 ? 256 TYR C CE1 1 
ATOM   5932  C CE2 . TYR C 1 260 ? -32.079 57.373  -12.598 1.00 34.27 ? 256 TYR C CE2 1 
ATOM   5933  C CZ  . TYR C 1 260 ? -31.100 58.252  -13.046 1.00 34.71 ? 256 TYR C CZ  1 
ATOM   5934  O OH  . TYR C 1 260 ? -31.348 59.056  -14.142 1.00 34.22 ? 256 TYR C OH  1 
ATOM   5935  N N   . ALA C 1 261 ? -31.830 54.556  -6.973  1.00 31.94 ? 257 ALA C N   1 
ATOM   5936  C CA  . ALA C 1 261 ? -31.847 53.418  -6.056  1.00 31.59 ? 257 ALA C CA  1 
ATOM   5937  C C   . ALA C 1 261 ? -32.275 52.152  -6.817  1.00 31.59 ? 257 ALA C C   1 
ATOM   5938  O O   . ALA C 1 261 ? -32.553 52.216  -8.018  1.00 31.50 ? 257 ALA C O   1 
ATOM   5939  C CB  . ALA C 1 261 ? -32.778 53.698  -4.892  1.00 31.46 ? 257 ALA C CB  1 
ATOM   5940  N N   . TYR C 1 262 ? -32.314 51.009  -6.131  1.00 31.73 ? 258 TYR C N   1 
ATOM   5941  C CA  . TYR C 1 262 ? -32.678 49.733  -6.766  1.00 31.89 ? 258 TYR C CA  1 
ATOM   5942  C C   . TYR C 1 262 ? -33.914 49.099  -6.135  1.00 32.39 ? 258 TYR C C   1 
ATOM   5943  O O   . TYR C 1 262 ? -33.938 48.846  -4.931  1.00 32.50 ? 258 TYR C O   1 
ATOM   5944  C CB  . TYR C 1 262 ? -31.512 48.735  -6.700  1.00 31.52 ? 258 TYR C CB  1 
ATOM   5945  C CG  . TYR C 1 262 ? -30.270 49.155  -7.455  1.00 30.54 ? 258 TYR C CG  1 
ATOM   5946  C CD1 . TYR C 1 262 ? -29.325 49.988  -6.867  1.00 29.71 ? 258 TYR C CD1 1 
ATOM   5947  C CD2 . TYR C 1 262 ? -30.037 48.714  -8.756  1.00 30.10 ? 258 TYR C CD2 1 
ATOM   5948  C CE1 . TYR C 1 262 ? -28.187 50.384  -7.555  1.00 29.67 ? 258 TYR C CE1 1 
ATOM   5949  C CE2 . TYR C 1 262 ? -28.891 49.102  -9.455  1.00 29.47 ? 258 TYR C CE2 1 
ATOM   5950  C CZ  . TYR C 1 262 ? -27.972 49.936  -8.844  1.00 29.69 ? 258 TYR C CZ  1 
ATOM   5951  O OH  . TYR C 1 262 ? -26.833 50.335  -9.512  1.00 30.46 ? 258 TYR C OH  1 
ATOM   5952  N N   . LYS C 1 263 ? -34.940 48.859  -6.948  1.00 33.20 ? 259 LYS C N   1 
ATOM   5953  C CA  . LYS C 1 263 ? -36.073 48.012  -6.558  1.00 34.15 ? 259 LYS C CA  1 
ATOM   5954  C C   . LYS C 1 263 ? -35.594 46.570  -6.505  1.00 34.36 ? 259 LYS C C   1 
ATOM   5955  O O   . LYS C 1 263 ? -34.980 46.086  -7.457  1.00 34.22 ? 259 LYS C O   1 
ATOM   5956  C CB  . LYS C 1 263 ? -37.193 48.080  -7.598  1.00 34.34 ? 259 LYS C CB  1 
ATOM   5957  C CG  . LYS C 1 263 ? -38.280 49.111  -7.382  1.00 35.88 ? 259 LYS C CG  1 
ATOM   5958  C CD  . LYS C 1 263 ? -39.138 49.218  -8.656  1.00 38.10 ? 259 LYS C CD  1 
ATOM   5959  C CE  . LYS C 1 263 ? -40.606 49.496  -8.338  1.00 39.96 ? 259 LYS C CE  1 
ATOM   5960  N NZ  . LYS C 1 263 ? -41.359 50.085  -9.494  1.00 40.56 ? 259 LYS C NZ  1 
ATOM   5961  N N   . ILE C 1 264 ? -35.872 45.888  -5.399  1.00 34.86 ? 260 ILE C N   1 
ATOM   5962  C CA  . ILE C 1 264 ? -35.592 44.461  -5.291  1.00 35.34 ? 260 ILE C CA  1 
ATOM   5963  C C   . ILE C 1 264 ? -36.846 43.724  -5.731  1.00 35.80 ? 260 ILE C C   1 
ATOM   5964  O O   . ILE C 1 264 ? -37.723 43.429  -4.915  1.00 35.97 ? 260 ILE C O   1 
ATOM   5965  C CB  . ILE C 1 264 ? -35.194 44.066  -3.851  1.00 35.34 ? 260 ILE C CB  1 
ATOM   5966  C CG1 . ILE C 1 264 ? -33.980 44.890  -3.401  1.00 35.60 ? 260 ILE C CG1 1 
ATOM   5967  C CG2 . ILE C 1 264 ? -34.916 42.564  -3.758  1.00 35.03 ? 260 ILE C CG2 1 
ATOM   5968  C CD1 . ILE C 1 264 ? -33.752 44.921  -1.899  1.00 36.12 ? 260 ILE C CD1 1 
ATOM   5969  N N   . VAL C 1 265 ? -36.940 43.453  -7.029  1.00 36.34 ? 261 VAL C N   1 
ATOM   5970  C CA  . VAL C 1 265 ? -38.158 42.865  -7.601  1.00 36.98 ? 261 VAL C CA  1 
ATOM   5971  C C   . VAL C 1 265 ? -38.260 41.355  -7.360  1.00 37.38 ? 261 VAL C C   1 
ATOM   5972  O O   . VAL C 1 265 ? -39.350 40.848  -7.070  1.00 37.63 ? 261 VAL C O   1 
ATOM   5973  C CB  . VAL C 1 265 ? -38.399 43.269  -9.109  1.00 37.00 ? 261 VAL C CB  1 
ATOM   5974  C CG1 . VAL C 1 265 ? -37.130 43.778  -9.772  1.00 36.84 ? 261 VAL C CG1 1 
ATOM   5975  C CG2 . VAL C 1 265 ? -39.036 42.125  -9.917  1.00 37.13 ? 261 VAL C CG2 1 
ATOM   5976  N N   . LYS C 1 266 ? -37.136 40.646  -7.460  1.00 37.70 ? 262 LYS C N   1 
ATOM   5977  C CA  . LYS C 1 266 ? -37.121 39.217  -7.139  1.00 38.06 ? 262 LYS C CA  1 
ATOM   5978  C C   . LYS C 1 266 ? -36.029 38.797  -6.152  1.00 38.17 ? 262 LYS C C   1 
ATOM   5979  O O   . LYS C 1 266 ? -34.833 38.973  -6.401  1.00 38.03 ? 262 LYS C O   1 
ATOM   5980  C CB  . LYS C 1 266 ? -37.066 38.350  -8.401  1.00 37.93 ? 262 LYS C CB  1 
ATOM   5981  C CG  . LYS C 1 266 ? -37.429 36.899  -8.136  1.00 38.97 ? 262 LYS C CG  1 
ATOM   5982  C CD  . LYS C 1 266 ? -37.409 36.067  -9.404  1.00 41.10 ? 262 LYS C CD  1 
ATOM   5983  C CE  . LYS C 1 266 ? -37.846 34.638  -9.116  1.00 42.10 ? 262 LYS C CE  1 
ATOM   5984  N NZ  . LYS C 1 266 ? -37.478 33.708  -10.218 1.00 42.68 ? 262 LYS C NZ  1 
ATOM   5985  N N   . LYS C 1 267 ? -36.476 38.240  -5.030  1.00 38.55 ? 263 LYS C N   1 
ATOM   5986  C CA  . LYS C 1 267 ? -35.613 37.573  -4.069  1.00 38.89 ? 263 LYS C CA  1 
ATOM   5987  C C   . LYS C 1 267 ? -35.646 36.075  -4.349  1.00 39.18 ? 263 LYS C C   1 
ATOM   5988  O O   . LYS C 1 267 ? -36.663 35.545  -4.798  1.00 39.24 ? 263 LYS C O   1 
ATOM   5989  C CB  . LYS C 1 267 ? -36.102 37.838  -2.651  1.00 39.03 ? 263 LYS C CB  1 
ATOM   5990  C CG  . LYS C 1 267 ? -36.029 39.293  -2.219  1.00 39.72 ? 263 LYS C CG  1 
ATOM   5991  C CD  . LYS C 1 267 ? -36.085 39.400  -0.708  1.00 41.62 ? 263 LYS C CD  1 
ATOM   5992  C CE  . LYS C 1 267 ? -37.430 39.905  -0.216  1.00 42.03 ? 263 LYS C CE  1 
ATOM   5993  N NZ  . LYS C 1 267 ? -37.423 41.389  -0.159  1.00 42.43 ? 263 LYS C NZ  1 
ATOM   5994  N N   . GLY C 1 268 ? -34.534 35.395  -4.091  1.00 39.55 ? 264 GLY C N   1 
ATOM   5995  C CA  . GLY C 1 268 ? -34.444 33.952  -4.312  1.00 39.82 ? 264 GLY C CA  1 
ATOM   5996  C C   . GLY C 1 268 ? -33.056 33.422  -4.019  1.00 40.20 ? 264 GLY C C   1 
ATOM   5997  O O   . GLY C 1 268 ? -32.231 34.121  -3.432  1.00 40.39 ? 264 GLY C O   1 
ATOM   5998  N N   . ASP C 1 269 A -32.797 32.180  -4.419  1.00 40.42 ? 264 ASP C N   1 
ATOM   5999  C CA  . ASP C 1 269 A -31.472 31.595  -4.251  1.00 40.71 ? 264 ASP C CA  1 
ATOM   6000  C C   . ASP C 1 269 A -30.524 32.045  -5.348  1.00 40.42 ? 264 ASP C C   1 
ATOM   6001  O O   . ASP C 1 269 A -30.801 31.884  -6.542  1.00 40.52 ? 264 ASP C O   1 
ATOM   6002  C CB  . ASP C 1 269 A -31.535 30.065  -4.165  1.00 41.08 ? 264 ASP C CB  1 
ATOM   6003  C CG  . ASP C 1 269 A -31.602 29.568  -2.731  1.00 42.54 ? 264 ASP C CG  1 
ATOM   6004  O OD1 . ASP C 1 269 A -30.964 28.535  -2.435  1.00 44.81 ? 264 ASP C OD1 1 
ATOM   6005  O OD2 . ASP C 1 269 A -32.271 30.217  -1.891  1.00 43.43 ? 264 ASP C OD2 1 
ATOM   6006  N N   . SER C 1 270 ? -29.410 32.628  -4.924  1.00 39.92 ? 265 SER C N   1 
ATOM   6007  C CA  . SER C 1 270 ? -28.386 33.110  -5.834  1.00 39.69 ? 265 SER C CA  1 
ATOM   6008  C C   . SER C 1 270 ? -27.024 32.946  -5.160  1.00 39.67 ? 265 SER C C   1 
ATOM   6009  O O   . SER C 1 270 ? -26.928 32.324  -4.102  1.00 39.45 ? 265 SER C O   1 
ATOM   6010  C CB  . SER C 1 270 ? -28.659 34.571  -6.206  1.00 39.47 ? 265 SER C CB  1 
ATOM   6011  O OG  . SER C 1 270 ? -27.750 35.040  -7.179  1.00 38.79 ? 265 SER C OG  1 
ATOM   6012  N N   . ALA C 1 271 ? -25.982 33.499  -5.777  1.00 39.85 ? 266 ALA C N   1 
ATOM   6013  C CA  . ALA C 1 271 ? -24.620 33.425  -5.260  1.00 39.99 ? 266 ALA C CA  1 
ATOM   6014  C C   . ALA C 1 271 ? -23.751 34.479  -5.929  1.00 40.12 ? 266 ALA C C   1 
ATOM   6015  O O   . ALA C 1 271 ? -24.061 34.920  -7.033  1.00 40.16 ? 266 ALA C O   1 
ATOM   6016  C CB  . ALA C 1 271 ? -24.034 32.032  -5.509  1.00 39.93 ? 266 ALA C CB  1 
ATOM   6017  N N   . ILE C 1 272 ? -22.677 34.883  -5.251  1.00 40.42 ? 267 ILE C N   1 
ATOM   6018  C CA  . ILE C 1 272 ? -21.600 35.633  -5.882  1.00 40.90 ? 267 ILE C CA  1 
ATOM   6019  C C   . ILE C 1 272 ? -20.441 34.672  -6.095  1.00 41.58 ? 267 ILE C C   1 
ATOM   6020  O O   . ILE C 1 272 ? -19.764 34.271  -5.140  1.00 41.54 ? 267 ILE C O   1 
ATOM   6021  C CB  . ILE C 1 272 ? -21.090 36.831  -5.034  1.00 40.91 ? 267 ILE C CB  1 
ATOM   6022  C CG1 . ILE C 1 272 ? -22.243 37.675  -4.470  1.00 40.75 ? 267 ILE C CG1 1 
ATOM   6023  C CG2 . ILE C 1 272 ? -20.103 37.677  -5.847  1.00 40.58 ? 267 ILE C CG2 1 
ATOM   6024  C CD1 . ILE C 1 272 ? -23.055 38.402  -5.497  1.00 40.36 ? 267 ILE C CD1 1 
ATOM   6025  N N   . MET C 1 273 ? -20.214 34.313  -7.354  1.00 42.25 ? 268 MET C N   1 
ATOM   6026  C CA  . MET C 1 273 ? -19.189 33.350  -7.706  1.00 43.08 ? 268 MET C CA  1 
ATOM   6027  C C   . MET C 1 273 ? -17.891 34.049  -8.104  1.00 43.58 ? 268 MET C C   1 
ATOM   6028  O O   . MET C 1 273 ? -17.892 34.929  -8.968  1.00 43.68 ? 268 MET C O   1 
ATOM   6029  C CB  . MET C 1 273 ? -19.693 32.464  -8.841  1.00 43.09 ? 268 MET C CB  1 
ATOM   6030  C CG  . MET C 1 273 ? -19.331 31.008  -8.688  1.00 44.02 ? 268 MET C CG  1 
ATOM   6031  S SD  . MET C 1 273 ? -20.434 29.906  -9.604  1.00 45.61 ? 268 MET C SD  1 
ATOM   6032  C CE  . MET C 1 273 ? -19.906 30.243  -11.281 1.00 45.91 ? 268 MET C CE  1 
ATOM   6033  N N   . LYS C 1 274 ? -16.796 33.667  -7.450  1.00 44.26 ? 269 LYS C N   1 
ATOM   6034  C CA  . LYS C 1 274 ? -15.461 34.137  -7.811  1.00 45.01 ? 269 LYS C CA  1 
ATOM   6035  C C   . LYS C 1 274 ? -14.885 33.229  -8.889  1.00 45.17 ? 269 LYS C C   1 
ATOM   6036  O O   . LYS C 1 274 ? -14.630 32.050  -8.645  1.00 45.26 ? 269 LYS C O   1 
ATOM   6037  C CB  . LYS C 1 274 ? -14.532 34.147  -6.599  1.00 45.11 ? 269 LYS C CB  1 
ATOM   6038  C CG  . LYS C 1 274 ? -14.947 35.087  -5.495  1.00 46.50 ? 269 LYS C CG  1 
ATOM   6039  C CD  . LYS C 1 274 ? -13.918 35.065  -4.374  1.00 49.05 ? 269 LYS C CD  1 
ATOM   6040  C CE  . LYS C 1 274 ? -14.453 35.758  -3.130  1.00 50.15 ? 269 LYS C CE  1 
ATOM   6041  N NZ  . LYS C 1 274 ? -13.458 35.772  -2.019  1.00 50.82 ? 269 LYS C NZ  1 
ATOM   6042  N N   . SER C 1 275 ? -14.691 33.786  -10.081 1.00 45.51 ? 270 SER C N   1 
ATOM   6043  C CA  . SER C 1 275 ? -14.252 33.023  -11.243 1.00 45.74 ? 270 SER C CA  1 
ATOM   6044  C C   . SER C 1 275 ? -13.659 33.958  -12.281 1.00 45.95 ? 270 SER C C   1 
ATOM   6045  O O   . SER C 1 275 ? -14.177 35.050  -12.510 1.00 46.05 ? 270 SER C O   1 
ATOM   6046  C CB  . SER C 1 275 ? -15.428 32.254  -11.857 1.00 45.65 ? 270 SER C CB  1 
ATOM   6047  O OG  . SER C 1 275 ? -15.016 31.508  -12.991 1.00 46.05 ? 270 SER C OG  1 
ATOM   6048  N N   . GLU C 1 276 ? -12.574 33.517  -12.908 1.00 46.36 ? 271 GLU C N   1 
ATOM   6049  C CA  . GLU C 1 276 ? -11.917 34.285  -13.965 1.00 46.72 ? 271 GLU C CA  1 
ATOM   6050  C C   . GLU C 1 276 ? -12.518 33.979  -15.335 1.00 46.88 ? 271 GLU C C   1 
ATOM   6051  O O   . GLU C 1 276 ? -12.200 34.640  -16.324 1.00 47.21 ? 271 GLU C O   1 
ATOM   6052  C CB  . GLU C 1 276 ? -10.407 34.013  -13.972 1.00 46.75 ? 271 GLU C CB  1 
ATOM   6053  C CG  . GLU C 1 276 ? -9.673  34.472  -12.708 1.00 47.18 ? 271 GLU C CG  1 
ATOM   6054  C CD  . GLU C 1 276 ? -9.743  35.978  -12.490 1.00 48.04 ? 271 GLU C CD  1 
ATOM   6055  O OE1 . GLU C 1 276 ? -9.338  36.733  -13.400 1.00 48.65 ? 271 GLU C OE1 1 
ATOM   6056  O OE2 . GLU C 1 276 ? -10.197 36.409  -11.406 1.00 48.36 ? 271 GLU C OE2 1 
ATOM   6057  N N   . LEU C 1 277 ? -13.399 32.983  -15.384 1.00 46.93 ? 272 LEU C N   1 
ATOM   6058  C CA  . LEU C 1 277 ? -13.983 32.530  -16.640 1.00 46.94 ? 272 LEU C CA  1 
ATOM   6059  C C   . LEU C 1 277 ? -15.016 33.527  -17.165 1.00 47.01 ? 272 LEU C C   1 
ATOM   6060  O O   . LEU C 1 277 ? -15.427 34.449  -16.453 1.00 47.05 ? 272 LEU C O   1 
ATOM   6061  C CB  . LEU C 1 277 ? -14.603 31.132  -16.475 1.00 46.87 ? 272 LEU C CB  1 
ATOM   6062  C CG  . LEU C 1 277 ? -13.746 30.018  -15.847 1.00 46.96 ? 272 LEU C CG  1 
ATOM   6063  C CD1 . LEU C 1 277 ? -14.604 28.828  -15.416 1.00 46.39 ? 272 LEU C CD1 1 
ATOM   6064  C CD2 . LEU C 1 277 ? -12.614 29.567  -16.771 1.00 46.60 ? 272 LEU C CD2 1 
ATOM   6065  N N   . GLU C 1 278 ? -15.415 33.344  -18.421 1.00 46.97 ? 273 GLU C N   1 
ATOM   6066  C CA  . GLU C 1 278 ? -16.469 34.155  -19.021 1.00 46.89 ? 273 GLU C CA  1 
ATOM   6067  C C   . GLU C 1 278 ? -17.602 33.276  -19.560 1.00 46.35 ? 273 GLU C C   1 
ATOM   6068  O O   . GLU C 1 278 ? -17.515 32.042  -19.516 1.00 46.22 ? 273 GLU C O   1 
ATOM   6069  C CB  . GLU C 1 278 ? -15.901 35.100  -20.096 1.00 47.29 ? 273 GLU C CB  1 
ATOM   6070  C CG  . GLU C 1 278 ? -14.889 34.469  -21.067 1.00 48.78 ? 273 GLU C CG  1 
ATOM   6071  C CD  . GLU C 1 278 ? -14.281 35.482  -22.037 1.00 50.59 ? 273 GLU C CD  1 
ATOM   6072  O OE1 . GLU C 1 278 ? -13.737 36.511  -21.572 1.00 51.14 ? 273 GLU C OE1 1 
ATOM   6073  O OE2 . GLU C 1 278 ? -14.344 35.246  -23.267 1.00 50.97 ? 273 GLU C OE2 1 
ATOM   6074  N N   . TYR C 1 279 ? -18.664 33.918  -20.046 1.00 45.80 ? 274 TYR C N   1 
ATOM   6075  C CA  . TYR C 1 279 ? -19.870 33.225  -20.508 1.00 45.25 ? 274 TYR C CA  1 
ATOM   6076  C C   . TYR C 1 279 ? -19.582 32.154  -21.562 1.00 45.17 ? 274 TYR C C   1 
ATOM   6077  O O   . TYR C 1 279 ? -18.837 32.391  -22.515 1.00 45.10 ? 274 TYR C O   1 
ATOM   6078  C CB  . TYR C 1 279 ? -20.893 34.233  -21.033 1.00 45.02 ? 274 TYR C CB  1 
ATOM   6079  C CG  . TYR C 1 279 ? -22.268 33.652  -21.291 1.00 44.35 ? 274 TYR C CG  1 
ATOM   6080  C CD1 . TYR C 1 279 ? -22.938 32.920  -20.307 1.00 43.31 ? 274 TYR C CD1 1 
ATOM   6081  C CD2 . TYR C 1 279 ? -22.912 33.858  -22.510 1.00 43.20 ? 274 TYR C CD2 1 
ATOM   6082  C CE1 . TYR C 1 279 ? -24.205 32.398  -20.538 1.00 42.83 ? 274 TYR C CE1 1 
ATOM   6083  C CE2 . TYR C 1 279 ? -24.179 33.340  -22.749 1.00 42.80 ? 274 TYR C CE2 1 
ATOM   6084  C CZ  . TYR C 1 279 ? -24.821 32.611  -21.764 1.00 42.67 ? 274 TYR C CZ  1 
ATOM   6085  O OH  . TYR C 1 279 ? -26.075 32.098  -22.009 1.00 41.72 ? 274 TYR C OH  1 
ATOM   6086  N N   . GLY C 1 280 ? -20.179 30.980  -21.376 1.00 45.01 ? 275 GLY C N   1 
ATOM   6087  C CA  . GLY C 1 280 ? -19.925 29.835  -22.243 1.00 44.87 ? 275 GLY C CA  1 
ATOM   6088  C C   . GLY C 1 280 ? -21.096 29.422  -23.114 1.00 44.85 ? 275 GLY C C   1 
ATOM   6089  O O   . GLY C 1 280 ? -21.093 28.323  -23.679 1.00 44.98 ? 275 GLY C O   1 
ATOM   6090  N N   . ASN C 1 281 ? -22.099 30.295  -23.209 1.00 44.66 ? 276 ASN C N   1 
ATOM   6091  C CA  . ASN C 1 281 ? -23.257 30.101  -24.097 1.00 44.61 ? 276 ASN C CA  1 
ATOM   6092  C C   . ASN C 1 281 ? -23.903 28.710  -23.990 1.00 44.56 ? 276 ASN C C   1 
ATOM   6093  O O   . ASN C 1 281 ? -24.297 28.108  -24.991 1.00 44.76 ? 276 ASN C O   1 
ATOM   6094  C CB  . ASN C 1 281 ? -22.889 30.453  -25.555 1.00 44.47 ? 276 ASN C CB  1 
ATOM   6095  C CG  . ASN C 1 281 ? -22.450 31.916  -25.719 1.00 44.56 ? 276 ASN C CG  1 
ATOM   6096  O OD1 . ASN C 1 281 ? -21.253 32.223  -25.724 1.00 43.99 ? 276 ASN C OD1 1 
ATOM   6097  N ND2 . ASN C 1 281 ? -23.423 32.821  -25.840 1.00 43.88 ? 276 ASN C ND2 1 
ATOM   6098  N N   . CYS C 1 282 ? -24.013 28.225  -22.755 1.00 44.37 ? 277 CYS C N   1 
ATOM   6099  C CA  . CYS C 1 282 ? -24.516 26.882  -22.457 1.00 44.04 ? 277 CYS C CA  1 
ATOM   6100  C C   . CYS C 1 282 ? -25.653 26.941  -21.440 1.00 43.56 ? 277 CYS C C   1 
ATOM   6101  O O   . CYS C 1 282 ? -25.948 28.004  -20.887 1.00 43.43 ? 277 CYS C O   1 
ATOM   6102  C CB  . CYS C 1 282 ? -23.380 25.993  -21.926 1.00 43.97 ? 277 CYS C CB  1 
ATOM   6103  S SG  . CYS C 1 282 ? -22.180 26.853  -20.841 1.00 45.19 ? 277 CYS C SG  1 
ATOM   6104  N N   . ASN C 1 283 ? -26.296 25.797  -21.214 1.00 43.12 ? 278 ASN C N   1 
ATOM   6105  C CA  . ASN C 1 283 ? -27.292 25.655  -20.156 1.00 42.60 ? 278 ASN C CA  1 
ATOM   6106  C C   . ASN C 1 283 ? -26.957 24.466  -19.256 1.00 42.02 ? 278 ASN C C   1 
ATOM   6107  O O   . ASN C 1 283 ? -26.554 23.412  -19.746 1.00 41.95 ? 278 ASN C O   1 
ATOM   6108  C CB  . ASN C 1 283 ? -28.692 25.497  -20.749 1.00 42.74 ? 278 ASN C CB  1 
ATOM   6109  C CG  . ASN C 1 283 ? -29.794 25.604  -19.701 1.00 43.28 ? 278 ASN C CG  1 
ATOM   6110  O OD1 . ASN C 1 283 ? -29.690 26.371  -18.744 1.00 44.27 ? 278 ASN C OD1 1 
ATOM   6111  N ND2 . ASN C 1 283 ? -30.864 24.842  -19.891 1.00 43.50 ? 278 ASN C ND2 1 
ATOM   6112  N N   . THR C 1 284 ? -27.111 24.644  -17.944 1.00 41.22 ? 279 THR C N   1 
ATOM   6113  C CA  . THR C 1 284 ? -26.890 23.559  -16.987 1.00 40.42 ? 279 THR C CA  1 
ATOM   6114  C C   . THR C 1 284 ? -27.921 23.538  -15.861 1.00 40.28 ? 279 THR C C   1 
ATOM   6115  O O   . THR C 1 284 ? -28.690 24.489  -15.685 1.00 40.22 ? 279 THR C O   1 
ATOM   6116  C CB  . THR C 1 284 ? -25.465 23.600  -16.374 1.00 40.38 ? 279 THR C CB  1 
ATOM   6117  O OG1 . THR C 1 284 ? -25.255 22.425  -15.584 1.00 40.00 ? 279 THR C OG1 1 
ATOM   6118  C CG2 . THR C 1 284 ? -25.267 24.838  -15.485 1.00 39.98 ? 279 THR C CG2 1 
ATOM   6119  N N   . LYS C 1 285 ? -27.923 22.443  -15.106 1.00 40.04 ? 280 LYS C N   1 
ATOM   6120  C CA  . LYS C 1 285 ? -28.688 22.341  -13.870 1.00 39.94 ? 280 LYS C CA  1 
ATOM   6121  C C   . LYS C 1 285 ? -27.794 22.620  -12.661 1.00 39.41 ? 280 LYS C C   1 
ATOM   6122  O O   . LYS C 1 285 ? -28.288 22.956  -11.586 1.00 39.51 ? 280 LYS C O   1 
ATOM   6123  C CB  . LYS C 1 285 ? -29.305 20.948  -13.727 1.00 40.24 ? 280 LYS C CB  1 
ATOM   6124  C CG  . LYS C 1 285 ? -30.510 20.675  -14.607 1.00 41.72 ? 280 LYS C CG  1 
ATOM   6125  C CD  . LYS C 1 285 ? -30.902 19.200  -14.528 1.00 44.32 ? 280 LYS C CD  1 
ATOM   6126  C CE  . LYS C 1 285 ? -31.905 18.810  -15.616 1.00 45.96 ? 280 LYS C CE  1 
ATOM   6127  N NZ  . LYS C 1 285 ? -33.268 19.390  -15.393 1.00 46.60 ? 280 LYS C NZ  1 
ATOM   6128  N N   . CYS C 1 286 ? -26.483 22.468  -12.841 1.00 38.83 ? 281 CYS C N   1 
ATOM   6129  C CA  . CYS C 1 286 ? -25.520 22.609  -11.746 1.00 38.39 ? 281 CYS C CA  1 
ATOM   6130  C C   . CYS C 1 286 ? -24.257 23.343  -12.193 1.00 37.68 ? 281 CYS C C   1 
ATOM   6131  O O   . CYS C 1 286 ? -23.631 22.971  -13.184 1.00 37.72 ? 281 CYS C O   1 
ATOM   6132  C CB  . CYS C 1 286 ? -25.177 21.236  -11.156 1.00 38.59 ? 281 CYS C CB  1 
ATOM   6133  S SG  . CYS C 1 286 ? -23.902 21.247  -9.861  1.00 40.36 ? 281 CYS C SG  1 
ATOM   6134  N N   . GLN C 1 287 ? -23.897 24.387  -11.453 1.00 37.02 ? 282 GLN C N   1 
ATOM   6135  C CA  . GLN C 1 287 ? -22.775 25.253  -11.806 1.00 36.43 ? 282 GLN C CA  1 
ATOM   6136  C C   . GLN C 1 287 ? -21.753 25.400  -10.676 1.00 36.45 ? 282 GLN C C   1 
ATOM   6137  O O   . GLN C 1 287 ? -22.115 25.621  -9.520  1.00 36.12 ? 282 GLN C O   1 
ATOM   6138  C CB  . GLN C 1 287 ? -23.285 26.639  -12.221 1.00 36.20 ? 282 GLN C CB  1 
ATOM   6139  C CG  . GLN C 1 287 ? -22.201 27.576  -12.726 1.00 35.07 ? 282 GLN C CG  1 
ATOM   6140  C CD  . GLN C 1 287 ? -21.686 27.186  -14.095 1.00 34.19 ? 282 GLN C CD  1 
ATOM   6141  O OE1 . GLN C 1 287 ? -22.447 27.125  -15.058 1.00 34.80 ? 282 GLN C OE1 1 
ATOM   6142  N NE2 . GLN C 1 287 ? -20.390 26.929  -14.192 1.00 33.26 ? 282 GLN C NE2 1 
ATOM   6143  N N   . THR C 1 288 ? -20.477 25.274  -11.033 1.00 36.68 ? 283 THR C N   1 
ATOM   6144  C CA  . THR C 1 288 ? -19.367 25.553  -10.123 1.00 36.87 ? 283 THR C CA  1 
ATOM   6145  C C   . THR C 1 288 ? -18.538 26.701  -10.703 1.00 37.04 ? 283 THR C C   1 
ATOM   6146  O O   . THR C 1 288 ? -18.635 26.981  -11.900 1.00 37.00 ? 283 THR C O   1 
ATOM   6147  C CB  . THR C 1 288 ? -18.451 24.321  -9.913  1.00 36.89 ? 283 THR C CB  1 
ATOM   6148  O OG1 . THR C 1 288 ? -17.572 24.174  -11.034 1.00 37.34 ? 283 THR C OG1 1 
ATOM   6149  C CG2 . THR C 1 288 ? -19.267 23.041  -9.709  1.00 36.43 ? 283 THR C CG2 1 
ATOM   6150  N N   . PRO C 1 289 ? -17.718 27.370  -9.864  1.00 37.33 ? 284 PRO C N   1 
ATOM   6151  C CA  . PRO C 1 289 ? -16.855 28.458  -10.345 1.00 37.39 ? 284 PRO C CA  1 
ATOM   6152  C C   . PRO C 1 289 ? -15.811 28.002  -11.369 1.00 37.52 ? 284 PRO C C   1 
ATOM   6153  O O   . PRO C 1 289 ? -15.178 28.842  -12.010 1.00 37.43 ? 284 PRO C O   1 
ATOM   6154  C CB  . PRO C 1 289 ? -16.160 28.951  -9.067  1.00 37.31 ? 284 PRO C CB  1 
ATOM   6155  C CG  . PRO C 1 289 ? -17.006 28.484  -7.954  1.00 37.24 ? 284 PRO C CG  1 
ATOM   6156  C CD  . PRO C 1 289 ? -17.620 27.205  -8.402  1.00 37.21 ? 284 PRO C CD  1 
ATOM   6157  N N   . MET C 1 290 ? -15.638 26.689  -11.508 1.00 37.81 ? 285 MET C N   1 
ATOM   6158  C CA  . MET C 1 290 ? -14.698 26.111  -12.473 1.00 38.31 ? 285 MET C CA  1 
ATOM   6159  C C   . MET C 1 290 ? -15.384 25.593  -13.736 1.00 38.14 ? 285 MET C C   1 
ATOM   6160  O O   . MET C 1 290 ? -14.740 25.431  -14.775 1.00 38.30 ? 285 MET C O   1 
ATOM   6161  C CB  . MET C 1 290 ? -13.930 24.951  -11.847 1.00 38.68 ? 285 MET C CB  1 
ATOM   6162  C CG  . MET C 1 290 ? -13.095 25.304  -10.634 1.00 40.49 ? 285 MET C CG  1 
ATOM   6163  S SD  . MET C 1 290 ? -12.479 23.783  -9.899  1.00 44.75 ? 285 MET C SD  1 
ATOM   6164  C CE  . MET C 1 290 ? -11.113 23.374  -10.998 1.00 43.87 ? 285 MET C CE  1 
ATOM   6165  N N   . GLY C 1 291 ? -16.679 25.310  -13.638 1.00 37.84 ? 286 GLY C N   1 
ATOM   6166  C CA  . GLY C 1 291 ? -17.424 24.767  -14.762 1.00 37.69 ? 286 GLY C CA  1 
ATOM   6167  C C   . GLY C 1 291 ? -18.738 24.141  -14.350 1.00 37.58 ? 286 GLY C C   1 
ATOM   6168  O O   . GLY C 1 291 ? -19.044 24.039  -13.165 1.00 37.45 ? 286 GLY C O   1 
ATOM   6169  N N   . ALA C 1 292 ? -19.516 23.724  -15.343 1.00 37.58 ? 287 ALA C N   1 
ATOM   6170  C CA  . ALA C 1 292 ? -20.835 23.151  -15.108 1.00 37.61 ? 287 ALA C CA  1 
ATOM   6171  C C   . ALA C 1 292 ? -20.755 21.636  -15.014 1.00 37.62 ? 287 ALA C C   1 
ATOM   6172  O O   . ALA C 1 292 ? -19.896 21.013  -15.640 1.00 37.60 ? 287 ALA C O   1 
ATOM   6173  C CB  . ALA C 1 292 ? -21.791 23.564  -16.205 1.00 37.49 ? 287 ALA C CB  1 
ATOM   6174  N N   . ILE C 1 293 ? -21.655 21.057  -14.225 1.00 37.71 ? 288 ILE C N   1 
ATOM   6175  C CA  . ILE C 1 293 ? -21.720 19.613  -14.047 1.00 37.89 ? 288 ILE C CA  1 
ATOM   6176  C C   . ILE C 1 293 ? -22.988 19.058  -14.681 1.00 38.21 ? 288 ILE C C   1 
ATOM   6177  O O   . ILE C 1 293 ? -24.097 19.496  -14.373 1.00 38.16 ? 288 ILE C O   1 
ATOM   6178  C CB  . ILE C 1 293 ? -21.642 19.212  -12.549 1.00 37.88 ? 288 ILE C CB  1 
ATOM   6179  C CG1 . ILE C 1 293 ? -20.232 19.447  -12.003 1.00 37.49 ? 288 ILE C CG1 1 
ATOM   6180  C CG2 . ILE C 1 293 ? -22.047 17.750  -12.351 1.00 37.72 ? 288 ILE C CG2 1 
ATOM   6181  C CD1 . ILE C 1 293 ? -20.132 19.325  -10.493 1.00 37.64 ? 288 ILE C CD1 1 
ATOM   6182  N N   . ASN C 1 294 ? -22.795 18.106  -15.588 1.00 38.75 ? 289 ASN C N   1 
ATOM   6183  C CA  . ASN C 1 294 ? -23.878 17.342  -16.186 1.00 39.20 ? 289 ASN C CA  1 
ATOM   6184  C C   . ASN C 1 294 ? -23.658 15.882  -15.818 1.00 39.43 ? 289 ASN C C   1 
ATOM   6185  O O   . ASN C 1 294 ? -22.827 15.197  -16.422 1.00 39.58 ? 289 ASN C O   1 
ATOM   6186  C CB  . ASN C 1 294 ? -23.888 17.530  -17.709 1.00 39.21 ? 289 ASN C CB  1 
ATOM   6187  C CG  . ASN C 1 294 ? -25.102 16.892  -18.380 1.00 39.85 ? 289 ASN C CG  1 
ATOM   6188  O OD1 . ASN C 1 294 ? -25.083 16.628  -19.586 1.00 41.50 ? 289 ASN C OD1 1 
ATOM   6189  N ND2 . ASN C 1 294 ? -26.163 16.649  -17.609 1.00 39.35 ? 289 ASN C ND2 1 
ATOM   6190  N N   . SER C 1 295 ? -24.387 15.413  -14.810 1.00 39.75 ? 290 SER C N   1 
ATOM   6191  C CA  . SER C 1 295 ? -24.103 14.107  -14.228 1.00 40.01 ? 290 SER C CA  1 
ATOM   6192  C C   . SER C 1 295 ? -25.284 13.410  -13.572 1.00 40.19 ? 290 SER C C   1 
ATOM   6193  O O   . SER C 1 295 ? -26.246 14.048  -13.139 1.00 40.18 ? 290 SER C O   1 
ATOM   6194  C CB  . SER C 1 295 ? -22.976 14.217  -13.200 1.00 40.08 ? 290 SER C CB  1 
ATOM   6195  O OG  . SER C 1 295 ? -22.640 12.937  -12.682 1.00 39.52 ? 290 SER C OG  1 
ATOM   6196  N N   . SER C 1 296 ? -25.155 12.087  -13.486 1.00 40.34 ? 291 SER C N   1 
ATOM   6197  C CA  . SER C 1 296 ? -26.118 11.203  -12.844 1.00 40.58 ? 291 SER C CA  1 
ATOM   6198  C C   . SER C 1 296 ? -25.605 10.744  -11.467 1.00 40.27 ? 291 SER C C   1 
ATOM   6199  O O   . SER C 1 296 ? -26.378 10.264  -10.634 1.00 40.26 ? 291 SER C O   1 
ATOM   6200  C CB  . SER C 1 296 ? -26.357 9.988   -13.748 1.00 40.74 ? 291 SER C CB  1 
ATOM   6201  O OG  . SER C 1 296 ? -27.483 9.244   -13.327 1.00 42.05 ? 291 SER C OG  1 
ATOM   6202  N N   . MET C 1 297 ? -24.299 10.898  -11.247 1.00 39.84 ? 292 MET C N   1 
ATOM   6203  C CA  . MET C 1 297 ? -23.629 10.469  -10.013 1.00 39.41 ? 292 MET C CA  1 
ATOM   6204  C C   . MET C 1 297 ? -24.173 11.182  -8.774  1.00 38.98 ? 292 MET C C   1 
ATOM   6205  O O   . MET C 1 297 ? -24.660 12.309  -8.875  1.00 38.97 ? 292 MET C O   1 
ATOM   6206  C CB  . MET C 1 297 ? -22.124 10.738  -10.098 1.00 39.54 ? 292 MET C CB  1 
ATOM   6207  C CG  . MET C 1 297 ? -21.407 10.174  -11.315 1.00 39.74 ? 292 MET C CG  1 
ATOM   6208  S SD  . MET C 1 297 ? -21.204 8.400   -11.243 1.00 40.56 ? 292 MET C SD  1 
ATOM   6209  C CE  . MET C 1 297 ? -19.618 8.203   -12.055 1.00 40.14 ? 292 MET C CE  1 
ATOM   6210  N N   . PRO C 1 298 ? -24.085 10.527  -7.599  1.00 38.49 ? 293 PRO C N   1 
ATOM   6211  C CA  . PRO C 1 298 ? -24.474 11.165  -6.341  1.00 37.96 ? 293 PRO C CA  1 
ATOM   6212  C C   . PRO C 1 298 ? -23.378 12.043  -5.716  1.00 37.28 ? 293 PRO C C   1 
ATOM   6213  O O   . PRO C 1 298 ? -23.687 12.883  -4.877  1.00 37.45 ? 293 PRO C O   1 
ATOM   6214  C CB  . PRO C 1 298 ? -24.768 9.970   -5.433  1.00 38.00 ? 293 PRO C CB  1 
ATOM   6215  C CG  . PRO C 1 298 ? -23.815 8.928   -5.903  1.00 38.33 ? 293 PRO C CG  1 
ATOM   6216  C CD  . PRO C 1 298 ? -23.750 9.102   -7.403  1.00 38.40 ? 293 PRO C CD  1 
ATOM   6217  N N   . PHE C 1 299 ? -22.121 11.845  -6.112  1.00 36.48 ? 294 PHE C N   1 
ATOM   6218  C CA  . PHE C 1 299 ? -20.997 12.634  -5.594  1.00 35.80 ? 294 PHE C CA  1 
ATOM   6219  C C   . PHE C 1 299 ? -20.170 13.292  -6.697  1.00 35.24 ? 294 PHE C C   1 
ATOM   6220  O O   . PHE C 1 299 ? -20.133 12.806  -7.828  1.00 35.22 ? 294 PHE C O   1 
ATOM   6221  C CB  . PHE C 1 299 ? -20.052 11.768  -4.750  1.00 35.88 ? 294 PHE C CB  1 
ATOM   6222  C CG  . PHE C 1 299 ? -20.672 11.208  -3.509  1.00 36.04 ? 294 PHE C CG  1 
ATOM   6223  C CD1 . PHE C 1 299 ? -21.002 9.856   -3.434  1.00 36.56 ? 294 PHE C CD1 1 
ATOM   6224  C CD2 . PHE C 1 299 ? -20.910 12.019  -2.406  1.00 36.00 ? 294 PHE C CD2 1 
ATOM   6225  C CE1 . PHE C 1 299 ? -21.573 9.325   -2.286  1.00 36.58 ? 294 PHE C CE1 1 
ATOM   6226  C CE2 . PHE C 1 299 ? -21.479 11.499  -1.254  1.00 36.20 ? 294 PHE C CE2 1 
ATOM   6227  C CZ  . PHE C 1 299 ? -21.809 10.150  -1.192  1.00 36.62 ? 294 PHE C CZ  1 
ATOM   6228  N N   . HIS C 1 300 ? -19.494 14.386  -6.344  1.00 34.58 ? 295 HIS C N   1 
ATOM   6229  C CA  . HIS C 1 300 ? -18.515 15.032  -7.218  1.00 33.95 ? 295 HIS C CA  1 
ATOM   6230  C C   . HIS C 1 300 ? -17.370 15.612  -6.383  1.00 33.84 ? 295 HIS C C   1 
ATOM   6231  O O   . HIS C 1 300 ? -17.500 15.773  -5.167  1.00 33.77 ? 295 HIS C O   1 
ATOM   6232  C CB  . HIS C 1 300 ? -19.177 16.125  -8.066  1.00 33.89 ? 295 HIS C CB  1 
ATOM   6233  C CG  . HIS C 1 300 ? -19.348 17.430  -7.350  1.00 33.31 ? 295 HIS C CG  1 
ATOM   6234  N ND1 . HIS C 1 300 ? -20.530 17.797  -6.743  1.00 32.49 ? 295 HIS C ND1 1 
ATOM   6235  C CD2 . HIS C 1 300 ? -18.484 18.452  -7.142  1.00 32.25 ? 295 HIS C CD2 1 
ATOM   6236  C CE1 . HIS C 1 300 ? -20.387 18.990  -6.194  1.00 32.37 ? 295 HIS C CE1 1 
ATOM   6237  N NE2 . HIS C 1 300 ? -19.154 19.409  -6.421  1.00 32.13 ? 295 HIS C NE2 1 
ATOM   6238  N N   . ASN C 1 301 ? -16.254 15.929  -7.033  1.00 33.67 ? 296 ASN C N   1 
ATOM   6239  C CA  . ASN C 1 301 ? -15.105 16.515  -6.341  1.00 33.73 ? 296 ASN C CA  1 
ATOM   6240  C C   . ASN C 1 301 ? -14.561 17.780  -7.022  1.00 33.56 ? 296 ASN C C   1 
ATOM   6241  O O   . ASN C 1 301 ? -13.386 18.119  -6.879  1.00 33.52 ? 296 ASN C O   1 
ATOM   6242  C CB  . ASN C 1 301 ? -13.996 15.465  -6.138  1.00 33.69 ? 296 ASN C CB  1 
ATOM   6243  C CG  . ASN C 1 301 ? -13.395 14.967  -7.451  1.00 34.37 ? 296 ASN C CG  1 
ATOM   6244  O OD1 . ASN C 1 301 ? -13.911 15.239  -8.542  1.00 35.29 ? 296 ASN C OD1 1 
ATOM   6245  N ND2 . ASN C 1 301 ? -12.297 14.227  -7.346  1.00 34.32 ? 296 ASN C ND2 1 
ATOM   6246  N N   . ILE C 1 302 ? -15.434 18.477  -7.745  1.00 33.36 ? 297 ILE C N   1 
ATOM   6247  C CA  . ILE C 1 302 ? -15.032 19.613  -8.581  1.00 33.12 ? 297 ILE C CA  1 
ATOM   6248  C C   . ILE C 1 302 ? -14.676 20.847  -7.750  1.00 32.95 ? 297 ILE C C   1 
ATOM   6249  O O   . ILE C 1 302 ? -13.581 21.391  -7.878  1.00 32.83 ? 297 ILE C O   1 
ATOM   6250  C CB  . ILE C 1 302 ? -16.135 19.971  -9.629  1.00 33.18 ? 297 ILE C CB  1 
ATOM   6251  C CG1 . ILE C 1 302 ? -16.631 18.718  -10.376 1.00 32.98 ? 297 ILE C CG1 1 
ATOM   6252  C CG2 . ILE C 1 302 ? -15.651 21.055  -10.598 1.00 32.95 ? 297 ILE C CG2 1 
ATOM   6253  C CD1 . ILE C 1 302 ? -15.557 17.938  -11.109 1.00 33.09 ? 297 ILE C CD1 1 
ATOM   6254  N N   . HIS C 1 303 ? -15.616 21.267  -6.904  1.00 32.77 ? 298 HIS C N   1 
ATOM   6255  C CA  . HIS C 1 303 ? -15.513 22.482  -6.102  1.00 32.65 ? 298 HIS C CA  1 
ATOM   6256  C C   . HIS C 1 303 ? -16.668 22.460  -5.102  1.00 32.62 ? 298 HIS C C   1 
ATOM   6257  O O   . HIS C 1 303 ? -17.775 22.062  -5.463  1.00 32.62 ? 298 HIS C O   1 
ATOM   6258  C CB  . HIS C 1 303 ? -15.623 23.719  -6.998  1.00 32.59 ? 298 HIS C CB  1 
ATOM   6259  C CG  . HIS C 1 303 ? -15.145 24.984  -6.357  1.00 32.68 ? 298 HIS C CG  1 
ATOM   6260  N ND1 . HIS C 1 303 ? -15.957 25.777  -5.575  1.00 33.16 ? 298 HIS C ND1 1 
ATOM   6261  C CD2 . HIS C 1 303 ? -13.939 25.599  -6.390  1.00 32.99 ? 298 HIS C CD2 1 
ATOM   6262  C CE1 . HIS C 1 303 ? -15.272 26.826  -5.155  1.00 33.65 ? 298 HIS C CE1 1 
ATOM   6263  N NE2 . HIS C 1 303 ? -14.044 26.741  -5.635  1.00 33.13 ? 298 HIS C NE2 1 
ATOM   6264  N N   . PRO C 1 304 ? -16.416 22.872  -3.843  1.00 32.78 ? 299 PRO C N   1 
ATOM   6265  C CA  . PRO C 1 304 ? -17.451 22.910  -2.804  1.00 32.92 ? 299 PRO C CA  1 
ATOM   6266  C C   . PRO C 1 304 ? -18.566 23.942  -3.030  1.00 33.36 ? 299 PRO C C   1 
ATOM   6267  O O   . PRO C 1 304 ? -19.700 23.705  -2.617  1.00 33.36 ? 299 PRO C O   1 
ATOM   6268  C CB  . PRO C 1 304 ? -16.664 23.257  -1.534  1.00 32.84 ? 299 PRO C CB  1 
ATOM   6269  C CG  . PRO C 1 304 ? -15.430 23.921  -2.016  1.00 32.81 ? 299 PRO C CG  1 
ATOM   6270  C CD  . PRO C 1 304 ? -15.090 23.220  -3.296  1.00 32.96 ? 299 PRO C CD  1 
ATOM   6271  N N   . LEU C 1 305 ? -18.251 25.073  -3.663  1.00 33.79 ? 300 LEU C N   1 
ATOM   6272  C CA  . LEU C 1 305 ? -19.237 26.139  -3.869  1.00 34.33 ? 300 LEU C CA  1 
ATOM   6273  C C   . LEU C 1 305 ? -19.978 25.970  -5.196  1.00 34.65 ? 300 LEU C C   1 
ATOM   6274  O O   . LEU C 1 305 ? -19.438 26.237  -6.267  1.00 34.67 ? 300 LEU C O   1 
ATOM   6275  C CB  . LEU C 1 305 ? -18.588 27.528  -3.770  1.00 34.43 ? 300 LEU C CB  1 
ATOM   6276  C CG  . LEU C 1 305 ? -17.894 27.903  -2.450  1.00 35.00 ? 300 LEU C CG  1 
ATOM   6277  C CD1 . LEU C 1 305 ? -17.089 29.196  -2.600  1.00 35.01 ? 300 LEU C CD1 1 
ATOM   6278  C CD2 . LEU C 1 305 ? -18.886 28.016  -1.291  1.00 35.18 ? 300 LEU C CD2 1 
ATOM   6279  N N   . THR C 1 306 ? -21.221 25.510  -5.108  1.00 34.94 ? 301 THR C N   1 
ATOM   6280  C CA  . THR C 1 306 ? -22.013 25.200  -6.284  1.00 35.27 ? 301 THR C CA  1 
ATOM   6281  C C   . THR C 1 306 ? -23.398 25.836  -6.192  1.00 35.57 ? 301 THR C C   1 
ATOM   6282  O O   . THR C 1 306 ? -23.837 26.238  -5.113  1.00 35.31 ? 301 THR C O   1 
ATOM   6283  C CB  . THR C 1 306 ? -22.177 23.663  -6.481  1.00 35.29 ? 301 THR C CB  1 
ATOM   6284  O OG1 . THR C 1 306 ? -23.172 23.159  -5.581  1.00 35.65 ? 301 THR C OG1 1 
ATOM   6285  C CG2 . THR C 1 306 ? -20.867 22.923  -6.252  1.00 35.37 ? 301 THR C CG2 1 
ATOM   6286  N N   . ILE C 1 307 ? -24.083 25.924  -7.330  1.00 36.10 ? 302 ILE C N   1 
ATOM   6287  C CA  . ILE C 1 307 ? -25.472 26.370  -7.351  1.00 36.78 ? 302 ILE C CA  1 
ATOM   6288  C C   . ILE C 1 307 ? -26.331 25.468  -8.253  1.00 37.35 ? 302 ILE C C   1 
ATOM   6289  O O   . ILE C 1 307 ? -25.871 25.004  -9.299  1.00 37.16 ? 302 ILE C O   1 
ATOM   6290  C CB  . ILE C 1 307 ? -25.595 27.889  -7.706  1.00 36.57 ? 302 ILE C CB  1 
ATOM   6291  C CG1 . ILE C 1 307 ? -27.005 28.404  -7.391  1.00 36.62 ? 302 ILE C CG1 1 
ATOM   6292  C CG2 . ILE C 1 307 ? -25.161 28.169  -9.154  1.00 36.65 ? 302 ILE C CG2 1 
ATOM   6293  C CD1 . ILE C 1 307 ? -27.164 29.916  -7.466  1.00 36.71 ? 302 ILE C CD1 1 
ATOM   6294  N N   . GLY C 1 308 ? -27.564 25.207  -7.818  1.00 38.11 ? 303 GLY C N   1 
ATOM   6295  C CA  . GLY C 1 308 ? -28.512 24.397  -8.586  1.00 39.20 ? 303 GLY C CA  1 
ATOM   6296  C C   . GLY C 1 308 ? -28.710 23.008  -8.010  1.00 39.93 ? 303 GLY C C   1 
ATOM   6297  O O   . GLY C 1 308 ? -28.411 22.774  -6.840  1.00 40.23 ? 303 GLY C O   1 
ATOM   6298  N N   . GLU C 1 309 ? -29.231 22.093  -8.830  1.00 40.58 ? 304 GLU C N   1 
ATOM   6299  C CA  . GLU C 1 309 ? -29.379 20.683  -8.442  1.00 41.38 ? 304 GLU C CA  1 
ATOM   6300  C C   . GLU C 1 309 ? -28.074 19.924  -8.688  1.00 41.47 ? 304 GLU C C   1 
ATOM   6301  O O   . GLU C 1 309 ? -27.780 19.498  -9.811  1.00 41.70 ? 304 GLU C O   1 
ATOM   6302  C CB  . GLU C 1 309 ? -30.578 20.011  -9.140  1.00 41.61 ? 304 GLU C CB  1 
ATOM   6303  C CG  . GLU C 1 309 ? -31.026 20.668  -10.458 1.00 43.61 ? 304 GLU C CG  1 
ATOM   6304  C CD  . GLU C 1 309 ? -32.363 20.129  -10.987 1.00 46.28 ? 304 GLU C CD  1 
ATOM   6305  O OE1 . GLU C 1 309 ? -33.276 20.952  -11.244 1.00 46.53 ? 304 GLU C OE1 1 
ATOM   6306  O OE2 . GLU C 1 309 ? -32.502 18.888  -11.149 1.00 47.19 ? 304 GLU C OE2 1 
ATOM   6307  N N   . CYS C 1 310 ? -27.293 19.774  -7.622  1.00 41.44 ? 305 CYS C N   1 
ATOM   6308  C CA  . CYS C 1 310 ? -25.944 19.223  -7.708  1.00 41.34 ? 305 CYS C CA  1 
ATOM   6309  C C   . CYS C 1 310 ? -25.785 17.930  -6.916  1.00 41.10 ? 305 CYS C C   1 
ATOM   6310  O O   . CYS C 1 310 ? -26.492 17.715  -5.927  1.00 41.32 ? 305 CYS C O   1 
ATOM   6311  C CB  . CYS C 1 310 ? -24.936 20.254  -7.193  1.00 41.33 ? 305 CYS C CB  1 
ATOM   6312  S SG  . CYS C 1 310 ? -24.895 21.782  -8.158  1.00 42.09 ? 305 CYS C SG  1 
ATOM   6313  N N   . PRO C 1 311 ? -24.855 17.059  -7.347  1.00 40.86 ? 306 PRO C N   1 
ATOM   6314  C CA  . PRO C 1 311 ? -24.403 15.983  -6.466  1.00 40.60 ? 306 PRO C CA  1 
ATOM   6315  C C   . PRO C 1 311 ? -23.700 16.560  -5.237  1.00 40.53 ? 306 PRO C C   1 
ATOM   6316  O O   . PRO C 1 311 ? -23.464 17.769  -5.167  1.00 40.47 ? 306 PRO C O   1 
ATOM   6317  C CB  . PRO C 1 311 ? -23.414 15.196  -7.339  1.00 40.57 ? 306 PRO C CB  1 
ATOM   6318  C CG  . PRO C 1 311 ? -23.114 16.076  -8.517  1.00 40.57 ? 306 PRO C CG  1 
ATOM   6319  C CD  . PRO C 1 311 ? -24.328 16.910  -8.716  1.00 40.86 ? 306 PRO C CD  1 
ATOM   6320  N N   . LYS C 1 312 ? -23.367 15.711  -4.273  1.00 40.43 ? 307 LYS C N   1 
ATOM   6321  C CA  . LYS C 1 312 ? -22.777 16.199  -3.032  1.00 40.37 ? 307 LYS C CA  1 
ATOM   6322  C C   . LYS C 1 312 ? -21.254 16.240  -3.093  1.00 39.85 ? 307 LYS C C   1 
ATOM   6323  O O   . LYS C 1 312 ? -20.607 15.250  -3.439  1.00 39.91 ? 307 LYS C O   1 
ATOM   6324  C CB  . LYS C 1 312 ? -23.285 15.396  -1.827  1.00 40.65 ? 307 LYS C CB  1 
ATOM   6325  C CG  . LYS C 1 312 ? -24.799 15.538  -1.569  1.00 41.77 ? 307 LYS C CG  1 
ATOM   6326  C CD  . LYS C 1 312 ? -25.299 16.974  -1.806  1.00 43.95 ? 307 LYS C CD  1 
ATOM   6327  C CE  . LYS C 1 312 ? -26.783 17.148  -1.471  1.00 44.86 ? 307 LYS C CE  1 
ATOM   6328  N NZ  . LYS C 1 312 ? -26.991 17.571  -0.050  1.00 45.41 ? 307 LYS C NZ  1 
ATOM   6329  N N   . TYR C 1 313 ? -20.688 17.399  -2.772  1.00 39.19 ? 308 TYR C N   1 
ATOM   6330  C CA  . TYR C 1 313 ? -19.244 17.574  -2.863  1.00 38.77 ? 308 TYR C CA  1 
ATOM   6331  C C   . TYR C 1 313 ? -18.494 16.723  -1.841  1.00 38.80 ? 308 TYR C C   1 
ATOM   6332  O O   . TYR C 1 313 ? -18.873 16.650  -0.673  1.00 38.74 ? 308 TYR C O   1 
ATOM   6333  C CB  . TYR C 1 313 ? -18.823 19.048  -2.743  1.00 38.35 ? 308 TYR C CB  1 
ATOM   6334  C CG  . TYR C 1 313 ? -17.315 19.225  -2.808  1.00 37.26 ? 308 TYR C CG  1 
ATOM   6335  C CD1 . TYR C 1 313 ? -16.645 19.234  -4.030  1.00 35.81 ? 308 TYR C CD1 1 
ATOM   6336  C CD2 . TYR C 1 313 ? -16.556 19.346  -1.648  1.00 35.89 ? 308 TYR C CD2 1 
ATOM   6337  C CE1 . TYR C 1 313 ? -15.262 19.380  -4.092  1.00 35.10 ? 308 TYR C CE1 1 
ATOM   6338  C CE2 . TYR C 1 313 ? -15.169 19.488  -1.703  1.00 35.47 ? 308 TYR C CE2 1 
ATOM   6339  C CZ  . TYR C 1 313 ? -14.531 19.508  -2.926  1.00 34.83 ? 308 TYR C CZ  1 
ATOM   6340  O OH  . TYR C 1 313 ? -13.162 19.649  -2.982  1.00 33.70 ? 308 TYR C OH  1 
ATOM   6341  N N   . VAL C 1 314 ? -17.418 16.098  -2.307  1.00 38.76 ? 309 VAL C N   1 
ATOM   6342  C CA  . VAL C 1 314 ? -16.566 15.271  -1.476  1.00 38.99 ? 309 VAL C CA  1 
ATOM   6343  C C   . VAL C 1 314 ? -15.121 15.534  -1.903  1.00 39.10 ? 309 VAL C C   1 
ATOM   6344  O O   . VAL C 1 314 ? -14.876 15.937  -3.036  1.00 39.04 ? 309 VAL C O   1 
ATOM   6345  C CB  . VAL C 1 314 ? -16.972 13.772  -1.598  1.00 39.00 ? 309 VAL C CB  1 
ATOM   6346  C CG1 . VAL C 1 314 ? -16.269 13.092  -2.761  1.00 38.71 ? 309 VAL C CG1 1 
ATOM   6347  C CG2 . VAL C 1 314 ? -16.712 13.037  -0.307  1.00 39.24 ? 309 VAL C CG2 1 
ATOM   6348  N N   . LYS C 1 315 ? -14.169 15.336  -0.999  1.00 39.48 ? 310 LYS C N   1 
ATOM   6349  C CA  . LYS C 1 315 ? -12.772 15.665  -1.298  1.00 40.00 ? 310 LYS C CA  1 
ATOM   6350  C C   . LYS C 1 315 ? -11.966 14.540  -1.956  1.00 40.22 ? 310 LYS C C   1 
ATOM   6351  O O   . LYS C 1 315 ? -10.886 14.788  -2.489  1.00 40.52 ? 310 LYS C O   1 
ATOM   6352  C CB  . LYS C 1 315 ? -12.054 16.195  -0.053  1.00 40.02 ? 310 LYS C CB  1 
ATOM   6353  C CG  . LYS C 1 315 ? -12.261 17.694  0.184   1.00 40.94 ? 310 LYS C CG  1 
ATOM   6354  C CD  . LYS C 1 315 ? -11.466 18.208  1.380   1.00 42.36 ? 310 LYS C CD  1 
ATOM   6355  C CE  . LYS C 1 315 ? -10.007 18.449  1.015   1.00 44.12 ? 310 LYS C CE  1 
ATOM   6356  N NZ  . LYS C 1 315 ? -9.189  18.847  2.200   1.00 45.46 ? 310 LYS C NZ  1 
ATOM   6357  N N   . SER C 1 316 ? -12.501 13.322  -1.942  1.00 40.40 ? 311 SER C N   1 
ATOM   6358  C CA  . SER C 1 316 ? -11.781 12.148  -2.441  1.00 40.61 ? 311 SER C CA  1 
ATOM   6359  C C   . SER C 1 316 ? -11.560 12.139  -3.950  1.00 40.84 ? 311 SER C C   1 
ATOM   6360  O O   . SER C 1 316 ? -12.280 12.798  -4.700  1.00 40.83 ? 311 SER C O   1 
ATOM   6361  C CB  . SER C 1 316 ? -12.477 10.855  -2.003  1.00 40.62 ? 311 SER C CB  1 
ATOM   6362  O OG  . SER C 1 316 ? -13.868 10.892  -2.235  1.00 40.22 ? 311 SER C OG  1 
ATOM   6363  N N   . ASN C 1 317 ? -10.550 11.385  -4.377  1.00 41.15 ? 312 ASN C N   1 
ATOM   6364  C CA  . ASN C 1 317 ? -10.220 11.242  -5.793  1.00 41.62 ? 312 ASN C CA  1 
ATOM   6365  C C   . ASN C 1 317 ? -10.832 9.992   -6.428  1.00 41.61 ? 312 ASN C C   1 
ATOM   6366  O O   . ASN C 1 317 ? -10.830 9.847   -7.652  1.00 41.73 ? 312 ASN C O   1 
ATOM   6367  C CB  . ASN C 1 317 ? -8.699  11.257  -5.991  1.00 41.86 ? 312 ASN C CB  1 
ATOM   6368  C CG  . ASN C 1 317 ? -8.109  12.655  -5.870  1.00 42.85 ? 312 ASN C CG  1 
ATOM   6369  O OD1 . ASN C 1 317 ? -8.200  13.465  -6.798  1.00 44.08 ? 312 ASN C OD1 1 
ATOM   6370  N ND2 . ASN C 1 317 ? -7.501  12.945  -4.721  1.00 43.08 ? 312 ASN C ND2 1 
ATOM   6371  N N   . ARG C 1 318 ? -11.357 9.103   -5.588  1.00 41.59 ? 313 ARG C N   1 
ATOM   6372  C CA  . ARG C 1 318 ? -11.951 7.842   -6.029  1.00 41.71 ? 313 ARG C CA  1 
ATOM   6373  C C   . ARG C 1 318 ? -13.027 7.367   -5.055  1.00 41.21 ? 313 ARG C C   1 
ATOM   6374  O O   . ARG C 1 318 ? -12.837 7.417   -3.840  1.00 41.35 ? 313 ARG C O   1 
ATOM   6375  C CB  . ARG C 1 318 ? -10.872 6.759   -6.167  1.00 42.01 ? 313 ARG C CB  1 
ATOM   6376  C CG  . ARG C 1 318 ? -10.280 6.615   -7.568  1.00 43.76 ? 313 ARG C CG  1 
ATOM   6377  C CD  . ARG C 1 318 ? -9.259  5.468   -7.652  1.00 46.87 ? 313 ARG C CD  1 
ATOM   6378  N NE  . ARG C 1 318 ? -9.748  4.224   -7.048  1.00 48.91 ? 313 ARG C NE  1 
ATOM   6379  C CZ  . ARG C 1 318 ? -10.533 3.335   -7.656  1.00 49.85 ? 313 ARG C CZ  1 
ATOM   6380  N NH1 . ARG C 1 318 ? -10.941 3.534   -8.907  1.00 50.22 ? 313 ARG C NH1 1 
ATOM   6381  N NH2 . ARG C 1 318 ? -10.918 2.241   -7.005  1.00 50.15 ? 313 ARG C NH2 1 
ATOM   6382  N N   . LEU C 1 319 ? -14.156 6.920   -5.599  1.00 40.50 ? 314 LEU C N   1 
ATOM   6383  C CA  . LEU C 1 319 ? -15.219 6.291   -4.817  1.00 39.99 ? 314 LEU C CA  1 
ATOM   6384  C C   . LEU C 1 319 ? -15.899 5.230   -5.669  1.00 39.71 ? 314 LEU C C   1 
ATOM   6385  O O   . LEU C 1 319 ? -16.676 5.553   -6.574  1.00 39.77 ? 314 LEU C O   1 
ATOM   6386  C CB  . LEU C 1 319 ? -16.256 7.312   -4.333  1.00 39.92 ? 314 LEU C CB  1 
ATOM   6387  C CG  . LEU C 1 319 ? -16.119 8.029   -2.985  1.00 39.94 ? 314 LEU C CG  1 
ATOM   6388  C CD1 . LEU C 1 319 ? -17.368 8.856   -2.731  1.00 39.41 ? 314 LEU C CD1 1 
ATOM   6389  C CD2 . LEU C 1 319 ? -15.885 7.064   -1.822  1.00 39.63 ? 314 LEU C CD2 1 
ATOM   6390  N N   . VAL C 1 320 ? -15.591 3.966   -5.391  1.00 39.19 ? 315 VAL C N   1 
ATOM   6391  C CA  . VAL C 1 320 ? -16.131 2.856   -6.176  1.00 38.81 ? 315 VAL C CA  1 
ATOM   6392  C C   . VAL C 1 320 ? -16.764 1.791   -5.281  1.00 38.49 ? 315 VAL C C   1 
ATOM   6393  O O   . VAL C 1 320 ? -16.121 1.231   -4.392  1.00 38.22 ? 315 VAL C O   1 
ATOM   6394  C CB  . VAL C 1 320 ? -15.071 2.223   -7.123  1.00 38.81 ? 315 VAL C CB  1 
ATOM   6395  C CG1 . VAL C 1 320 ? -15.704 1.147   -8.000  1.00 38.63 ? 315 VAL C CG1 1 
ATOM   6396  C CG2 . VAL C 1 320 ? -14.425 3.286   -8.003  1.00 38.61 ? 315 VAL C CG2 1 
ATOM   6397  N N   . LEU C 1 321 ? -18.036 1.528   -5.547  1.00 38.23 ? 316 LEU C N   1 
ATOM   6398  C CA  . LEU C 1 321 ? -18.831 0.575   -4.801  1.00 37.93 ? 316 LEU C CA  1 
ATOM   6399  C C   . LEU C 1 321 ? -18.784 -0.781  -5.496  1.00 37.79 ? 316 LEU C C   1 
ATOM   6400  O O   . LEU C 1 321 ? -19.019 -0.875  -6.702  1.00 37.49 ? 316 LEU C O   1 
ATOM   6401  C CB  . LEU C 1 321 ? -20.274 1.084   -4.748  1.00 37.81 ? 316 LEU C CB  1 
ATOM   6402  C CG  . LEU C 1 321 ? -21.172 0.938   -3.519  1.00 38.45 ? 316 LEU C CG  1 
ATOM   6403  C CD1 . LEU C 1 321 ? -20.473 1.280   -2.197  1.00 38.60 ? 316 LEU C CD1 1 
ATOM   6404  C CD2 . LEU C 1 321 ? -22.395 1.824   -3.712  1.00 38.89 ? 316 LEU C CD2 1 
ATOM   6405  N N   . ALA C 1 322 ? -18.467 -1.829  -4.740  1.00 37.82 ? 317 ALA C N   1 
ATOM   6406  C CA  . ALA C 1 322 ? -18.566 -3.196  -5.255  1.00 37.83 ? 317 ALA C CA  1 
ATOM   6407  C C   . ALA C 1 322 ? -20.032 -3.600  -5.385  1.00 37.83 ? 317 ALA C C   1 
ATOM   6408  O O   . ALA C 1 322 ? -20.846 -3.326  -4.497  1.00 37.60 ? 317 ALA C O   1 
ATOM   6409  C CB  . ALA C 1 322 ? -17.820 -4.175  -4.355  1.00 37.81 ? 317 ALA C CB  1 
ATOM   6410  N N   . THR C 1 323 ? -20.365 -4.234  -6.503  1.00 37.92 ? 318 THR C N   1 
ATOM   6411  C CA  . THR C 1 323 ? -21.719 -4.728  -6.733  1.00 38.14 ? 318 THR C CA  1 
ATOM   6412  C C   . THR C 1 323 ? -21.693 -6.228  -7.004  1.00 38.45 ? 318 THR C C   1 
ATOM   6413  O O   . THR C 1 323 ? -22.575 -6.967  -6.565  1.00 38.37 ? 318 THR C O   1 
ATOM   6414  C CB  . THR C 1 323 ? -22.426 -3.975  -7.888  1.00 38.13 ? 318 THR C CB  1 
ATOM   6415  O OG1 . THR C 1 323 ? -21.566 -3.924  -9.032  1.00 37.72 ? 318 THR C OG1 1 
ATOM   6416  C CG2 . THR C 1 323 ? -22.784 -2.546  -7.463  1.00 37.86 ? 318 THR C CG2 1 
ATOM   6417  N N   . GLY C 1 324 ? -20.664 -6.669  -7.719  1.00 38.94 ? 319 GLY C N   1 
ATOM   6418  C CA  . GLY C 1 324 ? -20.454 -8.086  -7.989  1.00 39.59 ? 319 GLY C CA  1 
ATOM   6419  C C   . GLY C 1 324 ? -19.538 -8.741  -6.971  1.00 40.00 ? 319 GLY C C   1 
ATOM   6420  O O   . GLY C 1 324 ? -19.339 -8.225  -5.869  1.00 39.88 ? 319 GLY C O   1 
ATOM   6421  N N   . LEU C 1 325 ? -18.974 -9.881  -7.355  1.00 40.51 ? 320 LEU C N   1 
ATOM   6422  C CA  . LEU C 1 325 ? -18.136 -10.680 -6.461  1.00 41.02 ? 320 LEU C CA  1 
ATOM   6423  C C   . LEU C 1 325 ? -16.677 -10.677 -6.903  1.00 41.30 ? 320 LEU C C   1 
ATOM   6424  O O   . LEU C 1 325 ? -16.340 -10.089 -7.929  1.00 41.14 ? 320 LEU C O   1 
ATOM   6425  C CB  . LEU C 1 325 ? -18.683 -12.112 -6.367  1.00 40.99 ? 320 LEU C CB  1 
ATOM   6426  C CG  . LEU C 1 325 ? -19.053 -12.831 -7.667  1.00 40.83 ? 320 LEU C CG  1 
ATOM   6427  C CD1 . LEU C 1 325 ? -17.861 -13.596 -8.206  1.00 40.95 ? 320 LEU C CD1 1 
ATOM   6428  C CD2 . LEU C 1 325 ? -20.214 -13.775 -7.436  1.00 40.95 ? 320 LEU C CD2 1 
ATOM   6429  N N   . ARG C 1 326 ? -15.824 -11.334 -6.118  1.00 41.96 ? 321 ARG C N   1 
ATOM   6430  C CA  . ARG C 1 326 ? -14.395 -11.442 -6.417  1.00 42.71 ? 321 ARG C CA  1 
ATOM   6431  C C   . ARG C 1 326 ? -14.150 -12.240 -7.702  1.00 43.21 ? 321 ARG C C   1 
ATOM   6432  O O   . ARG C 1 326 ? -14.518 -13.414 -7.799  1.00 43.32 ? 321 ARG C O   1 
ATOM   6433  C CB  . ARG C 1 326 ? -13.649 -12.080 -5.239  1.00 42.61 ? 321 ARG C CB  1 
ATOM   6434  C CG  . ARG C 1 326 ? -12.130 -12.066 -5.374  1.00 43.13 ? 321 ARG C CG  1 
ATOM   6435  C CD  . ARG C 1 326 ? -11.444 -12.795 -4.225  1.00 44.07 ? 321 ARG C CD  1 
ATOM   6436  N NE  . ARG C 1 326 ? -11.773 -12.214 -2.924  1.00 44.74 ? 321 ARG C NE  1 
ATOM   6437  C CZ  . ARG C 1 326 ? -11.056 -11.280 -2.303  1.00 45.52 ? 321 ARG C CZ  1 
ATOM   6438  N NH1 . ARG C 1 326 ? -9.942  -10.799 -2.853  1.00 45.42 ? 321 ARG C NH1 1 
ATOM   6439  N NH2 . ARG C 1 326 ? -11.456 -10.826 -1.121  1.00 45.33 ? 321 ARG C NH2 1 
ATOM   6440  N N   . ASN C 1 327 ? -13.530 -11.589 -8.684  1.00 43.90 ? 322 ASN C N   1 
ATOM   6441  C CA  . ASN C 1 327 ? -13.241 -12.213 -9.974  1.00 44.60 ? 322 ASN C CA  1 
ATOM   6442  C C   . ASN C 1 327 ? -12.083 -13.215 -9.917  1.00 45.18 ? 322 ASN C C   1 
ATOM   6443  O O   . ASN C 1 327 ? -11.225 -13.147 -9.025  1.00 45.31 ? 322 ASN C O   1 
ATOM   6444  C CB  . ASN C 1 327 ? -12.957 -11.140 -11.030 1.00 44.57 ? 322 ASN C CB  1 
ATOM   6445  C CG  . ASN C 1 327 ? -13.376 -11.564 -12.429 1.00 44.35 ? 322 ASN C CG  1 
ATOM   6446  O OD1 . ASN C 1 327 ? -13.844 -12.682 -12.647 1.00 43.59 ? 322 ASN C OD1 1 
ATOM   6447  N ND2 . ASN C 1 327 ? -13.218 -10.658 -13.384 1.00 44.53 ? 322 ASN C ND2 1 
ATOM   6448  N N   . THR C 1 328 ? -12.066 -14.136 -10.879 1.00 45.75 ? 323 THR C N   1 
ATOM   6449  C CA  . THR C 1 328 ? -11.033 -15.166 -10.970 1.00 46.12 ? 323 THR C CA  1 
ATOM   6450  C C   . THR C 1 328 ? -10.113 -14.895 -12.161 1.00 46.27 ? 323 THR C C   1 
ATOM   6451  O O   . THR C 1 328 ? -8.892  -14.812 -12.008 1.00 46.52 ? 323 THR C O   1 
ATOM   6452  C CB  . THR C 1 328 ? -11.665 -16.575 -11.103 1.00 46.32 ? 323 THR C CB  1 
ATOM   6453  O OG1 . THR C 1 328 ? -12.687 -16.741 -10.109 1.00 46.40 ? 323 THR C OG1 1 
ATOM   6454  C CG2 . THR C 1 328 ? -10.608 -17.676 -10.939 1.00 46.33 ? 323 THR C CG2 1 
ATOM   6455  N N   . GLY D 2 1   ? -12.407 -16.064 1.523   1.00 39.22 ? 1   GLY D N   1 
ATOM   6456  C CA  . GLY D 2 1   ? -13.154 -15.017 2.276   1.00 38.97 ? 1   GLY D CA  1 
ATOM   6457  C C   . GLY D 2 1   ? -13.764 -15.553 3.558   1.00 38.92 ? 1   GLY D C   1 
ATOM   6458  O O   . GLY D 2 1   ? -13.457 -16.668 3.992   1.00 38.81 ? 1   GLY D O   1 
ATOM   6459  N N   . LEU D 2 2   ? -14.649 -14.758 4.150   1.00 38.70 ? 2   LEU D N   1 
ATOM   6460  C CA  . LEU D 2 2   ? -15.223 -15.056 5.456   1.00 38.47 ? 2   LEU D CA  1 
ATOM   6461  C C   . LEU D 2 2   ? -16.002 -16.375 5.509   1.00 38.51 ? 2   LEU D C   1 
ATOM   6462  O O   . LEU D 2 2   ? -16.054 -17.023 6.554   1.00 38.66 ? 2   LEU D O   1 
ATOM   6463  C CB  . LEU D 2 2   ? -16.105 -13.888 5.910   1.00 38.28 ? 2   LEU D CB  1 
ATOM   6464  C CG  . LEU D 2 2   ? -16.174 -13.520 7.394   1.00 37.87 ? 2   LEU D CG  1 
ATOM   6465  C CD1 . LEU D 2 2   ? -14.802 -13.156 7.972   1.00 37.20 ? 2   LEU D CD1 1 
ATOM   6466  C CD2 . LEU D 2 2   ? -17.148 -12.376 7.589   1.00 37.18 ? 2   LEU D CD2 1 
ATOM   6467  N N   . PHE D 2 3   ? -16.593 -16.780 4.390   1.00 38.52 ? 3   PHE D N   1 
ATOM   6468  C CA  . PHE D 2 3   ? -17.439 -17.974 4.382   1.00 38.54 ? 3   PHE D CA  1 
ATOM   6469  C C   . PHE D 2 3   ? -16.827 -19.205 3.708   1.00 38.79 ? 3   PHE D C   1 
ATOM   6470  O O   . PHE D 2 3   ? -17.415 -20.284 3.741   1.00 38.88 ? 3   PHE D O   1 
ATOM   6471  C CB  . PHE D 2 3   ? -18.826 -17.651 3.819   1.00 38.42 ? 3   PHE D CB  1 
ATOM   6472  C CG  . PHE D 2 3   ? -19.657 -16.806 4.738   1.00 37.62 ? 3   PHE D CG  1 
ATOM   6473  C CD1 . PHE D 2 3   ? -20.411 -17.393 5.746   1.00 36.95 ? 3   PHE D CD1 1 
ATOM   6474  C CD2 . PHE D 2 3   ? -19.671 -15.422 4.612   1.00 36.62 ? 3   PHE D CD2 1 
ATOM   6475  C CE1 . PHE D 2 3   ? -21.172 -16.618 6.607   1.00 36.44 ? 3   PHE D CE1 1 
ATOM   6476  C CE2 . PHE D 2 3   ? -20.432 -14.640 5.467   1.00 35.94 ? 3   PHE D CE2 1 
ATOM   6477  C CZ  . PHE D 2 3   ? -21.181 -15.239 6.466   1.00 36.14 ? 3   PHE D CZ  1 
ATOM   6478  N N   . GLY D 2 4   ? -15.649 -19.039 3.111   1.00 39.08 ? 4   GLY D N   1 
ATOM   6479  C CA  . GLY D 2 4   ? -14.871 -20.164 2.586   1.00 39.64 ? 4   GLY D CA  1 
ATOM   6480  C C   . GLY D 2 4   ? -15.329 -20.771 1.264   1.00 40.16 ? 4   GLY D C   1 
ATOM   6481  O O   . GLY D 2 4   ? -14.740 -21.748 0.803   1.00 40.29 ? 4   GLY D O   1 
ATOM   6482  N N   . ALA D 2 5   ? -16.367 -20.198 0.653   1.00 40.40 ? 5   ALA D N   1 
ATOM   6483  C CA  . ALA D 2 5   ? -16.919 -20.716 -0.597  1.00 40.66 ? 5   ALA D CA  1 
ATOM   6484  C C   . ALA D 2 5   ? -16.233 -20.135 -1.836  1.00 41.02 ? 5   ALA D C   1 
ATOM   6485  O O   . ALA D 2 5   ? -15.595 -20.871 -2.592  1.00 41.17 ? 5   ALA D O   1 
ATOM   6486  C CB  . ALA D 2 5   ? -18.430 -20.500 -0.651  1.00 40.49 ? 5   ALA D CB  1 
ATOM   6487  N N   . ILE D 2 6   ? -16.366 -18.825 -2.044  1.00 41.28 ? 6   ILE D N   1 
ATOM   6488  C CA  . ILE D 2 6   ? -15.717 -18.153 -3.171  1.00 41.68 ? 6   ILE D CA  1 
ATOM   6489  C C   . ILE D 2 6   ? -14.201 -18.155 -2.963  1.00 42.16 ? 6   ILE D C   1 
ATOM   6490  O O   . ILE D 2 6   ? -13.715 -17.763 -1.903  1.00 42.12 ? 6   ILE D O   1 
ATOM   6491  C CB  . ILE D 2 6   ? -16.272 -16.710 -3.397  1.00 41.55 ? 6   ILE D CB  1 
ATOM   6492  C CG1 . ILE D 2 6   ? -17.714 -16.774 -3.917  1.00 41.29 ? 6   ILE D CG1 1 
ATOM   6493  C CG2 . ILE D 2 6   ? -15.390 -15.922 -4.374  1.00 41.12 ? 6   ILE D CG2 1 
ATOM   6494  C CD1 . ILE D 2 6   ? -18.389 -15.421 -4.102  1.00 40.77 ? 6   ILE D CD1 1 
ATOM   6495  N N   . ALA D 2 7   ? -13.471 -18.617 -3.977  1.00 42.89 ? 7   ALA D N   1 
ATOM   6496  C CA  . ALA D 2 7   ? -12.016 -18.809 -3.903  1.00 43.78 ? 7   ALA D CA  1 
ATOM   6497  C C   . ALA D 2 7   ? -11.604 -19.645 -2.684  1.00 44.30 ? 7   ALA D C   1 
ATOM   6498  O O   . ALA D 2 7   ? -10.539 -19.438 -2.097  1.00 44.43 ? 7   ALA D O   1 
ATOM   6499  C CB  . ALA D 2 7   ? -11.279 -17.460 -3.932  1.00 43.65 ? 7   ALA D CB  1 
ATOM   6500  N N   . GLY D 2 8   ? -12.467 -20.588 -2.314  1.00 44.87 ? 8   GLY D N   1 
ATOM   6501  C CA  . GLY D 2 8   ? -12.233 -21.458 -1.168  1.00 45.65 ? 8   GLY D CA  1 
ATOM   6502  C C   . GLY D 2 8   ? -12.309 -22.905 -1.599  1.00 46.08 ? 8   GLY D C   1 
ATOM   6503  O O   . GLY D 2 8   ? -11.435 -23.383 -2.324  1.00 46.26 ? 8   GLY D O   1 
ATOM   6504  N N   . PHE D 2 9   ? -13.358 -23.602 -1.167  1.00 46.46 ? 9   PHE D N   1 
ATOM   6505  C CA  . PHE D 2 9   ? -13.562 -24.985 -1.585  1.00 46.83 ? 9   PHE D CA  1 
ATOM   6506  C C   . PHE D 2 9   ? -14.085 -25.071 -3.023  1.00 47.19 ? 9   PHE D C   1 
ATOM   6507  O O   . PHE D 2 9   ? -14.071 -26.142 -3.633  1.00 47.35 ? 9   PHE D O   1 
ATOM   6508  C CB  . PHE D 2 9   ? -14.422 -25.773 -0.582  1.00 46.71 ? 9   PHE D CB  1 
ATOM   6509  C CG  . PHE D 2 9   ? -15.881 -25.392 -0.567  1.00 46.88 ? 9   PHE D CG  1 
ATOM   6510  C CD1 . PHE D 2 9   ? -16.781 -25.979 -1.456  1.00 46.73 ? 9   PHE D CD1 1 
ATOM   6511  C CD2 . PHE D 2 9   ? -16.366 -24.484 0.372   1.00 46.53 ? 9   PHE D CD2 1 
ATOM   6512  C CE1 . PHE D 2 9   ? -18.133 -25.645 -1.432  1.00 46.48 ? 9   PHE D CE1 1 
ATOM   6513  C CE2 . PHE D 2 9   ? -17.720 -24.145 0.406   1.00 46.53 ? 9   PHE D CE2 1 
ATOM   6514  C CZ  . PHE D 2 9   ? -18.605 -24.725 -0.500  1.00 46.45 ? 9   PHE D CZ  1 
ATOM   6515  N N   . ILE D 2 10  ? -14.543 -23.936 -3.548  1.00 47.60 ? 10  ILE D N   1 
ATOM   6516  C CA  . ILE D 2 10  ? -14.753 -23.757 -4.984  1.00 48.03 ? 10  ILE D CA  1 
ATOM   6517  C C   . ILE D 2 10  ? -13.667 -22.792 -5.488  1.00 48.40 ? 10  ILE D C   1 
ATOM   6518  O O   . ILE D 2 10  ? -13.786 -21.572 -5.345  1.00 48.66 ? 10  ILE D O   1 
ATOM   6519  C CB  . ILE D 2 10  ? -16.176 -23.231 -5.311  1.00 47.88 ? 10  ILE D CB  1 
ATOM   6520  C CG1 . ILE D 2 10  ? -17.234 -24.071 -4.592  1.00 47.92 ? 10  ILE D CG1 1 
ATOM   6521  C CG2 . ILE D 2 10  ? -16.421 -23.241 -6.822  1.00 48.11 ? 10  ILE D CG2 1 
ATOM   6522  C CD1 . ILE D 2 10  ? -18.645 -23.548 -4.710  1.00 47.66 ? 10  ILE D CD1 1 
ATOM   6523  N N   . GLU D 2 11  ? -12.614 -23.360 -6.077  1.00 48.77 ? 11  GLU D N   1 
ATOM   6524  C CA  . GLU D 2 11  ? -11.366 -22.635 -6.385  1.00 49.21 ? 11  GLU D CA  1 
ATOM   6525  C C   . GLU D 2 11  ? -11.477 -21.437 -7.344  1.00 49.08 ? 11  GLU D C   1 
ATOM   6526  O O   . GLU D 2 11  ? -10.637 -20.535 -7.299  1.00 49.18 ? 11  GLU D O   1 
ATOM   6527  C CB  . GLU D 2 11  ? -10.296 -23.610 -6.896  1.00 49.38 ? 11  GLU D CB  1 
ATOM   6528  C CG  . GLU D 2 11  ? -9.817  -24.618 -5.852  1.00 50.67 ? 11  GLU D CG  1 
ATOM   6529  C CD  . GLU D 2 11  ? -9.164  -25.846 -6.471  1.00 51.92 ? 11  GLU D CD  1 
ATOM   6530  O OE1 . GLU D 2 11  ? -9.739  -26.949 -6.340  1.00 52.07 ? 11  GLU D OE1 1 
ATOM   6531  O OE2 . GLU D 2 11  ? -8.085  -25.708 -7.095  1.00 52.32 ? 11  GLU D OE2 1 
ATOM   6532  N N   . GLY D 2 12  ? -12.493 -21.431 -8.205  1.00 48.82 ? 12  GLY D N   1 
ATOM   6533  C CA  . GLY D 2 12  ? -12.644 -20.366 -9.189  1.00 48.58 ? 12  GLY D CA  1 
ATOM   6534  C C   . GLY D 2 12  ? -14.045 -20.194 -9.737  1.00 48.55 ? 12  GLY D C   1 
ATOM   6535  O O   . GLY D 2 12  ? -14.906 -21.056 -9.559  1.00 48.64 ? 12  GLY D O   1 
ATOM   6536  N N   . GLY D 2 13  ? -14.269 -19.066 -10.404 1.00 48.47 ? 13  GLY D N   1 
ATOM   6537  C CA  . GLY D 2 13  ? -15.544 -18.772 -11.044 1.00 48.38 ? 13  GLY D CA  1 
ATOM   6538  C C   . GLY D 2 13  ? -15.623 -19.364 -12.437 1.00 48.45 ? 13  GLY D C   1 
ATOM   6539  O O   . GLY D 2 13  ? -14.622 -19.835 -12.975 1.00 48.43 ? 13  GLY D O   1 
ATOM   6540  N N   . TRP D 2 14  ? -16.821 -19.337 -13.015 1.00 48.59 ? 14  TRP D N   1 
ATOM   6541  C CA  . TRP D 2 14  ? -17.071 -19.926 -14.323 1.00 48.75 ? 14  TRP D CA  1 
ATOM   6542  C C   . TRP D 2 14  ? -17.277 -18.853 -15.379 1.00 49.16 ? 14  TRP D C   1 
ATOM   6543  O O   . TRP D 2 14  ? -18.230 -18.071 -15.313 1.00 49.11 ? 14  TRP D O   1 
ATOM   6544  C CB  . TRP D 2 14  ? -18.286 -20.866 -14.288 1.00 48.58 ? 14  TRP D CB  1 
ATOM   6545  C CG  . TRP D 2 14  ? -18.079 -22.136 -13.500 1.00 48.09 ? 14  TRP D CG  1 
ATOM   6546  C CD1 . TRP D 2 14  ? -16.894 -22.784 -13.272 1.00 48.26 ? 14  TRP D CD1 1 
ATOM   6547  C CD2 . TRP D 2 14  ? -19.094 -22.926 -12.863 1.00 47.84 ? 14  TRP D CD2 1 
ATOM   6548  N NE1 . TRP D 2 14  ? -17.107 -23.915 -12.516 1.00 48.37 ? 14  TRP D NE1 1 
ATOM   6549  C CE2 . TRP D 2 14  ? -18.448 -24.027 -12.254 1.00 47.75 ? 14  TRP D CE2 1 
ATOM   6550  C CE3 . TRP D 2 14  ? -20.485 -22.803 -12.737 1.00 47.49 ? 14  TRP D CE3 1 
ATOM   6551  C CZ2 . TRP D 2 14  ? -19.145 -24.998 -11.533 1.00 47.12 ? 14  TRP D CZ2 1 
ATOM   6552  C CZ3 . TRP D 2 14  ? -21.178 -23.776 -12.023 1.00 46.86 ? 14  TRP D CZ3 1 
ATOM   6553  C CH2 . TRP D 2 14  ? -20.506 -24.858 -11.433 1.00 46.85 ? 14  TRP D CH2 1 
ATOM   6554  N N   . GLN D 2 15  ? -16.376 -18.828 -16.357 1.00 49.57 ? 15  GLN D N   1 
ATOM   6555  C CA  . GLN D 2 15  ? -16.470 -17.896 -17.473 1.00 50.01 ? 15  GLN D CA  1 
ATOM   6556  C C   . GLN D 2 15  ? -17.700 -18.212 -18.332 1.00 50.12 ? 15  GLN D C   1 
ATOM   6557  O O   . GLN D 2 15  ? -18.316 -17.314 -18.905 1.00 50.08 ? 15  GLN D O   1 
ATOM   6558  C CB  . GLN D 2 15  ? -15.191 -17.962 -18.313 1.00 50.18 ? 15  GLN D CB  1 
ATOM   6559  C CG  . GLN D 2 15  ? -14.761 -16.634 -18.937 1.00 50.94 ? 15  GLN D CG  1 
ATOM   6560  C CD  . GLN D 2 15  ? -13.842 -15.814 -18.039 1.00 51.43 ? 15  GLN D CD  1 
ATOM   6561  O OE1 . GLN D 2 15  ? -13.818 -15.987 -16.821 1.00 52.15 ? 15  GLN D OE1 1 
ATOM   6562  N NE2 . GLN D 2 15  ? -13.082 -14.912 -18.646 1.00 51.62 ? 15  GLN D NE2 1 
ATOM   6563  N N   . GLY D 2 16  ? -18.064 -19.493 -18.389 1.00 50.40 ? 16  GLY D N   1 
ATOM   6564  C CA  . GLY D 2 16  ? -19.172 -19.963 -19.219 1.00 50.61 ? 16  GLY D CA  1 
ATOM   6565  C C   . GLY D 2 16  ? -20.576 -19.738 -18.683 1.00 50.89 ? 16  GLY D C   1 
ATOM   6566  O O   . GLY D 2 16  ? -21.554 -20.071 -19.359 1.00 50.93 ? 16  GLY D O   1 
ATOM   6567  N N   . MET D 2 17  ? -20.691 -19.182 -17.477 1.00 51.12 ? 17  MET D N   1 
ATOM   6568  C CA  . MET D 2 17  ? -22.006 -18.876 -16.906 1.00 51.37 ? 17  MET D CA  1 
ATOM   6569  C C   . MET D 2 17  ? -22.324 -17.378 -16.955 1.00 51.43 ? 17  MET D C   1 
ATOM   6570  O O   . MET D 2 17  ? -21.974 -16.619 -16.048 1.00 51.62 ? 17  MET D O   1 
ATOM   6571  C CB  . MET D 2 17  ? -22.141 -19.424 -15.483 1.00 51.35 ? 17  MET D CB  1 
ATOM   6572  C CG  . MET D 2 17  ? -23.569 -19.358 -14.949 1.00 51.86 ? 17  MET D CG  1 
ATOM   6573  S SD  . MET D 2 17  ? -23.752 -19.954 -13.261 1.00 52.78 ? 17  MET D SD  1 
ATOM   6574  C CE  . MET D 2 17  ? -22.804 -18.729 -12.352 1.00 52.36 ? 17  MET D CE  1 
ATOM   6575  N N   . VAL D 2 18  ? -23.001 -16.977 -18.026 1.00 51.45 ? 18  VAL D N   1 
ATOM   6576  C CA  . VAL D 2 18  ? -23.308 -15.576 -18.303 1.00 51.45 ? 18  VAL D CA  1 
ATOM   6577  C C   . VAL D 2 18  ? -24.713 -15.198 -17.831 1.00 51.49 ? 18  VAL D C   1 
ATOM   6578  O O   . VAL D 2 18  ? -25.114 -14.034 -17.885 1.00 51.59 ? 18  VAL D O   1 
ATOM   6579  C CB  . VAL D 2 18  ? -23.180 -15.272 -19.822 1.00 51.53 ? 18  VAL D CB  1 
ATOM   6580  C CG1 . VAL D 2 18  ? -21.735 -15.402 -20.276 1.00 51.49 ? 18  VAL D CG1 1 
ATOM   6581  C CG2 . VAL D 2 18  ? -24.091 -16.191 -20.650 1.00 51.36 ? 18  VAL D CG2 1 
ATOM   6582  N N   . ASP D 2 19  ? -25.447 -16.198 -17.361 1.00 51.44 ? 19  ASP D N   1 
ATOM   6583  C CA  . ASP D 2 19  ? -26.863 -16.064 -17.046 1.00 51.40 ? 19  ASP D CA  1 
ATOM   6584  C C   . ASP D 2 19  ? -27.117 -15.302 -15.737 1.00 50.93 ? 19  ASP D C   1 
ATOM   6585  O O   . ASP D 2 19  ? -28.114 -14.585 -15.618 1.00 50.90 ? 19  ASP D O   1 
ATOM   6586  C CB  . ASP D 2 19  ? -27.491 -17.466 -16.987 1.00 51.81 ? 19  ASP D CB  1 
ATOM   6587  C CG  . ASP D 2 19  ? -28.966 -17.479 -17.371 1.00 52.89 ? 19  ASP D CG  1 
ATOM   6588  O OD1 . ASP D 2 19  ? -29.552 -16.392 -17.587 1.00 54.02 ? 19  ASP D OD1 1 
ATOM   6589  O OD2 . ASP D 2 19  ? -29.539 -18.593 -17.456 1.00 53.86 ? 19  ASP D OD2 1 
ATOM   6590  N N   . GLY D 2 20  ? -26.218 -15.468 -14.764 1.00 50.27 ? 20  GLY D N   1 
ATOM   6591  C CA  . GLY D 2 20  ? -26.358 -14.841 -13.446 1.00 49.40 ? 20  GLY D CA  1 
ATOM   6592  C C   . GLY D 2 20  ? -25.081 -14.864 -12.623 1.00 48.82 ? 20  GLY D C   1 
ATOM   6593  O O   . GLY D 2 20  ? -23.994 -15.078 -13.161 1.00 48.80 ? 20  GLY D O   1 
ATOM   6594  N N   . TRP D 2 21  ? -25.214 -14.643 -11.316 1.00 48.25 ? 21  TRP D N   1 
ATOM   6595  C CA  . TRP D 2 21  ? -24.064 -14.614 -10.403 1.00 47.75 ? 21  TRP D CA  1 
ATOM   6596  C C   . TRP D 2 21  ? -23.694 -15.986 -9.841  1.00 47.79 ? 21  TRP D C   1 
ATOM   6597  O O   . TRP D 2 21  ? -22.513 -16.301 -9.683  1.00 47.58 ? 21  TRP D O   1 
ATOM   6598  C CB  . TRP D 2 21  ? -24.305 -13.640 -9.246  1.00 47.48 ? 21  TRP D CB  1 
ATOM   6599  C CG  . TRP D 2 21  ? -23.878 -12.220 -9.518  1.00 46.70 ? 21  TRP D CG  1 
ATOM   6600  C CD1 . TRP D 2 21  ? -22.831 -11.803 -10.298 1.00 45.69 ? 21  TRP D CD1 1 
ATOM   6601  C CD2 . TRP D 2 21  ? -24.465 -11.030 -8.972  1.00 45.42 ? 21  TRP D CD2 1 
ATOM   6602  N NE1 . TRP D 2 21  ? -22.747 -10.433 -10.285 1.00 44.90 ? 21  TRP D NE1 1 
ATOM   6603  C CE2 . TRP D 2 21  ? -23.736 -9.933  -9.480  1.00 44.52 ? 21  TRP D CE2 1 
ATOM   6604  C CE3 . TRP D 2 21  ? -25.543 -10.787 -8.110  1.00 44.67 ? 21  TRP D CE3 1 
ATOM   6605  C CZ2 . TRP D 2 21  ? -24.046 -8.613  -9.154  1.00 44.37 ? 21  TRP D CZ2 1 
ATOM   6606  C CZ3 . TRP D 2 21  ? -25.852 -9.472  -7.788  1.00 44.71 ? 21  TRP D CZ3 1 
ATOM   6607  C CH2 . TRP D 2 21  ? -25.104 -8.402  -8.308  1.00 44.46 ? 21  TRP D CH2 1 
ATOM   6608  N N   . TYR D 2 22  ? -24.708 -16.787 -9.521  1.00 47.92 ? 22  TYR D N   1 
ATOM   6609  C CA  . TYR D 2 22  ? -24.496 -18.135 -9.001  1.00 48.00 ? 22  TYR D CA  1 
ATOM   6610  C C   . TYR D 2 22  ? -25.352 -19.127 -9.775  1.00 48.41 ? 22  TYR D C   1 
ATOM   6611  O O   . TYR D 2 22  ? -26.426 -18.778 -10.261 1.00 48.41 ? 22  TYR D O   1 
ATOM   6612  C CB  . TYR D 2 22  ? -24.848 -18.220 -7.512  1.00 47.73 ? 22  TYR D CB  1 
ATOM   6613  C CG  . TYR D 2 22  ? -24.754 -16.920 -6.740  1.00 46.96 ? 22  TYR D CG  1 
ATOM   6614  C CD1 . TYR D 2 22  ? -23.519 -16.394 -6.361  1.00 46.09 ? 22  TYR D CD1 1 
ATOM   6615  C CD2 . TYR D 2 22  ? -25.905 -16.227 -6.374  1.00 46.04 ? 22  TYR D CD2 1 
ATOM   6616  C CE1 . TYR D 2 22  ? -23.434 -15.208 -5.648  1.00 45.66 ? 22  TYR D CE1 1 
ATOM   6617  C CE2 . TYR D 2 22  ? -25.832 -15.044 -5.659  1.00 45.72 ? 22  TYR D CE2 1 
ATOM   6618  C CZ  . TYR D 2 22  ? -24.595 -14.538 -5.301  1.00 45.75 ? 22  TYR D CZ  1 
ATOM   6619  O OH  . TYR D 2 22  ? -24.526 -13.362 -4.591  1.00 45.56 ? 22  TYR D OH  1 
ATOM   6620  N N   . GLY D 2 23  ? -24.884 -20.367 -9.883  1.00 48.94 ? 23  GLY D N   1 
ATOM   6621  C CA  . GLY D 2 23  ? -25.677 -21.401 -10.534 1.00 49.63 ? 23  GLY D CA  1 
ATOM   6622  C C   . GLY D 2 23  ? -25.102 -22.800 -10.514 1.00 50.05 ? 23  GLY D C   1 
ATOM   6623  O O   . GLY D 2 23  ? -24.350 -23.168 -9.610  1.00 49.90 ? 23  GLY D O   1 
ATOM   6624  N N   . TYR D 2 24  ? -25.465 -23.572 -11.535 1.00 50.70 ? 24  TYR D N   1 
ATOM   6625  C CA  . TYR D 2 24  ? -25.138 -24.989 -11.606 1.00 51.29 ? 24  TYR D CA  1 
ATOM   6626  C C   . TYR D 2 24  ? -24.514 -25.375 -12.937 1.00 52.19 ? 24  TYR D C   1 
ATOM   6627  O O   . TYR D 2 24  ? -24.770 -24.741 -13.964 1.00 52.22 ? 24  TYR D O   1 
ATOM   6628  C CB  . TYR D 2 24  ? -26.400 -25.828 -11.434 1.00 50.88 ? 24  TYR D CB  1 
ATOM   6629  C CG  . TYR D 2 24  ? -27.306 -25.435 -10.292 1.00 49.85 ? 24  TYR D CG  1 
ATOM   6630  C CD1 . TYR D 2 24  ? -27.151 -26.001 -9.029  1.00 48.43 ? 24  TYR D CD1 1 
ATOM   6631  C CD2 . TYR D 2 24  ? -28.347 -24.525 -10.485 1.00 48.91 ? 24  TYR D CD2 1 
ATOM   6632  C CE1 . TYR D 2 24  ? -27.995 -25.660 -7.981  1.00 47.67 ? 24  TYR D CE1 1 
ATOM   6633  C CE2 . TYR D 2 24  ? -29.196 -24.176 -9.440  1.00 48.18 ? 24  TYR D CE2 1 
ATOM   6634  C CZ  . TYR D 2 24  ? -29.013 -24.750 -8.191  1.00 47.54 ? 24  TYR D CZ  1 
ATOM   6635  O OH  . TYR D 2 24  ? -29.850 -24.414 -7.154  1.00 47.24 ? 24  TYR D OH  1 
ATOM   6636  N N   . HIS D 2 25  ? -23.692 -26.421 -12.906 1.00 53.46 ? 25  HIS D N   1 
ATOM   6637  C CA  . HIS D 2 25  ? -23.302 -27.148 -14.113 1.00 54.72 ? 25  HIS D CA  1 
ATOM   6638  C C   . HIS D 2 25  ? -23.663 -28.618 -13.921 1.00 55.44 ? 25  HIS D C   1 
ATOM   6639  O O   . HIS D 2 25  ? -23.240 -29.248 -12.946 1.00 55.42 ? 25  HIS D O   1 
ATOM   6640  C CB  . HIS D 2 25  ? -21.810 -26.989 -14.423 1.00 54.71 ? 25  HIS D CB  1 
ATOM   6641  C CG  . HIS D 2 25  ? -21.400 -27.590 -15.736 1.00 55.55 ? 25  HIS D CG  1 
ATOM   6642  N ND1 . HIS D 2 25  ? -20.636 -28.736 -15.826 1.00 55.66 ? 25  HIS D ND1 1 
ATOM   6643  C CD2 . HIS D 2 25  ? -21.657 -27.209 -17.011 1.00 55.99 ? 25  HIS D CD2 1 
ATOM   6644  C CE1 . HIS D 2 25  ? -20.435 -29.031 -17.098 1.00 55.78 ? 25  HIS D CE1 1 
ATOM   6645  N NE2 . HIS D 2 25  ? -21.045 -28.121 -17.838 1.00 56.06 ? 25  HIS D NE2 1 
ATOM   6646  N N   . HIS D 2 26  ? -24.458 -29.148 -14.849 1.00 56.42 ? 26  HIS D N   1 
ATOM   6647  C CA  . HIS D 2 26  ? -24.966 -30.513 -14.753 1.00 57.39 ? 26  HIS D CA  1 
ATOM   6648  C C   . HIS D 2 26  ? -24.621 -31.316 -16.001 1.00 58.03 ? 26  HIS D C   1 
ATOM   6649  O O   . HIS D 2 26  ? -24.812 -30.838 -17.123 1.00 58.13 ? 26  HIS D O   1 
ATOM   6650  C CB  . HIS D 2 26  ? -26.486 -30.497 -14.545 1.00 57.45 ? 26  HIS D CB  1 
ATOM   6651  C CG  . HIS D 2 26  ? -27.267 -30.253 -15.801 1.00 58.01 ? 26  HIS D CG  1 
ATOM   6652  N ND1 . HIS D 2 26  ? -27.241 -29.050 -16.472 1.00 58.65 ? 26  HIS D ND1 1 
ATOM   6653  C CD2 . HIS D 2 26  ? -28.082 -31.065 -16.515 1.00 58.53 ? 26  HIS D CD2 1 
ATOM   6654  C CE1 . HIS D 2 26  ? -28.012 -29.128 -17.543 1.00 58.80 ? 26  HIS D CE1 1 
ATOM   6655  N NE2 . HIS D 2 26  ? -28.535 -30.340 -17.591 1.00 58.70 ? 26  HIS D NE2 1 
ATOM   6656  N N   . SER D 2 27  ? -24.134 -32.538 -15.804 1.00 58.82 ? 27  SER D N   1 
ATOM   6657  C CA  . SER D 2 27  ? -23.780 -33.409 -16.920 1.00 59.43 ? 27  SER D CA  1 
ATOM   6658  C C   . SER D 2 27  ? -24.345 -34.817 -16.746 1.00 59.85 ? 27  SER D C   1 
ATOM   6659  O O   . SER D 2 27  ? -23.754 -35.653 -16.063 1.00 60.05 ? 27  SER D O   1 
ATOM   6660  C CB  . SER D 2 27  ? -22.260 -33.470 -17.088 1.00 59.46 ? 27  SER D CB  1 
ATOM   6661  O OG  . SER D 2 27  ? -21.661 -34.225 -16.049 1.00 59.62 ? 27  SER D OG  1 
ATOM   6662  N N   . ASN D 2 28  ? -25.489 -35.073 -17.372 1.00 60.29 ? 28  ASN D N   1 
ATOM   6663  C CA  . ASN D 2 28  ? -26.117 -36.390 -17.328 1.00 60.72 ? 28  ASN D CA  1 
ATOM   6664  C C   . ASN D 2 28  ? -26.066 -37.071 -18.691 1.00 61.24 ? 28  ASN D C   1 
ATOM   6665  O O   . ASN D 2 28  ? -25.263 -36.696 -19.546 1.00 61.24 ? 28  ASN D O   1 
ATOM   6666  C CB  . ASN D 2 28  ? -27.565 -36.280 -16.846 1.00 60.60 ? 28  ASN D CB  1 
ATOM   6667  C CG  . ASN D 2 28  ? -28.409 -35.391 -17.738 1.00 60.46 ? 28  ASN D CG  1 
ATOM   6668  O OD1 . ASN D 2 28  ? -29.581 -35.143 -17.456 1.00 60.05 ? 28  ASN D OD1 1 
ATOM   6669  N ND2 . ASN D 2 28  ? -27.816 -34.906 -18.823 1.00 60.81 ? 28  ASN D ND2 1 
ATOM   6670  N N   . GLU D 2 29  ? -26.920 -38.069 -18.896 1.00 61.72 ? 29  GLU D N   1 
ATOM   6671  C CA  . GLU D 2 29  ? -26.959 -38.765 -20.178 1.00 62.12 ? 29  GLU D CA  1 
ATOM   6672  C C   . GLU D 2 29  ? -27.222 -37.832 -21.360 1.00 62.13 ? 29  GLU D C   1 
ATOM   6673  O O   . GLU D 2 29  ? -26.690 -38.030 -22.457 1.00 62.21 ? 29  GLU D O   1 
ATOM   6674  C CB  . GLU D 2 29  ? -28.016 -39.881 -20.110 1.00 62.30 ? 29  GLU D CB  1 
ATOM   6675  C CG  . GLU D 2 29  ? -28.129 -40.769 -21.355 1.00 63.01 ? 29  GLU D CG  1 
ATOM   6676  C CD  . GLU D 2 29  ? -26.906 -41.643 -21.588 1.00 64.07 ? 29  GLU D CD  1 
ATOM   6677  O OE1 . GLU D 2 29  ? -26.531 -42.413 -20.675 1.00 64.58 ? 29  GLU D OE1 1 
ATOM   6678  O OE2 . GLU D 2 29  ? -26.326 -41.567 -22.695 1.00 64.39 ? 29  GLU D OE2 1 
ATOM   6679  N N   . GLN D 2 30  ? -28.026 -36.801 -21.113 1.00 62.00 ? 30  GLN D N   1 
ATOM   6680  C CA  . GLN D 2 30  ? -28.531 -35.922 -22.166 1.00 61.86 ? 30  GLN D CA  1 
ATOM   6681  C C   . GLN D 2 30  ? -27.653 -34.680 -22.388 1.00 61.71 ? 30  GLN D C   1 
ATOM   6682  O O   . GLN D 2 30  ? -28.134 -33.647 -22.866 1.00 61.60 ? 30  GLN D O   1 
ATOM   6683  C CB  . GLN D 2 30  ? -29.983 -35.534 -21.855 1.00 61.85 ? 30  GLN D CB  1 
ATOM   6684  C CG  . GLN D 2 30  ? -30.896 -36.737 -21.634 1.00 61.76 ? 30  GLN D CG  1 
ATOM   6685  C CD  . GLN D 2 30  ? -31.870 -36.534 -20.489 1.00 62.10 ? 30  GLN D CD  1 
ATOM   6686  O OE1 . GLN D 2 30  ? -31.605 -36.945 -19.357 1.00 62.01 ? 30  GLN D OE1 1 
ATOM   6687  N NE2 . GLN D 2 30  ? -33.000 -35.892 -20.773 1.00 61.75 ? 30  GLN D NE2 1 
ATOM   6688  N N   . GLY D 2 31  ? -26.368 -34.797 -22.048 1.00 61.55 ? 31  GLY D N   1 
ATOM   6689  C CA  . GLY D 2 31  ? -25.397 -33.709 -22.225 1.00 61.15 ? 31  GLY D CA  1 
ATOM   6690  C C   . GLY D 2 31  ? -25.246 -32.774 -21.031 1.00 60.79 ? 31  GLY D C   1 
ATOM   6691  O O   . GLY D 2 31  ? -26.099 -32.748 -20.133 1.00 60.55 ? 31  GLY D O   1 
ATOM   6692  N N   . SER D 2 32  ? -24.157 -32.002 -21.033 1.00 60.39 ? 32  SER D N   1 
ATOM   6693  C CA  . SER D 2 32  ? -23.862 -31.042 -19.962 1.00 60.05 ? 32  SER D CA  1 
ATOM   6694  C C   . SER D 2 32  ? -24.583 -29.701 -20.171 1.00 59.73 ? 32  SER D C   1 
ATOM   6695  O O   . SER D 2 32  ? -25.480 -29.598 -21.017 1.00 59.69 ? 32  SER D O   1 
ATOM   6696  C CB  . SER D 2 32  ? -22.346 -30.840 -19.810 1.00 60.06 ? 32  SER D CB  1 
ATOM   6697  O OG  . SER D 2 32  ? -21.795 -30.144 -20.916 1.00 60.28 ? 32  SER D OG  1 
ATOM   6698  N N   . GLY D 2 33  ? -24.199 -28.687 -19.393 1.00 59.18 ? 33  GLY D N   1 
ATOM   6699  C CA  . GLY D 2 33  ? -24.759 -27.342 -19.546 1.00 58.44 ? 33  GLY D CA  1 
ATOM   6700  C C   . GLY D 2 33  ? -24.777 -26.496 -18.285 1.00 57.85 ? 33  GLY D C   1 
ATOM   6701  O O   . GLY D 2 33  ? -25.127 -26.981 -17.205 1.00 57.94 ? 33  GLY D O   1 
ATOM   6702  N N   . TYR D 2 34  ? -24.391 -25.227 -18.431 1.00 57.12 ? 34  TYR D N   1 
ATOM   6703  C CA  . TYR D 2 34  ? -24.478 -24.239 -17.357 1.00 56.17 ? 34  TYR D CA  1 
ATOM   6704  C C   . TYR D 2 34  ? -25.906 -23.717 -17.226 1.00 55.85 ? 34  TYR D C   1 
ATOM   6705  O O   . TYR D 2 34  ? -26.630 -23.604 -18.220 1.00 55.78 ? 34  TYR D O   1 
ATOM   6706  C CB  . TYR D 2 34  ? -23.552 -23.050 -17.632 1.00 56.04 ? 34  TYR D CB  1 
ATOM   6707  C CG  . TYR D 2 34  ? -22.066 -23.342 -17.585 1.00 55.29 ? 34  TYR D CG  1 
ATOM   6708  C CD1 . TYR D 2 34  ? -21.394 -23.460 -16.369 1.00 54.31 ? 34  TYR D CD1 1 
ATOM   6709  C CD2 . TYR D 2 34  ? -21.325 -23.467 -18.763 1.00 54.80 ? 34  TYR D CD2 1 
ATOM   6710  C CE1 . TYR D 2 34  ? -20.025 -23.714 -16.327 1.00 53.91 ? 34  TYR D CE1 1 
ATOM   6711  C CE2 . TYR D 2 34  ? -19.956 -23.722 -18.732 1.00 54.05 ? 34  TYR D CE2 1 
ATOM   6712  C CZ  . TYR D 2 34  ? -19.314 -23.844 -17.511 1.00 53.97 ? 34  TYR D CZ  1 
ATOM   6713  O OH  . TYR D 2 34  ? -17.960 -24.095 -17.477 1.00 53.60 ? 34  TYR D OH  1 
ATOM   6714  N N   . ALA D 2 35  ? -26.303 -23.396 -15.997 1.00 55.31 ? 35  ALA D N   1 
ATOM   6715  C CA  . ALA D 2 35  ? -27.584 -22.736 -15.734 1.00 54.78 ? 35  ALA D CA  1 
ATOM   6716  C C   . ALA D 2 35  ? -27.494 -21.938 -14.441 1.00 54.47 ? 35  ALA D C   1 
ATOM   6717  O O   . ALA D 2 35  ? -26.873 -22.379 -13.474 1.00 54.47 ? 35  ALA D O   1 
ATOM   6718  C CB  . ALA D 2 35  ? -28.719 -23.750 -15.661 1.00 54.69 ? 35  ALA D CB  1 
ATOM   6719  N N   . ALA D 2 36  ? -28.111 -20.761 -14.435 1.00 53.97 ? 36  ALA D N   1 
ATOM   6720  C CA  . ALA D 2 36  ? -28.096 -19.893 -13.268 1.00 53.48 ? 36  ALA D CA  1 
ATOM   6721  C C   . ALA D 2 36  ? -29.209 -20.269 -12.306 1.00 53.14 ? 36  ALA D C   1 
ATOM   6722  O O   . ALA D 2 36  ? -30.273 -20.723 -12.725 1.00 53.23 ? 36  ALA D O   1 
ATOM   6723  C CB  . ALA D 2 36  ? -28.242 -18.441 -13.690 1.00 53.53 ? 36  ALA D CB  1 
ATOM   6724  N N   . ASP D 2 37  ? -28.960 -20.086 -11.015 1.00 52.64 ? 37  ASP D N   1 
ATOM   6725  C CA  . ASP D 2 37  ? -30.025 -20.188 -10.036 1.00 52.25 ? 37  ASP D CA  1 
ATOM   6726  C C   . ASP D 2 37  ? -30.703 -18.830 -9.933  1.00 52.06 ? 37  ASP D C   1 
ATOM   6727  O O   . ASP D 2 37  ? -30.075 -17.849 -9.543  1.00 52.00 ? 37  ASP D O   1 
ATOM   6728  C CB  . ASP D 2 37  ? -29.491 -20.617 -8.671  1.00 52.13 ? 37  ASP D CB  1 
ATOM   6729  C CG  . ASP D 2 37  ? -30.594 -20.797 -7.657  1.00 51.79 ? 37  ASP D CG  1 
ATOM   6730  O OD1 . ASP D 2 37  ? -31.456 -21.675 -7.866  1.00 52.04 ? 37  ASP D OD1 1 
ATOM   6731  O OD2 . ASP D 2 37  ? -30.613 -20.053 -6.661  1.00 51.39 ? 37  ASP D OD2 1 
ATOM   6732  N N   . LYS D 2 38  ? -31.984 -18.780 -10.288 1.00 51.92 ? 38  LYS D N   1 
ATOM   6733  C CA  . LYS D 2 38  ? -32.713 -17.514 -10.354 1.00 51.76 ? 38  LYS D CA  1 
ATOM   6734  C C   . LYS D 2 38  ? -33.157 -16.986 -8.993  1.00 51.34 ? 38  LYS D C   1 
ATOM   6735  O O   . LYS D 2 38  ? -33.177 -15.774 -8.782  1.00 51.29 ? 38  LYS D O   1 
ATOM   6736  C CB  . LYS D 2 38  ? -33.910 -17.618 -11.310 1.00 51.91 ? 38  LYS D CB  1 
ATOM   6737  C CG  . LYS D 2 38  ? -33.568 -17.385 -12.784 1.00 52.77 ? 38  LYS D CG  1 
ATOM   6738  C CD  . LYS D 2 38  ? -33.390 -15.895 -13.098 1.00 54.44 ? 38  LYS D CD  1 
ATOM   6739  C CE  . LYS D 2 38  ? -33.554 -15.603 -14.587 1.00 54.77 ? 38  LYS D CE  1 
ATOM   6740  N NZ  . LYS D 2 38  ? -32.430 -16.145 -15.403 1.00 55.29 ? 38  LYS D NZ  1 
ATOM   6741  N N   . GLU D 2 39  ? -33.516 -17.889 -8.083  1.00 50.87 ? 39  GLU D N   1 
ATOM   6742  C CA  . GLU D 2 39  ? -33.964 -17.498 -6.743  1.00 50.57 ? 39  GLU D CA  1 
ATOM   6743  C C   . GLU D 2 39  ? -32.868 -16.749 -5.962  1.00 49.85 ? 39  GLU D C   1 
ATOM   6744  O O   . GLU D 2 39  ? -33.134 -15.705 -5.360  1.00 49.83 ? 39  GLU D O   1 
ATOM   6745  C CB  . GLU D 2 39  ? -34.478 -18.713 -5.953  1.00 50.80 ? 39  GLU D CB  1 
ATOM   6746  C CG  . GLU D 2 39  ? -35.274 -18.346 -4.693  1.00 52.42 ? 39  GLU D CG  1 
ATOM   6747  C CD  . GLU D 2 39  ? -35.775 -19.563 -3.912  1.00 54.32 ? 39  GLU D CD  1 
ATOM   6748  O OE1 . GLU D 2 39  ? -36.703 -20.251 -4.398  1.00 54.88 ? 39  GLU D OE1 1 
ATOM   6749  O OE2 . GLU D 2 39  ? -35.252 -19.817 -2.802  1.00 54.44 ? 39  GLU D OE2 1 
ATOM   6750  N N   . SER D 2 40  ? -31.643 -17.266 -6.000  1.00 48.84 ? 40  SER D N   1 
ATOM   6751  C CA  . SER D 2 40  ? -30.539 -16.667 -5.254  1.00 47.98 ? 40  SER D CA  1 
ATOM   6752  C C   . SER D 2 40  ? -29.897 -15.473 -5.961  1.00 47.31 ? 40  SER D C   1 
ATOM   6753  O O   . SER D 2 40  ? -29.389 -14.565 -5.299  1.00 47.20 ? 40  SER D O   1 
ATOM   6754  C CB  . SER D 2 40  ? -29.479 -17.717 -4.906  1.00 47.98 ? 40  SER D CB  1 
ATOM   6755  O OG  . SER D 2 40  ? -28.843 -18.200 -6.072  1.00 48.00 ? 40  SER D OG  1 
ATOM   6756  N N   . THR D 2 41  ? -29.916 -15.476 -7.294  1.00 46.43 ? 41  THR D N   1 
ATOM   6757  C CA  . THR D 2 41  ? -29.383 -14.357 -8.078  1.00 45.56 ? 41  THR D CA  1 
ATOM   6758  C C   . THR D 2 41  ? -30.246 -13.102 -7.919  1.00 44.97 ? 41  THR D C   1 
ATOM   6759  O O   . THR D 2 41  ? -29.720 -12.004 -7.704  1.00 44.81 ? 41  THR D O   1 
ATOM   6760  C CB  . THR D 2 41  ? -29.220 -14.729 -9.567  1.00 45.48 ? 41  THR D CB  1 
ATOM   6761  O OG1 . THR D 2 41  ? -28.296 -15.817 -9.676  1.00 45.89 ? 41  THR D OG1 1 
ATOM   6762  C CG2 . THR D 2 41  ? -28.683 -13.550 -10.381 1.00 45.49 ? 41  THR D CG2 1 
ATOM   6763  N N   . GLN D 2 42  ? -31.563 -13.279 -8.006  1.00 44.18 ? 42  GLN D N   1 
ATOM   6764  C CA  . GLN D 2 42  ? -32.516 -12.189 -7.811  1.00 43.43 ? 42  GLN D CA  1 
ATOM   6765  C C   . GLN D 2 42  ? -32.440 -11.616 -6.399  1.00 42.78 ? 42  GLN D C   1 
ATOM   6766  O O   . GLN D 2 42  ? -32.542 -10.407 -6.214  1.00 42.73 ? 42  GLN D O   1 
ATOM   6767  C CB  . GLN D 2 42  ? -33.945 -12.658 -8.117  1.00 43.41 ? 42  GLN D CB  1 
ATOM   6768  C CG  . GLN D 2 42  ? -34.982 -11.534 -8.183  1.00 43.72 ? 42  GLN D CG  1 
ATOM   6769  C CD  . GLN D 2 42  ? -34.612 -10.430 -9.172  1.00 44.07 ? 42  GLN D CD  1 
ATOM   6770  O OE1 . GLN D 2 42  ? -34.127 -10.695 -10.277 1.00 43.94 ? 42  GLN D OE1 1 
ATOM   6771  N NE2 . GLN D 2 42  ? -34.845 -9.185  -8.776  1.00 43.98 ? 42  GLN D NE2 1 
ATOM   6772  N N   . LYS D 2 43  ? -32.266 -12.497 -5.417  1.00 42.13 ? 43  LYS D N   1 
ATOM   6773  C CA  . LYS D 2 43  ? -32.119 -12.109 -4.016  1.00 41.54 ? 43  LYS D CA  1 
ATOM   6774  C C   . LYS D 2 43  ? -30.886 -11.219 -3.825  1.00 40.80 ? 43  LYS D C   1 
ATOM   6775  O O   . LYS D 2 43  ? -30.933 -10.221 -3.107  1.00 40.52 ? 43  LYS D O   1 
ATOM   6776  C CB  . LYS D 2 43  ? -32.007 -13.362 -3.142  1.00 41.74 ? 43  LYS D CB  1 
ATOM   6777  C CG  . LYS D 2 43  ? -32.624 -13.243 -1.747  1.00 42.87 ? 43  LYS D CG  1 
ATOM   6778  C CD  . LYS D 2 43  ? -34.169 -13.245 -1.772  1.00 44.17 ? 43  LYS D CD  1 
ATOM   6779  C CE  . LYS D 2 43  ? -34.761 -14.582 -2.246  1.00 44.31 ? 43  LYS D CE  1 
ATOM   6780  N NZ  . LYS D 2 43  ? -34.493 -15.711 -1.305  1.00 44.18 ? 43  LYS D NZ  1 
ATOM   6781  N N   . ALA D 2 44  ? -29.793 -11.592 -4.489  1.00 40.02 ? 44  ALA D N   1 
ATOM   6782  C CA  . ALA D 2 44  ? -28.548 -10.837 -4.454  1.00 39.31 ? 44  ALA D CA  1 
ATOM   6783  C C   . ALA D 2 44  ? -28.668 -9.505  -5.195  1.00 38.85 ? 44  ALA D C   1 
ATOM   6784  O O   . ALA D 2 44  ? -28.206 -8.479  -4.698  1.00 38.71 ? 44  ALA D O   1 
ATOM   6785  C CB  . ALA D 2 44  ? -27.397 -11.671 -5.012  1.00 39.21 ? 44  ALA D CB  1 
ATOM   6786  N N   . ILE D 2 45  ? -29.291 -9.521  -6.373  1.00 38.33 ? 45  ILE D N   1 
ATOM   6787  C CA  . ILE D 2 45  ? -29.537 -8.287  -7.117  1.00 37.95 ? 45  ILE D CA  1 
ATOM   6788  C C   . ILE D 2 45  ? -30.361 -7.327  -6.253  1.00 37.77 ? 45  ILE D C   1 
ATOM   6789  O O   . ILE D 2 45  ? -29.977 -6.170  -6.063  1.00 37.69 ? 45  ILE D O   1 
ATOM   6790  C CB  . ILE D 2 45  ? -30.203 -8.548  -8.500  1.00 37.89 ? 45  ILE D CB  1 
ATOM   6791  C CG1 . ILE D 2 45  ? -29.190 -9.169  -9.465  1.00 37.74 ? 45  ILE D CG1 1 
ATOM   6792  C CG2 . ILE D 2 45  ? -30.770 -7.252  -9.101  1.00 37.50 ? 45  ILE D CG2 1 
ATOM   6793  C CD1 . ILE D 2 45  ? -29.816 -9.782  -10.712 1.00 37.30 ? 45  ILE D CD1 1 
ATOM   6794  N N   . ASP D 2 46  ? -31.466 -7.825  -5.703  1.00 37.51 ? 46  ASP D N   1 
ATOM   6795  C CA  . ASP D 2 46  ? -32.322 -7.029  -4.823  1.00 37.52 ? 46  ASP D CA  1 
ATOM   6796  C C   . ASP D 2 46  ? -31.573 -6.444  -3.624  1.00 37.11 ? 46  ASP D C   1 
ATOM   6797  O O   . ASP D 2 46  ? -31.733 -5.261  -3.313  1.00 37.28 ? 46  ASP D O   1 
ATOM   6798  C CB  . ASP D 2 46  ? -33.546 -7.837  -4.382  1.00 37.65 ? 46  ASP D CB  1 
ATOM   6799  C CG  . ASP D 2 46  ? -34.498 -8.124  -5.542  1.00 39.11 ? 46  ASP D CG  1 
ATOM   6800  O OD1 . ASP D 2 46  ? -35.555 -8.753  -5.319  1.00 40.15 ? 46  ASP D OD1 1 
ATOM   6801  O OD2 . ASP D 2 46  ? -34.187 -7.715  -6.687  1.00 40.62 ? 46  ASP D OD2 1 
ATOM   6802  N N   . GLY D 2 47  ? -30.745 -7.267  -2.977  1.00 36.55 ? 47  GLY D N   1 
ATOM   6803  C CA  . GLY D 2 47  ? -29.939 -6.833  -1.838  1.00 35.65 ? 47  GLY D CA  1 
ATOM   6804  C C   . GLY D 2 47  ? -28.944 -5.746  -2.205  1.00 35.19 ? 47  GLY D C   1 
ATOM   6805  O O   . GLY D 2 47  ? -28.893 -4.692  -1.564  1.00 34.83 ? 47  GLY D O   1 
ATOM   6806  N N   . VAL D 2 48  ? -28.157 -6.009  -3.244  1.00 34.75 ? 48  VAL D N   1 
ATOM   6807  C CA  . VAL D 2 48  ? -27.157 -5.060  -3.732  1.00 34.56 ? 48  VAL D CA  1 
ATOM   6808  C C   . VAL D 2 48  ? -27.794 -3.732  -4.175  1.00 34.54 ? 48  VAL D C   1 
ATOM   6809  O O   . VAL D 2 48  ? -27.305 -2.658  -3.814  1.00 34.59 ? 48  VAL D O   1 
ATOM   6810  C CB  . VAL D 2 48  ? -26.283 -5.684  -4.851  1.00 34.40 ? 48  VAL D CB  1 
ATOM   6811  C CG1 . VAL D 2 48  ? -25.408 -4.634  -5.529  1.00 34.15 ? 48  VAL D CG1 1 
ATOM   6812  C CG2 . VAL D 2 48  ? -25.420 -6.797  -4.277  1.00 34.20 ? 48  VAL D CG2 1 
ATOM   6813  N N   . THR D 2 49  ? -28.892 -3.813  -4.926  1.00 34.42 ? 49  THR D N   1 
ATOM   6814  C CA  . THR D 2 49  ? -29.632 -2.623  -5.360  1.00 34.27 ? 49  THR D CA  1 
ATOM   6815  C C   . THR D 2 49  ? -30.053 -1.772  -4.162  1.00 34.34 ? 49  THR D C   1 
ATOM   6816  O O   . THR D 2 49  ? -29.746 -0.581  -4.113  1.00 34.38 ? 49  THR D O   1 
ATOM   6817  C CB  . THR D 2 49  ? -30.864 -2.992  -6.227  1.00 34.19 ? 49  THR D CB  1 
ATOM   6818  O OG1 . THR D 2 49  ? -30.447 -3.843  -7.299  1.00 33.93 ? 49  THR D OG1 1 
ATOM   6819  C CG2 . THR D 2 49  ? -31.524 -1.747  -6.811  1.00 33.58 ? 49  THR D CG2 1 
ATOM   6820  N N   . ASN D 2 50  ? -30.732 -2.396  -3.198  1.00 34.58 ? 50  ASN D N   1 
ATOM   6821  C CA  . ASN D 2 50  ? -31.170 -1.717  -1.971  1.00 34.76 ? 50  ASN D CA  1 
ATOM   6822  C C   . ASN D 2 50  ? -30.030 -1.058  -1.196  1.00 34.63 ? 50  ASN D C   1 
ATOM   6823  O O   . ASN D 2 50  ? -30.199 0.034   -0.659  1.00 34.73 ? 50  ASN D O   1 
ATOM   6824  C CB  . ASN D 2 50  ? -31.927 -2.680  -1.049  1.00 34.84 ? 50  ASN D CB  1 
ATOM   6825  C CG  . ASN D 2 50  ? -33.267 -3.128  -1.624  1.00 35.62 ? 50  ASN D CG  1 
ATOM   6826  O OD1 . ASN D 2 50  ? -33.850 -2.464  -2.486  1.00 37.06 ? 50  ASN D OD1 1 
ATOM   6827  N ND2 . ASN D 2 50  ? -33.763 -4.262  -1.140  1.00 35.46 ? 50  ASN D ND2 1 
ATOM   6828  N N   . LYS D 2 51  ? -28.877 -1.723  -1.147  1.00 34.50 ? 51  LYS D N   1 
ATOM   6829  C CA  . LYS D 2 51  ? -27.695 -1.188  -0.468  1.00 34.59 ? 51  LYS D CA  1 
ATOM   6830  C C   . LYS D 2 51  ? -27.219 0.113   -1.114  1.00 34.66 ? 51  LYS D C   1 
ATOM   6831  O O   . LYS D 2 51  ? -26.956 1.101   -0.417  1.00 34.57 ? 51  LYS D O   1 
ATOM   6832  C CB  . LYS D 2 51  ? -26.561 -2.218  -0.454  1.00 34.35 ? 51  LYS D CB  1 
ATOM   6833  C CG  . LYS D 2 51  ? -25.228 -1.670  0.052   1.00 34.58 ? 51  LYS D CG  1 
ATOM   6834  C CD  . LYS D 2 51  ? -24.110 -2.705  -0.003  1.00 35.39 ? 51  LYS D CD  1 
ATOM   6835  C CE  . LYS D 2 51  ? -24.305 -3.814  1.016   1.00 34.76 ? 51  LYS D CE  1 
ATOM   6836  N NZ  . LYS D 2 51  ? -23.062 -4.609  1.183   1.00 35.54 ? 51  LYS D NZ  1 
ATOM   6837  N N   . VAL D 2 52  ? -27.114 0.094   -2.443  1.00 34.66 ? 52  VAL D N   1 
ATOM   6838  C CA  . VAL D 2 52  ? -26.663 1.238   -3.218  1.00 34.75 ? 52  VAL D CA  1 
ATOM   6839  C C   . VAL D 2 52  ? -27.607 2.422   -3.019  1.00 35.12 ? 52  VAL D C   1 
ATOM   6840  O O   . VAL D 2 52  ? -27.155 3.543   -2.731  1.00 34.87 ? 52  VAL D O   1 
ATOM   6841  C CB  . VAL D 2 52  ? -26.521 0.887   -4.727  1.00 34.81 ? 52  VAL D CB  1 
ATOM   6842  C CG1 . VAL D 2 52  ? -26.282 2.145   -5.569  1.00 34.19 ? 52  VAL D CG1 1 
ATOM   6843  C CG2 . VAL D 2 52  ? -25.393 -0.124  -4.940  1.00 34.23 ? 52  VAL D CG2 1 
ATOM   6844  N N   . ASN D 2 53  ? -28.909 2.168   -3.151  1.00 35.43 ? 53  ASN D N   1 
ATOM   6845  C CA  . ASN D 2 53  ? -29.920 3.208   -2.932  1.00 36.03 ? 53  ASN D CA  1 
ATOM   6846  C C   . ASN D 2 53  ? -29.905 3.746   -1.504  1.00 36.33 ? 53  ASN D C   1 
ATOM   6847  O O   . ASN D 2 53  ? -30.135 4.934   -1.291  1.00 36.64 ? 53  ASN D O   1 
ATOM   6848  C CB  . ASN D 2 53  ? -31.326 2.720   -3.302  1.00 35.84 ? 53  ASN D CB  1 
ATOM   6849  C CG  . ASN D 2 53  ? -31.505 2.524   -4.797  1.00 36.43 ? 53  ASN D CG  1 
ATOM   6850  O OD1 . ASN D 2 53  ? -30.944 3.263   -5.608  1.00 37.00 ? 53  ASN D OD1 1 
ATOM   6851  N ND2 . ASN D 2 53  ? -32.299 1.525   -5.170  1.00 36.38 ? 53  ASN D ND2 1 
ATOM   6852  N N   . SER D 2 54  ? -29.625 2.871   -0.540  1.00 36.59 ? 54  SER D N   1 
ATOM   6853  C CA  . SER D 2 54  ? -29.559 3.260   0.866   1.00 37.10 ? 54  SER D CA  1 
ATOM   6854  C C   . SER D 2 54  ? -28.399 4.198   1.146   1.00 37.54 ? 54  SER D C   1 
ATOM   6855  O O   . SER D 2 54  ? -28.554 5.157   1.894   1.00 37.56 ? 54  SER D O   1 
ATOM   6856  C CB  . SER D 2 54  ? -29.479 2.033   1.774   1.00 37.02 ? 54  SER D CB  1 
ATOM   6857  O OG  . SER D 2 54  ? -30.730 1.375   1.823   1.00 36.71 ? 54  SER D OG  1 
ATOM   6858  N N   . ILE D 2 55  ? -27.248 3.919   0.540   1.00 38.34 ? 55  ILE D N   1 
ATOM   6859  C CA  . ILE D 2 55  ? -26.067 4.775   0.665   1.00 39.15 ? 55  ILE D CA  1 
ATOM   6860  C C   . ILE D 2 55  ? -26.316 6.160   0.051   1.00 39.98 ? 55  ILE D C   1 
ATOM   6861  O O   . ILE D 2 55  ? -26.057 7.181   0.689   1.00 40.12 ? 55  ILE D O   1 
ATOM   6862  C CB  . ILE D 2 55  ? -24.810 4.102   0.061   1.00 39.02 ? 55  ILE D CB  1 
ATOM   6863  C CG1 . ILE D 2 55  ? -24.402 2.890   0.914   1.00 38.78 ? 55  ILE D CG1 1 
ATOM   6864  C CG2 . ILE D 2 55  ? -23.656 5.098   -0.060  1.00 38.92 ? 55  ILE D CG2 1 
ATOM   6865  C CD1 . ILE D 2 55  ? -23.413 1.938   0.247   1.00 37.80 ? 55  ILE D CD1 1 
ATOM   6866  N N   . ILE D 2 56  ? -26.838 6.188   -1.173  1.00 41.01 ? 56  ILE D N   1 
ATOM   6867  C CA  . ILE D 2 56  ? -27.190 7.442   -1.845  1.00 42.00 ? 56  ILE D CA  1 
ATOM   6868  C C   . ILE D 2 56  ? -28.225 8.252   -1.046  1.00 42.76 ? 56  ILE D C   1 
ATOM   6869  O O   . ILE D 2 56  ? -28.083 9.469   -0.904  1.00 42.72 ? 56  ILE D O   1 
ATOM   6870  C CB  . ILE D 2 56  ? -27.671 7.192   -3.301  1.00 41.96 ? 56  ILE D CB  1 
ATOM   6871  C CG1 . ILE D 2 56  ? -26.509 6.673   -4.159  1.00 41.90 ? 56  ILE D CG1 1 
ATOM   6872  C CG2 . ILE D 2 56  ? -28.280 8.463   -3.911  1.00 41.82 ? 56  ILE D CG2 1 
ATOM   6873  C CD1 . ILE D 2 56  ? -26.938 6.051   -5.486  1.00 41.89 ? 56  ILE D CD1 1 
ATOM   6874  N N   . ASP D 2 57  ? -29.240 7.570   -0.515  1.00 43.83 ? 57  ASP D N   1 
ATOM   6875  C CA  . ASP D 2 57  ? -30.286 8.216   0.286   1.00 45.08 ? 57  ASP D CA  1 
ATOM   6876  C C   . ASP D 2 57  ? -29.773 8.830   1.587   1.00 45.48 ? 57  ASP D C   1 
ATOM   6877  O O   . ASP D 2 57  ? -30.221 9.901   1.977   1.00 45.57 ? 57  ASP D O   1 
ATOM   6878  C CB  . ASP D 2 57  ? -31.435 7.245   0.592   1.00 45.41 ? 57  ASP D CB  1 
ATOM   6879  C CG  . ASP D 2 57  ? -32.296 6.932   -0.633  1.00 46.92 ? 57  ASP D CG  1 
ATOM   6880  O OD1 . ASP D 2 57  ? -33.407 6.382   -0.443  1.00 48.65 ? 57  ASP D OD1 1 
ATOM   6881  O OD2 . ASP D 2 57  ? -31.871 7.221   -1.778  1.00 48.19 ? 57  ASP D OD2 1 
ATOM   6882  N N   . LYS D 2 58  ? -28.842 8.154   2.257   1.00 46.28 ? 58  LYS D N   1 
ATOM   6883  C CA  . LYS D 2 58  ? -28.255 8.683   3.496   1.00 47.07 ? 58  LYS D CA  1 
ATOM   6884  C C   . LYS D 2 58  ? -27.405 9.937   3.256   1.00 47.54 ? 58  LYS D C   1 
ATOM   6885  O O   . LYS D 2 58  ? -27.107 10.680  4.191   1.00 47.56 ? 58  LYS D O   1 
ATOM   6886  C CB  . LYS D 2 58  ? -27.419 7.616   4.219   1.00 46.88 ? 58  LYS D CB  1 
ATOM   6887  C CG  . LYS D 2 58  ? -28.179 6.369   4.693   1.00 47.45 ? 58  LYS D CG  1 
ATOM   6888  C CD  . LYS D 2 58  ? -29.178 6.643   5.814   1.00 48.06 ? 58  LYS D CD  1 
ATOM   6889  C CE  . LYS D 2 58  ? -30.588 6.847   5.267   1.00 48.70 ? 58  LYS D CE  1 
ATOM   6890  N NZ  . LYS D 2 58  ? -31.559 7.181   6.345   1.00 48.89 ? 58  LYS D NZ  1 
ATOM   6891  N N   . MET D 2 59  ? -27.032 10.170  2.000   1.00 48.29 ? 59  MET D N   1 
ATOM   6892  C CA  . MET D 2 59  ? -26.157 11.283  1.642   1.00 49.12 ? 59  MET D CA  1 
ATOM   6893  C C   . MET D 2 59  ? -26.875 12.442  0.943   1.00 49.51 ? 59  MET D C   1 
ATOM   6894  O O   . MET D 2 59  ? -26.231 13.428  0.592   1.00 49.81 ? 59  MET D O   1 
ATOM   6895  C CB  . MET D 2 59  ? -25.002 10.797  0.758   1.00 49.26 ? 59  MET D CB  1 
ATOM   6896  C CG  . MET D 2 59  ? -24.185 9.645   1.328   1.00 49.92 ? 59  MET D CG  1 
ATOM   6897  S SD  . MET D 2 59  ? -23.060 10.137  2.640   1.00 51.64 ? 59  MET D SD  1 
ATOM   6898  C CE  . MET D 2 59  ? -22.226 8.590   2.970   1.00 51.06 ? 59  MET D CE  1 
ATOM   6899  N N   . ASN D 2 60  ? -28.189 12.334  0.732   1.00 49.94 ? 60  ASN D N   1 
ATOM   6900  C CA  . ASN D 2 60  ? -28.928 13.403  0.040   1.00 50.32 ? 60  ASN D CA  1 
ATOM   6901  C C   . ASN D 2 60  ? -29.104 14.659  0.895   1.00 50.21 ? 60  ASN D C   1 
ATOM   6902  O O   . ASN D 2 60  ? -29.157 15.773  0.379   1.00 50.29 ? 60  ASN D O   1 
ATOM   6903  C CB  . ASN D 2 60  ? -30.266 12.912  -0.551  1.00 50.53 ? 60  ASN D CB  1 
ATOM   6904  C CG  . ASN D 2 60  ? -31.289 12.514  0.510   1.00 51.21 ? 60  ASN D CG  1 
ATOM   6905  O OD1 . ASN D 2 60  ? -31.508 13.226  1.492   1.00 52.31 ? 60  ASN D OD1 1 
ATOM   6906  N ND2 . ASN D 2 60  ? -31.944 11.377  0.294   1.00 51.99 ? 60  ASN D ND2 1 
ATOM   6907  N N   . THR D 2 61  ? -29.191 14.463  2.204   1.00 50.12 ? 61  THR D N   1 
ATOM   6908  C CA  . THR D 2 61  ? -29.202 15.568  3.148   1.00 50.06 ? 61  THR D CA  1 
ATOM   6909  C C   . THR D 2 61  ? -27.814 15.661  3.788   1.00 49.85 ? 61  THR D C   1 
ATOM   6910  O O   . THR D 2 61  ? -27.526 15.017  4.803   1.00 50.10 ? 61  THR D O   1 
ATOM   6911  C CB  . THR D 2 61  ? -30.357 15.444  4.195   1.00 50.13 ? 61  THR D CB  1 
ATOM   6912  O OG1 . THR D 2 61  ? -30.182 16.417  5.232   1.00 50.43 ? 61  THR D OG1 1 
ATOM   6913  C CG2 . THR D 2 61  ? -30.427 14.032  4.809   1.00 50.57 ? 61  THR D CG2 1 
ATOM   6914  N N   . GLN D 2 62  ? -26.954 16.450  3.151   1.00 49.31 ? 62  GLN D N   1 
ATOM   6915  C CA  . GLN D 2 62  ? -25.549 16.568  3.526   1.00 48.92 ? 62  GLN D CA  1 
ATOM   6916  C C   . GLN D 2 62  ? -25.106 18.031  3.384   1.00 48.49 ? 62  GLN D C   1 
ATOM   6917  O O   . GLN D 2 62  ? -25.654 18.773  2.560   1.00 48.44 ? 62  GLN D O   1 
ATOM   6918  C CB  . GLN D 2 62  ? -24.696 15.641  2.648   1.00 48.95 ? 62  GLN D CB  1 
ATOM   6919  C CG  . GLN D 2 62  ? -23.187 15.785  2.815   1.00 49.56 ? 62  GLN D CG  1 
ATOM   6920  C CD  . GLN D 2 62  ? -22.394 15.213  1.644   1.00 50.85 ? 62  GLN D CD  1 
ATOM   6921  O OE1 . GLN D 2 62  ? -22.640 14.091  1.193   1.00 51.48 ? 62  GLN D OE1 1 
ATOM   6922  N NE2 . GLN D 2 62  ? -21.428 15.985  1.155   1.00 50.44 ? 62  GLN D NE2 1 
ATOM   6923  N N   . PHE D 2 63  ? -24.115 18.424  4.184   1.00 47.75 ? 63  PHE D N   1 
ATOM   6924  C CA  . PHE D 2 63  ? -23.651 19.810  4.266   1.00 47.14 ? 63  PHE D CA  1 
ATOM   6925  C C   . PHE D 2 63  ? -23.324 20.462  2.920   1.00 46.99 ? 63  PHE D C   1 
ATOM   6926  O O   . PHE D 2 63  ? -22.602 19.889  2.106   1.00 47.13 ? 63  PHE D O   1 
ATOM   6927  C CB  . PHE D 2 63  ? -22.433 19.912  5.188   1.00 46.86 ? 63  PHE D CB  1 
ATOM   6928  C CG  . PHE D 2 63  ? -21.889 21.302  5.307   1.00 45.77 ? 63  PHE D CG  1 
ATOM   6929  C CD1 . PHE D 2 63  ? -22.360 22.160  6.296   1.00 44.54 ? 63  PHE D CD1 1 
ATOM   6930  C CD2 . PHE D 2 63  ? -20.920 21.762  4.418   1.00 44.77 ? 63  PHE D CD2 1 
ATOM   6931  C CE1 . PHE D 2 63  ? -21.874 23.450  6.403   1.00 43.69 ? 63  PHE D CE1 1 
ATOM   6932  C CE2 . PHE D 2 63  ? -20.426 23.049  4.514   1.00 44.38 ? 63  PHE D CE2 1 
ATOM   6933  C CZ  . PHE D 2 63  ? -20.903 23.897  5.511   1.00 44.06 ? 63  PHE D CZ  1 
ATOM   6934  N N   . GLU D 2 64  ? -23.849 21.669  2.714   1.00 46.68 ? 64  GLU D N   1 
ATOM   6935  C CA  . GLU D 2 64  ? -23.551 22.463  1.527   1.00 46.57 ? 64  GLU D CA  1 
ATOM   6936  C C   . GLU D 2 64  ? -22.880 23.784  1.919   1.00 46.23 ? 64  GLU D C   1 
ATOM   6937  O O   . GLU D 2 64  ? -23.424 24.565  2.706   1.00 46.26 ? 64  GLU D O   1 
ATOM   6938  C CB  . GLU D 2 64  ? -24.822 22.723  0.709   1.00 46.87 ? 64  GLU D CB  1 
ATOM   6939  C CG  . GLU D 2 64  ? -25.478 21.459  0.127   1.00 48.02 ? 64  GLU D CG  1 
ATOM   6940  C CD  . GLU D 2 64  ? -26.952 21.655  -0.245  1.00 49.47 ? 64  GLU D CD  1 
ATOM   6941  O OE1 . GLU D 2 64  ? -27.378 22.814  -0.449  1.00 50.24 ? 64  GLU D OE1 1 
ATOM   6942  O OE2 . GLU D 2 64  ? -27.687 20.644  -0.338  1.00 49.52 ? 64  GLU D OE2 1 
ATOM   6943  N N   . ALA D 2 65  ? -21.694 24.016  1.363   1.00 45.65 ? 65  ALA D N   1 
ATOM   6944  C CA  . ALA D 2 65  ? -20.899 25.199  1.656   1.00 45.12 ? 65  ALA D CA  1 
ATOM   6945  C C   . ALA D 2 65  ? -21.447 26.441  0.965   1.00 44.88 ? 65  ALA D C   1 
ATOM   6946  O O   . ALA D 2 65  ? -21.799 26.400  -0.213  1.00 45.16 ? 65  ALA D O   1 
ATOM   6947  C CB  . ALA D 2 65  ? -19.455 24.966  1.249   1.00 45.13 ? 65  ALA D CB  1 
ATOM   6948  N N   . VAL D 2 66  ? -21.515 27.544  1.706   1.00 44.31 ? 66  VAL D N   1 
ATOM   6949  C CA  . VAL D 2 66  ? -21.944 28.831  1.160   1.00 43.51 ? 66  VAL D CA  1 
ATOM   6950  C C   . VAL D 2 66  ? -20.778 29.812  1.236   1.00 42.90 ? 66  VAL D C   1 
ATOM   6951  O O   . VAL D 2 66  ? -20.008 29.795  2.198   1.00 43.18 ? 66  VAL D O   1 
ATOM   6952  C CB  . VAL D 2 66  ? -23.174 29.404  1.913   1.00 43.63 ? 66  VAL D CB  1 
ATOM   6953  C CG1 . VAL D 2 66  ? -23.706 30.656  1.217   1.00 43.40 ? 66  VAL D CG1 1 
ATOM   6954  C CG2 . VAL D 2 66  ? -24.278 28.355  2.022   1.00 43.49 ? 66  VAL D CG2 1 
ATOM   6955  N N   . GLY D 2 67  ? -20.644 30.652  0.212   1.00 41.98 ? 67  GLY D N   1 
ATOM   6956  C CA  . GLY D 2 67  ? -19.575 31.640  0.154   1.00 40.72 ? 67  GLY D CA  1 
ATOM   6957  C C   . GLY D 2 67  ? -19.894 32.870  0.981   1.00 39.90 ? 67  GLY D C   1 
ATOM   6958  O O   . GLY D 2 67  ? -20.915 33.529  0.764   1.00 40.08 ? 67  GLY D O   1 
ATOM   6959  N N   . ARG D 2 68  ? -19.024 33.163  1.942   1.00 38.91 ? 68  ARG D N   1 
ATOM   6960  C CA  . ARG D 2 68  ? -19.120 34.373  2.758   1.00 37.61 ? 68  ARG D CA  1 
ATOM   6961  C C   . ARG D 2 68  ? -17.815 35.137  2.660   1.00 36.95 ? 68  ARG D C   1 
ATOM   6962  O O   . ARG D 2 68  ? -16.752 34.527  2.541   1.00 36.80 ? 68  ARG D O   1 
ATOM   6963  C CB  . ARG D 2 68  ? -19.393 34.023  4.216   1.00 37.54 ? 68  ARG D CB  1 
ATOM   6964  C CG  . ARG D 2 68  ? -20.715 33.343  4.455   1.00 36.42 ? 68  ARG D CG  1 
ATOM   6965  C CD  . ARG D 2 68  ? -20.797 32.825  5.860   1.00 34.85 ? 68  ARG D CD  1 
ATOM   6966  N NE  . ARG D 2 68  ? -21.924 31.917  6.018   1.00 34.98 ? 68  ARG D NE  1 
ATOM   6967  C CZ  . ARG D 2 68  ? -21.852 30.593  5.914   1.00 35.04 ? 68  ARG D CZ  1 
ATOM   6968  N NH1 . ARG D 2 68  ? -20.698 29.990  5.657   1.00 34.66 ? 68  ARG D NH1 1 
ATOM   6969  N NH2 . ARG D 2 68  ? -22.946 29.869  6.073   1.00 35.44 ? 68  ARG D NH2 1 
ATOM   6970  N N   . GLU D 2 69  ? -17.896 36.466  2.711   1.00 36.02 ? 69  GLU D N   1 
ATOM   6971  C CA  . GLU D 2 69  ? -16.701 37.309  2.640   1.00 35.15 ? 69  GLU D CA  1 
ATOM   6972  C C   . GLU D 2 69  ? -16.493 38.174  3.879   1.00 34.12 ? 69  GLU D C   1 
ATOM   6973  O O   . GLU D 2 69  ? -17.426 38.406  4.653   1.00 33.89 ? 69  GLU D O   1 
ATOM   6974  C CB  . GLU D 2 69  ? -16.708 38.154  1.369   1.00 35.45 ? 69  GLU D CB  1 
ATOM   6975  C CG  . GLU D 2 69  ? -16.371 37.349  0.132   1.00 37.32 ? 69  GLU D CG  1 
ATOM   6976  C CD  . GLU D 2 69  ? -15.804 38.200  -0.980  1.00 39.77 ? 69  GLU D CD  1 
ATOM   6977  O OE1 . GLU D 2 69  ? -16.593 38.810  -1.735  1.00 40.38 ? 69  GLU D OE1 1 
ATOM   6978  O OE2 . GLU D 2 69  ? -14.563 38.246  -1.105  1.00 40.96 ? 69  GLU D OE2 1 
ATOM   6979  N N   . PHE D 2 70  ? -15.257 38.635  4.065   1.00 33.12 ? 70  PHE D N   1 
ATOM   6980  C CA  . PHE D 2 70  ? -14.855 39.352  5.280   1.00 32.21 ? 70  PHE D CA  1 
ATOM   6981  C C   . PHE D 2 70  ? -13.808 40.436  4.989   1.00 32.04 ? 70  PHE D C   1 
ATOM   6982  O O   . PHE D 2 70  ? -13.019 40.310  4.053   1.00 31.77 ? 70  PHE D O   1 
ATOM   6983  C CB  . PHE D 2 70  ? -14.330 38.354  6.332   1.00 31.79 ? 70  PHE D CB  1 
ATOM   6984  C CG  . PHE D 2 70  ? -15.327 37.288  6.710   1.00 30.06 ? 70  PHE D CG  1 
ATOM   6985  C CD1 . PHE D 2 70  ? -16.251 37.509  7.729   1.00 29.34 ? 70  PHE D CD1 1 
ATOM   6986  C CD2 . PHE D 2 70  ? -15.351 36.066  6.038   1.00 28.39 ? 70  PHE D CD2 1 
ATOM   6987  C CE1 . PHE D 2 70  ? -17.187 36.527  8.076   1.00 28.71 ? 70  PHE D CE1 1 
ATOM   6988  C CE2 . PHE D 2 70  ? -16.271 35.085  6.370   1.00 27.58 ? 70  PHE D CE2 1 
ATOM   6989  C CZ  . PHE D 2 70  ? -17.195 35.311  7.391   1.00 28.49 ? 70  PHE D CZ  1 
ATOM   6990  N N   . ASN D 2 71  ? -13.801 41.506  5.780   1.00 32.00 ? 71  ASN D N   1 
ATOM   6991  C CA  . ASN D 2 71  ? -12.756 42.527  5.626   1.00 32.17 ? 71  ASN D CA  1 
ATOM   6992  C C   . ASN D 2 71  ? -11.523 42.250  6.510   1.00 32.26 ? 71  ASN D C   1 
ATOM   6993  O O   . ASN D 2 71  ? -11.506 41.271  7.265   1.00 32.08 ? 71  ASN D O   1 
ATOM   6994  C CB  . ASN D 2 71  ? -13.311 43.949  5.801   1.00 31.87 ? 71  ASN D CB  1 
ATOM   6995  C CG  . ASN D 2 71  ? -13.736 44.257  7.225   1.00 32.30 ? 71  ASN D CG  1 
ATOM   6996  O OD1 . ASN D 2 71  ? -13.102 43.831  8.197   1.00 31.38 ? 71  ASN D OD1 1 
ATOM   6997  N ND2 . ASN D 2 71  ? -14.811 45.026  7.355   1.00 32.28 ? 71  ASN D ND2 1 
ATOM   6998  N N   . ASN D 2 72  ? -10.501 43.102  6.409   1.00 32.38 ? 72  ASN D N   1 
ATOM   6999  C CA  . ASN D 2 72  ? -9.221  42.846  7.093   1.00 32.74 ? 72  ASN D CA  1 
ATOM   7000  C C   . ASN D 2 72  ? -9.236  43.042  8.607   1.00 32.20 ? 72  ASN D C   1 
ATOM   7001  O O   . ASN D 2 72  ? -8.243  42.756  9.283   1.00 32.56 ? 72  ASN D O   1 
ATOM   7002  C CB  . ASN D 2 72  ? -8.046  43.608  6.449   1.00 33.03 ? 72  ASN D CB  1 
ATOM   7003  C CG  . ASN D 2 72  ? -8.449  44.961  5.878   1.00 35.23 ? 72  ASN D CG  1 
ATOM   7004  O OD1 . ASN D 2 72  ? -9.406  45.601  6.338   1.00 37.69 ? 72  ASN D OD1 1 
ATOM   7005  N ND2 . ASN D 2 72  ? -7.709  45.407  4.860   1.00 36.94 ? 72  ASN D ND2 1 
ATOM   7006  N N   . LEU D 2 73  ? -10.359 43.517  9.134   1.00 31.51 ? 73  LEU D N   1 
ATOM   7007  C CA  . LEU D 2 73  ? -10.544 43.616  10.579  1.00 31.02 ? 73  LEU D CA  1 
ATOM   7008  C C   . LEU D 2 73  ? -11.515 42.555  11.087  1.00 30.60 ? 73  LEU D C   1 
ATOM   7009  O O   . LEU D 2 73  ? -12.032 42.654  12.197  1.00 30.55 ? 73  LEU D O   1 
ATOM   7010  C CB  . LEU D 2 73  ? -10.994 45.030  10.980  1.00 31.05 ? 73  LEU D CB  1 
ATOM   7011  C CG  . LEU D 2 73  ? -9.921  46.125  10.886  1.00 31.48 ? 73  LEU D CG  1 
ATOM   7012  C CD1 . LEU D 2 73  ? -10.449 47.455  11.405  1.00 31.15 ? 73  LEU D CD1 1 
ATOM   7013  C CD2 . LEU D 2 73  ? -8.641  45.726  11.630  1.00 30.95 ? 73  LEU D CD2 1 
ATOM   7014  N N   . GLU D 2 74  ? -11.743 41.537  10.260  1.00 30.37 ? 74  GLU D N   1 
ATOM   7015  C CA  . GLU D 2 74  ? -12.634 40.427  10.588  1.00 30.11 ? 74  GLU D CA  1 
ATOM   7016  C C   . GLU D 2 74  ? -11.936 39.085  10.364  1.00 30.14 ? 74  GLU D C   1 
ATOM   7017  O O   . GLU D 2 74  ? -12.568 38.107  9.943   1.00 29.99 ? 74  GLU D O   1 
ATOM   7018  C CB  . GLU D 2 74  ? -13.906 40.497  9.745   1.00 30.14 ? 74  GLU D CB  1 
ATOM   7019  C CG  . GLU D 2 74  ? -14.853 41.646  10.092  1.00 29.98 ? 74  GLU D CG  1 
ATOM   7020  C CD  . GLU D 2 74  ? -16.121 41.632  9.251   1.00 30.03 ? 74  GLU D CD  1 
ATOM   7021  O OE1 . GLU D 2 74  ? -16.033 41.329  8.036   1.00 30.09 ? 74  GLU D OE1 1 
ATOM   7022  O OE2 . GLU D 2 74  ? -17.205 41.928  9.804   1.00 29.56 ? 74  GLU D OE2 1 
ATOM   7023  N N   . ARG D 2 75  ? -10.638 39.042  10.654  1.00 29.94 ? 75  ARG D N   1 
ATOM   7024  C CA  . ARG D 2 75  ? -9.824  37.856  10.386  1.00 30.22 ? 75  ARG D CA  1 
ATOM   7025  C C   . ARG D 2 75  ? -10.192 36.649  11.246  1.00 29.75 ? 75  ARG D C   1 
ATOM   7026  O O   . ARG D 2 75  ? -10.232 35.534  10.739  1.00 29.76 ? 75  ARG D O   1 
ATOM   7027  C CB  . ARG D 2 75  ? -8.319  38.168  10.482  1.00 30.50 ? 75  ARG D CB  1 
ATOM   7028  C CG  . ARG D 2 75  ? -7.794  39.090  9.374   1.00 31.87 ? 75  ARG D CG  1 
ATOM   7029  C CD  . ARG D 2 75  ? -8.017  38.480  7.992   1.00 36.03 ? 75  ARG D CD  1 
ATOM   7030  N NE  . ARG D 2 75  ? -8.031  39.487  6.929   1.00 39.34 ? 75  ARG D NE  1 
ATOM   7031  C CZ  . ARG D 2 75  ? -7.110  39.595  5.972   1.00 40.76 ? 75  ARG D CZ  1 
ATOM   7032  N NH1 . ARG D 2 75  ? -6.081  38.753  5.925   1.00 41.64 ? 75  ARG D NH1 1 
ATOM   7033  N NH2 . ARG D 2 75  ? -7.218  40.547  5.055   1.00 41.50 ? 75  ARG D NH2 1 
ATOM   7034  N N   . ARG D 2 76  ? -10.474 36.880  12.528  1.00 29.43 ? 76  ARG D N   1 
ATOM   7035  C CA  . ARG D 2 76  ? -10.893 35.820  13.449  1.00 29.09 ? 76  ARG D CA  1 
ATOM   7036  C C   . ARG D 2 76  ? -12.127 35.051  12.959  1.00 29.28 ? 76  ARG D C   1 
ATOM   7037  O O   . ARG D 2 76  ? -12.121 33.815  12.932  1.00 29.09 ? 76  ARG D O   1 
ATOM   7038  C CB  . ARG D 2 76  ? -11.160 36.380  14.851  1.00 28.75 ? 76  ARG D CB  1 
ATOM   7039  C CG  . ARG D 2 76  ? -9.938  36.961  15.568  1.00 28.18 ? 76  ARG D CG  1 
ATOM   7040  C CD  . ARG D 2 76  ? -10.349 37.758  16.806  1.00 26.30 ? 76  ARG D CD  1 
ATOM   7041  N NE  . ARG D 2 76  ? -11.193 38.905  16.458  1.00 25.33 ? 76  ARG D NE  1 
ATOM   7042  C CZ  . ARG D 2 76  ? -12.171 39.384  17.221  1.00 24.15 ? 76  ARG D CZ  1 
ATOM   7043  N NH1 . ARG D 2 76  ? -12.444 38.820  18.389  1.00 24.24 ? 76  ARG D NH1 1 
ATOM   7044  N NH2 . ARG D 2 76  ? -12.884 40.425  16.814  1.00 22.51 ? 76  ARG D NH2 1 
ATOM   7045  N N   . ILE D 2 77  ? -13.179 35.773  12.582  1.00 29.38 ? 77  ILE D N   1 
ATOM   7046  C CA  . ILE D 2 77  ? -14.408 35.123  12.131  1.00 30.01 ? 77  ILE D CA  1 
ATOM   7047  C C   . ILE D 2 77  ? -14.292 34.528  10.715  1.00 30.29 ? 77  ILE D C   1 
ATOM   7048  O O   . ILE D 2 77  ? -14.961 33.542  10.401  1.00 30.34 ? 77  ILE D O   1 
ATOM   7049  C CB  . ILE D 2 77  ? -15.680 36.017  12.307  1.00 30.05 ? 77  ILE D CB  1 
ATOM   7050  C CG1 . ILE D 2 77  ? -15.660 37.220  11.363  1.00 29.80 ? 77  ILE D CG1 1 
ATOM   7051  C CG2 . ILE D 2 77  ? -15.826 36.458  13.772  1.00 29.96 ? 77  ILE D CG2 1 
ATOM   7052  C CD1 . ILE D 2 77  ? -16.890 38.121  11.484  1.00 30.12 ? 77  ILE D CD1 1 
ATOM   7053  N N   . GLU D 2 78  ? -13.433 35.120  9.885   1.00 30.44 ? 78  GLU D N   1 
ATOM   7054  C CA  . GLU D 2 78  ? -13.072 34.552  8.586   1.00 30.96 ? 78  GLU D CA  1 
ATOM   7055  C C   . GLU D 2 78  ? -12.337 33.228  8.780   1.00 30.97 ? 78  GLU D C   1 
ATOM   7056  O O   . GLU D 2 78  ? -12.545 32.269  8.030   1.00 31.03 ? 78  GLU D O   1 
ATOM   7057  C CB  . GLU D 2 78  ? -12.188 35.529  7.801   1.00 31.24 ? 78  GLU D CB  1 
ATOM   7058  C CG  . GLU D 2 78  ? -11.708 35.030  6.438   1.00 32.66 ? 78  GLU D CG  1 
ATOM   7059  C CD  . GLU D 2 78  ? -10.833 36.042  5.696   1.00 36.48 ? 78  GLU D CD  1 
ATOM   7060  O OE1 . GLU D 2 78  ? -10.602 37.166  6.217   1.00 38.58 ? 78  GLU D OE1 1 
ATOM   7061  O OE2 . GLU D 2 78  ? -10.375 35.714  4.576   1.00 37.70 ? 78  GLU D OE2 1 
ATOM   7062  N N   . ASN D 2 79  ? -11.476 33.186  9.793   1.00 30.88 ? 79  ASN D N   1 
ATOM   7063  C CA  . ASN D 2 79  ? -10.738 31.980  10.122  1.00 30.97 ? 79  ASN D CA  1 
ATOM   7064  C C   . ASN D 2 79  ? -11.675 30.910  10.682  1.00 30.48 ? 79  ASN D C   1 
ATOM   7065  O O   . ASN D 2 79  ? -11.527 29.730  10.378  1.00 30.46 ? 79  ASN D O   1 
ATOM   7066  C CB  . ASN D 2 79  ? -9.607  32.299  11.102  1.00 31.26 ? 79  ASN D CB  1 
ATOM   7067  C CG  . ASN D 2 79  ? -8.661  31.131  11.300  1.00 33.35 ? 79  ASN D CG  1 
ATOM   7068  O OD1 . ASN D 2 79  ? -8.630  30.516  12.372  1.00 34.95 ? 79  ASN D OD1 1 
ATOM   7069  N ND2 . ASN D 2 79  ? -7.888  30.808  10.260  1.00 35.09 ? 79  ASN D ND2 1 
ATOM   7070  N N   . LEU D 2 80  ? -12.646 31.347  11.481  1.00 30.09 ? 80  LEU D N   1 
ATOM   7071  C CA  . LEU D 2 80  ? -13.684 30.486  12.039  1.00 29.78 ? 80  LEU D CA  1 
ATOM   7072  C C   . LEU D 2 80  ? -14.589 29.919  10.940  1.00 29.79 ? 80  LEU D C   1 
ATOM   7073  O O   . LEU D 2 80  ? -14.827 28.713  10.905  1.00 29.49 ? 80  LEU D O   1 
ATOM   7074  C CB  . LEU D 2 80  ? -14.498 31.266  13.078  1.00 29.72 ? 80  LEU D CB  1 
ATOM   7075  C CG  . LEU D 2 80  ? -15.770 30.725  13.736  1.00 29.83 ? 80  LEU D CG  1 
ATOM   7076  C CD1 . LEU D 2 80  ? -15.536 29.402  14.413  1.00 31.52 ? 80  LEU D CD1 1 
ATOM   7077  C CD2 . LEU D 2 80  ? -16.256 31.731  14.756  1.00 30.90 ? 80  LEU D CD2 1 
ATOM   7078  N N   . ASN D 2 81  ? -15.073 30.795  10.053  1.00 29.74 ? 81  ASN D N   1 
ATOM   7079  C CA  . ASN D 2 81  ? -15.866 30.402  8.880   1.00 29.72 ? 81  ASN D CA  1 
ATOM   7080  C C   . ASN D 2 81  ? -15.188 29.327  8.034   1.00 30.21 ? 81  ASN D C   1 
ATOM   7081  O O   . ASN D 2 81  ? -15.788 28.291  7.742   1.00 30.13 ? 81  ASN D O   1 
ATOM   7082  C CB  . ASN D 2 81  ? -16.178 31.622  8.007   1.00 29.48 ? 81  ASN D CB  1 
ATOM   7083  C CG  . ASN D 2 81  ? -16.988 31.267  6.771   1.00 28.45 ? 81  ASN D CG  1 
ATOM   7084  O OD1 . ASN D 2 81  ? -18.171 30.932  6.863   1.00 27.87 ? 81  ASN D OD1 1 
ATOM   7085  N ND2 . ASN D 2 81  ? -16.356 31.346  5.610   1.00 25.74 ? 81  ASN D ND2 1 
ATOM   7086  N N   . LYS D 2 82  ? -13.939 29.586  7.652   1.00 30.81 ? 82  LYS D N   1 
ATOM   7087  C CA  . LYS D 2 82  ? -13.134 28.640  6.891   1.00 31.64 ? 82  LYS D CA  1 
ATOM   7088  C C   . LYS D 2 82  ? -13.004 27.303  7.623   1.00 32.03 ? 82  LYS D C   1 
ATOM   7089  O O   . LYS D 2 82  ? -13.146 26.239  7.019   1.00 32.33 ? 82  LYS D O   1 
ATOM   7090  C CB  . LYS D 2 82  ? -11.749 29.231  6.613   1.00 31.77 ? 82  LYS D CB  1 
ATOM   7091  C CG  . LYS D 2 82  ? -10.782 28.263  5.952   1.00 33.23 ? 82  LYS D CG  1 
ATOM   7092  C CD  . LYS D 2 82  ? -9.408  28.884  5.728   1.00 35.82 ? 82  LYS D CD  1 
ATOM   7093  C CE  . LYS D 2 82  ? -8.433  27.843  5.151   1.00 37.02 ? 82  LYS D CE  1 
ATOM   7094  N NZ  . LYS D 2 82  ? -7.191  28.464  4.590   1.00 37.72 ? 82  LYS D NZ  1 
ATOM   7095  N N   . LYS D 2 83  ? -12.750 27.369  8.926   1.00 32.36 ? 83  LYS D N   1 
ATOM   7096  C CA  . LYS D 2 83  ? -12.547 26.180  9.740   1.00 32.93 ? 83  LYS D CA  1 
ATOM   7097  C C   . LYS D 2 83  ? -13.853 25.381  9.890   1.00 33.03 ? 83  LYS D C   1 
ATOM   7098  O O   . LYS D 2 83  ? -13.844 24.150  9.864   1.00 32.99 ? 83  LYS D O   1 
ATOM   7099  C CB  . LYS D 2 83  ? -11.981 26.582  11.106  1.00 32.92 ? 83  LYS D CB  1 
ATOM   7100  C CG  . LYS D 2 83  ? -10.713 25.847  11.516  1.00 34.39 ? 83  LYS D CG  1 
ATOM   7101  C CD  . LYS D 2 83  ? -9.548  26.106  10.542  1.00 35.16 ? 83  LYS D CD  1 
ATOM   7102  C CE  . LYS D 2 83  ? -8.195  25.707  11.135  1.00 35.94 ? 83  LYS D CE  1 
ATOM   7103  N NZ  . LYS D 2 83  ? -8.200  24.363  11.800  1.00 36.59 ? 83  LYS D NZ  1 
ATOM   7104  N N   . MET D 2 84  ? -14.969 26.091  10.034  1.00 33.23 ? 84  MET D N   1 
ATOM   7105  C CA  . MET D 2 84  ? -16.286 25.468  10.078  1.00 33.62 ? 84  MET D CA  1 
ATOM   7106  C C   . MET D 2 84  ? -16.604 24.722  8.774   1.00 33.72 ? 84  MET D C   1 
ATOM   7107  O O   . MET D 2 84  ? -17.051 23.572  8.809   1.00 33.47 ? 84  MET D O   1 
ATOM   7108  C CB  . MET D 2 84  ? -17.371 26.511  10.350  1.00 33.67 ? 84  MET D CB  1 
ATOM   7109  C CG  . MET D 2 84  ? -18.737 25.914  10.641  1.00 34.50 ? 84  MET D CG  1 
ATOM   7110  S SD  . MET D 2 84  ? -20.037 26.555  9.559   1.00 37.99 ? 84  MET D SD  1 
ATOM   7111  C CE  . MET D 2 84  ? -19.817 25.586  8.099   1.00 36.23 ? 84  MET D CE  1 
ATOM   7112  N N   . GLU D 2 85  ? -16.370 25.377  7.635   1.00 33.93 ? 85  GLU D N   1 
ATOM   7113  C CA  . GLU D 2 85  ? -16.722 24.804  6.332   1.00 34.07 ? 85  GLU D CA  1 
ATOM   7114  C C   . GLU D 2 85  ? -15.857 23.603  5.968   1.00 34.00 ? 85  GLU D C   1 
ATOM   7115  O O   . GLU D 2 85  ? -16.380 22.548  5.608   1.00 33.74 ? 85  GLU D O   1 
ATOM   7116  C CB  . GLU D 2 85  ? -16.718 25.862  5.225   1.00 34.18 ? 85  GLU D CB  1 
ATOM   7117  C CG  . GLU D 2 85  ? -17.835 26.902  5.376   1.00 35.25 ? 85  GLU D CG  1 
ATOM   7118  C CD  . GLU D 2 85  ? -18.472 27.317  4.054   1.00 37.81 ? 85  GLU D CD  1 
ATOM   7119  O OE1 . GLU D 2 85  ? -17.749 27.421  3.030   1.00 38.93 ? 85  GLU D OE1 1 
ATOM   7120  O OE2 . GLU D 2 85  ? -19.705 27.545  4.047   1.00 37.65 ? 85  GLU D OE2 1 
ATOM   7121  N N   . ASP D 2 86  ? -14.541 23.767  6.091   1.00 34.11 ? 86  ASP D N   1 
ATOM   7122  C CA  . ASP D 2 86  ? -13.589 22.685  5.850   1.00 34.21 ? 86  ASP D CA  1 
ATOM   7123  C C   . ASP D 2 86  ? -13.801 21.500  6.788   1.00 33.79 ? 86  ASP D C   1 
ATOM   7124  O O   . ASP D 2 86  ? -13.517 20.357  6.422   1.00 33.65 ? 86  ASP D O   1 
ATOM   7125  C CB  . ASP D 2 86  ? -12.151 23.195  5.969   1.00 34.51 ? 86  ASP D CB  1 
ATOM   7126  C CG  . ASP D 2 86  ? -11.663 23.868  4.700   1.00 36.15 ? 86  ASP D CG  1 
ATOM   7127  O OD1 . ASP D 2 86  ? -12.133 23.499  3.597   1.00 38.03 ? 86  ASP D OD1 1 
ATOM   7128  O OD2 . ASP D 2 86  ? -10.801 24.767  4.802   1.00 37.99 ? 86  ASP D OD2 1 
ATOM   7129  N N   . GLY D 2 87  ? -14.306 21.788  7.987   1.00 33.35 ? 87  GLY D N   1 
ATOM   7130  C CA  . GLY D 2 87  ? -14.570 20.775  9.007   1.00 32.88 ? 87  GLY D CA  1 
ATOM   7131  C C   . GLY D 2 87  ? -15.687 19.812  8.643   1.00 32.49 ? 87  GLY D C   1 
ATOM   7132  O O   . GLY D 2 87  ? -15.534 18.601  8.795   1.00 32.25 ? 87  GLY D O   1 
ATOM   7133  N N   . PHE D 2 88  ? -16.807 20.352  8.170   1.00 32.14 ? 88  PHE D N   1 
ATOM   7134  C CA  . PHE D 2 88  ? -17.920 19.535  7.698   1.00 32.16 ? 88  PHE D CA  1 
ATOM   7135  C C   . PHE D 2 88  ? -17.537 18.793  6.428   1.00 32.25 ? 88  PHE D C   1 
ATOM   7136  O O   . PHE D 2 88  ? -17.874 17.621  6.252   1.00 32.22 ? 88  PHE D O   1 
ATOM   7137  C CB  . PHE D 2 88  ? -19.172 20.388  7.470   1.00 32.12 ? 88  PHE D CB  1 
ATOM   7138  C CG  . PHE D 2 88  ? -19.846 20.813  8.739   1.00 31.67 ? 88  PHE D CG  1 
ATOM   7139  C CD1 . PHE D 2 88  ? -20.415 19.871  9.588   1.00 31.25 ? 88  PHE D CD1 1 
ATOM   7140  C CD2 . PHE D 2 88  ? -19.903 22.152  9.091   1.00 31.13 ? 88  PHE D CD2 1 
ATOM   7141  C CE1 . PHE D 2 88  ? -21.025 20.263  10.771  1.00 31.84 ? 88  PHE D CE1 1 
ATOM   7142  C CE2 . PHE D 2 88  ? -20.517 22.554  10.265  1.00 30.53 ? 88  PHE D CE2 1 
ATOM   7143  C CZ  . PHE D 2 88  ? -21.078 21.611  11.106  1.00 31.33 ? 88  PHE D CZ  1 
ATOM   7144  N N   . LEU D 2 89  ? -16.820 19.493  5.557   1.00 32.27 ? 89  LEU D N   1 
ATOM   7145  C CA  . LEU D 2 89  ? -16.224 18.908  4.371   1.00 32.35 ? 89  LEU D CA  1 
ATOM   7146  C C   . LEU D 2 89  ? -15.426 17.642  4.673   1.00 32.08 ? 89  LEU D C   1 
ATOM   7147  O O   . LEU D 2 89  ? -15.636 16.609  4.039   1.00 31.90 ? 89  LEU D O   1 
ATOM   7148  C CB  . LEU D 2 89  ? -15.335 19.944  3.684   1.00 32.62 ? 89  LEU D CB  1 
ATOM   7149  C CG  . LEU D 2 89  ? -15.930 20.485  2.392   1.00 33.72 ? 89  LEU D CG  1 
ATOM   7150  C CD1 . LEU D 2 89  ? -15.142 21.680  1.867   1.00 34.86 ? 89  LEU D CD1 1 
ATOM   7151  C CD2 . LEU D 2 89  ? -15.919 19.343  1.395   1.00 35.40 ? 89  LEU D CD2 1 
ATOM   7152  N N   . ASP D 2 90  ? -14.524 17.731  5.649   1.00 31.77 ? 90  ASP D N   1 
ATOM   7153  C CA  . ASP D 2 90  ? -13.696 16.597  6.040   1.00 31.60 ? 90  ASP D CA  1 
ATOM   7154  C C   . ASP D 2 90  ? -14.527 15.471  6.665   1.00 31.21 ? 90  ASP D C   1 
ATOM   7155  O O   . ASP D 2 90  ? -14.317 14.300  6.352   1.00 30.91 ? 90  ASP D O   1 
ATOM   7156  C CB  . ASP D 2 90  ? -12.557 17.042  6.969   1.00 31.55 ? 90  ASP D CB  1 
ATOM   7157  C CG  . ASP D 2 90  ? -11.532 17.933  6.264   1.00 32.69 ? 90  ASP D CG  1 
ATOM   7158  O OD1 . ASP D 2 90  ? -11.250 17.708  5.062   1.00 33.50 ? 90  ASP D OD1 1 
ATOM   7159  O OD2 . ASP D 2 90  ? -11.002 18.868  6.914   1.00 33.72 ? 90  ASP D OD2 1 
ATOM   7160  N N   . VAL D 2 91  ? -15.470 15.847  7.529   1.00 30.95 ? 91  VAL D N   1 
ATOM   7161  C CA  . VAL D 2 91  ? -16.391 14.913  8.186   1.00 30.78 ? 91  VAL D CA  1 
ATOM   7162  C C   . VAL D 2 91  ? -17.228 14.107  7.181   1.00 30.96 ? 91  VAL D C   1 
ATOM   7163  O O   . VAL D 2 91  ? -17.401 12.896  7.337   1.00 30.95 ? 91  VAL D O   1 
ATOM   7164  C CB  . VAL D 2 91  ? -17.320 15.659  9.190   1.00 30.72 ? 91  VAL D CB  1 
ATOM   7165  C CG1 . VAL D 2 91  ? -18.527 14.806  9.580   1.00 30.49 ? 91  VAL D CG1 1 
ATOM   7166  C CG2 . VAL D 2 91  ? -16.544 16.064  10.429  1.00 30.32 ? 91  VAL D CG2 1 
ATOM   7167  N N   . TRP D 2 92  ? -17.732 14.779  6.151   1.00 31.09 ? 92  TRP D N   1 
ATOM   7168  C CA  . TRP D 2 92  ? -18.543 14.117  5.135   1.00 31.29 ? 92  TRP D CA  1 
ATOM   7169  C C   . TRP D 2 92  ? -17.726 13.302  4.143   1.00 31.26 ? 92  TRP D C   1 
ATOM   7170  O O   . TRP D 2 92  ? -18.209 12.294  3.633   1.00 31.52 ? 92  TRP D O   1 
ATOM   7171  C CB  . TRP D 2 92  ? -19.461 15.106  4.418   1.00 31.36 ? 92  TRP D CB  1 
ATOM   7172  C CG  . TRP D 2 92  ? -20.671 15.465  5.234   1.00 31.84 ? 92  TRP D CG  1 
ATOM   7173  C CD1 . TRP D 2 92  ? -20.961 16.684  5.771   1.00 32.51 ? 92  TRP D CD1 1 
ATOM   7174  C CD2 . TRP D 2 92  ? -21.749 14.590  5.612   1.00 31.80 ? 92  TRP D CD2 1 
ATOM   7175  N NE1 . TRP D 2 92  ? -22.159 16.628  6.452   1.00 33.19 ? 92  TRP D NE1 1 
ATOM   7176  C CE2 . TRP D 2 92  ? -22.661 15.356  6.371   1.00 32.00 ? 92  TRP D CE2 1 
ATOM   7177  C CE3 . TRP D 2 92  ? -22.034 13.235  5.378   1.00 31.65 ? 92  TRP D CE3 1 
ATOM   7178  C CZ2 . TRP D 2 92  ? -23.836 14.813  6.904   1.00 31.74 ? 92  TRP D CZ2 1 
ATOM   7179  C CZ3 . TRP D 2 92  ? -23.206 12.695  5.906   1.00 30.96 ? 92  TRP D CZ3 1 
ATOM   7180  C CH2 . TRP D 2 92  ? -24.091 13.485  6.659   1.00 31.22 ? 92  TRP D CH2 1 
ATOM   7181  N N   . THR D 2 93  ? -16.499 13.744  3.869   1.00 31.23 ? 93  THR D N   1 
ATOM   7182  C CA  . THR D 2 93  ? -15.546 12.957  3.090   1.00 31.03 ? 93  THR D CA  1 
ATOM   7183  C C   . THR D 2 93  ? -15.266 11.647  3.829   1.00 31.15 ? 93  THR D C   1 
ATOM   7184  O O   . THR D 2 93  ? -15.384 10.567  3.244   1.00 31.60 ? 93  THR D O   1 
ATOM   7185  C CB  . THR D 2 93  ? -14.237 13.746  2.807   1.00 30.94 ? 93  THR D CB  1 
ATOM   7186  O OG1 . THR D 2 93  ? -14.522 14.844  1.939   1.00 30.91 ? 93  THR D OG1 1 
ATOM   7187  C CG2 . THR D 2 93  ? -13.198 12.876  2.133   1.00 30.85 ? 93  THR D CG2 1 
ATOM   7188  N N   . TYR D 2 94  ? -14.937 11.748  5.116   1.00 30.89 ? 94  TYR D N   1 
ATOM   7189  C CA  . TYR D 2 94  ? -14.684 10.575  5.956   1.00 30.95 ? 94  TYR D CA  1 
ATOM   7190  C C   . TYR D 2 94  ? -15.849 9.572   5.951   1.00 31.05 ? 94  TYR D C   1 
ATOM   7191  O O   . TYR D 2 94  ? -15.638 8.383   5.752   1.00 30.74 ? 94  TYR D O   1 
ATOM   7192  C CB  . TYR D 2 94  ? -14.339 11.001  7.391   1.00 30.79 ? 94  TYR D CB  1 
ATOM   7193  C CG  . TYR D 2 94  ? -14.337 9.870   8.403   1.00 30.63 ? 94  TYR D CG  1 
ATOM   7194  C CD1 . TYR D 2 94  ? -13.171 9.161   8.686   1.00 30.76 ? 94  TYR D CD1 1 
ATOM   7195  C CD2 . TYR D 2 94  ? -15.502 9.519   9.085   1.00 30.67 ? 94  TYR D CD2 1 
ATOM   7196  C CE1 . TYR D 2 94  ? -13.165 8.127   9.616   1.00 30.90 ? 94  TYR D CE1 1 
ATOM   7197  C CE2 . TYR D 2 94  ? -15.510 8.493   10.006  1.00 31.09 ? 94  TYR D CE2 1 
ATOM   7198  C CZ  . TYR D 2 94  ? -14.341 7.801   10.272  1.00 31.87 ? 94  TYR D CZ  1 
ATOM   7199  O OH  . TYR D 2 94  ? -14.358 6.785   11.200  1.00 32.97 ? 94  TYR D OH  1 
ATOM   7200  N N   . ASN D 2 95  ? -17.065 10.064  6.169   1.00 31.39 ? 95  ASN D N   1 
ATOM   7201  C CA  . ASN D 2 95  ? -18.253 9.216   6.193   1.00 31.78 ? 95  ASN D CA  1 
ATOM   7202  C C   . ASN D 2 95  ? -18.474 8.450   4.902   1.00 31.98 ? 95  ASN D C   1 
ATOM   7203  O O   . ASN D 2 95  ? -18.848 7.283   4.936   1.00 32.12 ? 95  ASN D O   1 
ATOM   7204  C CB  . ASN D 2 95  ? -19.504 10.035  6.511   1.00 31.84 ? 95  ASN D CB  1 
ATOM   7205  C CG  . ASN D 2 95  ? -19.575 10.458  7.964   1.00 32.15 ? 95  ASN D CG  1 
ATOM   7206  O OD1 . ASN D 2 95  ? -20.094 11.526  8.278   1.00 33.76 ? 95  ASN D OD1 1 
ATOM   7207  N ND2 . ASN D 2 95  ? -19.057 9.624   8.857   1.00 32.61 ? 95  ASN D ND2 1 
ATOM   7208  N N   . ALA D 2 96  ? -18.237 9.113   3.773   1.00 32.27 ? 96  ALA D N   1 
ATOM   7209  C CA  . ALA D 2 96  ? -18.452 8.518   2.461   1.00 32.39 ? 96  ALA D CA  1 
ATOM   7210  C C   . ALA D 2 96  ? -17.389 7.474   2.134   1.00 32.66 ? 96  ALA D C   1 
ATOM   7211  O O   . ALA D 2 96  ? -17.713 6.374   1.685   1.00 32.74 ? 96  ALA D O   1 
ATOM   7212  C CB  . ALA D 2 96  ? -18.503 9.598   1.385   1.00 32.33 ? 96  ALA D CB  1 
ATOM   7213  N N   . GLU D 2 97  ? -16.124 7.820   2.360   1.00 33.01 ? 97  GLU D N   1 
ATOM   7214  C CA  . GLU D 2 97  ? -15.020 6.894   2.107   1.00 33.44 ? 97  GLU D CA  1 
ATOM   7215  C C   . GLU D 2 97  ? -15.131 5.651   2.997   1.00 33.57 ? 97  GLU D C   1 
ATOM   7216  O O   . GLU D 2 97  ? -14.921 4.524   2.529   1.00 33.80 ? 97  GLU D O   1 
ATOM   7217  C CB  . GLU D 2 97  ? -13.664 7.582   2.296   1.00 33.48 ? 97  GLU D CB  1 
ATOM   7218  C CG  . GLU D 2 97  ? -13.396 8.741   1.332   1.00 34.42 ? 97  GLU D CG  1 
ATOM   7219  C CD  . GLU D 2 97  ? -11.966 9.282   1.410   1.00 36.71 ? 97  GLU D CD  1 
ATOM   7220  O OE1 . GLU D 2 97  ? -11.287 9.096   2.451   1.00 37.47 ? 97  GLU D OE1 1 
ATOM   7221  O OE2 . GLU D 2 97  ? -11.514 9.901   0.421   1.00 37.22 ? 97  GLU D OE2 1 
ATOM   7222  N N   . LEU D 2 98  ? -15.493 5.866   4.263   1.00 33.53 ? 98  LEU D N   1 
ATOM   7223  C CA  . LEU D 2 98  ? -15.619 4.793   5.241   1.00 33.63 ? 98  LEU D CA  1 
ATOM   7224  C C   . LEU D 2 98  ? -16.818 3.887   4.977   1.00 33.81 ? 98  LEU D C   1 
ATOM   7225  O O   . LEU D 2 98  ? -16.709 2.668   5.121   1.00 33.88 ? 98  LEU D O   1 
ATOM   7226  C CB  . LEU D 2 98  ? -15.689 5.360   6.661   1.00 33.69 ? 98  LEU D CB  1 
ATOM   7227  C CG  . LEU D 2 98  ? -15.733 4.358   7.820   1.00 34.01 ? 98  LEU D CG  1 
ATOM   7228  C CD1 . LEU D 2 98  ? -14.342 3.820   8.145   1.00 34.17 ? 98  LEU D CD1 1 
ATOM   7229  C CD2 . LEU D 2 98  ? -16.359 4.999   9.041   1.00 34.47 ? 98  LEU D CD2 1 
ATOM   7230  N N   . LEU D 2 99  ? -17.955 4.477   4.604   1.00 33.89 ? 99  LEU D N   1 
ATOM   7231  C CA  . LEU D 2 99  ? -19.154 3.703   4.280   1.00 34.11 ? 99  LEU D CA  1 
ATOM   7232  C C   . LEU D 2 99  ? -18.879 2.769   3.105   1.00 34.24 ? 99  LEU D C   1 
ATOM   7233  O O   . LEU D 2 99  ? -19.225 1.587   3.150   1.00 34.11 ? 99  LEU D O   1 
ATOM   7234  C CB  . LEU D 2 99  ? -20.341 4.617   3.944   1.00 34.08 ? 99  LEU D CB  1 
ATOM   7235  C CG  . LEU D 2 99  ? -21.746 4.295   4.490   1.00 34.03 ? 99  LEU D CG  1 
ATOM   7236  C CD1 . LEU D 2 99  ? -22.805 4.957   3.638   1.00 34.06 ? 99  LEU D CD1 1 
ATOM   7237  C CD2 . LEU D 2 99  ? -22.044 2.813   4.603   1.00 34.10 ? 99  LEU D CD2 1 
ATOM   7238  N N   . VAL D 2 100 ? -18.244 3.311   2.067   1.00 34.49 ? 100 VAL D N   1 
ATOM   7239  C CA  . VAL D 2 100 ? -17.928 2.558   0.850   1.00 34.73 ? 100 VAL D CA  1 
ATOM   7240  C C   . VAL D 2 100 ? -17.011 1.364   1.166   1.00 34.87 ? 100 VAL D C   1 
ATOM   7241  O O   . VAL D 2 100 ? -17.304 0.234   0.783   1.00 34.53 ? 100 VAL D O   1 
ATOM   7242  C CB  . VAL D 2 100 ? -17.359 3.496   -0.259  1.00 34.68 ? 100 VAL D CB  1 
ATOM   7243  C CG1 . VAL D 2 100 ? -16.661 2.716   -1.367  1.00 34.51 ? 100 VAL D CG1 1 
ATOM   7244  C CG2 . VAL D 2 100 ? -18.477 4.363   -0.840  1.00 34.68 ? 100 VAL D CG2 1 
ATOM   7245  N N   . LEU D 2 101 ? -15.934 1.630   1.902   1.00 35.32 ? 101 LEU D N   1 
ATOM   7246  C CA  . LEU D 2 101 ? -15.013 0.596   2.379   1.00 35.50 ? 101 LEU D CA  1 
ATOM   7247  C C   . LEU D 2 101 ? -15.708 -0.522  3.151   1.00 35.76 ? 101 LEU D C   1 
ATOM   7248  O O   . LEU D 2 101 ? -15.519 -1.702  2.848   1.00 35.79 ? 101 LEU D O   1 
ATOM   7249  C CB  . LEU D 2 101 ? -13.936 1.229   3.261   1.00 35.56 ? 101 LEU D CB  1 
ATOM   7250  C CG  . LEU D 2 101 ? -12.512 1.443   2.738   1.00 35.70 ? 101 LEU D CG  1 
ATOM   7251  C CD1 . LEU D 2 101 ? -12.442 1.653   1.224   1.00 34.85 ? 101 LEU D CD1 1 
ATOM   7252  C CD2 . LEU D 2 101 ? -11.887 2.612   3.493   1.00 35.55 ? 101 LEU D CD2 1 
ATOM   7253  N N   . MET D 2 102 ? -16.513 -0.141  4.140   1.00 36.05 ? 102 MET D N   1 
ATOM   7254  C CA  . MET D 2 102 ? -17.160 -1.105  5.028   1.00 36.39 ? 102 MET D CA  1 
ATOM   7255  C C   . MET D 2 102 ? -18.200 -1.956  4.313   1.00 36.22 ? 102 MET D C   1 
ATOM   7256  O O   . MET D 2 102 ? -18.283 -3.158  4.557   1.00 36.28 ? 102 MET D O   1 
ATOM   7257  C CB  . MET D 2 102 ? -17.773 -0.406  6.244   1.00 36.54 ? 102 MET D CB  1 
ATOM   7258  C CG  . MET D 2 102 ? -16.743 0.105   7.234   1.00 38.07 ? 102 MET D CG  1 
ATOM   7259  S SD  . MET D 2 102 ? -17.487 0.942   8.648   1.00 42.03 ? 102 MET D SD  1 
ATOM   7260  C CE  . MET D 2 102 ? -18.001 -0.466  9.634   1.00 42.27 ? 102 MET D CE  1 
ATOM   7261  N N   . GLU D 2 103 ? -18.974 -1.332  3.429   1.00 36.10 ? 103 GLU D N   1 
ATOM   7262  C CA  . GLU D 2 103 ? -19.988 -2.042  2.656   1.00 36.21 ? 103 GLU D CA  1 
ATOM   7263  C C   . GLU D 2 103 ? -19.398 -2.929  1.558   1.00 36.05 ? 103 GLU D C   1 
ATOM   7264  O O   . GLU D 2 103 ? -19.958 -3.982  1.256   1.00 36.28 ? 103 GLU D O   1 
ATOM   7265  C CB  . GLU D 2 103 ? -21.038 -1.085  2.072   1.00 36.17 ? 103 GLU D CB  1 
ATOM   7266  C CG  . GLU D 2 103 ? -22.010 -0.487  3.109   1.00 37.04 ? 103 GLU D CG  1 
ATOM   7267  C CD  . GLU D 2 103 ? -22.650 -1.526  4.039   1.00 38.35 ? 103 GLU D CD  1 
ATOM   7268  O OE1 . GLU D 2 103 ? -23.058 -2.613  3.562   1.00 37.90 ? 103 GLU D OE1 1 
ATOM   7269  O OE2 . GLU D 2 103 ? -22.747 -1.245  5.257   1.00 38.97 ? 103 GLU D OE2 1 
ATOM   7270  N N   . ASN D 2 104 ? -18.281 -2.504  0.970   1.00 35.72 ? 104 ASN D N   1 
ATOM   7271  C CA  . ASN D 2 104 ? -17.595 -3.298  -0.049  1.00 35.47 ? 104 ASN D CA  1 
ATOM   7272  C C   . ASN D 2 104 ? -17.140 -4.648  0.494   1.00 35.39 ? 104 ASN D C   1 
ATOM   7273  O O   . ASN D 2 104 ? -17.293 -5.673  -0.169  1.00 35.37 ? 104 ASN D O   1 
ATOM   7274  C CB  . ASN D 2 104 ? -16.404 -2.539  -0.644  1.00 35.19 ? 104 ASN D CB  1 
ATOM   7275  C CG  . ASN D 2 104 ? -16.826 -1.444  -1.616  1.00 35.23 ? 104 ASN D CG  1 
ATOM   7276  O OD1 . ASN D 2 104 ? -18.000 -1.327  -1.987  1.00 34.71 ? 104 ASN D OD1 1 
ATOM   7277  N ND2 . ASN D 2 104 ? -15.862 -0.627  -2.028  1.00 34.57 ? 104 ASN D ND2 1 
ATOM   7278  N N   . GLU D 2 105 ? -16.587 -4.638  1.705   1.00 35.39 ? 105 GLU D N   1 
ATOM   7279  C CA  . GLU D 2 105 ? -16.206 -5.865  2.388   1.00 35.44 ? 105 GLU D CA  1 
ATOM   7280  C C   . GLU D 2 105 ? -17.444 -6.727  2.624   1.00 34.97 ? 105 GLU D C   1 
ATOM   7281  O O   . GLU D 2 105 ? -17.400 -7.947  2.468   1.00 34.78 ? 105 GLU D O   1 
ATOM   7282  C CB  . GLU D 2 105 ? -15.503 -5.553  3.711   1.00 35.55 ? 105 GLU D CB  1 
ATOM   7283  C CG  . GLU D 2 105 ? -14.636 -6.693  4.222   1.00 37.44 ? 105 GLU D CG  1 
ATOM   7284  C CD  . GLU D 2 105 ? -13.705 -6.272  5.350   1.00 40.44 ? 105 GLU D CD  1 
ATOM   7285  O OE1 . GLU D 2 105 ? -14.196 -6.071  6.483   1.00 41.92 ? 105 GLU D OE1 1 
ATOM   7286  O OE2 . GLU D 2 105 ? -12.479 -6.156  5.110   1.00 41.00 ? 105 GLU D OE2 1 
ATOM   7287  N N   . ARG D 2 106 ? -18.550 -6.080  2.978   1.00 34.61 ? 106 ARG D N   1 
ATOM   7288  C CA  . ARG D 2 106 ? -19.788 -6.791  3.275   1.00 34.45 ? 106 ARG D CA  1 
ATOM   7289  C C   . ARG D 2 106 ? -20.440 -7.374  2.026   1.00 33.77 ? 106 ARG D C   1 
ATOM   7290  O O   . ARG D 2 106 ? -20.991 -8.471  2.079   1.00 33.62 ? 106 ARG D O   1 
ATOM   7291  C CB  . ARG D 2 106 ? -20.763 -5.900  4.043   1.00 34.68 ? 106 ARG D CB  1 
ATOM   7292  C CG  . ARG D 2 106 ? -20.276 -5.539  5.436   1.00 35.90 ? 106 ARG D CG  1 
ATOM   7293  C CD  . ARG D 2 106 ? -21.422 -5.318  6.402   1.00 38.98 ? 106 ARG D CD  1 
ATOM   7294  N NE  . ARG D 2 106 ? -22.092 -6.576  6.754   1.00 41.50 ? 106 ARG D NE  1 
ATOM   7295  C CZ  . ARG D 2 106 ? -22.892 -6.739  7.807   1.00 42.57 ? 106 ARG D CZ  1 
ATOM   7296  N NH1 . ARG D 2 106 ? -23.133 -5.726  8.637   1.00 43.37 ? 106 ARG D NH1 1 
ATOM   7297  N NH2 . ARG D 2 106 ? -23.451 -7.920  8.035   1.00 43.21 ? 106 ARG D NH2 1 
ATOM   7298  N N   . THR D 2 107 ? -20.359 -6.642  0.914   1.00 33.11 ? 107 THR D N   1 
ATOM   7299  C CA  . THR D 2 107 ? -20.877 -7.098  -0.372  1.00 32.40 ? 107 THR D CA  1 
ATOM   7300  C C   . THR D 2 107 ? -20.135 -8.356  -0.814  1.00 32.13 ? 107 THR D C   1 
ATOM   7301  O O   . THR D 2 107 ? -20.753 -9.337  -1.221  1.00 31.65 ? 107 THR D O   1 
ATOM   7302  C CB  . THR D 2 107 ? -20.764 -5.999  -1.445  1.00 32.33 ? 107 THR D CB  1 
ATOM   7303  O OG1 . THR D 2 107 ? -21.558 -4.872  -1.054  1.00 32.65 ? 107 THR D OG1 1 
ATOM   7304  C CG2 . THR D 2 107 ? -21.250 -6.499  -2.807  1.00 31.85 ? 107 THR D CG2 1 
ATOM   7305  N N   . LEU D 2 108 ? -18.811 -8.316  -0.710  1.00 31.86 ? 108 LEU D N   1 
ATOM   7306  C CA  . LEU D 2 108 ? -17.969 -9.462  -1.020  1.00 31.99 ? 108 LEU D CA  1 
ATOM   7307  C C   . LEU D 2 108 ? -18.361 -10.709 -0.218  1.00 31.95 ? 108 LEU D C   1 
ATOM   7308  O O   . LEU D 2 108 ? -18.533 -11.788 -0.795  1.00 31.99 ? 108 LEU D O   1 
ATOM   7309  C CB  . LEU D 2 108 ? -16.495 -9.107  -0.810  1.00 32.01 ? 108 LEU D CB  1 
ATOM   7310  C CG  . LEU D 2 108 ? -15.665 -8.610  -2.005  1.00 32.55 ? 108 LEU D CG  1 
ATOM   7311  C CD1 . LEU D 2 108 ? -16.449 -7.764  -3.002  1.00 32.47 ? 108 LEU D CD1 1 
ATOM   7312  C CD2 . LEU D 2 108 ? -14.425 -7.861  -1.517  1.00 32.76 ? 108 LEU D CD2 1 
ATOM   7313  N N   . ASP D 2 109 ? -18.529 -10.546 1.095   1.00 31.63 ? 109 ASP D N   1 
ATOM   7314  C CA  . ASP D 2 109 ? -18.911 -11.648 1.979   1.00 31.55 ? 109 ASP D CA  1 
ATOM   7315  C C   . ASP D 2 109 ? -20.341 -12.122 1.726   1.00 31.18 ? 109 ASP D C   1 
ATOM   7316  O O   . ASP D 2 109 ? -20.642 -13.314 1.862   1.00 31.01 ? 109 ASP D O   1 
ATOM   7317  C CB  . ASP D 2 109 ? -18.741 -11.256 3.454   1.00 31.64 ? 109 ASP D CB  1 
ATOM   7318  C CG  . ASP D 2 109 ? -17.283 -11.031 3.841   1.00 32.53 ? 109 ASP D CG  1 
ATOM   7319  O OD1 . ASP D 2 109 ? -16.407 -11.764 3.330   1.00 34.12 ? 109 ASP D OD1 1 
ATOM   7320  O OD2 . ASP D 2 109 ? -17.012 -10.125 4.664   1.00 33.28 ? 109 ASP D OD2 1 
ATOM   7321  N N   . PHE D 2 110 ? -21.214 -11.183 1.370   1.00 30.70 ? 110 PHE D N   1 
ATOM   7322  C CA  . PHE D 2 110 ? -22.602 -11.489 1.038   1.00 30.33 ? 110 PHE D CA  1 
ATOM   7323  C C   . PHE D 2 110 ? -22.645 -12.502 -0.111  1.00 30.53 ? 110 PHE D C   1 
ATOM   7324  O O   . PHE D 2 110 ? -23.350 -13.509 -0.030  1.00 30.35 ? 110 PHE D O   1 
ATOM   7325  C CB  . PHE D 2 110 ? -23.358 -10.198 0.701   1.00 29.89 ? 110 PHE D CB  1 
ATOM   7326  C CG  . PHE D 2 110 ? -24.764 -10.410 0.200   1.00 29.76 ? 110 PHE D CG  1 
ATOM   7327  C CD1 . PHE D 2 110 ? -25.734 -10.994 1.009   1.00 29.33 ? 110 PHE D CD1 1 
ATOM   7328  C CD2 . PHE D 2 110 ? -25.124 -9.996  -1.074  1.00 29.53 ? 110 PHE D CD2 1 
ATOM   7329  C CE1 . PHE D 2 110 ? -27.029 -11.178 0.549   1.00 29.06 ? 110 PHE D CE1 1 
ATOM   7330  C CE2 . PHE D 2 110 ? -26.427 -10.167 -1.541  1.00 29.53 ? 110 PHE D CE2 1 
ATOM   7331  C CZ  . PHE D 2 110 ? -27.379 -10.760 -0.728  1.00 29.14 ? 110 PHE D CZ  1 
ATOM   7332  N N   . HIS D 2 111 ? -21.857 -12.247 -1.155  1.00 30.72 ? 111 HIS D N   1 
ATOM   7333  C CA  . HIS D 2 111 ? -21.742 -13.162 -2.283  1.00 31.22 ? 111 HIS D CA  1 
ATOM   7334  C C   . HIS D 2 111 ? -21.179 -14.513 -1.848  1.00 31.53 ? 111 HIS D C   1 
ATOM   7335  O O   . HIS D 2 111 ? -21.717 -15.558 -2.223  1.00 31.72 ? 111 HIS D O   1 
ATOM   7336  C CB  . HIS D 2 111 ? -20.882 -12.560 -3.395  1.00 30.91 ? 111 HIS D CB  1 
ATOM   7337  C CG  . HIS D 2 111 ? -21.505 -11.379 -4.066  1.00 31.23 ? 111 HIS D CG  1 
ATOM   7338  N ND1 . HIS D 2 111 ? -22.710 -11.450 -4.734  1.00 31.43 ? 111 HIS D ND1 1 
ATOM   7339  C CD2 . HIS D 2 111 ? -21.085 -10.097 -4.185  1.00 30.93 ? 111 HIS D CD2 1 
ATOM   7340  C CE1 . HIS D 2 111 ? -23.007 -10.262 -5.230  1.00 30.83 ? 111 HIS D CE1 1 
ATOM   7341  N NE2 . HIS D 2 111 ? -22.036 -9.424  -4.911  1.00 31.16 ? 111 HIS D NE2 1 
ATOM   7342  N N   . ASP D 2 112 ? -20.104 -14.476 -1.061  1.00 31.74 ? 112 ASP D N   1 
ATOM   7343  C CA  . ASP D 2 112 ? -19.479 -15.678 -0.516  1.00 32.12 ? 112 ASP D CA  1 
ATOM   7344  C C   . ASP D 2 112 ? -20.527 -16.528 0.216   1.00 32.33 ? 112 ASP D C   1 
ATOM   7345  O O   . ASP D 2 112 ? -20.653 -17.728 -0.036  1.00 32.58 ? 112 ASP D O   1 
ATOM   7346  C CB  . ASP D 2 112 ? -18.317 -15.292 0.416   1.00 32.26 ? 112 ASP D CB  1 
ATOM   7347  C CG  . ASP D 2 112 ? -17.361 -16.456 0.705   1.00 32.58 ? 112 ASP D CG  1 
ATOM   7348  O OD1 . ASP D 2 112 ? -17.480 -17.516 0.060   1.00 33.83 ? 112 ASP D OD1 1 
ATOM   7349  O OD2 . ASP D 2 112 ? -16.476 -16.305 1.576   1.00 32.03 ? 112 ASP D OD2 1 
ATOM   7350  N N   . SER D 2 113 ? -21.303 -15.881 1.082   1.00 32.29 ? 113 SER D N   1 
ATOM   7351  C CA  . SER D 2 113 ? -22.335 -16.543 1.869   1.00 32.21 ? 113 SER D CA  1 
ATOM   7352  C C   . SER D 2 113 ? -23.462 -17.146 1.029   1.00 32.39 ? 113 SER D C   1 
ATOM   7353  O O   . SER D 2 113 ? -23.977 -18.217 1.368   1.00 32.41 ? 113 SER D O   1 
ATOM   7354  C CB  . SER D 2 113 ? -22.914 -15.568 2.889   1.00 32.08 ? 113 SER D CB  1 
ATOM   7355  O OG  . SER D 2 113 ? -24.142 -16.043 3.387   1.00 32.12 ? 113 SER D OG  1 
ATOM   7356  N N   . ASN D 2 114 ? -23.851 -16.454 -0.044  1.00 32.45 ? 114 ASN D N   1 
ATOM   7357  C CA  . ASN D 2 114 ? -24.881 -16.947 -0.965  1.00 32.49 ? 114 ASN D CA  1 
ATOM   7358  C C   . ASN D 2 114 ? -24.461 -18.232 -1.679  1.00 33.07 ? 114 ASN D C   1 
ATOM   7359  O O   . ASN D 2 114 ? -25.267 -19.148 -1.842  1.00 33.37 ? 114 ASN D O   1 
ATOM   7360  C CB  . ASN D 2 114 ? -25.236 -15.890 -2.013  1.00 32.13 ? 114 ASN D CB  1 
ATOM   7361  C CG  . ASN D 2 114 ? -26.005 -14.714 -1.438  1.00 31.26 ? 114 ASN D CG  1 
ATOM   7362  O OD1 . ASN D 2 114 ? -25.896 -13.593 -1.940  1.00 30.60 ? 114 ASN D OD1 1 
ATOM   7363  N ND2 . ASN D 2 114 ? -26.788 -14.958 -0.397  1.00 29.11 ? 114 ASN D ND2 1 
ATOM   7364  N N   . VAL D 2 115 ? -23.195 -18.278 -2.098  1.00 33.53 ? 115 VAL D N   1 
ATOM   7365  C CA  . VAL D 2 115 ? -22.613 -19.434 -2.775  1.00 33.89 ? 115 VAL D CA  1 
ATOM   7366  C C   . VAL D 2 115 ? -22.620 -20.671 -1.871  1.00 34.27 ? 115 VAL D C   1 
ATOM   7367  O O   . VAL D 2 115 ? -23.073 -21.747 -2.286  1.00 34.33 ? 115 VAL D O   1 
ATOM   7368  C CB  . VAL D 2 115 ? -21.170 -19.129 -3.271  1.00 33.88 ? 115 VAL D CB  1 
ATOM   7369  C CG1 . VAL D 2 115 ? -20.523 -20.370 -3.867  1.00 34.07 ? 115 VAL D CG1 1 
ATOM   7370  C CG2 . VAL D 2 115 ? -21.186 -18.018 -4.298  1.00 33.77 ? 115 VAL D CG2 1 
ATOM   7371  N N   . LYS D 2 116 ? -22.127 -20.508 -0.640  1.00 34.45 ? 116 LYS D N   1 
ATOM   7372  C CA  . LYS D 2 116 ? -22.148 -21.573 0.359   1.00 34.62 ? 116 LYS D CA  1 
ATOM   7373  C C   . LYS D 2 116 ? -23.571 -22.058 0.647   1.00 34.79 ? 116 LYS D C   1 
ATOM   7374  O O   . LYS D 2 116 ? -23.817 -23.264 0.686   1.00 34.72 ? 116 LYS D O   1 
ATOM   7375  C CB  . LYS D 2 116 ? -21.481 -21.116 1.654   1.00 34.71 ? 116 LYS D CB  1 
ATOM   7376  C CG  . LYS D 2 116 ? -21.335 -22.217 2.683   1.00 35.25 ? 116 LYS D CG  1 
ATOM   7377  C CD  . LYS D 2 116 ? -21.263 -21.669 4.092   1.00 36.44 ? 116 LYS D CD  1 
ATOM   7378  C CE  . LYS D 2 116 ? -21.030 -22.791 5.101   1.00 36.78 ? 116 LYS D CE  1 
ATOM   7379  N NZ  . LYS D 2 116 ? -19.711 -23.457 4.873   1.00 36.78 ? 116 LYS D NZ  1 
ATOM   7380  N N   . ASN D 2 117 ? -24.498 -21.121 0.845   1.00 35.04 ? 117 ASN D N   1 
ATOM   7381  C CA  . ASN D 2 117 ? -25.896 -21.469 1.084   1.00 35.63 ? 117 ASN D CA  1 
ATOM   7382  C C   . ASN D 2 117 ? -26.509 -22.262 -0.075  1.00 35.99 ? 117 ASN D C   1 
ATOM   7383  O O   . ASN D 2 117 ? -27.246 -23.224 0.149   1.00 35.91 ? 117 ASN D O   1 
ATOM   7384  C CB  . ASN D 2 117 ? -26.738 -20.225 1.391   1.00 35.62 ? 117 ASN D CB  1 
ATOM   7385  C CG  . ASN D 2 117 ? -26.466 -19.645 2.779   1.00 36.20 ? 117 ASN D CG  1 
ATOM   7386  O OD1 . ASN D 2 117 ? -25.942 -20.324 3.669   1.00 36.60 ? 117 ASN D OD1 1 
ATOM   7387  N ND2 . ASN D 2 117 ? -26.835 -18.378 2.968   1.00 36.00 ? 117 ASN D ND2 1 
ATOM   7388  N N   . LEU D 2 118 ? -26.189 -21.861 -1.306  1.00 36.42 ? 118 LEU D N   1 
ATOM   7389  C CA  . LEU D 2 118 ? -26.658 -22.569 -2.496  1.00 37.00 ? 118 LEU D CA  1 
ATOM   7390  C C   . LEU D 2 118 ? -26.143 -24.012 -2.513  1.00 37.42 ? 118 LEU D C   1 
ATOM   7391  O O   . LEU D 2 118 ? -26.892 -24.949 -2.792  1.00 37.35 ? 118 LEU D O   1 
ATOM   7392  C CB  . LEU D 2 118 ? -26.220 -21.840 -3.771  1.00 36.91 ? 118 LEU D CB  1 
ATOM   7393  C CG  . LEU D 2 118 ? -26.734 -22.429 -5.090  1.00 37.05 ? 118 LEU D CG  1 
ATOM   7394  C CD1 . LEU D 2 118 ? -28.217 -22.142 -5.263  1.00 36.81 ? 118 LEU D CD1 1 
ATOM   7395  C CD2 . LEU D 2 118 ? -25.944 -21.899 -6.275  1.00 37.76 ? 118 LEU D CD2 1 
ATOM   7396  N N   . TYR D 2 119 ? -24.856 -24.165 -2.213  1.00 37.96 ? 119 TYR D N   1 
ATOM   7397  C CA  . TYR D 2 119 ? -24.210 -25.465 -2.099  1.00 38.50 ? 119 TYR D CA  1 
ATOM   7398  C C   . TYR D 2 119 ? -24.845 -26.338 -1.001  1.00 38.82 ? 119 TYR D C   1 
ATOM   7399  O O   . TYR D 2 119 ? -25.098 -27.529 -1.222  1.00 39.06 ? 119 TYR D O   1 
ATOM   7400  C CB  . TYR D 2 119 ? -22.711 -25.265 -1.854  1.00 38.43 ? 119 TYR D CB  1 
ATOM   7401  C CG  . TYR D 2 119 ? -21.936 -26.525 -1.562  1.00 38.86 ? 119 TYR D CG  1 
ATOM   7402  C CD1 . TYR D 2 119 ? -21.394 -27.288 -2.592  1.00 39.44 ? 119 TYR D CD1 1 
ATOM   7403  C CD2 . TYR D 2 119 ? -21.725 -26.945 -0.252  1.00 39.07 ? 119 TYR D CD2 1 
ATOM   7404  C CE1 . TYR D 2 119 ? -20.677 -28.444 -2.321  1.00 39.40 ? 119 TYR D CE1 1 
ATOM   7405  C CE2 . TYR D 2 119 ? -21.012 -28.095 0.024   1.00 39.31 ? 119 TYR D CE2 1 
ATOM   7406  C CZ  . TYR D 2 119 ? -20.489 -28.837 -1.014  1.00 39.60 ? 119 TYR D CZ  1 
ATOM   7407  O OH  . TYR D 2 119 ? -19.777 -29.978 -0.737  1.00 40.74 ? 119 TYR D OH  1 
ATOM   7408  N N   . ASP D 2 120 ? -25.109 -25.747 0.165   1.00 38.90 ? 120 ASP D N   1 
ATOM   7409  C CA  . ASP D 2 120 ? -25.721 -26.477 1.277   1.00 39.13 ? 120 ASP D CA  1 
ATOM   7410  C C   . ASP D 2 120 ? -27.157 -26.894 0.977   1.00 39.37 ? 120 ASP D C   1 
ATOM   7411  O O   . ASP D 2 120 ? -27.606 -27.938 1.441   1.00 39.66 ? 120 ASP D O   1 
ATOM   7412  C CB  . ASP D 2 120 ? -25.680 -25.659 2.576   1.00 39.11 ? 120 ASP D CB  1 
ATOM   7413  C CG  . ASP D 2 120 ? -24.312 -25.671 3.245   1.00 38.92 ? 120 ASP D CG  1 
ATOM   7414  O OD1 . ASP D 2 120 ? -23.518 -26.608 3.017   1.00 38.71 ? 120 ASP D OD1 1 
ATOM   7415  O OD2 . ASP D 2 120 ? -24.032 -24.732 4.016   1.00 40.09 ? 120 ASP D OD2 1 
ATOM   7416  N N   . LYS D 2 121 ? -27.869 -26.069 0.210   1.00 39.59 ? 121 LYS D N   1 
ATOM   7417  C CA  . LYS D 2 121 ? -29.241 -26.360 -0.215  1.00 39.76 ? 121 LYS D CA  1 
ATOM   7418  C C   . LYS D 2 121 ? -29.294 -27.653 -1.037  1.00 39.78 ? 121 LYS D C   1 
ATOM   7419  O O   . LYS D 2 121 ? -30.205 -28.464 -0.875  1.00 39.81 ? 121 LYS D O   1 
ATOM   7420  C CB  . LYS D 2 121 ? -29.808 -25.175 -1.011  1.00 39.73 ? 121 LYS D CB  1 
ATOM   7421  C CG  . LYS D 2 121 ? -31.161 -25.412 -1.689  1.00 40.34 ? 121 LYS D CG  1 
ATOM   7422  C CD  . LYS D 2 121 ? -31.444 -24.328 -2.734  1.00 41.55 ? 121 LYS D CD  1 
ATOM   7423  C CE  . LYS D 2 121 ? -32.571 -24.728 -3.682  1.00 42.67 ? 121 LYS D CE  1 
ATOM   7424  N NZ  . LYS D 2 121 ? -32.658 -23.830 -4.870  1.00 42.94 ? 121 LYS D NZ  1 
ATOM   7425  N N   . VAL D 2 122 ? -28.304 -27.833 -1.907  1.00 39.80 ? 122 VAL D N   1 
ATOM   7426  C CA  . VAL D 2 122 ? -28.183 -29.040 -2.719  1.00 39.90 ? 122 VAL D CA  1 
ATOM   7427  C C   . VAL D 2 122 ? -27.741 -30.220 -1.850  1.00 40.11 ? 122 VAL D C   1 
ATOM   7428  O O   . VAL D 2 122 ? -28.327 -31.306 -1.919  1.00 40.19 ? 122 VAL D O   1 
ATOM   7429  C CB  . VAL D 2 122 ? -27.215 -28.817 -3.921  1.00 39.79 ? 122 VAL D CB  1 
ATOM   7430  C CG1 . VAL D 2 122 ? -26.829 -30.135 -4.584  1.00 39.44 ? 122 VAL D CG1 1 
ATOM   7431  C CG2 . VAL D 2 122 ? -27.848 -27.882 -4.944  1.00 39.72 ? 122 VAL D CG2 1 
ATOM   7432  N N   . ARG D 2 123 ? -26.726 -29.984 -1.021  1.00 40.20 ? 123 ARG D N   1 
ATOM   7433  C CA  . ARG D 2 123 ? -26.161 -31.001 -0.133  1.00 40.40 ? 123 ARG D CA  1 
ATOM   7434  C C   . ARG D 2 123 ? -27.197 -31.585 0.834   1.00 40.28 ? 123 ARG D C   1 
ATOM   7435  O O   . ARG D 2 123 ? -27.215 -32.791 1.077   1.00 40.20 ? 123 ARG D O   1 
ATOM   7436  C CB  . ARG D 2 123 ? -24.977 -30.407 0.637   1.00 40.53 ? 123 ARG D CB  1 
ATOM   7437  C CG  . ARG D 2 123 ? -24.249 -31.370 1.553   1.00 41.28 ? 123 ARG D CG  1 
ATOM   7438  C CD  . ARG D 2 123 ? -23.190 -30.634 2.356   1.00 43.73 ? 123 ARG D CD  1 
ATOM   7439  N NE  . ARG D 2 123 ? -23.264 -30.980 3.774   1.00 45.62 ? 123 ARG D NE  1 
ATOM   7440  C CZ  . ARG D 2 123 ? -23.889 -30.252 4.696   1.00 46.17 ? 123 ARG D CZ  1 
ATOM   7441  N NH1 . ARG D 2 123 ? -24.493 -29.115 4.365   1.00 45.40 ? 123 ARG D NH1 1 
ATOM   7442  N NH2 . ARG D 2 123 ? -23.902 -30.660 5.959   1.00 47.15 ? 123 ARG D NH2 1 
ATOM   7443  N N   . LEU D 2 124 ? -28.057 -30.726 1.371   1.00 40.28 ? 124 LEU D N   1 
ATOM   7444  C CA  . LEU D 2 124 ? -29.090 -31.150 2.310   1.00 40.57 ? 124 LEU D CA  1 
ATOM   7445  C C   . LEU D 2 124 ? -30.306 -31.793 1.635   1.00 40.73 ? 124 LEU D C   1 
ATOM   7446  O O   . LEU D 2 124 ? -31.128 -32.421 2.302   1.00 40.84 ? 124 LEU D O   1 
ATOM   7447  C CB  . LEU D 2 124 ? -29.513 -29.976 3.198   1.00 40.64 ? 124 LEU D CB  1 
ATOM   7448  C CG  . LEU D 2 124 ? -28.813 -29.760 4.550   1.00 41.07 ? 124 LEU D CG  1 
ATOM   7449  C CD1 . LEU D 2 124 ? -27.565 -30.621 4.740   1.00 41.73 ? 124 LEU D CD1 1 
ATOM   7450  C CD2 . LEU D 2 124 ? -28.488 -28.293 4.765   1.00 41.51 ? 124 LEU D CD2 1 
ATOM   7451  N N   . GLN D 2 125 ? -30.385 -31.664 0.319   1.00 40.88 ? 125 GLN D N   1 
ATOM   7452  C CA  . GLN D 2 125 ? -31.429 -32.305 -0.459  1.00 41.02 ? 125 GLN D CA  1 
ATOM   7453  C C   . GLN D 2 125 ? -31.008 -33.718 -0.823  1.00 41.18 ? 125 GLN D C   1 
ATOM   7454  O O   . GLN D 2 125 ? -31.814 -34.640 -0.819  1.00 41.19 ? 125 GLN D O   1 
ATOM   7455  C CB  . GLN D 2 125 ? -31.672 -31.525 -1.744  1.00 40.98 ? 125 GLN D CB  1 
ATOM   7456  C CG  . GLN D 2 125 ? -32.844 -30.583 -1.711  1.00 40.62 ? 125 GLN D CG  1 
ATOM   7457  C CD  . GLN D 2 125 ? -33.060 -29.912 -3.045  1.00 40.87 ? 125 GLN D CD  1 
ATOM   7458  O OE1 . GLN D 2 125 ? -34.162 -29.909 -3.577  1.00 41.57 ? 125 GLN D OE1 1 
ATOM   7459  N NE2 . GLN D 2 125 ? -31.999 -29.351 -3.599  1.00 40.10 ? 125 GLN D NE2 1 
ATOM   7460  N N   . LEU D 2 126 ? -29.730 -33.868 -1.142  1.00 41.26 ? 126 LEU D N   1 
ATOM   7461  C CA  . LEU D 2 126 ? -29.185 -35.100 -1.688  1.00 41.50 ? 126 LEU D CA  1 
ATOM   7462  C C   . LEU D 2 126 ? -28.811 -36.136 -0.626  1.00 41.88 ? 126 LEU D C   1 
ATOM   7463  O O   . LEU D 2 126 ? -29.114 -37.323 -0.789  1.00 41.87 ? 126 LEU D O   1 
ATOM   7464  C CB  . LEU D 2 126 ? -27.989 -34.785 -2.590  1.00 41.35 ? 126 LEU D CB  1 
ATOM   7465  C CG  . LEU D 2 126 ? -28.220 -34.561 -4.092  1.00 41.38 ? 126 LEU D CG  1 
ATOM   7466  C CD1 . LEU D 2 126 ? -29.454 -33.721 -4.423  1.00 41.86 ? 126 LEU D CD1 1 
ATOM   7467  C CD2 . LEU D 2 126 ? -26.984 -33.959 -4.731  1.00 41.11 ? 126 LEU D CD2 1 
ATOM   7468  N N   . ARG D 2 127 ? -28.178 -35.681 0.457   1.00 42.31 ? 127 ARG D N   1 
ATOM   7469  C CA  . ARG D 2 127 ? -27.657 -36.551 1.529   1.00 42.74 ? 127 ARG D CA  1 
ATOM   7470  C C   . ARG D 2 127 ? -26.737 -37.648 0.983   1.00 42.97 ? 127 ARG D C   1 
ATOM   7471  O O   . ARG D 2 127 ? -25.745 -37.358 0.318   1.00 43.03 ? 127 ARG D O   1 
ATOM   7472  C CB  . ARG D 2 127 ? -28.781 -37.192 2.354   1.00 42.81 ? 127 ARG D CB  1 
ATOM   7473  C CG  . ARG D 2 127 ? -29.868 -36.276 2.857   1.00 43.21 ? 127 ARG D CG  1 
ATOM   7474  C CD  . ARG D 2 127 ? -30.697 -37.047 3.866   1.00 44.53 ? 127 ARG D CD  1 
ATOM   7475  N NE  . ARG D 2 127 ? -32.132 -36.873 3.669   1.00 45.80 ? 127 ARG D NE  1 
ATOM   7476  C CZ  . ARG D 2 127 ? -33.066 -37.628 4.246   1.00 46.70 ? 127 ARG D CZ  1 
ATOM   7477  N NH1 . ARG D 2 127 ? -32.724 -38.621 5.063   1.00 46.74 ? 127 ARG D NH1 1 
ATOM   7478  N NH2 . ARG D 2 127 ? -34.348 -37.392 4.002   1.00 47.30 ? 127 ARG D NH2 1 
ATOM   7479  N N   . ASP D 2 128 ? -27.083 -38.906 1.251   1.00 43.41 ? 128 ASP D N   1 
ATOM   7480  C CA  . ASP D 2 128 ? -26.268 -40.036 0.799   1.00 43.85 ? 128 ASP D CA  1 
ATOM   7481  C C   . ASP D 2 128 ? -26.712 -40.650 -0.540  1.00 44.04 ? 128 ASP D C   1 
ATOM   7482  O O   . ASP D 2 128 ? -26.184 -41.687 -0.947  1.00 44.18 ? 128 ASP D O   1 
ATOM   7483  C CB  . ASP D 2 128 ? -26.096 -41.097 1.910   1.00 43.81 ? 128 ASP D CB  1 
ATOM   7484  C CG  . ASP D 2 128 ? -27.414 -41.723 2.365   1.00 44.13 ? 128 ASP D CG  1 
ATOM   7485  O OD1 . ASP D 2 128 ? -28.497 -41.295 1.918   1.00 44.69 ? 128 ASP D OD1 1 
ATOM   7486  O OD2 . ASP D 2 128 ? -27.364 -42.662 3.188   1.00 44.23 ? 128 ASP D OD2 1 
ATOM   7487  N N   . ASN D 2 129 ? -27.655 -40.000 -1.226  1.00 44.26 ? 129 ASN D N   1 
ATOM   7488  C CA  . ASN D 2 129 ? -28.024 -40.391 -2.597  1.00 44.70 ? 129 ASN D CA  1 
ATOM   7489  C C   . ASN D 2 129 ? -26.981 -39.938 -3.617  1.00 45.20 ? 129 ASN D C   1 
ATOM   7490  O O   . ASN D 2 129 ? -27.036 -40.320 -4.787  1.00 45.24 ? 129 ASN D O   1 
ATOM   7491  C CB  . ASN D 2 129 ? -29.405 -39.845 -2.993  1.00 44.50 ? 129 ASN D CB  1 
ATOM   7492  C CG  . ASN D 2 129 ? -30.559 -40.654 -2.412  1.00 44.26 ? 129 ASN D CG  1 
ATOM   7493  O OD1 . ASN D 2 129 ? -31.722 -40.412 -2.740  1.00 43.57 ? 129 ASN D OD1 1 
ATOM   7494  N ND2 . ASN D 2 129 ? -30.246 -41.606 -1.542  1.00 44.43 ? 129 ASN D ND2 1 
ATOM   7495  N N   . ALA D 2 130 ? -26.041 -39.114 -3.163  1.00 45.96 ? 130 ALA D N   1 
ATOM   7496  C CA  . ALA D 2 130 ? -24.946 -38.626 -3.993  1.00 46.82 ? 130 ALA D CA  1 
ATOM   7497  C C   . ALA D 2 130 ? -23.641 -38.575 -3.202  1.00 47.51 ? 130 ALA D C   1 
ATOM   7498  O O   . ALA D 2 130 ? -23.653 -38.484 -1.971  1.00 47.51 ? 130 ALA D O   1 
ATOM   7499  C CB  . ALA D 2 130 ? -25.279 -37.249 -4.564  1.00 46.58 ? 130 ALA D CB  1 
ATOM   7500  N N   . LYS D 2 131 ? -22.527 -38.644 -3.927  1.00 48.56 ? 131 LYS D N   1 
ATOM   7501  C CA  . LYS D 2 131 ? -21.184 -38.562 -3.354  1.00 49.75 ? 131 LYS D CA  1 
ATOM   7502  C C   . LYS D 2 131 ? -20.694 -37.114 -3.405  1.00 50.32 ? 131 LYS D C   1 
ATOM   7503  O O   . LYS D 2 131 ? -20.770 -36.461 -4.452  1.00 50.47 ? 131 LYS D O   1 
ATOM   7504  C CB  . LYS D 2 131 ? -20.228 -39.467 -4.141  1.00 49.88 ? 131 LYS D CB  1 
ATOM   7505  C CG  . LYS D 2 131 ? -18.848 -39.665 -3.515  1.00 50.67 ? 131 LYS D CG  1 
ATOM   7506  C CD  . LYS D 2 131 ? -17.783 -39.990 -4.576  1.00 52.06 ? 131 LYS D CD  1 
ATOM   7507  C CE  . LYS D 2 131 ? -17.937 -41.393 -5.178  1.00 52.91 ? 131 LYS D CE  1 
ATOM   7508  N NZ  . LYS D 2 131 ? -17.484 -42.471 -4.249  1.00 53.49 ? 131 LYS D NZ  1 
ATOM   7509  N N   . GLU D 2 132 ? -20.196 -36.623 -2.275  1.00 51.05 ? 132 GLU D N   1 
ATOM   7510  C CA  . GLU D 2 132 ? -19.695 -35.254 -2.168  1.00 51.87 ? 132 GLU D CA  1 
ATOM   7511  C C   . GLU D 2 132 ? -18.221 -35.196 -2.575  1.00 52.32 ? 132 GLU D C   1 
ATOM   7512  O O   . GLU D 2 132 ? -17.335 -35.534 -1.783  1.00 52.46 ? 132 GLU D O   1 
ATOM   7513  C CB  . GLU D 2 132 ? -19.889 -34.733 -0.737  1.00 51.94 ? 132 GLU D CB  1 
ATOM   7514  C CG  . GLU D 2 132 ? -19.752 -33.219 -0.570  1.00 52.47 ? 132 GLU D CG  1 
ATOM   7515  C CD  . GLU D 2 132 ? -20.029 -32.745 0.856   1.00 53.27 ? 132 GLU D CD  1 
ATOM   7516  O OE1 . GLU D 2 132 ? -20.697 -33.472 1.625   1.00 53.94 ? 132 GLU D OE1 1 
ATOM   7517  O OE2 . GLU D 2 132 ? -19.580 -31.635 1.212   1.00 53.34 ? 132 GLU D OE2 1 
ATOM   7518  N N   . LEU D 2 133 ? -17.967 -34.767 -3.807  1.00 52.80 ? 133 LEU D N   1 
ATOM   7519  C CA  . LEU D 2 133 ? -16.607 -34.689 -4.328  1.00 53.29 ? 133 LEU D CA  1 
ATOM   7520  C C   . LEU D 2 133 ? -15.687 -33.882 -3.415  1.00 53.43 ? 133 LEU D C   1 
ATOM   7521  O O   . LEU D 2 133 ? -14.545 -34.270 -3.172  1.00 53.71 ? 133 LEU D O   1 
ATOM   7522  C CB  . LEU D 2 133 ? -16.607 -34.088 -5.735  1.00 53.39 ? 133 LEU D CB  1 
ATOM   7523  C CG  . LEU D 2 133 ? -16.675 -35.082 -6.897  1.00 53.92 ? 133 LEU D CG  1 
ATOM   7524  C CD1 . LEU D 2 133 ? -15.405 -35.916 -6.964  1.00 54.41 ? 133 LEU D CD1 1 
ATOM   7525  C CD2 . LEU D 2 133 ? -17.901 -35.973 -6.771  1.00 54.33 ? 133 LEU D CD2 1 
ATOM   7526  N N   . GLY D 2 134 ? -16.190 -32.758 -2.915  1.00 53.57 ? 134 GLY D N   1 
ATOM   7527  C CA  . GLY D 2 134 ? -15.396 -31.878 -2.054  1.00 53.59 ? 134 GLY D CA  1 
ATOM   7528  C C   . GLY D 2 134 ? -14.896 -30.614 -2.731  1.00 53.59 ? 134 GLY D C   1 
ATOM   7529  O O   . GLY D 2 134 ? -14.052 -29.903 -2.185  1.00 53.67 ? 134 GLY D O   1 
ATOM   7530  N N   . ASN D 2 135 ? -15.416 -30.337 -3.923  1.00 53.60 ? 135 ASN D N   1 
ATOM   7531  C CA  . ASN D 2 135 ? -15.034 -29.150 -4.678  1.00 53.61 ? 135 ASN D CA  1 
ATOM   7532  C C   . ASN D 2 135 ? -16.250 -28.404 -5.238  1.00 53.58 ? 135 ASN D C   1 
ATOM   7533  O O   . ASN D 2 135 ? -16.137 -27.627 -6.187  1.00 53.57 ? 135 ASN D O   1 
ATOM   7534  C CB  . ASN D 2 135 ? -14.056 -29.526 -5.798  1.00 53.60 ? 135 ASN D CB  1 
ATOM   7535  C CG  . ASN D 2 135 ? -14.684 -30.420 -6.857  1.00 53.95 ? 135 ASN D CG  1 
ATOM   7536  O OD1 . ASN D 2 135 ? -15.764 -30.987 -6.660  1.00 53.93 ? 135 ASN D OD1 1 
ATOM   7537  N ND2 . ASN D 2 135 ? -14.004 -30.551 -7.993  1.00 54.14 ? 135 ASN D ND2 1 
ATOM   7538  N N   . GLY D 2 136 ? -17.410 -28.652 -4.638  1.00 53.53 ? 136 GLY D N   1 
ATOM   7539  C CA  . GLY D 2 136 ? -18.661 -28.067 -5.098  1.00 53.65 ? 136 GLY D CA  1 
ATOM   7540  C C   . GLY D 2 136 ? -19.471 -28.969 -6.012  1.00 53.81 ? 136 GLY D C   1 
ATOM   7541  O O   . GLY D 2 136 ? -20.518 -28.559 -6.515  1.00 53.78 ? 136 GLY D O   1 
ATOM   7542  N N   . CYS D 2 137 ? -18.990 -30.193 -6.230  1.00 54.00 ? 137 CYS D N   1 
ATOM   7543  C CA  . CYS D 2 137 ? -19.657 -31.140 -7.130  1.00 54.20 ? 137 CYS D CA  1 
ATOM   7544  C C   . CYS D 2 137 ? -20.207 -32.371 -6.414  1.00 54.27 ? 137 CYS D C   1 
ATOM   7545  O O   . CYS D 2 137 ? -19.660 -32.817 -5.401  1.00 54.11 ? 137 CYS D O   1 
ATOM   7546  C CB  . CYS D 2 137 ? -18.725 -31.568 -8.266  1.00 54.14 ? 137 CYS D CB  1 
ATOM   7547  S SG  . CYS D 2 137 ? -18.218 -30.230 -9.364  1.00 54.89 ? 137 CYS D SG  1 
ATOM   7548  N N   . PHE D 2 138 ? -21.292 -32.914 -6.961  1.00 54.48 ? 138 PHE D N   1 
ATOM   7549  C CA  . PHE D 2 138 ? -21.932 -34.104 -6.408  1.00 54.80 ? 138 PHE D CA  1 
ATOM   7550  C C   . PHE D 2 138 ? -22.092 -35.188 -7.468  1.00 55.01 ? 138 PHE D C   1 
ATOM   7551  O O   . PHE D 2 138 ? -22.708 -34.956 -8.511  1.00 54.87 ? 138 PHE D O   1 
ATOM   7552  C CB  . PHE D 2 138 ? -23.298 -33.754 -5.802  1.00 54.70 ? 138 PHE D CB  1 
ATOM   7553  C CG  . PHE D 2 138 ? -23.222 -32.861 -4.595  1.00 54.58 ? 138 PHE D CG  1 
ATOM   7554  C CD1 . PHE D 2 138 ? -23.063 -33.401 -3.323  1.00 54.37 ? 138 PHE D CD1 1 
ATOM   7555  C CD2 . PHE D 2 138 ? -23.321 -31.480 -4.728  1.00 54.65 ? 138 PHE D CD2 1 
ATOM   7556  C CE1 . PHE D 2 138 ? -22.998 -32.580 -2.201  1.00 54.42 ? 138 PHE D CE1 1 
ATOM   7557  C CE2 . PHE D 2 138 ? -23.254 -30.650 -3.612  1.00 54.68 ? 138 PHE D CE2 1 
ATOM   7558  C CZ  . PHE D 2 138 ? -23.092 -31.202 -2.347  1.00 54.58 ? 138 PHE D CZ  1 
ATOM   7559  N N   . GLU D 2 139 ? -21.530 -36.366 -7.197  1.00 55.36 ? 139 GLU D N   1 
ATOM   7560  C CA  . GLU D 2 139 ? -21.691 -37.520 -8.084  1.00 55.81 ? 139 GLU D CA  1 
ATOM   7561  C C   . GLU D 2 139 ? -22.903 -38.351 -7.654  1.00 55.81 ? 139 GLU D C   1 
ATOM   7562  O O   . GLU D 2 139 ? -22.935 -38.889 -6.546  1.00 55.67 ? 139 GLU D O   1 
ATOM   7563  C CB  . GLU D 2 139 ? -20.420 -38.379 -8.100  1.00 55.96 ? 139 GLU D CB  1 
ATOM   7564  C CG  . GLU D 2 139 ? -20.432 -39.521 -9.121  1.00 56.79 ? 139 GLU D CG  1 
ATOM   7565  C CD  . GLU D 2 139 ? -19.349 -40.562 -8.859  1.00 57.78 ? 139 GLU D CD  1 
ATOM   7566  O OE1 . GLU D 2 139 ? -19.697 -41.736 -8.594  1.00 58.23 ? 139 GLU D OE1 1 
ATOM   7567  O OE2 . GLU D 2 139 ? -18.152 -40.206 -8.909  1.00 58.08 ? 139 GLU D OE2 1 
ATOM   7568  N N   . PHE D 2 140 ? -23.893 -38.443 -8.539  1.00 55.96 ? 140 PHE D N   1 
ATOM   7569  C CA  . PHE D 2 140 ? -25.126 -39.185 -8.265  1.00 56.18 ? 140 PHE D CA  1 
ATOM   7570  C C   . PHE D 2 140 ? -24.929 -40.703 -8.247  1.00 56.30 ? 140 PHE D C   1 
ATOM   7571  O O   . PHE D 2 140 ? -24.345 -41.279 -9.170  1.00 56.21 ? 140 PHE D O   1 
ATOM   7572  C CB  . PHE D 2 140 ? -26.212 -38.818 -9.278  1.00 56.16 ? 140 PHE D CB  1 
ATOM   7573  C CG  . PHE D 2 140 ? -26.890 -37.508 -8.996  1.00 56.33 ? 140 PHE D CG  1 
ATOM   7574  C CD1 . PHE D 2 140 ? -27.974 -37.446 -8.130  1.00 56.16 ? 140 PHE D CD1 1 
ATOM   7575  C CD2 . PHE D 2 140 ? -26.451 -36.338 -9.605  1.00 56.68 ? 140 PHE D CD2 1 
ATOM   7576  C CE1 . PHE D 2 140 ? -28.610 -36.236 -7.868  1.00 56.51 ? 140 PHE D CE1 1 
ATOM   7577  C CE2 . PHE D 2 140 ? -27.080 -35.124 -9.351  1.00 56.71 ? 140 PHE D CE2 1 
ATOM   7578  C CZ  . PHE D 2 140 ? -28.161 -35.073 -8.479  1.00 56.80 ? 140 PHE D CZ  1 
ATOM   7579  N N   . TYR D 2 141 ? -25.424 -41.339 -7.188  1.00 56.47 ? 141 TYR D N   1 
ATOM   7580  C CA  . TYR D 2 141 ? -25.397 -42.796 -7.078  1.00 56.63 ? 141 TYR D CA  1 
ATOM   7581  C C   . TYR D 2 141 ? -26.529 -43.453 -7.876  1.00 56.82 ? 141 TYR D C   1 
ATOM   7582  O O   . TYR D 2 141 ? -26.574 -44.676 -8.009  1.00 57.03 ? 141 TYR D O   1 
ATOM   7583  C CB  . TYR D 2 141 ? -25.443 -43.238 -5.609  1.00 56.45 ? 141 TYR D CB  1 
ATOM   7584  C CG  . TYR D 2 141 ? -24.135 -43.083 -4.856  1.00 56.37 ? 141 TYR D CG  1 
ATOM   7585  C CD1 . TYR D 2 141 ? -22.931 -43.557 -5.390  1.00 56.13 ? 141 TYR D CD1 1 
ATOM   7586  C CD2 . TYR D 2 141 ? -24.104 -42.485 -3.593  1.00 56.40 ? 141 TYR D CD2 1 
ATOM   7587  C CE1 . TYR D 2 141 ? -21.729 -43.424 -4.694  1.00 56.13 ? 141 TYR D CE1 1 
ATOM   7588  C CE2 . TYR D 2 141 ? -22.904 -42.348 -2.886  1.00 56.22 ? 141 TYR D CE2 1 
ATOM   7589  C CZ  . TYR D 2 141 ? -21.724 -42.821 -3.442  1.00 56.27 ? 141 TYR D CZ  1 
ATOM   7590  O OH  . TYR D 2 141 ? -20.541 -42.690 -2.748  1.00 56.28 ? 141 TYR D OH  1 
ATOM   7591  N N   . HIS D 2 142 ? -27.440 -42.634 -8.398  1.00 56.92 ? 142 HIS D N   1 
ATOM   7592  C CA  . HIS D 2 142 ? -28.493 -43.104 -9.287  1.00 57.07 ? 142 HIS D CA  1 
ATOM   7593  C C   . HIS D 2 142 ? -28.481 -42.313 -10.594 1.00 57.34 ? 142 HIS D C   1 
ATOM   7594  O O   . HIS D 2 142 ? -27.629 -41.445 -10.800 1.00 57.36 ? 142 HIS D O   1 
ATOM   7595  C CB  . HIS D 2 142 ? -29.862 -43.020 -8.603  1.00 56.97 ? 142 HIS D CB  1 
ATOM   7596  C CG  . HIS D 2 142 ? -30.356 -41.621 -8.395  1.00 57.26 ? 142 HIS D CG  1 
ATOM   7597  N ND1 . HIS D 2 142 ? -31.229 -41.004 -9.264  1.00 57.63 ? 142 HIS D ND1 1 
ATOM   7598  C CD2 . HIS D 2 142 ? -30.105 -40.723 -7.413  1.00 57.45 ? 142 HIS D CD2 1 
ATOM   7599  C CE1 . HIS D 2 142 ? -31.491 -39.783 -8.830  1.00 57.31 ? 142 HIS D CE1 1 
ATOM   7600  N NE2 . HIS D 2 142 ? -30.823 -39.588 -7.707  1.00 57.45 ? 142 HIS D NE2 1 
ATOM   7601  N N   . LYS D 2 143 ? -29.420 -42.625 -11.479 1.00 57.66 ? 143 LYS D N   1 
ATOM   7602  C CA  . LYS D 2 143 ? -29.545 -41.913 -12.738 1.00 58.07 ? 143 LYS D CA  1 
ATOM   7603  C C   . LYS D 2 143 ? -30.509 -40.747 -12.552 1.00 58.23 ? 143 LYS D C   1 
ATOM   7604  O O   . LYS D 2 143 ? -31.639 -40.933 -12.089 1.00 58.20 ? 143 LYS D O   1 
ATOM   7605  C CB  . LYS D 2 143 ? -30.028 -42.863 -13.842 1.00 58.22 ? 143 LYS D CB  1 
ATOM   7606  C CG  . LYS D 2 143 ? -29.640 -42.452 -15.263 1.00 58.72 ? 143 LYS D CG  1 
ATOM   7607  C CD  . LYS D 2 143 ? -28.149 -42.671 -15.540 1.00 59.61 ? 143 LYS D CD  1 
ATOM   7608  C CE  . LYS D 2 143 ? -27.789 -42.285 -16.976 1.00 59.79 ? 143 LYS D CE  1 
ATOM   7609  N NZ  . LYS D 2 143 ? -26.315 -42.252 -17.197 1.00 59.63 ? 143 LYS D NZ  1 
ATOM   7610  N N   . CYS D 2 144 ? -30.053 -39.546 -12.901 1.00 58.44 ? 144 CYS D N   1 
ATOM   7611  C CA  . CYS D 2 144 ? -30.841 -38.329 -12.707 1.00 58.61 ? 144 CYS D CA  1 
ATOM   7612  C C   . CYS D 2 144 ? -31.025 -37.574 -14.028 1.00 58.74 ? 144 CYS D C   1 
ATOM   7613  O O   . CYS D 2 144 ? -30.110 -36.901 -14.514 1.00 58.76 ? 144 CYS D O   1 
ATOM   7614  C CB  . CYS D 2 144 ? -30.200 -37.449 -11.619 1.00 58.57 ? 144 CYS D CB  1 
ATOM   7615  S SG  . CYS D 2 144 ? -31.092 -35.932 -11.140 1.00 58.65 ? 144 CYS D SG  1 
ATOM   7616  N N   . ASP D 2 145 ? -32.218 -37.713 -14.605 1.00 58.95 ? 145 ASP D N   1 
ATOM   7617  C CA  . ASP D 2 145 ? -32.565 -37.071 -15.877 1.00 59.14 ? 145 ASP D CA  1 
ATOM   7618  C C   . ASP D 2 145 ? -32.816 -35.567 -15.708 1.00 59.21 ? 145 ASP D C   1 
ATOM   7619  O O   . ASP D 2 145 ? -32.845 -35.061 -14.582 1.00 59.22 ? 145 ASP D O   1 
ATOM   7620  C CB  . ASP D 2 145 ? -33.773 -37.767 -16.531 1.00 59.15 ? 145 ASP D CB  1 
ATOM   7621  C CG  . ASP D 2 145 ? -35.050 -37.684 -15.687 1.00 59.31 ? 145 ASP D CG  1 
ATOM   7622  O OD1 . ASP D 2 145 ? -36.135 -37.979 -16.231 1.00 59.69 ? 145 ASP D OD1 1 
ATOM   7623  O OD2 . ASP D 2 145 ? -34.986 -37.337 -14.490 1.00 59.17 ? 145 ASP D OD2 1 
ATOM   7624  N N   . ASN D 2 146 ? -33.001 -34.863 -16.825 1.00 59.11 ? 146 ASN D N   1 
ATOM   7625  C CA  . ASN D 2 146 ? -33.189 -33.409 -16.810 1.00 59.03 ? 146 ASN D CA  1 
ATOM   7626  C C   . ASN D 2 146 ? -34.287 -32.941 -15.851 1.00 58.89 ? 146 ASN D C   1 
ATOM   7627  O O   . ASN D 2 146 ? -34.110 -31.940 -15.150 1.00 58.96 ? 146 ASN D O   1 
ATOM   7628  C CB  . ASN D 2 146 ? -33.434 -32.860 -18.225 1.00 59.01 ? 146 ASN D CB  1 
ATOM   7629  C CG  . ASN D 2 146 ? -32.219 -33.011 -19.145 1.00 59.04 ? 146 ASN D CG  1 
ATOM   7630  O OD1 . ASN D 2 146 ? -32.346 -32.896 -20.362 1.00 59.15 ? 146 ASN D OD1 1 
ATOM   7631  N ND2 . ASN D 2 146 ? -31.046 -33.267 -18.570 1.00 58.96 ? 146 ASN D ND2 1 
ATOM   7632  N N   . GLU D 2 147 ? -35.402 -33.671 -15.811 1.00 58.64 ? 147 GLU D N   1 
ATOM   7633  C CA  . GLU D 2 147 ? -36.509 -33.347 -14.904 1.00 58.50 ? 147 GLU D CA  1 
ATOM   7634  C C   . GLU D 2 147 ? -36.139 -33.569 -13.427 1.00 58.12 ? 147 GLU D C   1 
ATOM   7635  O O   . GLU D 2 147 ? -36.651 -32.877 -12.542 1.00 58.07 ? 147 GLU D O   1 
ATOM   7636  C CB  . GLU D 2 147 ? -37.785 -34.122 -15.276 1.00 58.59 ? 147 GLU D CB  1 
ATOM   7637  C CG  . GLU D 2 147 ? -39.060 -33.558 -14.627 1.00 59.44 ? 147 GLU D CG  1 
ATOM   7638  C CD  . GLU D 2 147 ? -40.353 -34.210 -15.114 1.00 60.60 ? 147 GLU D CD  1 
ATOM   7639  O OE1 . GLU D 2 147 ? -40.324 -35.375 -15.577 1.00 60.56 ? 147 GLU D OE1 1 
ATOM   7640  O OE2 . GLU D 2 147 ? -41.411 -33.547 -15.018 1.00 60.76 ? 147 GLU D OE2 1 
ATOM   7641  N N   . CYS D 2 148 ? -35.253 -34.533 -13.178 1.00 57.70 ? 148 CYS D N   1 
ATOM   7642  C CA  . CYS D 2 148 ? -34.719 -34.799 -11.840 1.00 57.22 ? 148 CYS D CA  1 
ATOM   7643  C C   . CYS D 2 148 ? -33.756 -33.674 -11.423 1.00 56.64 ? 148 CYS D C   1 
ATOM   7644  O O   . CYS D 2 148 ? -33.803 -33.192 -10.289 1.00 56.40 ? 148 CYS D O   1 
ATOM   7645  C CB  . CYS D 2 148 ? -34.048 -36.185 -11.811 1.00 57.35 ? 148 CYS D CB  1 
ATOM   7646  S SG  . CYS D 2 148 ? -32.909 -36.558 -10.446 1.00 58.12 ? 148 CYS D SG  1 
ATOM   7647  N N   . MET D 2 149 ? -32.902 -33.257 -12.360 1.00 55.96 ? 149 MET D N   1 
ATOM   7648  C CA  . MET D 2 149 ? -31.987 -32.131 -12.163 1.00 55.21 ? 149 MET D CA  1 
ATOM   7649  C C   . MET D 2 149 ? -32.752 -30.863 -11.802 1.00 54.81 ? 149 MET D C   1 
ATOM   7650  O O   . MET D 2 149 ? -32.337 -30.109 -10.922 1.00 54.73 ? 149 MET D O   1 
ATOM   7651  C CB  . MET D 2 149 ? -31.159 -31.882 -13.425 1.00 55.04 ? 149 MET D CB  1 
ATOM   7652  C CG  . MET D 2 149 ? -30.209 -33.004 -13.797 1.00 54.61 ? 149 MET D CG  1 
ATOM   7653  S SD  . MET D 2 149 ? -28.778 -33.114 -12.713 1.00 53.90 ? 149 MET D SD  1 
ATOM   7654  C CE  . MET D 2 149 ? -27.695 -34.149 -13.692 1.00 53.30 ? 149 MET D CE  1 
ATOM   7655  N N   . GLU D 2 150 ? -33.874 -30.648 -12.484 1.00 54.30 ? 150 GLU D N   1 
ATOM   7656  C CA  . GLU D 2 150 ? -34.735 -29.494 -12.242 1.00 53.92 ? 150 GLU D CA  1 
ATOM   7657  C C   . GLU D 2 150 ? -35.346 -29.503 -10.834 1.00 53.45 ? 150 GLU D C   1 
ATOM   7658  O O   . GLU D 2 150 ? -35.553 -28.440 -10.248 1.00 53.49 ? 150 GLU D O   1 
ATOM   7659  C CB  . GLU D 2 150 ? -35.828 -29.398 -13.321 1.00 53.99 ? 150 GLU D CB  1 
ATOM   7660  C CG  . GLU D 2 150 ? -36.747 -28.169 -13.225 1.00 54.33 ? 150 GLU D CG  1 
ATOM   7661  C CD  . GLU D 2 150 ? -36.006 -26.840 -13.368 1.00 55.01 ? 150 GLU D CD  1 
ATOM   7662  O OE1 . GLU D 2 150 ? -35.197 -26.693 -14.310 1.00 55.06 ? 150 GLU D OE1 1 
ATOM   7663  O OE2 . GLU D 2 150 ? -36.245 -25.937 -12.538 1.00 55.51 ? 150 GLU D OE2 1 
ATOM   7664  N N   . SER D 2 151 ? -35.624 -30.690 -10.297 1.00 52.76 ? 151 SER D N   1 
ATOM   7665  C CA  . SER D 2 151 ? -36.158 -30.810 -8.935  1.00 52.32 ? 151 SER D CA  1 
ATOM   7666  C C   . SER D 2 151 ? -35.097 -30.490 -7.876  1.00 51.90 ? 151 SER D C   1 
ATOM   7667  O O   . SER D 2 151 ? -35.424 -30.070 -6.760  1.00 51.73 ? 151 SER D O   1 
ATOM   7668  C CB  . SER D 2 151 ? -36.765 -32.200 -8.695  1.00 52.37 ? 151 SER D CB  1 
ATOM   7669  O OG  . SER D 2 151 ? -35.802 -33.227 -8.867  1.00 52.24 ? 151 SER D OG  1 
ATOM   7670  N N   . VAL D 2 152 ? -33.833 -30.695 -8.238  1.00 51.36 ? 152 VAL D N   1 
ATOM   7671  C CA  . VAL D 2 152 ? -32.705 -30.324 -7.389  1.00 51.01 ? 152 VAL D CA  1 
ATOM   7672  C C   . VAL D 2 152 ? -32.605 -28.796 -7.327  1.00 50.79 ? 152 VAL D C   1 
ATOM   7673  O O   . VAL D 2 152 ? -32.498 -28.216 -6.247  1.00 50.62 ? 152 VAL D O   1 
ATOM   7674  C CB  . VAL D 2 152 ? -31.379 -30.950 -7.901  1.00 50.93 ? 152 VAL D CB  1 
ATOM   7675  C CG1 . VAL D 2 152 ? -30.194 -30.499 -7.058  1.00 50.77 ? 152 VAL D CG1 1 
ATOM   7676  C CG2 . VAL D 2 152 ? -31.474 -32.466 -7.909  1.00 50.81 ? 152 VAL D CG2 1 
ATOM   7677  N N   . LYS D 2 153 ? -32.665 -28.160 -8.495  1.00 50.64 ? 153 LYS D N   1 
ATOM   7678  C CA  . LYS D 2 153 ? -32.625 -26.703 -8.612  1.00 50.51 ? 153 LYS D CA  1 
ATOM   7679  C C   . LYS D 2 153 ? -33.903 -26.054 -8.079  1.00 50.73 ? 153 LYS D C   1 
ATOM   7680  O O   . LYS D 2 153 ? -33.862 -24.941 -7.558  1.00 50.91 ? 153 LYS D O   1 
ATOM   7681  C CB  . LYS D 2 153 ? -32.380 -26.292 -10.067 1.00 50.28 ? 153 LYS D CB  1 
ATOM   7682  C CG  . LYS D 2 153 ? -31.094 -26.860 -10.658 1.00 49.32 ? 153 LYS D CG  1 
ATOM   7683  C CD  . LYS D 2 153 ? -31.009 -26.651 -12.163 1.00 48.07 ? 153 LYS D CD  1 
ATOM   7684  C CE  . LYS D 2 153 ? -29.708 -27.211 -12.711 1.00 47.49 ? 153 LYS D CE  1 
ATOM   7685  N NZ  . LYS D 2 153 ? -29.562 -27.042 -14.185 1.00 47.63 ? 153 LYS D NZ  1 
ATOM   7686  N N   . ASN D 2 154 ? -35.025 -26.765 -8.201  1.00 50.89 ? 154 ASN D N   1 
ATOM   7687  C CA  . ASN D 2 154 ? -36.343 -26.289 -7.763  1.00 51.02 ? 154 ASN D CA  1 
ATOM   7688  C C   . ASN D 2 154 ? -36.483 -26.329 -6.236  1.00 50.68 ? 154 ASN D C   1 
ATOM   7689  O O   . ASN D 2 154 ? -37.339 -25.652 -5.662  1.00 50.73 ? 154 ASN D O   1 
ATOM   7690  C CB  . ASN D 2 154 ? -37.443 -27.164 -8.392  1.00 51.23 ? 154 ASN D CB  1 
ATOM   7691  C CG  . ASN D 2 154 ? -38.423 -26.374 -9.261  1.00 52.31 ? 154 ASN D CG  1 
ATOM   7692  O OD1 . ASN D 2 154 ? -38.984 -25.361 -8.835  1.00 53.73 ? 154 ASN D OD1 1 
ATOM   7693  N ND2 . ASN D 2 154 ? -38.650 -26.857 -10.484 1.00 52.59 ? 154 ASN D ND2 1 
ATOM   7694  N N   . GLY D 2 155 ? -35.646 -27.139 -5.589  1.00 50.39 ? 155 GLY D N   1 
ATOM   7695  C CA  . GLY D 2 155 ? -35.752 -27.396 -4.149  1.00 49.77 ? 155 GLY D CA  1 
ATOM   7696  C C   . GLY D 2 155 ? -36.801 -28.445 -3.797  1.00 49.43 ? 155 GLY D C   1 
ATOM   7697  O O   . GLY D 2 155 ? -37.242 -28.525 -2.646  1.00 49.26 ? 155 GLY D O   1 
ATOM   7698  N N   . THR D 2 156 ? -37.196 -29.252 -4.786  1.00 48.94 ? 156 THR D N   1 
ATOM   7699  C CA  . THR D 2 156 ? -38.255 -30.256 -4.606  1.00 48.64 ? 156 THR D CA  1 
ATOM   7700  C C   . THR D 2 156 ? -37.794 -31.689 -4.911  1.00 48.40 ? 156 THR D C   1 
ATOM   7701  O O   . THR D 2 156 ? -38.618 -32.556 -5.206  1.00 48.31 ? 156 THR D O   1 
ATOM   7702  C CB  . THR D 2 156 ? -39.511 -29.940 -5.468  1.00 48.63 ? 156 THR D CB  1 
ATOM   7703  O OG1 . THR D 2 156 ? -39.168 -29.977 -6.860  1.00 48.70 ? 156 THR D OG1 1 
ATOM   7704  C CG2 . THR D 2 156 ? -40.095 -28.578 -5.118  1.00 48.61 ? 156 THR D CG2 1 
ATOM   7705  N N   . TYR D 2 157 ? -36.482 -31.923 -4.835  1.00 48.14 ? 157 TYR D N   1 
ATOM   7706  C CA  . TYR D 2 157 ? -35.879 -33.240 -5.072  1.00 47.71 ? 157 TYR D CA  1 
ATOM   7707  C C   . TYR D 2 157 ? -36.461 -34.302 -4.143  1.00 47.56 ? 157 TYR D C   1 
ATOM   7708  O O   . TYR D 2 157 ? -36.531 -34.109 -2.926  1.00 47.46 ? 157 TYR D O   1 
ATOM   7709  C CB  . TYR D 2 157 ? -34.358 -33.159 -4.906  1.00 47.74 ? 157 TYR D CB  1 
ATOM   7710  C CG  . TYR D 2 157 ? -33.623 -34.483 -4.977  1.00 47.47 ? 157 TYR D CG  1 
ATOM   7711  C CD1 . TYR D 2 157 ? -33.442 -35.141 -6.193  1.00 47.24 ? 157 TYR D CD1 1 
ATOM   7712  C CD2 . TYR D 2 157 ? -33.084 -35.064 -3.827  1.00 46.90 ? 157 TYR D CD2 1 
ATOM   7713  C CE1 . TYR D 2 157 ? -32.758 -36.354 -6.260  1.00 47.10 ? 157 TYR D CE1 1 
ATOM   7714  C CE2 . TYR D 2 157 ? -32.396 -36.274 -3.883  1.00 46.73 ? 157 TYR D CE2 1 
ATOM   7715  C CZ  . TYR D 2 157 ? -32.236 -36.915 -5.102  1.00 46.87 ? 157 TYR D CZ  1 
ATOM   7716  O OH  . TYR D 2 157 ? -31.553 -38.114 -5.170  1.00 46.39 ? 157 TYR D OH  1 
ATOM   7717  N N   . ASP D 2 158 ? -36.879 -35.419 -4.733  1.00 47.32 ? 158 ASP D N   1 
ATOM   7718  C CA  . ASP D 2 158 ? -37.569 -36.476 -3.999  1.00 47.20 ? 158 ASP D CA  1 
ATOM   7719  C C   . ASP D 2 158 ? -36.568 -37.522 -3.494  1.00 46.65 ? 158 ASP D C   1 
ATOM   7720  O O   . ASP D 2 158 ? -36.282 -38.503 -4.187  1.00 46.59 ? 158 ASP D O   1 
ATOM   7721  C CB  . ASP D 2 158 ? -38.633 -37.120 -4.899  1.00 47.52 ? 158 ASP D CB  1 
ATOM   7722  C CG  . ASP D 2 158 ? -39.836 -37.645 -4.124  1.00 48.59 ? 158 ASP D CG  1 
ATOM   7723  O OD1 . ASP D 2 158 ? -39.742 -37.844 -2.890  1.00 49.72 ? 158 ASP D OD1 1 
ATOM   7724  O OD2 . ASP D 2 158 ? -40.887 -37.866 -4.765  1.00 49.83 ? 158 ASP D OD2 1 
ATOM   7725  N N   . TYR D 2 159 ? -36.033 -37.298 -2.292  1.00 45.95 ? 159 TYR D N   1 
ATOM   7726  C CA  . TYR D 2 159 ? -35.026 -38.193 -1.710  1.00 45.26 ? 159 TYR D CA  1 
ATOM   7727  C C   . TYR D 2 159 ? -35.537 -39.623 -1.480  1.00 45.16 ? 159 TYR D C   1 
ATOM   7728  O O   . TYR D 2 159 ? -34.869 -40.576 -1.891  1.00 44.79 ? 159 TYR D O   1 
ATOM   7729  C CB  . TYR D 2 159 ? -34.428 -37.625 -0.414  1.00 44.97 ? 159 TYR D CB  1 
ATOM   7730  C CG  . TYR D 2 159 ? -33.497 -38.595 0.295   1.00 44.09 ? 159 TYR D CG  1 
ATOM   7731  C CD1 . TYR D 2 159 ? -32.144 -38.652 -0.030  1.00 43.63 ? 159 TYR D CD1 1 
ATOM   7732  C CD2 . TYR D 2 159 ? -33.975 -39.469 1.276   1.00 43.09 ? 159 TYR D CD2 1 
ATOM   7733  C CE1 . TYR D 2 159 ? -31.285 -39.543 0.608   1.00 42.82 ? 159 TYR D CE1 1 
ATOM   7734  C CE2 . TYR D 2 159 ? -33.126 -40.367 1.915   1.00 42.46 ? 159 TYR D CE2 1 
ATOM   7735  C CZ  . TYR D 2 159 ? -31.781 -40.395 1.575   1.00 42.51 ? 159 TYR D CZ  1 
ATOM   7736  O OH  . TYR D 2 159 ? -30.928 -41.272 2.198   1.00 41.17 ? 159 TYR D OH  1 
ATOM   7737  N N   . PRO D 2 160 ? -36.702 -39.778 -0.808  1.00 45.16 ? 160 PRO D N   1 
ATOM   7738  C CA  . PRO D 2 160 ? -37.225 -41.125 -0.573  1.00 45.36 ? 160 PRO D CA  1 
ATOM   7739  C C   . PRO D 2 160 ? -37.444 -41.933 -1.854  1.00 45.54 ? 160 PRO D C   1 
ATOM   7740  O O   . PRO D 2 160 ? -37.266 -43.153 -1.832  1.00 45.39 ? 160 PRO D O   1 
ATOM   7741  C CB  . PRO D 2 160 ? -38.555 -40.861 0.140   1.00 45.32 ? 160 PRO D CB  1 
ATOM   7742  C CG  . PRO D 2 160 ? -38.331 -39.582 0.851   1.00 44.97 ? 160 PRO D CG  1 
ATOM   7743  C CD  . PRO D 2 160 ? -37.516 -38.763 -0.107  1.00 45.09 ? 160 PRO D CD  1 
ATOM   7744  N N   . GLN D 2 161 ? -37.799 -41.256 -2.950  1.00 45.80 ? 161 GLN D N   1 
ATOM   7745  C CA  . GLN D 2 161 ? -38.018 -41.910 -4.252  1.00 46.11 ? 161 GLN D CA  1 
ATOM   7746  C C   . GLN D 2 161 ? -36.775 -42.613 -4.818  1.00 46.10 ? 161 GLN D C   1 
ATOM   7747  O O   . GLN D 2 161 ? -36.895 -43.662 -5.452  1.00 46.29 ? 161 GLN D O   1 
ATOM   7748  C CB  . GLN D 2 161 ? -38.603 -40.922 -5.279  1.00 46.22 ? 161 GLN D CB  1 
ATOM   7749  C CG  . GLN D 2 161 ? -38.968 -41.517 -6.656  1.00 47.19 ? 161 GLN D CG  1 
ATOM   7750  C CD  . GLN D 2 161 ? -40.052 -42.604 -6.594  1.00 48.79 ? 161 GLN D CD  1 
ATOM   7751  O OE1 . GLN D 2 161 ? -39.771 -43.771 -6.300  1.00 48.76 ? 161 GLN D OE1 1 
ATOM   7752  N NE2 . GLN D 2 161 ? -41.293 -42.220 -6.892  1.00 48.92 ? 161 GLN D NE2 1 
ATOM   7753  N N   . TYR D 2 162 ? -35.592 -42.048 -4.581  1.00 46.07 ? 162 TYR D N   1 
ATOM   7754  C CA  . TYR D 2 162 ? -34.354 -42.619 -5.124  1.00 46.26 ? 162 TYR D CA  1 
ATOM   7755  C C   . TYR D 2 162 ? -33.451 -43.310 -4.092  1.00 46.12 ? 162 TYR D C   1 
ATOM   7756  O O   . TYR D 2 162 ? -32.418 -43.864 -4.463  1.00 46.09 ? 162 TYR D O   1 
ATOM   7757  C CB  . TYR D 2 162 ? -33.539 -41.551 -5.872  1.00 46.32 ? 162 TYR D CB  1 
ATOM   7758  C CG  . TYR D 2 162 ? -34.282 -40.841 -6.980  1.00 47.29 ? 162 TYR D CG  1 
ATOM   7759  C CD1 . TYR D 2 162 ? -34.431 -41.425 -8.243  1.00 48.02 ? 162 TYR D CD1 1 
ATOM   7760  C CD2 . TYR D 2 162 ? -34.828 -39.576 -6.772  1.00 47.82 ? 162 TYR D CD2 1 
ATOM   7761  C CE1 . TYR D 2 162 ? -35.112 -40.763 -9.266  1.00 48.03 ? 162 TYR D CE1 1 
ATOM   7762  C CE2 . TYR D 2 162 ? -35.512 -38.910 -7.781  1.00 48.16 ? 162 TYR D CE2 1 
ATOM   7763  C CZ  . TYR D 2 162 ? -35.651 -39.504 -9.024  1.00 48.28 ? 162 TYR D CZ  1 
ATOM   7764  O OH  . TYR D 2 162 ? -36.328 -38.831 -10.017 1.00 48.14 ? 162 TYR D OH  1 
ATOM   7765  N N   . SER D 2 163 ? -33.833 -43.281 -2.816  1.00 46.29 ? 163 SER D N   1 
ATOM   7766  C CA  . SER D 2 163 ? -32.954 -43.749 -1.729  1.00 46.59 ? 163 SER D CA  1 
ATOM   7767  C C   . SER D 2 163 ? -32.608 -45.245 -1.771  1.00 46.85 ? 163 SER D C   1 
ATOM   7768  O O   . SER D 2 163 ? -31.469 -45.630 -1.485  1.00 46.69 ? 163 SER D O   1 
ATOM   7769  C CB  . SER D 2 163 ? -33.510 -43.361 -0.352  1.00 46.51 ? 163 SER D CB  1 
ATOM   7770  O OG  . SER D 2 163 ? -34.635 -44.145 0.003   1.00 46.46 ? 163 SER D OG  1 
ATOM   7771  N N   . GLU D 2 164 ? -33.589 -46.074 -2.129  1.00 47.24 ? 164 GLU D N   1 
ATOM   7772  C CA  . GLU D 2 164 ? -33.393 -47.526 -2.223  1.00 47.67 ? 164 GLU D CA  1 
ATOM   7773  C C   . GLU D 2 164 ? -32.438 -47.875 -3.368  1.00 47.82 ? 164 GLU D C   1 
ATOM   7774  O O   . GLU D 2 164 ? -31.516 -48.674 -3.193  1.00 47.72 ? 164 GLU D O   1 
ATOM   7775  C CB  . GLU D 2 164 ? -34.734 -48.253 -2.392  1.00 47.68 ? 164 GLU D CB  1 
ATOM   7776  C CG  . GLU D 2 164 ? -35.789 -47.909 -1.343  1.00 48.38 ? 164 GLU D CG  1 
ATOM   7777  C CD  . GLU D 2 164 ? -35.937 -48.960 -0.250  1.00 49.36 ? 164 GLU D CD  1 
ATOM   7778  O OE1 . GLU D 2 164 ? -36.031 -48.569 0.933   1.00 49.85 ? 164 GLU D OE1 1 
ATOM   7779  O OE2 . GLU D 2 164 ? -35.980 -50.173 -0.566  1.00 49.57 ? 164 GLU D OE2 1 
ATOM   7780  N N   . GLU D 2 165 ? -32.659 -47.258 -4.527  1.00 48.33 ? 165 GLU D N   1 
ATOM   7781  C CA  . GLU D 2 165 ? -31.786 -47.417 -5.691  1.00 48.90 ? 165 GLU D CA  1 
ATOM   7782  C C   . GLU D 2 165 ? -30.363 -46.940 -5.377  1.00 49.23 ? 165 GLU D C   1 
ATOM   7783  O O   . GLU D 2 165 ? -29.383 -47.566 -5.788  1.00 49.12 ? 165 GLU D O   1 
ATOM   7784  C CB  . GLU D 2 165 ? -32.367 -46.656 -6.890  1.00 48.94 ? 165 GLU D CB  1 
ATOM   7785  C CG  . GLU D 2 165 ? -31.590 -46.798 -8.203  1.00 49.45 ? 165 GLU D CG  1 
ATOM   7786  C CD  . GLU D 2 165 ? -32.185 -45.970 -9.344  1.00 50.82 ? 165 GLU D CD  1 
ATOM   7787  O OE1 . GLU D 2 165 ? -33.312 -45.439 -9.190  1.00 50.56 ? 165 GLU D OE1 1 
ATOM   7788  O OE2 . GLU D 2 165 ? -31.521 -45.853 -10.403 1.00 50.85 ? 165 GLU D OE2 1 
ATOM   7789  N N   . ALA D 2 166 ? -30.259 -45.838 -4.639  1.00 49.83 ? 166 ALA D N   1 
ATOM   7790  C CA  . ALA D 2 166 ? -28.963 -45.297 -4.243  1.00 50.57 ? 166 ALA D CA  1 
ATOM   7791  C C   . ALA D 2 166 ? -28.246 -46.199 -3.233  1.00 51.04 ? 166 ALA D C   1 
ATOM   7792  O O   . ALA D 2 166 ? -27.033 -46.378 -3.320  1.00 50.88 ? 166 ALA D O   1 
ATOM   7793  C CB  . ALA D 2 166 ? -29.117 -43.881 -3.698  1.00 50.53 ? 166 ALA D CB  1 
ATOM   7794  N N   . ARG D 2 167 ? -29.009 -46.765 -2.296  1.00 51.88 ? 167 ARG D N   1 
ATOM   7795  C CA  . ARG D 2 167 ? -28.494 -47.672 -1.259  1.00 52.78 ? 167 ARG D CA  1 
ATOM   7796  C C   . ARG D 2 167 ? -27.777 -48.884 -1.862  1.00 53.12 ? 167 ARG D C   1 
ATOM   7797  O O   . ARG D 2 167 ? -26.664 -49.215 -1.457  1.00 53.13 ? 167 ARG D O   1 
ATOM   7798  C CB  . ARG D 2 167 ? -29.643 -48.122 -0.335  1.00 52.99 ? 167 ARG D CB  1 
ATOM   7799  C CG  . ARG D 2 167 ? -29.257 -48.979 0.886   1.00 54.08 ? 167 ARG D CG  1 
ATOM   7800  C CD  . ARG D 2 167 ? -28.632 -48.138 1.997   1.00 57.09 ? 167 ARG D CD  1 
ATOM   7801  N NE  . ARG D 2 167 ? -28.563 -48.829 3.291   1.00 58.79 ? 167 ARG D NE  1 
ATOM   7802  C CZ  . ARG D 2 167 ? -27.576 -48.676 4.177   1.00 59.40 ? 167 ARG D CZ  1 
ATOM   7803  N NH1 . ARG D 2 167 ? -26.551 -47.874 3.915   1.00 59.51 ? 167 ARG D NH1 1 
ATOM   7804  N NH2 . ARG D 2 167 ? -27.602 -49.342 5.325   1.00 59.73 ? 167 ARG D NH2 1 
ATOM   7805  N N   . LEU D 2 168 ? -28.418 -49.522 -2.839  1.00 53.72 ? 168 LEU D N   1 
ATOM   7806  C CA  . LEU D 2 168 ? -27.885 -50.723 -3.490  1.00 54.35 ? 168 LEU D CA  1 
ATOM   7807  C C   . LEU D 2 168 ? -26.653 -50.458 -4.359  1.00 54.84 ? 168 LEU D C   1 
ATOM   7808  O O   . LEU D 2 168 ? -25.651 -51.171 -4.251  1.00 54.88 ? 168 LEU D O   1 
ATOM   7809  C CB  . LEU D 2 168 ? -28.984 -51.418 -4.307  1.00 54.28 ? 168 LEU D CB  1 
ATOM   7810  C CG  . LEU D 2 168 ? -29.851 -52.524 -3.680  1.00 54.42 ? 168 LEU D CG  1 
ATOM   7811  C CD1 . LEU D 2 168 ? -30.024 -52.417 -2.159  1.00 54.24 ? 168 LEU D CD1 1 
ATOM   7812  C CD2 . LEU D 2 168 ? -31.212 -52.558 -4.375  1.00 54.53 ? 168 LEU D CD2 1 
ATOM   7813  N N   . ASN D 2 169 ? -26.734 -49.441 -5.218  1.00 55.51 ? 169 ASN D N   1 
ATOM   7814  C CA  . ASN D 2 169 ? -25.602 -49.030 -6.053  1.00 56.23 ? 169 ASN D CA  1 
ATOM   7815  C C   . ASN D 2 169 ? -24.374 -48.652 -5.223  1.00 56.84 ? 169 ASN D C   1 
ATOM   7816  O O   . ASN D 2 169 ? -23.244 -48.958 -5.602  1.00 56.90 ? 169 ASN D O   1 
ATOM   7817  C CB  . ASN D 2 169 ? -26.000 -47.866 -6.970  1.00 56.15 ? 169 ASN D CB  1 
ATOM   7818  C CG  . ASN D 2 169 ? -26.899 -48.298 -8.125  1.00 56.09 ? 169 ASN D CG  1 
ATOM   7819  O OD1 . ASN D 2 169 ? -26.892 -49.457 -8.541  1.00 55.91 ? 169 ASN D OD1 1 
ATOM   7820  N ND2 . ASN D 2 169 ? -27.667 -47.355 -8.655  1.00 55.90 ? 169 ASN D ND2 1 
ATOM   7821  N N   . ARG D 2 170 ? -24.618 -47.996 -4.089  1.00 57.66 ? 170 ARG D N   1 
ATOM   7822  C CA  . ARG D 2 170 ? -23.574 -47.576 -3.154  1.00 58.54 ? 170 ARG D CA  1 
ATOM   7823  C C   . ARG D 2 170 ? -22.890 -48.776 -2.498  1.00 59.22 ? 170 ARG D C   1 
ATOM   7824  O O   . ARG D 2 170 ? -21.658 -48.837 -2.443  1.00 59.38 ? 170 ARG D O   1 
ATOM   7825  C CB  . ARG D 2 170 ? -24.179 -46.664 -2.081  1.00 58.42 ? 170 ARG D CB  1 
ATOM   7826  C CG  . ARG D 2 170 ? -23.186 -45.962 -1.156  1.00 58.52 ? 170 ARG D CG  1 
ATOM   7827  C CD  . ARG D 2 170 ? -23.870 -45.523 0.136   1.00 57.78 ? 170 ARG D CD  1 
ATOM   7828  N NE  . ARG D 2 170 ? -25.156 -44.886 -0.134  1.00 57.82 ? 170 ARG D NE  1 
ATOM   7829  C CZ  . ARG D 2 170 ? -26.222 -44.956 0.660   1.00 58.19 ? 170 ARG D CZ  1 
ATOM   7830  N NH1 . ARG D 2 170 ? -26.178 -45.639 1.794   1.00 58.12 ? 170 ARG D NH1 1 
ATOM   7831  N NH2 . ARG D 2 170 ? -27.346 -44.345 0.310   1.00 58.85 ? 170 ARG D NH2 1 
ATOM   7832  N N   . GLU D 2 171 ? -23.699 -49.721 -2.012  1.00 60.01 ? 171 GLU D N   1 
ATOM   7833  C CA  . GLU D 2 171 ? -23.219 -50.917 -1.301  1.00 60.76 ? 171 GLU D CA  1 
ATOM   7834  C C   . GLU D 2 171 ? -22.238 -51.790 -2.095  1.00 61.15 ? 171 GLU D C   1 
ATOM   7835  O O   . GLU D 2 171 ? -21.485 -52.566 -1.502  1.00 61.26 ? 171 GLU D O   1 
ATOM   7836  C CB  . GLU D 2 171 ? -24.399 -51.773 -0.827  1.00 60.76 ? 171 GLU D CB  1 
ATOM   7837  C CG  . GLU D 2 171 ? -25.070 -51.276 0.451   1.00 61.53 ? 171 GLU D CG  1 
ATOM   7838  C CD  . GLU D 2 171 ? -26.299 -52.097 0.846   1.00 62.60 ? 171 GLU D CD  1 
ATOM   7839  O OE1 . GLU D 2 171 ? -26.829 -52.860 0.005   1.00 62.47 ? 171 GLU D OE1 1 
ATOM   7840  O OE2 . GLU D 2 171 ? -26.742 -51.971 2.009   1.00 63.26 ? 171 GLU D OE2 1 
ATOM   7841  N N   . GLU D 2 172 ? -22.251 -51.662 -3.422  1.00 61.62 ? 172 GLU D N   1 
ATOM   7842  C CA  . GLU D 2 172 ? -21.368 -52.444 -4.291  1.00 62.09 ? 172 GLU D CA  1 
ATOM   7843  C C   . GLU D 2 172 ? -19.893 -52.042 -4.136  1.00 62.15 ? 172 GLU D C   1 
ATOM   7844  O O   . GLU D 2 172 ? -19.398 -51.128 -4.804  1.00 62.30 ? 172 GLU D O   1 
ATOM   7845  C CB  . GLU D 2 172 ? -21.818 -52.333 -5.751  1.00 62.19 ? 172 GLU D CB  1 
ATOM   7846  C CG  . GLU D 2 172 ? -21.153 -53.336 -6.688  1.00 63.06 ? 172 GLU D CG  1 
ATOM   7847  C CD  . GLU D 2 172 ? -21.494 -53.098 -8.150  1.00 64.09 ? 172 GLU D CD  1 
ATOM   7848  O OE1 . GLU D 2 172 ? -22.569 -52.525 -8.436  1.00 64.50 ? 172 GLU D OE1 1 
ATOM   7849  O OE2 . GLU D 2 172 ? -20.683 -53.489 -9.019  1.00 64.56 ? 172 GLU D OE2 1 
ATOM   7850  N N   . PRO E 1 7   ? -38.616 -46.412 16.722  1.00 52.99 ? 9   PRO E N   1 
ATOM   7851  C CA  . PRO E 1 7   ? -37.630 -46.318 15.640  1.00 52.84 ? 9   PRO E CA  1 
ATOM   7852  C C   . PRO E 1 7   ? -37.712 -44.982 14.885  1.00 52.62 ? 9   PRO E C   1 
ATOM   7853  O O   . PRO E 1 7   ? -36.874 -44.703 14.019  1.00 52.54 ? 9   PRO E O   1 
ATOM   7854  C CB  . PRO E 1 7   ? -38.005 -47.487 14.714  1.00 52.93 ? 9   PRO E CB  1 
ATOM   7855  C CG  . PRO E 1 7   ? -38.914 -48.377 15.531  1.00 53.19 ? 9   PRO E CG  1 
ATOM   7856  C CD  . PRO E 1 7   ? -39.631 -47.446 16.460  1.00 53.16 ? 9   PRO E CD  1 
ATOM   7857  N N   . GLY E 1 8   ? -38.721 -44.177 15.218  1.00 52.28 ? 10  GLY E N   1 
ATOM   7858  C CA  . GLY E 1 8   ? -38.901 -42.847 14.638  1.00 51.69 ? 10  GLY E CA  1 
ATOM   7859  C C   . GLY E 1 8   ? -38.737 -41.751 15.680  1.00 51.26 ? 10  GLY E C   1 
ATOM   7860  O O   . GLY E 1 8   ? -39.543 -40.816 15.744  1.00 51.21 ? 10  GLY E O   1 
ATOM   7861  N N   . ASP E 1 9   ? -37.696 -41.876 16.500  1.00 50.54 ? 11  ASP E N   1 
ATOM   7862  C CA  . ASP E 1 9   ? -37.384 -40.881 17.526  1.00 50.00 ? 11  ASP E CA  1 
ATOM   7863  C C   . ASP E 1 9   ? -36.572 -39.728 16.938  1.00 49.38 ? 11  ASP E C   1 
ATOM   7864  O O   . ASP E 1 9   ? -35.538 -39.945 16.295  1.00 49.20 ? 11  ASP E O   1 
ATOM   7865  C CB  . ASP E 1 9   ? -36.631 -41.526 18.698  1.00 50.08 ? 11  ASP E CB  1 
ATOM   7866  C CG  . ASP E 1 9   ? -37.536 -42.362 19.599  1.00 50.50 ? 11  ASP E CG  1 
ATOM   7867  O OD1 . ASP E 1 9   ? -38.735 -42.544 19.278  1.00 50.25 ? 11  ASP E OD1 1 
ATOM   7868  O OD2 . ASP E 1 9   ? -37.039 -42.838 20.643  1.00 51.34 ? 11  ASP E OD2 1 
ATOM   7869  N N   . GLN E 1 10  ? -37.045 -38.503 17.155  1.00 48.62 ? 12  GLN E N   1 
ATOM   7870  C CA  . GLN E 1 10  ? -36.384 -37.333 16.577  1.00 47.88 ? 12  GLN E CA  1 
ATOM   7871  C C   . GLN E 1 10  ? -36.308 -36.103 17.479  1.00 47.19 ? 12  GLN E C   1 
ATOM   7872  O O   . GLN E 1 10  ? -37.219 -35.818 18.260  1.00 46.88 ? 12  GLN E O   1 
ATOM   7873  C CB  . GLN E 1 10  ? -36.992 -36.969 15.213  1.00 48.01 ? 12  GLN E CB  1 
ATOM   7874  C CG  . GLN E 1 10  ? -38.464 -36.567 15.225  1.00 48.30 ? 12  GLN E CG  1 
ATOM   7875  C CD  . GLN E 1 10  ? -38.861 -35.781 13.982  1.00 48.67 ? 12  GLN E CD  1 
ATOM   7876  O OE1 . GLN E 1 10  ? -38.257 -35.933 12.915  1.00 48.32 ? 12  GLN E OE1 1 
ATOM   7877  N NE2 . GLN E 1 10  ? -39.882 -34.935 14.117  1.00 47.90 ? 12  GLN E NE2 1 
ATOM   7878  N N   . ILE E 1 11  ? -35.189 -35.395 17.359  1.00 46.50 ? 13  ILE E N   1 
ATOM   7879  C CA  . ILE E 1 11  ? -35.011 -34.078 17.955  1.00 45.73 ? 13  ILE E CA  1 
ATOM   7880  C C   . ILE E 1 11  ? -34.801 -33.043 16.843  1.00 45.41 ? 13  ILE E C   1 
ATOM   7881  O O   . ILE E 1 11  ? -34.014 -33.258 15.911  1.00 45.20 ? 13  ILE E O   1 
ATOM   7882  C CB  . ILE E 1 11  ? -33.853 -34.052 19.003  1.00 45.74 ? 13  ILE E CB  1 
ATOM   7883  C CG1 . ILE E 1 11  ? -33.900 -32.758 19.826  1.00 45.76 ? 13  ILE E CG1 1 
ATOM   7884  C CG2 . ILE E 1 11  ? -32.482 -34.280 18.341  1.00 45.08 ? 13  ILE E CG2 1 
ATOM   7885  C CD1 . ILE E 1 11  ? -33.086 -32.798 21.107  1.00 46.20 ? 13  ILE E CD1 1 
ATOM   7886  N N   . CYS E 1 12  ? -35.533 -31.937 16.940  1.00 45.00 ? 14  CYS E N   1 
ATOM   7887  C CA  . CYS E 1 12  ? -35.448 -30.861 15.960  1.00 44.79 ? 14  CYS E CA  1 
ATOM   7888  C C   . CYS E 1 12  ? -34.942 -29.573 16.599  1.00 44.23 ? 14  CYS E C   1 
ATOM   7889  O O   . CYS E 1 12  ? -35.224 -29.290 17.763  1.00 44.04 ? 14  CYS E O   1 
ATOM   7890  C CB  . CYS E 1 12  ? -36.809 -30.629 15.297  1.00 44.87 ? 14  CYS E CB  1 
ATOM   7891  S SG  . CYS E 1 12  ? -37.464 -32.080 14.419  1.00 46.25 ? 14  CYS E SG  1 
ATOM   7892  N N   . ILE E 1 13  ? -34.184 -28.801 15.831  1.00 43.70 ? 15  ILE E N   1 
ATOM   7893  C CA  . ILE E 1 13  ? -33.699 -27.508 16.295  1.00 43.12 ? 15  ILE E CA  1 
ATOM   7894  C C   . ILE E 1 13  ? -34.430 -26.417 15.541  1.00 42.72 ? 15  ILE E C   1 
ATOM   7895  O O   . ILE E 1 13  ? -34.552 -26.479 14.319  1.00 42.60 ? 15  ILE E O   1 
ATOM   7896  C CB  . ILE E 1 13  ? -32.168 -27.389 16.142  1.00 43.17 ? 15  ILE E CB  1 
ATOM   7897  C CG1 . ILE E 1 13  ? -31.485 -28.281 17.177  1.00 43.06 ? 15  ILE E CG1 1 
ATOM   7898  C CG2 . ILE E 1 13  ? -31.697 -25.947 16.327  1.00 42.96 ? 15  ILE E CG2 1 
ATOM   7899  C CD1 . ILE E 1 13  ? -30.489 -29.222 16.580  1.00 43.68 ? 15  ILE E CD1 1 
ATOM   7900  N N   . GLY E 1 14  ? -34.935 -25.435 16.283  1.00 42.41 ? 16  GLY E N   1 
ATOM   7901  C CA  . GLY E 1 14  ? -35.695 -24.339 15.695  1.00 41.95 ? 16  GLY E CA  1 
ATOM   7902  C C   . GLY E 1 14  ? -35.615 -23.037 16.466  1.00 41.62 ? 16  GLY E C   1 
ATOM   7903  O O   . GLY E 1 14  ? -34.843 -22.903 17.418  1.00 41.67 ? 16  GLY E O   1 
ATOM   7904  N N   . TYR E 1 15  ? -36.431 -22.076 16.050  1.00 41.26 ? 17  TYR E N   1 
ATOM   7905  C CA  . TYR E 1 15  ? -36.391 -20.734 16.609  1.00 40.92 ? 17  TYR E CA  1 
ATOM   7906  C C   . TYR E 1 15  ? -37.789 -20.162 16.802  1.00 40.98 ? 17  TYR E C   1 
ATOM   7907  O O   . TYR E 1 15  ? -38.746 -20.627 16.183  1.00 40.89 ? 17  TYR E O   1 
ATOM   7908  C CB  . TYR E 1 15  ? -35.527 -19.805 15.740  1.00 40.59 ? 17  TYR E CB  1 
ATOM   7909  C CG  . TYR E 1 15  ? -35.934 -19.743 14.282  1.00 39.89 ? 17  TYR E CG  1 
ATOM   7910  C CD1 . TYR E 1 15  ? -36.814 -18.758 13.820  1.00 39.30 ? 17  TYR E CD1 1 
ATOM   7911  C CD2 . TYR E 1 15  ? -35.431 -20.660 13.360  1.00 38.91 ? 17  TYR E CD2 1 
ATOM   7912  C CE1 . TYR E 1 15  ? -37.187 -18.698 12.477  1.00 38.96 ? 17  TYR E CE1 1 
ATOM   7913  C CE2 . TYR E 1 15  ? -35.801 -20.609 12.022  1.00 39.01 ? 17  TYR E CE2 1 
ATOM   7914  C CZ  . TYR E 1 15  ? -36.677 -19.629 11.585  1.00 39.03 ? 17  TYR E CZ  1 
ATOM   7915  O OH  . TYR E 1 15  ? -37.033 -19.582 10.254  1.00 39.26 ? 17  TYR E OH  1 
ATOM   7916  N N   . HIS E 1 16  ? -37.878 -19.152 17.666  1.00 41.13 ? 18  HIS E N   1 
ATOM   7917  C CA  . HIS E 1 16  ? -39.125 -18.493 18.049  1.00 41.34 ? 18  HIS E CA  1 
ATOM   7918  C C   . HIS E 1 16  ? -39.824 -17.814 16.876  1.00 41.42 ? 18  HIS E C   1 
ATOM   7919  O O   . HIS E 1 16  ? -39.180 -17.326 15.948  1.00 41.53 ? 18  HIS E O   1 
ATOM   7920  C CB  . HIS E 1 16  ? -38.830 -17.465 19.151  1.00 41.53 ? 18  HIS E CB  1 
ATOM   7921  C CG  . HIS E 1 16  ? -40.045 -16.766 19.685  1.00 42.46 ? 18  HIS E CG  1 
ATOM   7922  N ND1 . HIS E 1 16  ? -40.803 -17.275 20.717  1.00 42.93 ? 18  HIS E ND1 1 
ATOM   7923  C CD2 . HIS E 1 16  ? -40.624 -15.591 19.337  1.00 43.08 ? 18  HIS E CD2 1 
ATOM   7924  C CE1 . HIS E 1 16  ? -41.800 -16.447 20.978  1.00 43.51 ? 18  HIS E CE1 1 
ATOM   7925  N NE2 . HIS E 1 16  ? -41.715 -15.418 20.154  1.00 43.41 ? 18  HIS E NE2 1 
ATOM   7926  N N   . ALA E 1 17  ? -41.152 -17.807 16.928  1.00 41.57 ? 19  ALA E N   1 
ATOM   7927  C CA  . ALA E 1 17  ? -41.987 -17.057 16.000  1.00 41.70 ? 19  ALA E CA  1 
ATOM   7928  C C   . ALA E 1 17  ? -43.211 -16.587 16.770  1.00 41.94 ? 19  ALA E C   1 
ATOM   7929  O O   . ALA E 1 17  ? -43.541 -17.167 17.805  1.00 42.07 ? 19  ALA E O   1 
ATOM   7930  C CB  . ALA E 1 17  ? -42.387 -17.921 14.827  1.00 41.73 ? 19  ALA E CB  1 
ATOM   7931  N N   . ASN E 1 18  A -43.868 -15.532 16.286  1.00 42.29 ? 19  ASN E N   1 
ATOM   7932  C CA  . ASN E 1 18  A -45.021 -14.947 16.987  1.00 42.79 ? 19  ASN E CA  1 
ATOM   7933  C C   . ASN E 1 18  A -45.909 -14.057 16.106  1.00 43.11 ? 19  ASN E C   1 
ATOM   7934  O O   . ASN E 1 18  A -45.732 -14.005 14.890  1.00 43.13 ? 19  ASN E O   1 
ATOM   7935  C CB  . ASN E 1 18  A -44.560 -14.177 18.234  1.00 42.69 ? 19  ASN E CB  1 
ATOM   7936  C CG  . ASN E 1 18  A -43.729 -12.948 17.897  1.00 43.04 ? 19  ASN E CG  1 
ATOM   7937  O OD1 . ASN E 1 18  A -43.761 -12.444 16.773  1.00 43.20 ? 19  ASN E OD1 1 
ATOM   7938  N ND2 . ASN E 1 18  A -42.980 -12.458 18.878  1.00 43.41 ? 19  ASN E ND2 1 
ATOM   7939  N N   . ASN E 1 19  ? -46.843 -13.347 16.738  1.00 43.49 ? 20  ASN E N   1 
ATOM   7940  C CA  . ASN E 1 19  ? -47.823 -12.525 16.026  1.00 44.15 ? 20  ASN E CA  1 
ATOM   7941  C C   . ASN E 1 19  ? -47.393 -11.061 15.806  1.00 44.21 ? 20  ASN E C   1 
ATOM   7942  O O   . ASN E 1 19  ? -48.177 -10.246 15.305  1.00 44.41 ? 20  ASN E O   1 
ATOM   7943  C CB  . ASN E 1 19  ? -49.188 -12.580 16.741  1.00 44.34 ? 20  ASN E CB  1 
ATOM   7944  C CG  . ASN E 1 19  ? -49.771 -14.002 16.822  1.00 45.40 ? 20  ASN E CG  1 
ATOM   7945  O OD1 . ASN E 1 19  ? -50.433 -14.359 17.806  1.00 45.90 ? 20  ASN E OD1 1 
ATOM   7946  N ND2 . ASN E 1 19  ? -49.531 -14.811 15.786  1.00 45.57 ? 20  ASN E ND2 1 
ATOM   7947  N N   . SER E 1 20  ? -46.151 -10.737 16.170  1.00 44.09 ? 21  SER E N   1 
ATOM   7948  C CA  . SER E 1 20  ? -45.632 -9.364  16.082  1.00 43.74 ? 21  SER E CA  1 
ATOM   7949  C C   . SER E 1 20  ? -45.661 -8.811  14.656  1.00 43.52 ? 21  SER E C   1 
ATOM   7950  O O   . SER E 1 20  ? -45.380 -9.534  13.694  1.00 43.37 ? 21  SER E O   1 
ATOM   7951  C CB  . SER E 1 20  ? -44.211 -9.287  16.649  1.00 43.70 ? 21  SER E CB  1 
ATOM   7952  O OG  . SER E 1 20  ? -43.615 -8.025  16.398  1.00 43.92 ? 21  SER E OG  1 
ATOM   7953  N N   . THR E 1 21  ? -46.008 -7.528  14.535  1.00 43.07 ? 22  THR E N   1 
ATOM   7954  C CA  . THR E 1 21  ? -46.060 -6.852  13.235  1.00 42.70 ? 22  THR E CA  1 
ATOM   7955  C C   . THR E 1 21  ? -45.019 -5.742  13.101  1.00 42.11 ? 22  THR E C   1 
ATOM   7956  O O   . THR E 1 21  ? -44.960 -5.062  12.077  1.00 41.94 ? 22  THR E O   1 
ATOM   7957  C CB  . THR E 1 21  ? -47.461 -6.265  12.952  1.00 42.92 ? 22  THR E CB  1 
ATOM   7958  O OG1 . THR E 1 21  ? -47.909 -5.516  14.090  1.00 43.19 ? 22  THR E OG1 1 
ATOM   7959  C CG2 . THR E 1 21  ? -48.460 -7.379  12.642  1.00 42.90 ? 22  THR E CG2 1 
ATOM   7960  N N   . GLU E 1 22  ? -44.198 -5.575  14.136  1.00 41.53 ? 23  GLU E N   1 
ATOM   7961  C CA  . GLU E 1 22  ? -43.215 -4.495  14.187  1.00 41.02 ? 23  GLU E CA  1 
ATOM   7962  C C   . GLU E 1 22  ? -42.096 -4.684  13.170  1.00 40.09 ? 23  GLU E C   1 
ATOM   7963  O O   . GLU E 1 22  ? -41.552 -5.779  13.023  1.00 39.98 ? 23  GLU E O   1 
ATOM   7964  C CB  . GLU E 1 22  ? -42.662 -4.335  15.604  1.00 41.43 ? 23  GLU E CB  1 
ATOM   7965  C CG  . GLU E 1 22  ? -43.579 -3.527  16.522  1.00 43.32 ? 23  GLU E CG  1 
ATOM   7966  C CD  . GLU E 1 22  ? -43.135 -3.534  17.980  1.00 46.24 ? 23  GLU E CD  1 
ATOM   7967  O OE1 . GLU E 1 22  ? -42.293 -4.382  18.360  1.00 47.26 ? 23  GLU E OE1 1 
ATOM   7968  O OE2 . GLU E 1 22  ? -43.641 -2.688  18.755  1.00 47.47 ? 23  GLU E OE2 1 
ATOM   7969  N N   . GLN E 1 23  ? -41.774 -3.599  12.467  1.00 39.10 ? 24  GLN E N   1 
ATOM   7970  C CA  . GLN E 1 23  ? -40.879 -3.629  11.310  1.00 37.87 ? 24  GLN E CA  1 
ATOM   7971  C C   . GLN E 1 23  ? -39.618 -2.811  11.532  1.00 36.79 ? 24  GLN E C   1 
ATOM   7972  O O   . GLN E 1 23  ? -39.651 -1.779  12.202  1.00 36.78 ? 24  GLN E O   1 
ATOM   7973  C CB  . GLN E 1 23  ? -41.602 -3.090  10.073  1.00 38.04 ? 24  GLN E CB  1 
ATOM   7974  C CG  . GLN E 1 23  ? -42.524 -4.082  9.387   1.00 38.63 ? 24  GLN E CG  1 
ATOM   7975  C CD  . GLN E 1 23  ? -43.333 -3.453  8.258   1.00 39.40 ? 24  GLN E CD  1 
ATOM   7976  O OE1 . GLN E 1 23  ? -43.606 -2.249  8.263   1.00 39.82 ? 24  GLN E OE1 1 
ATOM   7977  N NE2 . GLN E 1 23  ? -43.731 -4.270  7.292   1.00 39.05 ? 24  GLN E NE2 1 
ATOM   7978  N N   . VAL E 1 24  ? -38.514 -3.276  10.956  1.00 35.50 ? 25  VAL E N   1 
ATOM   7979  C CA  . VAL E 1 24  ? -37.243 -2.552  10.983  1.00 34.39 ? 25  VAL E CA  1 
ATOM   7980  C C   . VAL E 1 24  ? -36.635 -2.494  9.581   1.00 34.15 ? 25  VAL E C   1 
ATOM   7981  O O   . VAL E 1 24  ? -37.064 -3.230  8.691   1.00 33.90 ? 25  VAL E O   1 
ATOM   7982  C CB  . VAL E 1 24  ? -36.220 -3.186  11.970  1.00 34.19 ? 25  VAL E CB  1 
ATOM   7983  C CG1 . VAL E 1 24  ? -36.760 -3.193  13.393  1.00 33.34 ? 25  VAL E CG1 1 
ATOM   7984  C CG2 . VAL E 1 24  ? -35.810 -4.594  11.521  1.00 33.96 ? 25  VAL E CG2 1 
ATOM   7985  N N   . ASP E 1 25  ? -35.646 -1.618  9.389   1.00 33.75 ? 26  ASP E N   1 
ATOM   7986  C CA  . ASP E 1 25  ? -34.894 -1.559  8.129   1.00 33.63 ? 26  ASP E CA  1 
ATOM   7987  C C   . ASP E 1 25  ? -33.451 -2.010  8.327   1.00 33.37 ? 26  ASP E C   1 
ATOM   7988  O O   . ASP E 1 25  ? -32.913 -1.906  9.431   1.00 33.15 ? 26  ASP E O   1 
ATOM   7989  C CB  . ASP E 1 25  ? -34.897 -0.141  7.533   1.00 33.58 ? 26  ASP E CB  1 
ATOM   7990  C CG  . ASP E 1 25  ? -36.297 0.452   7.398   1.00 34.51 ? 26  ASP E CG  1 
ATOM   7991  O OD1 . ASP E 1 25  ? -37.286 -0.304  7.212   1.00 34.48 ? 26  ASP E OD1 1 
ATOM   7992  O OD2 . ASP E 1 25  ? -36.401 1.696   7.473   1.00 35.38 ? 26  ASP E OD2 1 
ATOM   7993  N N   . THR E 1 26  ? -32.842 -2.521  7.255   1.00 33.32 ? 27  THR E N   1 
ATOM   7994  C CA  . THR E 1 26  ? -31.394 -2.766  7.199   1.00 33.32 ? 27  THR E CA  1 
ATOM   7995  C C   . THR E 1 26  ? -30.810 -2.079  5.959   1.00 33.43 ? 27  THR E C   1 
ATOM   7996  O O   . THR E 1 26  ? -31.550 -1.470  5.193   1.00 33.68 ? 27  THR E O   1 
ATOM   7997  C CB  . THR E 1 26  ? -31.038 -4.282  7.213   1.00 33.44 ? 27  THR E CB  1 
ATOM   7998  O OG1 . THR E 1 26  ? -31.557 -4.929  6.039   1.00 33.37 ? 27  THR E OG1 1 
ATOM   7999  C CG2 . THR E 1 26  ? -31.593 -4.963  8.468   1.00 32.87 ? 27  THR E CG2 1 
ATOM   8000  N N   . ILE E 1 27  ? -29.508 -2.194  5.752   1.00 33.57 ? 28  ILE E N   1 
ATOM   8001  C CA  . ILE E 1 27  ? -28.904 -1.640  4.553   1.00 33.51 ? 28  ILE E CA  1 
ATOM   8002  C C   . ILE E 1 27  ? -29.509 -2.304  3.323   1.00 33.48 ? 28  ILE E C   1 
ATOM   8003  O O   . ILE E 1 27  ? -29.844 -1.641  2.348   1.00 33.47 ? 28  ILE E O   1 
ATOM   8004  C CB  . ILE E 1 27  ? -27.387 -1.850  4.540   1.00 33.60 ? 28  ILE E CB  1 
ATOM   8005  C CG1 . ILE E 1 27  ? -26.734 -1.049  5.662   1.00 33.47 ? 28  ILE E CG1 1 
ATOM   8006  C CG2 . ILE E 1 27  ? -26.810 -1.452  3.203   1.00 33.31 ? 28  ILE E CG2 1 
ATOM   8007  C CD1 . ILE E 1 27  ? -26.700 0.415   5.404   1.00 34.09 ? 28  ILE E CD1 1 
ATOM   8008  N N   . MET E 1 28  ? -29.704 -3.617  3.396   1.00 39.12 ? 31  MET E N   1 
ATOM   8009  C CA  . MET E 1 28  ? -30.135 -4.405  2.244   1.00 38.92 ? 31  MET E CA  1 
ATOM   8010  C C   . MET E 1 28  ? -31.637 -4.655  2.086   1.00 38.84 ? 31  MET E C   1 
ATOM   8011  O O   . MET E 1 28  ? -32.082 -5.002  1.002   1.00 38.75 ? 31  MET E O   1 
ATOM   8012  C CB  . MET E 1 28  ? -29.398 -5.743  2.226   1.00 38.97 ? 31  MET E CB  1 
ATOM   8013  C CG  . MET E 1 28  ? -27.973 -5.649  1.745   1.00 38.72 ? 31  MET E CG  1 
ATOM   8014  S SD  . MET E 1 28  ? -27.270 -7.264  1.427   1.00 40.14 ? 31  MET E SD  1 
ATOM   8015  C CE  . MET E 1 28  ? -26.291 -6.923  -0.020  1.00 40.62 ? 31  MET E CE  1 
ATOM   8016  N N   . GLU E 1 29  ? -32.412 -4.492  3.150   1.00 38.82 ? 32  GLU E N   1 
ATOM   8017  C CA  . GLU E 1 29  ? -33.842 -4.785  3.096   1.00 38.95 ? 32  GLU E CA  1 
ATOM   8018  C C   . GLU E 1 29  ? -34.679 -3.814  3.925   1.00 38.81 ? 32  GLU E C   1 
ATOM   8019  O O   . GLU E 1 29  ? -34.271 -3.410  5.006   1.00 38.69 ? 32  GLU E O   1 
ATOM   8020  C CB  . GLU E 1 29  ? -34.093 -6.217  3.564   1.00 39.06 ? 32  GLU E CB  1 
ATOM   8021  C CG  . GLU E 1 29  ? -35.358 -6.845  3.020   1.00 40.23 ? 32  GLU E CG  1 
ATOM   8022  C CD  . GLU E 1 29  ? -35.585 -8.240  3.557   1.00 41.91 ? 32  GLU E CD  1 
ATOM   8023  O OE1 . GLU E 1 29  ? -34.617 -8.847  4.056   1.00 42.54 ? 32  GLU E OE1 1 
ATOM   8024  O OE2 . GLU E 1 29  ? -36.727 -8.730  3.483   1.00 41.87 ? 32  GLU E OE2 1 
ATOM   8025  N N   . LYS E 1 30  ? -35.855 -3.444  3.422   1.00 38.66 ? 33  LYS E N   1 
ATOM   8026  C CA  . LYS E 1 30  ? -36.705 -2.507  4.144   1.00 38.72 ? 33  LYS E CA  1 
ATOM   8027  C C   . LYS E 1 30  ? -37.934 -3.223  4.684   1.00 38.66 ? 33  LYS E C   1 
ATOM   8028  O O   . LYS E 1 30  ? -38.369 -4.232  4.125   1.00 38.70 ? 33  LYS E O   1 
ATOM   8029  C CB  . LYS E 1 30  ? -37.131 -1.348  3.230   1.00 38.81 ? 33  LYS E CB  1 
ATOM   8030  C CG  . LYS E 1 30  ? -35.993 -0.664  2.480   1.00 39.04 ? 33  LYS E CG  1 
ATOM   8031  C CD  . LYS E 1 30  ? -35.074 0.096   3.425   1.00 40.02 ? 33  LYS E CD  1 
ATOM   8032  C CE  . LYS E 1 30  ? -33.707 0.323   2.807   1.00 39.89 ? 33  LYS E CE  1 
ATOM   8033  N NZ  . LYS E 1 30  ? -32.812 1.069   3.733   1.00 39.78 ? 33  LYS E NZ  1 
ATOM   8034  N N   . ASN E 1 31  ? -38.501 -2.700  5.765   1.00 38.61 ? 34  ASN E N   1 
ATOM   8035  C CA  . ASN E 1 31  ? -39.722 -3.259  6.337   1.00 38.68 ? 34  ASN E CA  1 
ATOM   8036  C C   . ASN E 1 31  ? -39.654 -4.765  6.591   1.00 37.86 ? 34  ASN E C   1 
ATOM   8037  O O   . ASN E 1 31  ? -40.464 -5.531  6.070   1.00 37.93 ? 34  ASN E O   1 
ATOM   8038  C CB  . ASN E 1 31  ? -40.925 -2.934  5.448   1.00 39.32 ? 34  ASN E CB  1 
ATOM   8039  C CG  . ASN E 1 31  ? -41.125 -1.443  5.260   1.00 41.18 ? 34  ASN E CG  1 
ATOM   8040  O OD1 . ASN E 1 31  ? -40.908 -0.655  6.181   1.00 47.53 ? 34  ASN E OD1 1 
ATOM   8041  N ND2 . ASN E 1 31  ? -41.540 -1.047  4.063   1.00 42.21 ? 34  ASN E ND2 1 
ATOM   8042  N N   . VAL E 1 32  ? -38.685 -5.178  7.401   1.00 37.01 ? 35  VAL E N   1 
ATOM   8043  C CA  . VAL E 1 32  ? -38.545 -6.572  7.806   1.00 36.08 ? 35  VAL E CA  1 
ATOM   8044  C C   . VAL E 1 32  ? -39.301 -6.773  9.116   1.00 35.79 ? 35  VAL E C   1 
ATOM   8045  O O   . VAL E 1 32  ? -39.037 -6.079  10.103  1.00 35.45 ? 35  VAL E O   1 
ATOM   8046  C CB  . VAL E 1 32  ? -37.054 -6.965  8.015   1.00 36.11 ? 35  VAL E CB  1 
ATOM   8047  C CG1 . VAL E 1 32  ? -36.919 -8.447  8.368   1.00 35.08 ? 35  VAL E CG1 1 
ATOM   8048  C CG2 . VAL E 1 32  ? -36.218 -6.625  6.778   1.00 35.80 ? 35  VAL E CG2 1 
ATOM   8049  N N   . THR E 1 33  A -40.240 -7.719  9.116   1.00 35.26 ? 35  THR E N   1 
ATOM   8050  C CA  . THR E 1 33  A -41.005 -8.051  10.312  1.00 35.01 ? 35  THR E CA  1 
ATOM   8051  C C   . THR E 1 33  A -40.132 -8.844  11.288  1.00 34.92 ? 35  THR E C   1 
ATOM   8052  O O   . THR E 1 33  A -39.415 -9.768  10.890  1.00 34.60 ? 35  THR E O   1 
ATOM   8053  C CB  . THR E 1 33  A -42.295 -8.836  9.967   1.00 35.15 ? 35  THR E CB  1 
ATOM   8054  O OG1 . THR E 1 33  A -43.030 -8.135  8.956   1.00 35.21 ? 35  THR E OG1 1 
ATOM   8055  C CG2 . THR E 1 33  A -43.184 -8.993  11.197  1.00 34.96 ? 35  THR E CG2 1 
ATOM   8056  N N   . VAL E 1 34  ? -40.190 -8.463  12.562  1.00 34.73 ? 36  VAL E N   1 
ATOM   8057  C CA  . VAL E 1 34  ? -39.363 -9.070  13.604  1.00 34.53 ? 36  VAL E CA  1 
ATOM   8058  C C   . VAL E 1 34  ? -40.193 -9.422  14.832  1.00 34.61 ? 36  VAL E C   1 
ATOM   8059  O O   . VAL E 1 34  ? -41.236 -8.818  15.076  1.00 34.53 ? 36  VAL E O   1 
ATOM   8060  C CB  . VAL E 1 34  ? -38.162 -8.161  14.021  1.00 34.60 ? 36  VAL E CB  1 
ATOM   8061  C CG1 . VAL E 1 34  ? -37.122 -8.089  12.912  1.00 34.29 ? 36  VAL E CG1 1 
ATOM   8062  C CG2 . VAL E 1 34  ? -38.629 -6.752  14.451  1.00 34.17 ? 36  VAL E CG2 1 
ATOM   8063  N N   . THR E 1 35  ? -39.710 -10.391 15.604  1.00 34.82 ? 37  THR E N   1 
ATOM   8064  C CA  . THR E 1 35  ? -40.412 -10.877 16.794  1.00 35.08 ? 37  THR E CA  1 
ATOM   8065  C C   . THR E 1 35  ? -40.387 -9.860  17.931  1.00 35.53 ? 37  THR E C   1 
ATOM   8066  O O   . THR E 1 35  ? -41.375 -9.695  18.656  1.00 35.60 ? 37  THR E O   1 
ATOM   8067  C CB  . THR E 1 35  ? -39.818 -12.211 17.297  1.00 35.03 ? 37  THR E CB  1 
ATOM   8068  O OG1 . THR E 1 35  ? -38.408 -12.065 17.501  1.00 34.25 ? 37  THR E OG1 1 
ATOM   8069  C CG2 . THR E 1 35  ? -40.067 -13.326 16.287  1.00 34.94 ? 37  THR E CG2 1 
ATOM   8070  N N   . HIS E 1 36  ? -39.253 -9.180  18.082  1.00 35.85 ? 38  HIS E N   1 
ATOM   8071  C CA  . HIS E 1 36  ? -39.105 -8.151  19.107  1.00 36.32 ? 38  HIS E CA  1 
ATOM   8072  C C   . HIS E 1 36  ? -38.329 -6.961  18.569  1.00 36.30 ? 38  HIS E C   1 
ATOM   8073  O O   . HIS E 1 36  ? -37.441 -7.116  17.728  1.00 36.35 ? 38  HIS E O   1 
ATOM   8074  C CB  . HIS E 1 36  ? -38.427 -8.720  20.359  1.00 36.51 ? 38  HIS E CB  1 
ATOM   8075  C CG  . HIS E 1 36  ? -39.138 -9.901  20.943  1.00 37.37 ? 38  HIS E CG  1 
ATOM   8076  N ND1 . HIS E 1 36  ? -38.828 -11.200 20.600  1.00 38.06 ? 38  HIS E ND1 1 
ATOM   8077  C CD2 . HIS E 1 36  ? -40.159 -9.980  21.830  1.00 37.96 ? 38  HIS E CD2 1 
ATOM   8078  C CE1 . HIS E 1 36  ? -39.616 -12.028 21.264  1.00 38.14 ? 38  HIS E CE1 1 
ATOM   8079  N NE2 . HIS E 1 36  ? -40.434 -11.314 22.015  1.00 37.81 ? 38  HIS E NE2 1 
ATOM   8080  N N   . ALA E 1 37  ? -38.676 -5.776  19.060  1.00 36.29 ? 39  ALA E N   1 
ATOM   8081  C CA  . ALA E 1 37  ? -38.086 -4.531  18.582  1.00 36.35 ? 39  ALA E CA  1 
ATOM   8082  C C   . ALA E 1 37  ? -38.158 -3.459  19.654  1.00 36.50 ? 39  ALA E C   1 
ATOM   8083  O O   . ALA E 1 37  ? -39.032 -3.489  20.521  1.00 36.39 ? 39  ALA E O   1 
ATOM   8084  C CB  . ALA E 1 37  ? -38.790 -4.055  17.317  1.00 36.09 ? 39  ALA E CB  1 
ATOM   8085  N N   . GLN E 1 38  ? -37.233 -2.508  19.585  1.00 36.67 ? 40  GLN E N   1 
ATOM   8086  C CA  . GLN E 1 38  ? -37.247 -1.374  20.490  1.00 36.91 ? 40  GLN E CA  1 
ATOM   8087  C C   . GLN E 1 38  ? -37.278 -0.056  19.711  1.00 37.00 ? 40  GLN E C   1 
ATOM   8088  O O   . GLN E 1 38  ? -36.325 0.293   19.001  1.00 37.02 ? 40  GLN E O   1 
ATOM   8089  C CB  . GLN E 1 38  ? -36.048 -1.429  21.443  1.00 36.80 ? 40  GLN E CB  1 
ATOM   8090  C CG  . GLN E 1 38  ? -36.180 -0.529  22.668  1.00 36.98 ? 40  GLN E CG  1 
ATOM   8091  C CD  . GLN E 1 38  ? -35.044 -0.714  23.660  1.00 37.74 ? 40  GLN E CD  1 
ATOM   8092  O OE1 . GLN E 1 38  ? -34.634 -1.840  23.958  1.00 38.55 ? 40  GLN E OE1 1 
ATOM   8093  N NE2 . GLN E 1 38  ? -34.530 0.392   24.179  1.00 37.69 ? 40  GLN E NE2 1 
ATOM   8094  N N   . ASP E 1 39  ? -38.394 0.654   19.828  1.00 36.92 ? 41  ASP E N   1 
ATOM   8095  C CA  . ASP E 1 39  ? -38.481 2.022   19.344  1.00 36.97 ? 41  ASP E CA  1 
ATOM   8096  C C   . ASP E 1 39  ? -37.661 2.890   20.304  1.00 36.85 ? 41  ASP E C   1 
ATOM   8097  O O   . ASP E 1 39  ? -37.868 2.836   21.520  1.00 36.86 ? 41  ASP E O   1 
ATOM   8098  C CB  . ASP E 1 39  ? -39.948 2.478   19.287  1.00 36.93 ? 41  ASP E CB  1 
ATOM   8099  C CG  . ASP E 1 39  ? -40.124 3.869   18.676  1.00 37.41 ? 41  ASP E CG  1 
ATOM   8100  O OD1 . ASP E 1 39  ? -39.138 4.453   18.171  1.00 38.91 ? 41  ASP E OD1 1 
ATOM   8101  O OD2 . ASP E 1 39  ? -41.262 4.383   18.699  1.00 36.77 ? 41  ASP E OD2 1 
ATOM   8102  N N   . ILE E 1 40  ? -36.718 3.657   19.755  1.00 36.72 ? 42  ILE E N   1 
ATOM   8103  C CA  . ILE E 1 40  ? -35.848 4.532   20.555  1.00 36.46 ? 42  ILE E CA  1 
ATOM   8104  C C   . ILE E 1 40  ? -36.082 6.031   20.295  1.00 36.52 ? 42  ILE E C   1 
ATOM   8105  O O   . ILE E 1 40  ? -35.345 6.878   20.803  1.00 36.42 ? 42  ILE E O   1 
ATOM   8106  C CB  . ILE E 1 40  ? -34.342 4.186   20.370  1.00 36.58 ? 42  ILE E CB  1 
ATOM   8107  C CG1 . ILE E 1 40  ? -33.930 4.245   18.891  1.00 36.36 ? 42  ILE E CG1 1 
ATOM   8108  C CG2 . ILE E 1 40  ? -34.006 2.827   21.012  1.00 36.07 ? 42  ILE E CG2 1 
ATOM   8109  C CD1 . ILE E 1 40  ? -32.422 4.208   18.663  1.00 35.89 ? 42  ILE E CD1 1 
ATOM   8110  N N   . LEU E 1 41  ? -37.121 6.344   19.521  1.00 36.45 ? 43  LEU E N   1 
ATOM   8111  C CA  . LEU E 1 41  ? -37.433 7.717   19.126  1.00 36.45 ? 43  LEU E CA  1 
ATOM   8112  C C   . LEU E 1 41  ? -38.753 8.215   19.723  1.00 36.72 ? 43  LEU E C   1 
ATOM   8113  O O   . LEU E 1 41  ? -39.810 7.612   19.515  1.00 36.73 ? 43  LEU E O   1 
ATOM   8114  C CB  . LEU E 1 41  ? -37.475 7.824   17.596  1.00 36.25 ? 43  LEU E CB  1 
ATOM   8115  C CG  . LEU E 1 41  ? -37.868 9.156   16.945  1.00 35.91 ? 43  LEU E CG  1 
ATOM   8116  C CD1 . LEU E 1 41  ? -36.796 10.213  17.174  1.00 34.99 ? 43  LEU E CD1 1 
ATOM   8117  C CD2 . LEU E 1 41  ? -38.133 8.977   15.453  1.00 34.70 ? 43  LEU E CD2 1 
ATOM   8118  N N   . GLU E 1 42  ? -38.684 9.320   20.462  1.00 36.94 ? 44  GLU E N   1 
ATOM   8119  C CA  . GLU E 1 42  ? -39.882 9.971   20.994  1.00 37.29 ? 44  GLU E CA  1 
ATOM   8120  C C   . GLU E 1 42  ? -40.453 10.935  19.957  1.00 37.03 ? 44  GLU E C   1 
ATOM   8121  O O   . GLU E 1 42  ? -39.726 11.752  19.398  1.00 36.87 ? 44  GLU E O   1 
ATOM   8122  C CB  . GLU E 1 42  ? -39.570 10.699  22.303  1.00 37.41 ? 44  GLU E CB  1 
ATOM   8123  C CG  . GLU E 1 42  ? -40.734 11.472  22.904  1.00 38.87 ? 44  GLU E CG  1 
ATOM   8124  C CD  . GLU E 1 42  ? -41.973 10.618  23.105  1.00 41.27 ? 44  GLU E CD  1 
ATOM   8125  O OE1 . GLU E 1 42  ? -41.907 9.605   23.838  1.00 41.66 ? 44  GLU E OE1 1 
ATOM   8126  O OE2 . GLU E 1 42  ? -43.023 10.971  22.527  1.00 43.09 ? 44  GLU E OE2 1 
ATOM   8127  N N   . LYS E 1 43  ? -41.754 10.832  19.706  1.00 36.93 ? 45  LYS E N   1 
ATOM   8128  C CA  . LYS E 1 43  ? -42.399 11.623  18.656  1.00 36.96 ? 45  LYS E CA  1 
ATOM   8129  C C   . LYS E 1 43  ? -43.536 12.534  19.146  1.00 36.96 ? 45  LYS E C   1 
ATOM   8130  O O   . LYS E 1 43  ? -44.153 13.236  18.342  1.00 37.11 ? 45  LYS E O   1 
ATOM   8131  C CB  . LYS E 1 43  ? -42.891 10.711  17.519  1.00 36.92 ? 45  LYS E CB  1 
ATOM   8132  C CG  . LYS E 1 43  ? -41.773 10.050  16.713  1.00 37.20 ? 45  LYS E CG  1 
ATOM   8133  C CD  . LYS E 1 43  ? -42.290 9.185   15.557  1.00 38.32 ? 45  LYS E CD  1 
ATOM   8134  C CE  . LYS E 1 43  ? -42.869 7.835   16.012  1.00 38.89 ? 45  LYS E CE  1 
ATOM   8135  N NZ  . LYS E 1 43  ? -41.922 7.005   16.819  1.00 38.34 ? 45  LYS E NZ  1 
ATOM   8136  N N   . THR E 1 44  ? -43.808 12.537  20.450  1.00 36.88 ? 46  THR E N   1 
ATOM   8137  C CA  . THR E 1 44  ? -44.894 13.362  20.985  1.00 37.07 ? 46  THR E CA  1 
ATOM   8138  C C   . THR E 1 44  ? -44.463 14.342  22.076  1.00 36.95 ? 46  THR E C   1 
ATOM   8139  O O   . THR E 1 44  ? -43.427 14.168  22.723  1.00 37.12 ? 46  THR E O   1 
ATOM   8140  C CB  . THR E 1 44  ? -46.093 12.518  21.507  1.00 37.12 ? 46  THR E CB  1 
ATOM   8141  O OG1 . THR E 1 44  ? -45.644 11.616  22.525  1.00 37.77 ? 46  THR E OG1 1 
ATOM   8142  C CG2 . THR E 1 44  ? -46.756 11.732  20.371  1.00 37.32 ? 46  THR E CG2 1 
ATOM   8143  N N   . HIS E 1 45  ? -45.284 15.374  22.251  1.00 36.71 ? 47  HIS E N   1 
ATOM   8144  C CA  . HIS E 1 45  ? -45.113 16.395  23.273  1.00 36.40 ? 47  HIS E CA  1 
ATOM   8145  C C   . HIS E 1 45  ? -46.510 16.827  23.711  1.00 36.59 ? 47  HIS E C   1 
ATOM   8146  O O   . HIS E 1 45  ? -47.496 16.527  23.031  1.00 36.38 ? 47  HIS E O   1 
ATOM   8147  C CB  . HIS E 1 45  ? -44.321 17.591  22.726  1.00 36.24 ? 47  HIS E CB  1 
ATOM   8148  C CG  . HIS E 1 45  ? -44.915 18.203  21.491  1.00 35.55 ? 47  HIS E CG  1 
ATOM   8149  N ND1 . HIS E 1 45  ? -45.821 19.241  21.536  1.00 35.65 ? 47  HIS E ND1 1 
ATOM   8150  C CD2 . HIS E 1 45  ? -44.727 17.927  20.180  1.00 34.62 ? 47  HIS E CD2 1 
ATOM   8151  C CE1 . HIS E 1 45  ? -46.172 19.573  20.307  1.00 35.03 ? 47  HIS E CE1 1 
ATOM   8152  N NE2 . HIS E 1 45  ? -45.521 18.792  19.464  1.00 34.97 ? 47  HIS E NE2 1 
ATOM   8153  N N   . ASN E 1 46  ? -46.597 17.526  24.840  1.00 36.59 ? 48  ASN E N   1 
ATOM   8154  C CA  . ASN E 1 46  ? -47.890 17.957  25.359  1.00 36.64 ? 48  ASN E CA  1 
ATOM   8155  C C   . ASN E 1 46  ? -48.370 19.322  24.844  1.00 36.90 ? 48  ASN E C   1 
ATOM   8156  O O   . ASN E 1 46  ? -49.446 19.785  25.225  1.00 37.09 ? 48  ASN E O   1 
ATOM   8157  C CB  . ASN E 1 46  ? -47.922 17.880  26.891  1.00 36.44 ? 48  ASN E CB  1 
ATOM   8158  C CG  . ASN E 1 46  ? -46.965 18.846  27.556  1.00 36.13 ? 48  ASN E CG  1 
ATOM   8159  O OD1 . ASN E 1 46  ? -46.405 19.744  26.920  1.00 35.72 ? 48  ASN E OD1 1 
ATOM   8160  N ND2 . ASN E 1 46  ? -46.779 18.670  28.852  1.00 35.34 ? 48  ASN E ND2 1 
ATOM   8161  N N   . GLY E 1 47  ? -47.573 19.950  23.980  1.00 37.03 ? 49  GLY E N   1 
ATOM   8162  C CA  . GLY E 1 47  ? -47.948 21.206  23.323  1.00 37.42 ? 49  GLY E CA  1 
ATOM   8163  C C   . GLY E 1 47  ? -48.121 22.405  24.243  1.00 37.85 ? 49  GLY E C   1 
ATOM   8164  O O   . GLY E 1 47  ? -48.880 23.325  23.933  1.00 37.94 ? 49  GLY E O   1 
ATOM   8165  N N   . LYS E 1 48  ? -47.403 22.402  25.363  1.00 38.14 ? 50  LYS E N   1 
ATOM   8166  C CA  . LYS E 1 48  ? -47.547 23.420  26.399  1.00 38.64 ? 50  LYS E CA  1 
ATOM   8167  C C   . LYS E 1 48  ? -46.192 23.861  26.955  1.00 38.81 ? 50  LYS E C   1 
ATOM   8168  O O   . LYS E 1 48  ? -45.273 23.048  27.080  1.00 38.93 ? 50  LYS E O   1 
ATOM   8169  C CB  . LYS E 1 48  ? -48.412 22.875  27.544  1.00 38.72 ? 50  LYS E CB  1 
ATOM   8170  C CG  . LYS E 1 48  ? -49.902 22.711  27.211  1.00 39.51 ? 50  LYS E CG  1 
ATOM   8171  C CD  . LYS E 1 48  ? -50.536 21.510  27.928  1.00 40.67 ? 50  LYS E CD  1 
ATOM   8172  C CE  . LYS E 1 48  ? -50.625 21.709  29.437  1.00 41.43 ? 50  LYS E CE  1 
ATOM   8173  N NZ  . LYS E 1 48  ? -51.016 20.467  30.174  1.00 41.80 ? 50  LYS E NZ  1 
ATOM   8174  N N   . LEU E 1 49  ? -46.084 25.148  27.289  1.00 39.01 ? 51  LEU E N   1 
ATOM   8175  C CA  . LEU E 1 49  ? -44.924 25.698  27.998  1.00 39.14 ? 51  LEU E CA  1 
ATOM   8176  C C   . LEU E 1 49  ? -45.083 25.507  29.504  1.00 39.46 ? 51  LEU E C   1 
ATOM   8177  O O   . LEU E 1 49  ? -45.970 26.105  30.123  1.00 39.49 ? 51  LEU E O   1 
ATOM   8178  C CB  . LEU E 1 49  ? -44.754 27.186  27.690  1.00 38.95 ? 51  LEU E CB  1 
ATOM   8179  C CG  . LEU E 1 49  ? -44.658 27.627  26.228  1.00 39.22 ? 51  LEU E CG  1 
ATOM   8180  C CD1 . LEU E 1 49  ? -44.595 29.139  26.146  1.00 39.41 ? 51  LEU E CD1 1 
ATOM   8181  C CD2 . LEU E 1 49  ? -43.460 27.004  25.531  1.00 38.48 ? 51  LEU E CD2 1 
ATOM   8182  N N   . CYS E 1 50  ? -44.217 24.683  30.091  1.00 39.74 ? 52  CYS E N   1 
ATOM   8183  C CA  . CYS E 1 50  ? -44.353 24.290  31.494  1.00 40.16 ? 52  CYS E CA  1 
ATOM   8184  C C   . CYS E 1 50  ? -43.277 24.868  32.404  1.00 40.17 ? 52  CYS E C   1 
ATOM   8185  O O   . CYS E 1 50  ? -42.363 25.558  31.950  1.00 40.36 ? 52  CYS E O   1 
ATOM   8186  C CB  . CYS E 1 50  ? -44.329 22.767  31.617  1.00 40.19 ? 52  CYS E CB  1 
ATOM   8187  S SG  . CYS E 1 50  ? -45.433 21.885  30.517  1.00 41.21 ? 52  CYS E SG  1 
ATOM   8188  N N   . ASP E 1 51  ? -43.402 24.573  33.696  1.00 40.33 ? 53  ASP E N   1 
ATOM   8189  C CA  . ASP E 1 51  ? -42.354 24.844  34.670  1.00 40.48 ? 53  ASP E CA  1 
ATOM   8190  C C   . ASP E 1 51  ? -41.200 23.899  34.407  1.00 40.49 ? 53  ASP E C   1 
ATOM   8191  O O   . ASP E 1 51  ? -41.407 22.774  33.943  1.00 40.47 ? 53  ASP E O   1 
ATOM   8192  C CB  . ASP E 1 51  ? -42.870 24.604  36.089  1.00 40.62 ? 53  ASP E CB  1 
ATOM   8193  C CG  . ASP E 1 51  ? -43.974 25.567  36.492  1.00 41.07 ? 53  ASP E CG  1 
ATOM   8194  O OD1 . ASP E 1 51  ? -44.128 26.620  35.837  1.00 41.27 ? 53  ASP E OD1 1 
ATOM   8195  O OD2 . ASP E 1 51  ? -44.689 25.271  37.475  1.00 41.52 ? 53  ASP E OD2 1 
ATOM   8196  N N   . LEU E 1 52  A -39.986 24.351  34.699  1.00 40.63 ? 53  LEU E N   1 
ATOM   8197  C CA  . LEU E 1 52  A -38.811 23.502  34.545  1.00 40.77 ? 53  LEU E CA  1 
ATOM   8198  C C   . LEU E 1 52  A -38.264 23.098  35.914  1.00 40.99 ? 53  LEU E C   1 
ATOM   8199  O O   . LEU E 1 52  A -37.628 23.902  36.609  1.00 40.87 ? 53  LEU E O   1 
ATOM   8200  C CB  . LEU E 1 52  A -37.741 24.187  33.686  1.00 40.68 ? 53  LEU E CB  1 
ATOM   8201  C CG  . LEU E 1 52  A -36.543 23.337  33.241  1.00 40.31 ? 53  LEU E CG  1 
ATOM   8202  C CD1 . LEU E 1 52  A -36.967 22.226  32.278  1.00 40.05 ? 53  LEU E CD1 1 
ATOM   8203  C CD2 . LEU E 1 52  A -35.477 24.224  32.610  1.00 39.44 ? 53  LEU E CD2 1 
ATOM   8204  N N   . ASP E 1 53  ? -38.527 21.840  36.276  1.00 41.25 ? 54  ASP E N   1 
ATOM   8205  C CA  . ASP E 1 53  ? -38.218 21.281  37.600  1.00 41.66 ? 54  ASP E CA  1 
ATOM   8206  C C   . ASP E 1 53  ? -38.772 22.137  38.753  1.00 41.39 ? 54  ASP E C   1 
ATOM   8207  O O   . ASP E 1 53  ? -38.084 22.401  39.746  1.00 41.37 ? 54  ASP E O   1 
ATOM   8208  C CB  . ASP E 1 53  ? -36.711 21.015  37.759  1.00 41.96 ? 54  ASP E CB  1 
ATOM   8209  C CG  . ASP E 1 53  ? -36.407 19.892  38.754  1.00 43.56 ? 54  ASP E CG  1 
ATOM   8210  O OD1 . ASP E 1 53  ? -37.357 19.266  39.283  1.00 44.25 ? 54  ASP E OD1 1 
ATOM   8211  O OD2 . ASP E 1 53  ? -35.205 19.635  39.006  1.00 45.52 ? 54  ASP E OD2 1 
ATOM   8212  N N   . GLY E 1 54  ? -40.021 22.571  38.597  1.00 41.07 ? 55  GLY E N   1 
ATOM   8213  C CA  . GLY E 1 54  ? -40.719 23.333  39.625  1.00 40.83 ? 55  GLY E CA  1 
ATOM   8214  C C   . GLY E 1 54  ? -40.418 24.823  39.641  1.00 40.71 ? 55  GLY E C   1 
ATOM   8215  O O   . GLY E 1 54  ? -40.796 25.518  40.586  1.00 40.90 ? 55  GLY E O   1 
ATOM   8216  N N   . VAL E 1 55  ? -39.729 25.314  38.612  1.00 40.31 ? 56  VAL E N   1 
ATOM   8217  C CA  . VAL E 1 55  ? -39.466 26.750  38.479  1.00 39.86 ? 56  VAL E CA  1 
ATOM   8218  C C   . VAL E 1 55  ? -40.166 27.314  37.238  1.00 39.68 ? 56  VAL E C   1 
ATOM   8219  O O   . VAL E 1 55  ? -39.925 26.872  36.110  1.00 39.67 ? 56  VAL E O   1 
ATOM   8220  C CB  . VAL E 1 55  ? -37.955 27.079  38.441  1.00 39.78 ? 56  VAL E CB  1 
ATOM   8221  C CG1 . VAL E 1 55  ? -37.746 28.585  38.456  1.00 39.65 ? 56  VAL E CG1 1 
ATOM   8222  C CG2 . VAL E 1 55  ? -37.229 26.434  39.615  1.00 39.56 ? 56  VAL E CG2 1 
ATOM   8223  N N   . LYS E 1 56  ? -41.039 28.288  37.468  1.00 39.39 ? 57  LYS E N   1 
ATOM   8224  C CA  . LYS E 1 56  ? -41.830 28.891  36.407  1.00 39.26 ? 57  LYS E CA  1 
ATOM   8225  C C   . LYS E 1 56  ? -40.976 29.783  35.506  1.00 38.97 ? 57  LYS E C   1 
ATOM   8226  O O   . LYS E 1 56  ? -40.152 30.559  35.996  1.00 38.86 ? 57  LYS E O   1 
ATOM   8227  C CB  . LYS E 1 56  ? -43.006 29.685  36.991  1.00 39.28 ? 57  LYS E CB  1 
ATOM   8228  C CG  . LYS E 1 56  ? -44.044 30.100  35.958  1.00 40.03 ? 57  LYS E CG  1 
ATOM   8229  C CD  . LYS E 1 56  ? -45.013 31.134  36.500  1.00 41.60 ? 57  LYS E CD  1 
ATOM   8230  C CE  . LYS E 1 56  ? -45.903 31.664  35.387  1.00 42.37 ? 57  LYS E CE  1 
ATOM   8231  N NZ  . LYS E 1 56  ? -46.824 32.729  35.873  1.00 43.48 ? 57  LYS E NZ  1 
ATOM   8232  N N   . PRO E 1 57  ? -41.168 29.663  34.179  1.00 38.73 ? 58  PRO E N   1 
ATOM   8233  C CA  . PRO E 1 57  ? -40.528 30.560  33.226  1.00 38.49 ? 58  PRO E CA  1 
ATOM   8234  C C   . PRO E 1 57  ? -41.084 31.978  33.296  1.00 38.42 ? 58  PRO E C   1 
ATOM   8235  O O   . PRO E 1 57  ? -42.136 32.208  33.889  1.00 38.21 ? 58  PRO E O   1 
ATOM   8236  C CB  . PRO E 1 57  ? -40.890 29.943  31.872  1.00 38.65 ? 58  PRO E CB  1 
ATOM   8237  C CG  . PRO E 1 57  ? -42.120 29.134  32.126  1.00 38.55 ? 58  PRO E CG  1 
ATOM   8238  C CD  . PRO E 1 57  ? -41.922 28.590  33.501  1.00 38.69 ? 58  PRO E CD  1 
ATOM   8239  N N   . LEU E 1 58  ? -40.360 32.914  32.696  1.00 38.54 ? 59  LEU E N   1 
ATOM   8240  C CA  . LEU E 1 58  ? -40.838 34.273  32.500  1.00 38.53 ? 59  LEU E CA  1 
ATOM   8241  C C   . LEU E 1 58  ? -41.433 34.380  31.094  1.00 38.71 ? 59  LEU E C   1 
ATOM   8242  O O   . LEU E 1 58  ? -40.712 34.297  30.095  1.00 38.71 ? 59  LEU E O   1 
ATOM   8243  C CB  . LEU E 1 58  ? -39.690 35.269  32.697  1.00 38.33 ? 59  LEU E CB  1 
ATOM   8244  C CG  . LEU E 1 58  ? -39.893 36.727  32.278  1.00 38.42 ? 59  LEU E CG  1 
ATOM   8245  C CD1 . LEU E 1 58  ? -40.994 37.398  33.097  1.00 38.47 ? 59  LEU E CD1 1 
ATOM   8246  C CD2 . LEU E 1 58  ? -38.588 37.499  32.385  1.00 38.57 ? 59  LEU E CD2 1 
ATOM   8247  N N   . ILE E 1 59  ? -42.753 34.542  31.025  1.00 38.99 ? 60  ILE E N   1 
ATOM   8248  C CA  . ILE E 1 59  ? -43.468 34.611  29.746  1.00 39.26 ? 60  ILE E CA  1 
ATOM   8249  C C   . ILE E 1 59  ? -43.873 36.056  29.471  1.00 39.46 ? 60  ILE E C   1 
ATOM   8250  O O   . ILE E 1 59  ? -44.811 36.574  30.076  1.00 39.68 ? 60  ILE E O   1 
ATOM   8251  C CB  . ILE E 1 59  ? -44.687 33.648  29.727  1.00 39.23 ? 60  ILE E CB  1 
ATOM   8252  C CG1 . ILE E 1 59  ? -44.205 32.200  29.811  1.00 39.56 ? 60  ILE E CG1 1 
ATOM   8253  C CG2 . ILE E 1 59  ? -45.536 33.836  28.463  1.00 39.19 ? 60  ILE E CG2 1 
ATOM   8254  C CD1 . ILE E 1 59  ? -45.088 31.314  30.640  1.00 40.00 ? 60  ILE E CD1 1 
ATOM   8255  N N   . LEU E 1 60  ? -43.151 36.695  28.555  1.00 39.77 ? 61  LEU E N   1 
ATOM   8256  C CA  . LEU E 1 60  ? -43.266 38.137  28.321  1.00 40.27 ? 61  LEU E CA  1 
ATOM   8257  C C   . LEU E 1 60  ? -44.506 38.564  27.525  1.00 40.76 ? 61  LEU E C   1 
ATOM   8258  O O   . LEU E 1 60  ? -44.781 39.761  27.388  1.00 40.74 ? 61  LEU E O   1 
ATOM   8259  C CB  . LEU E 1 60  ? -41.984 38.678  27.669  1.00 40.14 ? 61  LEU E CB  1 
ATOM   8260  C CG  . LEU E 1 60  ? -40.689 38.610  28.489  1.00 39.71 ? 61  LEU E CG  1 
ATOM   8261  C CD1 . LEU E 1 60  ? -39.509 39.101  27.668  1.00 38.43 ? 61  LEU E CD1 1 
ATOM   8262  C CD2 . LEU E 1 60  ? -40.797 39.391  29.801  1.00 39.12 ? 61  LEU E CD2 1 
ATOM   8263  N N   . ARG E 1 61  ? -45.250 37.583  27.026  1.00 41.37 ? 62  ARG E N   1 
ATOM   8264  C CA  . ARG E 1 61  ? -46.495 37.843  26.313  1.00 41.97 ? 62  ARG E CA  1 
ATOM   8265  C C   . ARG E 1 61  ? -46.238 38.795  25.150  1.00 42.01 ? 62  ARG E C   1 
ATOM   8266  O O   . ARG E 1 61  ? -45.537 38.454  24.198  1.00 41.98 ? 62  ARG E O   1 
ATOM   8267  C CB  . ARG E 1 61  ? -47.541 38.430  27.263  1.00 42.13 ? 62  ARG E CB  1 
ATOM   8268  C CG  . ARG E 1 61  ? -48.143 37.419  28.225  1.00 43.97 ? 62  ARG E CG  1 
ATOM   8269  C CD  . ARG E 1 61  ? -48.621 38.090  29.503  1.00 46.78 ? 62  ARG E CD  1 
ATOM   8270  N NE  . ARG E 1 61  ? -49.933 38.709  29.337  1.00 49.26 ? 62  ARG E NE  1 
ATOM   8271  C CZ  . ARG E 1 61  ? -51.072 38.032  29.239  1.00 50.03 ? 62  ARG E CZ  1 
ATOM   8272  N NH1 . ARG E 1 61  ? -51.064 36.707  29.290  1.00 50.89 ? 62  ARG E NH1 1 
ATOM   8273  N NH2 . ARG E 1 61  ? -52.220 38.678  29.090  1.00 50.63 ? 62  ARG E NH2 1 
ATOM   8274  N N   . ASP E 1 62  ? -46.816 39.989  25.232  1.00 42.18 ? 63  ASP E N   1 
ATOM   8275  C CA  . ASP E 1 62  ? -46.708 40.965  24.153  1.00 42.29 ? 63  ASP E CA  1 
ATOM   8276  C C   . ASP E 1 62  ? -45.559 41.949  24.322  1.00 41.98 ? 63  ASP E C   1 
ATOM   8277  O O   . ASP E 1 62  ? -45.408 42.883  23.529  1.00 41.89 ? 63  ASP E O   1 
ATOM   8278  C CB  . ASP E 1 62  ? -48.045 41.699  24.005  1.00 42.66 ? 63  ASP E CB  1 
ATOM   8279  C CG  . ASP E 1 62  ? -49.145 40.801  23.465  1.00 44.01 ? 63  ASP E CG  1 
ATOM   8280  O OD1 . ASP E 1 62  ? -48.864 39.989  22.552  1.00 45.25 ? 63  ASP E OD1 1 
ATOM   8281  O OD2 . ASP E 1 62  ? -50.296 40.906  23.950  1.00 45.80 ? 63  ASP E OD2 1 
ATOM   8282  N N   . CYS E 1 63  ? -44.749 41.726  25.354  1.00 41.60 ? 64  CYS E N   1 
ATOM   8283  C CA  . CYS E 1 63  ? -43.603 42.578  25.629  1.00 41.31 ? 64  CYS E CA  1 
ATOM   8284  C C   . CYS E 1 63  ? -42.302 41.945  25.153  1.00 40.45 ? 64  CYS E C   1 
ATOM   8285  O O   . CYS E 1 63  ? -42.125 40.731  25.215  1.00 40.39 ? 64  CYS E O   1 
ATOM   8286  C CB  . CYS E 1 63  ? -43.529 42.921  27.119  1.00 41.45 ? 64  CYS E CB  1 
ATOM   8287  S SG  . CYS E 1 63  ? -44.917 43.948  27.693  1.00 44.05 ? 64  CYS E SG  1 
ATOM   8288  N N   . SER E 1 64  ? -41.404 42.785  24.654  1.00 39.68 ? 65  SER E N   1 
ATOM   8289  C CA  . SER E 1 64  ? -40.057 42.362  24.323  1.00 38.76 ? 65  SER E CA  1 
ATOM   8290  C C   . SER E 1 64  ? -39.181 42.576  25.546  1.00 38.14 ? 65  SER E C   1 
ATOM   8291  O O   . SER E 1 64  ? -39.627 43.138  26.549  1.00 37.81 ? 65  SER E O   1 
ATOM   8292  C CB  . SER E 1 64  ? -39.519 43.170  23.145  1.00 38.65 ? 65  SER E CB  1 
ATOM   8293  O OG  . SER E 1 64  ? -39.334 44.518  23.524  1.00 38.57 ? 65  SER E OG  1 
ATOM   8294  N N   . VAL E 1 65  ? -37.934 42.128  25.454  1.00 37.55 ? 66  VAL E N   1 
ATOM   8295  C CA  . VAL E 1 65  ? -36.967 42.306  26.533  1.00 37.03 ? 66  VAL E CA  1 
ATOM   8296  C C   . VAL E 1 65  ? -36.749 43.792  26.820  1.00 36.77 ? 66  VAL E C   1 
ATOM   8297  O O   . VAL E 1 65  ? -36.852 44.223  27.969  1.00 36.75 ? 66  VAL E O   1 
ATOM   8298  C CB  . VAL E 1 65  ? -35.639 41.573  26.226  1.00 36.91 ? 66  VAL E CB  1 
ATOM   8299  C CG1 . VAL E 1 65  ? -34.540 42.001  27.184  1.00 36.62 ? 66  VAL E CG1 1 
ATOM   8300  C CG2 . VAL E 1 65  ? -35.852 40.064  26.288  1.00 36.49 ? 66  VAL E CG2 1 
ATOM   8301  N N   . ALA E 1 66  ? -36.479 44.572  25.774  1.00 36.41 ? 67  ALA E N   1 
ATOM   8302  C CA  . ALA E 1 66  ? -36.306 46.018  25.928  1.00 36.24 ? 67  ALA E CA  1 
ATOM   8303  C C   . ALA E 1 66  ? -37.494 46.639  26.657  1.00 35.95 ? 67  ALA E C   1 
ATOM   8304  O O   . ALA E 1 66  ? -37.311 47.445  27.569  1.00 35.87 ? 67  ALA E O   1 
ATOM   8305  C CB  . ALA E 1 66  ? -36.089 46.694  24.577  1.00 36.04 ? 67  ALA E CB  1 
ATOM   8306  N N   . GLY E 1 67  ? -38.701 46.237  26.257  1.00 35.90 ? 68  GLY E N   1 
ATOM   8307  C CA  . GLY E 1 67  ? -39.944 46.733  26.847  1.00 35.79 ? 68  GLY E CA  1 
ATOM   8308  C C   . GLY E 1 67  ? -40.028 46.437  28.327  1.00 35.79 ? 68  GLY E C   1 
ATOM   8309  O O   . GLY E 1 67  ? -40.460 47.280  29.112  1.00 35.50 ? 68  GLY E O   1 
ATOM   8310  N N   . TRP E 1 68  ? -39.601 45.231  28.697  1.00 35.98 ? 69  TRP E N   1 
ATOM   8311  C CA  . TRP E 1 68  ? -39.537 44.804  30.089  1.00 36.16 ? 69  TRP E CA  1 
ATOM   8312  C C   . TRP E 1 68  ? -38.501 45.597  30.884  1.00 36.34 ? 69  TRP E C   1 
ATOM   8313  O O   . TRP E 1 68  ? -38.827 46.177  31.923  1.00 36.37 ? 69  TRP E O   1 
ATOM   8314  C CB  . TRP E 1 68  ? -39.261 43.295  30.164  1.00 36.18 ? 69  TRP E CB  1 
ATOM   8315  C CG  . TRP E 1 68  ? -38.738 42.791  31.499  1.00 36.42 ? 69  TRP E CG  1 
ATOM   8316  C CD1 . TRP E 1 68  ? -39.177 43.142  32.745  1.00 36.63 ? 69  TRP E CD1 1 
ATOM   8317  C CD2 . TRP E 1 68  ? -37.701 41.819  31.703  1.00 36.30 ? 69  TRP E CD2 1 
ATOM   8318  N NE1 . TRP E 1 68  ? -38.468 42.464  33.708  1.00 36.61 ? 69  TRP E NE1 1 
ATOM   8319  C CE2 . TRP E 1 68  ? -37.557 41.646  33.096  1.00 35.89 ? 69  TRP E CE2 1 
ATOM   8320  C CE3 . TRP E 1 68  ? -36.875 41.085  30.840  1.00 36.00 ? 69  TRP E CE3 1 
ATOM   8321  C CZ2 . TRP E 1 68  ? -36.623 40.772  33.650  1.00 36.21 ? 69  TRP E CZ2 1 
ATOM   8322  C CZ3 . TRP E 1 68  ? -35.945 40.217  31.392  1.00 36.25 ? 69  TRP E CZ3 1 
ATOM   8323  C CH2 . TRP E 1 68  ? -35.828 40.067  32.786  1.00 36.28 ? 69  TRP E CH2 1 
ATOM   8324  N N   . LEU E 1 69  ? -37.267 45.639  30.384  1.00 36.52 ? 70  LEU E N   1 
ATOM   8325  C CA  . LEU E 1 69  ? -36.151 46.239  31.128  1.00 36.70 ? 70  LEU E CA  1 
ATOM   8326  C C   . LEU E 1 69  ? -36.253 47.754  31.281  1.00 36.99 ? 70  LEU E C   1 
ATOM   8327  O O   . LEU E 1 69  ? -35.965 48.289  32.353  1.00 37.17 ? 70  LEU E O   1 
ATOM   8328  C CB  . LEU E 1 69  ? -34.800 45.841  30.518  1.00 36.57 ? 70  LEU E CB  1 
ATOM   8329  C CG  . LEU E 1 69  ? -34.411 44.353  30.559  1.00 36.19 ? 70  LEU E CG  1 
ATOM   8330  C CD1 . LEU E 1 69  ? -33.050 44.138  29.917  1.00 34.92 ? 70  LEU E CD1 1 
ATOM   8331  C CD2 . LEU E 1 69  ? -34.442 43.777  31.981  1.00 35.85 ? 70  LEU E CD2 1 
ATOM   8332  N N   . LEU E 1 70  ? -36.659 48.441  30.216  1.00 37.20 ? 71  LEU E N   1 
ATOM   8333  C CA  . LEU E 1 70  ? -36.866 49.886  30.271  1.00 37.47 ? 71  LEU E CA  1 
ATOM   8334  C C   . LEU E 1 70  ? -38.168 50.265  30.983  1.00 37.89 ? 71  LEU E C   1 
ATOM   8335  O O   . LEU E 1 70  ? -38.308 51.384  31.477  1.00 37.91 ? 71  LEU E O   1 
ATOM   8336  C CB  . LEU E 1 70  ? -36.837 50.491  28.866  1.00 37.38 ? 71  LEU E CB  1 
ATOM   8337  C CG  . LEU E 1 70  ? -35.497 50.524  28.126  1.00 37.14 ? 71  LEU E CG  1 
ATOM   8338  C CD1 . LEU E 1 70  ? -35.698 50.965  26.683  1.00 36.94 ? 71  LEU E CD1 1 
ATOM   8339  C CD2 . LEU E 1 70  ? -34.496 51.435  28.828  1.00 36.98 ? 71  LEU E CD2 1 
ATOM   8340  N N   . GLY E 1 71  ? -39.112 49.329  31.032  1.00 38.30 ? 72  GLY E N   1 
ATOM   8341  C CA  . GLY E 1 71  ? -40.408 49.569  31.642  1.00 38.96 ? 72  GLY E CA  1 
ATOM   8342  C C   . GLY E 1 71  ? -41.383 50.327  30.755  1.00 39.58 ? 72  GLY E C   1 
ATOM   8343  O O   . GLY E 1 71  ? -41.892 51.374  31.145  1.00 39.55 ? 72  GLY E O   1 
ATOM   8344  N N   . ASN E 1 72  ? -41.632 49.807  29.555  1.00 40.30 ? 73  ASN E N   1 
ATOM   8345  C CA  . ASN E 1 72  ? -42.760 50.256  28.741  1.00 40.92 ? 73  ASN E CA  1 
ATOM   8346  C C   . ASN E 1 72  ? -44.009 50.181  29.623  1.00 41.58 ? 73  ASN E C   1 
ATOM   8347  O O   . ASN E 1 72  ? -44.232 49.166  30.290  1.00 41.55 ? 73  ASN E O   1 
ATOM   8348  C CB  . ASN E 1 72  ? -42.908 49.370  27.496  1.00 40.73 ? 73  ASN E CB  1 
ATOM   8349  C CG  . ASN E 1 72  ? -43.935 49.904  26.493  1.00 40.67 ? 73  ASN E CG  1 
ATOM   8350  O OD1 . ASN E 1 72  ? -45.130 49.988  26.781  1.00 40.16 ? 73  ASN E OD1 1 
ATOM   8351  N ND2 . ASN E 1 72  ? -43.469 50.233  25.296  1.00 40.07 ? 73  ASN E ND2 1 
ATOM   8352  N N   . PRO E 1 73  ? -44.807 51.267  29.663  1.00 42.21 ? 74  PRO E N   1 
ATOM   8353  C CA  . PRO E 1 73  ? -45.974 51.319  30.552  1.00 42.81 ? 74  PRO E CA  1 
ATOM   8354  C C   . PRO E 1 73  ? -47.030 50.251  30.254  1.00 43.45 ? 74  PRO E C   1 
ATOM   8355  O O   . PRO E 1 73  ? -47.841 49.930  31.122  1.00 43.54 ? 74  PRO E O   1 
ATOM   8356  C CB  . PRO E 1 73  ? -46.539 52.727  30.329  1.00 42.71 ? 74  PRO E CB  1 
ATOM   8357  C CG  . PRO E 1 73  ? -45.937 53.203  29.063  1.00 42.56 ? 74  PRO E CG  1 
ATOM   8358  C CD  . PRO E 1 73  ? -44.613 52.530  28.932  1.00 42.29 ? 74  PRO E CD  1 
ATOM   8359  N N   . MET E 1 74  ? -47.005 49.695  29.045  1.00 44.25 ? 75  MET E N   1 
ATOM   8360  C CA  . MET E 1 74  ? -47.870 48.570  28.688  1.00 45.03 ? 75  MET E CA  1 
ATOM   8361  C C   . MET E 1 74  ? -47.419 47.267  29.358  1.00 45.11 ? 75  MET E C   1 
ATOM   8362  O O   . MET E 1 74  ? -48.166 46.287  29.380  1.00 45.29 ? 75  MET E O   1 
ATOM   8363  C CB  . MET E 1 74  ? -47.890 48.372  27.169  1.00 45.40 ? 75  MET E CB  1 
ATOM   8364  C CG  . MET E 1 74  ? -48.388 49.567  26.356  1.00 47.08 ? 75  MET E CG  1 
ATOM   8365  S SD  . MET E 1 74  ? -50.058 50.082  26.793  1.00 50.49 ? 75  MET E SD  1 
ATOM   8366  C CE  . MET E 1 74  ? -50.615 50.728  25.210  1.00 51.21 ? 75  MET E CE  1 
ATOM   8367  N N   . CYS E 1 75  ? -46.200 47.267  29.897  1.00 45.14 ? 76  CYS E N   1 
ATOM   8368  C CA  . CYS E 1 75  ? -45.569 46.064  30.434  1.00 45.24 ? 76  CYS E CA  1 
ATOM   8369  C C   . CYS E 1 75  ? -45.520 46.065  31.959  1.00 45.43 ? 76  CYS E C   1 
ATOM   8370  O O   . CYS E 1 75  ? -44.586 45.523  32.557  1.00 45.62 ? 76  CYS E O   1 
ATOM   8371  C CB  . CYS E 1 75  ? -44.151 45.913  29.863  1.00 45.10 ? 76  CYS E CB  1 
ATOM   8372  S SG  . CYS E 1 75  ? -44.073 45.784  28.058  1.00 45.20 ? 76  CYS E SG  1 
ATOM   8373  N N   . ASP E 1 76  ? -46.534 46.661  32.582  1.00 45.62 ? 77  ASP E N   1 
ATOM   8374  C CA  . ASP E 1 76  ? -46.619 46.757  34.042  1.00 45.88 ? 77  ASP E CA  1 
ATOM   8375  C C   . ASP E 1 76  ? -46.721 45.406  34.760  1.00 45.73 ? 77  ASP E C   1 
ATOM   8376  O O   . ASP E 1 76  ? -46.432 45.316  35.955  1.00 45.69 ? 77  ASP E O   1 
ATOM   8377  C CB  . ASP E 1 76  ? -47.779 47.668  34.460  1.00 46.12 ? 77  ASP E CB  1 
ATOM   8378  C CG  . ASP E 1 76  ? -47.386 49.144  34.519  1.00 47.52 ? 77  ASP E CG  1 
ATOM   8379  O OD1 . ASP E 1 76  ? -48.306 49.995  34.569  1.00 49.30 ? 77  ASP E OD1 1 
ATOM   8380  O OD2 . ASP E 1 76  ? -46.173 49.462  34.530  1.00 48.04 ? 77  ASP E OD2 1 
ATOM   8381  N N   . GLU E 1 77  ? -47.119 44.361  34.030  1.00 45.52 ? 78  GLU E N   1 
ATOM   8382  C CA  . GLU E 1 77  ? -47.143 42.995  34.569  1.00 45.32 ? 78  GLU E CA  1 
ATOM   8383  C C   . GLU E 1 77  ? -45.759 42.558  35.066  1.00 45.10 ? 78  GLU E C   1 
ATOM   8384  O O   . GLU E 1 77  ? -45.647 41.762  36.003  1.00 44.96 ? 78  GLU E O   1 
ATOM   8385  C CB  . GLU E 1 77  ? -47.669 41.994  33.521  1.00 45.25 ? 78  GLU E CB  1 
ATOM   8386  C CG  . GLU E 1 77  ? -47.772 40.539  34.028  1.00 45.54 ? 78  GLU E CG  1 
ATOM   8387  C CD  . GLU E 1 77  ? -48.241 39.541  32.971  1.00 46.50 ? 78  GLU E CD  1 
ATOM   8388  O OE1 . GLU E 1 77  ? -48.815 39.968  31.943  1.00 46.33 ? 78  GLU E OE1 1 
ATOM   8389  O OE2 . GLU E 1 77  ? -48.046 38.319  33.178  1.00 46.31 ? 78  GLU E OE2 1 
ATOM   8390  N N   . PHE E 1 78  ? -44.713 43.092  34.433  1.00 44.87 ? 79  PHE E N   1 
ATOM   8391  C CA  . PHE E 1 78  ? -43.343 42.654  34.692  1.00 44.47 ? 79  PHE E CA  1 
ATOM   8392  C C   . PHE E 1 78  ? -42.532 43.700  35.448  1.00 44.53 ? 79  PHE E C   1 
ATOM   8393  O O   . PHE E 1 78  ? -41.306 43.755  35.322  1.00 44.70 ? 79  PHE E O   1 
ATOM   8394  C CB  . PHE E 1 78  ? -42.654 42.272  33.374  1.00 44.23 ? 79  PHE E CB  1 
ATOM   8395  C CG  . PHE E 1 78  ? -43.459 41.338  32.524  1.00 42.78 ? 79  PHE E CG  1 
ATOM   8396  C CD1 . PHE E 1 78  ? -43.535 39.986  32.836  1.00 41.68 ? 79  PHE E CD1 1 
ATOM   8397  C CD2 . PHE E 1 78  ? -44.159 41.813  31.423  1.00 42.31 ? 79  PHE E CD2 1 
ATOM   8398  C CE1 . PHE E 1 78  ? -44.290 39.120  32.059  1.00 41.39 ? 79  PHE E CE1 1 
ATOM   8399  C CE2 . PHE E 1 78  ? -44.918 40.956  30.636  1.00 41.36 ? 79  PHE E CE2 1 
ATOM   8400  C CZ  . PHE E 1 78  ? -44.986 39.609  30.957  1.00 41.42 ? 79  PHE E CZ  1 
ATOM   8401  N N   . ILE E 1 79  ? -43.219 44.516  36.242  1.00 44.47 ? 80  ILE E N   1 
ATOM   8402  C CA  . ILE E 1 79  ? -42.568 45.584  37.006  1.00 44.54 ? 80  ILE E CA  1 
ATOM   8403  C C   . ILE E 1 79  ? -41.612 45.026  38.071  1.00 44.27 ? 80  ILE E C   1 
ATOM   8404  O O   . ILE E 1 79  ? -40.529 45.567  38.287  1.00 44.38 ? 80  ILE E O   1 
ATOM   8405  C CB  . ILE E 1 79  ? -43.608 46.621  37.584  1.00 44.69 ? 80  ILE E CB  1 
ATOM   8406  C CG1 . ILE E 1 79  ? -42.915 47.914  38.019  1.00 45.09 ? 80  ILE E CG1 1 
ATOM   8407  C CG2 . ILE E 1 79  ? -44.456 46.028  38.717  1.00 44.71 ? 80  ILE E CG2 1 
ATOM   8408  C CD1 . ILE E 1 79  ? -42.454 48.788  36.859  1.00 46.13 ? 80  ILE E CD1 1 
ATOM   8409  N N   . ASN E 1 80  ? -42.021 43.940  38.719  1.00 44.05 ? 81  ASN E N   1 
ATOM   8410  C CA  . ASN E 1 80  ? -41.139 43.162  39.588  1.00 43.86 ? 81  ASN E CA  1 
ATOM   8411  C C   . ASN E 1 80  ? -41.336 41.669  39.345  1.00 43.47 ? 81  ASN E C   1 
ATOM   8412  O O   . ASN E 1 80  ? -42.391 41.110  39.652  1.00 43.56 ? 81  ASN E O   1 
ATOM   8413  C CB  . ASN E 1 80  ? -41.347 43.517  41.063  1.00 44.07 ? 81  ASN E CB  1 
ATOM   8414  C CG  . ASN E 1 80  ? -40.593 44.770  41.472  1.00 44.60 ? 81  ASN E CG  1 
ATOM   8415  O OD1 . ASN E 1 80  ? -39.366 44.825  41.381  1.00 45.91 ? 81  ASN E OD1 1 
ATOM   8416  N ND2 . ASN E 1 80  ? -41.323 45.782  41.926  1.00 44.64 ? 81  ASN E ND2 1 
ATOM   8417  N N   . VAL E 1 81  ? -40.313 41.038  38.780  1.00 42.92 ? 82  VAL E N   1 
ATOM   8418  C CA  . VAL E 1 81  ? -40.386 39.648  38.342  1.00 42.53 ? 82  VAL E CA  1 
ATOM   8419  C C   . VAL E 1 81  ? -39.615 38.747  39.311  1.00 41.97 ? 82  VAL E C   1 
ATOM   8420  O O   . VAL E 1 81  ? -38.547 39.131  39.789  1.00 42.06 ? 82  VAL E O   1 
ATOM   8421  C CB  . VAL E 1 81  ? -39.871 39.515  36.869  1.00 42.61 ? 82  VAL E CB  1 
ATOM   8422  C CG1 . VAL E 1 81  ? -39.436 38.100  36.531  1.00 43.01 ? 82  VAL E CG1 1 
ATOM   8423  C CG2 . VAL E 1 81  ? -40.937 39.988  35.889  1.00 42.79 ? 82  VAL E CG2 1 
ATOM   8424  N N   . PRO E 1 82  A -40.168 37.558  39.624  1.00 41.42 ? 82  PRO E N   1 
ATOM   8425  C CA  . PRO E 1 82  A -39.457 36.600  40.472  1.00 41.15 ? 82  PRO E CA  1 
ATOM   8426  C C   . PRO E 1 82  A -38.495 35.733  39.655  1.00 40.81 ? 82  PRO E C   1 
ATOM   8427  O O   . PRO E 1 82  A -38.543 35.761  38.424  1.00 41.01 ? 82  PRO E O   1 
ATOM   8428  C CB  . PRO E 1 82  A -40.590 35.743  41.032  1.00 41.03 ? 82  PRO E CB  1 
ATOM   8429  C CG  . PRO E 1 82  A -41.601 35.720  39.926  1.00 41.05 ? 82  PRO E CG  1 
ATOM   8430  C CD  . PRO E 1 82  A -41.521 37.079  39.274  1.00 41.39 ? 82  PRO E CD  1 
ATOM   8431  N N   . GLU E 1 83  ? -37.640 34.973  40.339  1.00 40.22 ? 83  GLU E N   1 
ATOM   8432  C CA  . GLU E 1 83  ? -36.710 34.028  39.703  1.00 39.76 ? 83  GLU E CA  1 
ATOM   8433  C C   . GLU E 1 83  ? -37.374 33.195  38.599  1.00 39.13 ? 83  GLU E C   1 
ATOM   8434  O O   . GLU E 1 83  ? -38.502 32.724  38.757  1.00 39.00 ? 83  GLU E O   1 
ATOM   8435  C CB  . GLU E 1 83  ? -36.100 33.112  40.770  1.00 39.97 ? 83  GLU E CB  1 
ATOM   8436  C CG  . GLU E 1 83  ? -35.168 32.026  40.251  1.00 40.98 ? 83  GLU E CG  1 
ATOM   8437  C CD  . GLU E 1 83  ? -34.457 31.272  41.368  1.00 42.82 ? 83  GLU E CD  1 
ATOM   8438  O OE1 . GLU E 1 83  ? -33.952 31.919  42.315  1.00 43.20 ? 83  GLU E OE1 1 
ATOM   8439  O OE2 . GLU E 1 83  ? -34.391 30.026  41.292  1.00 43.71 ? 83  GLU E OE2 1 
ATOM   8440  N N   . TRP E 1 84  ? -36.670 33.031  37.480  1.00 38.31 ? 84  TRP E N   1 
ATOM   8441  C CA  . TRP E 1 84  ? -37.171 32.239  36.357  1.00 37.50 ? 84  TRP E CA  1 
ATOM   8442  C C   . TRP E 1 84  ? -36.256 31.059  36.022  1.00 37.25 ? 84  TRP E C   1 
ATOM   8443  O O   . TRP E 1 84  ? -35.109 31.004  36.465  1.00 37.20 ? 84  TRP E O   1 
ATOM   8444  C CB  . TRP E 1 84  ? -37.384 33.123  35.119  1.00 37.30 ? 84  TRP E CB  1 
ATOM   8445  C CG  . TRP E 1 84  ? -36.124 33.771  34.619  1.00 36.10 ? 84  TRP E CG  1 
ATOM   8446  C CD1 . TRP E 1 84  ? -35.183 33.211  33.807  1.00 35.48 ? 84  TRP E CD1 1 
ATOM   8447  C CD2 . TRP E 1 84  ? -35.668 35.098  34.905  1.00 35.23 ? 84  TRP E CD2 1 
ATOM   8448  N NE1 . TRP E 1 84  ? -34.168 34.101  33.571  1.00 34.96 ? 84  TRP E NE1 1 
ATOM   8449  C CE2 . TRP E 1 84  ? -34.440 35.270  34.231  1.00 34.60 ? 84  TRP E CE2 1 
ATOM   8450  C CE3 . TRP E 1 84  ? -36.176 36.159  35.667  1.00 34.44 ? 84  TRP E CE3 1 
ATOM   8451  C CZ2 . TRP E 1 84  ? -33.710 36.461  34.291  1.00 34.21 ? 84  TRP E CZ2 1 
ATOM   8452  C CZ3 . TRP E 1 84  ? -35.449 37.343  35.726  1.00 34.30 ? 84  TRP E CZ3 1 
ATOM   8453  C CH2 . TRP E 1 84  ? -34.228 37.482  35.042  1.00 33.84 ? 84  TRP E CH2 1 
ATOM   8454  N N   . SER E 1 85  ? -36.780 30.118  35.242  1.00 36.89 ? 85  SER E N   1 
ATOM   8455  C CA  . SER E 1 85  ? -35.998 28.998  34.739  1.00 36.76 ? 85  SER E CA  1 
ATOM   8456  C C   . SER E 1 85  ? -35.576 29.269  33.294  1.00 36.65 ? 85  SER E C   1 
ATOM   8457  O O   . SER E 1 85  ? -34.420 29.063  32.925  1.00 36.86 ? 85  SER E O   1 
ATOM   8458  C CB  . SER E 1 85  ? -36.800 27.703  34.833  1.00 36.82 ? 85  SER E CB  1 
ATOM   8459  O OG  . SER E 1 85  ? -38.051 27.839  34.185  1.00 37.14 ? 85  SER E OG  1 
ATOM   8460  N N   . TYR E 1 86  ? -36.522 29.727  32.481  1.00 36.15 ? 86  TYR E N   1 
ATOM   8461  C CA  . TYR E 1 86  ? -36.224 30.191  31.134  1.00 35.73 ? 86  TYR E CA  1 
ATOM   8462  C C   . TYR E 1 86  ? -37.107 31.389  30.791  1.00 35.74 ? 86  TYR E C   1 
ATOM   8463  O O   . TYR E 1 86  ? -38.094 31.643  31.477  1.00 35.65 ? 86  TYR E O   1 
ATOM   8464  C CB  . TYR E 1 86  ? -36.346 29.054  30.103  1.00 35.45 ? 86  TYR E CB  1 
ATOM   8465  C CG  . TYR E 1 86  ? -37.707 28.396  29.999  1.00 34.85 ? 86  TYR E CG  1 
ATOM   8466  C CD1 . TYR E 1 86  ? -38.578 28.725  28.962  1.00 33.94 ? 86  TYR E CD1 1 
ATOM   8467  C CD2 . TYR E 1 86  ? -38.117 27.431  30.922  1.00 33.81 ? 86  TYR E CD2 1 
ATOM   8468  C CE1 . TYR E 1 86  ? -39.823 28.126  28.851  1.00 33.11 ? 86  TYR E CE1 1 
ATOM   8469  C CE2 . TYR E 1 86  ? -39.366 26.827  30.821  1.00 33.56 ? 86  TYR E CE2 1 
ATOM   8470  C CZ  . TYR E 1 86  ? -40.217 27.183  29.779  1.00 33.62 ? 86  TYR E CZ  1 
ATOM   8471  O OH  . TYR E 1 86  ? -41.463 26.600  29.658  1.00 32.58 ? 86  TYR E OH  1 
ATOM   8472  N N   . ILE E 1 87  ? -36.727 32.142  29.760  1.00 35.64 ? 87  ILE E N   1 
ATOM   8473  C CA  . ILE E 1 87  ? -37.526 33.271  29.292  1.00 35.66 ? 87  ILE E CA  1 
ATOM   8474  C C   . ILE E 1 87  ? -38.181 32.922  27.954  1.00 35.84 ? 87  ILE E C   1 
ATOM   8475  O O   . ILE E 1 87  ? -37.550 32.323  27.086  1.00 35.74 ? 87  ILE E O   1 
ATOM   8476  C CB  . ILE E 1 87  ? -36.674 34.561  29.183  1.00 35.75 ? 87  ILE E CB  1 
ATOM   8477  C CG1 . ILE E 1 87  ? -36.211 35.003  30.576  1.00 35.73 ? 87  ILE E CG1 1 
ATOM   8478  C CG2 . ILE E 1 87  ? -37.456 35.694  28.502  1.00 35.48 ? 87  ILE E CG2 1 
ATOM   8479  C CD1 . ILE E 1 87  ? -34.943 35.822  30.584  1.00 35.72 ? 87  ILE E CD1 1 
ATOM   8480  N N   . VAL E 1 88  ? -39.456 33.280  27.811  1.00 36.07 ? 88  VAL E N   1 
ATOM   8481  C CA  . VAL E 1 88  ? -40.189 33.087  26.558  1.00 36.23 ? 88  VAL E CA  1 
ATOM   8482  C C   . VAL E 1 88  ? -40.517 34.444  25.937  1.00 36.48 ? 88  VAL E C   1 
ATOM   8483  O O   . VAL E 1 88  ? -41.124 35.293  26.586  1.00 36.45 ? 88  VAL E O   1 
ATOM   8484  C CB  . VAL E 1 88  ? -41.490 32.248  26.762  1.00 36.18 ? 88  VAL E CB  1 
ATOM   8485  C CG1 . VAL E 1 88  ? -42.350 32.228  25.494  1.00 35.43 ? 88  VAL E CG1 1 
ATOM   8486  C CG2 . VAL E 1 88  ? -41.151 30.831  27.176  1.00 35.91 ? 88  VAL E CG2 1 
ATOM   8487  N N   . GLU E 1 89  ? -40.100 34.638  24.686  1.00 36.90 ? 89  GLU E N   1 
ATOM   8488  C CA  . GLU E 1 89  ? -40.413 35.857  23.930  1.00 37.57 ? 89  GLU E CA  1 
ATOM   8489  C C   . GLU E 1 89  ? -41.102 35.519  22.600  1.00 37.90 ? 89  GLU E C   1 
ATOM   8490  O O   . GLU E 1 89  ? -40.760 34.531  21.956  1.00 38.16 ? 89  GLU E O   1 
ATOM   8491  C CB  . GLU E 1 89  ? -39.136 36.662  23.678  1.00 37.38 ? 89  GLU E CB  1 
ATOM   8492  C CG  . GLU E 1 89  ? -39.370 38.113  23.292  1.00 37.74 ? 89  GLU E CG  1 
ATOM   8493  C CD  . GLU E 1 89  ? -38.102 38.819  22.834  1.00 38.54 ? 89  GLU E CD  1 
ATOM   8494  O OE1 . GLU E 1 89  ? -37.940 40.016  23.164  1.00 39.18 ? 89  GLU E OE1 1 
ATOM   8495  O OE2 . GLU E 1 89  ? -37.269 38.187  22.145  1.00 38.22 ? 89  GLU E OE2 1 
ATOM   8496  N N   . LYS E 1 90  ? -42.073 36.331  22.195  1.00 38.39 ? 90  LYS E N   1 
ATOM   8497  C CA  . LYS E 1 90  ? -42.729 36.141  20.896  1.00 38.91 ? 90  LYS E CA  1 
ATOM   8498  C C   . LYS E 1 90  ? -41.820 36.568  19.739  1.00 39.31 ? 90  LYS E C   1 
ATOM   8499  O O   . LYS E 1 90  ? -40.802 37.236  19.957  1.00 39.38 ? 90  LYS E O   1 
ATOM   8500  C CB  . LYS E 1 90  ? -44.057 36.894  20.843  1.00 38.77 ? 90  LYS E CB  1 
ATOM   8501  C CG  . LYS E 1 90  ? -45.205 36.144  21.484  1.00 39.30 ? 90  LYS E CG  1 
ATOM   8502  C CD  . LYS E 1 90  ? -46.540 36.800  21.176  1.00 39.46 ? 90  LYS E CD  1 
ATOM   8503  C CE  . LYS E 1 90  ? -47.701 35.929  21.631  1.00 39.99 ? 90  LYS E CE  1 
ATOM   8504  N NZ  . LYS E 1 90  ? -47.827 35.870  23.111  1.00 40.55 ? 90  LYS E NZ  1 
ATOM   8505  N N   . ALA E 1 91  ? -42.183 36.173  18.518  1.00 39.66 ? 91  ALA E N   1 
ATOM   8506  C CA  . ALA E 1 91  ? -41.419 36.542  17.321  1.00 40.04 ? 91  ALA E CA  1 
ATOM   8507  C C   . ALA E 1 91  ? -41.493 38.045  17.031  1.00 40.31 ? 91  ALA E C   1 
ATOM   8508  O O   . ALA E 1 91  ? -40.495 38.659  16.640  1.00 40.33 ? 91  ALA E O   1 
ATOM   8509  C CB  . ALA E 1 91  ? -41.889 35.739  16.113  1.00 40.09 ? 91  ALA E CB  1 
ATOM   8510  N N   . SER E 1 92  ? -42.677 38.626  17.227  1.00 40.49 ? 92  SER E N   1 
ATOM   8511  C CA  . SER E 1 92  ? -42.874 40.064  17.077  1.00 40.69 ? 92  SER E CA  1 
ATOM   8512  C C   . SER E 1 92  ? -43.691 40.623  18.239  1.00 40.72 ? 92  SER E C   1 
ATOM   8513  O O   . SER E 1 92  ? -44.915 40.758  18.135  1.00 40.85 ? 92  SER E O   1 
ATOM   8514  C CB  . SER E 1 92  ? -43.553 40.382  15.745  1.00 40.66 ? 92  SER E CB  1 
ATOM   8515  O OG  . SER E 1 92  ? -42.766 39.917  14.668  1.00 41.57 ? 92  SER E OG  1 
ATOM   8516  N N   . PRO E 1 93  ? -43.016 40.940  19.360  1.00 40.70 ? 93  PRO E N   1 
ATOM   8517  C CA  . PRO E 1 93  ? -43.689 41.543  20.508  1.00 40.69 ? 93  PRO E CA  1 
ATOM   8518  C C   . PRO E 1 93  ? -44.216 42.936  20.154  1.00 40.97 ? 93  PRO E C   1 
ATOM   8519  O O   . PRO E 1 93  ? -43.527 43.702  19.474  1.00 41.18 ? 93  PRO E O   1 
ATOM   8520  C CB  . PRO E 1 93  ? -42.576 41.644  21.555  1.00 40.63 ? 93  PRO E CB  1 
ATOM   8521  C CG  . PRO E 1 93  ? -41.493 40.722  21.080  1.00 40.55 ? 93  PRO E CG  1 
ATOM   8522  C CD  . PRO E 1 93  ? -41.575 40.747  19.602  1.00 40.53 ? 93  PRO E CD  1 
ATOM   8523  N N   . ALA E 1 94  ? -45.429 43.254  20.601  1.00 40.98 ? 94  ALA E N   1 
ATOM   8524  C CA  . ALA E 1 94  ? -46.069 44.521  20.246  1.00 41.10 ? 94  ALA E CA  1 
ATOM   8525  C C   . ALA E 1 94  ? -45.454 45.711  20.981  1.00 41.20 ? 94  ALA E C   1 
ATOM   8526  O O   . ALA E 1 94  ? -45.329 46.800  20.417  1.00 41.22 ? 94  ALA E O   1 
ATOM   8527  C CB  . ALA E 1 94  ? -47.573 44.453  20.509  1.00 40.95 ? 94  ALA E CB  1 
ATOM   8528  N N   . ASN E 1 95  ? -45.072 45.488  22.237  1.00 41.09 ? 95  ASN E N   1 
ATOM   8529  C CA  . ASN E 1 95  ? -44.615 46.551  23.126  1.00 41.05 ? 95  ASN E CA  1 
ATOM   8530  C C   . ASN E 1 95  ? -43.089 46.576  23.271  1.00 40.96 ? 95  ASN E C   1 
ATOM   8531  O O   . ASN E 1 95  ? -42.517 45.824  24.068  1.00 40.86 ? 95  ASN E O   1 
ATOM   8532  C CB  . ASN E 1 95  ? -45.298 46.420  24.496  1.00 41.15 ? 95  ASN E CB  1 
ATOM   8533  C CG  . ASN E 1 95  ? -46.815 46.301  24.390  1.00 41.44 ? 95  ASN E CG  1 
ATOM   8534  O OD1 . ASN E 1 95  ? -47.484 47.194  23.870  1.00 42.45 ? 95  ASN E OD1 1 
ATOM   8535  N ND2 . ASN E 1 95  ? -47.362 45.199  24.890  1.00 40.95 ? 95  ASN E ND2 1 
ATOM   8536  N N   . ASP E 1 96  ? -42.359 47.340  22.428  1.00 39.72 ? 96  ASP E N   1 
ATOM   8537  C CA  . ASP E 1 96  ? -40.908 47.472  22.465  1.00 39.62 ? 96  ASP E CA  1 
ATOM   8538  C C   . ASP E 1 96  ? -40.258 48.786  22.878  1.00 39.65 ? 96  ASP E C   1 
ATOM   8539  O O   . ASP E 1 96  ? -39.867 48.958  24.033  1.00 39.51 ? 96  ASP E O   1 
ATOM   8540  C CB  . ASP E 1 96  ? -40.303 47.158  21.097  1.00 39.52 ? 96  ASP E CB  1 
ATOM   8541  C CG  . ASP E 1 96  ? -38.806 46.927  21.161  1.00 39.75 ? 96  ASP E CG  1 
ATOM   8542  O OD1 . ASP E 1 96  ? -38.338 46.321  22.147  1.00 40.04 ? 96  ASP E OD1 1 
ATOM   8543  O OD2 . ASP E 1 96  ? -38.097 47.352  20.224  1.00 39.60 ? 96  ASP E OD2 1 
ATOM   8544  N N   . LEU E 1 97  A -39.973 49.666  21.963  1.00 40.12 ? 96  LEU E N   1 
ATOM   8545  C CA  . LEU E 1 97  A -39.632 51.056  22.246  1.00 40.49 ? 96  LEU E CA  1 
ATOM   8546  C C   . LEU E 1 97  A -40.842 51.902  21.860  1.00 40.76 ? 96  LEU E C   1 
ATOM   8547  O O   . LEU E 1 97  A -41.002 52.268  20.688  1.00 40.47 ? 96  LEU E O   1 
ATOM   8548  C CB  . LEU E 1 97  A -38.393 51.518  21.466  1.00 40.34 ? 96  LEU E CB  1 
ATOM   8549  C CG  . LEU E 1 97  A -37.063 50.798  21.709  1.00 40.37 ? 96  LEU E CG  1 
ATOM   8550  C CD1 . LEU E 1 97  A -36.093 51.100  20.585  1.00 40.06 ? 96  LEU E CD1 1 
ATOM   8551  C CD2 . LEU E 1 97  A -36.453 51.156  23.053  1.00 39.58 ? 96  LEU E CD2 1 
ATOM   8552  N N   . CYS E 1 98  ? -41.675 52.191  22.849  1.00 41.56 ? 97  CYS E N   1 
ATOM   8553  C CA  . CYS E 1 98  ? -42.875 53.006  22.605  1.00 41.96 ? 97  CYS E CA  1 
ATOM   8554  C C   . CYS E 1 98  ? -42.492 54.333  21.943  1.00 41.53 ? 97  CYS E C   1 
ATOM   8555  O O   . CYS E 1 98  ? -43.031 54.683  20.892  1.00 41.51 ? 97  CYS E O   1 
ATOM   8556  C CB  . CYS E 1 98  ? -43.692 53.217  23.886  1.00 42.26 ? 97  CYS E CB  1 
ATOM   8557  S SG  . CYS E 1 98  ? -42.783 53.891  25.299  1.00 44.72 ? 97  CYS E SG  1 
ATOM   8558  N N   . TYR E 1 99  ? -41.541 55.044  22.549  1.00 41.03 ? 98  TYR E N   1 
ATOM   8559  C CA  . TYR E 1 99  ? -40.855 56.141  21.875  1.00 40.64 ? 98  TYR E CA  1 
ATOM   8560  C C   . TYR E 1 99  ? -39.754 55.548  20.986  1.00 40.42 ? 98  TYR E C   1 
ATOM   8561  O O   . TYR E 1 99  ? -38.875 54.849  21.480  1.00 40.55 ? 98  TYR E O   1 
ATOM   8562  C CB  . TYR E 1 99  ? -40.259 57.121  22.891  1.00 40.41 ? 98  TYR E CB  1 
ATOM   8563  C CG  . TYR E 1 99  ? -39.981 58.488  22.311  1.00 39.86 ? 98  TYR E CG  1 
ATOM   8564  C CD1 . TYR E 1 99  ? -40.829 59.564  22.572  1.00 39.15 ? 98  TYR E CD1 1 
ATOM   8565  C CD2 . TYR E 1 99  ? -38.873 58.708  21.490  1.00 39.42 ? 98  TYR E CD2 1 
ATOM   8566  C CE1 . TYR E 1 99  ? -40.576 60.829  22.032  1.00 38.50 ? 98  TYR E CE1 1 
ATOM   8567  C CE2 . TYR E 1 99  ? -38.615 59.962  20.944  1.00 38.80 ? 98  TYR E CE2 1 
ATOM   8568  C CZ  . TYR E 1 99  ? -39.469 61.016  21.220  1.00 38.30 ? 98  TYR E CZ  1 
ATOM   8569  O OH  . TYR E 1 99  ? -39.204 62.253  20.683  1.00 38.06 ? 98  TYR E OH  1 
ATOM   8570  N N   . PRO E 1 100 ? -39.799 55.822  19.670  1.00 40.21 ? 99  PRO E N   1 
ATOM   8571  C CA  . PRO E 1 100 ? -38.906 55.133  18.735  1.00 40.02 ? 99  PRO E CA  1 
ATOM   8572  C C   . PRO E 1 100 ? -37.424 55.399  18.991  1.00 40.08 ? 99  PRO E C   1 
ATOM   8573  O O   . PRO E 1 100 ? -37.070 56.413  19.602  1.00 40.31 ? 99  PRO E O   1 
ATOM   8574  C CB  . PRO E 1 100 ? -39.315 55.705  17.375  1.00 39.93 ? 99  PRO E CB  1 
ATOM   8575  C CG  . PRO E 1 100 ? -39.936 57.027  17.688  1.00 39.90 ? 99  PRO E CG  1 
ATOM   8576  C CD  . PRO E 1 100 ? -40.645 56.820  18.987  1.00 40.17 ? 99  PRO E CD  1 
ATOM   8577  N N   . GLY E 1 101 ? -36.570 54.492  18.523  1.00 39.86 ? 100 GLY E N   1 
ATOM   8578  C CA  . GLY E 1 101 ? -35.134 54.682  18.616  1.00 39.61 ? 100 GLY E CA  1 
ATOM   8579  C C   . GLY E 1 101 ? -34.325 53.404  18.585  1.00 39.62 ? 100 GLY E C   1 
ATOM   8580  O O   . GLY E 1 101 ? -34.724 52.429  17.943  1.00 39.64 ? 100 GLY E O   1 
ATOM   8581  N N   . ASP E 1 102 ? -33.187 53.417  19.285  1.00 39.29 ? 101 ASP E N   1 
ATOM   8582  C CA  . ASP E 1 102 ? -32.222 52.315  19.247  1.00 39.02 ? 101 ASP E CA  1 
ATOM   8583  C C   . ASP E 1 102 ? -31.808 51.851  20.640  1.00 38.39 ? 101 ASP E C   1 
ATOM   8584  O O   . ASP E 1 102 ? -31.700 52.653  21.574  1.00 38.34 ? 101 ASP E O   1 
ATOM   8585  C CB  . ASP E 1 102 ? -30.957 52.716  18.475  1.00 39.29 ? 101 ASP E CB  1 
ATOM   8586  C CG  . ASP E 1 102 ? -31.232 53.102  17.027  1.00 40.81 ? 101 ASP E CG  1 
ATOM   8587  O OD1 . ASP E 1 102 ? -32.258 52.677  16.450  1.00 41.80 ? 101 ASP E OD1 1 
ATOM   8588  O OD2 . ASP E 1 102 ? -30.394 53.837  16.454  1.00 43.14 ? 101 ASP E OD2 1 
ATOM   8589  N N   . PHE E 1 103 ? -31.566 50.549  20.759  1.00 37.53 ? 102 PHE E N   1 
ATOM   8590  C CA  . PHE E 1 103 ? -31.018 49.962  21.975  1.00 36.77 ? 102 PHE E CA  1 
ATOM   8591  C C   . PHE E 1 103 ? -29.620 49.447  21.653  1.00 36.06 ? 102 PHE E C   1 
ATOM   8592  O O   . PHE E 1 103 ? -29.467 48.444  20.959  1.00 35.63 ? 102 PHE E O   1 
ATOM   8593  C CB  . PHE E 1 103 ? -31.908 48.820  22.472  1.00 36.95 ? 102 PHE E CB  1 
ATOM   8594  C CG  . PHE E 1 103 ? -31.772 48.532  23.942  1.00 37.46 ? 102 PHE E CG  1 
ATOM   8595  C CD1 . PHE E 1 103 ? -32.893 48.535  24.763  1.00 37.92 ? 102 PHE E CD1 1 
ATOM   8596  C CD2 . PHE E 1 103 ? -30.528 48.253  24.510  1.00 37.89 ? 102 PHE E CD2 1 
ATOM   8597  C CE1 . PHE E 1 103 ? -32.784 48.265  26.127  1.00 38.16 ? 102 PHE E CE1 1 
ATOM   8598  C CE2 . PHE E 1 103 ? -30.409 47.987  25.870  1.00 38.36 ? 102 PHE E CE2 1 
ATOM   8599  C CZ  . PHE E 1 103 ? -31.539 47.993  26.680  1.00 38.57 ? 102 PHE E CZ  1 
ATOM   8600  N N   . ASN E 1 104 ? -28.608 50.149  22.153  1.00 35.39 ? 103 ASN E N   1 
ATOM   8601  C CA  . ASN E 1 104 ? -27.215 49.821  21.870  1.00 34.99 ? 103 ASN E CA  1 
ATOM   8602  C C   . ASN E 1 104 ? -26.832 48.455  22.429  1.00 34.30 ? 103 ASN E C   1 
ATOM   8603  O O   . ASN E 1 104 ? -27.122 48.153  23.587  1.00 34.29 ? 103 ASN E O   1 
ATOM   8604  C CB  . ASN E 1 104 ? -26.299 50.900  22.444  1.00 35.32 ? 103 ASN E CB  1 
ATOM   8605  C CG  . ASN E 1 104 ? -24.979 51.000  21.709  1.00 36.63 ? 103 ASN E CG  1 
ATOM   8606  O OD1 . ASN E 1 104 ? -24.916 51.520  20.589  1.00 37.49 ? 103 ASN E OD1 1 
ATOM   8607  N ND2 . ASN E 1 104 ? -23.908 50.521  22.345  1.00 37.27 ? 103 ASN E ND2 1 
ATOM   8608  N N   . ASN E 1 105 ? -26.202 47.631  21.591  1.00 33.54 ? 104 ASN E N   1 
ATOM   8609  C CA  . ASN E 1 105 ? -25.768 46.280  21.971  1.00 32.84 ? 104 ASN E CA  1 
ATOM   8610  C C   . ASN E 1 105 ? -26.878 45.409  22.575  1.00 32.47 ? 104 ASN E C   1 
ATOM   8611  O O   . ASN E 1 105 ? -26.664 44.695  23.557  1.00 31.92 ? 104 ASN E O   1 
ATOM   8612  C CB  . ASN E 1 105 ? -24.549 46.348  22.900  1.00 32.88 ? 104 ASN E CB  1 
ATOM   8613  C CG  . ASN E 1 105 ? -23.303 46.817  22.183  1.00 33.18 ? 104 ASN E CG  1 
ATOM   8614  O OD1 . ASN E 1 105 ? -22.790 47.904  22.454  1.00 33.97 ? 104 ASN E OD1 1 
ATOM   8615  N ND2 . ASN E 1 105 ? -22.818 46.009  21.246  1.00 33.12 ? 104 ASN E ND2 1 
ATOM   8616  N N   . TYR E 1 106 ? -28.057 45.472  21.957  1.00 32.22 ? 105 TYR E N   1 
ATOM   8617  C CA  . TYR E 1 106 ? -29.252 44.765  22.427  1.00 32.02 ? 105 TYR E CA  1 
ATOM   8618  C C   . TYR E 1 106 ? -29.089 43.243  22.463  1.00 31.94 ? 105 TYR E C   1 
ATOM   8619  O O   . TYR E 1 106 ? -29.543 42.593  23.403  1.00 31.87 ? 105 TYR E O   1 
ATOM   8620  C CB  . TYR E 1 106 ? -30.458 45.157  21.564  1.00 31.78 ? 105 TYR E CB  1 
ATOM   8621  C CG  . TYR E 1 106 ? -31.795 44.589  22.002  1.00 31.61 ? 105 TYR E CG  1 
ATOM   8622  C CD1 . TYR E 1 106 ? -32.307 44.842  23.277  1.00 31.39 ? 105 TYR E CD1 1 
ATOM   8623  C CD2 . TYR E 1 106 ? -32.568 43.829  21.123  1.00 31.41 ? 105 TYR E CD2 1 
ATOM   8624  C CE1 . TYR E 1 106 ? -33.541 44.328  23.673  1.00 31.06 ? 105 TYR E CE1 1 
ATOM   8625  C CE2 . TYR E 1 106 ? -33.805 43.316  21.507  1.00 31.46 ? 105 TYR E CE2 1 
ATOM   8626  C CZ  . TYR E 1 106 ? -34.286 43.571  22.779  1.00 31.67 ? 105 TYR E CZ  1 
ATOM   8627  O OH  . TYR E 1 106 ? -35.510 43.066  23.155  1.00 31.67 ? 105 TYR E OH  1 
ATOM   8628  N N   . GLU E 1 107 ? -28.441 42.688  21.442  1.00 31.89 ? 106 GLU E N   1 
ATOM   8629  C CA  . GLU E 1 107 ? -28.274 41.237  21.335  1.00 32.08 ? 106 GLU E CA  1 
ATOM   8630  C C   . GLU E 1 107 ? -27.276 40.692  22.363  1.00 31.92 ? 106 GLU E C   1 
ATOM   8631  O O   . GLU E 1 107 ? -27.459 39.592  22.877  1.00 31.80 ? 106 GLU E O   1 
ATOM   8632  C CB  . GLU E 1 107 ? -27.882 40.821  19.909  1.00 32.03 ? 106 GLU E CB  1 
ATOM   8633  C CG  . GLU E 1 107 ? -29.009 40.946  18.875  1.00 32.65 ? 106 GLU E CG  1 
ATOM   8634  C CD  . GLU E 1 107 ? -29.308 42.389  18.485  1.00 33.35 ? 106 GLU E CD  1 
ATOM   8635  O OE1 . GLU E 1 107 ? -28.361 43.209  18.433  1.00 33.77 ? 106 GLU E OE1 1 
ATOM   8636  O OE2 . GLU E 1 107 ? -30.492 42.702  18.233  1.00 33.21 ? 106 GLU E OE2 1 
ATOM   8637  N N   . GLU E 1 108 ? -26.235 41.466  22.660  1.00 31.92 ? 107 GLU E N   1 
ATOM   8638  C CA  . GLU E 1 108 ? -25.277 41.107  23.709  1.00 32.07 ? 107 GLU E CA  1 
ATOM   8639  C C   . GLU E 1 108 ? -25.931 41.090  25.097  1.00 32.28 ? 107 GLU E C   1 
ATOM   8640  O O   . GLU E 1 108 ? -25.600 40.250  25.935  1.00 32.25 ? 107 GLU E O   1 
ATOM   8641  C CB  . GLU E 1 108 ? -24.048 42.027  23.679  1.00 31.71 ? 107 GLU E CB  1 
ATOM   8642  C CG  . GLU E 1 108 ? -23.038 41.693  22.567  1.00 31.95 ? 107 GLU E CG  1 
ATOM   8643  C CD  . GLU E 1 108 ? -22.417 40.301  22.711  1.00 32.52 ? 107 GLU E CD  1 
ATOM   8644  O OE1 . GLU E 1 108 ? -21.869 39.993  23.797  1.00 33.44 ? 107 GLU E OE1 1 
ATOM   8645  O OE2 . GLU E 1 108 ? -22.472 39.514  21.739  1.00 31.70 ? 107 GLU E OE2 1 
ATOM   8646  N N   . LEU E 1 109 ? -26.875 42.002  25.319  1.00 32.60 ? 108 LEU E N   1 
ATOM   8647  C CA  . LEU E 1 109 ? -27.644 42.032  26.560  1.00 32.88 ? 108 LEU E CA  1 
ATOM   8648  C C   . LEU E 1 109 ? -28.597 40.844  26.643  1.00 32.95 ? 108 LEU E C   1 
ATOM   8649  O O   . LEU E 1 109 ? -28.775 40.261  27.710  1.00 33.22 ? 108 LEU E O   1 
ATOM   8650  C CB  . LEU E 1 109 ? -28.409 43.356  26.704  1.00 32.89 ? 108 LEU E CB  1 
ATOM   8651  C CG  . LEU E 1 109 ? -29.222 43.566  27.987  1.00 33.08 ? 108 LEU E CG  1 
ATOM   8652  C CD1 . LEU E 1 109 ? -28.382 43.321  29.240  1.00 33.30 ? 108 LEU E CD1 1 
ATOM   8653  C CD2 . LEU E 1 109 ? -29.811 44.960  28.009  1.00 34.03 ? 108 LEU E CD2 1 
ATOM   8654  N N   . LYS E 1 110 ? -29.200 40.495  25.512  1.00 33.17 ? 109 LYS E N   1 
ATOM   8655  C CA  . LYS E 1 110 ? -30.056 39.316  25.395  1.00 33.45 ? 109 LYS E CA  1 
ATOM   8656  C C   . LYS E 1 110 ? -29.285 38.048  25.801  1.00 33.59 ? 109 LYS E C   1 
ATOM   8657  O O   . LYS E 1 110 ? -29.819 37.173  26.484  1.00 33.50 ? 109 LYS E O   1 
ATOM   8658  C CB  . LYS E 1 110 ? -30.537 39.190  23.947  1.00 33.57 ? 109 LYS E CB  1 
ATOM   8659  C CG  . LYS E 1 110 ? -32.001 38.847  23.759  1.00 34.04 ? 109 LYS E CG  1 
ATOM   8660  C CD  . LYS E 1 110 ? -32.815 40.093  23.472  1.00 34.56 ? 109 LYS E CD  1 
ATOM   8661  C CE  . LYS E 1 110 ? -34.133 39.745  22.806  1.00 36.18 ? 109 LYS E CE  1 
ATOM   8662  N NZ  . LYS E 1 110 ? -33.974 39.463  21.344  1.00 37.38 ? 109 LYS E NZ  1 
ATOM   8663  N N   . HIS E 1 111 ? -28.024 37.965  25.375  1.00 33.87 ? 110 HIS E N   1 
ATOM   8664  C CA  . HIS E 1 111 ? -27.163 36.825  25.683  1.00 34.09 ? 110 HIS E CA  1 
ATOM   8665  C C   . HIS E 1 111 ? -26.793 36.754  27.166  1.00 34.46 ? 110 HIS E C   1 
ATOM   8666  O O   . HIS E 1 111 ? -26.812 35.677  27.766  1.00 34.32 ? 110 HIS E O   1 
ATOM   8667  C CB  . HIS E 1 111 ? -25.890 36.852  24.834  1.00 33.71 ? 110 HIS E CB  1 
ATOM   8668  C CG  . HIS E 1 111 ? -24.945 35.738  25.151  1.00 33.46 ? 110 HIS E CG  1 
ATOM   8669  N ND1 . HIS E 1 111 ? -23.910 35.873  26.053  1.00 33.30 ? 110 HIS E ND1 1 
ATOM   8670  C CD2 . HIS E 1 111 ? -24.901 34.457  24.716  1.00 32.60 ? 110 HIS E CD2 1 
ATOM   8671  C CE1 . HIS E 1 111 ? -23.261 34.726  26.149  1.00 32.84 ? 110 HIS E CE1 1 
ATOM   8672  N NE2 . HIS E 1 111 ? -23.842 33.852  25.347  1.00 32.51 ? 110 HIS E NE2 1 
ATOM   8673  N N   . LEU E 1 112 ? -26.443 37.900  27.745  1.00 35.00 ? 111 LEU E N   1 
ATOM   8674  C CA  . LEU E 1 112 ? -26.146 37.982  29.171  1.00 35.87 ? 111 LEU E CA  1 
ATOM   8675  C C   . LEU E 1 112 ? -27.371 37.543  29.971  1.00 36.20 ? 111 LEU E C   1 
ATOM   8676  O O   . LEU E 1 112 ? -27.255 36.857  30.988  1.00 36.26 ? 111 LEU E O   1 
ATOM   8677  C CB  . LEU E 1 112 ? -25.724 39.405  29.546  1.00 35.86 ? 111 LEU E CB  1 
ATOM   8678  C CG  . LEU E 1 112 ? -25.301 39.676  30.996  1.00 36.91 ? 111 LEU E CG  1 
ATOM   8679  C CD1 . LEU E 1 112 ? -24.218 40.758  31.045  1.00 37.04 ? 111 LEU E CD1 1 
ATOM   8680  C CD2 . LEU E 1 112 ? -26.501 40.059  31.880  1.00 37.34 ? 111 LEU E CD2 1 
ATOM   8681  N N   . LEU E 1 113 ? -28.542 37.932  29.480  1.00 36.69 ? 112 LEU E N   1 
ATOM   8682  C CA  . LEU E 1 113 ? -29.815 37.578  30.089  1.00 37.30 ? 112 LEU E CA  1 
ATOM   8683  C C   . LEU E 1 113 ? -30.078 36.071  30.067  1.00 37.43 ? 112 LEU E C   1 
ATOM   8684  O O   . LEU E 1 113 ? -30.738 35.543  30.960  1.00 37.55 ? 112 LEU E O   1 
ATOM   8685  C CB  . LEU E 1 113 ? -30.940 38.330  29.381  1.00 37.46 ? 112 LEU E CB  1 
ATOM   8686  C CG  . LEU E 1 113 ? -32.309 38.490  30.032  1.00 38.20 ? 112 LEU E CG  1 
ATOM   8687  C CD1 . LEU E 1 113 ? -32.217 39.192  31.378  1.00 38.05 ? 112 LEU E CD1 1 
ATOM   8688  C CD2 . LEU E 1 113 ? -33.206 39.272  29.081  1.00 38.68 ? 112 LEU E CD2 1 
ATOM   8689  N N   . SER E 1 114 ? -29.559 35.386  29.050  1.00 37.70 ? 113 SER E N   1 
ATOM   8690  C CA  . SER E 1 114 ? -29.662 33.930  28.964  1.00 37.99 ? 113 SER E CA  1 
ATOM   8691  C C   . SER E 1 114 ? -28.660 33.225  29.896  1.00 38.48 ? 113 SER E C   1 
ATOM   8692  O O   . SER E 1 114 ? -28.647 31.997  29.998  1.00 38.37 ? 113 SER E O   1 
ATOM   8693  C CB  . SER E 1 114 ? -29.493 33.459  27.514  1.00 37.82 ? 113 SER E CB  1 
ATOM   8694  O OG  . SER E 1 114 ? -28.170 33.665  27.046  1.00 37.53 ? 113 SER E OG  1 
ATOM   8695  N N   . ARG E 1 115 ? -27.831 34.017  30.570  1.00 39.13 ? 114 ARG E N   1 
ATOM   8696  C CA  . ARG E 1 115 ? -26.862 33.518  31.542  1.00 39.94 ? 114 ARG E CA  1 
ATOM   8697  C C   . ARG E 1 115 ? -27.293 33.882  32.965  1.00 40.16 ? 114 ARG E C   1 
ATOM   8698  O O   . ARG E 1 115 ? -26.497 33.825  33.905  1.00 40.30 ? 114 ARG E O   1 
ATOM   8699  C CB  . ARG E 1 115 ? -25.470 34.092  31.231  1.00 40.10 ? 114 ARG E CB  1 
ATOM   8700  C CG  . ARG E 1 115 ? -24.510 33.126  30.545  1.00 40.96 ? 114 ARG E CG  1 
ATOM   8701  C CD  . ARG E 1 115 ? -25.113 32.454  29.328  1.00 42.49 ? 114 ARG E CD  1 
ATOM   8702  N NE  . ARG E 1 115 ? -24.616 31.088  29.178  1.00 44.06 ? 114 ARG E NE  1 
ATOM   8703  C CZ  . ARG E 1 115 ? -25.356 29.989  29.315  1.00 44.59 ? 114 ARG E CZ  1 
ATOM   8704  N NH1 . ARG E 1 115 ? -26.652 30.074  29.594  1.00 45.07 ? 114 ARG E NH1 1 
ATOM   8705  N NH2 . ARG E 1 115 ? -24.798 28.797  29.159  1.00 44.82 ? 114 ARG E NH2 1 
ATOM   8706  N N   . THR E 1 116 ? -28.570 34.229  33.107  1.00 40.47 ? 115 THR E N   1 
ATOM   8707  C CA  . THR E 1 116 ? -29.123 34.792  34.335  1.00 40.77 ? 115 THR E CA  1 
ATOM   8708  C C   . THR E 1 116 ? -30.451 34.117  34.690  1.00 40.85 ? 115 THR E C   1 
ATOM   8709  O O   . THR E 1 116 ? -31.185 33.682  33.799  1.00 40.72 ? 115 THR E O   1 
ATOM   8710  C CB  . THR E 1 116 ? -29.355 36.303  34.148  1.00 40.80 ? 115 THR E CB  1 
ATOM   8711  O OG1 . THR E 1 116 ? -28.108 36.939  33.840  1.00 41.18 ? 115 THR E OG1 1 
ATOM   8712  C CG2 . THR E 1 116 ? -29.938 36.932  35.402  1.00 41.31 ? 115 THR E CG2 1 
ATOM   8713  N N   . ASN E 1 117 ? -30.760 34.038  35.985  1.00 41.11 ? 116 ASN E N   1 
ATOM   8714  C CA  . ASN E 1 117 ? -32.051 33.498  36.438  1.00 41.57 ? 116 ASN E CA  1 
ATOM   8715  C C   . ASN E 1 117 ? -32.935 34.481  37.221  1.00 41.93 ? 116 ASN E C   1 
ATOM   8716  O O   . ASN E 1 117 ? -34.142 34.266  37.341  1.00 41.92 ? 116 ASN E O   1 
ATOM   8717  C CB  . ASN E 1 117 ? -31.856 32.224  37.272  1.00 41.35 ? 116 ASN E CB  1 
ATOM   8718  C CG  . ASN E 1 117 ? -31.197 31.101  36.496  1.00 41.11 ? 116 ASN E CG  1 
ATOM   8719  O OD1 . ASN E 1 117 ? -30.013 30.821  36.679  1.00 41.89 ? 116 ASN E OD1 1 
ATOM   8720  N ND2 . ASN E 1 117 ? -31.961 30.446  35.633  1.00 40.42 ? 116 ASN E ND2 1 
ATOM   8721  N N   . HIS E 1 118 ? -32.341 35.542  37.765  1.00 42.49 ? 117 HIS E N   1 
ATOM   8722  C CA  . HIS E 1 118 ? -33.079 36.456  38.636  1.00 43.18 ? 117 HIS E CA  1 
ATOM   8723  C C   . HIS E 1 118 ? -32.548 37.890  38.634  1.00 43.43 ? 117 HIS E C   1 
ATOM   8724  O O   . HIS E 1 118 ? -31.351 38.126  38.811  1.00 43.27 ? 117 HIS E O   1 
ATOM   8725  C CB  . HIS E 1 118 ? -33.142 35.897  40.066  1.00 43.45 ? 117 HIS E CB  1 
ATOM   8726  C CG  . HIS E 1 118 ? -34.133 36.591  40.951  1.00 44.53 ? 117 HIS E CG  1 
ATOM   8727  N ND1 . HIS E 1 118 ? -35.315 37.122  40.477  1.00 45.97 ? 117 HIS E ND1 1 
ATOM   8728  C CD2 . HIS E 1 118 ? -34.129 36.817  42.286  1.00 45.59 ? 117 HIS E CD2 1 
ATOM   8729  C CE1 . HIS E 1 118 ? -35.986 37.663  41.478  1.00 46.33 ? 117 HIS E CE1 1 
ATOM   8730  N NE2 . HIS E 1 118 ? -35.287 37.494  42.587  1.00 46.51 ? 117 HIS E NE2 1 
ATOM   8731  N N   . PHE E 1 119 ? -33.472 38.830  38.432  1.00 43.91 ? 118 PHE E N   1 
ATOM   8732  C CA  . PHE E 1 119 ? -33.201 40.269  38.396  1.00 44.36 ? 118 PHE E CA  1 
ATOM   8733  C C   . PHE E 1 119 ? -33.977 40.966  39.512  1.00 44.73 ? 118 PHE E C   1 
ATOM   8734  O O   . PHE E 1 119 ? -35.211 41.032  39.473  1.00 44.82 ? 118 PHE E O   1 
ATOM   8735  C CB  . PHE E 1 119 ? -33.652 40.851  37.051  1.00 44.42 ? 118 PHE E CB  1 
ATOM   8736  C CG  . PHE E 1 119 ? -32.574 40.918  36.001  1.00 44.38 ? 118 PHE E CG  1 
ATOM   8737  C CD1 . PHE E 1 119 ? -31.383 40.221  36.138  1.00 44.17 ? 118 PHE E CD1 1 
ATOM   8738  C CD2 . PHE E 1 119 ? -32.777 41.669  34.849  1.00 44.56 ? 118 PHE E CD2 1 
ATOM   8739  C CE1 . PHE E 1 119 ? -30.405 40.288  35.155  1.00 44.33 ? 118 PHE E CE1 1 
ATOM   8740  C CE2 . PHE E 1 119 ? -31.805 41.743  33.862  1.00 44.71 ? 118 PHE E CE2 1 
ATOM   8741  C CZ  . PHE E 1 119 ? -30.615 41.047  34.016  1.00 44.67 ? 118 PHE E CZ  1 
ATOM   8742  N N   . GLU E 1 120 ? -33.259 41.479  40.506  1.00 45.01 ? 119 GLU E N   1 
ATOM   8743  C CA  . GLU E 1 120 ? -33.886 42.197  41.603  1.00 45.36 ? 119 GLU E CA  1 
ATOM   8744  C C   . GLU E 1 120 ? -33.775 43.693  41.330  1.00 45.47 ? 119 GLU E C   1 
ATOM   8745  O O   . GLU E 1 120 ? -32.677 44.240  41.223  1.00 45.49 ? 119 GLU E O   1 
ATOM   8746  C CB  . GLU E 1 120 ? -33.241 41.816  42.940  1.00 45.60 ? 119 GLU E CB  1 
ATOM   8747  C CG  . GLU E 1 120 ? -33.984 42.313  44.187  1.00 46.80 ? 119 GLU E CG  1 
ATOM   8748  C CD  . GLU E 1 120 ? -33.297 41.901  45.487  1.00 48.48 ? 119 GLU E CD  1 
ATOM   8749  O OE1 . GLU E 1 120 ? -33.152 40.680  45.730  1.00 48.36 ? 119 GLU E OE1 1 
ATOM   8750  O OE2 . GLU E 1 120 ? -32.906 42.801  46.268  1.00 49.13 ? 119 GLU E OE2 1 
ATOM   8751  N N   . LYS E 1 121 ? -34.923 44.346  41.206  1.00 45.57 ? 120 LYS E N   1 
ATOM   8752  C CA  . LYS E 1 121 ? -34.974 45.759  40.863  1.00 45.69 ? 120 LYS E CA  1 
ATOM   8753  C C   . LYS E 1 121 ? -34.711 46.631  42.084  1.00 45.71 ? 120 LYS E C   1 
ATOM   8754  O O   . LYS E 1 121 ? -35.312 46.426  43.143  1.00 45.51 ? 120 LYS E O   1 
ATOM   8755  C CB  . LYS E 1 121 ? -36.340 46.089  40.272  1.00 45.73 ? 120 LYS E CB  1 
ATOM   8756  C CG  . LYS E 1 121 ? -36.381 47.326  39.412  1.00 45.83 ? 120 LYS E CG  1 
ATOM   8757  C CD  . LYS E 1 121 ? -37.797 47.536  38.930  1.00 46.71 ? 120 LYS E CD  1 
ATOM   8758  C CE  . LYS E 1 121 ? -37.816 48.060  37.525  1.00 47.21 ? 120 LYS E CE  1 
ATOM   8759  N NZ  . LYS E 1 121 ? -39.122 47.777  36.871  1.00 47.71 ? 120 LYS E NZ  1 
ATOM   8760  N N   . ILE E 1 122 ? -33.805 47.594  41.935  1.00 45.84 ? 121 ILE E N   1 
ATOM   8761  C CA  . ILE E 1 122 ? -33.545 48.573  42.994  1.00 46.13 ? 121 ILE E CA  1 
ATOM   8762  C C   . ILE E 1 122 ? -33.501 49.995  42.457  1.00 46.16 ? 121 ILE E C   1 
ATOM   8763  O O   . ILE E 1 122 ? -33.099 50.228  41.316  1.00 46.00 ? 121 ILE E O   1 
ATOM   8764  C CB  . ILE E 1 122 ? -32.243 48.287  43.803  1.00 46.16 ? 121 ILE E CB  1 
ATOM   8765  C CG1 . ILE E 1 122 ? -31.014 48.234  42.891  1.00 46.36 ? 121 ILE E CG1 1 
ATOM   8766  C CG2 . ILE E 1 122 ? -32.382 47.012  44.643  1.00 46.62 ? 121 ILE E CG2 1 
ATOM   8767  C CD1 . ILE E 1 122 ? -29.741 48.708  43.576  1.00 47.08 ? 121 ILE E CD1 1 
ATOM   8768  N N   . GLN E 1 123 ? -33.928 50.937  43.293  1.00 46.39 ? 122 GLN E N   1 
ATOM   8769  C CA  . GLN E 1 123 ? -33.862 52.353  42.967  1.00 46.69 ? 122 GLN E CA  1 
ATOM   8770  C C   . GLN E 1 123 ? -32.439 52.835  43.209  1.00 46.67 ? 122 GLN E C   1 
ATOM   8771  O O   . GLN E 1 123 ? -31.851 52.535  44.250  1.00 46.89 ? 122 GLN E O   1 
ATOM   8772  C CB  . GLN E 1 123 ? -34.858 53.149  43.816  1.00 46.57 ? 122 GLN E CB  1 
ATOM   8773  C CG  . GLN E 1 123 ? -35.027 54.602  43.381  1.00 47.28 ? 122 GLN E CG  1 
ATOM   8774  C CD  . GLN E 1 123 ? -36.069 55.353  44.195  1.00 47.99 ? 122 GLN E CD  1 
ATOM   8775  O OE1 . GLN E 1 123 ? -35.991 55.417  45.423  1.00 47.80 ? 122 GLN E OE1 1 
ATOM   8776  N NE2 . GLN E 1 123 ? -37.047 55.936  43.507  1.00 48.10 ? 122 GLN E NE2 1 
ATOM   8777  N N   . ILE E 1 124 ? -31.882 53.558  42.243  1.00 46.68 ? 123 ILE E N   1 
ATOM   8778  C CA  . ILE E 1 124 ? -30.510 54.059  42.360  1.00 46.94 ? 123 ILE E CA  1 
ATOM   8779  C C   . ILE E 1 124 ? -30.445 55.586  42.307  1.00 47.27 ? 123 ILE E C   1 
ATOM   8780  O O   . ILE E 1 124 ? -29.553 56.192  42.904  1.00 47.35 ? 123 ILE E O   1 
ATOM   8781  C CB  . ILE E 1 124 ? -29.533 53.413  41.324  1.00 46.81 ? 123 ILE E CB  1 
ATOM   8782  C CG1 . ILE E 1 124 ? -30.008 53.639  39.882  1.00 46.84 ? 123 ILE E CG1 1 
ATOM   8783  C CG2 . ILE E 1 124 ? -29.363 51.925  41.606  1.00 46.51 ? 123 ILE E CG2 1 
ATOM   8784  C CD1 . ILE E 1 124 ? -28.910 53.510  38.842  1.00 46.63 ? 123 ILE E CD1 1 
ATOM   8785  N N   . ILE E 1 125 ? -31.384 56.194  41.583  1.00 47.61 ? 124 ILE E N   1 
ATOM   8786  C CA  . ILE E 1 125 ? -31.553 57.647  41.567  1.00 47.98 ? 124 ILE E CA  1 
ATOM   8787  C C   . ILE E 1 125 ? -33.050 57.983  41.641  1.00 48.44 ? 124 ILE E C   1 
ATOM   8788  O O   . ILE E 1 125 ? -33.754 57.912  40.626  1.00 48.62 ? 124 ILE E O   1 
ATOM   8789  C CB  . ILE E 1 125 ? -30.918 58.315  40.318  1.00 47.83 ? 124 ILE E CB  1 
ATOM   8790  C CG1 . ILE E 1 125 ? -29.480 57.829  40.094  1.00 47.78 ? 124 ILE E CG1 1 
ATOM   8791  C CG2 . ILE E 1 125 ? -30.966 59.840  40.452  1.00 47.92 ? 124 ILE E CG2 1 
ATOM   8792  C CD1 . ILE E 1 125 ? -28.833 58.323  38.808  1.00 47.28 ? 124 ILE E CD1 1 
ATOM   8793  N N   . PRO E 1 126 ? -33.540 58.346  42.844  1.00 48.84 ? 125 PRO E N   1 
ATOM   8794  C CA  . PRO E 1 126 ? -34.958 58.654  43.055  1.00 49.07 ? 125 PRO E CA  1 
ATOM   8795  C C   . PRO E 1 126 ? -35.433 59.785  42.155  1.00 49.42 ? 125 PRO E C   1 
ATOM   8796  O O   . PRO E 1 126 ? -34.675 60.731  41.911  1.00 49.67 ? 125 PRO E O   1 
ATOM   8797  C CB  . PRO E 1 126 ? -35.006 59.097  44.519  1.00 49.07 ? 125 PRO E CB  1 
ATOM   8798  C CG  . PRO E 1 126 ? -33.810 58.465  45.148  1.00 49.07 ? 125 PRO E CG  1 
ATOM   8799  C CD  . PRO E 1 126 ? -32.759 58.482  44.089  1.00 48.85 ? 125 PRO E CD  1 
ATOM   8800  N N   . LYS E 1 127 A -36.669 59.680  41.664  1.00 49.63 ? 125 LYS E N   1 
ATOM   8801  C CA  . LYS E 1 127 A -37.250 60.689  40.768  1.00 49.79 ? 125 LYS E CA  1 
ATOM   8802  C C   . LYS E 1 127 A -37.544 62.014  41.484  1.00 50.03 ? 125 LYS E C   1 
ATOM   8803  O O   . LYS E 1 127 A -37.502 63.083  40.870  1.00 50.09 ? 125 LYS E O   1 
ATOM   8804  C CB  . LYS E 1 127 A -38.511 60.143  40.087  1.00 49.81 ? 125 LYS E CB  1 
ATOM   8805  C CG  . LYS E 1 127 A -38.952 60.919  38.844  1.00 49.81 ? 125 LYS E CG  1 
ATOM   8806  C CD  . LYS E 1 127 A -39.626 60.022  37.812  1.00 49.50 ? 125 LYS E CD  1 
ATOM   8807  C CE  . LYS E 1 127 A -41.106 59.832  38.091  1.00 50.01 ? 125 LYS E CE  1 
ATOM   8808  N NZ  . LYS E 1 127 A -41.749 58.979  37.049  1.00 49.93 ? 125 LYS E NZ  1 
ATOM   8809  N N   . SER E 1 128 B -37.823 61.936  42.784  1.00 50.23 ? 125 SER E N   1 
ATOM   8810  C CA  . SER E 1 128 B -38.082 63.121  43.612  1.00 50.42 ? 125 SER E CA  1 
ATOM   8811  C C   . SER E 1 128 B -36.813 63.920  43.931  1.00 50.45 ? 125 SER E C   1 
ATOM   8812  O O   . SER E 1 128 B -36.879 64.969  44.578  1.00 50.38 ? 125 SER E O   1 
ATOM   8813  C CB  . SER E 1 128 B -38.762 62.706  44.919  1.00 50.44 ? 125 SER E CB  1 
ATOM   8814  O OG  . SER E 1 128 B -37.916 61.860  45.680  1.00 50.68 ? 125 SER E OG  1 
ATOM   8815  N N   . SER E 1 129 ? -35.666 63.418  43.474  1.00 50.42 ? 126 SER E N   1 
ATOM   8816  C CA  . SER E 1 129 ? -34.364 63.997  43.798  1.00 50.34 ? 126 SER E CA  1 
ATOM   8817  C C   . SER E 1 129 ? -33.918 65.095  42.822  1.00 50.25 ? 126 SER E C   1 
ATOM   8818  O O   . SER E 1 129 ? -32.874 65.725  43.019  1.00 50.22 ? 126 SER E O   1 
ATOM   8819  C CB  . SER E 1 129 ? -33.314 62.885  43.879  1.00 50.36 ? 126 SER E CB  1 
ATOM   8820  O OG  . SER E 1 129 ? -32.001 63.408  43.806  1.00 50.56 ? 126 SER E OG  1 
ATOM   8821  N N   . TRP E 1 130 ? -34.707 65.329  41.781  1.00 50.11 ? 127 TRP E N   1 
ATOM   8822  C CA  . TRP E 1 130 ? -34.348 66.313  40.768  1.00 50.12 ? 127 TRP E CA  1 
ATOM   8823  C C   . TRP E 1 130 ? -34.953 67.679  41.087  1.00 50.47 ? 127 TRP E C   1 
ATOM   8824  O O   . TRP E 1 130 ? -36.068 68.001  40.660  1.00 50.65 ? 127 TRP E O   1 
ATOM   8825  C CB  . TRP E 1 130 ? -34.753 65.821  39.377  1.00 49.93 ? 127 TRP E CB  1 
ATOM   8826  C CG  . TRP E 1 130 ? -34.091 64.529  38.997  1.00 48.97 ? 127 TRP E CG  1 
ATOM   8827  C CD1 . TRP E 1 130 ? -34.637 63.279  39.059  1.00 48.27 ? 127 TRP E CD1 1 
ATOM   8828  C CD2 . TRP E 1 130 ? -32.755 64.359  38.508  1.00 48.05 ? 127 TRP E CD2 1 
ATOM   8829  N NE1 . TRP E 1 130 ? -33.729 62.343  38.632  1.00 47.60 ? 127 TRP E NE1 1 
ATOM   8830  C CE2 . TRP E 1 130 ? -32.565 62.977  38.285  1.00 47.71 ? 127 TRP E CE2 1 
ATOM   8831  C CE3 . TRP E 1 130 ? -31.701 65.241  38.230  1.00 47.57 ? 127 TRP E CE3 1 
ATOM   8832  C CZ2 . TRP E 1 130 ? -31.360 62.453  37.800  1.00 46.97 ? 127 TRP E CZ2 1 
ATOM   8833  C CZ3 . TRP E 1 130 ? -30.505 64.719  37.747  1.00 47.30 ? 127 TRP E CZ3 1 
ATOM   8834  C CH2 . TRP E 1 130 ? -30.346 63.336  37.538  1.00 46.69 ? 127 TRP E CH2 1 
ATOM   8835  N N   . SER E 1 131 ? -34.196 68.475  41.838  1.00 50.70 ? 128 SER E N   1 
ATOM   8836  C CA  . SER E 1 131 ? -34.667 69.757  42.362  1.00 50.90 ? 128 SER E CA  1 
ATOM   8837  C C   . SER E 1 131 ? -34.672 70.864  41.311  1.00 51.13 ? 128 SER E C   1 
ATOM   8838  O O   . SER E 1 131 ? -35.580 71.697  41.283  1.00 51.17 ? 128 SER E O   1 
ATOM   8839  C CB  . SER E 1 131 ? -33.816 70.184  43.562  1.00 50.88 ? 128 SER E CB  1 
ATOM   8840  O OG  . SER E 1 131 ? -33.700 69.135  44.512  1.00 50.74 ? 128 SER E OG  1 
ATOM   8841  N N   . ASN E 1 132 ? -33.658 70.865  40.449  1.00 51.38 ? 129 ASN E N   1 
ATOM   8842  C CA  . ASN E 1 132 ? -33.470 71.938  39.478  1.00 51.56 ? 129 ASN E CA  1 
ATOM   8843  C C   . ASN E 1 132 ? -33.883 71.569  38.059  1.00 51.43 ? 129 ASN E C   1 
ATOM   8844  O O   . ASN E 1 132 ? -33.551 72.273  37.099  1.00 51.31 ? 129 ASN E O   1 
ATOM   8845  C CB  . ASN E 1 132 ? -32.021 72.431  39.510  1.00 51.89 ? 129 ASN E CB  1 
ATOM   8846  C CG  . ASN E 1 132 ? -31.762 73.413  40.642  1.00 52.86 ? 129 ASN E CG  1 
ATOM   8847  O OD1 . ASN E 1 132 ? -31.152 74.464  40.435  1.00 54.43 ? 129 ASN E OD1 1 
ATOM   8848  N ND2 . ASN E 1 132 ? -32.230 73.081  41.844  1.00 53.29 ? 129 ASN E ND2 1 
ATOM   8849  N N   . HIS E 1 133 ? -34.612 70.462  37.939  1.00 51.41 ? 130 HIS E N   1 
ATOM   8850  C CA  . HIS E 1 133 ? -35.102 69.983  36.652  1.00 51.27 ? 130 HIS E CA  1 
ATOM   8851  C C   . HIS E 1 133 ? -36.521 69.446  36.791  1.00 51.59 ? 130 HIS E C   1 
ATOM   8852  O O   . HIS E 1 133 ? -36.884 68.884  37.829  1.00 51.53 ? 130 HIS E O   1 
ATOM   8853  C CB  . HIS E 1 133 ? -34.174 68.899  36.089  1.00 51.00 ? 130 HIS E CB  1 
ATOM   8854  C CG  . HIS E 1 133 ? -32.765 69.360  35.873  1.00 50.08 ? 130 HIS E CG  1 
ATOM   8855  N ND1 . HIS E 1 133 ? -31.808 69.317  36.865  1.00 48.97 ? 130 HIS E ND1 1 
ATOM   8856  C CD2 . HIS E 1 133 ? -32.155 69.885  34.784  1.00 49.00 ? 130 HIS E CD2 1 
ATOM   8857  C CE1 . HIS E 1 133 ? -30.670 69.795  36.396  1.00 48.63 ? 130 HIS E CE1 1 
ATOM   8858  N NE2 . HIS E 1 133 ? -30.852 70.142  35.135  1.00 48.94 ? 130 HIS E NE2 1 
ATOM   8859  N N   . ASP E 1 134 ? -37.316 69.634  35.740  1.00 51.94 ? 131 ASP E N   1 
ATOM   8860  C CA  . ASP E 1 134 ? -38.669 69.094  35.673  1.00 52.16 ? 131 ASP E CA  1 
ATOM   8861  C C   . ASP E 1 134 ? -38.590 67.606  35.367  1.00 52.14 ? 131 ASP E C   1 
ATOM   8862  O O   . ASP E 1 134 ? -38.068 67.204  34.323  1.00 52.32 ? 131 ASP E O   1 
ATOM   8863  C CB  . ASP E 1 134 ? -39.486 69.823  34.600  1.00 52.28 ? 131 ASP E CB  1 
ATOM   8864  C CG  . ASP E 1 134 ? -40.962 69.425  34.597  1.00 52.92 ? 131 ASP E CG  1 
ATOM   8865  O OD1 . ASP E 1 134 ? -41.373 68.549  35.389  1.00 53.52 ? 131 ASP E OD1 1 
ATOM   8866  O OD2 . ASP E 1 134 ? -41.719 70.002  33.786  1.00 53.66 ? 131 ASP E OD2 1 
ATOM   8867  N N   . ALA E 1 135 ? -39.097 66.802  36.294  1.00 52.06 ? 132 ALA E N   1 
ATOM   8868  C CA  . ALA E 1 135 ? -39.107 65.353  36.160  1.00 51.96 ? 132 ALA E CA  1 
ATOM   8869  C C   . ALA E 1 135 ? -40.444 64.849  35.628  1.00 52.06 ? 132 ALA E C   1 
ATOM   8870  O O   . ALA E 1 135 ? -40.490 63.880  34.868  1.00 52.16 ? 132 ALA E O   1 
ATOM   8871  C CB  . ALA E 1 135 ? -38.800 64.704  37.497  1.00 51.90 ? 132 ALA E CB  1 
ATOM   8872  N N   . SER E 1 136 ? -41.522 65.534  36.005  1.00 52.00 ? 133 SER E N   1 
ATOM   8873  C CA  . SER E 1 136 ? -42.878 65.009  35.843  1.00 51.89 ? 133 SER E CA  1 
ATOM   8874  C C   . SER E 1 136 ? -43.540 65.218  34.476  1.00 51.53 ? 133 SER E C   1 
ATOM   8875  O O   . SER E 1 136 ? -44.471 64.489  34.137  1.00 51.68 ? 133 SER E O   1 
ATOM   8876  C CB  . SER E 1 136 ? -43.784 65.563  36.943  1.00 52.02 ? 133 SER E CB  1 
ATOM   8877  O OG  . SER E 1 136 ? -43.882 66.972  36.837  1.00 52.62 ? 133 SER E OG  1 
ATOM   8878  N N   . SER E 1 137 A -43.083 66.199  33.700  1.00 51.01 ? 133 SER E N   1 
ATOM   8879  C CA  . SER E 1 137 A -43.741 66.515  32.423  1.00 50.51 ? 133 SER E CA  1 
ATOM   8880  C C   . SER E 1 137 A -43.012 65.951  31.195  1.00 49.96 ? 133 SER E C   1 
ATOM   8881  O O   . SER E 1 137 A -43.246 66.393  30.066  1.00 49.86 ? 133 SER E O   1 
ATOM   8882  C CB  . SER E 1 137 A -43.974 68.027  32.280  1.00 50.60 ? 133 SER E CB  1 
ATOM   8883  O OG  . SER E 1 137 A -42.811 68.687  31.811  1.00 50.90 ? 133 SER E OG  1 
ATOM   8884  N N   . GLY E 1 138 ? -42.132 64.979  31.424  1.00 49.43 ? 134 GLY E N   1 
ATOM   8885  C CA  . GLY E 1 138 ? -41.404 64.317  30.344  1.00 48.61 ? 134 GLY E CA  1 
ATOM   8886  C C   . GLY E 1 138 ? -42.150 63.079  29.894  1.00 48.11 ? 134 GLY E C   1 
ATOM   8887  O O   . GLY E 1 138 ? -41.720 61.952  30.152  1.00 47.87 ? 134 GLY E O   1 
ATOM   8888  N N   . VAL E 1 139 ? -43.283 63.304  29.233  1.00 47.61 ? 135 VAL E N   1 
ATOM   8889  C CA  . VAL E 1 139 ? -44.158 62.232  28.764  1.00 47.15 ? 135 VAL E CA  1 
ATOM   8890  C C   . VAL E 1 139 ? -44.449 62.397  27.273  1.00 46.93 ? 135 VAL E C   1 
ATOM   8891  O O   . VAL E 1 139 ? -44.141 63.431  26.685  1.00 46.93 ? 135 VAL E O   1 
ATOM   8892  C CB  . VAL E 1 139 ? -45.484 62.153  29.582  1.00 47.23 ? 135 VAL E CB  1 
ATOM   8893  C CG1 . VAL E 1 139 ? -45.209 61.724  31.025  1.00 46.94 ? 135 VAL E CG1 1 
ATOM   8894  C CG2 . VAL E 1 139 ? -46.252 63.481  29.535  1.00 46.92 ? 135 VAL E CG2 1 
ATOM   8895  N N   . SER E 1 140 ? -45.037 61.374  26.662  1.00 46.70 ? 136 SER E N   1 
ATOM   8896  C CA  . SER E 1 140 ? -45.255 61.374  25.223  1.00 46.42 ? 136 SER E CA  1 
ATOM   8897  C C   . SER E 1 140 ? -46.511 60.601  24.877  1.00 46.48 ? 136 SER E C   1 
ATOM   8898  O O   . SER E 1 140 ? -46.883 59.664  25.582  1.00 46.51 ? 136 SER E O   1 
ATOM   8899  C CB  . SER E 1 140 ? -44.048 60.755  24.509  1.00 46.34 ? 136 SER E CB  1 
ATOM   8900  O OG  . SER E 1 140 ? -44.216 60.755  23.103  1.00 46.02 ? 136 SER E OG  1 
ATOM   8901  N N   . SER E 1 141 ? -47.159 60.998  23.786  1.00 46.61 ? 137 SER E N   1 
ATOM   8902  C CA  . SER E 1 141 ? -48.304 60.260  23.253  1.00 46.71 ? 137 SER E CA  1 
ATOM   8903  C C   . SER E 1 141 ? -47.863 58.929  22.629  1.00 46.88 ? 137 SER E C   1 
ATOM   8904  O O   . SER E 1 141 ? -48.678 58.025  22.436  1.00 46.88 ? 137 SER E O   1 
ATOM   8905  C CB  . SER E 1 141 ? -49.073 61.113  22.235  1.00 46.69 ? 137 SER E CB  1 
ATOM   8906  O OG  . SER E 1 141 ? -48.262 61.448  21.122  1.00 46.18 ? 137 SER E OG  1 
ATOM   8907  N N   . ALA E 1 142 ? -46.569 58.820  22.325  1.00 47.10 ? 138 ALA E N   1 
ATOM   8908  C CA  . ALA E 1 142 ? -45.972 57.586  21.807  1.00 47.32 ? 138 ALA E CA  1 
ATOM   8909  C C   . ALA E 1 142 ? -45.905 56.492  22.868  1.00 47.57 ? 138 ALA E C   1 
ATOM   8910  O O   . ALA E 1 142 ? -45.802 55.311  22.537  1.00 47.62 ? 138 ALA E O   1 
ATOM   8911  C CB  . ALA E 1 142 ? -44.591 57.861  21.260  1.00 47.16 ? 138 ALA E CB  1 
ATOM   8912  N N   . CYS E 1 143 ? -45.967 56.894  24.136  1.00 47.91 ? 139 CYS E N   1 
ATOM   8913  C CA  . CYS E 1 143 ? -45.924 55.959  25.252  1.00 48.37 ? 139 CYS E CA  1 
ATOM   8914  C C   . CYS E 1 143 ? -47.160 56.090  26.142  1.00 48.90 ? 139 CYS E C   1 
ATOM   8915  O O   . CYS E 1 143 ? -47.044 56.492  27.297  1.00 48.87 ? 139 CYS E O   1 
ATOM   8916  C CB  . CYS E 1 143 ? -44.651 56.173  26.083  1.00 48.12 ? 139 CYS E CB  1 
ATOM   8917  S SG  . CYS E 1 143 ? -43.104 55.917  25.179  1.00 47.95 ? 139 CYS E SG  1 
ATOM   8918  N N   . PRO E 1 144 ? -48.350 55.739  25.615  1.00 49.58 ? 140 PRO E N   1 
ATOM   8919  C CA  . PRO E 1 144 ? -49.554 55.887  26.438  1.00 50.11 ? 140 PRO E CA  1 
ATOM   8920  C C   . PRO E 1 144 ? -49.610 54.862  27.562  1.00 50.67 ? 140 PRO E C   1 
ATOM   8921  O O   . PRO E 1 144 ? -48.974 53.810  27.472  1.00 50.90 ? 140 PRO E O   1 
ATOM   8922  C CB  . PRO E 1 144 ? -50.691 55.641  25.444  1.00 50.11 ? 140 PRO E CB  1 
ATOM   8923  C CG  . PRO E 1 144 ? -50.099 54.757  24.403  1.00 49.88 ? 140 PRO E CG  1 
ATOM   8924  C CD  . PRO E 1 144 ? -48.652 55.144  24.297  1.00 49.63 ? 140 PRO E CD  1 
ATOM   8925  N N   . TYR E 1 145 ? -50.354 55.181  28.614  1.00 51.31 ? 141 TYR E N   1 
ATOM   8926  C CA  . TYR E 1 145 ? -50.604 54.236  29.693  1.00 52.13 ? 141 TYR E CA  1 
ATOM   8927  C C   . TYR E 1 145 ? -52.089 53.875  29.681  1.00 52.42 ? 141 TYR E C   1 
ATOM   8928  O O   . TYR E 1 145 ? -52.498 52.927  29.003  1.00 52.72 ? 141 TYR E O   1 
ATOM   8929  C CB  . TYR E 1 145 ? -50.151 54.820  31.040  1.00 52.26 ? 141 TYR E CB  1 
ATOM   8930  C CG  . TYR E 1 145 ? -50.403 53.952  32.264  1.00 53.15 ? 141 TYR E CG  1 
ATOM   8931  C CD1 . TYR E 1 145 ? -50.338 52.556  32.198  1.00 54.26 ? 141 TYR E CD1 1 
ATOM   8932  C CD2 . TYR E 1 145 ? -50.673 54.539  33.503  1.00 54.31 ? 141 TYR E CD2 1 
ATOM   8933  C CE1 . TYR E 1 145 ? -50.567 51.767  33.333  1.00 54.90 ? 141 TYR E CE1 1 
ATOM   8934  C CE2 . TYR E 1 145 ? -50.895 53.766  34.642  1.00 54.91 ? 141 TYR E CE2 1 
ATOM   8935  C CZ  . TYR E 1 145 ? -50.839 52.383  34.552  1.00 55.53 ? 141 TYR E CZ  1 
ATOM   8936  O OH  . TYR E 1 145 ? -51.062 51.624  35.683  1.00 56.39 ? 141 TYR E OH  1 
ATOM   8937  N N   . HIS E 1 146 ? -52.892 54.636  30.417  1.00 52.63 ? 142 HIS E N   1 
ATOM   8938  C CA  . HIS E 1 146 ? -54.337 54.476  30.377  1.00 52.68 ? 142 HIS E CA  1 
ATOM   8939  C C   . HIS E 1 146 ? -54.938 55.629  29.583  1.00 52.46 ? 142 HIS E C   1 
ATOM   8940  O O   . HIS E 1 146 ? -55.583 56.519  30.145  1.00 52.44 ? 142 HIS E O   1 
ATOM   8941  C CB  . HIS E 1 146 ? -54.913 54.398  31.793  1.00 52.89 ? 142 HIS E CB  1 
ATOM   8942  C CG  . HIS E 1 146 ? -54.549 53.141  32.524  1.00 53.68 ? 142 HIS E CG  1 
ATOM   8943  N ND1 . HIS E 1 146 ? -54.299 53.114  33.880  1.00 54.37 ? 142 HIS E ND1 1 
ATOM   8944  C CD2 . HIS E 1 146 ? -54.384 51.868  32.087  1.00 54.04 ? 142 HIS E CD2 1 
ATOM   8945  C CE1 . HIS E 1 146 ? -54.001 51.880  34.247  1.00 54.44 ? 142 HIS E CE1 1 
ATOM   8946  N NE2 . HIS E 1 146 ? -54.045 51.105  33.178  1.00 54.56 ? 142 HIS E NE2 1 
ATOM   8947  N N   . GLY E 1 147 ? -54.693 55.611  28.271  1.00 52.14 ? 143 GLY E N   1 
ATOM   8948  C CA  . GLY E 1 147 ? -55.117 56.683  27.368  1.00 51.66 ? 143 GLY E CA  1 
ATOM   8949  C C   . GLY E 1 147 ? -54.469 58.035  27.643  1.00 51.33 ? 143 GLY E C   1 
ATOM   8950  O O   . GLY E 1 147 ? -54.931 59.060  27.141  1.00 51.45 ? 143 GLY E O   1 
ATOM   8951  N N   . LYS E 1 148 ? -53.399 58.038  28.438  1.00 50.86 ? 144 LYS E N   1 
ATOM   8952  C CA  . LYS E 1 148 ? -52.729 59.275  28.834  1.00 50.21 ? 144 LYS E CA  1 
ATOM   8953  C C   . LYS E 1 148 ? -51.233 59.185  28.562  1.00 49.33 ? 144 LYS E C   1 
ATOM   8954  O O   . LYS E 1 148 ? -50.635 58.125  28.736  1.00 49.18 ? 144 LYS E O   1 
ATOM   8955  C CB  . LYS E 1 148 ? -52.970 59.552  30.317  1.00 50.50 ? 144 LYS E CB  1 
ATOM   8956  C CG  . LYS E 1 148 ? -53.445 60.969  30.616  1.00 51.49 ? 144 LYS E CG  1 
ATOM   8957  C CD  . LYS E 1 148 ? -53.608 61.205  32.121  1.00 52.96 ? 144 LYS E CD  1 
ATOM   8958  C CE  . LYS E 1 148 ? -54.900 61.971  32.448  1.00 53.71 ? 144 LYS E CE  1 
ATOM   8959  N NZ  . LYS E 1 148 ? -55.124 63.194  31.609  1.00 53.99 ? 144 LYS E NZ  1 
ATOM   8960  N N   . SER E 1 149 ? -50.642 60.300  28.135  1.00 48.41 ? 145 SER E N   1 
ATOM   8961  C CA  . SER E 1 149 ? -49.206 60.370  27.859  1.00 47.51 ? 145 SER E CA  1 
ATOM   8962  C C   . SER E 1 149 ? -48.352 59.915  29.047  1.00 46.96 ? 145 SER E C   1 
ATOM   8963  O O   . SER E 1 149 ? -48.511 60.404  30.166  1.00 46.97 ? 145 SER E O   1 
ATOM   8964  C CB  . SER E 1 149 ? -48.810 61.781  27.431  1.00 47.43 ? 145 SER E CB  1 
ATOM   8965  O OG  . SER E 1 149 ? -49.177 62.027  26.090  1.00 47.35 ? 145 SER E OG  1 
ATOM   8966  N N   . SER E 1 150 ? -47.462 58.961  28.791  1.00 46.17 ? 146 SER E N   1 
ATOM   8967  C CA  . SER E 1 150 ? -46.582 58.415  29.817  1.00 45.45 ? 146 SER E CA  1 
ATOM   8968  C C   . SER E 1 150 ? -45.173 58.223  29.246  1.00 45.03 ? 146 SER E C   1 
ATOM   8969  O O   . SER E 1 150 ? -44.814 58.842  28.234  1.00 44.93 ? 146 SER E O   1 
ATOM   8970  C CB  . SER E 1 150 ? -47.154 57.097  30.352  1.00 45.52 ? 146 SER E CB  1 
ATOM   8971  O OG  . SER E 1 150 ? -46.527 56.707  31.561  1.00 45.44 ? 146 SER E OG  1 
ATOM   8972  N N   . PHE E 1 151 ? -44.377 57.377  29.898  1.00 44.35 ? 147 PHE E N   1 
ATOM   8973  C CA  . PHE E 1 151 ? -42.994 57.133  29.493  1.00 43.77 ? 147 PHE E CA  1 
ATOM   8974  C C   . PHE E 1 151 ? -42.487 55.840  30.114  1.00 43.52 ? 147 PHE E C   1 
ATOM   8975  O O   . PHE E 1 151 ? -43.167 55.243  30.953  1.00 43.37 ? 147 PHE E O   1 
ATOM   8976  C CB  . PHE E 1 151 ? -42.098 58.314  29.905  1.00 43.63 ? 147 PHE E CB  1 
ATOM   8977  C CG  . PHE E 1 151 ? -40.777 58.361  29.185  1.00 42.91 ? 147 PHE E CG  1 
ATOM   8978  C CD1 . PHE E 1 151 ? -40.723 58.571  27.811  1.00 42.63 ? 147 PHE E CD1 1 
ATOM   8979  C CD2 . PHE E 1 151 ? -39.585 58.208  29.887  1.00 42.70 ? 147 PHE E CD2 1 
ATOM   8980  C CE1 . PHE E 1 151 ? -39.499 58.616  27.142  1.00 42.53 ? 147 PHE E CE1 1 
ATOM   8981  C CE2 . PHE E 1 151 ? -38.359 58.251  29.232  1.00 42.13 ? 147 PHE E CE2 1 
ATOM   8982  C CZ  . PHE E 1 151 ? -38.315 58.454  27.857  1.00 42.44 ? 147 PHE E CZ  1 
ATOM   8983  N N   . PHE E 1 152 ? -41.306 55.402  29.678  1.00 43.25 ? 148 PHE E N   1 
ATOM   8984  C CA  . PHE E 1 152 ? -40.601 54.282  30.294  1.00 43.00 ? 148 PHE E CA  1 
ATOM   8985  C C   . PHE E 1 152 ? -40.477 54.522  31.795  1.00 43.16 ? 148 PHE E C   1 
ATOM   8986  O O   . PHE E 1 152 ? -40.063 55.600  32.226  1.00 43.23 ? 148 PHE E O   1 
ATOM   8987  C CB  . PHE E 1 152 ? -39.204 54.121  29.686  1.00 42.83 ? 148 PHE E CB  1 
ATOM   8988  C CG  . PHE E 1 152 ? -39.198 53.887  28.200  1.00 41.93 ? 148 PHE E CG  1 
ATOM   8989  C CD1 . PHE E 1 152 ? -39.572 52.654  27.671  1.00 41.36 ? 148 PHE E CD1 1 
ATOM   8990  C CD2 . PHE E 1 152 ? -38.788 54.891  27.330  1.00 41.23 ? 148 PHE E CD2 1 
ATOM   8991  C CE1 . PHE E 1 152 ? -39.558 52.430  26.297  1.00 41.11 ? 148 PHE E CE1 1 
ATOM   8992  C CE2 . PHE E 1 152 ? -38.767 54.679  25.956  1.00 41.40 ? 148 PHE E CE2 1 
ATOM   8993  C CZ  . PHE E 1 152 ? -39.153 53.444  25.437  1.00 41.30 ? 148 PHE E CZ  1 
ATOM   8994  N N   . ARG E 1 153 ? -40.833 53.514  32.584  1.00 43.37 ? 149 ARG E N   1 
ATOM   8995  C CA  . ARG E 1 153 ? -40.915 53.662  34.040  1.00 43.71 ? 149 ARG E CA  1 
ATOM   8996  C C   . ARG E 1 153 ? -39.571 53.651  34.767  1.00 43.72 ? 149 ARG E C   1 
ATOM   8997  O O   . ARG E 1 153 ? -39.464 54.155  35.887  1.00 44.06 ? 149 ARG E O   1 
ATOM   8998  C CB  . ARG E 1 153 ? -41.822 52.584  34.636  1.00 43.71 ? 149 ARG E CB  1 
ATOM   8999  C CG  . ARG E 1 153 ? -43.270 52.690  34.206  1.00 44.61 ? 149 ARG E CG  1 
ATOM   9000  C CD  . ARG E 1 153 ? -44.198 52.176  35.300  1.00 46.72 ? 149 ARG E CD  1 
ATOM   9001  N NE  . ARG E 1 153 ? -45.585 52.100  34.851  1.00 47.70 ? 149 ARG E NE  1 
ATOM   9002  C CZ  . ARG E 1 153 ? -46.404 53.143  34.740  1.00 48.74 ? 149 ARG E CZ  1 
ATOM   9003  N NH1 . ARG E 1 153 ? -45.989 54.370  35.041  1.00 48.28 ? 149 ARG E NH1 1 
ATOM   9004  N NH2 . ARG E 1 153 ? -47.647 52.955  34.315  1.00 49.55 ? 149 ARG E NH2 1 
ATOM   9005  N N   . ASN E 1 154 ? -38.555 53.069  34.140  1.00 43.64 ? 150 ASN E N   1 
ATOM   9006  C CA  . ASN E 1 154 ? -37.275 52.866  34.803  1.00 43.59 ? 150 ASN E CA  1 
ATOM   9007  C C   . ASN E 1 154 ? -36.240 53.948  34.505  1.00 43.65 ? 150 ASN E C   1 
ATOM   9008  O O   . ASN E 1 154 ? -35.182 53.986  35.134  1.00 43.66 ? 150 ASN E O   1 
ATOM   9009  C CB  . ASN E 1 154 ? -36.730 51.475  34.479  1.00 43.58 ? 150 ASN E CB  1 
ATOM   9010  C CG  . ASN E 1 154 ? -37.686 50.368  34.890  1.00 43.80 ? 150 ASN E CG  1 
ATOM   9011  O OD1 . ASN E 1 154 ? -38.532 50.552  35.763  1.00 43.92 ? 150 ASN E OD1 1 
ATOM   9012  N ND2 . ASN E 1 154 ? -37.554 49.209  34.260  1.00 44.69 ? 150 ASN E ND2 1 
ATOM   9013  N N   . VAL E 1 155 ? -36.555 54.827  33.556  1.00 43.51 ? 151 VAL E N   1 
ATOM   9014  C CA  . VAL E 1 155 ? -35.685 55.957  33.221  1.00 43.41 ? 151 VAL E CA  1 
ATOM   9015  C C   . VAL E 1 155 ? -36.455 57.278  33.213  1.00 43.53 ? 151 VAL E C   1 
ATOM   9016  O O   . VAL E 1 155 ? -37.662 57.298  32.985  1.00 43.64 ? 151 VAL E O   1 
ATOM   9017  C CB  . VAL E 1 155 ? -34.938 55.758  31.868  1.00 43.38 ? 151 VAL E CB  1 
ATOM   9018  C CG1 . VAL E 1 155 ? -33.866 54.676  31.996  1.00 43.13 ? 151 VAL E CG1 1 
ATOM   9019  C CG2 . VAL E 1 155 ? -35.912 55.449  30.728  1.00 43.04 ? 151 VAL E CG2 1 
ATOM   9020  N N   . VAL E 1 156 ? -35.747 58.378  33.455  1.00 43.79 ? 152 VAL E N   1 
ATOM   9021  C CA  . VAL E 1 156 ? -36.376 59.688  33.616  1.00 43.87 ? 152 VAL E CA  1 
ATOM   9022  C C   . VAL E 1 156 ? -35.994 60.641  32.483  1.00 43.98 ? 152 VAL E C   1 
ATOM   9023  O O   . VAL E 1 156 ? -34.813 60.881  32.231  1.00 43.88 ? 152 VAL E O   1 
ATOM   9024  C CB  . VAL E 1 156 ? -36.034 60.318  34.994  1.00 43.85 ? 152 VAL E CB  1 
ATOM   9025  C CG1 . VAL E 1 156 ? -36.868 61.569  35.239  1.00 44.17 ? 152 VAL E CG1 1 
ATOM   9026  C CG2 . VAL E 1 156 ? -36.265 59.311  36.120  1.00 43.79 ? 152 VAL E CG2 1 
ATOM   9027  N N   . TRP E 1 157 ? -37.008 61.172  31.804  1.00 44.28 ? 153 TRP E N   1 
ATOM   9028  C CA  . TRP E 1 157 ? -36.813 62.137  30.722  1.00 44.67 ? 153 TRP E CA  1 
ATOM   9029  C C   . TRP E 1 157 ? -36.868 63.570  31.257  1.00 45.15 ? 153 TRP E C   1 
ATOM   9030  O O   . TRP E 1 157 ? -37.906 64.227  31.189  1.00 45.34 ? 153 TRP E O   1 
ATOM   9031  C CB  . TRP E 1 157 ? -37.861 61.915  29.625  1.00 44.40 ? 153 TRP E CB  1 
ATOM   9032  C CG  . TRP E 1 157 ? -37.746 62.822  28.423  1.00 43.85 ? 153 TRP E CG  1 
ATOM   9033  C CD1 . TRP E 1 157 ? -36.744 63.713  28.148  1.00 43.77 ? 153 TRP E CD1 1 
ATOM   9034  C CD2 . TRP E 1 157 ? -38.651 62.887  27.316  1.00 43.27 ? 153 TRP E CD2 1 
ATOM   9035  N NE1 . TRP E 1 157 ? -36.983 64.342  26.948  1.00 43.20 ? 153 TRP E NE1 1 
ATOM   9036  C CE2 . TRP E 1 157 ? -38.146 63.852  26.416  1.00 43.07 ? 153 TRP E CE2 1 
ATOM   9037  C CE3 . TRP E 1 157 ? -39.847 62.229  26.999  1.00 42.81 ? 153 TRP E CE3 1 
ATOM   9038  C CZ2 . TRP E 1 157 ? -38.795 64.175  25.222  1.00 42.83 ? 153 TRP E CZ2 1 
ATOM   9039  C CZ3 . TRP E 1 157 ? -40.491 62.553  25.813  1.00 42.47 ? 153 TRP E CZ3 1 
ATOM   9040  C CH2 . TRP E 1 157 ? -39.961 63.515  24.939  1.00 42.64 ? 153 TRP E CH2 1 
ATOM   9041  N N   . LEU E 1 158 ? -35.741 64.049  31.778  1.00 45.59 ? 154 LEU E N   1 
ATOM   9042  C CA  . LEU E 1 158 ? -35.676 65.355  32.432  1.00 45.94 ? 154 LEU E CA  1 
ATOM   9043  C C   . LEU E 1 158 ? -35.851 66.516  31.456  1.00 46.45 ? 154 LEU E C   1 
ATOM   9044  O O   . LEU E 1 158 ? -35.235 66.548  30.386  1.00 46.45 ? 154 LEU E O   1 
ATOM   9045  C CB  . LEU E 1 158 ? -34.364 65.512  33.207  1.00 45.80 ? 154 LEU E CB  1 
ATOM   9046  C CG  . LEU E 1 158 ? -34.052 64.491  34.307  1.00 45.68 ? 154 LEU E CG  1 
ATOM   9047  C CD1 . LEU E 1 158 ? -32.568 64.487  34.631  1.00 45.05 ? 154 LEU E CD1 1 
ATOM   9048  C CD2 . LEU E 1 158 ? -34.877 64.743  35.559  1.00 45.33 ? 154 LEU E CD2 1 
ATOM   9049  N N   . ILE E 1 159 ? -36.700 67.465  31.843  1.00 46.97 ? 155 ILE E N   1 
ATOM   9050  C CA  . ILE E 1 159 ? -36.933 68.678  31.061  1.00 47.57 ? 155 ILE E CA  1 
ATOM   9051  C C   . ILE E 1 159 ? -36.489 69.897  31.876  1.00 47.82 ? 155 ILE E C   1 
ATOM   9052  O O   . ILE E 1 159 ? -36.432 69.837  33.107  1.00 47.96 ? 155 ILE E O   1 
ATOM   9053  C CB  . ILE E 1 159 ? -38.440 68.817  30.660  1.00 47.71 ? 155 ILE E CB  1 
ATOM   9054  C CG1 . ILE E 1 159 ? -39.013 67.485  30.138  1.00 47.83 ? 155 ILE E CG1 1 
ATOM   9055  C CG2 . ILE E 1 159 ? -38.651 69.951  29.646  1.00 47.63 ? 155 ILE E CG2 1 
ATOM   9056  C CD1 . ILE E 1 159 ? -38.433 67.004  28.803  1.00 47.55 ? 155 ILE E CD1 1 
ATOM   9057  N N   . LYS E 1 160 ? -36.168 70.987  31.181  1.00 48.18 ? 156 LYS E N   1 
ATOM   9058  C CA  . LYS E 1 160 ? -35.842 72.277  31.802  1.00 48.54 ? 156 LYS E CA  1 
ATOM   9059  C C   . LYS E 1 160 ? -36.908 72.785  32.791  1.00 49.04 ? 156 LYS E C   1 
ATOM   9060  O O   . LYS E 1 160 ? -38.103 72.539  32.614  1.00 49.21 ? 156 LYS E O   1 
ATOM   9061  C CB  . LYS E 1 160 ? -35.588 73.335  30.721  1.00 48.34 ? 156 LYS E CB  1 
ATOM   9062  C CG  . LYS E 1 160 ? -36.835 73.793  29.971  1.00 47.73 ? 156 LYS E CG  1 
ATOM   9063  C CD  . LYS E 1 160 ? -36.512 74.918  29.005  1.00 47.49 ? 156 LYS E CD  1 
ATOM   9064  C CE  . LYS E 1 160 ? -37.779 75.552  28.458  1.00 46.95 ? 156 LYS E CE  1 
ATOM   9065  N NZ  . LYS E 1 160 ? -37.505 76.284  27.194  1.00 46.46 ? 156 LYS E NZ  1 
ATOM   9066  N N   . LYS E 1 161 ? -36.456 73.490  33.828  1.00 49.59 ? 157 LYS E N   1 
ATOM   9067  C CA  . LYS E 1 161 ? -37.336 74.073  34.846  1.00 50.07 ? 157 LYS E CA  1 
ATOM   9068  C C   . LYS E 1 161 ? -37.108 75.580  34.918  1.00 50.21 ? 157 LYS E C   1 
ATOM   9069  O O   . LYS E 1 161 ? -35.965 76.027  35.067  1.00 50.50 ? 157 LYS E O   1 
ATOM   9070  C CB  . LYS E 1 161 ? -37.056 73.447  36.212  1.00 50.21 ? 157 LYS E CB  1 
ATOM   9071  C CG  . LYS E 1 161 ? -37.977 73.929  37.319  1.00 51.24 ? 157 LYS E CG  1 
ATOM   9072  C CD  . LYS E 1 161 ? -37.423 73.605  38.697  1.00 52.47 ? 157 LYS E CD  1 
ATOM   9073  C CE  . LYS E 1 161 ? -38.364 74.097  39.787  1.00 53.27 ? 157 LYS E CE  1 
ATOM   9074  N NZ  . LYS E 1 161 ? -37.749 74.009  41.141  1.00 54.00 ? 157 LYS E NZ  1 
ATOM   9075  N N   . ASN E 1 162 ? -38.193 76.352  34.819  1.00 50.20 ? 158 ASN E N   1 
ATOM   9076  C CA  . ASN E 1 162 ? -38.128 77.822  34.814  1.00 50.11 ? 158 ASN E CA  1 
ATOM   9077  C C   . ASN E 1 162 ? -37.076 78.363  33.845  1.00 50.01 ? 158 ASN E C   1 
ATOM   9078  O O   . ASN E 1 162 ? -36.144 79.073  34.245  1.00 50.16 ? 158 ASN E O   1 
ATOM   9079  C CB  . ASN E 1 162 ? -37.914 78.373  36.231  1.00 50.08 ? 158 ASN E CB  1 
ATOM   9080  C CG  . ASN E 1 162 ? -39.194 78.406  37.042  1.00 50.51 ? 158 ASN E CG  1 
ATOM   9081  O OD1 . ASN E 1 162 ? -39.348 77.667  38.016  1.00 50.43 ? 158 ASN E OD1 1 
ATOM   9082  N ND2 . ASN E 1 162 ? -40.132 79.262  36.634  1.00 51.41 ? 158 ASN E ND2 1 
ATOM   9083  N N   . SER E 1 163 ? -37.239 78.002  32.573  1.00 49.73 ? 159 SER E N   1 
ATOM   9084  C CA  . SER E 1 163 ? -36.302 78.345  31.492  1.00 49.46 ? 159 SER E CA  1 
ATOM   9085  C C   . SER E 1 163 ? -34.826 78.042  31.792  1.00 49.09 ? 159 SER E C   1 
ATOM   9086  O O   . SER E 1 163 ? -33.923 78.700  31.264  1.00 49.20 ? 159 SER E O   1 
ATOM   9087  C CB  . SER E 1 163 ? -36.499 79.794  31.029  1.00 49.61 ? 159 SER E CB  1 
ATOM   9088  O OG  . SER E 1 163 ? -37.522 79.862  30.049  1.00 50.00 ? 159 SER E OG  1 
ATOM   9089  N N   . ALA E 1 164 ? -34.585 77.031  32.624  1.00 48.59 ? 160 ALA E N   1 
ATOM   9090  C CA  . ALA E 1 164 ? -33.224 76.682  33.017  1.00 47.92 ? 160 ALA E CA  1 
ATOM   9091  C C   . ALA E 1 164 ? -32.974 75.180  33.015  1.00 47.40 ? 160 ALA E C   1 
ATOM   9092  O O   . ALA E 1 164 ? -33.812 74.392  33.461  1.00 47.08 ? 160 ALA E O   1 
ATOM   9093  C CB  . ALA E 1 164 ? -32.894 77.278  34.384  1.00 48.07 ? 160 ALA E CB  1 
ATOM   9094  N N   . TYR E 1 165 ? -31.813 74.799  32.491  1.00 46.78 ? 161 TYR E N   1 
ATOM   9095  C CA  . TYR E 1 165 ? -31.325 73.431  32.595  1.00 46.26 ? 161 TYR E CA  1 
ATOM   9096  C C   . TYR E 1 165 ? -29.877 73.479  33.080  1.00 45.83 ? 161 TYR E C   1 
ATOM   9097  O O   . TYR E 1 165 ? -28.948 73.516  32.267  1.00 45.89 ? 161 TYR E O   1 
ATOM   9098  C CB  . TYR E 1 165 ? -31.436 72.702  31.253  1.00 46.03 ? 161 TYR E CB  1 
ATOM   9099  C CG  . TYR E 1 165 ? -31.384 71.185  31.343  1.00 46.19 ? 161 TYR E CG  1 
ATOM   9100  C CD1 . TYR E 1 165 ? -32.500 70.410  31.010  1.00 45.85 ? 161 TYR E CD1 1 
ATOM   9101  C CD2 . TYR E 1 165 ? -30.219 70.522  31.746  1.00 45.94 ? 161 TYR E CD2 1 
ATOM   9102  C CE1 . TYR E 1 165 ? -32.460 69.016  31.082  1.00 45.41 ? 161 TYR E CE1 1 
ATOM   9103  C CE2 . TYR E 1 165 ? -30.170 69.132  31.825  1.00 45.73 ? 161 TYR E CE2 1 
ATOM   9104  C CZ  . TYR E 1 165 ? -31.293 68.384  31.488  1.00 45.88 ? 161 TYR E CZ  1 
ATOM   9105  O OH  . TYR E 1 165 ? -31.244 67.007  31.561  1.00 45.21 ? 161 TYR E OH  1 
ATOM   9106  N N   . PRO E 1 166 ? -29.683 73.503  34.410  1.00 45.41 ? 162 PRO E N   1 
ATOM   9107  C CA  . PRO E 1 166 ? -28.345 73.502  34.996  1.00 45.21 ? 162 PRO E CA  1 
ATOM   9108  C C   . PRO E 1 166 ? -27.625 72.174  34.758  1.00 44.99 ? 162 PRO E C   1 
ATOM   9109  O O   . PRO E 1 166 ? -28.278 71.133  34.600  1.00 44.93 ? 162 PRO E O   1 
ATOM   9110  C CB  . PRO E 1 166 ? -28.610 73.680  36.499  1.00 45.20 ? 162 PRO E CB  1 
ATOM   9111  C CG  . PRO E 1 166 ? -30.014 74.142  36.611  1.00 45.46 ? 162 PRO E CG  1 
ATOM   9112  C CD  . PRO E 1 166 ? -30.731 73.557  35.443  1.00 45.47 ? 162 PRO E CD  1 
ATOM   9113  N N   . THR E 1 167 ? -26.294 72.223  34.738  1.00 44.49 ? 163 THR E N   1 
ATOM   9114  C CA  . THR E 1 167 ? -25.456 71.037  34.584  1.00 44.12 ? 163 THR E CA  1 
ATOM   9115  C C   . THR E 1 167 ? -25.712 70.032  35.709  1.00 43.77 ? 163 THR E C   1 
ATOM   9116  O O   . THR E 1 167 ? -25.681 70.381  36.891  1.00 43.77 ? 163 THR E O   1 
ATOM   9117  C CB  . THR E 1 167 ? -23.959 71.422  34.520  1.00 44.18 ? 163 THR E CB  1 
ATOM   9118  O OG1 . THR E 1 167 ? -23.747 72.294  33.405  1.00 44.48 ? 163 THR E OG1 1 
ATOM   9119  C CG2 . THR E 1 167 ? -23.071 70.197  34.356  1.00 44.30 ? 163 THR E CG2 1 
ATOM   9120  N N   . ILE E 1 168 ? -25.987 68.792  35.316  1.00 43.22 ? 164 ILE E N   1 
ATOM   9121  C CA  . ILE E 1 168 ? -26.221 67.697  36.247  1.00 42.67 ? 164 ILE E CA  1 
ATOM   9122  C C   . ILE E 1 168 ? -24.903 66.984  36.540  1.00 42.63 ? 164 ILE E C   1 
ATOM   9123  O O   . ILE E 1 168 ? -24.142 66.676  35.621  1.00 42.57 ? 164 ILE E O   1 
ATOM   9124  C CB  . ILE E 1 168 ? -27.246 66.692  35.669  1.00 42.59 ? 164 ILE E CB  1 
ATOM   9125  C CG1 . ILE E 1 168 ? -28.634 67.332  35.588  1.00 42.22 ? 164 ILE E CG1 1 
ATOM   9126  C CG2 . ILE E 1 168 ? -27.292 65.409  36.496  1.00 42.36 ? 164 ILE E CG2 1 
ATOM   9127  C CD1 . ILE E 1 168 ? -29.550 66.720  34.533  1.00 41.15 ? 164 ILE E CD1 1 
ATOM   9128  N N   . LYS E 1 169 ? -24.632 66.747  37.822  1.00 42.45 ? 165 LYS E N   1 
ATOM   9129  C CA  . LYS E 1 169 ? -23.505 65.924  38.245  1.00 42.35 ? 165 LYS E CA  1 
ATOM   9130  C C   . LYS E 1 169 ? -24.002 64.945  39.289  1.00 42.31 ? 165 LYS E C   1 
ATOM   9131  O O   . LYS E 1 169 ? -24.233 65.318  40.435  1.00 42.65 ? 165 LYS E O   1 
ATOM   9132  C CB  . LYS E 1 169 ? -22.362 66.783  38.800  1.00 42.38 ? 165 LYS E CB  1 
ATOM   9133  C CG  . LYS E 1 169 ? -21.616 67.568  37.733  1.00 42.53 ? 165 LYS E CG  1 
ATOM   9134  C CD  . LYS E 1 169 ? -20.652 68.578  38.323  1.00 43.25 ? 165 LYS E CD  1 
ATOM   9135  C CE  . LYS E 1 169 ? -19.922 69.330  37.215  1.00 43.41 ? 165 LYS E CE  1 
ATOM   9136  N NZ  . LYS E 1 169 ? -18.910 70.274  37.754  1.00 43.92 ? 165 LYS E NZ  1 
ATOM   9137  N N   . ARG E 1 170 ? -24.199 63.696  38.882  1.00 42.31 ? 166 ARG E N   1 
ATOM   9138  C CA  . ARG E 1 170 ? -24.698 62.665  39.785  1.00 42.22 ? 166 ARG E CA  1 
ATOM   9139  C C   . ARG E 1 170 ? -23.783 61.456  39.775  1.00 42.13 ? 166 ARG E C   1 
ATOM   9140  O O   . ARG E 1 170 ? -23.144 61.157  38.762  1.00 42.23 ? 166 ARG E O   1 
ATOM   9141  C CB  . ARG E 1 170 ? -26.129 62.246  39.420  1.00 42.30 ? 166 ARG E CB  1 
ATOM   9142  C CG  . ARG E 1 170 ? -27.171 63.371  39.472  1.00 42.61 ? 166 ARG E CG  1 
ATOM   9143  C CD  . ARG E 1 170 ? -27.333 63.967  40.873  1.00 43.24 ? 166 ARG E CD  1 
ATOM   9144  N NE  . ARG E 1 170 ? -28.019 63.060  41.792  1.00 43.23 ? 166 ARG E NE  1 
ATOM   9145  C CZ  . ARG E 1 170 ? -29.338 63.011  41.960  1.00 43.59 ? 166 ARG E CZ  1 
ATOM   9146  N NH1 . ARG E 1 170 ? -30.139 63.813  41.268  1.00 44.28 ? 166 ARG E NH1 1 
ATOM   9147  N NH2 . ARG E 1 170 ? -29.859 62.153  42.822  1.00 43.60 ? 166 ARG E NH2 1 
ATOM   9148  N N   . SER E 1 171 ? -23.727 60.771  40.914  1.00 41.95 ? 167 SER E N   1 
ATOM   9149  C CA  . SER E 1 171 ? -22.934 59.558  41.065  1.00 41.78 ? 167 SER E CA  1 
ATOM   9150  C C   . SER E 1 171 ? -23.754 58.453  41.713  1.00 41.60 ? 167 SER E C   1 
ATOM   9151  O O   . SER E 1 171 ? -24.730 58.722  42.410  1.00 41.69 ? 167 SER E O   1 
ATOM   9152  C CB  . SER E 1 171 ? -21.692 59.839  41.912  1.00 41.81 ? 167 SER E CB  1 
ATOM   9153  O OG  . SER E 1 171 ? -20.809 60.714  41.237  1.00 41.96 ? 167 SER E OG  1 
ATOM   9154  N N   . TYR E 1 172 ? -23.364 57.209  41.466  1.00 41.55 ? 168 TYR E N   1 
ATOM   9155  C CA  . TYR E 1 172 ? -23.911 56.076  42.201  1.00 41.64 ? 168 TYR E CA  1 
ATOM   9156  C C   . TYR E 1 172 ? -22.861 54.988  42.392  1.00 42.08 ? 168 TYR E C   1 
ATOM   9157  O O   . TYR E 1 172 ? -22.265 54.514  41.421  1.00 42.18 ? 168 TYR E O   1 
ATOM   9158  C CB  . TYR E 1 172 ? -25.162 55.486  41.530  1.00 41.36 ? 168 TYR E CB  1 
ATOM   9159  C CG  . TYR E 1 172 ? -25.571 54.181  42.173  1.00 40.51 ? 168 TYR E CG  1 
ATOM   9160  C CD1 . TYR E 1 172 ? -26.338 54.167  43.338  1.00 39.36 ? 168 TYR E CD1 1 
ATOM   9161  C CD2 . TYR E 1 172 ? -25.146 52.960  41.648  1.00 39.53 ? 168 TYR E CD2 1 
ATOM   9162  C CE1 . TYR E 1 172 ? -26.691 52.972  43.949  1.00 38.73 ? 168 TYR E CE1 1 
ATOM   9163  C CE2 . TYR E 1 172 ? -25.489 51.762  42.253  1.00 38.82 ? 168 TYR E CE2 1 
ATOM   9164  C CZ  . TYR E 1 172 ? -26.263 51.774  43.401  1.00 38.49 ? 168 TYR E CZ  1 
ATOM   9165  O OH  . TYR E 1 172 ? -26.607 50.586  43.998  1.00 37.95 ? 168 TYR E OH  1 
ATOM   9166  N N   . ASN E 1 173 ? -22.664 54.595  43.647  1.00 42.57 ? 169 ASN E N   1 
ATOM   9167  C CA  . ASN E 1 173 ? -21.741 53.531  44.018  1.00 43.18 ? 169 ASN E CA  1 
ATOM   9168  C C   . ASN E 1 173 ? -22.504 52.225  44.168  1.00 42.96 ? 169 ASN E C   1 
ATOM   9169  O O   . ASN E 1 173 ? -23.500 52.176  44.887  1.00 42.95 ? 169 ASN E O   1 
ATOM   9170  C CB  . ASN E 1 173 ? -21.076 53.867  45.355  1.00 43.60 ? 169 ASN E CB  1 
ATOM   9171  C CG  . ASN E 1 173 ? -19.570 53.708  45.322  1.00 45.20 ? 169 ASN E CG  1 
ATOM   9172  O OD1 . ASN E 1 173 ? -19.023 52.695  45.766  1.00 48.50 ? 169 ASN E OD1 1 
ATOM   9173  N ND2 . ASN E 1 173 ? -18.885 54.729  44.807  1.00 47.26 ? 169 ASN E ND2 1 
ATOM   9174  N N   . ASN E 1 174 ? -22.047 51.171  43.497  1.00 42.88 ? 170 ASN E N   1 
ATOM   9175  C CA  . ASN E 1 174 ? -22.638 49.845  43.697  1.00 42.84 ? 170 ASN E CA  1 
ATOM   9176  C C   . ASN E 1 174 ? -22.167 49.226  45.012  1.00 43.11 ? 170 ASN E C   1 
ATOM   9177  O O   . ASN E 1 174 ? -21.172 48.503  45.055  1.00 42.96 ? 170 ASN E O   1 
ATOM   9178  C CB  . ASN E 1 174 ? -22.357 48.907  42.516  1.00 42.48 ? 170 ASN E CB  1 
ATOM   9179  C CG  . ASN E 1 174 ? -23.125 47.595  42.615  1.00 41.40 ? 170 ASN E CG  1 
ATOM   9180  O OD1 . ASN E 1 174 ? -24.081 47.475  43.379  1.00 40.36 ? 170 ASN E OD1 1 
ATOM   9181  N ND2 . ASN E 1 174 ? -22.705 46.605  41.840  1.00 40.74 ? 170 ASN E ND2 1 
ATOM   9182  N N   . THR E 1 175 ? -22.901 49.520  46.080  1.00 43.70 ? 171 THR E N   1 
ATOM   9183  C CA  . THR E 1 175 ? -22.549 49.060  47.422  1.00 44.23 ? 171 THR E CA  1 
ATOM   9184  C C   . THR E 1 175 ? -23.269 47.753  47.765  1.00 44.53 ? 171 THR E C   1 
ATOM   9185  O O   . THR E 1 175 ? -23.428 47.404  48.939  1.00 44.85 ? 171 THR E O   1 
ATOM   9186  C CB  . THR E 1 175 ? -22.854 50.142  48.482  1.00 44.24 ? 171 THR E CB  1 
ATOM   9187  O OG1 . THR E 1 175 ? -24.243 50.486  48.431  1.00 44.65 ? 171 THR E OG1 1 
ATOM   9188  C CG2 . THR E 1 175 ? -22.021 51.403  48.230  1.00 44.36 ? 171 THR E CG2 1 
ATOM   9189  N N   . ASN E 1 176 ? -23.693 47.034  46.728  1.00 44.70 ? 172 ASN E N   1 
ATOM   9190  C CA  . ASN E 1 176 ? -24.332 45.732  46.874  1.00 44.88 ? 172 ASN E CA  1 
ATOM   9191  C C   . ASN E 1 176 ? -23.329 44.621  46.568  1.00 44.93 ? 172 ASN E C   1 
ATOM   9192  O O   . ASN E 1 176 ? -22.220 44.891  46.101  1.00 44.90 ? 172 ASN E O   1 
ATOM   9193  C CB  . ASN E 1 176 ? -25.546 45.628  45.947  1.00 45.10 ? 172 ASN E CB  1 
ATOM   9194  C CG  . ASN E 1 176 ? -26.424 46.874  45.987  1.00 45.71 ? 172 ASN E CG  1 
ATOM   9195  O OD1 . ASN E 1 176 ? -27.233 47.057  46.900  1.00 46.29 ? 172 ASN E OD1 1 
ATOM   9196  N ND2 . ASN E 1 176 ? -26.268 47.735  44.986  1.00 45.77 ? 172 ASN E ND2 1 
ATOM   9197  N N   . GLN E 1 177 ? -23.720 43.377  46.827  1.00 44.97 ? 173 GLN E N   1 
ATOM   9198  C CA  . GLN E 1 177 ? -22.815 42.241  46.674  1.00 45.11 ? 173 GLN E CA  1 
ATOM   9199  C C   . GLN E 1 177 ? -22.872 41.632  45.274  1.00 44.85 ? 173 GLN E C   1 
ATOM   9200  O O   . GLN E 1 177 ? -22.068 40.758  44.939  1.00 44.99 ? 173 GLN E O   1 
ATOM   9201  C CB  . GLN E 1 177 ? -23.135 41.171  47.719  1.00 45.45 ? 173 GLN E CB  1 
ATOM   9202  C CG  . GLN E 1 177 ? -21.904 40.558  48.369  1.00 46.93 ? 173 GLN E CG  1 
ATOM   9203  C CD  . GLN E 1 177 ? -21.164 41.547  49.259  1.00 49.04 ? 173 GLN E CD  1 
ATOM   9204  O OE1 . GLN E 1 177 ? -21.783 42.289  50.032  1.00 49.94 ? 173 GLN E OE1 1 
ATOM   9205  N NE2 . GLN E 1 177 ? -19.834 41.565  49.153  1.00 49.27 ? 173 GLN E NE2 1 
ATOM   9206  N N   . GLU E 1 178 ? -23.821 42.098  44.465  1.00 44.28 ? 174 GLU E N   1 
ATOM   9207  C CA  . GLU E 1 178 ? -24.046 41.563  43.123  1.00 43.57 ? 174 GLU E CA  1 
ATOM   9208  C C   . GLU E 1 178 ? -23.678 42.568  42.025  1.00 42.75 ? 174 GLU E C   1 
ATOM   9209  O O   . GLU E 1 178 ? -23.612 43.779  42.270  1.00 42.64 ? 174 GLU E O   1 
ATOM   9210  C CB  . GLU E 1 178 ? -25.512 41.131  42.965  1.00 43.83 ? 174 GLU E CB  1 
ATOM   9211  C CG  . GLU E 1 178 ? -25.970 40.000  43.903  1.00 44.88 ? 174 GLU E CG  1 
ATOM   9212  C CD  . GLU E 1 178 ? -26.747 40.481  45.143  1.00 46.51 ? 174 GLU E CD  1 
ATOM   9213  O OE1 . GLU E 1 178 ? -26.991 39.644  46.044  1.00 47.08 ? 174 GLU E OE1 1 
ATOM   9214  O OE2 . GLU E 1 178 ? -27.124 41.675  45.225  1.00 46.55 ? 174 GLU E OE2 1 
ATOM   9215  N N   . ASP E 1 179 ? -23.426 42.057  40.819  1.00 41.69 ? 175 ASP E N   1 
ATOM   9216  C CA  . ASP E 1 179 ? -23.291 42.901  39.631  1.00 40.62 ? 175 ASP E CA  1 
ATOM   9217  C C   . ASP E 1 179 ? -24.608 43.640  39.402  1.00 39.70 ? 175 ASP E C   1 
ATOM   9218  O O   . ASP E 1 179 ? -25.682 43.104  39.677  1.00 39.61 ? 175 ASP E O   1 
ATOM   9219  C CB  . ASP E 1 179 ? -22.943 42.064  38.389  1.00 40.79 ? 175 ASP E CB  1 
ATOM   9220  C CG  . ASP E 1 179 ? -21.536 41.458  38.441  1.00 41.11 ? 175 ASP E CG  1 
ATOM   9221  O OD1 . ASP E 1 179 ? -20.611 42.096  38.983  1.00 42.02 ? 175 ASP E OD1 1 
ATOM   9222  O OD2 . ASP E 1 179 ? -21.350 40.339  37.916  1.00 41.41 ? 175 ASP E OD2 1 
ATOM   9223  N N   . LEU E 1 180 ? -24.525 44.868  38.898  1.00 38.58 ? 176 LEU E N   1 
ATOM   9224  C CA  . LEU E 1 180 ? -25.712 45.688  38.694  1.00 37.54 ? 176 LEU E CA  1 
ATOM   9225  C C   . LEU E 1 180 ? -25.852 46.192  37.256  1.00 36.72 ? 176 LEU E C   1 
ATOM   9226  O O   . LEU E 1 180 ? -25.018 46.972  36.784  1.00 36.83 ? 176 LEU E O   1 
ATOM   9227  C CB  . LEU E 1 180 ? -25.700 46.872  39.667  1.00 37.78 ? 176 LEU E CB  1 
ATOM   9228  C CG  . LEU E 1 180 ? -26.995 47.671  39.850  1.00 38.17 ? 176 LEU E CG  1 
ATOM   9229  C CD1 . LEU E 1 180 ? -28.000 46.900  40.695  1.00 39.54 ? 176 LEU E CD1 1 
ATOM   9230  C CD2 . LEU E 1 180 ? -26.692 49.001  40.496  1.00 38.08 ? 176 LEU E CD2 1 
ATOM   9231  N N   . LEU E 1 181 ? -26.909 45.752  36.571  1.00 35.34 ? 177 LEU E N   1 
ATOM   9232  C CA  . LEU E 1 181 ? -27.251 46.273  35.242  1.00 34.14 ? 177 LEU E CA  1 
ATOM   9233  C C   . LEU E 1 181 ? -27.875 47.659  35.332  1.00 33.38 ? 177 LEU E C   1 
ATOM   9234  O O   . LEU E 1 181 ? -28.953 47.820  35.898  1.00 33.20 ? 177 LEU E O   1 
ATOM   9235  C CB  . LEU E 1 181 ? -28.205 45.325  34.498  1.00 34.18 ? 177 LEU E CB  1 
ATOM   9236  C CG  . LEU E 1 181 ? -28.799 45.812  33.168  1.00 33.61 ? 177 LEU E CG  1 
ATOM   9237  C CD1 . LEU E 1 181 ? -27.717 46.033  32.114  1.00 32.81 ? 177 LEU E CD1 1 
ATOM   9238  C CD2 . LEU E 1 181 ? -29.852 44.839  32.655  1.00 33.70 ? 177 LEU E CD2 1 
ATOM   9239  N N   . VAL E 1 182 ? -27.200 48.645  34.749  1.00 32.72 ? 178 VAL E N   1 
ATOM   9240  C CA  . VAL E 1 182 ? -27.649 50.040  34.776  1.00 32.07 ? 178 VAL E CA  1 
ATOM   9241  C C   . VAL E 1 182 ? -27.999 50.515  33.360  1.00 31.84 ? 178 VAL E C   1 
ATOM   9242  O O   . VAL E 1 182 ? -27.273 50.219  32.404  1.00 31.86 ? 178 VAL E O   1 
ATOM   9243  C CB  . VAL E 1 182 ? -26.570 50.967  35.411  1.00 31.97 ? 178 VAL E CB  1 
ATOM   9244  C CG1 . VAL E 1 182 ? -27.053 52.415  35.492  1.00 31.46 ? 178 VAL E CG1 1 
ATOM   9245  C CG2 . VAL E 1 182 ? -26.184 50.461  36.791  1.00 31.68 ? 178 VAL E CG2 1 
ATOM   9246  N N   . LEU E 1 183 ? -29.105 51.253  33.238  1.00 31.39 ? 179 LEU E N   1 
ATOM   9247  C CA  . LEU E 1 183 ? -29.591 51.740  31.941  1.00 30.74 ? 179 LEU E CA  1 
ATOM   9248  C C   . LEU E 1 183 ? -29.805 53.249  31.925  1.00 30.26 ? 179 LEU E C   1 
ATOM   9249  O O   . LEU E 1 183 ? -30.276 53.823  32.896  1.00 30.03 ? 179 LEU E O   1 
ATOM   9250  C CB  . LEU E 1 183 ? -30.899 51.044  31.566  1.00 30.86 ? 179 LEU E CB  1 
ATOM   9251  C CG  . LEU E 1 183 ? -30.927 49.512  31.540  1.00 31.21 ? 179 LEU E CG  1 
ATOM   9252  C CD1 . LEU E 1 183 ? -32.251 49.006  32.077  1.00 31.67 ? 179 LEU E CD1 1 
ATOM   9253  C CD2 . LEU E 1 183 ? -30.679 48.987  30.134  1.00 31.08 ? 179 LEU E CD2 1 
ATOM   9254  N N   . TRP E 1 184 ? -29.449 53.877  30.808  1.00 29.95 ? 180 TRP E N   1 
ATOM   9255  C CA  . TRP E 1 184 ? -29.699 55.295  30.576  1.00 29.59 ? 180 TRP E CA  1 
ATOM   9256  C C   . TRP E 1 184 ? -29.853 55.533  29.076  1.00 29.95 ? 180 TRP E C   1 
ATOM   9257  O O   . TRP E 1 184 ? -29.735 54.604  28.273  1.00 29.67 ? 180 TRP E O   1 
ATOM   9258  C CB  . TRP E 1 184 ? -28.568 56.162  31.149  1.00 29.17 ? 180 TRP E CB  1 
ATOM   9259  C CG  . TRP E 1 184 ? -27.272 56.055  30.392  1.00 28.05 ? 180 TRP E CG  1 
ATOM   9260  C CD1 . TRP E 1 184 ? -26.805 56.915  29.441  1.00 27.33 ? 180 TRP E CD1 1 
ATOM   9261  C CD2 . TRP E 1 184 ? -26.282 55.022  30.518  1.00 27.37 ? 180 TRP E CD2 1 
ATOM   9262  N NE1 . TRP E 1 184 ? -25.585 56.486  28.969  1.00 27.03 ? 180 TRP E NE1 1 
ATOM   9263  C CE2 . TRP E 1 184 ? -25.241 55.327  29.614  1.00 27.17 ? 180 TRP E CE2 1 
ATOM   9264  C CE3 . TRP E 1 184 ? -26.171 53.872  31.311  1.00 27.20 ? 180 TRP E CE3 1 
ATOM   9265  C CZ2 . TRP E 1 184 ? -24.106 54.521  29.475  1.00 27.25 ? 180 TRP E CZ2 1 
ATOM   9266  C CZ3 . TRP E 1 184 ? -25.036 53.069  31.173  1.00 27.42 ? 180 TRP E CZ3 1 
ATOM   9267  C CH2 . TRP E 1 184 ? -24.021 53.401  30.261  1.00 26.91 ? 180 TRP E CH2 1 
ATOM   9268  N N   . GLY E 1 185 ? -30.102 56.783  28.699  1.00 30.35 ? 181 GLY E N   1 
ATOM   9269  C CA  . GLY E 1 185 ? -30.298 57.108  27.304  1.00 30.84 ? 181 GLY E CA  1 
ATOM   9270  C C   . GLY E 1 185 ? -30.091 58.557  26.944  1.00 31.36 ? 181 GLY E C   1 
ATOM   9271  O O   . GLY E 1 185 ? -29.737 59.387  27.789  1.00 31.35 ? 181 GLY E O   1 
ATOM   9272  N N   . ILE E 1 186 ? -30.318 58.846  25.668  1.00 31.87 ? 182 ILE E N   1 
ATOM   9273  C CA  . ILE E 1 186 ? -30.204 60.189  25.122  1.00 32.39 ? 182 ILE E CA  1 
ATOM   9274  C C   . ILE E 1 186 ? -31.388 60.470  24.185  1.00 32.96 ? 182 ILE E C   1 
ATOM   9275  O O   . ILE E 1 186 ? -31.885 59.565  23.512  1.00 32.99 ? 182 ILE E O   1 
ATOM   9276  C CB  . ILE E 1 186 ? -28.840 60.387  24.400  1.00 32.17 ? 182 ILE E CB  1 
ATOM   9277  C CG1 . ILE E 1 186 ? -28.615 61.861  24.042  1.00 32.38 ? 182 ILE E CG1 1 
ATOM   9278  C CG2 . ILE E 1 186 ? -28.719 59.477  23.173  1.00 32.18 ? 182 ILE E CG2 1 
ATOM   9279  C CD1 . ILE E 1 186 ? -27.251 62.165  23.432  1.00 32.06 ? 182 ILE E CD1 1 
ATOM   9280  N N   . HIS E 1 187 ? -31.842 61.719  24.164  1.00 33.81 ? 183 HIS E N   1 
ATOM   9281  C CA  . HIS E 1 187 ? -32.906 62.149  23.265  1.00 34.57 ? 183 HIS E CA  1 
ATOM   9282  C C   . HIS E 1 187 ? -32.329 62.939  22.101  1.00 35.13 ? 183 HIS E C   1 
ATOM   9283  O O   . HIS E 1 187 ? -31.659 63.945  22.307  1.00 35.45 ? 183 HIS E O   1 
ATOM   9284  C CB  . HIS E 1 187 ? -33.938 62.992  24.019  1.00 34.55 ? 183 HIS E CB  1 
ATOM   9285  C CG  . HIS E 1 187 ? -35.036 63.522  23.151  1.00 35.35 ? 183 HIS E CG  1 
ATOM   9286  N ND1 . HIS E 1 187 ? -35.221 64.869  22.925  1.00 36.05 ? 183 HIS E ND1 1 
ATOM   9287  C CD2 . HIS E 1 187 ? -35.998 62.885  22.439  1.00 35.93 ? 183 HIS E CD2 1 
ATOM   9288  C CE1 . HIS E 1 187 ? -36.253 65.040  22.118  1.00 36.16 ? 183 HIS E CE1 1 
ATOM   9289  N NE2 . HIS E 1 187 ? -36.742 63.852  21.808  1.00 36.13 ? 183 HIS E NE2 1 
ATOM   9290  N N   . HIS E 1 188 ? -32.573 62.462  20.883  1.00 35.87 ? 184 HIS E N   1 
ATOM   9291  C CA  . HIS E 1 188 ? -32.212 63.187  19.667  1.00 36.84 ? 184 HIS E CA  1 
ATOM   9292  C C   . HIS E 1 188 ? -33.450 63.935  19.137  1.00 37.87 ? 184 HIS E C   1 
ATOM   9293  O O   . HIS E 1 188 ? -34.363 63.307  18.594  1.00 37.73 ? 184 HIS E O   1 
ATOM   9294  C CB  . HIS E 1 188 ? -31.701 62.226  18.585  1.00 36.76 ? 184 HIS E CB  1 
ATOM   9295  C CG  . HIS E 1 188 ? -30.586 61.328  19.026  1.00 36.23 ? 184 HIS E CG  1 
ATOM   9296  N ND1 . HIS E 1 188 ? -29.288 61.767  19.172  1.00 35.99 ? 184 HIS E ND1 1 
ATOM   9297  C CD2 . HIS E 1 188 ? -30.570 60.007  19.321  1.00 35.63 ? 184 HIS E CD2 1 
ATOM   9298  C CE1 . HIS E 1 188 ? -28.525 60.760  19.556  1.00 35.70 ? 184 HIS E CE1 1 
ATOM   9299  N NE2 . HIS E 1 188 ? -29.278 59.680  19.652  1.00 35.50 ? 184 HIS E NE2 1 
ATOM   9300  N N   . PRO E 1 189 ? -33.489 65.275  19.298  1.00 38.81 ? 185 PRO E N   1 
ATOM   9301  C CA  . PRO E 1 189 ? -34.648 66.077  18.892  1.00 39.72 ? 185 PRO E CA  1 
ATOM   9302  C C   . PRO E 1 189 ? -34.734 66.279  17.384  1.00 40.75 ? 185 PRO E C   1 
ATOM   9303  O O   . PRO E 1 189 ? -33.751 66.067  16.669  1.00 40.87 ? 185 PRO E O   1 
ATOM   9304  C CB  . PRO E 1 189 ? -34.408 67.426  19.585  1.00 39.81 ? 185 PRO E CB  1 
ATOM   9305  C CG  . PRO E 1 189 ? -33.240 67.213  20.506  1.00 39.43 ? 185 PRO E CG  1 
ATOM   9306  C CD  . PRO E 1 189 ? -32.447 66.115  19.906  1.00 38.80 ? 185 PRO E CD  1 
ATOM   9307  N N   . ASN E 1 190 ? -35.902 66.694  16.902  1.00 42.19 ? 186 ASN E N   1 
ATOM   9308  C CA  . ASN E 1 190 ? -36.106 66.853  15.460  1.00 43.51 ? 186 ASN E CA  1 
ATOM   9309  C C   . ASN E 1 190 ? -35.513 68.122  14.845  1.00 44.12 ? 186 ASN E C   1 
ATOM   9310  O O   . ASN E 1 190 ? -35.073 68.100  13.701  1.00 44.38 ? 186 ASN E O   1 
ATOM   9311  C CB  . ASN E 1 190 ? -37.579 66.655  15.069  1.00 43.75 ? 186 ASN E CB  1 
ATOM   9312  C CG  . ASN E 1 190 ? -38.429 67.887  15.313  1.00 44.60 ? 186 ASN E CG  1 
ATOM   9313  O OD1 . ASN E 1 190 ? -38.618 68.712  14.413  1.00 45.39 ? 186 ASN E OD1 1 
ATOM   9314  N ND2 . ASN E 1 190 ? -38.951 68.017  16.527  1.00 44.53 ? 186 ASN E ND2 1 
ATOM   9315  N N   . ASP E 1 191 ? -35.501 69.223  15.594  1.00 45.11 ? 187 ASP E N   1 
ATOM   9316  C CA  . ASP E 1 191 ? -34.905 70.480  15.107  1.00 46.23 ? 187 ASP E CA  1 
ATOM   9317  C C   . ASP E 1 191 ? -34.374 71.363  16.236  1.00 46.61 ? 187 ASP E C   1 
ATOM   9318  O O   . ASP E 1 191 ? -34.601 71.077  17.419  1.00 46.58 ? 187 ASP E O   1 
ATOM   9319  C CB  . ASP E 1 191 ? -35.878 71.267  14.209  1.00 46.41 ? 187 ASP E CB  1 
ATOM   9320  C CG  . ASP E 1 191 ? -37.154 71.689  14.933  1.00 47.75 ? 187 ASP E CG  1 
ATOM   9321  O OD1 . ASP E 1 191 ? -37.513 71.079  15.964  1.00 48.64 ? 187 ASP E OD1 1 
ATOM   9322  O OD2 . ASP E 1 191 ? -37.815 72.636  14.453  1.00 50.10 ? 187 ASP E OD2 1 
ATOM   9323  N N   . ALA E 1 192 ? -33.667 72.429  15.855  1.00 47.09 ? 188 ALA E N   1 
ATOM   9324  C CA  . ALA E 1 192 ? -33.091 73.384  16.810  1.00 47.61 ? 188 ALA E CA  1 
ATOM   9325  C C   . ALA E 1 192 ? -34.151 74.010  17.720  1.00 47.93 ? 188 ALA E C   1 
ATOM   9326  O O   . ALA E 1 192 ? -33.875 74.322  18.882  1.00 48.18 ? 188 ALA E O   1 
ATOM   9327  C CB  . ALA E 1 192 ? -32.299 74.468  16.077  1.00 47.41 ? 188 ALA E CB  1 
ATOM   9328  N N   . ALA E 1 193 ? -35.361 74.174  17.188  1.00 48.30 ? 189 ALA E N   1 
ATOM   9329  C CA  . ALA E 1 193 ? -36.471 74.755  17.941  1.00 48.58 ? 189 ALA E CA  1 
ATOM   9330  C C   . ALA E 1 193 ? -36.944 73.838  19.069  1.00 48.71 ? 189 ALA E C   1 
ATOM   9331  O O   . ALA E 1 193 ? -37.333 74.318  20.137  1.00 48.80 ? 189 ALA E O   1 
ATOM   9332  C CB  . ALA E 1 193 ? -37.626 75.102  17.007  1.00 48.56 ? 189 ALA E CB  1 
ATOM   9333  N N   . GLU E 1 194 ? -36.910 72.525  18.833  1.00 48.80 ? 190 GLU E N   1 
ATOM   9334  C CA  . GLU E 1 194 ? -37.299 71.558  19.863  1.00 48.94 ? 190 GLU E CA  1 
ATOM   9335  C C   . GLU E 1 194 ? -36.224 71.411  20.940  1.00 48.53 ? 190 GLU E C   1 
ATOM   9336  O O   . GLU E 1 194 ? -36.535 71.076  22.081  1.00 48.47 ? 190 GLU E O   1 
ATOM   9337  C CB  . GLU E 1 194 ? -37.638 70.192  19.257  1.00 49.29 ? 190 GLU E CB  1 
ATOM   9338  C CG  . GLU E 1 194 ? -38.538 69.334  20.156  1.00 50.93 ? 190 GLU E CG  1 
ATOM   9339  C CD  . GLU E 1 194 ? -38.617 67.866  19.743  1.00 53.02 ? 190 GLU E CD  1 
ATOM   9340  O OE1 . GLU E 1 194 ? -37.981 67.469  18.739  1.00 53.46 ? 190 GLU E OE1 1 
ATOM   9341  O OE2 . GLU E 1 194 ? -39.325 67.103  20.441  1.00 53.97 ? 190 GLU E OE2 1 
ATOM   9342  N N   . GLN E 1 195 ? -34.969 71.667  20.569  1.00 48.24 ? 191 GLN E N   1 
ATOM   9343  C CA  . GLN E 1 195 ? -33.842 71.640  21.508  1.00 48.19 ? 191 GLN E CA  1 
ATOM   9344  C C   . GLN E 1 195 ? -33.970 72.750  22.557  1.00 48.18 ? 191 GLN E C   1 
ATOM   9345  O O   . GLN E 1 195 ? -33.808 72.502  23.754  1.00 48.03 ? 191 GLN E O   1 
ATOM   9346  C CB  . GLN E 1 195 ? -32.506 71.743  20.750  1.00 48.16 ? 191 GLN E CB  1 
ATOM   9347  C CG  . GLN E 1 195 ? -31.240 71.719  21.618  1.00 47.82 ? 191 GLN E CG  1 
ATOM   9348  C CD  . GLN E 1 195 ? -31.064 70.431  22.413  1.00 47.96 ? 191 GLN E CD  1 
ATOM   9349  O OE1 . GLN E 1 195 ? -31.477 69.355  21.986  1.00 48.38 ? 191 GLN E OE1 1 
ATOM   9350  N NE2 . GLN E 1 195 ? -30.437 70.541  23.576  1.00 47.77 ? 191 GLN E NE2 1 
ATOM   9351  N N   . THR E 1 196 ? -34.272 73.962  22.088  1.00 48.29 ? 192 THR E N   1 
ATOM   9352  C CA  . THR E 1 196 ? -34.536 75.123  22.944  1.00 48.35 ? 192 THR E CA  1 
ATOM   9353  C C   . THR E 1 196 ? -35.703 74.869  23.906  1.00 48.13 ? 192 THR E C   1 
ATOM   9354  O O   . THR E 1 196 ? -35.565 75.043  25.119  1.00 48.13 ? 192 THR E O   1 
ATOM   9355  C CB  . THR E 1 196 ? -34.847 76.381  22.093  1.00 48.51 ? 192 THR E CB  1 
ATOM   9356  O OG1 . THR E 1 196 ? -33.798 76.596  21.137  1.00 49.08 ? 192 THR E OG1 1 
ATOM   9357  C CG2 . THR E 1 196 ? -34.984 77.621  22.973  1.00 49.01 ? 192 THR E CG2 1 
ATOM   9358  N N   . LYS E 1 197 ? -36.840 74.442  23.356  1.00 47.76 ? 193 LYS E N   1 
ATOM   9359  C CA  . LYS E 1 197 ? -38.083 74.287  24.116  1.00 47.41 ? 193 LYS E CA  1 
ATOM   9360  C C   . LYS E 1 197 ? -37.971 73.252  25.236  1.00 47.16 ? 193 LYS E C   1 
ATOM   9361  O O   . LYS E 1 197 ? -38.662 73.352  26.254  1.00 47.16 ? 193 LYS E O   1 
ATOM   9362  C CB  . LYS E 1 197 ? -39.243 73.957  23.163  1.00 47.43 ? 193 LYS E CB  1 
ATOM   9363  C CG  . LYS E 1 197 ? -40.594 73.688  23.828  1.00 47.96 ? 193 LYS E CG  1 
ATOM   9364  C CD  . LYS E 1 197 ? -40.864 72.189  23.982  1.00 48.70 ? 193 LYS E CD  1 
ATOM   9365  C CE  . LYS E 1 197 ? -42.007 71.908  24.957  1.00 49.23 ? 193 LYS E CE  1 
ATOM   9366  N NZ  . LYS E 1 197 ? -43.344 72.243  24.393  1.00 49.81 ? 193 LYS E NZ  1 
ATOM   9367  N N   . LEU E 1 198 ? -37.097 72.266  25.046  1.00 46.81 ? 194 LEU E N   1 
ATOM   9368  C CA  . LEU E 1 198 ? -36.972 71.158  25.992  1.00 46.26 ? 194 LEU E CA  1 
ATOM   9369  C C   . LEU E 1 198 ? -35.835 71.332  27.004  1.00 45.90 ? 194 LEU E C   1 
ATOM   9370  O O   . LEU E 1 198 ? -36.008 71.020  28.184  1.00 45.67 ? 194 LEU E O   1 
ATOM   9371  C CB  . LEU E 1 198 ? -36.822 69.823  25.245  1.00 46.31 ? 194 LEU E CB  1 
ATOM   9372  C CG  . LEU E 1 198 ? -38.013 69.228  24.471  1.00 46.43 ? 194 LEU E CG  1 
ATOM   9373  C CD1 . LEU E 1 198 ? -37.566 68.018  23.671  1.00 45.99 ? 194 LEU E CD1 1 
ATOM   9374  C CD2 . LEU E 1 198 ? -39.184 68.849  25.378  1.00 46.23 ? 194 LEU E CD2 1 
ATOM   9375  N N   . TYR E 1 199 ? -34.683 71.830  26.547  1.00 45.50 ? 195 TYR E N   1 
ATOM   9376  C CA  . TYR E 1 199 ? -33.472 71.861  27.385  1.00 45.17 ? 195 TYR E CA  1 
ATOM   9377  C C   . TYR E 1 199 ? -32.762 73.227  27.463  1.00 45.26 ? 195 TYR E C   1 
ATOM   9378  O O   . TYR E 1 199 ? -31.741 73.362  28.145  1.00 44.96 ? 195 TYR E O   1 
ATOM   9379  C CB  . TYR E 1 199 ? -32.490 70.751  26.955  1.00 44.95 ? 195 TYR E CB  1 
ATOM   9380  C CG  . TYR E 1 199 ? -33.152 69.422  26.616  1.00 44.02 ? 195 TYR E CG  1 
ATOM   9381  C CD1 . TYR E 1 199 ? -33.205 68.962  25.296  1.00 43.48 ? 195 TYR E CD1 1 
ATOM   9382  C CD2 . TYR E 1 199 ? -33.742 68.638  27.609  1.00 42.94 ? 195 TYR E CD2 1 
ATOM   9383  C CE1 . TYR E 1 199 ? -33.823 67.750  24.975  1.00 42.76 ? 195 TYR E CE1 1 
ATOM   9384  C CE2 . TYR E 1 199 ? -34.360 67.429  27.301  1.00 43.02 ? 195 TYR E CE2 1 
ATOM   9385  C CZ  . TYR E 1 199 ? -34.396 66.993  25.983  1.00 42.84 ? 195 TYR E CZ  1 
ATOM   9386  O OH  . TYR E 1 199 ? -35.003 65.797  25.682  1.00 42.87 ? 195 TYR E OH  1 
ATOM   9387  N N   . GLN E 1 200 ? -33.310 74.228  26.767  1.00 45.37 ? 196 GLN E N   1 
ATOM   9388  C CA  . GLN E 1 200 ? -32.803 75.616  26.780  1.00 45.39 ? 196 GLN E CA  1 
ATOM   9389  C C   . GLN E 1 200 ? -31.444 75.804  26.092  1.00 45.26 ? 196 GLN E C   1 
ATOM   9390  O O   . GLN E 1 200 ? -31.295 76.696  25.253  1.00 45.38 ? 196 GLN E O   1 
ATOM   9391  C CB  . GLN E 1 200 ? -32.791 76.204  28.205  1.00 45.46 ? 196 GLN E CB  1 
ATOM   9392  C CG  . GLN E 1 200 ? -32.454 77.700  28.293  1.00 46.20 ? 196 GLN E CG  1 
ATOM   9393  C CD  . GLN E 1 200 ? -33.587 78.613  27.819  1.00 47.28 ? 196 GLN E CD  1 
ATOM   9394  O OE1 . GLN E 1 200 ? -33.373 79.506  26.993  1.00 47.22 ? 196 GLN E OE1 1 
ATOM   9395  N NE2 . GLN E 1 200 ? -34.795 78.392  28.339  1.00 47.22 ? 196 GLN E NE2 1 
ATOM   9396  N N   . ASN E 1 201 ? -30.463 74.973  26.443  1.00 44.94 ? 197 ASN E N   1 
ATOM   9397  C CA  . ASN E 1 201 ? -29.115 75.093  25.880  1.00 44.74 ? 197 ASN E CA  1 
ATOM   9398  C C   . ASN E 1 201 ? -29.044 74.509  24.467  1.00 44.51 ? 197 ASN E C   1 
ATOM   9399  O O   . ASN E 1 201 ? -29.540 73.409  24.230  1.00 44.57 ? 197 ASN E O   1 
ATOM   9400  C CB  . ASN E 1 201 ? -28.079 74.423  26.795  1.00 44.77 ? 197 ASN E CB  1 
ATOM   9401  C CG  . ASN E 1 201 ? -28.316 74.721  28.275  1.00 44.85 ? 197 ASN E CG  1 
ATOM   9402  O OD1 . ASN E 1 201 ? -28.424 75.880  28.677  1.00 44.93 ? 197 ASN E OD1 1 
ATOM   9403  N ND2 . ASN E 1 201 ? -28.396 73.668  29.089  1.00 44.26 ? 197 ASN E ND2 1 
ATOM   9404  N N   . PRO E 1 202 ? -28.436 75.247  23.519  1.00 44.31 ? 198 PRO E N   1 
ATOM   9405  C CA  . PRO E 1 202 ? -28.381 74.747  22.138  1.00 44.00 ? 198 PRO E CA  1 
ATOM   9406  C C   . PRO E 1 202 ? -27.276 73.705  21.902  1.00 43.77 ? 198 PRO E C   1 
ATOM   9407  O O   . PRO E 1 202 ? -27.386 72.892  20.979  1.00 43.85 ? 198 PRO E O   1 
ATOM   9408  C CB  . PRO E 1 202 ? -28.119 76.013  21.318  1.00 43.89 ? 198 PRO E CB  1 
ATOM   9409  C CG  . PRO E 1 202 ? -27.389 76.928  22.252  1.00 44.16 ? 198 PRO E CG  1 
ATOM   9410  C CD  . PRO E 1 202 ? -27.795 76.570  23.663  1.00 44.18 ? 198 PRO E CD  1 
ATOM   9411  N N   . THR E 1 203 ? -26.227 73.741  22.726  1.00 43.36 ? 199 THR E N   1 
ATOM   9412  C CA  . THR E 1 203 ? -25.091 72.824  22.608  1.00 42.82 ? 199 THR E CA  1 
ATOM   9413  C C   . THR E 1 203 ? -24.957 71.990  23.878  1.00 42.41 ? 199 THR E C   1 
ATOM   9414  O O   . THR E 1 203 ? -24.506 72.482  24.918  1.00 42.52 ? 199 THR E O   1 
ATOM   9415  C CB  . THR E 1 203 ? -23.781 73.585  22.324  1.00 42.94 ? 199 THR E CB  1 
ATOM   9416  O OG1 . THR E 1 203 ? -23.997 74.515  21.254  1.00 43.13 ? 199 THR E OG1 1 
ATOM   9417  C CG2 . THR E 1 203 ? -22.658 72.621  21.938  1.00 42.49 ? 199 THR E CG2 1 
ATOM   9418  N N   . THR E 1 204 ? -25.355 70.724  23.780  1.00 41.69 ? 200 THR E N   1 
ATOM   9419  C CA  . THR E 1 204 ? -25.462 69.850  24.946  1.00 40.87 ? 200 THR E CA  1 
ATOM   9420  C C   . THR E 1 204 ? -24.617 68.582  24.827  1.00 40.18 ? 200 THR E C   1 
ATOM   9421  O O   . THR E 1 204 ? -24.053 68.296  23.768  1.00 39.99 ? 200 THR E O   1 
ATOM   9422  C CB  . THR E 1 204 ? -26.918 69.470  25.194  1.00 41.03 ? 200 THR E CB  1 
ATOM   9423  O OG1 . THR E 1 204 ? -27.485 68.972  23.976  1.00 41.31 ? 200 THR E OG1 1 
ATOM   9424  C CG2 . THR E 1 204 ? -27.715 70.693  25.660  1.00 41.26 ? 200 THR E CG2 1 
ATOM   9425  N N   . TYR E 1 205 ? -24.530 67.835  25.927  1.00 39.39 ? 201 TYR E N   1 
ATOM   9426  C CA  . TYR E 1 205 ? -23.730 66.612  25.996  1.00 38.61 ? 201 TYR E CA  1 
ATOM   9427  C C   . TYR E 1 205 ? -24.183 65.692  27.133  1.00 38.09 ? 201 TYR E C   1 
ATOM   9428  O O   . TYR E 1 205 ? -24.866 66.128  28.063  1.00 37.85 ? 201 TYR E O   1 
ATOM   9429  C CB  . TYR E 1 205 ? -22.235 66.948  26.160  1.00 38.72 ? 201 TYR E CB  1 
ATOM   9430  C CG  . TYR E 1 205 ? -21.884 67.582  27.494  1.00 39.13 ? 201 TYR E CG  1 
ATOM   9431  C CD1 . TYR E 1 205 ? -21.569 66.792  28.600  1.00 39.32 ? 201 TYR E CD1 1 
ATOM   9432  C CD2 . TYR E 1 205 ? -21.871 68.969  27.650  1.00 39.62 ? 201 TYR E CD2 1 
ATOM   9433  C CE1 . TYR E 1 205 ? -21.255 67.362  29.826  1.00 40.26 ? 201 TYR E CE1 1 
ATOM   9434  C CE2 . TYR E 1 205 ? -21.557 69.553  28.882  1.00 40.05 ? 201 TYR E CE2 1 
ATOM   9435  C CZ  . TYR E 1 205 ? -21.249 68.742  29.963  1.00 40.39 ? 201 TYR E CZ  1 
ATOM   9436  O OH  . TYR E 1 205 ? -20.936 69.299  31.185  1.00 41.22 ? 201 TYR E OH  1 
ATOM   9437  N N   . ILE E 1 206 ? -23.806 64.418  27.034  1.00 37.48 ? 202 ILE E N   1 
ATOM   9438  C CA  . ILE E 1 206 ? -23.850 63.484  28.157  1.00 36.98 ? 202 ILE E CA  1 
ATOM   9439  C C   . ILE E 1 206 ? -22.502 62.771  28.246  1.00 36.62 ? 202 ILE E C   1 
ATOM   9440  O O   . ILE E 1 206 ? -22.042 62.191  27.266  1.00 36.46 ? 202 ILE E O   1 
ATOM   9441  C CB  . ILE E 1 206 ? -24.982 62.428  28.025  1.00 37.12 ? 202 ILE E CB  1 
ATOM   9442  C CG1 . ILE E 1 206 ? -26.360 63.054  28.250  1.00 37.02 ? 202 ILE E CG1 1 
ATOM   9443  C CG2 . ILE E 1 206 ? -24.798 61.298  29.031  1.00 37.19 ? 202 ILE E CG2 1 
ATOM   9444  C CD1 . ILE E 1 206 ? -27.108 63.345  26.991  1.00 36.45 ? 202 ILE E CD1 1 
ATOM   9445  N N   . SER E 1 207 ? -21.868 62.827  29.415  1.00 36.17 ? 203 SER E N   1 
ATOM   9446  C CA  . SER E 1 207 ? -20.632 62.081  29.650  1.00 35.50 ? 203 SER E CA  1 
ATOM   9447  C C   . SER E 1 207 ? -20.852 61.015  30.713  1.00 35.10 ? 203 SER E C   1 
ATOM   9448  O O   . SER E 1 207 ? -21.433 61.296  31.758  1.00 34.97 ? 203 SER E O   1 
ATOM   9449  C CB  . SER E 1 207 ? -19.495 63.017  30.058  1.00 35.42 ? 203 SER E CB  1 
ATOM   9450  O OG  . SER E 1 207 ? -19.695 63.524  31.363  1.00 35.32 ? 203 SER E OG  1 
ATOM   9451  N N   . VAL E 1 208 ? -20.408 59.791  30.433  1.00 34.72 ? 204 VAL E N   1 
ATOM   9452  C CA  . VAL E 1 208 ? -20.553 58.678  31.380  1.00 34.33 ? 204 VAL E CA  1 
ATOM   9453  C C   . VAL E 1 208 ? -19.224 57.954  31.586  1.00 34.02 ? 204 VAL E C   1 
ATOM   9454  O O   . VAL E 1 208 ? -18.573 57.539  30.625  1.00 33.75 ? 204 VAL E O   1 
ATOM   9455  C CB  . VAL E 1 208 ? -21.651 57.657  30.962  1.00 34.28 ? 204 VAL E CB  1 
ATOM   9456  C CG1 . VAL E 1 208 ? -22.009 56.758  32.130  1.00 34.02 ? 204 VAL E CG1 1 
ATOM   9457  C CG2 . VAL E 1 208 ? -22.905 58.360  30.471  1.00 34.75 ? 204 VAL E CG2 1 
ATOM   9458  N N   . GLY E 1 209 ? -18.834 57.811  32.850  1.00 33.83 ? 205 GLY E N   1 
ATOM   9459  C CA  . GLY E 1 209 ? -17.574 57.175  33.206  1.00 33.87 ? 205 GLY E CA  1 
ATOM   9460  C C   . GLY E 1 209 ? -17.697 56.180  34.344  1.00 33.97 ? 205 GLY E C   1 
ATOM   9461  O O   . GLY E 1 209 ? -18.262 56.489  35.392  1.00 33.87 ? 205 GLY E O   1 
ATOM   9462  N N   . THR E 1 210 ? -17.198 54.970  34.111  1.00 34.08 ? 206 THR E N   1 
ATOM   9463  C CA  . THR E 1 210 ? -16.983 53.987  35.168  1.00 34.27 ? 206 THR E CA  1 
ATOM   9464  C C   . THR E 1 210 ? -15.498 53.618  35.119  1.00 34.56 ? 206 THR E C   1 
ATOM   9465  O O   . THR E 1 210 ? -14.724 54.262  34.408  1.00 34.52 ? 206 THR E O   1 
ATOM   9466  C CB  . THR E 1 210 ? -17.874 52.724  35.009  1.00 34.32 ? 206 THR E CB  1 
ATOM   9467  O OG1 . THR E 1 210 ? -17.383 51.903  33.940  1.00 34.15 ? 206 THR E OG1 1 
ATOM   9468  C CG2 . THR E 1 210 ? -19.332 53.097  34.750  1.00 33.84 ? 206 THR E CG2 1 
ATOM   9469  N N   . SER E 1 211 ? -15.088 52.594  35.861  1.00 34.93 ? 207 SER E N   1 
ATOM   9470  C CA  . SER E 1 211 ? -13.685 52.172  35.815  1.00 35.55 ? 207 SER E CA  1 
ATOM   9471  C C   . SER E 1 211 ? -13.307 51.561  34.459  1.00 35.66 ? 207 SER E C   1 
ATOM   9472  O O   . SER E 1 211 ? -12.137 51.564  34.089  1.00 36.14 ? 207 SER E O   1 
ATOM   9473  C CB  . SER E 1 211 ? -13.347 51.218  36.964  1.00 35.42 ? 207 SER E CB  1 
ATOM   9474  O OG  . SER E 1 211 ? -14.001 49.976  36.795  1.00 36.79 ? 207 SER E OG  1 
ATOM   9475  N N   . THR E 1 212 ? -14.299 51.058  33.723  1.00 35.77 ? 208 THR E N   1 
ATOM   9476  C CA  . THR E 1 212 ? -14.072 50.461  32.402  1.00 35.61 ? 208 THR E CA  1 
ATOM   9477  C C   . THR E 1 212 ? -14.792 51.203  31.277  1.00 35.41 ? 208 THR E C   1 
ATOM   9478  O O   . THR E 1 212 ? -14.506 50.979  30.108  1.00 35.53 ? 208 THR E O   1 
ATOM   9479  C CB  . THR E 1 212 ? -14.490 48.966  32.357  1.00 35.72 ? 208 THR E CB  1 
ATOM   9480  O OG1 . THR E 1 212 ? -15.883 48.840  32.665  1.00 35.48 ? 208 THR E OG1 1 
ATOM   9481  C CG2 . THR E 1 212 ? -13.671 48.131  33.350  1.00 36.16 ? 208 THR E CG2 1 
ATOM   9482  N N   . LEU E 1 213 ? -15.727 52.081  31.625  1.00 35.33 ? 209 LEU E N   1 
ATOM   9483  C CA  . LEU E 1 213 ? -16.511 52.798  30.617  1.00 35.02 ? 209 LEU E CA  1 
ATOM   9484  C C   . LEU E 1 213 ? -16.112 54.262  30.468  1.00 34.97 ? 209 LEU E C   1 
ATOM   9485  O O   . LEU E 1 213 ? -15.847 54.954  31.456  1.00 34.85 ? 209 LEU E O   1 
ATOM   9486  C CB  . LEU E 1 213 ? -18.011 52.693  30.921  1.00 35.05 ? 209 LEU E CB  1 
ATOM   9487  C CG  . LEU E 1 213 ? -18.988 53.394  29.969  1.00 34.80 ? 209 LEU E CG  1 
ATOM   9488  C CD1 . LEU E 1 213 ? -19.215 52.573  28.694  1.00 34.56 ? 209 LEU E CD1 1 
ATOM   9489  C CD2 . LEU E 1 213 ? -20.297 53.671  30.681  1.00 35.20 ? 209 LEU E CD2 1 
ATOM   9490  N N   . ASN E 1 214 ? -16.073 54.718  29.219  1.00 34.94 ? 210 ASN E N   1 
ATOM   9491  C CA  . ASN E 1 214 ? -15.845 56.117  28.895  1.00 35.04 ? 210 ASN E CA  1 
ATOM   9492  C C   . ASN E 1 214 ? -16.665 56.506  27.666  1.00 35.47 ? 210 ASN E C   1 
ATOM   9493  O O   . ASN E 1 214 ? -16.385 56.043  26.558  1.00 35.45 ? 210 ASN E O   1 
ATOM   9494  C CB  . ASN E 1 214 ? -14.349 56.381  28.656  1.00 34.70 ? 210 ASN E CB  1 
ATOM   9495  C CG  . ASN E 1 214 ? -14.036 57.861  28.439  1.00 34.68 ? 210 ASN E CG  1 
ATOM   9496  O OD1 . ASN E 1 214 ? -14.433 58.716  29.229  1.00 35.11 ? 210 ASN E OD1 1 
ATOM   9497  N ND2 . ASN E 1 214 ? -13.316 58.163  27.367  1.00 34.19 ? 210 ASN E ND2 1 
ATOM   9498  N N   . GLN E 1 215 ? -17.683 57.344  27.859  1.00 35.88 ? 211 GLN E N   1 
ATOM   9499  C CA  . GLN E 1 215 ? -18.457 57.856  26.727  1.00 36.46 ? 211 GLN E CA  1 
ATOM   9500  C C   . GLN E 1 215 ? -18.883 59.315  26.875  1.00 36.63 ? 211 GLN E C   1 
ATOM   9501  O O   . GLN E 1 215 ? -19.174 59.784  27.977  1.00 36.59 ? 211 GLN E O   1 
ATOM   9502  C CB  . GLN E 1 215 ? -19.666 56.962  26.414  1.00 36.57 ? 211 GLN E CB  1 
ATOM   9503  C CG  . GLN E 1 215 ? -20.825 57.071  27.384  1.00 37.70 ? 211 GLN E CG  1 
ATOM   9504  C CD  . GLN E 1 215 ? -22.075 56.314  26.927  1.00 39.33 ? 211 GLN E CD  1 
ATOM   9505  O OE1 . GLN E 1 215 ? -23.198 56.703  27.255  1.00 39.93 ? 211 GLN E OE1 1 
ATOM   9506  N NE2 . GLN E 1 215 ? -21.883 55.230  26.179  1.00 39.24 ? 211 GLN E NE2 1 
ATOM   9507  N N   . ARG E 1 216 ? -18.888 60.023  25.749  1.00 36.81 ? 212 ARG E N   1 
ATOM   9508  C CA  . ARG E 1 216 ? -19.416 61.375  25.677  1.00 36.99 ? 212 ARG E CA  1 
ATOM   9509  C C   . ARG E 1 216 ? -20.353 61.468  24.471  1.00 37.13 ? 212 ARG E C   1 
ATOM   9510  O O   . ARG E 1 216 ? -19.914 61.478  23.316  1.00 37.01 ? 212 ARG E O   1 
ATOM   9511  C CB  . ARG E 1 216 ? -18.290 62.410  25.606  1.00 37.11 ? 212 ARG E CB  1 
ATOM   9512  C CG  . ARG E 1 216 ? -18.706 63.827  26.019  1.00 37.88 ? 212 ARG E CG  1 
ATOM   9513  C CD  . ARG E 1 216 ? -17.547 64.795  25.876  1.00 39.23 ? 212 ARG E CD  1 
ATOM   9514  N NE  . ARG E 1 216 ? -17.915 66.185  26.154  1.00 40.91 ? 212 ARG E NE  1 
ATOM   9515  C CZ  . ARG E 1 216 ? -17.725 66.809  27.318  1.00 42.17 ? 212 ARG E CZ  1 
ATOM   9516  N NH1 . ARG E 1 216 ? -17.176 66.178  28.356  1.00 41.80 ? 212 ARG E NH1 1 
ATOM   9517  N NH2 . ARG E 1 216 ? -18.087 68.079  27.447  1.00 42.64 ? 212 ARG E NH2 1 
ATOM   9518  N N   . LEU E 1 217 ? -21.650 61.512  24.761  1.00 37.33 ? 213 LEU E N   1 
ATOM   9519  C CA  . LEU E 1 217 ? -22.685 61.544  23.745  1.00 37.62 ? 213 LEU E CA  1 
ATOM   9520  C C   . LEU E 1 217 ? -23.099 62.972  23.433  1.00 37.83 ? 213 LEU E C   1 
ATOM   9521  O O   . LEU E 1 217 ? -23.329 63.774  24.341  1.00 37.77 ? 213 LEU E O   1 
ATOM   9522  C CB  . LEU E 1 217 ? -23.911 60.754  24.208  1.00 37.55 ? 213 LEU E CB  1 
ATOM   9523  C CG  . LEU E 1 217 ? -23.743 59.296  24.645  1.00 38.40 ? 213 LEU E CG  1 
ATOM   9524  C CD1 . LEU E 1 217 ? -24.979 58.827  25.415  1.00 38.33 ? 213 LEU E CD1 1 
ATOM   9525  C CD2 . LEU E 1 217 ? -23.446 58.372  23.455  1.00 38.42 ? 213 LEU E CD2 1 
ATOM   9526  N N   . VAL E 1 218 ? -23.187 63.278  22.141  1.00 38.11 ? 214 VAL E N   1 
ATOM   9527  C CA  . VAL E 1 218 ? -23.729 64.547  21.671  1.00 38.21 ? 214 VAL E CA  1 
ATOM   9528  C C   . VAL E 1 218 ? -25.037 64.252  20.933  1.00 38.42 ? 214 VAL E C   1 
ATOM   9529  O O   . VAL E 1 218 ? -25.084 63.350  20.092  1.00 38.29 ? 214 VAL E O   1 
ATOM   9530  C CB  . VAL E 1 218 ? -22.724 65.305  20.757  1.00 38.36 ? 214 VAL E CB  1 
ATOM   9531  C CG1 . VAL E 1 218 ? -23.316 66.627  20.251  1.00 38.21 ? 214 VAL E CG1 1 
ATOM   9532  C CG2 . VAL E 1 218 ? -21.413 65.572  21.497  1.00 38.01 ? 214 VAL E CG2 1 
ATOM   9533  N N   . PRO E 1 219 ? -26.111 64.998  21.261  1.00 38.72 ? 215 PRO E N   1 
ATOM   9534  C CA  . PRO E 1 219 ? -27.408 64.794  20.617  1.00 38.83 ? 215 PRO E CA  1 
ATOM   9535  C C   . PRO E 1 219 ? -27.344 65.072  19.123  1.00 38.92 ? 215 PRO E C   1 
ATOM   9536  O O   . PRO E 1 219 ? -26.638 65.981  18.687  1.00 39.04 ? 215 PRO E O   1 
ATOM   9537  C CB  . PRO E 1 219 ? -28.308 65.826  21.304  1.00 38.99 ? 215 PRO E CB  1 
ATOM   9538  C CG  . PRO E 1 219 ? -27.618 66.142  22.586  1.00 38.66 ? 215 PRO E CG  1 
ATOM   9539  C CD  . PRO E 1 219 ? -26.172 66.058  22.284  1.00 38.71 ? 215 PRO E CD  1 
ATOM   9540  N N   . GLU E 1 220 ? -28.073 64.279  18.352  1.00 39.04 ? 216 GLU E N   1 
ATOM   9541  C CA  . GLU E 1 220 ? -28.099 64.422  16.906  1.00 39.35 ? 216 GLU E CA  1 
ATOM   9542  C C   . GLU E 1 220 ? -29.437 65.012  16.489  1.00 39.40 ? 216 GLU E C   1 
ATOM   9543  O O   . GLU E 1 220 ? -30.459 64.333  16.505  1.00 39.47 ? 216 GLU E O   1 
ATOM   9544  C CB  . GLU E 1 220 ? -27.868 63.066  16.240  1.00 39.34 ? 216 GLU E CB  1 
ATOM   9545  C CG  . GLU E 1 220 ? -26.511 62.461  16.547  1.00 39.63 ? 216 GLU E CG  1 
ATOM   9546  C CD  . GLU E 1 220 ? -26.437 60.974  16.261  1.00 40.46 ? 216 GLU E CD  1 
ATOM   9547  O OE1 . GLU E 1 220 ? -27.340 60.429  15.580  1.00 41.09 ? 216 GLU E OE1 1 
ATOM   9548  O OE2 . GLU E 1 220 ? -25.463 60.346  16.723  1.00 40.57 ? 216 GLU E OE2 1 
ATOM   9549  N N   . ILE E 1 221 ? -29.425 66.288  16.130  1.00 39.66 ? 217 ILE E N   1 
ATOM   9550  C CA  . ILE E 1 221 ? -30.656 67.017  15.842  1.00 39.88 ? 217 ILE E CA  1 
ATOM   9551  C C   . ILE E 1 221 ? -30.999 66.945  14.351  1.00 40.03 ? 217 ILE E C   1 
ATOM   9552  O O   . ILE E 1 221 ? -30.278 67.490  13.509  1.00 39.90 ? 217 ILE E O   1 
ATOM   9553  C CB  . ILE E 1 221 ? -30.553 68.478  16.327  1.00 39.93 ? 217 ILE E CB  1 
ATOM   9554  C CG1 . ILE E 1 221 ? -30.386 68.518  17.855  1.00 40.00 ? 217 ILE E CG1 1 
ATOM   9555  C CG2 . ILE E 1 221 ? -31.772 69.270  15.898  1.00 39.71 ? 217 ILE E CG2 1 
ATOM   9556  C CD1 . ILE E 1 221 ? -29.731 69.793  18.384  1.00 39.90 ? 217 ILE E CD1 1 
ATOM   9557  N N   . ALA E 1 222 ? -32.098 66.256  14.041  1.00 40.16 ? 218 ALA E N   1 
ATOM   9558  C CA  . ALA E 1 222 ? -32.503 65.987  12.656  1.00 40.37 ? 218 ALA E CA  1 
ATOM   9559  C C   . ALA E 1 222 ? -33.940 65.486  12.574  1.00 40.51 ? 218 ALA E C   1 
ATOM   9560  O O   . ALA E 1 222 ? -34.439 64.848  13.504  1.00 40.66 ? 218 ALA E O   1 
ATOM   9561  C CB  . ALA E 1 222 ? -31.566 64.970  12.012  1.00 40.27 ? 218 ALA E CB  1 
ATOM   9562  N N   . THR E 1 223 ? -34.606 65.778  11.460  1.00 40.80 ? 219 THR E N   1 
ATOM   9563  C CA  . THR E 1 223 ? -35.964 65.285  11.248  1.00 41.05 ? 219 THR E CA  1 
ATOM   9564  C C   . THR E 1 223 ? -35.932 63.886  10.638  1.00 40.85 ? 219 THR E C   1 
ATOM   9565  O O   . THR E 1 223 ? -35.294 63.642  9.615   1.00 40.75 ? 219 THR E O   1 
ATOM   9566  C CB  . THR E 1 223 ? -36.848 66.282  10.445  1.00 41.25 ? 219 THR E CB  1 
ATOM   9567  O OG1 . THR E 1 223 ? -37.113 67.432  11.261  1.00 42.13 ? 219 THR E OG1 1 
ATOM   9568  C CG2 . THR E 1 223 ? -38.188 65.652  10.056  1.00 41.10 ? 219 THR E CG2 1 
ATOM   9569  N N   . ARG E 1 224 ? -36.609 62.973  11.320  1.00 40.81 ? 220 ARG E N   1 
ATOM   9570  C CA  . ARG E 1 224 ? -36.672 61.578  10.943  1.00 40.83 ? 220 ARG E CA  1 
ATOM   9571  C C   . ARG E 1 224 ? -38.153 61.260  10.781  1.00 40.99 ? 220 ARG E C   1 
ATOM   9572  O O   . ARG E 1 224 ? -38.986 61.932  11.397  1.00 40.97 ? 220 ARG E O   1 
ATOM   9573  C CB  . ARG E 1 224 ? -36.054 60.724  12.054  1.00 40.87 ? 220 ARG E CB  1 
ATOM   9574  C CG  . ARG E 1 224 ? -34.608 61.104  12.403  1.00 40.55 ? 220 ARG E CG  1 
ATOM   9575  C CD  . ARG E 1 224 ? -34.421 61.243  13.902  1.00 39.90 ? 220 ARG E CD  1 
ATOM   9576  N NE  . ARG E 1 224 ? -33.009 61.211  14.277  1.00 40.65 ? 220 ARG E NE  1 
ATOM   9577  C CZ  . ARG E 1 224 ? -32.382 62.149  14.985  1.00 40.17 ? 220 ARG E CZ  1 
ATOM   9578  N NH1 . ARG E 1 224 ? -33.031 63.218  15.429  1.00 39.64 ? 220 ARG E NH1 1 
ATOM   9579  N NH2 . ARG E 1 224 ? -31.094 62.008  15.259  1.00 40.47 ? 220 ARG E NH2 1 
ATOM   9580  N N   . PRO E 1 225 ? -38.495 60.253  9.947   1.00 41.01 ? 221 PRO E N   1 
ATOM   9581  C CA  . PRO E 1 225 ? -39.905 59.919  9.728   1.00 41.00 ? 221 PRO E CA  1 
ATOM   9582  C C   . PRO E 1 225 ? -40.641 59.646  11.030  1.00 41.07 ? 221 PRO E C   1 
ATOM   9583  O O   . PRO E 1 225 ? -40.033 59.196  11.998  1.00 41.17 ? 221 PRO E O   1 
ATOM   9584  C CB  . PRO E 1 225 ? -39.838 58.640  8.890   1.00 40.97 ? 221 PRO E CB  1 
ATOM   9585  C CG  . PRO E 1 225 ? -38.549 58.728  8.174   1.00 41.05 ? 221 PRO E CG  1 
ATOM   9586  C CD  . PRO E 1 225 ? -37.602 59.420  9.117   1.00 41.05 ? 221 PRO E CD  1 
ATOM   9587  N N   . LYS E 1 226 ? -41.940 59.932  11.050  1.00 41.23 ? 222 LYS E N   1 
ATOM   9588  C CA  . LYS E 1 226 ? -42.762 59.705  12.231  1.00 41.25 ? 222 LYS E CA  1 
ATOM   9589  C C   . LYS E 1 226 ? -42.892 58.215  12.511  1.00 41.06 ? 222 LYS E C   1 
ATOM   9590  O O   . LYS E 1 226 ? -43.114 57.423  11.596  1.00 41.29 ? 222 LYS E O   1 
ATOM   9591  C CB  . LYS E 1 226 ? -44.153 60.303  12.037  1.00 41.57 ? 222 LYS E CB  1 
ATOM   9592  C CG  . LYS E 1 226 ? -44.180 61.793  11.726  1.00 42.90 ? 222 LYS E CG  1 
ATOM   9593  C CD  . LYS E 1 226 ? -44.328 62.630  12.989  1.00 44.69 ? 222 LYS E CD  1 
ATOM   9594  C CE  . LYS E 1 226 ? -44.775 64.044  12.659  1.00 45.53 ? 222 LYS E CE  1 
ATOM   9595  N NZ  . LYS E 1 226 ? -46.109 64.043  11.994  1.00 46.54 ? 222 LYS E NZ  1 
ATOM   9596  N N   . VAL E 1 227 ? -42.721 57.841  13.774  1.00 40.79 ? 223 VAL E N   1 
ATOM   9597  C CA  . VAL E 1 227 ? -43.019 56.496  14.252  1.00 40.47 ? 223 VAL E CA  1 
ATOM   9598  C C   . VAL E 1 227 ? -43.703 56.686  15.594  1.00 40.50 ? 223 VAL E C   1 
ATOM   9599  O O   . VAL E 1 227 ? -43.114 57.265  16.516  1.00 40.54 ? 223 VAL E O   1 
ATOM   9600  C CB  . VAL E 1 227 ? -41.747 55.630  14.434  1.00 40.49 ? 223 VAL E CB  1 
ATOM   9601  C CG1 . VAL E 1 227 ? -42.119 54.217  14.882  1.00 40.30 ? 223 VAL E CG1 1 
ATOM   9602  C CG2 . VAL E 1 227 ? -40.928 55.575  13.156  1.00 40.00 ? 223 VAL E CG2 1 
ATOM   9603  N N   . ASN E 1 228 ? -44.944 56.208  15.700  1.00 40.23 ? 224 ASN E N   1 
ATOM   9604  C CA  . ASN E 1 228 ? -45.805 56.493  16.857  1.00 40.05 ? 224 ASN E CA  1 
ATOM   9605  C C   . ASN E 1 228 ? -45.938 58.004  17.095  1.00 39.76 ? 224 ASN E C   1 
ATOM   9606  O O   . ASN E 1 228 ? -45.977 58.469  18.238  1.00 39.72 ? 224 ASN E O   1 
ATOM   9607  C CB  . ASN E 1 228 ? -45.294 55.793  18.126  1.00 40.26 ? 224 ASN E CB  1 
ATOM   9608  C CG  . ASN E 1 228 ? -45.319 54.278  18.020  1.00 41.14 ? 224 ASN E CG  1 
ATOM   9609  O OD1 . ASN E 1 228 ? -45.809 53.709  17.039  1.00 41.89 ? 224 ASN E OD1 1 
ATOM   9610  N ND2 . ASN E 1 228 ? -44.781 53.612  19.040  1.00 41.38 ? 224 ASN E ND2 1 
ATOM   9611  N N   . GLY E 1 229 ? -45.986 58.759  16.000  1.00 39.43 ? 225 GLY E N   1 
ATOM   9612  C CA  . GLY E 1 229 ? -46.137 60.209  16.048  1.00 38.85 ? 225 GLY E CA  1 
ATOM   9613  C C   . GLY E 1 229 ? -44.843 60.981  16.219  1.00 38.59 ? 225 GLY E C   1 
ATOM   9614  O O   . GLY E 1 229 ? -44.842 62.210  16.131  1.00 38.76 ? 225 GLY E O   1 
ATOM   9615  N N   . GLN E 1 230 ? -43.734 60.275  16.447  1.00 38.13 ? 226 GLN E N   1 
ATOM   9616  C CA  . GLN E 1 230 ? -42.481 60.944  16.821  1.00 37.27 ? 226 GLN E CA  1 
ATOM   9617  C C   . GLN E 1 230 ? -41.469 61.108  15.696  1.00 36.80 ? 226 GLN E C   1 
ATOM   9618  O O   . GLN E 1 230 ? -41.123 60.154  14.998  1.00 36.59 ? 226 GLN E O   1 
ATOM   9619  C CB  . GLN E 1 230 ? -41.834 60.266  18.029  1.00 37.32 ? 226 GLN E CB  1 
ATOM   9620  C CG  . GLN E 1 230 ? -42.766 60.099  19.222  1.00 37.29 ? 226 GLN E CG  1 
ATOM   9621  C CD  . GLN E 1 230 ? -43.493 61.381  19.591  1.00 37.53 ? 226 GLN E CD  1 
ATOM   9622  O OE1 . GLN E 1 230 ? -42.877 62.442  19.729  1.00 38.09 ? 226 GLN E OE1 1 
ATOM   9623  N NE2 . GLN E 1 230 ? -44.809 61.290  19.751  1.00 36.81 ? 226 GLN E NE2 1 
ATOM   9624  N N   . SER E 1 231 ? -41.001 62.344  15.553  1.00 36.37 ? 227 SER E N   1 
ATOM   9625  C CA  . SER E 1 231 ? -40.035 62.741  14.536  1.00 35.90 ? 227 SER E CA  1 
ATOM   9626  C C   . SER E 1 231 ? -38.598 62.705  15.080  1.00 35.57 ? 227 SER E C   1 
ATOM   9627  O O   . SER E 1 231 ? -37.626 62.732  14.314  1.00 35.47 ? 227 SER E O   1 
ATOM   9628  C CB  . SER E 1 231 ? -40.379 64.147  14.040  1.00 35.86 ? 227 SER E CB  1 
ATOM   9629  O OG  . SER E 1 231 ? -39.488 64.569  13.027  1.00 36.49 ? 227 SER E OG  1 
ATOM   9630  N N   . GLY E 1 232 ? -38.475 62.666  16.404  1.00 35.06 ? 228 GLY E N   1 
ATOM   9631  C CA  . GLY E 1 232 ? -37.184 62.497  17.054  1.00 34.76 ? 228 GLY E CA  1 
ATOM   9632  C C   . GLY E 1 232 ? -36.933 61.032  17.370  1.00 34.68 ? 228 GLY E C   1 
ATOM   9633  O O   . GLY E 1 232 ? -37.771 60.171  17.087  1.00 34.64 ? 228 GLY E O   1 
ATOM   9634  N N   . ARG E 1 233 ? -35.775 60.744  17.951  1.00 34.46 ? 229 ARG E N   1 
ATOM   9635  C CA  . ARG E 1 233 ? -35.442 59.385  18.357  1.00 34.29 ? 229 ARG E CA  1 
ATOM   9636  C C   . ARG E 1 233 ? -34.840 59.366  19.748  1.00 34.21 ? 229 ARG E C   1 
ATOM   9637  O O   . ARG E 1 233 ? -34.318 60.373  20.225  1.00 34.15 ? 229 ARG E O   1 
ATOM   9638  C CB  . ARG E 1 233 ? -34.464 58.738  17.366  1.00 34.11 ? 229 ARG E CB  1 
ATOM   9639  C CG  . ARG E 1 233 ? -35.018 58.482  15.969  1.00 33.98 ? 229 ARG E CG  1 
ATOM   9640  C CD  . ARG E 1 233 ? -36.206 57.538  15.981  1.00 34.41 ? 229 ARG E CD  1 
ATOM   9641  N NE  . ARG E 1 233 ? -36.710 57.288  14.632  1.00 34.95 ? 229 ARG E NE  1 
ATOM   9642  C CZ  . ARG E 1 233 ? -37.729 57.932  14.062  1.00 34.94 ? 229 ARG E CZ  1 
ATOM   9643  N NH1 . ARG E 1 233 ? -38.382 58.886  14.711  1.00 34.27 ? 229 ARG E NH1 1 
ATOM   9644  N NH2 . ARG E 1 233 ? -38.098 57.614  12.830  1.00 35.13 ? 229 ARG E NH2 1 
ATOM   9645  N N   . MET E 1 234 ? -34.921 58.211  20.396  1.00 34.17 ? 230 MET E N   1 
ATOM   9646  C CA  . MET E 1 234 ? -34.152 57.973  21.606  1.00 34.09 ? 230 MET E CA  1 
ATOM   9647  C C   . MET E 1 234 ? -33.180 56.821  21.438  1.00 33.79 ? 230 MET E C   1 
ATOM   9648  O O   . MET E 1 234 ? -33.441 55.877  20.692  1.00 33.86 ? 230 MET E O   1 
ATOM   9649  C CB  . MET E 1 234 ? -35.065 57.755  22.798  1.00 34.38 ? 230 MET E CB  1 
ATOM   9650  C CG  . MET E 1 234 ? -35.444 59.063  23.436  1.00 35.62 ? 230 MET E CG  1 
ATOM   9651  S SD  . MET E 1 234 ? -36.500 58.867  24.854  1.00 38.14 ? 230 MET E SD  1 
ATOM   9652  C CE  . MET E 1 234 ? -37.189 60.518  24.906  1.00 38.84 ? 230 MET E CE  1 
ATOM   9653  N N   . GLU E 1 235 ? -32.044 56.920  22.117  1.00 33.21 ? 231 GLU E N   1 
ATOM   9654  C CA  . GLU E 1 235 ? -31.010 55.911  22.022  1.00 32.82 ? 231 GLU E CA  1 
ATOM   9655  C C   . GLU E 1 235 ? -30.629 55.486  23.432  1.00 32.58 ? 231 GLU E C   1 
ATOM   9656  O O   . GLU E 1 235 ? -30.355 56.331  24.283  1.00 32.64 ? 231 GLU E O   1 
ATOM   9657  C CB  . GLU E 1 235 ? -29.804 56.458  21.255  1.00 32.79 ? 231 GLU E CB  1 
ATOM   9658  C CG  . GLU E 1 235 ? -28.759 55.418  20.867  1.00 32.92 ? 231 GLU E CG  1 
ATOM   9659  C CD  . GLU E 1 235 ? -27.566 56.017  20.128  1.00 33.66 ? 231 GLU E CD  1 
ATOM   9660  O OE1 . GLU E 1 235 ? -26.620 55.261  19.823  1.00 33.81 ? 231 GLU E OE1 1 
ATOM   9661  O OE2 . GLU E 1 235 ? -27.562 57.238  19.854  1.00 34.23 ? 231 GLU E OE2 1 
ATOM   9662  N N   . PHE E 1 236 ? -30.620 54.178  23.670  1.00 32.09 ? 232 PHE E N   1 
ATOM   9663  C CA  . PHE E 1 236 ? -30.380 53.642  25.003  1.00 31.78 ? 232 PHE E CA  1 
ATOM   9664  C C   . PHE E 1 236 ? -29.072 52.882  25.129  1.00 31.38 ? 232 PHE E C   1 
ATOM   9665  O O   . PHE E 1 236 ? -28.633 52.216  24.200  1.00 31.49 ? 232 PHE E O   1 
ATOM   9666  C CB  . PHE E 1 236 ? -31.559 52.775  25.453  1.00 31.74 ? 232 PHE E CB  1 
ATOM   9667  C CG  . PHE E 1 236 ? -32.823 53.555  25.645  1.00 32.22 ? 232 PHE E CG  1 
ATOM   9668  C CD1 . PHE E 1 236 ? -33.814 53.546  24.668  1.00 32.68 ? 232 PHE E CD1 1 
ATOM   9669  C CD2 . PHE E 1 236 ? -33.004 54.336  26.783  1.00 31.92 ? 232 PHE E CD2 1 
ATOM   9670  C CE1 . PHE E 1 236 ? -34.981 54.283  24.832  1.00 32.91 ? 232 PHE E CE1 1 
ATOM   9671  C CE2 . PHE E 1 236 ? -34.163 55.078  26.957  1.00 32.82 ? 232 PHE E CE2 1 
ATOM   9672  C CZ  . PHE E 1 236 ? -35.156 55.054  25.976  1.00 32.97 ? 232 PHE E CZ  1 
ATOM   9673  N N   . PHE E 1 237 ? -28.465 52.991  26.303  1.00 30.99 ? 233 PHE E N   1 
ATOM   9674  C CA  . PHE E 1 237 ? -27.183 52.371  26.579  1.00 30.56 ? 233 PHE E CA  1 
ATOM   9675  C C   . PHE E 1 237 ? -27.273 51.618  27.887  1.00 30.43 ? 233 PHE E C   1 
ATOM   9676  O O   . PHE E 1 237 ? -28.169 51.868  28.693  1.00 30.40 ? 233 PHE E O   1 
ATOM   9677  C CB  . PHE E 1 237 ? -26.083 53.433  26.651  1.00 30.35 ? 233 PHE E CB  1 
ATOM   9678  C CG  . PHE E 1 237 ? -25.917 54.211  25.384  1.00 30.25 ? 233 PHE E CG  1 
ATOM   9679  C CD1 . PHE E 1 237 ? -26.649 55.376  25.165  1.00 30.25 ? 233 PHE E CD1 1 
ATOM   9680  C CD2 . PHE E 1 237 ? -25.041 53.772  24.395  1.00 30.22 ? 233 PHE E CD2 1 
ATOM   9681  C CE1 . PHE E 1 237 ? -26.509 56.092  23.974  1.00 30.25 ? 233 PHE E CE1 1 
ATOM   9682  C CE2 . PHE E 1 237 ? -24.890 54.485  23.204  1.00 29.80 ? 233 PHE E CE2 1 
ATOM   9683  C CZ  . PHE E 1 237 ? -25.621 55.647  22.995  1.00 29.64 ? 233 PHE E CZ  1 
ATOM   9684  N N   . TRP E 1 238 ? -26.341 50.692  28.094  1.00 30.34 ? 234 TRP E N   1 
ATOM   9685  C CA  . TRP E 1 238 ? -26.312 49.901  29.316  1.00 30.07 ? 234 TRP E CA  1 
ATOM   9686  C C   . TRP E 1 238 ? -24.892 49.531  29.694  1.00 30.26 ? 234 TRP E C   1 
ATOM   9687  O O   . TRP E 1 238 ? -24.001 49.495  28.852  1.00 30.02 ? 234 TRP E O   1 
ATOM   9688  C CB  . TRP E 1 238 ? -27.178 48.646  29.174  1.00 29.81 ? 234 TRP E CB  1 
ATOM   9689  C CG  . TRP E 1 238 ? -26.709 47.694  28.117  1.00 29.09 ? 234 TRP E CG  1 
ATOM   9690  C CD1 . TRP E 1 238 ? -27.018 47.734  26.791  1.00 27.94 ? 234 TRP E CD1 1 
ATOM   9691  C CD2 . TRP E 1 238 ? -25.854 46.554  28.298  1.00 28.04 ? 234 TRP E CD2 1 
ATOM   9692  N NE1 . TRP E 1 238 ? -26.410 46.696  26.131  1.00 28.27 ? 234 TRP E NE1 1 
ATOM   9693  C CE2 . TRP E 1 238 ? -25.689 45.954  27.030  1.00 28.30 ? 234 TRP E CE2 1 
ATOM   9694  C CE3 . TRP E 1 238 ? -25.216 45.980  29.409  1.00 27.43 ? 234 TRP E CE3 1 
ATOM   9695  C CZ2 . TRP E 1 238 ? -24.909 44.808  26.836  1.00 27.88 ? 234 TRP E CZ2 1 
ATOM   9696  C CZ3 . TRP E 1 238 ? -24.440 44.841  29.223  1.00 27.41 ? 234 TRP E CZ3 1 
ATOM   9697  C CH2 . TRP E 1 238 ? -24.292 44.266  27.940  1.00 28.48 ? 234 TRP E CH2 1 
ATOM   9698  N N   . THR E 1 239 ? -24.689 49.272  30.978  1.00 30.77 ? 235 THR E N   1 
ATOM   9699  C CA  . THR E 1 239 ? -23.398 48.841  31.476  1.00 31.17 ? 235 THR E CA  1 
ATOM   9700  C C   . THR E 1 239 ? -23.596 47.903  32.648  1.00 31.70 ? 235 THR E C   1 
ATOM   9701  O O   . THR E 1 239 ? -24.606 47.985  33.359  1.00 31.77 ? 235 THR E O   1 
ATOM   9702  C CB  . THR E 1 239 ? -22.521 50.043  31.899  1.00 31.16 ? 235 THR E CB  1 
ATOM   9703  O OG1 . THR E 1 239 ? -21.140 49.672  31.842  1.00 31.40 ? 235 THR E OG1 1 
ATOM   9704  C CG2 . THR E 1 239 ? -22.863 50.528  33.307  1.00 30.95 ? 235 THR E CG2 1 
ATOM   9705  N N   . ILE E 1 240 ? -22.645 46.994  32.828  1.00 32.32 ? 236 ILE E N   1 
ATOM   9706  C CA  . ILE E 1 240 ? -22.590 46.185  34.033  1.00 32.81 ? 236 ILE E CA  1 
ATOM   9707  C C   . ILE E 1 240 ? -21.624 46.872  34.989  1.00 33.21 ? 236 ILE E C   1 
ATOM   9708  O O   . ILE E 1 240 ? -20.437 47.014  34.699  1.00 33.09 ? 236 ILE E O   1 
ATOM   9709  C CB  . ILE E 1 240 ? -22.135 44.734  33.757  1.00 32.90 ? 236 ILE E CB  1 
ATOM   9710  C CG1 . ILE E 1 240 ? -23.087 44.037  32.779  1.00 32.94 ? 236 ILE E CG1 1 
ATOM   9711  C CG2 . ILE E 1 240 ? -22.007 43.943  35.072  1.00 32.89 ? 236 ILE E CG2 1 
ATOM   9712  C CD1 . ILE E 1 240 ? -24.530 43.859  33.283  1.00 33.15 ? 236 ILE E CD1 1 
ATOM   9713  N N   . LEU E 1 241 ? -22.159 47.319  36.118  1.00 33.78 ? 237 LEU E N   1 
ATOM   9714  C CA  . LEU E 1 241 ? -21.364 47.955  37.149  1.00 34.39 ? 237 LEU E CA  1 
ATOM   9715  C C   . LEU E 1 241 ? -21.047 46.944  38.246  1.00 34.75 ? 237 LEU E C   1 
ATOM   9716  O O   . LEU E 1 241 ? -21.951 46.395  38.882  1.00 34.79 ? 237 LEU E O   1 
ATOM   9717  C CB  . LEU E 1 241 ? -22.116 49.159  37.711  1.00 34.44 ? 237 LEU E CB  1 
ATOM   9718  C CG  . LEU E 1 241 ? -21.380 50.052  38.703  1.00 34.89 ? 237 LEU E CG  1 
ATOM   9719  C CD1 . LEU E 1 241 ? -20.233 50.807  38.024  1.00 34.56 ? 237 LEU E CD1 1 
ATOM   9720  C CD2 . LEU E 1 241 ? -22.383 51.008  39.327  1.00 35.25 ? 237 LEU E CD2 1 
ATOM   9721  N N   . LYS E 1 242 ? -19.758 46.686  38.443  1.00 35.36 ? 238 LYS E N   1 
ATOM   9722  C CA  . LYS E 1 242 ? -19.297 45.733  39.456  1.00 35.94 ? 238 LYS E CA  1 
ATOM   9723  C C   . LYS E 1 242 ? -19.431 46.298  40.872  1.00 35.72 ? 238 LYS E C   1 
ATOM   9724  O O   . LYS E 1 242 ? -19.416 47.517  41.045  1.00 35.46 ? 238 LYS E O   1 
ATOM   9725  C CB  . LYS E 1 242 ? -17.845 45.329  39.184  1.00 36.26 ? 238 LYS E CB  1 
ATOM   9726  C CG  . LYS E 1 242 ? -17.698 44.258  38.121  1.00 37.81 ? 238 LYS E CG  1 
ATOM   9727  C CD  . LYS E 1 242 ? -16.239 44.004  37.797  1.00 40.49 ? 238 LYS E CD  1 
ATOM   9728  C CE  . LYS E 1 242 ? -16.099 42.905  36.753  1.00 42.02 ? 238 LYS E CE  1 
ATOM   9729  N NZ  . LYS E 1 242 ? -14.723 42.865  36.183  1.00 43.48 ? 238 LYS E NZ  1 
ATOM   9730  N N   . PRO E 1 243 ? -19.571 45.412  41.885  1.00 35.86 ? 239 PRO E N   1 
ATOM   9731  C CA  . PRO E 1 243 ? -19.568 45.815  43.293  1.00 35.98 ? 239 PRO E CA  1 
ATOM   9732  C C   . PRO E 1 243 ? -18.387 46.730  43.614  1.00 36.28 ? 239 PRO E C   1 
ATOM   9733  O O   . PRO E 1 243 ? -17.246 46.413  43.265  1.00 36.29 ? 239 PRO E O   1 
ATOM   9734  C CB  . PRO E 1 243 ? -19.409 44.489  44.033  1.00 35.94 ? 239 PRO E CB  1 
ATOM   9735  C CG  . PRO E 1 243 ? -20.037 43.495  43.147  1.00 36.24 ? 239 PRO E CG  1 
ATOM   9736  C CD  . PRO E 1 243 ? -19.797 43.960  41.735  1.00 35.97 ? 239 PRO E CD  1 
ATOM   9737  N N   . ASN E 1 244 ? -18.682 47.861  44.252  1.00 36.46 ? 240 ASN E N   1 
ATOM   9738  C CA  . ASN E 1 244 ? -17.690 48.876  44.642  1.00 37.03 ? 240 ASN E CA  1 
ATOM   9739  C C   . ASN E 1 244 ? -17.199 49.817  43.536  1.00 36.87 ? 240 ASN E C   1 
ATOM   9740  O O   . ASN E 1 244 ? -16.438 50.752  43.811  1.00 36.91 ? 240 ASN E O   1 
ATOM   9741  C CB  . ASN E 1 244 ? -16.507 48.265  45.421  1.00 37.32 ? 240 ASN E CB  1 
ATOM   9742  C CG  . ASN E 1 244 ? -16.884 47.869  46.835  1.00 38.47 ? 240 ASN E CG  1 
ATOM   9743  O OD1 . ASN E 1 244 ? -16.451 46.832  47.335  1.00 39.96 ? 240 ASN E OD1 1 
ATOM   9744  N ND2 . ASN E 1 244 ? -17.708 48.690  47.485  1.00 40.10 ? 240 ASN E ND2 1 
ATOM   9745  N N   . ASP E 1 245 ? -17.630 49.587  42.299  1.00 36.68 ? 241 ASP E N   1 
ATOM   9746  C CA  . ASP E 1 245 ? -17.371 50.566  41.249  1.00 36.48 ? 241 ASP E CA  1 
ATOM   9747  C C   . ASP E 1 245 ? -18.493 51.598  41.217  1.00 36.13 ? 241 ASP E C   1 
ATOM   9748  O O   . ASP E 1 245 ? -19.632 51.306  41.584  1.00 36.21 ? 241 ASP E O   1 
ATOM   9749  C CB  . ASP E 1 245 ? -17.171 49.912  39.874  1.00 36.68 ? 241 ASP E CB  1 
ATOM   9750  C CG  . ASP E 1 245 ? -16.517 50.861  38.861  1.00 37.34 ? 241 ASP E CG  1 
ATOM   9751  O OD1 . ASP E 1 245 ? -15.802 51.801  39.292  1.00 37.88 ? 241 ASP E OD1 1 
ATOM   9752  O OD2 . ASP E 1 245 ? -16.720 50.675  37.639  1.00 36.98 ? 241 ASP E OD2 1 
ATOM   9753  N N   . ALA E 1 246 ? -18.154 52.811  40.799  1.00 35.80 ? 242 ALA E N   1 
ATOM   9754  C CA  . ALA E 1 246 ? -19.115 53.897  40.717  1.00 35.53 ? 242 ALA E CA  1 
ATOM   9755  C C   . ALA E 1 246 ? -19.355 54.318  39.270  1.00 35.50 ? 242 ALA E C   1 
ATOM   9756  O O   . ALA E 1 246 ? -18.488 54.154  38.406  1.00 35.06 ? 242 ALA E O   1 
ATOM   9757  C CB  . ALA E 1 246 ? -18.637 55.077  41.534  1.00 35.34 ? 242 ALA E CB  1 
ATOM   9758  N N   . ILE E 1 247 ? -20.541 54.866  39.020  1.00 35.60 ? 243 ILE E N   1 
ATOM   9759  C CA  . ILE E 1 247 ? -20.869 55.448  37.722  1.00 35.62 ? 243 ILE E CA  1 
ATOM   9760  C C   . ILE E 1 247 ? -21.160 56.940  37.896  1.00 35.61 ? 243 ILE E C   1 
ATOM   9761  O O   . ILE E 1 247 ? -21.943 57.324  38.762  1.00 35.77 ? 243 ILE E O   1 
ATOM   9762  C CB  . ILE E 1 247 ? -22.038 54.675  37.022  1.00 35.57 ? 243 ILE E CB  1 
ATOM   9763  C CG1 . ILE E 1 247 ? -22.317 55.236  35.620  1.00 35.74 ? 243 ILE E CG1 1 
ATOM   9764  C CG2 . ILE E 1 247 ? -23.302 54.649  37.892  1.00 35.46 ? 243 ILE E CG2 1 
ATOM   9765  C CD1 . ILE E 1 247 ? -23.084 54.273  34.707  1.00 35.45 ? 243 ILE E CD1 1 
ATOM   9766  N N   . ASN E 1 248 ? -20.497 57.773  37.095  1.00 35.73 ? 244 ASN E N   1 
ATOM   9767  C CA  . ASN E 1 248 ? -20.676 59.226  37.153  1.00 35.91 ? 244 ASN E CA  1 
ATOM   9768  C C   . ASN E 1 248 ? -21.307 59.793  35.880  1.00 36.15 ? 244 ASN E C   1 
ATOM   9769  O O   . ASN E 1 248 ? -20.750 59.661  34.781  1.00 35.98 ? 244 ASN E O   1 
ATOM   9770  C CB  . ASN E 1 248 ? -19.338 59.936  37.408  1.00 35.91 ? 244 ASN E CB  1 
ATOM   9771  C CG  . ASN E 1 248 ? -18.642 59.450  38.659  1.00 36.30 ? 244 ASN E CG  1 
ATOM   9772  O OD1 . ASN E 1 248 ? -18.981 59.853  39.772  1.00 37.16 ? 244 ASN E OD1 1 
ATOM   9773  N ND2 . ASN E 1 248 ? -17.647 58.592  38.482  1.00 36.26 ? 244 ASN E ND2 1 
ATOM   9774  N N   . PHE E 1 249 ? -22.457 60.443  36.042  1.00 36.37 ? 245 PHE E N   1 
ATOM   9775  C CA  . PHE E 1 249 ? -23.137 61.116  34.938  1.00 36.65 ? 245 PHE E CA  1 
ATOM   9776  C C   . PHE E 1 249 ? -22.934 62.634  34.989  1.00 36.86 ? 245 PHE E C   1 
ATOM   9777  O O   . PHE E 1 249 ? -23.004 63.249  36.057  1.00 37.12 ? 245 PHE E O   1 
ATOM   9778  C CB  . PHE E 1 249 ? -24.641 60.813  34.969  1.00 36.64 ? 245 PHE E CB  1 
ATOM   9779  C CG  . PHE E 1 249 ? -24.989 59.369  34.726  1.00 36.38 ? 245 PHE E CG  1 
ATOM   9780  C CD1 . PHE E 1 249 ? -25.139 58.489  35.786  1.00 36.64 ? 245 PHE E CD1 1 
ATOM   9781  C CD2 . PHE E 1 249 ? -25.197 58.897  33.431  1.00 36.75 ? 245 PHE E CD2 1 
ATOM   9782  C CE1 . PHE E 1 249 ? -25.475 57.152  35.561  1.00 37.17 ? 245 PHE E CE1 1 
ATOM   9783  C CE2 . PHE E 1 249 ? -25.535 57.566  33.192  1.00 36.24 ? 245 PHE E CE2 1 
ATOM   9784  C CZ  . PHE E 1 249 ? -25.676 56.693  34.255  1.00 36.76 ? 245 PHE E CZ  1 
ATOM   9785  N N   . GLU E 1 250 ? -22.685 63.231  33.830  1.00 36.96 ? 246 GLU E N   1 
ATOM   9786  C CA  . GLU E 1 250 ? -22.692 64.683  33.692  1.00 37.16 ? 246 GLU E CA  1 
ATOM   9787  C C   . GLU E 1 250 ? -23.418 65.086  32.399  1.00 36.99 ? 246 GLU E C   1 
ATOM   9788  O O   . GLU E 1 250 ? -23.175 64.505  31.334  1.00 37.00 ? 246 GLU E O   1 
ATOM   9789  C CB  . GLU E 1 250 ? -21.269 65.251  33.742  1.00 37.18 ? 246 GLU E CB  1 
ATOM   9790  C CG  . GLU E 1 250 ? -21.207 66.776  33.804  1.00 38.47 ? 246 GLU E CG  1 
ATOM   9791  C CD  . GLU E 1 250 ? -19.788 67.322  33.912  1.00 40.34 ? 246 GLU E CD  1 
ATOM   9792  O OE1 . GLU E 1 250 ? -19.406 68.141  33.045  1.00 40.55 ? 246 GLU E OE1 1 
ATOM   9793  O OE2 . GLU E 1 250 ? -19.060 66.941  34.861  1.00 40.85 ? 246 GLU E OE2 1 
ATOM   9794  N N   . SER E 1 251 ? -24.304 66.077  32.503  1.00 36.61 ? 247 SER E N   1 
ATOM   9795  C CA  . SER E 1 251 ? -25.123 66.506  31.374  1.00 36.46 ? 247 SER E CA  1 
ATOM   9796  C C   . SER E 1 251 ? -25.761 67.883  31.563  1.00 36.53 ? 247 SER E C   1 
ATOM   9797  O O   . SER E 1 251 ? -26.141 68.256  32.675  1.00 36.27 ? 247 SER E O   1 
ATOM   9798  C CB  . SER E 1 251 ? -26.229 65.481  31.119  1.00 36.40 ? 247 SER E CB  1 
ATOM   9799  O OG  . SER E 1 251 ? -27.054 65.878  30.044  1.00 35.87 ? 247 SER E OG  1 
ATOM   9800  N N   . ASN E 1 252 ? -25.891 68.618  30.460  1.00 36.62 ? 248 ASN E N   1 
ATOM   9801  C CA  . ASN E 1 252 ? -26.672 69.853  30.433  1.00 37.00 ? 248 ASN E CA  1 
ATOM   9802  C C   . ASN E 1 252 ? -27.837 69.798  29.425  1.00 37.05 ? 248 ASN E C   1 
ATOM   9803  O O   . ASN E 1 252 ? -28.242 70.830  28.874  1.00 37.37 ? 248 ASN E O   1 
ATOM   9804  C CB  . ASN E 1 252 ? -25.769 71.063  30.162  1.00 36.99 ? 248 ASN E CB  1 
ATOM   9805  C CG  . ASN E 1 252 ? -25.113 71.010  28.796  1.00 38.01 ? 248 ASN E CG  1 
ATOM   9806  O OD1 . ASN E 1 252 ? -24.992 69.941  28.193  1.00 39.76 ? 248 ASN E OD1 1 
ATOM   9807  N ND2 . ASN E 1 252 ? -24.682 72.164  28.299  1.00 38.23 ? 248 ASN E ND2 1 
ATOM   9808  N N   . GLY E 1 253 ? -28.374 68.598  29.195  1.00 36.82 ? 249 GLY E N   1 
ATOM   9809  C CA  . GLY E 1 253 ? -29.527 68.417  28.304  1.00 36.42 ? 249 GLY E CA  1 
ATOM   9810  C C   . GLY E 1 253 ? -29.632 67.050  27.651  1.00 36.09 ? 249 GLY E C   1 
ATOM   9811  O O   . GLY E 1 253 ? -28.658 66.303  27.602  1.00 36.31 ? 249 GLY E O   1 
ATOM   9812  N N   . ASN E 1 254 ? -30.823 66.733  27.144  1.00 35.61 ? 250 ASN E N   1 
ATOM   9813  C CA  . ASN E 1 254 ? -31.086 65.503  26.376  1.00 35.34 ? 250 ASN E CA  1 
ATOM   9814  C C   . ASN E 1 254 ? -30.792 64.191  27.120  1.00 35.16 ? 250 ASN E C   1 
ATOM   9815  O O   . ASN E 1 254 ? -30.686 63.129  26.509  1.00 34.76 ? 250 ASN E O   1 
ATOM   9816  C CB  . ASN E 1 254 ? -30.331 65.513  25.038  1.00 35.25 ? 250 ASN E CB  1 
ATOM   9817  C CG  . ASN E 1 254 ? -30.430 66.838  24.310  1.00 35.30 ? 250 ASN E CG  1 
ATOM   9818  O OD1 . ASN E 1 254 ? -29.941 67.869  24.790  1.00 34.93 ? 250 ASN E OD1 1 
ATOM   9819  N ND2 . ASN E 1 254 ? -31.030 66.813  23.121  1.00 34.82 ? 250 ASN E ND2 1 
ATOM   9820  N N   . PHE E 1 255 ? -30.675 64.277  28.439  1.00 35.13 ? 251 PHE E N   1 
ATOM   9821  C CA  . PHE E 1 255 ? -30.268 63.153  29.272  1.00 35.12 ? 251 PHE E CA  1 
ATOM   9822  C C   . PHE E 1 255 ? -31.486 62.357  29.727  1.00 35.43 ? 251 PHE E C   1 
ATOM   9823  O O   . PHE E 1 255 ? -32.409 62.913  30.332  1.00 35.82 ? 251 PHE E O   1 
ATOM   9824  C CB  . PHE E 1 255 ? -29.466 63.690  30.468  1.00 34.78 ? 251 PHE E CB  1 
ATOM   9825  C CG  . PHE E 1 255 ? -29.011 62.643  31.452  1.00 34.16 ? 251 PHE E CG  1 
ATOM   9826  C CD1 . PHE E 1 255 ? -28.633 61.367  31.039  1.00 34.56 ? 251 PHE E CD1 1 
ATOM   9827  C CD2 . PHE E 1 255 ? -28.908 62.962  32.800  1.00 33.62 ? 251 PHE E CD2 1 
ATOM   9828  C CE1 . PHE E 1 255 ? -28.195 60.410  31.967  1.00 34.49 ? 251 PHE E CE1 1 
ATOM   9829  C CE2 . PHE E 1 255 ? -28.470 62.026  33.731  1.00 34.10 ? 251 PHE E CE2 1 
ATOM   9830  C CZ  . PHE E 1 255 ? -28.111 60.745  33.316  1.00 34.45 ? 251 PHE E CZ  1 
ATOM   9831  N N   . ILE E 1 256 ? -31.495 61.060  29.422  1.00 35.48 ? 252 ILE E N   1 
ATOM   9832  C CA  . ILE E 1 256 ? -32.529 60.167  29.938  1.00 35.68 ? 252 ILE E CA  1 
ATOM   9833  C C   . ILE E 1 256 ? -31.955 59.393  31.127  1.00 36.10 ? 252 ILE E C   1 
ATOM   9834  O O   . ILE E 1 256 ? -31.386 58.308  30.978  1.00 36.23 ? 252 ILE E O   1 
ATOM   9835  C CB  . ILE E 1 256 ? -33.117 59.212  28.851  1.00 35.57 ? 252 ILE E CB  1 
ATOM   9836  C CG1 . ILE E 1 256 ? -33.370 59.947  27.526  1.00 35.42 ? 252 ILE E CG1 1 
ATOM   9837  C CG2 . ILE E 1 256 ? -34.390 58.530  29.354  1.00 35.15 ? 252 ILE E CG2 1 
ATOM   9838  C CD1 . ILE E 1 256 ? -34.404 61.058  27.587  1.00 35.59 ? 252 ILE E CD1 1 
ATOM   9839  N N   . ALA E 1 257 ? -32.111 59.979  32.308  1.00 36.46 ? 253 ALA E N   1 
ATOM   9840  C CA  . ALA E 1 257 ? -31.488 59.487  33.531  1.00 36.86 ? 253 ALA E CA  1 
ATOM   9841  C C   . ALA E 1 257 ? -32.056 58.153  34.006  1.00 37.19 ? 253 ALA E C   1 
ATOM   9842  O O   . ALA E 1 257 ? -33.235 57.887  33.809  1.00 37.34 ? 253 ALA E O   1 
ATOM   9843  C CB  . ALA E 1 257 ? -31.635 60.528  34.623  1.00 36.81 ? 253 ALA E CB  1 
ATOM   9844  N N   . PRO E 1 258 ? -31.220 57.316  34.648  1.00 37.52 ? 254 PRO E N   1 
ATOM   9845  C CA  . PRO E 1 258 ? -31.747 56.116  35.303  1.00 37.81 ? 254 PRO E CA  1 
ATOM   9846  C C   . PRO E 1 258 ? -32.547 56.469  36.551  1.00 38.11 ? 254 PRO E C   1 
ATOM   9847  O O   . PRO E 1 258 ? -32.336 57.526  37.149  1.00 38.16 ? 254 PRO E O   1 
ATOM   9848  C CB  . PRO E 1 258 ? -30.486 55.345  35.730  1.00 37.71 ? 254 PRO E CB  1 
ATOM   9849  C CG  . PRO E 1 258 ? -29.323 56.088  35.183  1.00 37.60 ? 254 PRO E CG  1 
ATOM   9850  C CD  . PRO E 1 258 ? -29.767 57.464  34.846  1.00 37.52 ? 254 PRO E CD  1 
ATOM   9851  N N   . GLU E 1 259 ? -33.456 55.581  36.930  1.00 38.48 ? 255 GLU E N   1 
ATOM   9852  C CA  . GLU E 1 259 ? -34.100 55.639  38.229  1.00 39.19 ? 255 GLU E CA  1 
ATOM   9853  C C   . GLU E 1 259 ? -33.952 54.276  38.898  1.00 39.33 ? 255 GLU E C   1 
ATOM   9854  O O   . GLU E 1 259 ? -33.533 54.184  40.053  1.00 39.41 ? 255 GLU E O   1 
ATOM   9855  C CB  . GLU E 1 259 ? -35.575 56.025  38.092  1.00 39.40 ? 255 GLU E CB  1 
ATOM   9856  C CG  . GLU E 1 259 ? -36.337 56.016  39.415  1.00 41.26 ? 255 GLU E CG  1 
ATOM   9857  C CD  . GLU E 1 259 ? -37.718 56.655  39.336  1.00 43.84 ? 255 GLU E CD  1 
ATOM   9858  O OE1 . GLU E 1 259 ? -38.267 56.811  38.216  1.00 45.08 ? 255 GLU E OE1 1 
ATOM   9859  O OE2 . GLU E 1 259 ? -38.259 56.999  40.413  1.00 44.35 ? 255 GLU E OE2 1 
ATOM   9860  N N   . TYR E 1 260 ? -34.292 53.227  38.152  1.00 39.49 ? 256 TYR E N   1 
ATOM   9861  C CA  . TYR E 1 260 ? -34.175 51.854  38.619  1.00 39.68 ? 256 TYR E CA  1 
ATOM   9862  C C   . TYR E 1 260 ? -33.106 51.082  37.847  1.00 39.57 ? 256 TYR E C   1 
ATOM   9863  O O   . TYR E 1 260 ? -32.925 51.283  36.644  1.00 39.42 ? 256 TYR E O   1 
ATOM   9864  C CB  . TYR E 1 260 ? -35.523 51.132  38.494  1.00 39.94 ? 256 TYR E CB  1 
ATOM   9865  C CG  . TYR E 1 260 ? -36.593 51.628  39.445  1.00 40.99 ? 256 TYR E CG  1 
ATOM   9866  C CD1 . TYR E 1 260 ? -37.634 52.444  38.994  1.00 41.68 ? 256 TYR E CD1 1 
ATOM   9867  C CD2 . TYR E 1 260 ? -36.570 51.273  40.797  1.00 41.62 ? 256 TYR E CD2 1 
ATOM   9868  C CE1 . TYR E 1 260 ? -38.622 52.901  39.871  1.00 42.51 ? 256 TYR E CE1 1 
ATOM   9869  C CE2 . TYR E 1 260 ? -37.547 51.723  41.678  1.00 42.53 ? 256 TYR E CE2 1 
ATOM   9870  C CZ  . TYR E 1 260 ? -38.570 52.538  41.212  1.00 43.00 ? 256 TYR E CZ  1 
ATOM   9871  O OH  . TYR E 1 260 ? -39.538 52.982  42.090  1.00 43.30 ? 256 TYR E OH  1 
ATOM   9872  N N   . ALA E 1 261 ? -32.407 50.199  38.555  1.00 39.51 ? 257 ALA E N   1 
ATOM   9873  C CA  . ALA E 1 261 ? -31.425 49.300  37.959  1.00 39.55 ? 257 ALA E CA  1 
ATOM   9874  C C   . ALA E 1 261 ? -31.725 47.860  38.398  1.00 39.63 ? 257 ALA E C   1 
ATOM   9875  O O   . ALA E 1 261 ? -32.689 47.629  39.128  1.00 39.63 ? 257 ALA E O   1 
ATOM   9876  C CB  . ALA E 1 261 ? -30.014 49.720  38.353  1.00 39.47 ? 257 ALA E CB  1 
ATOM   9877  N N   . TYR E 1 262 ? -30.918 46.899  37.950  1.00 39.77 ? 258 TYR E N   1 
ATOM   9878  C CA  . TYR E 1 262 ? -31.189 45.486  38.228  1.00 40.06 ? 258 TYR E CA  1 
ATOM   9879  C C   . TYR E 1 262 ? -30.022 44.770  38.902  1.00 40.37 ? 258 TYR E C   1 
ATOM   9880  O O   . TYR E 1 262 ? -28.907 44.749  38.376  1.00 40.22 ? 258 TYR E O   1 
ATOM   9881  C CB  . TYR E 1 262 ? -31.580 44.737  36.947  1.00 39.96 ? 258 TYR E CB  1 
ATOM   9882  C CG  . TYR E 1 262 ? -32.887 45.179  36.324  1.00 40.07 ? 258 TYR E CG  1 
ATOM   9883  C CD1 . TYR E 1 262 ? -32.916 46.189  35.362  1.00 40.16 ? 258 TYR E CD1 1 
ATOM   9884  C CD2 . TYR E 1 262 ? -34.091 44.580  36.686  1.00 40.20 ? 258 TYR E CD2 1 
ATOM   9885  C CE1 . TYR E 1 262 ? -34.110 46.599  34.785  1.00 40.44 ? 258 TYR E CE1 1 
ATOM   9886  C CE2 . TYR E 1 262 ? -35.295 44.983  36.113  1.00 40.14 ? 258 TYR E CE2 1 
ATOM   9887  C CZ  . TYR E 1 262 ? -35.295 45.993  35.163  1.00 40.54 ? 258 TYR E CZ  1 
ATOM   9888  O OH  . TYR E 1 262 ? -36.478 46.397  34.587  1.00 41.02 ? 258 TYR E OH  1 
ATOM   9889  N N   . LYS E 1 263 ? -30.295 44.199  40.074  1.00 40.80 ? 259 LYS E N   1 
ATOM   9890  C CA  . LYS E 1 263 ? -29.370 43.297  40.748  1.00 41.31 ? 259 LYS E CA  1 
ATOM   9891  C C   . LYS E 1 263 ? -29.403 41.955  40.044  1.00 41.45 ? 259 LYS E C   1 
ATOM   9892  O O   . LYS E 1 263 ? -30.446 41.296  40.016  1.00 41.32 ? 259 LYS E O   1 
ATOM   9893  C CB  . LYS E 1 263 ? -29.801 43.054  42.192  1.00 41.34 ? 259 LYS E CB  1 
ATOM   9894  C CG  . LYS E 1 263 ? -29.288 44.009  43.239  1.00 41.93 ? 259 LYS E CG  1 
ATOM   9895  C CD  . LYS E 1 263 ? -29.971 43.651  44.556  1.00 43.12 ? 259 LYS E CD  1 
ATOM   9896  C CE  . LYS E 1 263 ? -29.268 44.225  45.762  1.00 44.12 ? 259 LYS E CE  1 
ATOM   9897  N NZ  . LYS E 1 263 ? -29.977 43.803  47.002  1.00 44.33 ? 259 LYS E NZ  1 
ATOM   9898  N N   . ILE E 1 264 ? -28.268 41.550  39.481  1.00 41.79 ? 260 ILE E N   1 
ATOM   9899  C CA  . ILE E 1 264 ? -28.122 40.193  38.966  1.00 41.92 ? 260 ILE E CA  1 
ATOM   9900  C C   . ILE E 1 264 ? -27.773 39.309  40.159  1.00 42.21 ? 260 ILE E C   1 
ATOM   9901  O O   . ILE E 1 264 ? -26.605 39.134  40.500  1.00 42.38 ? 260 ILE E O   1 
ATOM   9902  C CB  . ILE E 1 264 ? -27.056 40.098  37.849  1.00 41.86 ? 260 ILE E CB  1 
ATOM   9903  C CG1 . ILE E 1 264 ? -27.318 41.158  36.770  1.00 41.54 ? 260 ILE E CG1 1 
ATOM   9904  C CG2 . ILE E 1 264 ? -27.038 38.689  37.246  1.00 41.67 ? 260 ILE E CG2 1 
ATOM   9905  C CD1 . ILE E 1 264 ? -26.160 41.390  35.806  1.00 41.39 ? 260 ILE E CD1 1 
ATOM   9906  N N   . VAL E 1 265 ? -28.809 38.781  40.801  1.00 42.62 ? 261 VAL E N   1 
ATOM   9907  C CA  . VAL E 1 265 ? -28.668 38.028  42.052  1.00 43.20 ? 261 VAL E CA  1 
ATOM   9908  C C   . VAL E 1 265 ? -28.333 36.548  41.824  1.00 43.48 ? 261 VAL E C   1 
ATOM   9909  O O   . VAL E 1 265 ? -27.724 35.901  42.683  1.00 43.46 ? 261 VAL E O   1 
ATOM   9910  C CB  . VAL E 1 265 ? -29.925 38.213  42.971  1.00 43.16 ? 261 VAL E CB  1 
ATOM   9911  C CG1 . VAL E 1 265 ? -31.195 38.211  42.157  1.00 43.30 ? 261 VAL E CG1 1 
ATOM   9912  C CG2 . VAL E 1 265 ? -29.992 37.159  44.081  1.00 43.41 ? 261 VAL E CG2 1 
ATOM   9913  N N   . LYS E 1 266 ? -28.719 36.024  40.664  1.00 43.79 ? 262 LYS E N   1 
ATOM   9914  C CA  . LYS E 1 266 ? -28.494 34.621  40.339  1.00 44.14 ? 262 LYS E CA  1 
ATOM   9915  C C   . LYS E 1 266 ? -28.069 34.462  38.883  1.00 44.33 ? 262 LYS E C   1 
ATOM   9916  O O   . LYS E 1 266 ? -28.732 34.969  37.975  1.00 44.47 ? 262 LYS E O   1 
ATOM   9917  C CB  . LYS E 1 266 ? -29.760 33.805  40.622  1.00 44.08 ? 262 LYS E CB  1 
ATOM   9918  C CG  . LYS E 1 266 ? -29.756 32.405  40.034  1.00 44.73 ? 262 LYS E CG  1 
ATOM   9919  C CD  . LYS E 1 266 ? -29.810 31.309  41.082  1.00 45.64 ? 262 LYS E CD  1 
ATOM   9920  C CE  . LYS E 1 266 ? -30.173 29.988  40.414  1.00 46.51 ? 262 LYS E CE  1 
ATOM   9921  N NZ  . LYS E 1 266 ? -30.857 29.038  41.327  1.00 47.23 ? 262 LYS E NZ  1 
ATOM   9922  N N   . LYS E 1 267 ? -26.956 33.759  38.681  1.00 44.63 ? 263 LYS E N   1 
ATOM   9923  C CA  . LYS E 1 267 ? -26.465 33.396  37.354  1.00 44.83 ? 263 LYS E CA  1 
ATOM   9924  C C   . LYS E 1 267 ? -26.614 31.892  37.140  1.00 44.85 ? 263 LYS E C   1 
ATOM   9925  O O   . LYS E 1 267 ? -26.545 31.120  38.095  1.00 44.87 ? 263 LYS E O   1 
ATOM   9926  C CB  . LYS E 1 267 ? -24.997 33.801  37.203  1.00 45.06 ? 263 LYS E CB  1 
ATOM   9927  C CG  . LYS E 1 267 ? -24.775 35.288  36.911  1.00 45.98 ? 263 LYS E CG  1 
ATOM   9928  C CD  . LYS E 1 267 ? -23.333 35.569  36.494  1.00 47.40 ? 263 LYS E CD  1 
ATOM   9929  C CE  . LYS E 1 267 ? -22.503 36.144  37.640  1.00 47.87 ? 263 LYS E CE  1 
ATOM   9930  N NZ  . LYS E 1 267 ? -22.598 37.634  37.698  1.00 48.03 ? 263 LYS E NZ  1 
ATOM   9931  N N   . GLY E 1 268 ? -26.823 31.477  35.893  1.00 44.98 ? 264 GLY E N   1 
ATOM   9932  C CA  . GLY E 1 268 ? -26.919 30.052  35.571  1.00 45.02 ? 264 GLY E CA  1 
ATOM   9933  C C   . GLY E 1 268 ? -27.321 29.742  34.143  1.00 45.12 ? 264 GLY E C   1 
ATOM   9934  O O   . GLY E 1 268 ? -27.323 30.620  33.280  1.00 45.24 ? 264 GLY E O   1 
ATOM   9935  N N   . ASP E 1 269 A -27.659 28.479  33.894  1.00 45.19 ? 264 ASP E N   1 
ATOM   9936  C CA  . ASP E 1 269 A -28.121 28.045  32.579  1.00 45.30 ? 264 ASP E CA  1 
ATOM   9937  C C   . ASP E 1 269 A -29.570 28.440  32.350  1.00 44.92 ? 264 ASP E C   1 
ATOM   9938  O O   . ASP E 1 269 A -30.491 27.739  32.782  1.00 45.15 ? 264 ASP E O   1 
ATOM   9939  C CB  . ASP E 1 269 A -27.967 26.527  32.414  1.00 45.57 ? 264 ASP E CB  1 
ATOM   9940  C CG  . ASP E 1 269 A -26.514 26.084  32.356  1.00 46.68 ? 264 ASP E CG  1 
ATOM   9941  O OD1 . ASP E 1 269 A -25.653 26.883  31.914  1.00 47.36 ? 264 ASP E OD1 1 
ATOM   9942  O OD2 . ASP E 1 269 A -26.238 24.928  32.751  1.00 47.93 ? 264 ASP E OD2 1 
ATOM   9943  N N   . SER E 1 270 ? -29.767 29.572  31.682  1.00 44.37 ? 265 SER E N   1 
ATOM   9944  C CA  . SER E 1 270 ? -31.097 29.988  31.251  1.00 43.76 ? 265 SER E CA  1 
ATOM   9945  C C   . SER E 1 270 ? -31.149 30.059  29.727  1.00 43.30 ? 265 SER E C   1 
ATOM   9946  O O   . SER E 1 270 ? -30.186 29.683  29.056  1.00 43.26 ? 265 SER E O   1 
ATOM   9947  C CB  . SER E 1 270 ? -31.474 31.329  31.872  1.00 43.69 ? 265 SER E CB  1 
ATOM   9948  O OG  . SER E 1 270 ? -32.859 31.581  31.711  1.00 43.91 ? 265 SER E OG  1 
ATOM   9949  N N   . ALA E 1 271 ? -32.272 30.537  29.192  1.00 42.66 ? 266 ALA E N   1 
ATOM   9950  C CA  . ALA E 1 271 ? -32.480 30.626  27.748  1.00 42.07 ? 266 ALA E CA  1 
ATOM   9951  C C   . ALA E 1 271 ? -33.573 31.621  27.397  1.00 41.63 ? 266 ALA E C   1 
ATOM   9952  O O   . ALA E 1 271 ? -34.511 31.818  28.170  1.00 41.80 ? 266 ALA E O   1 
ATOM   9953  C CB  . ALA E 1 271 ? -32.832 29.246  27.171  1.00 41.91 ? 266 ALA E CB  1 
ATOM   9954  N N   . ILE E 1 272 ? -33.442 32.242  26.227  1.00 41.03 ? 267 ILE E N   1 
ATOM   9955  C CA  . ILE E 1 272 ? -34.545 32.967  25.611  1.00 40.41 ? 267 ILE E CA  1 
ATOM   9956  C C   . ILE E 1 272 ? -35.162 32.074  24.540  1.00 40.13 ? 267 ILE E C   1 
ATOM   9957  O O   . ILE E 1 272 ? -34.562 31.859  23.485  1.00 39.90 ? 267 ILE E O   1 
ATOM   9958  C CB  . ILE E 1 272 ? -34.103 34.301  24.953  1.00 40.50 ? 267 ILE E CB  1 
ATOM   9959  C CG1 . ILE E 1 272 ? -33.110 35.073  25.841  1.00 40.67 ? 267 ILE E CG1 1 
ATOM   9960  C CG2 . ILE E 1 272 ? -35.334 35.143  24.565  1.00 39.58 ? 267 ILE E CG2 1 
ATOM   9961  C CD1 . ILE E 1 272 ? -33.739 35.958  26.902  1.00 41.19 ? 267 ILE E CD1 1 
ATOM   9962  N N   . MET E 1 273 ? -36.348 31.546  24.826  1.00 39.71 ? 268 MET E N   1 
ATOM   9963  C CA  . MET E 1 273 ? -37.100 30.748  23.865  1.00 39.75 ? 268 MET E CA  1 
ATOM   9964  C C   . MET E 1 273 ? -38.018 31.609  23.013  1.00 39.55 ? 268 MET E C   1 
ATOM   9965  O O   . MET E 1 273 ? -38.755 32.445  23.530  1.00 39.37 ? 268 MET E O   1 
ATOM   9966  C CB  . MET E 1 273 ? -37.925 29.677  24.580  1.00 39.89 ? 268 MET E CB  1 
ATOM   9967  C CG  . MET E 1 273 ? -37.492 28.249  24.292  1.00 40.85 ? 268 MET E CG  1 
ATOM   9968  S SD  . MET E 1 273 ? -38.384 26.994  25.248  1.00 42.22 ? 268 MET E SD  1 
ATOM   9969  C CE  . MET E 1 273 ? -40.055 27.625  25.196  1.00 41.03 ? 268 MET E CE  1 
ATOM   9970  N N   . LYS E 1 274 ? -37.967 31.398  21.703  1.00 39.64 ? 269 LYS E N   1 
ATOM   9971  C CA  . LYS E 1 274 ? -38.888 32.063  20.787  1.00 39.78 ? 269 LYS E CA  1 
ATOM   9972  C C   . LYS E 1 274 ? -40.097 31.167  20.517  1.00 39.63 ? 269 LYS E C   1 
ATOM   9973  O O   . LYS E 1 274 ? -39.985 30.140  19.840  1.00 39.31 ? 269 LYS E O   1 
ATOM   9974  C CB  . LYS E 1 274 ? -38.192 32.479  19.487  1.00 39.75 ? 269 LYS E CB  1 
ATOM   9975  C CG  . LYS E 1 274 ? -36.967 33.375  19.702  1.00 41.17 ? 269 LYS E CG  1 
ATOM   9976  C CD  . LYS E 1 274 ? -37.092 34.731  18.981  1.00 42.78 ? 269 LYS E CD  1 
ATOM   9977  C CE  . LYS E 1 274 ? -37.794 35.769  19.862  1.00 43.40 ? 269 LYS E CE  1 
ATOM   9978  N NZ  . LYS E 1 274 ? -37.792 37.157  19.295  1.00 43.67 ? 269 LYS E NZ  1 
ATOM   9979  N N   . SER E 1 275 ? -41.242 31.563  21.076  1.00 39.57 ? 270 SER E N   1 
ATOM   9980  C CA  . SER E 1 275 ? -42.476 30.787  20.983  1.00 39.53 ? 270 SER E CA  1 
ATOM   9981  C C   . SER E 1 275 ? -43.716 31.666  21.063  1.00 39.67 ? 270 SER E C   1 
ATOM   9982  O O   . SER E 1 275 ? -43.765 32.622  21.840  1.00 39.67 ? 270 SER E O   1 
ATOM   9983  C CB  . SER E 1 275 ? -42.532 29.733  22.088  1.00 39.51 ? 270 SER E CB  1 
ATOM   9984  O OG  . SER E 1 275 ? -43.653 28.885  21.914  1.00 39.09 ? 270 SER E OG  1 
ATOM   9985  N N   . GLU E 1 276 ? -44.717 31.327  20.255  1.00 39.77 ? 271 GLU E N   1 
ATOM   9986  C CA  . GLU E 1 276 ? -45.997 32.030  20.272  1.00 39.81 ? 271 GLU E CA  1 
ATOM   9987  C C   . GLU E 1 276 ? -46.913 31.473  21.358  1.00 39.70 ? 271 GLU E C   1 
ATOM   9988  O O   . GLU E 1 276 ? -47.931 32.085  21.687  1.00 39.67 ? 271 GLU E O   1 
ATOM   9989  C CB  . GLU E 1 276 ? -46.692 31.959  18.902  1.00 40.02 ? 271 GLU E CB  1 
ATOM   9990  C CG  . GLU E 1 276 ? -45.863 32.482  17.727  1.00 40.27 ? 271 GLU E CG  1 
ATOM   9991  C CD  . GLU E 1 276 ? -45.438 33.931  17.896  1.00 41.33 ? 271 GLU E CD  1 
ATOM   9992  O OE1 . GLU E 1 276 ? -46.299 34.774  18.239  1.00 41.43 ? 271 GLU E OE1 1 
ATOM   9993  O OE2 . GLU E 1 276 ? -44.240 34.228  17.681  1.00 41.66 ? 271 GLU E OE2 1 
ATOM   9994  N N   . LEU E 1 277 ? -46.540 30.322  21.916  1.00 39.62 ? 272 LEU E N   1 
ATOM   9995  C CA  . LEU E 1 277 ? -47.338 29.664  22.956  1.00 39.66 ? 272 LEU E CA  1 
ATOM   9996  C C   . LEU E 1 277 ? -47.334 30.437  24.272  1.00 39.89 ? 272 LEU E C   1 
ATOM   9997  O O   . LEU E 1 277 ? -46.461 31.279  24.514  1.00 39.52 ? 272 LEU E O   1 
ATOM   9998  C CB  . LEU E 1 277 ? -46.866 28.219  23.188  1.00 39.44 ? 272 LEU E CB  1 
ATOM   9999  C CG  . LEU E 1 277 ? -46.915 27.205  22.035  1.00 38.89 ? 272 LEU E CG  1 
ATOM   10000 C CD1 . LEU E 1 277 ? -46.539 25.819  22.540  1.00 37.83 ? 272 LEU E CD1 1 
ATOM   10001 C CD2 . LEU E 1 277 ? -48.280 27.171  21.350  1.00 38.00 ? 272 LEU E CD2 1 
ATOM   10002 N N   . GLU E 1 278 ? -48.325 30.149  25.113  1.00 40.37 ? 273 GLU E N   1 
ATOM   10003 C CA  . GLU E 1 278 ? -48.447 30.796  26.421  1.00 40.76 ? 273 GLU E CA  1 
ATOM   10004 C C   . GLU E 1 278 ? -48.355 29.754  27.542  1.00 40.49 ? 273 GLU E C   1 
ATOM   10005 O O   . GLU E 1 278 ? -48.195 28.558  27.270  1.00 40.36 ? 273 GLU E O   1 
ATOM   10006 C CB  . GLU E 1 278 ? -49.746 31.601  26.489  1.00 40.99 ? 273 GLU E CB  1 
ATOM   10007 C CG  . GLU E 1 278 ? -49.597 32.958  27.168  1.00 42.93 ? 273 GLU E CG  1 
ATOM   10008 C CD  . GLU E 1 278 ? -50.289 34.086  26.405  1.00 45.06 ? 273 GLU E CD  1 
ATOM   10009 O OE1 . GLU E 1 278 ? -51.227 34.696  26.972  1.00 45.89 ? 273 GLU E OE1 1 
ATOM   10010 O OE2 . GLU E 1 278 ? -49.891 34.364  25.245  1.00 45.05 ? 273 GLU E OE2 1 
ATOM   10011 N N   . TYR E 1 279 ? -48.442 30.209  28.792  1.00 40.39 ? 274 TYR E N   1 
ATOM   10012 C CA  . TYR E 1 279 ? -48.254 29.338  29.958  1.00 40.26 ? 274 TYR E CA  1 
ATOM   10013 C C   . TYR E 1 279 ? -49.260 28.192  30.023  1.00 40.27 ? 274 TYR E C   1 
ATOM   10014 O O   . TYR E 1 279 ? -50.457 28.394  29.834  1.00 40.18 ? 274 TYR E O   1 
ATOM   10015 C CB  . TYR E 1 279 ? -48.300 30.152  31.250  1.00 40.20 ? 274 TYR E CB  1 
ATOM   10016 C CG  . TYR E 1 279 ? -47.837 29.392  32.472  1.00 40.03 ? 274 TYR E CG  1 
ATOM   10017 C CD1 . TYR E 1 279 ? -46.681 28.604  32.438  1.00 39.70 ? 274 TYR E CD1 1 
ATOM   10018 C CD2 . TYR E 1 279 ? -48.546 29.474  33.667  1.00 40.04 ? 274 TYR E CD2 1 
ATOM   10019 C CE1 . TYR E 1 279 ? -46.251 27.909  33.561  1.00 39.89 ? 274 TYR E CE1 1 
ATOM   10020 C CE2 . TYR E 1 279 ? -48.124 28.787  34.800  1.00 40.80 ? 274 TYR E CE2 1 
ATOM   10021 C CZ  . TYR E 1 279 ? -46.976 28.008  34.742  1.00 40.64 ? 274 TYR E CZ  1 
ATOM   10022 O OH  . TYR E 1 279 ? -46.567 27.333  35.865  1.00 40.12 ? 274 TYR E OH  1 
ATOM   10023 N N   . GLY E 1 280 ? -48.763 26.991  30.307  1.00 40.36 ? 275 GLY E N   1 
ATOM   10024 C CA  . GLY E 1 280 ? -49.587 25.790  30.249  1.00 40.55 ? 275 GLY E CA  1 
ATOM   10025 C C   . GLY E 1 280 ? -49.936 25.124  31.564  1.00 40.71 ? 275 GLY E C   1 
ATOM   10026 O O   . GLY E 1 280 ? -50.562 24.063  31.563  1.00 40.62 ? 275 GLY E O   1 
ATOM   10027 N N   . ASN E 1 281 ? -49.537 25.735  32.681  1.00 41.08 ? 276 ASN E N   1 
ATOM   10028 C CA  . ASN E 1 281 ? -49.857 25.217  34.023  1.00 41.49 ? 276 ASN E CA  1 
ATOM   10029 C C   . ASN E 1 281 ? -49.484 23.752  34.227  1.00 41.44 ? 276 ASN E C   1 
ATOM   10030 O O   . ASN E 1 281 ? -50.251 22.986  34.806  1.00 41.58 ? 276 ASN E O   1 
ATOM   10031 C CB  . ASN E 1 281 ? -51.344 25.426  34.344  1.00 41.61 ? 276 ASN E CB  1 
ATOM   10032 C CG  . ASN E 1 281 ? -51.619 26.778  34.959  1.00 42.59 ? 276 ASN E CG  1 
ATOM   10033 O OD1 . ASN E 1 281 ? -51.263 27.032  36.113  1.00 43.57 ? 276 ASN E OD1 1 
ATOM   10034 N ND2 . ASN E 1 281 ? -52.261 27.657  34.196  1.00 42.96 ? 276 ASN E ND2 1 
ATOM   10035 N N   . CYS E 1 282 ? -48.308 23.374  33.735  1.00 41.44 ? 277 CYS E N   1 
ATOM   10036 C CA  . CYS E 1 282 ? -47.811 22.004  33.828  1.00 41.54 ? 277 CYS E CA  1 
ATOM   10037 C C   . CYS E 1 282 ? -46.400 22.015  34.392  1.00 41.17 ? 277 CYS E C   1 
ATOM   10038 O O   . CYS E 1 282 ? -45.820 23.077  34.610  1.00 41.11 ? 277 CYS E O   1 
ATOM   10039 C CB  . CYS E 1 282 ? -47.810 21.341  32.442  1.00 41.67 ? 277 CYS E CB  1 
ATOM   10040 S SG  . CYS E 1 282 ? -47.314 22.467  31.082  1.00 43.38 ? 277 CYS E SG  1 
ATOM   10041 N N   . ASN E 1 283 ? -45.850 20.828  34.618  1.00 41.12 ? 278 ASN E N   1 
ATOM   10042 C CA  . ASN E 1 283 ? -44.470 20.688  35.071  1.00 41.01 ? 278 ASN E CA  1 
ATOM   10043 C C   . ASN E 1 283 ? -43.726 19.693  34.190  1.00 40.76 ? 278 ASN E C   1 
ATOM   10044 O O   . ASN E 1 283 ? -44.282 18.671  33.786  1.00 40.80 ? 278 ASN E O   1 
ATOM   10045 C CB  . ASN E 1 283 ? -44.426 20.258  36.545  1.00 41.07 ? 278 ASN E CB  1 
ATOM   10046 C CG  . ASN E 1 283 ? -43.038 20.389  37.161  1.00 41.48 ? 278 ASN E CG  1 
ATOM   10047 O OD1 . ASN E 1 283 ? -42.340 21.389  36.970  1.00 41.00 ? 278 ASN E OD1 1 
ATOM   10048 N ND2 . ASN E 1 283 ? -42.638 19.374  37.915  1.00 42.40 ? 278 ASN E ND2 1 
ATOM   10049 N N   . THR E 1 284 ? -42.470 19.999  33.885  1.00 40.58 ? 279 THR E N   1 
ATOM   10050 C CA  . THR E 1 284 ? -41.667 19.148  33.004  1.00 40.24 ? 279 THR E CA  1 
ATOM   10051 C C   . THR E 1 284 ? -40.191 19.178  33.380  1.00 40.05 ? 279 THR E C   1 
ATOM   10052 O O   . THR E 1 284 ? -39.744 20.068  34.104  1.00 40.00 ? 279 THR E O   1 
ATOM   10053 C CB  . THR E 1 284 ? -41.839 19.545  31.506  1.00 40.17 ? 279 THR E CB  1 
ATOM   10054 O OG1 . THR E 1 284 ? -41.341 18.497  30.668  1.00 40.56 ? 279 THR E OG1 1 
ATOM   10055 C CG2 . THR E 1 284 ? -41.104 20.849  31.172  1.00 39.61 ? 279 THR E CG2 1 
ATOM   10056 N N   . LYS E 1 285 ? -39.443 18.196  32.885  1.00 40.00 ? 280 LYS E N   1 
ATOM   10057 C CA  . LYS E 1 285 ? -37.984 18.211  33.004  1.00 39.99 ? 280 LYS E CA  1 
ATOM   10058 C C   . LYS E 1 285 ? -37.303 18.563  31.679  1.00 39.49 ? 280 LYS E C   1 
ATOM   10059 O O   . LYS E 1 285 ? -36.125 18.921  31.657  1.00 39.36 ? 280 LYS E O   1 
ATOM   10060 C CB  . LYS E 1 285 ? -37.467 16.889  33.568  1.00 40.13 ? 280 LYS E CB  1 
ATOM   10061 C CG  . LYS E 1 285 ? -37.758 16.736  35.049  1.00 41.60 ? 280 LYS E CG  1 
ATOM   10062 C CD  . LYS E 1 285 ? -37.019 15.557  35.657  1.00 43.90 ? 280 LYS E CD  1 
ATOM   10063 C CE  . LYS E 1 285 ? -37.112 15.593  37.176  1.00 44.65 ? 280 LYS E CE  1 
ATOM   10064 N NZ  . LYS E 1 285 ? -36.648 14.311  37.769  1.00 45.88 ? 280 LYS E NZ  1 
ATOM   10065 N N   . CYS E 1 286 ? -38.064 18.484  30.588  1.00 39.08 ? 281 CYS E N   1 
ATOM   10066 C CA  . CYS E 1 286 ? -37.567 18.824  29.256  1.00 38.77 ? 281 CYS E CA  1 
ATOM   10067 C C   . CYS E 1 286 ? -38.577 19.693  28.501  1.00 38.11 ? 281 CYS E C   1 
ATOM   10068 O O   . CYS E 1 286 ? -39.721 19.285  28.293  1.00 38.08 ? 281 CYS E O   1 
ATOM   10069 C CB  . CYS E 1 286 ? -37.263 17.544  28.471  1.00 38.88 ? 281 CYS E CB  1 
ATOM   10070 S SG  . CYS E 1 286 ? -36.674 17.830  26.794  1.00 40.48 ? 281 CYS E SG  1 
ATOM   10071 N N   . GLN E 1 287 ? -38.145 20.883  28.085  1.00 37.39 ? 282 GLN E N   1 
ATOM   10072 C CA  . GLN E 1 287 ? -39.026 21.841  27.411  1.00 36.78 ? 282 GLN E CA  1 
ATOM   10073 C C   . GLN E 1 287 ? -38.506 22.264  26.036  1.00 36.53 ? 282 GLN E C   1 
ATOM   10074 O O   . GLN E 1 287 ? -37.331 22.595  25.888  1.00 36.26 ? 282 GLN E O   1 
ATOM   10075 C CB  . GLN E 1 287 ? -39.231 23.080  28.290  1.00 36.74 ? 282 GLN E CB  1 
ATOM   10076 C CG  . GLN E 1 287 ? -40.172 24.134  27.715  1.00 36.18 ? 282 GLN E CG  1 
ATOM   10077 C CD  . GLN E 1 287 ? -41.623 23.693  27.713  1.00 36.23 ? 282 GLN E CD  1 
ATOM   10078 O OE1 . GLN E 1 287 ? -42.222 23.490  28.767  1.00 36.25 ? 282 GLN E OE1 1 
ATOM   10079 N NE2 . GLN E 1 287 ? -42.200 23.556  26.523  1.00 35.84 ? 282 GLN E NE2 1 
ATOM   10080 N N   . THR E 1 288 ? -39.396 22.243  25.043  1.00 36.29 ? 283 THR E N   1 
ATOM   10081 C CA  . THR E 1 288 ? -39.114 22.773  23.706  1.00 36.03 ? 283 THR E CA  1 
ATOM   10082 C C   . THR E 1 288 ? -40.004 23.989  23.455  1.00 36.10 ? 283 THR E C   1 
ATOM   10083 O O   . THR E 1 288 ? -40.973 24.204  24.186  1.00 35.79 ? 283 THR E O   1 
ATOM   10084 C CB  . THR E 1 288 ? -39.349 21.723  22.571  1.00 35.94 ? 283 THR E CB  1 
ATOM   10085 O OG1 . THR E 1 288 ? -40.749 21.592  22.306  1.00 35.64 ? 283 THR E OG1 1 
ATOM   10086 C CG2 . THR E 1 288 ? -38.766 20.362  22.924  1.00 35.64 ? 283 THR E CG2 1 
ATOM   10087 N N   . PRO E 1 289 ? -39.678 24.794  22.424  1.00 36.34 ? 284 PRO E N   1 
ATOM   10088 C CA  . PRO E 1 289 ? -40.536 25.905  22.014  1.00 36.55 ? 284 PRO E CA  1 
ATOM   10089 C C   . PRO E 1 289 ? -41.922 25.481  21.527  1.00 36.84 ? 284 PRO E C   1 
ATOM   10090 O O   . PRO E 1 289 ? -42.806 26.331  21.421  1.00 37.00 ? 284 PRO E O   1 
ATOM   10091 C CB  . PRO E 1 289 ? -39.752 26.538  20.861  1.00 36.54 ? 284 PRO E CB  1 
ATOM   10092 C CG  . PRO E 1 289 ? -38.344 26.199  21.151  1.00 36.44 ? 284 PRO E CG  1 
ATOM   10093 C CD  . PRO E 1 289 ? -38.397 24.813  21.695  1.00 36.27 ? 284 PRO E CD  1 
ATOM   10094 N N   . MET E 1 290 ? -42.107 24.191  21.242  1.00 37.16 ? 285 MET E N   1 
ATOM   10095 C CA  . MET E 1 290 ? -43.384 23.670  20.739  1.00 37.79 ? 285 MET E CA  1 
ATOM   10096 C C   . MET E 1 290 ? -44.234 22.980  21.807  1.00 37.65 ? 285 MET E C   1 
ATOM   10097 O O   . MET E 1 290 ? -45.428 22.741  21.593  1.00 37.84 ? 285 MET E O   1 
ATOM   10098 C CB  . MET E 1 290 ? -43.157 22.679  19.596  1.00 38.04 ? 285 MET E CB  1 
ATOM   10099 C CG  . MET E 1 290 ? -42.284 23.185  18.470  1.00 40.01 ? 285 MET E CG  1 
ATOM   10100 S SD  . MET E 1 290 ? -42.445 22.119  17.032  1.00 44.16 ? 285 MET E SD  1 
ATOM   10101 C CE  . MET E 1 290 ? -43.804 22.938  16.174  1.00 43.55 ? 285 MET E CE  1 
ATOM   10102 N N   . GLY E 1 291 ? -43.613 22.649  22.937  1.00 37.32 ? 286 GLY E N   1 
ATOM   10103 C CA  . GLY E 1 291 ? -44.250 21.848  23.980  1.00 37.11 ? 286 GLY E CA  1 
ATOM   10104 C C   . GLY E 1 291 ? -43.235 21.069  24.796  1.00 37.03 ? 286 GLY E C   1 
ATOM   10105 O O   . GLY E 1 291 ? -42.052 21.038  24.455  1.00 36.93 ? 286 GLY E O   1 
ATOM   10106 N N   . ALA E 1 292 ? -43.698 20.438  25.874  1.00 36.98 ? 287 ALA E N   1 
ATOM   10107 C CA  . ALA E 1 292 ? -42.814 19.733  26.808  1.00 36.86 ? 287 ALA E CA  1 
ATOM   10108 C C   . ALA E 1 292 ? -42.749 18.227  26.556  1.00 36.98 ? 287 ALA E C   1 
ATOM   10109 O O   . ALA E 1 292 ? -43.726 17.621  26.117  1.00 36.99 ? 287 ALA E O   1 
ATOM   10110 C CB  . ALA E 1 292 ? -43.234 20.009  28.229  1.00 36.64 ? 287 ALA E CB  1 
ATOM   10111 N N   . ILE E 1 293 ? -41.594 17.633  26.853  1.00 37.15 ? 288 ILE E N   1 
ATOM   10112 C CA  . ILE E 1 293 ? -41.375 16.202  26.648  1.00 37.32 ? 288 ILE E CA  1 
ATOM   10113 C C   . ILE E 1 293 ? -41.256 15.464  27.979  1.00 37.78 ? 288 ILE E C   1 
ATOM   10114 O O   . ILE E 1 293 ? -40.577 15.932  28.892  1.00 37.80 ? 288 ILE E O   1 
ATOM   10115 C CB  . ILE E 1 293 ? -40.111 15.937  25.783  1.00 37.17 ? 288 ILE E CB  1 
ATOM   10116 C CG1 . ILE E 1 293 ? -40.280 16.535  24.385  1.00 36.58 ? 288 ILE E CG1 1 
ATOM   10117 C CG2 . ILE E 1 293 ? -39.810 14.443  25.687  1.00 36.74 ? 288 ILE E CG2 1 
ATOM   10118 C CD1 . ILE E 1 293 ? -38.979 16.690  23.614  1.00 35.46 ? 288 ILE E CD1 1 
ATOM   10119 N N   . ASN E 1 294 ? -41.931 14.317  28.072  1.00 38.40 ? 289 ASN E N   1 
ATOM   10120 C CA  . ASN E 1 294 ? -41.815 13.392  29.202  1.00 39.30 ? 289 ASN E CA  1 
ATOM   10121 C C   . ASN E 1 294 ? -41.545 11.986  28.653  1.00 39.54 ? 289 ASN E C   1 
ATOM   10122 O O   . ASN E 1 294 ? -42.472 11.249  28.300  1.00 39.62 ? 289 ASN E O   1 
ATOM   10123 C CB  . ASN E 1 294 ? -43.087 13.421  30.067  1.00 39.46 ? 289 ASN E CB  1 
ATOM   10124 C CG  . ASN E 1 294 ? -42.955 12.610  31.367  1.00 41.20 ? 289 ASN E CG  1 
ATOM   10125 O OD1 . ASN E 1 294 ? -43.949 12.076  31.881  1.00 43.23 ? 289 ASN E OD1 1 
ATOM   10126 N ND2 . ASN E 1 294 ? -41.736 12.527  31.907  1.00 41.43 ? 289 ASN E ND2 1 
ATOM   10127 N N   . SER E 1 295 ? -40.268 11.625  28.562  1.00 39.91 ? 290 SER E N   1 
ATOM   10128 C CA  . SER E 1 295 ? -39.882 10.410  27.855  1.00 40.28 ? 290 SER E CA  1 
ATOM   10129 C C   . SER E 1 295 ? -38.581 9.786   28.348  1.00 40.56 ? 290 SER E C   1 
ATOM   10130 O O   . SER E 1 295 ? -37.640 10.488  28.718  1.00 40.60 ? 290 SER E O   1 
ATOM   10131 C CB  . SER E 1 295 ? -39.779 10.696  26.355  1.00 40.27 ? 290 SER E CB  1 
ATOM   10132 O OG  . SER E 1 295 ? -39.620 9.502   25.615  1.00 40.12 ? 290 SER E OG  1 
ATOM   10133 N N   . SER E 1 296 ? -38.546 8.455   28.330  1.00 41.05 ? 291 SER E N   1 
ATOM   10134 C CA  . SER E 1 296 ? -37.347 7.684   28.659  1.00 41.33 ? 291 SER E CA  1 
ATOM   10135 C C   . SER E 1 296 ? -36.549 7.317   27.403  1.00 41.35 ? 291 SER E C   1 
ATOM   10136 O O   . SER E 1 296 ? -35.444 6.780   27.503  1.00 41.71 ? 291 SER E O   1 
ATOM   10137 C CB  . SER E 1 296 ? -37.723 6.419   29.433  1.00 41.43 ? 291 SER E CB  1 
ATOM   10138 O OG  . SER E 1 296 ? -38.279 6.745   30.697  1.00 41.96 ? 291 SER E OG  1 
ATOM   10139 N N   . MET E 1 297 ? -37.114 7.611   26.231  1.00 41.00 ? 292 MET E N   1 
ATOM   10140 C CA  . MET E 1 297 ? -36.438 7.407   24.949  1.00 40.75 ? 292 MET E CA  1 
ATOM   10141 C C   . MET E 1 297 ? -35.125 8.193   24.891  1.00 40.14 ? 292 MET E C   1 
ATOM   10142 O O   . MET E 1 297 ? -35.037 9.281   25.453  1.00 40.32 ? 292 MET E O   1 
ATOM   10143 C CB  . MET E 1 297 ? -37.332 7.859   23.789  1.00 41.06 ? 292 MET E CB  1 
ATOM   10144 C CG  . MET E 1 297 ? -38.687 7.173   23.692  1.00 41.78 ? 292 MET E CG  1 
ATOM   10145 S SD  . MET E 1 297 ? -38.563 5.459   23.182  1.00 44.65 ? 292 MET E SD  1 
ATOM   10146 C CE  . MET E 1 297 ? -40.245 5.130   22.648  1.00 43.08 ? 292 MET E CE  1 
ATOM   10147 N N   . PRO E 1 298 ? -34.099 7.636   24.222  1.00 39.54 ? 293 PRO E N   1 
ATOM   10148 C CA  . PRO E 1 298 ? -32.839 8.358   24.014  1.00 39.00 ? 293 PRO E CA  1 
ATOM   10149 C C   . PRO E 1 298 ? -32.888 9.411   22.900  1.00 38.43 ? 293 PRO E C   1 
ATOM   10150 O O   . PRO E 1 298 ? -31.985 10.245  22.812  1.00 38.71 ? 293 PRO E O   1 
ATOM   10151 C CB  . PRO E 1 298 ? -31.858 7.245   23.633  1.00 39.14 ? 293 PRO E CB  1 
ATOM   10152 C CG  . PRO E 1 298 ? -32.720 6.176   23.038  1.00 39.47 ? 293 PRO E CG  1 
ATOM   10153 C CD  . PRO E 1 298 ? -33.993 6.218   23.826  1.00 39.52 ? 293 PRO E CD  1 
ATOM   10154 N N   . PHE E 1 299 ? -33.915 9.370   22.053  1.00 37.47 ? 294 PHE E N   1 
ATOM   10155 C CA  . PHE E 1 299 ? -34.033 10.337  20.960  1.00 36.60 ? 294 PHE E CA  1 
ATOM   10156 C C   . PHE E 1 299 ? -35.418 10.970  20.853  1.00 35.91 ? 294 PHE E C   1 
ATOM   10157 O O   . PHE E 1 299 ? -36.423 10.379  21.268  1.00 35.56 ? 294 PHE E O   1 
ATOM   10158 C CB  . PHE E 1 299 ? -33.655 9.700   19.619  1.00 36.78 ? 294 PHE E CB  1 
ATOM   10159 C CG  . PHE E 1 299 ? -32.262 9.148   19.580  1.00 37.55 ? 294 PHE E CG  1 
ATOM   10160 C CD1 . PHE E 1 299 ? -32.038 7.786   19.749  1.00 38.43 ? 294 PHE E CD1 1 
ATOM   10161 C CD2 . PHE E 1 299 ? -31.172 9.988   19.383  1.00 38.50 ? 294 PHE E CD2 1 
ATOM   10162 C CE1 . PHE E 1 299 ? -30.754 7.266   19.724  1.00 38.87 ? 294 PHE E CE1 1 
ATOM   10163 C CE2 . PHE E 1 299 ? -29.883 9.479   19.352  1.00 39.04 ? 294 PHE E CE2 1 
ATOM   10164 C CZ  . PHE E 1 299 ? -29.674 8.114   19.522  1.00 39.70 ? 294 PHE E CZ  1 
ATOM   10165 N N   . HIS E 1 300 ? -35.450 12.182  20.296  1.00 34.96 ? 295 HIS E N   1 
ATOM   10166 C CA  . HIS E 1 300 ? -36.700 12.852  19.938  1.00 34.01 ? 295 HIS E CA  1 
ATOM   10167 C C   . HIS E 1 300 ? -36.528 13.654  18.650  1.00 33.52 ? 295 HIS E C   1 
ATOM   10168 O O   . HIS E 1 300 ? -35.405 14.005  18.280  1.00 33.51 ? 295 HIS E O   1 
ATOM   10169 C CB  . HIS E 1 300 ? -37.202 13.738  21.082  1.00 33.74 ? 295 HIS E CB  1 
ATOM   10170 C CG  . HIS E 1 300 ? -36.552 15.085  21.142  1.00 33.56 ? 295 HIS E CG  1 
ATOM   10171 N ND1 . HIS E 1 300 ? -35.369 15.312  21.812  1.00 33.11 ? 295 HIS E ND1 1 
ATOM   10172 C CD2 . HIS E 1 300 ? -36.931 16.281  20.632  1.00 32.96 ? 295 HIS E CD2 1 
ATOM   10173 C CE1 . HIS E 1 300 ? -35.042 16.588  21.705  1.00 32.64 ? 295 HIS E CE1 1 
ATOM   10174 N NE2 . HIS E 1 300 ? -35.973 17.198  20.994  1.00 33.09 ? 295 HIS E NE2 1 
ATOM   10175 N N   . ASN E 1 301 ? -37.639 13.937  17.974  1.00 32.83 ? 296 ASN E N   1 
ATOM   10176 C CA  . ASN E 1 301 ? -37.617 14.734  16.750  1.00 32.37 ? 296 ASN E CA  1 
ATOM   10177 C C   . ASN E 1 301 ? -38.567 15.936  16.794  1.00 32.56 ? 296 ASN E C   1 
ATOM   10178 O O   . ASN E 1 301 ? -39.063 16.391  15.752  1.00 32.59 ? 296 ASN E O   1 
ATOM   10179 C CB  . ASN E 1 301 ? -37.892 13.854  15.515  1.00 32.10 ? 296 ASN E CB  1 
ATOM   10180 C CG  . ASN E 1 301 ? -39.328 13.329  15.451  1.00 30.74 ? 296 ASN E CG  1 
ATOM   10181 O OD1 . ASN E 1 301 ? -40.148 13.580  16.331  1.00 29.58 ? 296 ASN E OD1 1 
ATOM   10182 N ND2 . ASN E 1 301 ? -39.628 12.597  14.395  1.00 29.38 ? 296 ASN E ND2 1 
ATOM   10183 N N   . ILE E 1 302 ? -38.817 16.445  17.997  1.00 32.43 ? 297 ILE E N   1 
ATOM   10184 C CA  . ILE E 1 302 ? -39.749 17.555  18.176  1.00 32.66 ? 297 ILE E CA  1 
ATOM   10185 C C   . ILE E 1 302 ? -39.143 18.865  17.674  1.00 33.06 ? 297 ILE E C   1 
ATOM   10186 O O   . ILE E 1 302 ? -39.602 19.421  16.673  1.00 32.97 ? 297 ILE E O   1 
ATOM   10187 C CB  . ILE E 1 302 ? -40.204 17.722  19.657  1.00 32.56 ? 297 ILE E CB  1 
ATOM   10188 C CG1 . ILE E 1 302 ? -40.655 16.382  20.274  1.00 32.12 ? 297 ILE E CG1 1 
ATOM   10189 C CG2 . ILE E 1 302 ? -41.279 18.816  19.774  1.00 32.23 ? 297 ILE E CG2 1 
ATOM   10190 C CD1 . ILE E 1 302 ? -41.767 15.654  19.537  1.00 31.40 ? 297 ILE E CD1 1 
ATOM   10191 N N   . HIS E 1 303 ? -38.109 19.337  18.370  1.00 33.35 ? 298 HIS E N   1 
ATOM   10192 C CA  . HIS E 1 303 ? -37.470 20.610  18.063  1.00 33.71 ? 298 HIS E CA  1 
ATOM   10193 C C   . HIS E 1 303 ? -36.004 20.563  18.512  1.00 34.08 ? 298 HIS E C   1 
ATOM   10194 O O   . HIS E 1 303 ? -35.699 19.997  19.563  1.00 34.11 ? 298 HIS E O   1 
ATOM   10195 C CB  . HIS E 1 303 ? -38.213 21.745  18.771  1.00 33.62 ? 298 HIS E CB  1 
ATOM   10196 C CG  . HIS E 1 303 ? -37.984 23.094  18.166  1.00 33.82 ? 298 HIS E CG  1 
ATOM   10197 N ND1 . HIS E 1 303 ? -36.854 23.840  18.418  1.00 33.83 ? 298 HIS E ND1 1 
ATOM   10198 C CD2 . HIS E 1 303 ? -38.748 23.840  17.331  1.00 34.30 ? 298 HIS E CD2 1 
ATOM   10199 C CE1 . HIS E 1 303 ? -36.925 24.982  17.756  1.00 33.62 ? 298 HIS E CE1 1 
ATOM   10200 N NE2 . HIS E 1 303 ? -38.066 25.008  17.092  1.00 33.97 ? 298 HIS E NE2 1 
ATOM   10201 N N   . PRO E 1 304 ? -35.088 21.142  17.711  1.00 34.34 ? 299 PRO E N   1 
ATOM   10202 C CA  . PRO E 1 304 ? -33.667 21.097  18.065  1.00 34.61 ? 299 PRO E CA  1 
ATOM   10203 C C   . PRO E 1 304 ? -33.292 21.883  19.325  1.00 35.10 ? 299 PRO E C   1 
ATOM   10204 O O   . PRO E 1 304 ? -32.363 21.484  20.034  1.00 35.16 ? 299 PRO E O   1 
ATOM   10205 C CB  . PRO E 1 304 ? -32.979 21.703  16.833  1.00 34.51 ? 299 PRO E CB  1 
ATOM   10206 C CG  . PRO E 1 304 ? -34.040 22.467  16.129  1.00 34.05 ? 299 PRO E CG  1 
ATOM   10207 C CD  . PRO E 1 304 ? -35.293 21.700  16.362  1.00 34.17 ? 299 PRO E CD  1 
ATOM   10208 N N   . LEU E 1 305 ? -34.011 22.970  19.607  1.00 35.54 ? 300 LEU E N   1 
ATOM   10209 C CA  . LEU E 1 305 ? -33.652 23.887  20.697  1.00 35.99 ? 300 LEU E CA  1 
ATOM   10210 C C   . LEU E 1 305 ? -34.359 23.595  22.026  1.00 36.21 ? 300 LEU E C   1 
ATOM   10211 O O   . LEU E 1 305 ? -35.372 24.213  22.343  1.00 36.50 ? 300 LEU E O   1 
ATOM   10212 C CB  . LEU E 1 305 ? -33.921 25.341  20.273  1.00 36.08 ? 300 LEU E CB  1 
ATOM   10213 C CG  . LEU E 1 305 ? -33.140 25.912  19.084  1.00 36.79 ? 300 LEU E CG  1 
ATOM   10214 C CD1 . LEU E 1 305 ? -33.744 27.229  18.607  1.00 36.46 ? 300 LEU E CD1 1 
ATOM   10215 C CD2 . LEU E 1 305 ? -31.657 26.083  19.427  1.00 36.51 ? 300 LEU E CD2 1 
ATOM   10216 N N   . THR E 1 306 ? -33.818 22.673  22.815  1.00 36.40 ? 301 THR E N   1 
ATOM   10217 C CA  . THR E 1 306 ? -34.444 22.311  24.090  1.00 36.60 ? 301 THR E CA  1 
ATOM   10218 C C   . THR E 1 306 ? -33.701 22.860  25.315  1.00 36.81 ? 301 THR E C   1 
ATOM   10219 O O   . THR E 1 306 ? -32.582 23.351  25.202  1.00 36.75 ? 301 THR E O   1 
ATOM   10220 C CB  . THR E 1 306 ? -34.600 20.773  24.237  1.00 36.60 ? 301 THR E CB  1 
ATOM   10221 O OG1 . THR E 1 306 ? -33.338 20.185  24.579  1.00 36.78 ? 301 THR E OG1 1 
ATOM   10222 C CG2 . THR E 1 306 ? -35.130 20.144  22.952  1.00 36.57 ? 301 THR E CG2 1 
ATOM   10223 N N   . ILE E 1 307 ? -34.343 22.779  26.478  1.00 37.18 ? 302 ILE E N   1 
ATOM   10224 C CA  . ILE E 1 307 ? -33.693 23.054  27.758  1.00 37.71 ? 302 ILE E CA  1 
ATOM   10225 C C   . ILE E 1 307 ? -34.113 22.017  28.803  1.00 38.15 ? 302 ILE E C   1 
ATOM   10226 O O   . ILE E 1 307 ? -35.249 21.540  28.787  1.00 38.28 ? 302 ILE E O   1 
ATOM   10227 C CB  . ILE E 1 307 ? -33.950 24.506  28.263  1.00 37.85 ? 302 ILE E CB  1 
ATOM   10228 C CG1 . ILE E 1 307 ? -33.138 24.783  29.541  1.00 37.80 ? 302 ILE E CG1 1 
ATOM   10229 C CG2 . ILE E 1 307 ? -35.456 24.773  28.461  1.00 37.80 ? 302 ILE E CG2 1 
ATOM   10230 C CD1 . ILE E 1 307 ? -32.884 26.256  29.839  1.00 37.85 ? 302 ILE E CD1 1 
ATOM   10231 N N   . GLY E 1 308 ? -33.186 21.661  29.692  1.00 38.60 ? 303 GLY E N   1 
ATOM   10232 C CA  . GLY E 1 308 ? -33.441 20.672  30.734  1.00 39.25 ? 303 GLY E CA  1 
ATOM   10233 C C   . GLY E 1 308 ? -32.777 19.342  30.433  1.00 39.93 ? 303 GLY E C   1 
ATOM   10234 O O   . GLY E 1 308 ? -31.836 19.280  29.643  1.00 40.04 ? 303 GLY E O   1 
ATOM   10235 N N   . GLU E 1 309 ? -33.265 18.279  31.069  1.00 40.48 ? 304 GLU E N   1 
ATOM   10236 C CA  . GLU E 1 309 ? -32.720 16.935  30.877  1.00 41.21 ? 304 GLU E CA  1 
ATOM   10237 C C   . GLU E 1 309 ? -33.488 16.230  29.763  1.00 41.13 ? 304 GLU E C   1 
ATOM   10238 O O   . GLU E 1 309 ? -34.557 15.658  29.987  1.00 41.23 ? 304 GLU E O   1 
ATOM   10239 C CB  . GLU E 1 309 ? -32.781 16.135  32.180  1.00 41.52 ? 304 GLU E CB  1 
ATOM   10240 C CG  . GLU E 1 309 ? -31.976 16.744  33.334  1.00 43.66 ? 304 GLU E CG  1 
ATOM   10241 C CD  . GLU E 1 309 ? -32.303 16.110  34.683  1.00 46.66 ? 304 GLU E CD  1 
ATOM   10242 O OE1 . GLU E 1 309 ? -32.190 14.865  34.805  1.00 48.16 ? 304 GLU E OE1 1 
ATOM   10243 O OE2 . GLU E 1 309 ? -32.673 16.856  35.621  1.00 46.89 ? 304 GLU E OE2 1 
ATOM   10244 N N   . CYS E 1 310 ? -32.927 16.278  28.559  1.00 40.99 ? 305 CYS E N   1 
ATOM   10245 C CA  . CYS E 1 310 ? -33.652 15.899  27.352  1.00 40.76 ? 305 CYS E CA  1 
ATOM   10246 C C   . CYS E 1 310 ? -33.024 14.726  26.601  1.00 40.32 ? 305 CYS E C   1 
ATOM   10247 O O   . CYS E 1 310 ? -31.815 14.495  26.704  1.00 40.16 ? 305 CYS E O   1 
ATOM   10248 C CB  . CYS E 1 310 ? -33.750 17.109  26.415  1.00 40.77 ? 305 CYS E CB  1 
ATOM   10249 S SG  . CYS E 1 310 ? -34.746 18.471  27.072  1.00 42.24 ? 305 CYS E SG  1 
ATOM   10250 N N   . PRO E 1 311 ? -33.851 13.975  25.845  1.00 39.90 ? 306 PRO E N   1 
ATOM   10251 C CA  . PRO E 1 311 ? -33.299 13.074  24.846  1.00 39.59 ? 306 PRO E CA  1 
ATOM   10252 C C   . PRO E 1 311 ? -32.545 13.873  23.783  1.00 39.30 ? 306 PRO E C   1 
ATOM   10253 O O   . PRO E 1 311 ? -32.698 15.093  23.699  1.00 39.05 ? 306 PRO E O   1 
ATOM   10254 C CB  . PRO E 1 311 ? -34.541 12.394  24.245  1.00 39.44 ? 306 PRO E CB  1 
ATOM   10255 C CG  . PRO E 1 311 ? -35.707 13.190  24.712  1.00 39.61 ? 306 PRO E CG  1 
ATOM   10256 C CD  . PRO E 1 311 ? -35.304 13.791  26.006  1.00 39.92 ? 306 PRO E CD  1 
ATOM   10257 N N   . LYS E 1 312 ? -31.732 13.185  22.992  1.00 39.03 ? 307 LYS E N   1 
ATOM   10258 C CA  . LYS E 1 312 ? -30.899 13.835  21.997  1.00 38.99 ? 307 LYS E CA  1 
ATOM   10259 C C   . LYS E 1 312 ? -31.685 14.020  20.699  1.00 38.55 ? 307 LYS E C   1 
ATOM   10260 O O   . LYS E 1 312 ? -32.321 13.086  20.210  1.00 38.55 ? 307 LYS E O   1 
ATOM   10261 C CB  . LYS E 1 312 ? -29.616 13.024  21.778  1.00 39.35 ? 307 LYS E CB  1 
ATOM   10262 C CG  . LYS E 1 312 ? -28.775 12.814  23.052  1.00 40.27 ? 307 LYS E CG  1 
ATOM   10263 C CD  . LYS E 1 312 ? -27.834 13.985  23.309  1.00 42.03 ? 307 LYS E CD  1 
ATOM   10264 C CE  . LYS E 1 312 ? -27.263 13.965  24.720  1.00 43.20 ? 307 LYS E CE  1 
ATOM   10265 N NZ  . LYS E 1 312 ? -28.084 14.776  25.672  1.00 43.68 ? 307 LYS E NZ  1 
ATOM   10266 N N   . TYR E 1 313 ? -31.651 15.234  20.157  1.00 37.93 ? 308 TYR E N   1 
ATOM   10267 C CA  . TYR E 1 313 ? -32.453 15.571  18.988  1.00 37.51 ? 308 TYR E CA  1 
ATOM   10268 C C   . TYR E 1 313 ? -31.956 14.927  17.695  1.00 37.55 ? 308 TYR E C   1 
ATOM   10269 O O   . TYR E 1 313 ? -30.758 14.893  17.421  1.00 37.61 ? 308 TYR E O   1 
ATOM   10270 C CB  . TYR E 1 313 ? -32.552 17.084  18.812  1.00 37.24 ? 308 TYR E CB  1 
ATOM   10271 C CG  . TYR E 1 313 ? -33.261 17.486  17.540  1.00 36.52 ? 308 TYR E CG  1 
ATOM   10272 C CD1 . TYR E 1 313 ? -34.646 17.406  17.440  1.00 35.57 ? 308 TYR E CD1 1 
ATOM   10273 C CD2 . TYR E 1 313 ? -32.544 17.927  16.430  1.00 35.62 ? 308 TYR E CD2 1 
ATOM   10274 C CE1 . TYR E 1 313 ? -35.300 17.768  16.276  1.00 35.26 ? 308 TYR E CE1 1 
ATOM   10275 C CE2 . TYR E 1 313 ? -33.191 18.285  15.258  1.00 35.28 ? 308 TYR E CE2 1 
ATOM   10276 C CZ  . TYR E 1 313 ? -34.569 18.208  15.191  1.00 34.94 ? 308 TYR E CZ  1 
ATOM   10277 O OH  . TYR E 1 313 ? -35.218 18.564  14.037  1.00 35.08 ? 308 TYR E OH  1 
ATOM   10278 N N   . VAL E 1 314 ? -32.900 14.447  16.895  1.00 37.53 ? 309 VAL E N   1 
ATOM   10279 C CA  . VAL E 1 314 ? -32.601 13.851  15.597  1.00 37.63 ? 309 VAL E CA  1 
ATOM   10280 C C   . VAL E 1 314 ? -33.688 14.281  14.594  1.00 37.64 ? 309 VAL E C   1 
ATOM   10281 O O   . VAL E 1 314 ? -34.733 14.773  15.002  1.00 37.62 ? 309 VAL E O   1 
ATOM   10282 C CB  . VAL E 1 314 ? -32.448 12.304  15.738  1.00 37.58 ? 309 VAL E CB  1 
ATOM   10283 C CG1 . VAL E 1 314 ? -33.790 11.597  15.659  1.00 37.28 ? 309 VAL E CG1 1 
ATOM   10284 C CG2 . VAL E 1 314 ? -31.487 11.762  14.716  1.00 37.68 ? 309 VAL E CG2 1 
ATOM   10285 N N   . LYS E 1 315 ? -33.444 14.132  13.296  1.00 37.96 ? 310 LYS E N   1 
ATOM   10286 C CA  . LYS E 1 315 ? -34.415 14.598  12.289  1.00 38.35 ? 310 LYS E CA  1 
ATOM   10287 C C   . LYS E 1 315 ? -35.236 13.512  11.595  1.00 38.60 ? 310 LYS E C   1 
ATOM   10288 O O   . LYS E 1 315 ? -36.045 13.809  10.711  1.00 38.85 ? 310 LYS E O   1 
ATOM   10289 C CB  . LYS E 1 315 ? -33.742 15.492  11.245  1.00 38.24 ? 310 LYS E CB  1 
ATOM   10290 C CG  . LYS E 1 315 ? -33.977 16.972  11.483  1.00 38.48 ? 310 LYS E CG  1 
ATOM   10291 C CD  . LYS E 1 315 ? -32.874 17.834  10.885  1.00 39.28 ? 310 LYS E CD  1 
ATOM   10292 C CE  . LYS E 1 315 ? -32.909 17.836  9.369   1.00 39.67 ? 310 LYS E CE  1 
ATOM   10293 N NZ  . LYS E 1 315 ? -31.959 18.838  8.830   1.00 40.95 ? 310 LYS E NZ  1 
ATOM   10294 N N   . SER E 1 316 ? -35.035 12.263  12.000  1.00 38.88 ? 311 SER E N   1 
ATOM   10295 C CA  . SER E 1 316 ? -35.766 11.136  11.423  1.00 39.08 ? 311 SER E CA  1 
ATOM   10296 C C   . SER E 1 316 ? -37.251 11.115  11.790  1.00 39.20 ? 311 SER E C   1 
ATOM   10297 O O   . SER E 1 316 ? -37.680 11.742  12.758  1.00 38.82 ? 311 SER E O   1 
ATOM   10298 C CB  . SER E 1 316 ? -35.101 9.808   11.800  1.00 38.99 ? 311 SER E CB  1 
ATOM   10299 O OG  . SER E 1 316 ? -34.099 9.995   12.787  1.00 39.13 ? 311 SER E OG  1 
ATOM   10300 N N   . ASN E 1 317 ? -38.019 10.390  10.981  1.00 39.65 ? 312 ASN E N   1 
ATOM   10301 C CA  . ASN E 1 317 ? -39.420 10.102  11.256  1.00 40.10 ? 312 ASN E CA  1 
ATOM   10302 C C   . ASN E 1 317 ? -39.555 8.801   12.035  1.00 39.80 ? 312 ASN E C   1 
ATOM   10303 O O   . ASN E 1 317 ? -40.551 8.587   12.726  1.00 40.10 ? 312 ASN E O   1 
ATOM   10304 C CB  . ASN E 1 317 ? -40.205 9.992   9.945   1.00 40.50 ? 312 ASN E CB  1 
ATOM   10305 C CG  . ASN E 1 317 ? -39.891 11.121  8.978   1.00 41.96 ? 312 ASN E CG  1 
ATOM   10306 O OD1 . ASN E 1 317 ? -40.197 12.291  9.236   1.00 43.31 ? 312 ASN E OD1 1 
ATOM   10307 N ND2 . ASN E 1 317 ? -39.274 10.773  7.852   1.00 43.54 ? 312 ASN E ND2 1 
ATOM   10308 N N   . ARG E 1 318 ? -38.548 7.937   11.910  1.00 39.38 ? 313 ARG E N   1 
ATOM   10309 C CA  . ARG E 1 318 ? -38.545 6.611   12.527  1.00 39.04 ? 313 ARG E CA  1 
ATOM   10310 C C   . ARG E 1 318 ? -37.140 6.179   12.929  1.00 38.30 ? 313 ARG E C   1 
ATOM   10311 O O   . ARG E 1 318 ? -36.186 6.388   12.183  1.00 38.29 ? 313 ARG E O   1 
ATOM   10312 C CB  . ARG E 1 318 ? -39.120 5.572   11.560  1.00 39.40 ? 313 ARG E CB  1 
ATOM   10313 C CG  . ARG E 1 318 ? -40.625 5.368   11.650  1.00 40.61 ? 313 ARG E CG  1 
ATOM   10314 C CD  . ARG E 1 318 ? -41.095 4.257   10.708  1.00 43.36 ? 313 ARG E CD  1 
ATOM   10315 N NE  . ARG E 1 318 ? -40.293 3.034   10.822  1.00 45.30 ? 313 ARG E NE  1 
ATOM   10316 C CZ  . ARG E 1 318 ? -40.567 2.006   11.626  1.00 46.07 ? 313 ARG E CZ  1 
ATOM   10317 N NH1 . ARG E 1 318 ? -41.636 2.024   12.419  1.00 45.88 ? 313 ARG E NH1 1 
ATOM   10318 N NH2 . ARG E 1 318 ? -39.759 0.950   11.638  1.00 46.12 ? 313 ARG E NH2 1 
ATOM   10319 N N   . LEU E 1 319 ? -37.026 5.575   14.110  1.00 37.55 ? 314 LEU E N   1 
ATOM   10320 C CA  . LEU E 1 319 ? -35.781 4.942   14.565  1.00 36.58 ? 314 LEU E CA  1 
ATOM   10321 C C   . LEU E 1 319 ? -36.086 3.723   15.425  1.00 36.06 ? 314 LEU E C   1 
ATOM   10322 O O   . LEU E 1 319 ? -36.192 3.826   16.650  1.00 36.16 ? 314 LEU E O   1 
ATOM   10323 C CB  . LEU E 1 319 ? -34.901 5.920   15.349  1.00 36.46 ? 314 LEU E CB  1 
ATOM   10324 C CG  . LEU E 1 319 ? -33.791 6.709   14.647  1.00 36.58 ? 314 LEU E CG  1 
ATOM   10325 C CD1 . LEU E 1 319 ? -32.834 7.276   15.698  1.00 36.58 ? 314 LEU E CD1 1 
ATOM   10326 C CD2 . LEU E 1 319 ? -33.018 5.867   13.635  1.00 36.07 ? 314 LEU E CD2 1 
ATOM   10327 N N   . VAL E 1 320 ? -36.234 2.572   14.780  1.00 35.28 ? 315 VAL E N   1 
ATOM   10328 C CA  . VAL E 1 320 ? -36.569 1.340   15.487  1.00 34.67 ? 315 VAL E CA  1 
ATOM   10329 C C   . VAL E 1 320 ? -35.422 0.334   15.421  1.00 34.53 ? 315 VAL E C   1 
ATOM   10330 O O   . VAL E 1 320 ? -34.928 -0.011  14.348  1.00 34.39 ? 315 VAL E O   1 
ATOM   10331 C CB  . VAL E 1 320 ? -37.890 0.717   14.978  1.00 34.61 ? 315 VAL E CB  1 
ATOM   10332 C CG1 . VAL E 1 320 ? -38.206 -0.576  15.726  1.00 33.84 ? 315 VAL E CG1 1 
ATOM   10333 C CG2 . VAL E 1 320 ? -39.039 1.716   15.125  1.00 34.06 ? 315 VAL E CG2 1 
ATOM   10334 N N   . LEU E 1 321 ? -35.007 -0.119  16.595  1.00 34.33 ? 316 LEU E N   1 
ATOM   10335 C CA  . LEU E 1 321 ? -33.906 -1.047  16.740  1.00 34.27 ? 316 LEU E CA  1 
ATOM   10336 C C   . LEU E 1 321 ? -34.457 -2.478  16.752  1.00 34.32 ? 316 LEU E C   1 
ATOM   10337 O O   . LEU E 1 321 ? -35.454 -2.762  17.418  1.00 34.40 ? 316 LEU E O   1 
ATOM   10338 C CB  . LEU E 1 321 ? -33.181 -0.724  18.049  1.00 34.21 ? 316 LEU E CB  1 
ATOM   10339 C CG  . LEU E 1 321 ? -31.657 -0.717  18.205  1.00 34.32 ? 316 LEU E CG  1 
ATOM   10340 C CD1 . LEU E 1 321 ? -30.907 -0.239  16.966  1.00 33.44 ? 316 LEU E CD1 1 
ATOM   10341 C CD2 . LEU E 1 321 ? -31.291 0.140   19.410  1.00 33.56 ? 316 LEU E CD2 1 
ATOM   10342 N N   . ALA E 1 322 ? -33.832 -3.369  15.989  1.00 34.34 ? 317 ALA E N   1 
ATOM   10343 C CA  . ALA E 1 322 ? -34.171 -4.787  16.047  1.00 34.25 ? 317 ALA E CA  1 
ATOM   10344 C C   . ALA E 1 322 ? -33.524 -5.421  17.276  1.00 34.43 ? 317 ALA E C   1 
ATOM   10345 O O   . ALA E 1 322 ? -32.333 -5.221  17.535  1.00 34.25 ? 317 ALA E O   1 
ATOM   10346 C CB  . ALA E 1 322 ? -33.721 -5.498  14.783  1.00 34.23 ? 317 ALA E CB  1 
ATOM   10347 N N   . THR E 1 323 ? -34.316 -6.166  18.042  1.00 34.60 ? 318 THR E N   1 
ATOM   10348 C CA  . THR E 1 323 ? -33.794 -6.903  19.191  1.00 34.84 ? 318 THR E CA  1 
ATOM   10349 C C   . THR E 1 323 ? -34.036 -8.395  19.014  1.00 34.81 ? 318 THR E C   1 
ATOM   10350 O O   . THR E 1 323 ? -33.168 -9.215  19.323  1.00 34.99 ? 318 THR E O   1 
ATOM   10351 C CB  . THR E 1 323 ? -34.400 -6.423  20.528  1.00 34.92 ? 318 THR E CB  1 
ATOM   10352 O OG1 . THR E 1 323 ? -35.828 -6.470  20.453  1.00 35.62 ? 318 THR E OG1 1 
ATOM   10353 C CG2 . THR E 1 323 ? -33.952 -4.996  20.849  1.00 34.35 ? 318 THR E CG2 1 
ATOM   10354 N N   . GLY E 1 324 ? -35.214 -8.739  18.503  1.00 34.67 ? 319 GLY E N   1 
ATOM   10355 C CA  . GLY E 1 324 ? -35.551 -10.123 18.201  1.00 34.49 ? 319 GLY E CA  1 
ATOM   10356 C C   . GLY E 1 324 ? -35.095 -10.515 16.810  1.00 34.55 ? 319 GLY E C   1 
ATOM   10357 O O   . GLY E 1 324 ? -34.244 -9.853  16.217  1.00 34.59 ? 319 GLY E O   1 
ATOM   10358 N N   . LEU E 1 325 ? -35.674 -11.589 16.282  1.00 34.45 ? 320 LEU E N   1 
ATOM   10359 C CA  . LEU E 1 325 ? -35.246 -12.142 15.004  1.00 34.47 ? 320 LEU E CA  1 
ATOM   10360 C C   . LEU E 1 325 ? -36.314 -12.003 13.920  1.00 34.73 ? 320 LEU E C   1 
ATOM   10361 O O   . LEU E 1 325 ? -37.435 -11.566 14.194  1.00 34.59 ? 320 LEU E O   1 
ATOM   10362 C CB  . LEU E 1 325 ? -34.813 -13.607 15.183  1.00 34.43 ? 320 LEU E CB  1 
ATOM   10363 C CG  . LEU E 1 325 ? -35.762 -14.576 15.899  1.00 34.22 ? 320 LEU E CG  1 
ATOM   10364 C CD1 . LEU E 1 325 ? -36.751 -15.187 14.915  1.00 33.50 ? 320 LEU E CD1 1 
ATOM   10365 C CD2 . LEU E 1 325 ? -34.985 -15.667 16.604  1.00 33.26 ? 320 LEU E CD2 1 
ATOM   10366 N N   . ARG E 1 326 ? -35.952 -12.375 12.694  1.00 35.20 ? 321 ARG E N   1 
ATOM   10367 C CA  . ARG E 1 326 ? -36.871 -12.364 11.559  1.00 36.05 ? 321 ARG E CA  1 
ATOM   10368 C C   . ARG E 1 326 ? -38.100 -13.257 11.810  1.00 36.31 ? 321 ARG E C   1 
ATOM   10369 O O   . ARG E 1 326 ? -37.969 -14.466 11.999  1.00 36.14 ? 321 ARG E O   1 
ATOM   10370 C CB  . ARG E 1 326 ? -36.136 -12.801 10.287  1.00 36.13 ? 321 ARG E CB  1 
ATOM   10371 C CG  . ARG E 1 326 ? -36.910 -12.565 8.998   1.00 37.27 ? 321 ARG E CG  1 
ATOM   10372 C CD  . ARG E 1 326 ? -36.179 -13.151 7.794   1.00 39.53 ? 321 ARG E CD  1 
ATOM   10373 N NE  . ARG E 1 326 ? -34.920 -12.453 7.526   1.00 41.08 ? 321 ARG E NE  1 
ATOM   10374 C CZ  . ARG E 1 326 ? -34.798 -11.412 6.707   1.00 41.29 ? 321 ARG E CZ  1 
ATOM   10375 N NH1 . ARG E 1 326 ? -35.859 -10.935 6.064   1.00 40.86 ? 321 ARG E NH1 1 
ATOM   10376 N NH2 . ARG E 1 326 ? -33.610 -10.844 6.534   1.00 41.69 ? 321 ARG E NH2 1 
ATOM   10377 N N   . ASN E 1 327 ? -39.281 -12.641 11.818  1.00 36.85 ? 322 ASN E N   1 
ATOM   10378 C CA  . ASN E 1 327 ? -40.541 -13.340 12.073  1.00 37.66 ? 322 ASN E CA  1 
ATOM   10379 C C   . ASN E 1 327 ? -41.013 -14.159 10.866  1.00 38.19 ? 322 ASN E C   1 
ATOM   10380 O O   . ASN E 1 327 ? -40.675 -13.842 9.720   1.00 38.54 ? 322 ASN E O   1 
ATOM   10381 C CB  . ASN E 1 327 ? -41.622 -12.345 12.503  1.00 37.61 ? 322 ASN E CB  1 
ATOM   10382 C CG  . ASN E 1 327 ? -42.719 -12.988 13.346  1.00 38.01 ? 322 ASN E CG  1 
ATOM   10383 O OD1 . ASN E 1 327 ? -42.591 -14.127 13.804  1.00 38.09 ? 322 ASN E OD1 1 
ATOM   10384 N ND2 . ASN E 1 327 ? -43.803 -12.250 13.560  1.00 37.67 ? 322 ASN E ND2 1 
ATOM   10385 N N   . THR E 1 328 ? -41.783 -15.213 11.134  1.00 38.71 ? 323 THR E N   1 
ATOM   10386 C CA  . THR E 1 328 ? -42.255 -16.135 10.094  1.00 39.20 ? 323 THR E CA  1 
ATOM   10387 C C   . THR E 1 328 ? -43.643 -15.748 9.574   1.00 39.44 ? 323 THR E C   1 
ATOM   10388 O O   . THR E 1 328 ? -43.838 -15.575 8.364   1.00 39.81 ? 323 THR E O   1 
ATOM   10389 C CB  . THR E 1 328 ? -42.255 -17.598 10.607  1.00 39.20 ? 323 THR E CB  1 
ATOM   10390 O OG1 . THR E 1 328 ? -40.909 -18.000 10.873  1.00 39.05 ? 323 THR E OG1 1 
ATOM   10391 C CG2 . THR E 1 328 ? -42.862 -18.557 9.583   1.00 39.37 ? 323 THR E CG2 1 
ATOM   10392 N N   . GLY F 2 1   ? -30.707 -15.437 5.209   1.00 32.04 ? 1   GLY F N   1 
ATOM   10393 C CA  . GLY F 2 1   ? -29.663 -14.822 6.071   1.00 31.95 ? 1   GLY F CA  1 
ATOM   10394 C C   . GLY F 2 1   ? -28.263 -15.264 5.700   1.00 31.94 ? 1   GLY F C   1 
ATOM   10395 O O   . GLY F 2 1   ? -28.077 -16.164 4.883   1.00 32.01 ? 1   GLY F O   1 
ATOM   10396 N N   . LEU F 2 2   ? -27.279 -14.629 6.327   1.00 31.87 ? 2   LEU F N   1 
ATOM   10397 C CA  . LEU F 2 2   ? -25.867 -14.868 6.050   1.00 31.94 ? 2   LEU F CA  1 
ATOM   10398 C C   . LEU F 2 2   ? -25.416 -16.285 6.423   1.00 32.13 ? 2   LEU F C   1 
ATOM   10399 O O   . LEU F 2 2   ? -24.415 -16.780 5.903   1.00 32.29 ? 2   LEU F O   1 
ATOM   10400 C CB  . LEU F 2 2   ? -25.034 -13.840 6.821   1.00 31.88 ? 2   LEU F CB  1 
ATOM   10401 C CG  . LEU F 2 2   ? -23.989 -12.975 6.112   1.00 31.93 ? 2   LEU F CG  1 
ATOM   10402 C CD1 . LEU F 2 2   ? -24.512 -12.357 4.812   1.00 31.41 ? 2   LEU F CD1 1 
ATOM   10403 C CD2 . LEU F 2 2   ? -23.490 -11.889 7.057   1.00 31.83 ? 2   LEU F CD2 1 
ATOM   10404 N N   . PHE F 2 3   ? -26.155 -16.934 7.321   1.00 32.17 ? 3   PHE F N   1 
ATOM   10405 C CA  . PHE F 2 3   ? -25.739 -18.227 7.863   1.00 32.37 ? 3   PHE F CA  1 
ATOM   10406 C C   . PHE F 2 3   ? -26.625 -19.415 7.449   1.00 32.55 ? 3   PHE F C   1 
ATOM   10407 O O   . PHE F 2 3   ? -26.373 -20.557 7.846   1.00 32.36 ? 3   PHE F O   1 
ATOM   10408 C CB  . PHE F 2 3   ? -25.566 -18.127 9.383   1.00 32.16 ? 3   PHE F CB  1 
ATOM   10409 C CG  . PHE F 2 3   ? -24.417 -17.258 9.788   1.00 32.16 ? 3   PHE F CG  1 
ATOM   10410 C CD1 . PHE F 2 3   ? -23.144 -17.799 9.948   1.00 31.81 ? 3   PHE F CD1 1 
ATOM   10411 C CD2 . PHE F 2 3   ? -24.595 -15.889 9.981   1.00 32.21 ? 3   PHE F CD2 1 
ATOM   10412 C CE1 . PHE F 2 3   ? -22.067 -16.995 10.307  1.00 31.55 ? 3   PHE F CE1 1 
ATOM   10413 C CE2 . PHE F 2 3   ? -23.518 -15.074 10.334  1.00 31.97 ? 3   PHE F CE2 1 
ATOM   10414 C CZ  . PHE F 2 3   ? -22.256 -15.630 10.500  1.00 31.78 ? 3   PHE F CZ  1 
ATOM   10415 N N   . GLY F 2 4   ? -27.651 -19.132 6.650   1.00 32.86 ? 4   GLY F N   1 
ATOM   10416 C CA  . GLY F 2 4   ? -28.427 -20.168 5.962   1.00 33.34 ? 4   GLY F CA  1 
ATOM   10417 C C   . GLY F 2 4   ? -29.359 -21.010 6.813   1.00 33.52 ? 4   GLY F C   1 
ATOM   10418 O O   . GLY F 2 4   ? -29.840 -22.043 6.356   1.00 33.57 ? 4   GLY F O   1 
ATOM   10419 N N   . ALA F 2 5   ? -29.636 -20.561 8.036   1.00 33.78 ? 5   ALA F N   1 
ATOM   10420 C CA  . ALA F 2 5   ? -30.429 -21.342 8.984   1.00 34.05 ? 5   ALA F CA  1 
ATOM   10421 C C   . ALA F 2 5   ? -31.837 -20.783 9.149   1.00 34.34 ? 5   ALA F C   1 
ATOM   10422 O O   . ALA F 2 5   ? -32.811 -21.441 8.777   1.00 34.45 ? 5   ALA F O   1 
ATOM   10423 C CB  . ALA F 2 5   ? -29.715 -21.441 10.336  1.00 33.83 ? 5   ALA F CB  1 
ATOM   10424 N N   . ILE F 2 6   ? -31.940 -19.576 9.707   1.00 34.74 ? 6   ILE F N   1 
ATOM   10425 C CA  . ILE F 2 6   ? -33.225 -18.896 9.854   1.00 35.08 ? 6   ILE F CA  1 
ATOM   10426 C C   . ILE F 2 6   ? -33.770 -18.616 8.462   1.00 35.51 ? 6   ILE F C   1 
ATOM   10427 O O   . ILE F 2 6   ? -33.061 -18.070 7.620   1.00 35.64 ? 6   ILE F O   1 
ATOM   10428 C CB  . ILE F 2 6   ? -33.102 -17.603 10.693  1.00 34.97 ? 6   ILE F CB  1 
ATOM   10429 C CG1 . ILE F 2 6   ? -32.926 -17.966 12.171  1.00 34.56 ? 6   ILE F CG1 1 
ATOM   10430 C CG2 . ILE F 2 6   ? -34.322 -16.703 10.496  1.00 34.80 ? 6   ILE F CG2 1 
ATOM   10431 C CD1 . ILE F 2 6   ? -32.744 -16.783 13.108  1.00 34.15 ? 6   ILE F CD1 1 
ATOM   10432 N N   . ALA F 2 7   ? -35.015 -19.033 8.223   1.00 36.08 ? 7   ALA F N   1 
ATOM   10433 C CA  . ALA F 2 7   ? -35.625 -19.010 6.887   1.00 36.51 ? 7   ALA F CA  1 
ATOM   10434 C C   . ALA F 2 7   ? -34.673 -19.586 5.829   1.00 37.01 ? 7   ALA F C   1 
ATOM   10435 O O   . ALA F 2 7   ? -34.592 -19.079 4.702   1.00 37.35 ? 7   ALA F O   1 
ATOM   10436 C CB  . ALA F 2 7   ? -36.078 -17.592 6.521   1.00 36.32 ? 7   ALA F CB  1 
ATOM   10437 N N   . GLY F 2 8   ? -33.950 -20.641 6.211   1.00 37.28 ? 8   GLY F N   1 
ATOM   10438 C CA  . GLY F 2 8   ? -32.952 -21.282 5.350   1.00 37.76 ? 8   GLY F CA  1 
ATOM   10439 C C   . GLY F 2 8   ? -33.185 -22.777 5.289   1.00 38.11 ? 8   GLY F C   1 
ATOM   10440 O O   . GLY F 2 8   ? -34.215 -23.223 4.785   1.00 38.19 ? 8   GLY F O   1 
ATOM   10441 N N   . PHE F 2 9   ? -32.247 -23.562 5.818   1.00 38.49 ? 9   PHE F N   1 
ATOM   10442 C CA  . PHE F 2 9   ? -32.476 -25.007 5.942   1.00 38.89 ? 9   PHE F CA  1 
ATOM   10443 C C   . PHE F 2 9   ? -33.499 -25.345 7.037   1.00 39.07 ? 9   PHE F C   1 
ATOM   10444 O O   . PHE F 2 9   ? -33.976 -26.474 7.109   1.00 39.11 ? 9   PHE F O   1 
ATOM   10445 C CB  . PHE F 2 9   ? -31.163 -25.810 6.079   1.00 39.07 ? 9   PHE F CB  1 
ATOM   10446 C CG  . PHE F 2 9   ? -30.517 -25.738 7.442   1.00 39.32 ? 9   PHE F CG  1 
ATOM   10447 C CD1 . PHE F 2 9   ? -30.855 -26.648 8.439   1.00 40.16 ? 9   PHE F CD1 1 
ATOM   10448 C CD2 . PHE F 2 9   ? -29.538 -24.787 7.712   1.00 39.46 ? 9   PHE F CD2 1 
ATOM   10449 C CE1 . PHE F 2 9   ? -30.244 -26.591 9.699   1.00 40.76 ? 9   PHE F CE1 1 
ATOM   10450 C CE2 . PHE F 2 9   ? -28.923 -24.724 8.963   1.00 40.18 ? 9   PHE F CE2 1 
ATOM   10451 C CZ  . PHE F 2 9   ? -29.276 -25.628 9.958   1.00 40.31 ? 9   PHE F CZ  1 
ATOM   10452 N N   . ILE F 2 10  ? -33.823 -24.362 7.880   1.00 39.28 ? 10  ILE F N   1 
ATOM   10453 C CA  . ILE F 2 10  ? -34.988 -24.445 8.763   1.00 39.71 ? 10  ILE F CA  1 
ATOM   10454 C C   . ILE F 2 10  ? -36.026 -23.456 8.249   1.00 40.28 ? 10  ILE F C   1 
ATOM   10455 O O   . ILE F 2 10  ? -35.885 -22.246 8.430   1.00 40.60 ? 10  ILE F O   1 
ATOM   10456 C CB  . ILE F 2 10  ? -34.656 -24.164 10.247  1.00 39.52 ? 10  ILE F CB  1 
ATOM   10457 C CG1 . ILE F 2 10  ? -33.538 -25.093 10.732  1.00 39.26 ? 10  ILE F CG1 1 
ATOM   10458 C CG2 . ILE F 2 10  ? -35.905 -24.340 11.111  1.00 39.16 ? 10  ILE F CG2 1 
ATOM   10459 C CD1 . ILE F 2 10  ? -32.962 -24.715 12.075  1.00 38.73 ? 10  ILE F CD1 1 
ATOM   10460 N N   . GLU F 2 11  ? -37.066 -23.997 7.618   1.00 40.89 ? 11  GLU F N   1 
ATOM   10461 C CA  . GLU F 2 11  ? -38.016 -23.229 6.812   1.00 41.53 ? 11  GLU F CA  1 
ATOM   10462 C C   . GLU F 2 11  ? -38.762 -22.131 7.565   1.00 41.36 ? 11  GLU F C   1 
ATOM   10463 O O   . GLU F 2 11  ? -38.875 -21.011 7.066   1.00 41.57 ? 11  GLU F O   1 
ATOM   10464 C CB  . GLU F 2 11  ? -39.010 -24.174 6.132   1.00 41.83 ? 11  GLU F CB  1 
ATOM   10465 C CG  . GLU F 2 11  ? -39.571 -23.639 4.821   1.00 44.07 ? 11  GLU F CG  1 
ATOM   10466 C CD  . GLU F 2 11  ? -40.454 -24.651 4.103   1.00 47.17 ? 11  GLU F CD  1 
ATOM   10467 O OE1 . GLU F 2 11  ? -41.277 -25.312 4.782   1.00 48.31 ? 11  GLU F OE1 1 
ATOM   10468 O OE2 . GLU F 2 11  ? -40.328 -24.780 2.861   1.00 48.09 ? 11  GLU F OE2 1 
ATOM   10469 N N   . GLY F 2 12  ? -39.271 -22.449 8.752   1.00 41.25 ? 12  GLY F N   1 
ATOM   10470 C CA  . GLY F 2 12  ? -40.003 -21.472 9.556   1.00 41.13 ? 12  GLY F CA  1 
ATOM   10471 C C   . GLY F 2 12  ? -39.747 -21.567 11.048  1.00 41.22 ? 12  GLY F C   1 
ATOM   10472 O O   . GLY F 2 12  ? -39.152 -22.536 11.533  1.00 41.05 ? 12  GLY F O   1 
ATOM   10473 N N   . GLY F 2 13  ? -40.195 -20.547 11.774  1.00 41.24 ? 13  GLY F N   1 
ATOM   10474 C CA  . GLY F 2 13  ? -40.118 -20.533 13.228  1.00 41.51 ? 13  GLY F CA  1 
ATOM   10475 C C   . GLY F 2 13  ? -41.283 -21.277 13.845  1.00 41.96 ? 13  GLY F C   1 
ATOM   10476 O O   . GLY F 2 13  ? -42.191 -21.724 13.138  1.00 41.92 ? 13  GLY F O   1 
ATOM   10477 N N   . TRP F 2 14  ? -41.260 -21.407 15.169  1.00 42.36 ? 14  TRP F N   1 
ATOM   10478 C CA  . TRP F 2 14  ? -42.298 -22.133 15.888  1.00 42.76 ? 14  TRP F CA  1 
ATOM   10479 C C   . TRP F 2 14  ? -43.130 -21.228 16.778  1.00 43.54 ? 14  TRP F C   1 
ATOM   10480 O O   . TRP F 2 14  ? -42.622 -20.640 17.733  1.00 43.58 ? 14  TRP F O   1 
ATOM   10481 C CB  . TRP F 2 14  ? -41.691 -23.257 16.730  1.00 42.41 ? 14  TRP F CB  1 
ATOM   10482 C CG  . TRP F 2 14  ? -41.021 -24.338 15.937  1.00 41.30 ? 14  TRP F CG  1 
ATOM   10483 C CD1 . TRP F 2 14  ? -41.355 -24.770 14.682  1.00 40.27 ? 14  TRP F CD1 1 
ATOM   10484 C CD2 . TRP F 2 14  ? -39.923 -25.152 16.361  1.00 39.99 ? 14  TRP F CD2 1 
ATOM   10485 N NE1 . TRP F 2 14  ? -40.519 -25.788 14.294  1.00 39.79 ? 14  TRP F NE1 1 
ATOM   10486 C CE2 . TRP F 2 14  ? -39.634 -26.047 15.306  1.00 39.65 ? 14  TRP F CE2 1 
ATOM   10487 C CE3 . TRP F 2 14  ? -39.151 -25.210 17.530  1.00 39.25 ? 14  TRP F CE3 1 
ATOM   10488 C CZ2 . TRP F 2 14  ? -38.602 -26.991 15.383  1.00 39.11 ? 14  TRP F CZ2 1 
ATOM   10489 C CZ3 . TRP F 2 14  ? -38.121 -26.152 17.607  1.00 38.82 ? 14  TRP F CZ3 1 
ATOM   10490 C CH2 . TRP F 2 14  ? -37.861 -27.029 16.538  1.00 38.63 ? 14  TRP F CH2 1 
ATOM   10491 N N   . GLN F 2 15  ? -44.418 -21.139 16.463  1.00 44.67 ? 15  GLN F N   1 
ATOM   10492 C CA  . GLN F 2 15  ? -45.384 -20.390 17.265  1.00 45.87 ? 15  GLN F CA  1 
ATOM   10493 C C   . GLN F 2 15  ? -45.571 -21.047 18.636  1.00 46.44 ? 15  GLN F C   1 
ATOM   10494 O O   . GLN F 2 15  ? -46.004 -20.399 19.590  1.00 46.49 ? 15  GLN F O   1 
ATOM   10495 C CB  . GLN F 2 15  ? -46.727 -20.340 16.531  1.00 46.11 ? 15  GLN F CB  1 
ATOM   10496 C CG  . GLN F 2 15  ? -47.461 -19.005 16.613  1.00 47.31 ? 15  GLN F CG  1 
ATOM   10497 C CD  . GLN F 2 15  ? -47.113 -18.049 15.469  1.00 49.04 ? 15  GLN F CD  1 
ATOM   10498 O OE1 . GLN F 2 15  ? -47.730 -16.989 15.329  1.00 49.69 ? 15  GLN F OE1 1 
ATOM   10499 N NE2 . GLN F 2 15  ? -46.127 -18.419 14.649  1.00 48.75 ? 15  GLN F NE2 1 
ATOM   10500 N N   . GLY F 2 16  ? -45.240 -22.336 18.721  1.00 47.23 ? 16  GLY F N   1 
ATOM   10501 C CA  . GLY F 2 16  ? -45.397 -23.119 19.946  1.00 48.00 ? 16  GLY F CA  1 
ATOM   10502 C C   . GLY F 2 16  ? -44.310 -22.950 20.996  1.00 48.63 ? 16  GLY F C   1 
ATOM   10503 O O   . GLY F 2 16  ? -44.520 -23.293 22.162  1.00 48.65 ? 16  GLY F O   1 
ATOM   10504 N N   . MET F 2 17  ? -43.151 -22.427 20.596  1.00 49.24 ? 17  MET F N   1 
ATOM   10505 C CA  . MET F 2 17  ? -42.036 -22.235 21.530  1.00 49.97 ? 17  MET F CA  1 
ATOM   10506 C C   . MET F 2 17  ? -41.953 -20.803 22.060  1.00 50.26 ? 17  MET F C   1 
ATOM   10507 O O   . MET F 2 17  ? -41.384 -19.917 21.414  1.00 50.26 ? 17  MET F O   1 
ATOM   10508 C CB  . MET F 2 17  ? -40.708 -22.654 20.899  1.00 49.99 ? 17  MET F CB  1 
ATOM   10509 C CG  . MET F 2 17  ? -39.587 -22.814 21.914  1.00 50.90 ? 17  MET F CG  1 
ATOM   10510 S SD  . MET F 2 17  ? -37.987 -23.117 21.154  1.00 53.31 ? 17  MET F SD  1 
ATOM   10511 C CE  . MET F 2 17  ? -37.676 -21.506 20.422  1.00 52.89 ? 17  MET F CE  1 
ATOM   10512 N N   . VAL F 2 18  ? -42.512 -20.598 23.251  1.00 50.68 ? 18  VAL F N   1 
ATOM   10513 C CA  . VAL F 2 18  ? -42.640 -19.268 23.847  1.00 51.10 ? 18  VAL F CA  1 
ATOM   10514 C C   . VAL F 2 18  ? -41.637 -19.066 24.990  1.00 51.26 ? 18  VAL F C   1 
ATOM   10515 O O   . VAL F 2 18  ? -41.597 -18.006 25.622  1.00 51.48 ? 18  VAL F O   1 
ATOM   10516 C CB  . VAL F 2 18  ? -44.085 -19.018 24.368  1.00 51.25 ? 18  VAL F CB  1 
ATOM   10517 C CG1 . VAL F 2 18  ? -44.396 -17.516 24.408  1.00 51.63 ? 18  VAL F CG1 1 
ATOM   10518 C CG2 . VAL F 2 18  ? -45.114 -19.750 23.506  1.00 51.05 ? 18  VAL F CG2 1 
ATOM   10519 N N   . ASP F 2 19  ? -40.820 -20.085 25.237  1.00 51.34 ? 19  ASP F N   1 
ATOM   10520 C CA  . ASP F 2 19  ? -39.884 -20.087 26.360  1.00 51.30 ? 19  ASP F CA  1 
ATOM   10521 C C   . ASP F 2 19  ? -38.606 -19.280 26.073  1.00 50.82 ? 19  ASP F C   1 
ATOM   10522 O O   . ASP F 2 19  ? -37.921 -18.847 27.002  1.00 50.83 ? 19  ASP F O   1 
ATOM   10523 C CB  . ASP F 2 19  ? -39.542 -21.535 26.741  1.00 51.63 ? 19  ASP F CB  1 
ATOM   10524 C CG  . ASP F 2 19  ? -39.211 -21.695 28.217  1.00 52.90 ? 19  ASP F CG  1 
ATOM   10525 O OD1 . ASP F 2 19  ? -38.118 -21.251 28.648  1.00 53.95 ? 19  ASP F OD1 1 
ATOM   10526 O OD2 . ASP F 2 19  ? -40.044 -22.284 28.944  1.00 54.04 ? 19  ASP F OD2 1 
ATOM   10527 N N   . GLY F 2 20  ? -38.292 -19.080 24.793  1.00 50.26 ? 20  GLY F N   1 
ATOM   10528 C CA  . GLY F 2 20  ? -37.085 -18.341 24.398  1.00 49.53 ? 20  GLY F CA  1 
ATOM   10529 C C   . GLY F 2 20  ? -36.972 -18.078 22.906  1.00 48.91 ? 20  GLY F C   1 
ATOM   10530 O O   . GLY F 2 20  ? -37.956 -18.203 22.175  1.00 49.00 ? 20  GLY F O   1 
ATOM   10531 N N   . TRP F 2 21  ? -35.769 -17.720 22.455  1.00 48.24 ? 21  TRP F N   1 
ATOM   10532 C CA  . TRP F 2 21  ? -35.525 -17.423 21.036  1.00 47.52 ? 21  TRP F CA  1 
ATOM   10533 C C   . TRP F 2 21  ? -35.146 -18.650 20.200  1.00 47.23 ? 21  TRP F C   1 
ATOM   10534 O O   . TRP F 2 21  ? -35.592 -18.791 19.060  1.00 46.91 ? 21  TRP F O   1 
ATOM   10535 C CB  . TRP F 2 21  ? -34.470 -16.318 20.865  1.00 47.38 ? 21  TRP F CB  1 
ATOM   10536 C CG  . TRP F 2 21  ? -35.010 -14.908 20.980  1.00 46.76 ? 21  TRP F CG  1 
ATOM   10537 C CD1 . TRP F 2 21  ? -36.266 -14.477 20.653  1.00 46.63 ? 21  TRP F CD1 1 
ATOM   10538 C CD2 . TRP F 2 21  ? -34.293 -13.746 21.425  1.00 46.20 ? 21  TRP F CD2 1 
ATOM   10539 N NE1 . TRP F 2 21  ? -36.381 -13.125 20.882  1.00 46.77 ? 21  TRP F NE1 1 
ATOM   10540 C CE2 . TRP F 2 21  ? -35.184 -12.652 21.355  1.00 46.32 ? 21  TRP F CE2 1 
ATOM   10541 C CE3 . TRP F 2 21  ? -32.987 -13.525 21.882  1.00 46.23 ? 21  TRP F CE3 1 
ATOM   10542 C CZ2 . TRP F 2 21  ? -34.811 -11.354 21.724  1.00 46.15 ? 21  TRP F CZ2 1 
ATOM   10543 C CZ3 . TRP F 2 21  ? -32.616 -12.234 22.248  1.00 46.35 ? 21  TRP F CZ3 1 
ATOM   10544 C CH2 . TRP F 2 21  ? -33.527 -11.166 22.166  1.00 46.06 ? 21  TRP F CH2 1 
ATOM   10545 N N   . TYR F 2 22  ? -34.313 -19.521 20.763  1.00 47.00 ? 22  TYR F N   1 
ATOM   10546 C CA  . TYR F 2 22  ? -33.902 -20.754 20.088  1.00 46.73 ? 22  TYR F CA  1 
ATOM   10547 C C   . TYR F 2 22  ? -34.136 -21.961 20.995  1.00 46.65 ? 22  TYR F C   1 
ATOM   10548 O O   . TYR F 2 22  ? -34.082 -21.841 22.221  1.00 46.61 ? 22  TYR F O   1 
ATOM   10549 C CB  . TYR F 2 22  ? -32.422 -20.696 19.694  1.00 46.67 ? 22  TYR F CB  1 
ATOM   10550 C CG  . TYR F 2 22  ? -31.850 -19.304 19.525  1.00 46.11 ? 22  TYR F CG  1 
ATOM   10551 C CD1 . TYR F 2 22  ? -32.154 -18.529 18.402  1.00 45.46 ? 22  TYR F CD1 1 
ATOM   10552 C CD2 . TYR F 2 22  ? -30.989 -18.770 20.480  1.00 45.76 ? 22  TYR F CD2 1 
ATOM   10553 C CE1 . TYR F 2 22  ? -31.624 -17.253 18.242  1.00 45.03 ? 22  TYR F CE1 1 
ATOM   10554 C CE2 . TYR F 2 22  ? -30.450 -17.491 20.331  1.00 45.85 ? 22  TYR F CE2 1 
ATOM   10555 C CZ  . TYR F 2 22  ? -30.772 -16.739 19.211  1.00 45.46 ? 22  TYR F CZ  1 
ATOM   10556 O OH  . TYR F 2 22  ? -30.239 -15.478 19.063  1.00 44.80 ? 22  TYR F OH  1 
ATOM   10557 N N   . GLY F 2 23  ? -34.387 -23.123 20.398  1.00 46.49 ? 23  GLY F N   1 
ATOM   10558 C CA  . GLY F 2 23  ? -34.577 -24.339 21.187  1.00 46.27 ? 23  GLY F CA  1 
ATOM   10559 C C   . GLY F 2 23  ? -34.821 -25.627 20.423  1.00 46.12 ? 23  GLY F C   1 
ATOM   10560 O O   . GLY F 2 23  ? -34.363 -25.799 19.290  1.00 45.93 ? 23  GLY F O   1 
ATOM   10561 N N   . TYR F 2 24  ? -35.566 -26.527 21.060  1.00 46.10 ? 24  TYR F N   1 
ATOM   10562 C CA  . TYR F 2 24  ? -35.746 -27.886 20.570  1.00 46.02 ? 24  TYR F CA  1 
ATOM   10563 C C   . TYR F 2 24  ? -37.210 -28.303 20.504  1.00 46.26 ? 24  TYR F C   1 
ATOM   10564 O O   . TYR F 2 24  ? -38.046 -27.798 21.255  1.00 46.20 ? 24  TYR F O   1 
ATOM   10565 C CB  . TYR F 2 24  ? -35.006 -28.872 21.475  1.00 45.72 ? 24  TYR F CB  1 
ATOM   10566 C CG  . TYR F 2 24  ? -33.588 -28.491 21.819  1.00 44.95 ? 24  TYR F CG  1 
ATOM   10567 C CD1 . TYR F 2 24  ? -32.530 -28.884 21.007  1.00 44.29 ? 24  TYR F CD1 1 
ATOM   10568 C CD2 . TYR F 2 24  ? -33.301 -27.750 22.967  1.00 44.35 ? 24  TYR F CD2 1 
ATOM   10569 C CE1 . TYR F 2 24  ? -31.222 -28.546 21.318  1.00 44.00 ? 24  TYR F CE1 1 
ATOM   10570 C CE2 . TYR F 2 24  ? -31.990 -27.407 23.291  1.00 43.97 ? 24  TYR F CE2 1 
ATOM   10571 C CZ  . TYR F 2 24  ? -30.956 -27.809 22.461  1.00 44.01 ? 24  TYR F CZ  1 
ATOM   10572 O OH  . TYR F 2 24  ? -29.652 -27.482 22.763  1.00 44.09 ? 24  TYR F OH  1 
ATOM   10573 N N   . HIS F 2 25  ? -37.504 -29.225 19.590  1.00 46.74 ? 25  HIS F N   1 
ATOM   10574 C CA  . HIS F 2 25  ? -38.732 -30.016 19.641  1.00 47.35 ? 25  HIS F CA  1 
ATOM   10575 C C   . HIS F 2 25  ? -38.342 -31.492 19.642  1.00 47.95 ? 25  HIS F C   1 
ATOM   10576 O O   . HIS F 2 25  ? -37.670 -31.968 18.726  1.00 47.76 ? 25  HIS F O   1 
ATOM   10577 C CB  . HIS F 2 25  ? -39.678 -29.698 18.476  1.00 47.07 ? 25  HIS F CB  1 
ATOM   10578 C CG  . HIS F 2 25  ? -40.975 -30.449 18.530  1.00 46.70 ? 25  HIS F CG  1 
ATOM   10579 N ND1 . HIS F 2 25  ? -42.123 -29.917 19.079  1.00 46.06 ? 25  HIS F ND1 1 
ATOM   10580 C CD2 . HIS F 2 25  ? -41.302 -31.696 18.111  1.00 46.10 ? 25  HIS F CD2 1 
ATOM   10581 C CE1 . HIS F 2 25  ? -43.102 -30.800 18.991  1.00 45.84 ? 25  HIS F CE1 1 
ATOM   10582 N NE2 . HIS F 2 25  ? -42.630 -31.889 18.410  1.00 45.68 ? 25  HIS F NE2 1 
ATOM   10583 N N   . HIS F 2 26  ? -38.749 -32.198 20.693  1.00 48.99 ? 26  HIS F N   1 
ATOM   10584 C CA  . HIS F 2 26  ? -38.443 -33.617 20.843  1.00 49.84 ? 26  HIS F CA  1 
ATOM   10585 C C   . HIS F 2 26  ? -39.677 -34.445 20.541  1.00 50.28 ? 26  HIS F C   1 
ATOM   10586 O O   . HIS F 2 26  ? -40.804 -33.972 20.698  1.00 50.37 ? 26  HIS F O   1 
ATOM   10587 C CB  . HIS F 2 26  ? -37.914 -33.926 22.255  1.00 50.00 ? 26  HIS F CB  1 
ATOM   10588 C CG  . HIS F 2 26  ? -38.988 -34.110 23.286  1.00 50.56 ? 26  HIS F CG  1 
ATOM   10589 N ND1 . HIS F 2 26  ? -39.537 -33.057 23.986  1.00 51.31 ? 26  HIS F ND1 1 
ATOM   10590 C CD2 . HIS F 2 26  ? -39.610 -35.225 23.736  1.00 51.19 ? 26  HIS F CD2 1 
ATOM   10591 C CE1 . HIS F 2 26  ? -40.454 -33.515 24.820  1.00 51.43 ? 26  HIS F CE1 1 
ATOM   10592 N NE2 . HIS F 2 26  ? -40.517 -34.828 24.689  1.00 51.87 ? 26  HIS F NE2 1 
ATOM   10593 N N   . SER F 2 27  ? -39.450 -35.678 20.100  1.00 50.90 ? 27  SER F N   1 
ATOM   10594 C CA  . SER F 2 27  ? -40.521 -36.628 19.833  1.00 51.51 ? 27  SER F CA  1 
ATOM   10595 C C   . SER F 2 27  ? -40.002 -38.044 20.051  1.00 52.02 ? 27  SER F C   1 
ATOM   10596 O O   . SER F 2 27  ? -39.071 -38.494 19.371  1.00 52.11 ? 27  SER F O   1 
ATOM   10597 C CB  . SER F 2 27  ? -41.054 -36.458 18.408  1.00 51.49 ? 27  SER F CB  1 
ATOM   10598 O OG  . SER F 2 27  ? -42.170 -37.296 18.173  1.00 51.54 ? 27  SER F OG  1 
ATOM   10599 N N   . ASN F 2 28  ? -40.592 -38.728 21.027  1.00 52.62 ? 28  ASN F N   1 
ATOM   10600 C CA  . ASN F 2 28  ? -40.257 -40.119 21.319  1.00 53.23 ? 28  ASN F CA  1 
ATOM   10601 C C   . ASN F 2 28  ? -41.472 -40.903 21.819  1.00 53.99 ? 28  ASN F C   1 
ATOM   10602 O O   . ASN F 2 28  ? -42.608 -40.417 21.745  1.00 54.18 ? 28  ASN F O   1 
ATOM   10603 C CB  . ASN F 2 28  ? -39.069 -40.216 22.295  1.00 52.93 ? 28  ASN F CB  1 
ATOM   10604 C CG  . ASN F 2 28  ? -39.354 -39.593 23.658  1.00 52.24 ? 28  ASN F CG  1 
ATOM   10605 O OD1 . ASN F 2 28  ? -40.503 -39.343 24.028  1.00 51.38 ? 28  ASN F OD1 1 
ATOM   10606 N ND2 . ASN F 2 28  ? -38.294 -39.349 24.416  1.00 51.51 ? 28  ASN F ND2 1 
ATOM   10607 N N   . GLU F 2 29  ? -41.226 -42.108 22.329  1.00 54.85 ? 29  GLU F N   1 
ATOM   10608 C CA  . GLU F 2 29  ? -42.289 -42.989 22.818  1.00 55.52 ? 29  GLU F CA  1 
ATOM   10609 C C   . GLU F 2 29  ? -43.137 -42.370 23.937  1.00 55.57 ? 29  GLU F C   1 
ATOM   10610 O O   . GLU F 2 29  ? -44.356 -42.566 23.980  1.00 55.55 ? 29  GLU F O   1 
ATOM   10611 C CB  . GLU F 2 29  ? -41.701 -44.334 23.250  1.00 55.79 ? 29  GLU F CB  1 
ATOM   10612 C CG  . GLU F 2 29  ? -41.482 -45.301 22.090  1.00 57.01 ? 29  GLU F CG  1 
ATOM   10613 C CD  . GLU F 2 29  ? -42.790 -45.858 21.541  1.00 58.85 ? 29  GLU F CD  1 
ATOM   10614 O OE1 . GLU F 2 29  ? -43.022 -45.744 20.313  1.00 59.35 ? 29  GLU F OE1 1 
ATOM   10615 O OE2 . GLU F 2 29  ? -43.589 -46.400 22.342  1.00 59.20 ? 29  GLU F OE2 1 
ATOM   10616 N N   . GLN F 2 30  ? -42.488 -41.621 24.827  1.00 55.65 ? 30  GLN F N   1 
ATOM   10617 C CA  . GLN F 2 30  ? -43.188 -40.884 25.877  1.00 55.71 ? 30  GLN F CA  1 
ATOM   10618 C C   . GLN F 2 30  ? -43.424 -39.411 25.500  1.00 55.92 ? 30  GLN F C   1 
ATOM   10619 O O   . GLN F 2 30  ? -42.832 -38.497 26.088  1.00 56.15 ? 30  GLN F O   1 
ATOM   10620 C CB  . GLN F 2 30  ? -42.472 -41.022 27.228  1.00 55.57 ? 30  GLN F CB  1 
ATOM   10621 C CG  . GLN F 2 30  ? -40.947 -40.974 27.159  1.00 55.28 ? 30  GLN F CG  1 
ATOM   10622 C CD  . GLN F 2 30  ? -40.274 -41.311 28.482  1.00 54.59 ? 30  GLN F CD  1 
ATOM   10623 O OE1 . GLN F 2 30  ? -39.047 -41.406 28.558  1.00 54.23 ? 30  GLN F OE1 1 
ATOM   10624 N NE2 . GLN F 2 30  ? -41.073 -41.497 29.528  1.00 54.14 ? 30  GLN F NE2 1 
ATOM   10625 N N   . GLY F 2 31  ? -44.285 -39.202 24.501  1.00 55.90 ? 31  GLY F N   1 
ATOM   10626 C CA  . GLY F 2 31  ? -44.792 -37.873 24.141  1.00 55.67 ? 31  GLY F CA  1 
ATOM   10627 C C   . GLY F 2 31  ? -43.822 -36.926 23.453  1.00 55.50 ? 31  GLY F C   1 
ATOM   10628 O O   . GLY F 2 31  ? -42.623 -37.206 23.344  1.00 55.49 ? 31  GLY F O   1 
ATOM   10629 N N   . SER F 2 32  ? -44.358 -35.795 22.996  1.00 55.20 ? 32  SER F N   1 
ATOM   10630 C CA  . SER F 2 32  ? -43.582 -34.780 22.280  1.00 54.89 ? 32  SER F CA  1 
ATOM   10631 C C   . SER F 2 32  ? -43.847 -33.377 22.837  1.00 54.67 ? 32  SER F C   1 
ATOM   10632 O O   . SER F 2 32  ? -44.858 -33.150 23.507  1.00 54.61 ? 32  SER F O   1 
ATOM   10633 C CB  . SER F 2 32  ? -43.912 -34.824 20.787  1.00 54.79 ? 32  SER F CB  1 
ATOM   10634 O OG  . SER F 2 32  ? -45.243 -34.404 20.554  1.00 54.75 ? 32  SER F OG  1 
ATOM   10635 N N   . GLY F 2 33  ? -42.943 -32.439 22.557  1.00 54.43 ? 33  GLY F N   1 
ATOM   10636 C CA  . GLY F 2 33  ? -43.117 -31.060 23.017  1.00 54.09 ? 33  GLY F CA  1 
ATOM   10637 C C   . GLY F 2 33  ? -42.016 -30.077 22.660  1.00 53.84 ? 33  GLY F C   1 
ATOM   10638 O O   . GLY F 2 33  ? -41.020 -30.435 22.020  1.00 53.83 ? 33  GLY F O   1 
ATOM   10639 N N   . TYR F 2 34  ? -42.211 -28.829 23.084  1.00 53.49 ? 34  TYR F N   1 
ATOM   10640 C CA  . TYR F 2 34  ? -41.256 -27.749 22.856  1.00 52.96 ? 34  TYR F CA  1 
ATOM   10641 C C   . TYR F 2 34  ? -40.500 -27.397 24.130  1.00 52.86 ? 34  TYR F C   1 
ATOM   10642 O O   . TYR F 2 34  ? -41.086 -27.322 25.211  1.00 52.97 ? 34  TYR F O   1 
ATOM   10643 C CB  . TYR F 2 34  ? -41.974 -26.493 22.344  1.00 52.79 ? 34  TYR F CB  1 
ATOM   10644 C CG  . TYR F 2 34  ? -42.570 -26.608 20.960  1.00 51.95 ? 34  TYR F CG  1 
ATOM   10645 C CD1 . TYR F 2 34  ? -41.774 -26.471 19.824  1.00 51.14 ? 34  TYR F CD1 1 
ATOM   10646 C CD2 . TYR F 2 34  ? -43.936 -26.828 20.784  1.00 51.70 ? 34  TYR F CD2 1 
ATOM   10647 C CE1 . TYR F 2 34  ? -42.316 -26.568 18.547  1.00 50.59 ? 34  TYR F CE1 1 
ATOM   10648 C CE2 . TYR F 2 34  ? -44.492 -26.928 19.506  1.00 51.38 ? 34  TYR F CE2 1 
ATOM   10649 C CZ  . TYR F 2 34  ? -43.674 -26.795 18.393  1.00 50.84 ? 34  TYR F CZ  1 
ATOM   10650 O OH  . TYR F 2 34  ? -44.207 -26.889 17.127  1.00 50.22 ? 34  TYR F OH  1 
ATOM   10651 N N   . ALA F 2 35  ? -39.196 -27.175 23.992  1.00 52.70 ? 35  ALA F N   1 
ATOM   10652 C CA  . ALA F 2 35  ? -38.375 -26.626 25.072  1.00 52.59 ? 35  ALA F CA  1 
ATOM   10653 C C   . ALA F 2 35  ? -37.302 -25.699 24.504  1.00 52.53 ? 35  ALA F C   1 
ATOM   10654 O O   . ALA F 2 35  ? -36.687 -26.002 23.479  1.00 52.59 ? 35  ALA F O   1 
ATOM   10655 C CB  . ALA F 2 35  ? -37.743 -27.738 25.889  1.00 52.56 ? 35  ALA F CB  1 
ATOM   10656 N N   . ALA F 2 36  ? -37.083 -24.571 25.173  1.00 52.39 ? 36  ALA F N   1 
ATOM   10657 C CA  . ALA F 2 36  ? -36.094 -23.596 24.723  1.00 52.25 ? 36  ALA F CA  1 
ATOM   10658 C C   . ALA F 2 36  ? -34.724 -23.867 25.331  1.00 52.11 ? 36  ALA F C   1 
ATOM   10659 O O   . ALA F 2 36  ? -34.624 -24.266 26.492  1.00 52.08 ? 36  ALA F O   1 
ATOM   10660 C CB  . ALA F 2 36  ? -36.553 -22.188 25.057  1.00 52.20 ? 36  ALA F CB  1 
ATOM   10661 N N   . ASP F 2 37  ? -33.677 -23.659 24.537  1.00 52.08 ? 37  ASP F N   1 
ATOM   10662 C CA  . ASP F 2 37  ? -32.308 -23.714 25.037  1.00 52.21 ? 37  ASP F CA  1 
ATOM   10663 C C   . ASP F 2 37  ? -32.002 -22.429 25.802  1.00 52.35 ? 37  ASP F C   1 
ATOM   10664 O O   . ASP F 2 37  ? -31.703 -21.394 25.201  1.00 52.38 ? 37  ASP F O   1 
ATOM   10665 C CB  . ASP F 2 37  ? -31.310 -23.918 23.896  1.00 52.14 ? 37  ASP F CB  1 
ATOM   10666 C CG  . ASP F 2 37  ? -29.874 -24.043 24.387  1.00 52.19 ? 37  ASP F CG  1 
ATOM   10667 O OD1 . ASP F 2 37  ? -29.368 -25.180 24.474  1.00 52.63 ? 37  ASP F OD1 1 
ATOM   10668 O OD2 . ASP F 2 37  ? -29.248 -23.008 24.690  1.00 51.94 ? 37  ASP F OD2 1 
ATOM   10669 N N   . LYS F 2 38  ? -32.085 -22.513 27.128  1.00 52.53 ? 38  LYS F N   1 
ATOM   10670 C CA  . LYS F 2 38  ? -31.889 -21.364 28.014  1.00 52.74 ? 38  LYS F CA  1 
ATOM   10671 C C   . LYS F 2 38  ? -30.523 -20.698 27.857  1.00 52.55 ? 38  LYS F C   1 
ATOM   10672 O O   . LYS F 2 38  ? -30.430 -19.468 27.849  1.00 52.46 ? 38  LYS F O   1 
ATOM   10673 C CB  . LYS F 2 38  ? -32.114 -21.766 29.476  1.00 52.92 ? 38  LYS F CB  1 
ATOM   10674 C CG  . LYS F 2 38  ? -33.568 -22.057 29.827  1.00 53.97 ? 38  LYS F CG  1 
ATOM   10675 C CD  . LYS F 2 38  ? -33.743 -22.237 31.330  1.00 55.52 ? 38  LYS F CD  1 
ATOM   10676 C CE  . LYS F 2 38  ? -35.211 -22.191 31.728  1.00 56.19 ? 38  LYS F CE  1 
ATOM   10677 N NZ  . LYS F 2 38  ? -35.363 -21.894 33.181  1.00 56.68 ? 38  LYS F NZ  1 
ATOM   10678 N N   . GLU F 2 39  ? -29.476 -21.511 27.721  1.00 52.35 ? 39  GLU F N   1 
ATOM   10679 C CA  . GLU F 2 39  ? -28.104 -21.010 27.636  1.00 52.30 ? 39  GLU F CA  1 
ATOM   10680 C C   . GLU F 2 39  ? -27.910 -20.024 26.479  1.00 51.80 ? 39  GLU F C   1 
ATOM   10681 O O   . GLU F 2 39  ? -27.612 -18.847 26.700  1.00 51.91 ? 39  GLU F O   1 
ATOM   10682 C CB  . GLU F 2 39  ? -27.112 -22.173 27.517  1.00 52.53 ? 39  GLU F CB  1 
ATOM   10683 C CG  . GLU F 2 39  ? -25.653 -21.754 27.652  1.00 53.99 ? 39  GLU F CG  1 
ATOM   10684 C CD  . GLU F 2 39  ? -24.720 -22.592 26.794  1.00 55.91 ? 39  GLU F CD  1 
ATOM   10685 O OE1 . GLU F 2 39  ? -24.426 -23.748 27.176  1.00 56.63 ? 39  GLU F OE1 1 
ATOM   10686 O OE2 . GLU F 2 39  ? -24.275 -22.087 25.737  1.00 56.59 ? 39  GLU F OE2 1 
ATOM   10687 N N   . SER F 2 40  ? -28.093 -20.509 25.253  1.00 51.11 ? 40  SER F N   1 
ATOM   10688 C CA  . SER F 2 40  ? -27.892 -19.700 24.054  1.00 50.37 ? 40  SER F CA  1 
ATOM   10689 C C   . SER F 2 40  ? -28.864 -18.518 23.960  1.00 49.87 ? 40  SER F C   1 
ATOM   10690 O O   . SER F 2 40  ? -28.528 -17.482 23.380  1.00 49.75 ? 40  SER F O   1 
ATOM   10691 C CB  . SER F 2 40  ? -27.993 -20.571 22.803  1.00 50.35 ? 40  SER F CB  1 
ATOM   10692 O OG  . SER F 2 40  ? -29.265 -21.189 22.726  1.00 50.55 ? 40  SER F OG  1 
ATOM   10693 N N   . THR F 2 41  ? -30.061 -18.681 24.523  1.00 49.14 ? 41  THR F N   1 
ATOM   10694 C CA  . THR F 2 41  ? -31.043 -17.600 24.586  1.00 48.61 ? 41  THR F CA  1 
ATOM   10695 C C   . THR F 2 41  ? -30.541 -16.461 25.480  1.00 48.43 ? 41  THR F C   1 
ATOM   10696 O O   . THR F 2 41  ? -30.567 -15.296 25.077  1.00 48.53 ? 41  THR F O   1 
ATOM   10697 C CB  . THR F 2 41  ? -32.426 -18.104 25.067  1.00 48.51 ? 41  THR F CB  1 
ATOM   10698 O OG1 . THR F 2 41  ? -32.872 -19.167 24.215  1.00 48.29 ? 41  THR F OG1 1 
ATOM   10699 C CG2 . THR F 2 41  ? -33.460 -16.983 25.036  1.00 48.54 ? 41  THR F CG2 1 
ATOM   10700 N N   . GLN F 2 42  ? -30.076 -16.806 26.682  1.00 47.99 ? 42  GLN F N   1 
ATOM   10701 C CA  . GLN F 2 42  ? -29.526 -15.835 27.627  1.00 47.48 ? 42  GLN F CA  1 
ATOM   10702 C C   . GLN F 2 42  ? -28.280 -15.151 27.056  1.00 47.14 ? 42  GLN F C   1 
ATOM   10703 O O   . GLN F 2 42  ? -28.119 -13.936 27.181  1.00 46.99 ? 42  GLN F O   1 
ATOM   10704 C CB  . GLN F 2 42  ? -29.214 -16.505 28.974  1.00 47.46 ? 42  GLN F CB  1 
ATOM   10705 C CG  . GLN F 2 42  ? -28.777 -15.542 30.085  1.00 47.46 ? 42  GLN F CG  1 
ATOM   10706 C CD  . GLN F 2 42  ? -29.826 -14.483 30.404  1.00 47.44 ? 42  GLN F CD  1 
ATOM   10707 O OE1 . GLN F 2 42  ? -30.981 -14.796 30.695  1.00 46.86 ? 42  GLN F OE1 1 
ATOM   10708 N NE2 . GLN F 2 42  ? -29.422 -13.220 30.349  1.00 48.13 ? 42  GLN F NE2 1 
ATOM   10709 N N   . LYS F 2 43  ? -27.417 -15.946 26.426  1.00 46.77 ? 43  LYS F N   1 
ATOM   10710 C CA  . LYS F 2 43  ? -26.225 -15.456 25.730  1.00 46.46 ? 43  LYS F CA  1 
ATOM   10711 C C   . LYS F 2 43  ? -26.588 -14.382 24.696  1.00 46.04 ? 43  LYS F C   1 
ATOM   10712 O O   . LYS F 2 43  ? -25.866 -13.396 24.535  1.00 46.03 ? 43  LYS F O   1 
ATOM   10713 C CB  . LYS F 2 43  ? -25.526 -16.634 25.048  1.00 46.65 ? 43  LYS F CB  1 
ATOM   10714 C CG  . LYS F 2 43  ? -24.037 -16.473 24.791  1.00 47.39 ? 43  LYS F CG  1 
ATOM   10715 C CD  . LYS F 2 43  ? -23.440 -17.819 24.361  1.00 49.25 ? 43  LYS F CD  1 
ATOM   10716 C CE  . LYS F 2 43  ? -21.991 -17.702 23.886  1.00 50.24 ? 43  LYS F CE  1 
ATOM   10717 N NZ  . LYS F 2 43  ? -21.034 -17.454 25.008  1.00 50.77 ? 43  LYS F NZ  1 
ATOM   10718 N N   . ALA F 2 44  ? -27.723 -14.575 24.022  1.00 45.46 ? 44  ALA F N   1 
ATOM   10719 C CA  . ALA F 2 44  ? -28.213 -13.654 22.997  1.00 44.90 ? 44  ALA F CA  1 
ATOM   10720 C C   . ALA F 2 44  ? -28.879 -12.406 23.578  1.00 44.57 ? 44  ALA F C   1 
ATOM   10721 O O   . ALA F 2 44  ? -28.708 -11.305 23.046  1.00 44.43 ? 44  ALA F O   1 
ATOM   10722 C CB  . ALA F 2 44  ? -29.170 -14.372 22.059  1.00 44.90 ? 44  ALA F CB  1 
ATOM   10723 N N   . ILE F 2 45  ? -29.641 -12.582 24.657  1.00 44.13 ? 45  ILE F N   1 
ATOM   10724 C CA  . ILE F 2 45  ? -30.303 -11.464 25.335  1.00 43.91 ? 45  ILE F CA  1 
ATOM   10725 C C   . ILE F 2 45  ? -29.260 -10.487 25.883  1.00 43.71 ? 45  ILE F C   1 
ATOM   10726 O O   . ILE F 2 45  ? -29.413 -9.268  25.763  1.00 43.70 ? 45  ILE F O   1 
ATOM   10727 C CB  . ILE F 2 45  ? -31.267 -11.947 26.463  1.00 43.98 ? 45  ILE F CB  1 
ATOM   10728 C CG1 . ILE F 2 45  ? -32.517 -12.597 25.856  1.00 43.88 ? 45  ILE F CG1 1 
ATOM   10729 C CG2 . ILE F 2 45  ? -31.678 -10.783 27.370  1.00 43.85 ? 45  ILE F CG2 1 
ATOM   10730 C CD1 . ILE F 2 45  ? -33.319 -13.456 26.824  1.00 44.13 ? 45  ILE F CD1 1 
ATOM   10731 N N   . ASP F 2 46  ? -28.192 -11.034 26.456  1.00 43.27 ? 46  ASP F N   1 
ATOM   10732 C CA  . ASP F 2 46  ? -27.112 -10.224 27.002  1.00 43.04 ? 46  ASP F CA  1 
ATOM   10733 C C   . ASP F 2 46  ? -26.373 -9.452  25.916  1.00 42.67 ? 46  ASP F C   1 
ATOM   10734 O O   . ASP F 2 46  ? -26.005 -8.298  26.122  1.00 42.76 ? 46  ASP F O   1 
ATOM   10735 C CB  . ASP F 2 46  ? -26.142 -11.093 27.809  1.00 43.11 ? 46  ASP F CB  1 
ATOM   10736 C CG  . ASP F 2 46  ? -26.789 -11.692 29.049  1.00 43.34 ? 46  ASP F CG  1 
ATOM   10737 O OD1 . ASP F 2 46  ? -27.733 -11.077 29.597  1.00 42.83 ? 46  ASP F OD1 1 
ATOM   10738 O OD2 . ASP F 2 46  ? -26.351 -12.781 29.477  1.00 44.15 ? 46  ASP F OD2 1 
ATOM   10739 N N   . GLY F 2 47  ? -26.165 -10.091 24.767  1.00 42.23 ? 47  GLY F N   1 
ATOM   10740 C CA  . GLY F 2 47  ? -25.516 -9.452  23.625  1.00 41.74 ? 47  GLY F CA  1 
ATOM   10741 C C   . GLY F 2 47  ? -26.340 -8.308  23.055  1.00 41.45 ? 47  GLY F C   1 
ATOM   10742 O O   . GLY F 2 47  ? -25.812 -7.231  22.772  1.00 41.35 ? 47  GLY F O   1 
ATOM   10743 N N   . VAL F 2 48  ? -27.638 -8.550  22.898  1.00 40.99 ? 48  VAL F N   1 
ATOM   10744 C CA  . VAL F 2 48  ? -28.566 -7.549  22.382  1.00 40.71 ? 48  VAL F CA  1 
ATOM   10745 C C   . VAL F 2 48  ? -28.749 -6.377  23.362  1.00 40.35 ? 48  VAL F C   1 
ATOM   10746 O O   . VAL F 2 48  ? -28.703 -5.219  22.946  1.00 40.30 ? 48  VAL F O   1 
ATOM   10747 C CB  . VAL F 2 48  ? -29.928 -8.189  21.978  1.00 40.77 ? 48  VAL F CB  1 
ATOM   10748 C CG1 . VAL F 2 48  ? -30.958 -7.131  21.661  1.00 40.94 ? 48  VAL F CG1 1 
ATOM   10749 C CG2 . VAL F 2 48  ? -29.752 -9.106  20.767  1.00 40.80 ? 48  VAL F CG2 1 
ATOM   10750 N N   . THR F 2 49  ? -28.940 -6.676  24.648  1.00 39.93 ? 49  THR F N   1 
ATOM   10751 C CA  . THR F 2 49  ? -29.060 -5.638  25.677  1.00 39.52 ? 49  THR F CA  1 
ATOM   10752 C C   . THR F 2 49  ? -27.840 -4.716  25.664  1.00 39.52 ? 49  THR F C   1 
ATOM   10753 O O   . THR F 2 49  ? -27.982 -3.491  25.614  1.00 39.44 ? 49  THR F O   1 
ATOM   10754 C CB  . THR F 2 49  ? -29.256 -6.238  27.090  1.00 39.62 ? 49  THR F CB  1 
ATOM   10755 O OG1 . THR F 2 49  ? -30.406 -7.092  27.094  1.00 39.47 ? 49  THR F OG1 1 
ATOM   10756 C CG2 . THR F 2 49  ? -29.447 -5.139  28.143  1.00 39.15 ? 49  THR F CG2 1 
ATOM   10757 N N   . ASN F 2 50  ? -26.650 -5.311  25.688  1.00 39.42 ? 50  ASN F N   1 
ATOM   10758 C CA  . ASN F 2 50  ? -25.401 -4.557  25.627  1.00 39.48 ? 50  ASN F CA  1 
ATOM   10759 C C   . ASN F 2 50  ? -25.244 -3.724  24.352  1.00 39.49 ? 50  ASN F C   1 
ATOM   10760 O O   . ASN F 2 50  ? -24.761 -2.594  24.412  1.00 39.62 ? 50  ASN F O   1 
ATOM   10761 C CB  . ASN F 2 50  ? -24.197 -5.485  25.818  1.00 39.55 ? 50  ASN F CB  1 
ATOM   10762 C CG  . ASN F 2 50  ? -24.188 -6.168  27.184  1.00 40.03 ? 50  ASN F CG  1 
ATOM   10763 O OD1 . ASN F 2 50  ? -24.761 -5.668  28.159  1.00 40.65 ? 50  ASN F OD1 1 
ATOM   10764 N ND2 . ASN F 2 50  ? -23.537 -7.321  27.255  1.00 39.61 ? 50  ASN F ND2 1 
ATOM   10765 N N   . LYS F 2 51  ? -25.653 -4.280  23.209  1.00 39.36 ? 51  LYS F N   1 
ATOM   10766 C CA  . LYS F 2 51  ? -25.628 -3.552  21.940  1.00 39.15 ? 51  LYS F CA  1 
ATOM   10767 C C   . LYS F 2 51  ? -26.520 -2.305  21.978  1.00 39.34 ? 51  LYS F C   1 
ATOM   10768 O O   . LYS F 2 51  ? -26.104 -1.228  21.539  1.00 39.24 ? 51  LYS F O   1 
ATOM   10769 C CB  . LYS F 2 51  ? -26.006 -4.468  20.768  1.00 39.09 ? 51  LYS F CB  1 
ATOM   10770 C CG  . LYS F 2 51  ? -26.620 -3.742  19.566  1.00 38.47 ? 51  LYS F CG  1 
ATOM   10771 C CD  . LYS F 2 51  ? -26.088 -4.239  18.241  1.00 37.47 ? 51  LYS F CD  1 
ATOM   10772 C CE  . LYS F 2 51  ? -26.469 -5.678  17.959  1.00 37.03 ? 51  LYS F CE  1 
ATOM   10773 N NZ  . LYS F 2 51  ? -26.175 -6.044  16.555  1.00 35.38 ? 51  LYS F NZ  1 
ATOM   10774 N N   . VAL F 2 52  ? -27.733 -2.461  22.510  1.00 39.42 ? 52  VAL F N   1 
ATOM   10775 C CA  . VAL F 2 52  ? -28.671 -1.351  22.664  1.00 39.56 ? 52  VAL F CA  1 
ATOM   10776 C C   . VAL F 2 52  ? -28.064 -0.263  23.553  1.00 39.89 ? 52  VAL F C   1 
ATOM   10777 O O   . VAL F 2 52  ? -28.083 0.918   23.195  1.00 39.89 ? 52  VAL F O   1 
ATOM   10778 C CB  . VAL F 2 52  ? -30.042 -1.820  23.232  1.00 39.50 ? 52  VAL F CB  1 
ATOM   10779 C CG1 . VAL F 2 52  ? -30.956 -0.631  23.518  1.00 39.35 ? 52  VAL F CG1 1 
ATOM   10780 C CG2 . VAL F 2 52  ? -30.725 -2.784  22.269  1.00 39.32 ? 52  VAL F CG2 1 
ATOM   10781 N N   . ASN F 2 53  ? -27.508 -0.671  24.694  1.00 40.26 ? 53  ASN F N   1 
ATOM   10782 C CA  . ASN F 2 53  ? -26.886 0.262   25.635  1.00 40.68 ? 53  ASN F CA  1 
ATOM   10783 C C   . ASN F 2 53  ? -25.714 1.039   25.041  1.00 40.91 ? 53  ASN F C   1 
ATOM   10784 O O   . ASN F 2 53  ? -25.636 2.253   25.208  1.00 40.83 ? 53  ASN F O   1 
ATOM   10785 C CB  . ASN F 2 53  ? -26.452 -0.452  26.921  1.00 40.77 ? 53  ASN F CB  1 
ATOM   10786 C CG  . ASN F 2 53  ? -27.627 -0.912  27.764  1.00 40.96 ? 53  ASN F CG  1 
ATOM   10787 O OD1 . ASN F 2 53  ? -28.713 -0.336  27.708  1.00 41.43 ? 53  ASN F OD1 1 
ATOM   10788 N ND2 . ASN F 2 53  ? -27.412 -1.958  28.555  1.00 41.10 ? 53  ASN F ND2 1 
ATOM   10789 N N   . SER F 2 54  ? -24.816 0.348   24.339  1.00 41.38 ? 54  SER F N   1 
ATOM   10790 C CA  . SER F 2 54  ? -23.655 1.016   23.733  1.00 41.98 ? 54  SER F CA  1 
ATOM   10791 C C   . SER F 2 54  ? -24.019 1.979   22.602  1.00 42.32 ? 54  SER F C   1 
ATOM   10792 O O   . SER F 2 54  ? -23.309 2.957   22.379  1.00 42.71 ? 54  SER F O   1 
ATOM   10793 C CB  . SER F 2 54  ? -22.567 0.025   23.297  1.00 41.88 ? 54  SER F CB  1 
ATOM   10794 O OG  . SER F 2 54  ? -23.014 -1.310  23.377  1.00 42.22 ? 54  SER F OG  1 
ATOM   10795 N N   . ILE F 2 55  ? -25.120 1.705   21.905  1.00 42.82 ? 55  ILE F N   1 
ATOM   10796 C CA  . ILE F 2 55  ? -25.666 2.639   20.919  1.00 43.22 ? 55  ILE F CA  1 
ATOM   10797 C C   . ILE F 2 55  ? -26.133 3.919   21.610  1.00 43.80 ? 55  ILE F C   1 
ATOM   10798 O O   . ILE F 2 55  ? -25.755 5.018   21.203  1.00 43.93 ? 55  ILE F O   1 
ATOM   10799 C CB  . ILE F 2 55  ? -26.816 2.012   20.090  1.00 43.20 ? 55  ILE F CB  1 
ATOM   10800 C CG1 . ILE F 2 55  ? -26.249 1.015   19.071  1.00 42.86 ? 55  ILE F CG1 1 
ATOM   10801 C CG2 . ILE F 2 55  ? -27.634 3.098   19.383  1.00 42.86 ? 55  ILE F CG2 1 
ATOM   10802 C CD1 . ILE F 2 55  ? -27.296 0.229   18.305  1.00 42.38 ? 55  ILE F CD1 1 
ATOM   10803 N N   . ILE F 2 56  ? -26.936 3.764   22.663  1.00 44.42 ? 56  ILE F N   1 
ATOM   10804 C CA  . ILE F 2 56  ? -27.418 4.892   23.467  1.00 45.06 ? 56  ILE F CA  1 
ATOM   10805 C C   . ILE F 2 56  ? -26.258 5.683   24.097  1.00 45.70 ? 56  ILE F C   1 
ATOM   10806 O O   . ILE F 2 56  ? -26.245 6.918   24.042  1.00 45.76 ? 56  ILE F O   1 
ATOM   10807 C CB  . ILE F 2 56  ? -28.425 4.420   24.553  1.00 45.03 ? 56  ILE F CB  1 
ATOM   10808 C CG1 . ILE F 2 56  ? -29.713 3.908   23.893  1.00 45.29 ? 56  ILE F CG1 1 
ATOM   10809 C CG2 . ILE F 2 56  ? -28.721 5.542   25.561  1.00 44.74 ? 56  ILE F CG2 1 
ATOM   10810 C CD1 . ILE F 2 56  ? -30.648 3.136   24.825  1.00 45.48 ? 56  ILE F CD1 1 
ATOM   10811 N N   . ASP F 2 57  ? -25.289 4.965   24.669  1.00 46.35 ? 57  ASP F N   1 
ATOM   10812 C CA  . ASP F 2 57  ? -24.127 5.577   25.335  1.00 47.05 ? 57  ASP F CA  1 
ATOM   10813 C C   . ASP F 2 57  ? -23.221 6.366   24.389  1.00 47.12 ? 57  ASP F C   1 
ATOM   10814 O O   . ASP F 2 57  ? -22.614 7.354   24.799  1.00 46.97 ? 57  ASP F O   1 
ATOM   10815 C CB  . ASP F 2 57  ? -23.287 4.518   26.070  1.00 47.18 ? 57  ASP F CB  1 
ATOM   10816 C CG  . ASP F 2 57  ? -24.065 3.794   27.162  1.00 48.35 ? 57  ASP F CG  1 
ATOM   10817 O OD1 . ASP F 2 57  ? -23.574 2.740   27.630  1.00 49.52 ? 57  ASP F OD1 1 
ATOM   10818 O OD2 . ASP F 2 57  ? -25.168 4.260   27.543  1.00 49.33 ? 57  ASP F OD2 1 
ATOM   10819 N N   . LYS F 2 58  ? -23.124 5.921   23.136  1.00 47.34 ? 58  LYS F N   1 
ATOM   10820 C CA  . LYS F 2 58  ? -22.259 6.571   22.146  1.00 47.69 ? 58  LYS F CA  1 
ATOM   10821 C C   . LYS F 2 58  ? -22.809 7.902   21.628  1.00 47.72 ? 58  LYS F C   1 
ATOM   10822 O O   . LYS F 2 58  ? -22.072 8.697   21.045  1.00 47.85 ? 58  LYS F O   1 
ATOM   10823 C CB  . LYS F 2 58  ? -21.939 5.618   20.987  1.00 47.75 ? 58  LYS F CB  1 
ATOM   10824 C CG  . LYS F 2 58  ? -20.503 5.078   20.993  1.00 48.70 ? 58  LYS F CG  1 
ATOM   10825 C CD  . LYS F 2 58  ? -20.118 4.431   22.329  1.00 50.07 ? 58  LYS F CD  1 
ATOM   10826 C CE  . LYS F 2 58  ? -18.603 4.361   22.489  1.00 50.72 ? 58  LYS F CE  1 
ATOM   10827 N NZ  . LYS F 2 58  ? -18.197 3.977   23.876  1.00 50.79 ? 58  LYS F NZ  1 
ATOM   10828 N N   . MET F 2 59  ? -24.098 8.135   21.858  1.00 47.75 ? 59  MET F N   1 
ATOM   10829 C CA  . MET F 2 59  ? -24.768 9.369   21.453  1.00 47.74 ? 59  MET F CA  1 
ATOM   10830 C C   . MET F 2 59  ? -24.868 10.365  22.606  1.00 47.69 ? 59  MET F C   1 
ATOM   10831 O O   . MET F 2 59  ? -25.340 11.487  22.426  1.00 47.83 ? 59  MET F O   1 
ATOM   10832 C CB  . MET F 2 59  ? -26.165 9.052   20.915  1.00 47.77 ? 59  MET F CB  1 
ATOM   10833 C CG  . MET F 2 59  ? -26.173 8.021   19.808  1.00 47.62 ? 59  MET F CG  1 
ATOM   10834 S SD  . MET F 2 59  ? -25.478 8.661   18.286  1.00 47.75 ? 59  MET F SD  1 
ATOM   10835 C CE  . MET F 2 59  ? -25.476 7.184   17.278  1.00 47.37 ? 59  MET F CE  1 
ATOM   10836 N N   . ASN F 2 60  ? -24.407 9.944   23.780  1.00 47.71 ? 60  ASN F N   1 
ATOM   10837 C CA  . ASN F 2 60  ? -24.450 10.732  25.020  1.00 47.79 ? 60  ASN F CA  1 
ATOM   10838 C C   . ASN F 2 60  ? -23.807 12.130  24.925  1.00 47.58 ? 60  ASN F C   1 
ATOM   10839 O O   . ASN F 2 60  ? -24.143 13.035  25.697  1.00 47.58 ? 60  ASN F O   1 
ATOM   10840 C CB  . ASN F 2 60  ? -23.862 9.878   26.162  1.00 47.94 ? 60  ASN F CB  1 
ATOM   10841 C CG  . ASN F 2 60  ? -23.337 10.695  27.325  1.00 48.92 ? 60  ASN F CG  1 
ATOM   10842 O OD1 . ASN F 2 60  ? -24.098 11.343  28.047  1.00 50.08 ? 60  ASN F OD1 1 
ATOM   10843 N ND2 . ASN F 2 60  ? -22.022 10.644  27.532  1.00 49.45 ? 60  ASN F ND2 1 
ATOM   10844 N N   . THR F 2 61  ? -22.911 12.308  23.959  1.00 47.35 ? 61  THR F N   1 
ATOM   10845 C CA  . THR F 2 61  ? -22.224 13.582  23.764  1.00 47.16 ? 61  THR F CA  1 
ATOM   10846 C C   . THR F 2 61  ? -22.510 14.189  22.389  1.00 47.11 ? 61  THR F C   1 
ATOM   10847 O O   . THR F 2 61  ? -21.628 14.805  21.776  1.00 47.24 ? 61  THR F O   1 
ATOM   10848 C CB  . THR F 2 61  ? -20.696 13.430  23.934  1.00 47.14 ? 61  THR F CB  1 
ATOM   10849 O OG1 . THR F 2 61  ? -20.236 12.329  23.137  1.00 46.83 ? 61  THR F OG1 1 
ATOM   10850 C CG2 . THR F 2 61  ? -20.327 13.199  25.399  1.00 47.27 ? 61  THR F CG2 1 
ATOM   10851 N N   . GLN F 2 62  ? -23.737 14.029  21.902  1.00 46.78 ? 62  GLN F N   1 
ATOM   10852 C CA  . GLN F 2 62  ? -24.083 14.594  20.599  1.00 46.66 ? 62  GLN F CA  1 
ATOM   10853 C C   . GLN F 2 62  ? -24.401 16.094  20.696  1.00 46.34 ? 62  GLN F C   1 
ATOM   10854 O O   . GLN F 2 62  ? -24.570 16.628  21.798  1.00 46.42 ? 62  GLN F O   1 
ATOM   10855 C CB  . GLN F 2 62  ? -25.169 13.765  19.889  1.00 46.75 ? 62  GLN F CB  1 
ATOM   10856 C CG  . GLN F 2 62  ? -26.594 14.301  19.871  1.00 47.13 ? 62  GLN F CG  1 
ATOM   10857 C CD  . GLN F 2 62  ? -27.507 13.450  18.987  1.00 48.01 ? 62  GLN F CD  1 
ATOM   10858 O OE1 . GLN F 2 62  ? -27.142 12.345  18.573  1.00 48.30 ? 62  GLN F OE1 1 
ATOM   10859 N NE2 . GLN F 2 62  ? -28.696 13.963  18.696  1.00 47.59 ? 62  GLN F NE2 1 
ATOM   10860 N N   . PHE F 2 63  ? -24.444 16.766  19.546  1.00 45.77 ? 63  PHE F N   1 
ATOM   10861 C CA  . PHE F 2 63  ? -24.595 18.220  19.495  1.00 45.11 ? 63  PHE F CA  1 
ATOM   10862 C C   . PHE F 2 63  ? -25.900 18.709  20.100  1.00 45.04 ? 63  PHE F C   1 
ATOM   10863 O O   . PHE F 2 63  ? -26.966 18.146  19.848  1.00 44.94 ? 63  PHE F O   1 
ATOM   10864 C CB  . PHE F 2 63  ? -24.460 18.732  18.059  1.00 44.93 ? 63  PHE F CB  1 
ATOM   10865 C CG  . PHE F 2 63  ? -24.331 20.225  17.957  1.00 43.92 ? 63  PHE F CG  1 
ATOM   10866 C CD1 . PHE F 2 63  ? -23.124 20.854  18.251  1.00 43.34 ? 63  PHE F CD1 1 
ATOM   10867 C CD2 . PHE F 2 63  ? -25.414 21.005  17.562  1.00 43.44 ? 63  PHE F CD2 1 
ATOM   10868 C CE1 . PHE F 2 63  ? -22.998 22.240  18.163  1.00 42.85 ? 63  PHE F CE1 1 
ATOM   10869 C CE2 . PHE F 2 63  ? -25.298 22.391  17.467  1.00 43.30 ? 63  PHE F CE2 1 
ATOM   10870 C CZ  . PHE F 2 63  ? -24.086 23.010  17.768  1.00 42.93 ? 63  PHE F CZ  1 
ATOM   10871 N N   . GLU F 2 64  ? -25.792 19.768  20.897  1.00 44.98 ? 64  GLU F N   1 
ATOM   10872 C CA  . GLU F 2 64  ? -26.941 20.407  21.527  1.00 44.86 ? 64  GLU F CA  1 
ATOM   10873 C C   . GLU F 2 64  ? -27.037 21.864  21.077  1.00 44.37 ? 64  GLU F C   1 
ATOM   10874 O O   . GLU F 2 64  ? -26.173 22.689  21.394  1.00 44.42 ? 64  GLU F O   1 
ATOM   10875 C CB  . GLU F 2 64  ? -26.845 20.286  23.051  1.00 45.09 ? 64  GLU F CB  1 
ATOM   10876 C CG  . GLU F 2 64  ? -26.903 18.827  23.539  1.00 46.93 ? 64  GLU F CG  1 
ATOM   10877 C CD  . GLU F 2 64  ? -26.221 18.597  24.881  1.00 49.03 ? 64  GLU F CD  1 
ATOM   10878 O OE1 . GLU F 2 64  ? -26.263 19.499  25.749  1.00 50.26 ? 64  GLU F OE1 1 
ATOM   10879 O OE2 . GLU F 2 64  ? -25.647 17.500  25.069  1.00 50.34 ? 64  GLU F OE2 1 
ATOM   10880 N N   . ALA F 2 65  ? -28.089 22.162  20.321  1.00 43.81 ? 65  ALA F N   1 
ATOM   10881 C CA  . ALA F 2 65  ? -28.267 23.473  19.708  1.00 43.27 ? 65  ALA F CA  1 
ATOM   10882 C C   . ALA F 2 65  ? -28.649 24.543  20.723  1.00 43.00 ? 65  ALA F C   1 
ATOM   10883 O O   . ALA F 2 65  ? -29.471 24.308  21.610  1.00 43.15 ? 65  ALA F O   1 
ATOM   10884 C CB  . ALA F 2 65  ? -29.297 23.398  18.584  1.00 43.14 ? 65  ALA F CB  1 
ATOM   10885 N N   . VAL F 2 66  ? -28.038 25.716  20.583  1.00 42.50 ? 66  VAL F N   1 
ATOM   10886 C CA  . VAL F 2 66  ? -28.337 26.863  21.426  1.00 42.01 ? 66  VAL F CA  1 
ATOM   10887 C C   . VAL F 2 66  ? -28.830 27.994  20.535  1.00 41.93 ? 66  VAL F C   1 
ATOM   10888 O O   . VAL F 2 66  ? -28.188 28.331  19.536  1.00 41.99 ? 66  VAL F O   1 
ATOM   10889 C CB  . VAL F 2 66  ? -27.097 27.323  22.237  1.00 42.02 ? 66  VAL F CB  1 
ATOM   10890 C CG1 . VAL F 2 66  ? -27.405 28.586  23.050  1.00 41.95 ? 66  VAL F CG1 1 
ATOM   10891 C CG2 . VAL F 2 66  ? -26.622 26.217  23.154  1.00 41.50 ? 66  VAL F CG2 1 
ATOM   10892 N N   . GLY F 2 67  ? -29.981 28.562  20.898  1.00 41.79 ? 67  GLY F N   1 
ATOM   10893 C CA  . GLY F 2 67  ? -30.585 29.668  20.159  1.00 41.34 ? 67  GLY F CA  1 
ATOM   10894 C C   . GLY F 2 67  ? -29.805 30.950  20.354  1.00 41.20 ? 67  GLY F C   1 
ATOM   10895 O O   . GLY F 2 67  ? -29.540 31.361  21.483  1.00 41.54 ? 67  GLY F O   1 
ATOM   10896 N N   . ARG F 2 68  ? -29.413 31.569  19.248  1.00 40.91 ? 68  ARG F N   1 
ATOM   10897 C CA  . ARG F 2 68  ? -28.702 32.839  19.290  1.00 40.56 ? 68  ARG F CA  1 
ATOM   10898 C C   . ARG F 2 68  ? -29.445 33.868  18.453  1.00 40.19 ? 68  ARG F C   1 
ATOM   10899 O O   . ARG F 2 68  ? -30.138 33.511  17.499  1.00 40.27 ? 68  ARG F O   1 
ATOM   10900 C CB  . ARG F 2 68  ? -27.264 32.668  18.795  1.00 40.76 ? 68  ARG F CB  1 
ATOM   10901 C CG  . ARG F 2 68  ? -26.383 31.883  19.747  1.00 41.02 ? 68  ARG F CG  1 
ATOM   10902 C CD  . ARG F 2 68  ? -24.984 31.713  19.209  1.00 41.87 ? 68  ARG F CD  1 
ATOM   10903 N NE  . ARG F 2 68  ? -24.299 30.614  19.885  1.00 43.08 ? 68  ARG F NE  1 
ATOM   10904 C CZ  . ARG F 2 68  ? -24.302 29.347  19.468  1.00 44.07 ? 68  ARG F CZ  1 
ATOM   10905 N NH1 . ARG F 2 68  ? -24.947 28.989  18.363  1.00 43.75 ? 68  ARG F NH1 1 
ATOM   10906 N NH2 . ARG F 2 68  ? -23.654 28.427  20.163  1.00 44.68 ? 68  ARG F NH2 1 
ATOM   10907 N N   . GLU F 2 69  ? -29.308 35.141  18.816  1.00 39.60 ? 69  GLU F N   1 
ATOM   10908 C CA  . GLU F 2 69  ? -29.977 36.218  18.090  1.00 39.07 ? 69  GLU F CA  1 
ATOM   10909 C C   . GLU F 2 69  ? -29.008 37.238  17.510  1.00 37.96 ? 69  GLU F C   1 
ATOM   10910 O O   . GLU F 2 69  ? -28.000 37.582  18.134  1.00 37.88 ? 69  GLU F O   1 
ATOM   10911 C CB  . GLU F 2 69  ? -31.024 36.900  18.972  1.00 39.60 ? 69  GLU F CB  1 
ATOM   10912 C CG  . GLU F 2 69  ? -32.391 36.213  18.935  1.00 42.33 ? 69  GLU F CG  1 
ATOM   10913 C CD  . GLU F 2 69  ? -33.355 36.739  19.993  1.00 45.83 ? 69  GLU F CD  1 
ATOM   10914 O OE1 . GLU F 2 69  ? -32.900 37.024  21.128  1.00 47.24 ? 69  GLU F OE1 1 
ATOM   10915 O OE2 . GLU F 2 69  ? -34.569 36.858  19.692  1.00 46.59 ? 69  GLU F OE2 1 
ATOM   10916 N N   . PHE F 2 70  ? -29.335 37.710  16.308  1.00 36.83 ? 70  PHE F N   1 
ATOM   10917 C CA  . PHE F 2 70  ? -28.516 38.668  15.564  1.00 35.65 ? 70  PHE F CA  1 
ATOM   10918 C C   . PHE F 2 70  ? -29.388 39.776  14.961  1.00 35.39 ? 70  PHE F C   1 
ATOM   10919 O O   . PHE F 2 70  ? -30.563 39.552  14.656  1.00 35.12 ? 70  PHE F O   1 
ATOM   10920 C CB  . PHE F 2 70  ? -27.752 37.946  14.450  1.00 35.23 ? 70  PHE F CB  1 
ATOM   10921 C CG  . PHE F 2 70  ? -26.944 36.775  14.924  1.00 33.94 ? 70  PHE F CG  1 
ATOM   10922 C CD1 . PHE F 2 70  ? -25.652 36.953  15.408  1.00 33.33 ? 70  PHE F CD1 1 
ATOM   10923 C CD2 . PHE F 2 70  ? -27.474 35.486  14.890  1.00 33.56 ? 70  PHE F CD2 1 
ATOM   10924 C CE1 . PHE F 2 70  ? -24.898 35.868  15.856  1.00 32.56 ? 70  PHE F CE1 1 
ATOM   10925 C CE2 . PHE F 2 70  ? -26.727 34.394  15.330  1.00 32.50 ? 70  PHE F CE2 1 
ATOM   10926 C CZ  . PHE F 2 70  ? -25.438 34.587  15.813  1.00 32.37 ? 70  PHE F CZ  1 
ATOM   10927 N N   . ASN F 2 71  ? -28.823 40.971  14.790  1.00 34.94 ? 71  ASN F N   1 
ATOM   10928 C CA  . ASN F 2 71  ? -29.578 42.069  14.181  1.00 34.60 ? 71  ASN F CA  1 
ATOM   10929 C C   . ASN F 2 71  ? -29.453 42.082  12.654  1.00 34.32 ? 71  ASN F C   1 
ATOM   10930 O O   . ASN F 2 71  ? -28.806 41.204  12.080  1.00 34.39 ? 71  ASN F O   1 
ATOM   10931 C CB  . ASN F 2 71  ? -29.245 43.429  14.819  1.00 34.40 ? 71  ASN F CB  1 
ATOM   10932 C CG  . ASN F 2 71  ? -27.781 43.793  14.711  1.00 34.72 ? 71  ASN F CG  1 
ATOM   10933 O OD1 . ASN F 2 71  ? -27.254 43.990  13.620  1.00 34.39 ? 71  ASN F OD1 1 
ATOM   10934 N ND2 . ASN F 2 71  ? -27.118 43.910  15.858  1.00 35.48 ? 71  ASN F ND2 1 
ATOM   10935 N N   . ASN F 2 72  ? -30.078 43.066  12.005  1.00 33.77 ? 72  ASN F N   1 
ATOM   10936 C CA  . ASN F 2 72  ? -30.096 43.148  10.542  1.00 33.35 ? 72  ASN F CA  1 
ATOM   10937 C C   . ASN F 2 72  ? -28.743 43.502  9.906   1.00 32.81 ? 72  ASN F C   1 
ATOM   10938 O O   . ASN F 2 72  ? -28.605 43.494  8.679   1.00 32.95 ? 72  ASN F O   1 
ATOM   10939 C CB  . ASN F 2 72  ? -31.209 44.094  10.058  1.00 33.50 ? 72  ASN F CB  1 
ATOM   10940 C CG  . ASN F 2 72  ? -30.925 45.558  10.376  1.00 34.41 ? 72  ASN F CG  1 
ATOM   10941 O OD1 . ASN F 2 72  ? -30.729 45.938  11.533  1.00 35.46 ? 72  ASN F OD1 1 
ATOM   10942 N ND2 . ASN F 2 72  ? -30.905 46.388  9.341   1.00 35.47 ? 72  ASN F ND2 1 
ATOM   10943 N N   . LEU F 2 73  ? -27.755 43.815  10.743  1.00 32.00 ? 73  LEU F N   1 
ATOM   10944 C CA  . LEU F 2 73  ? -26.398 44.113  10.284  1.00 31.33 ? 73  LEU F CA  1 
ATOM   10945 C C   . LEU F 2 73  ? -25.454 42.924  10.482  1.00 30.58 ? 73  LEU F C   1 
ATOM   10946 O O   . LEU F 2 73  ? -24.250 43.049  10.263  1.00 30.25 ? 73  LEU F O   1 
ATOM   10947 C CB  . LEU F 2 73  ? -25.830 45.340  11.017  1.00 31.49 ? 73  LEU F CB  1 
ATOM   10948 C CG  . LEU F 2 73  ? -26.637 46.650  11.094  1.00 32.56 ? 73  LEU F CG  1 
ATOM   10949 C CD1 . LEU F 2 73  ? -26.157 47.526  12.269  1.00 31.56 ? 73  LEU F CD1 1 
ATOM   10950 C CD2 . LEU F 2 73  ? -26.633 47.429  9.762   1.00 31.87 ? 73  LEU F CD2 1 
ATOM   10951 N N   . GLU F 2 74  ? -26.001 41.784  10.899  1.00 29.99 ? 74  GLU F N   1 
ATOM   10952 C CA  . GLU F 2 74  ? -25.201 40.589  11.208  1.00 29.91 ? 74  GLU F CA  1 
ATOM   10953 C C   . GLU F 2 74  ? -25.736 39.336  10.500  1.00 29.96 ? 74  GLU F C   1 
ATOM   10954 O O   . GLU F 2 74  ? -25.799 38.256  11.086  1.00 29.88 ? 74  GLU F O   1 
ATOM   10955 C CB  . GLU F 2 74  ? -25.121 40.362  12.727  1.00 29.81 ? 74  GLU F CB  1 
ATOM   10956 C CG  . GLU F 2 74  ? -24.385 41.463  13.516  1.00 29.61 ? 74  GLU F CG  1 
ATOM   10957 C CD  . GLU F 2 74  ? -24.539 41.322  15.033  1.00 30.44 ? 74  GLU F CD  1 
ATOM   10958 O OE1 . GLU F 2 74  ? -25.614 40.872  15.500  1.00 30.31 ? 74  GLU F OE1 1 
ATOM   10959 O OE2 . GLU F 2 74  ? -23.578 41.665  15.763  1.00 29.89 ? 74  GLU F OE2 1 
ATOM   10960 N N   . ARG F 2 75  ? -26.108 39.505  9.232   1.00 30.11 ? 75  ARG F N   1 
ATOM   10961 C CA  . ARG F 2 75  ? -26.671 38.447  8.399   1.00 30.34 ? 75  ARG F CA  1 
ATOM   10962 C C   . ARG F 2 75  ? -25.680 37.351  8.029   1.00 29.82 ? 75  ARG F C   1 
ATOM   10963 O O   . ARG F 2 75  ? -26.059 36.184  7.970   1.00 29.90 ? 75  ARG F O   1 
ATOM   10964 C CB  . ARG F 2 75  ? -27.291 39.042  7.130   1.00 30.75 ? 75  ARG F CB  1 
ATOM   10965 C CG  . ARG F 2 75  ? -28.819 39.049  7.115   1.00 33.62 ? 75  ARG F CG  1 
ATOM   10966 C CD  . ARG F 2 75  ? -29.434 40.054  8.085   1.00 37.76 ? 75  ARG F CD  1 
ATOM   10967 N NE  . ARG F 2 75  ? -30.831 39.718  8.370   1.00 41.29 ? 75  ARG F NE  1 
ATOM   10968 C CZ  . ARG F 2 75  ? -31.877 40.167  7.673   1.00 43.62 ? 75  ARG F CZ  1 
ATOM   10969 N NH1 . ARG F 2 75  ? -31.703 40.989  6.640   1.00 44.12 ? 75  ARG F NH1 1 
ATOM   10970 N NH2 . ARG F 2 75  ? -33.106 39.796  8.013   1.00 44.57 ? 75  ARG F NH2 1 
ATOM   10971 N N   . ARG F 2 76  ? -24.428 37.729  7.772   1.00 29.36 ? 76  ARG F N   1 
ATOM   10972 C CA  . ARG F 2 76  ? -23.352 36.770  7.506   1.00 28.99 ? 76  ARG F CA  1 
ATOM   10973 C C   . ARG F 2 76  ? -23.168 35.797  8.670   1.00 29.17 ? 76  ARG F C   1 
ATOM   10974 O O   . ARG F 2 76  ? -23.110 34.581  8.467   1.00 28.99 ? 76  ARG F O   1 
ATOM   10975 C CB  . ARG F 2 76  ? -22.029 37.490  7.239   1.00 28.75 ? 76  ARG F CB  1 
ATOM   10976 C CG  . ARG F 2 76  ? -21.926 38.172  5.881   1.00 27.83 ? 76  ARG F CG  1 
ATOM   10977 C CD  . ARG F 2 76  ? -20.660 38.994  5.791   1.00 25.48 ? 76  ARG F CD  1 
ATOM   10978 N NE  . ARG F 2 76  ? -20.641 40.046  6.808   1.00 24.46 ? 76  ARG F NE  1 
ATOM   10979 C CZ  . ARG F 2 76  ? -19.544 40.487  7.414   1.00 22.93 ? 76  ARG F CZ  1 
ATOM   10980 N NH1 . ARG F 2 76  ? -18.358 39.977  7.115   1.00 23.16 ? 76  ARG F NH1 1 
ATOM   10981 N NH2 . ARG F 2 76  ? -19.634 41.442  8.323   1.00 22.37 ? 76  ARG F NH2 1 
ATOM   10982 N N   . ILE F 2 77  ? -23.085 36.341  9.883   1.00 29.33 ? 77  ILE F N   1 
ATOM   10983 C CA  . ILE F 2 77  ? -22.889 35.530  11.084  1.00 29.78 ? 77  ILE F CA  1 
ATOM   10984 C C   . ILE F 2 77  ? -24.153 34.749  11.467  1.00 29.87 ? 77  ILE F C   1 
ATOM   10985 O O   . ILE F 2 77  ? -24.056 33.617  11.937  1.00 29.91 ? 77  ILE F O   1 
ATOM   10986 C CB  . ILE F 2 77  ? -22.359 36.368  12.278  1.00 29.82 ? 77  ILE F CB  1 
ATOM   10987 C CG1 . ILE F 2 77  ? -20.961 36.904  11.965  1.00 30.69 ? 77  ILE F CG1 1 
ATOM   10988 C CG2 . ILE F 2 77  ? -22.275 35.519  13.533  1.00 29.87 ? 77  ILE F CG2 1 
ATOM   10989 C CD1 . ILE F 2 77  ? -20.450 37.949  12.963  1.00 32.53 ? 77  ILE F CD1 1 
ATOM   10990 N N   . GLU F 2 78  ? -25.326 35.348  11.258  1.00 29.97 ? 78  GLU F N   1 
ATOM   10991 C CA  . GLU F 2 78  ? -26.589 34.648  11.459  1.00 30.17 ? 78  GLU F CA  1 
ATOM   10992 C C   . GLU F 2 78  ? -26.674 33.444  10.529  1.00 29.90 ? 78  GLU F C   1 
ATOM   10993 O O   . GLU F 2 78  ? -27.109 32.366  10.936  1.00 30.17 ? 78  GLU F O   1 
ATOM   10994 C CB  . GLU F 2 78  ? -27.785 35.582  11.246  1.00 30.39 ? 78  GLU F CB  1 
ATOM   10995 C CG  . GLU F 2 78  ? -29.151 34.907  11.457  1.00 32.77 ? 78  GLU F CG  1 
ATOM   10996 C CD  . GLU F 2 78  ? -30.337 35.849  11.258  1.00 36.59 ? 78  GLU F CD  1 
ATOM   10997 O OE1 . GLU F 2 78  ? -30.369 36.590  10.246  1.00 38.36 ? 78  GLU F OE1 1 
ATOM   10998 O OE2 . GLU F 2 78  ? -31.253 35.839  12.115  1.00 38.08 ? 78  GLU F OE2 1 
ATOM   10999 N N   . ASN F 2 79  ? -26.247 33.633  9.284   1.00 29.60 ? 79  ASN F N   1 
ATOM   11000 C CA  . ASN F 2 79  ? -26.221 32.557  8.303   1.00 29.33 ? 79  ASN F CA  1 
ATOM   11001 C C   . ASN F 2 79  ? -25.170 31.489  8.644   1.00 29.30 ? 79  ASN F C   1 
ATOM   11002 O O   . ASN F 2 79  ? -25.412 30.293  8.484   1.00 28.95 ? 79  ASN F O   1 
ATOM   11003 C CB  . ASN F 2 79  ? -25.997 33.133  6.901   1.00 29.27 ? 79  ASN F CB  1 
ATOM   11004 C CG  . ASN F 2 79  ? -25.961 32.064  5.823   1.00 29.22 ? 79  ASN F CG  1 
ATOM   11005 O OD1 . ASN F 2 79  ? -24.908 31.796  5.243   1.00 29.79 ? 79  ASN F OD1 1 
ATOM   11006 N ND2 . ASN F 2 79  ? -27.106 31.449  5.551   1.00 27.88 ? 79  ASN F ND2 1 
ATOM   11007 N N   . LEU F 2 80  ? -24.009 31.932  9.121   1.00 29.44 ? 80  LEU F N   1 
ATOM   11008 C CA  . LEU F 2 80  ? -22.957 31.022  9.584   1.00 29.53 ? 80  LEU F CA  1 
ATOM   11009 C C   . LEU F 2 80  ? -23.461 30.164  10.751  1.00 29.49 ? 80  LEU F C   1 
ATOM   11010 O O   . LEU F 2 80  ? -23.304 28.946  10.740  1.00 29.34 ? 80  LEU F O   1 
ATOM   11011 C CB  . LEU F 2 80  ? -21.687 31.817  9.925   1.00 29.37 ? 80  LEU F CB  1 
ATOM   11012 C CG  . LEU F 2 80  ? -20.516 31.387  10.821  1.00 29.67 ? 80  LEU F CG  1 
ATOM   11013 C CD1 . LEU F 2 80  ? -20.009 29.978  10.571  1.00 29.27 ? 80  LEU F CD1 1 
ATOM   11014 C CD2 . LEU F 2 80  ? -19.379 32.396  10.655  1.00 29.36 ? 80  LEU F CD2 1 
ATOM   11015 N N   . ASN F 2 81  ? -24.101 30.808  11.724  1.00 29.74 ? 81  ASN F N   1 
ATOM   11016 C CA  . ASN F 2 81  ? -24.730 30.120  12.845  1.00 30.06 ? 81  ASN F CA  1 
ATOM   11017 C C   . ASN F 2 81  ? -25.745 29.049  12.436  1.00 30.73 ? 81  ASN F C   1 
ATOM   11018 O O   . ASN F 2 81  ? -25.742 27.952  12.991  1.00 30.82 ? 81  ASN F O   1 
ATOM   11019 C CB  . ASN F 2 81  ? -25.406 31.128  13.773  1.00 29.70 ? 81  ASN F CB  1 
ATOM   11020 C CG  . ASN F 2 81  ? -25.962 30.480  15.034  1.00 29.70 ? 81  ASN F CG  1 
ATOM   11021 O OD1 . ASN F 2 81  ? -25.212 29.937  15.851  1.00 29.18 ? 81  ASN F OD1 1 
ATOM   11022 N ND2 . ASN F 2 81  ? -27.280 30.550  15.206  1.00 28.55 ? 81  ASN F ND2 1 
ATOM   11023 N N   . LYS F 2 82  ? -26.613 29.369  11.478  1.00 31.46 ? 82  LYS F N   1 
ATOM   11024 C CA  . LYS F 2 82  ? -27.654 28.442  11.068  1.00 32.23 ? 82  LYS F CA  1 
ATOM   11025 C C   . LYS F 2 82  ? -27.101 27.228  10.340  1.00 32.55 ? 82  LYS F C   1 
ATOM   11026 O O   . LYS F 2 82  ? -27.526 26.099  10.599  1.00 32.74 ? 82  LYS F O   1 
ATOM   11027 C CB  . LYS F 2 82  ? -28.710 29.119  10.201  1.00 32.53 ? 82  LYS F CB  1 
ATOM   11028 C CG  . LYS F 2 82  ? -30.047 28.402  10.285  1.00 33.83 ? 82  LYS F CG  1 
ATOM   11029 C CD  . LYS F 2 82  ? -30.881 28.563  9.029   1.00 36.71 ? 82  LYS F CD  1 
ATOM   11030 C CE  . LYS F 2 82  ? -32.083 27.619  9.082   1.00 37.74 ? 82  LYS F CE  1 
ATOM   11031 N NZ  . LYS F 2 82  ? -33.235 28.161  8.310   1.00 39.96 ? 82  LYS F NZ  1 
ATOM   11032 N N   . LYS F 2 83  ? -26.162 27.461  9.429   1.00 32.98 ? 83  LYS F N   1 
ATOM   11033 C CA  . LYS F 2 83  ? -25.579 26.379  8.651   1.00 33.38 ? 83  LYS F CA  1 
ATOM   11034 C C   . LYS F 2 83  ? -24.709 25.468  9.509   1.00 33.55 ? 83  LYS F C   1 
ATOM   11035 O O   . LYS F 2 83  ? -24.619 24.273  9.249   1.00 33.78 ? 83  LYS F O   1 
ATOM   11036 C CB  . LYS F 2 83  ? -24.788 26.916  7.453   1.00 33.48 ? 83  LYS F CB  1 
ATOM   11037 C CG  . LYS F 2 83  ? -25.583 27.803  6.486   1.00 34.20 ? 83  LYS F CG  1 
ATOM   11038 C CD  . LYS F 2 83  ? -26.784 27.111  5.842   1.00 35.69 ? 83  LYS F CD  1 
ATOM   11039 C CE  . LYS F 2 83  ? -27.447 28.040  4.818   1.00 36.68 ? 83  LYS F CE  1 
ATOM   11040 N NZ  . LYS F 2 83  ? -28.788 27.578  4.348   1.00 37.09 ? 83  LYS F NZ  1 
ATOM   11041 N N   . MET F 2 84  ? -24.076 26.021  10.537  1.00 34.01 ? 84  MET F N   1 
ATOM   11042 C CA  . MET F 2 84  ? -23.265 25.195  11.420  1.00 34.41 ? 84  MET F CA  1 
ATOM   11043 C C   . MET F 2 84  ? -24.117 24.332  12.351  1.00 34.12 ? 84  MET F C   1 
ATOM   11044 O O   . MET F 2 84  ? -23.796 23.169  12.567  1.00 33.98 ? 84  MET F O   1 
ATOM   11045 C CB  . MET F 2 84  ? -22.226 26.018  12.186  1.00 34.81 ? 84  MET F CB  1 
ATOM   11046 C CG  . MET F 2 84  ? -22.689 26.603  13.498  1.00 37.40 ? 84  MET F CG  1 
ATOM   11047 S SD  . MET F 2 84  ? -21.590 26.057  14.818  1.00 41.63 ? 84  MET F SD  1 
ATOM   11048 C CE  . MET F 2 84  ? -22.632 26.331  16.252  1.00 40.39 ? 84  MET F CE  1 
ATOM   11049 N N   . GLU F 2 85  ? -25.209 24.889  12.873  1.00 34.16 ? 85  GLU F N   1 
ATOM   11050 C CA  . GLU F 2 85  ? -26.099 24.130  13.751  1.00 34.35 ? 85  GLU F CA  1 
ATOM   11051 C C   . GLU F 2 85  ? -26.837 23.038  12.980  1.00 34.14 ? 85  GLU F C   1 
ATOM   11052 O O   . GLU F 2 85  ? -26.856 21.889  13.412  1.00 34.30 ? 85  GLU F O   1 
ATOM   11053 C CB  . GLU F 2 85  ? -27.053 25.045  14.534  1.00 34.52 ? 85  GLU F CB  1 
ATOM   11054 C CG  . GLU F 2 85  ? -26.318 25.907  15.593  1.00 36.36 ? 85  GLU F CG  1 
ATOM   11055 C CD  . GLU F 2 85  ? -27.137 26.222  16.852  1.00 38.09 ? 85  GLU F CD  1 
ATOM   11056 O OE1 . GLU F 2 85  ? -28.371 26.439  16.756  1.00 38.93 ? 85  GLU F OE1 1 
ATOM   11057 O OE2 . GLU F 2 85  ? -26.526 26.270  17.944  1.00 38.52 ? 85  GLU F OE2 1 
ATOM   11058 N N   . ASP F 2 86  ? -27.404 23.388  11.826  1.00 33.94 ? 86  ASP F N   1 
ATOM   11059 C CA  . ASP F 2 86  ? -28.006 22.405  10.924  1.00 33.78 ? 86  ASP F CA  1 
ATOM   11060 C C   . ASP F 2 86  ? -26.981 21.361  10.491  1.00 32.99 ? 86  ASP F C   1 
ATOM   11061 O O   . ASP F 2 86  ? -27.318 20.187  10.336  1.00 32.96 ? 86  ASP F O   1 
ATOM   11062 C CB  . ASP F 2 86  ? -28.608 23.085  9.686   1.00 34.19 ? 86  ASP F CB  1 
ATOM   11063 C CG  . ASP F 2 86  ? -29.965 23.722  9.961   1.00 36.27 ? 86  ASP F CG  1 
ATOM   11064 O OD1 . ASP F 2 86  ? -30.716 23.208  10.824  1.00 38.75 ? 86  ASP F OD1 1 
ATOM   11065 O OD2 . ASP F 2 86  ? -30.289 24.741  9.305   1.00 38.66 ? 86  ASP F OD2 1 
ATOM   11066 N N   . GLY F 2 87  ? -25.738 21.805  10.301  1.00 32.03 ? 87  GLY F N   1 
ATOM   11067 C CA  . GLY F 2 87  ? -24.620 20.932  9.958   1.00 31.11 ? 87  GLY F CA  1 
ATOM   11068 C C   . GLY F 2 87  ? -24.407 19.792  10.937  1.00 30.53 ? 87  GLY F C   1 
ATOM   11069 O O   . GLY F 2 87  ? -24.361 18.629  10.537  1.00 30.44 ? 87  GLY F O   1 
ATOM   11070 N N   . PHE F 2 88  ? -24.279 20.123  12.220  1.00 29.91 ? 88  PHE F N   1 
ATOM   11071 C CA  . PHE F 2 88  ? -24.118 19.109  13.262  1.00 29.58 ? 88  PHE F CA  1 
ATOM   11072 C C   . PHE F 2 88  ? -25.379 18.258  13.418  1.00 29.48 ? 88  PHE F C   1 
ATOM   11073 O O   . PHE F 2 88  ? -25.299 17.048  13.623  1.00 29.30 ? 88  PHE F O   1 
ATOM   11074 C CB  . PHE F 2 88  ? -23.747 19.748  14.597  1.00 29.22 ? 88  PHE F CB  1 
ATOM   11075 C CG  . PHE F 2 88  ? -22.343 20.268  14.655  1.00 28.93 ? 88  PHE F CG  1 
ATOM   11076 C CD1 . PHE F 2 88  ? -21.260 19.396  14.623  1.00 28.86 ? 88  PHE F CD1 1 
ATOM   11077 C CD2 . PHE F 2 88  ? -22.101 21.630  14.765  1.00 28.03 ? 88  PHE F CD2 1 
ATOM   11078 C CE1 . PHE F 2 88  ? -19.954 19.875  14.681  1.00 28.75 ? 88  PHE F CE1 1 
ATOM   11079 C CE2 . PHE F 2 88  ? -20.801 22.121  14.829  1.00 28.54 ? 88  PHE F CE2 1 
ATOM   11080 C CZ  . PHE F 2 88  ? -19.723 21.242  14.790  1.00 28.86 ? 88  PHE F CZ  1 
ATOM   11081 N N   . LEU F 2 89  ? -26.535 18.904  13.310  1.00 29.32 ? 89  LEU F N   1 
ATOM   11082 C CA  . LEU F 2 89  ? -27.821 18.219  13.334  1.00 29.57 ? 89  LEU F CA  1 
ATOM   11083 C C   . LEU F 2 89  ? -27.964 17.160  12.234  1.00 29.52 ? 89  LEU F C   1 
ATOM   11084 O O   . LEU F 2 89  ? -28.482 16.075  12.490  1.00 29.51 ? 89  LEU F O   1 
ATOM   11085 C CB  . LEU F 2 89  ? -28.958 19.234  13.232  1.00 29.57 ? 89  LEU F CB  1 
ATOM   11086 C CG  . LEU F 2 89  ? -29.704 19.710  14.483  1.00 29.86 ? 89  LEU F CG  1 
ATOM   11087 C CD1 . LEU F 2 89  ? -28.851 19.768  15.751  1.00 30.08 ? 89  LEU F CD1 1 
ATOM   11088 C CD2 . LEU F 2 89  ? -30.362 21.060  14.194  1.00 30.28 ? 89  LEU F CD2 1 
ATOM   11089 N N   . ASP F 2 90  ? -27.510 17.475  11.021  1.00 29.39 ? 90  ASP F N   1 
ATOM   11090 C CA  . ASP F 2 90  ? -27.558 16.514  9.919   1.00 29.32 ? 90  ASP F CA  1 
ATOM   11091 C C   . ASP F 2 90  ? -26.558 15.390  10.150  1.00 29.08 ? 90  ASP F C   1 
ATOM   11092 O O   . ASP F 2 90  ? -26.868 14.217  9.909   1.00 29.14 ? 90  ASP F O   1 
ATOM   11093 C CB  . ASP F 2 90  ? -27.298 17.186  8.565   1.00 29.42 ? 90  ASP F CB  1 
ATOM   11094 C CG  . ASP F 2 90  ? -28.417 18.130  8.149   1.00 30.57 ? 90  ASP F CG  1 
ATOM   11095 O OD1 . ASP F 2 90  ? -29.552 17.983  8.643   1.00 31.13 ? 90  ASP F OD1 1 
ATOM   11096 O OD2 . ASP F 2 90  ? -28.160 19.036  7.322   1.00 33.56 ? 90  ASP F OD2 1 
ATOM   11097 N N   . VAL F 2 91  ? -25.365 15.757  10.622  1.00 28.71 ? 91  VAL F N   1 
ATOM   11098 C CA  . VAL F 2 91  ? -24.316 14.785  10.916  1.00 28.33 ? 91  VAL F CA  1 
ATOM   11099 C C   . VAL F 2 91  ? -24.815 13.749  11.924  1.00 28.17 ? 91  VAL F C   1 
ATOM   11100 O O   . VAL F 2 91  ? -24.793 12.551  11.632  1.00 28.57 ? 91  VAL F O   1 
ATOM   11101 C CB  . VAL F 2 91  ? -22.993 15.463  11.369  1.00 28.36 ? 91  VAL F CB  1 
ATOM   11102 C CG1 . VAL F 2 91  ? -22.040 14.456  12.030  1.00 28.16 ? 91  VAL F CG1 1 
ATOM   11103 C CG2 . VAL F 2 91  ? -22.304 16.128  10.178  1.00 28.11 ? 91  VAL F CG2 1 
ATOM   11104 N N   . TRP F 2 92  ? -25.302 14.206  13.076  1.00 27.51 ? 92  TRP F N   1 
ATOM   11105 C CA  . TRP F 2 92  ? -25.782 13.293  14.117  1.00 27.16 ? 92  TRP F CA  1 
ATOM   11106 C C   . TRP F 2 92  ? -27.006 12.483  13.707  1.00 27.03 ? 92  TRP F C   1 
ATOM   11107 O O   . TRP F 2 92  ? -27.136 11.328  14.107  1.00 27.19 ? 92  TRP F O   1 
ATOM   11108 C CB  . TRP F 2 92  ? -26.013 14.024  15.443  1.00 27.04 ? 92  TRP F CB  1 
ATOM   11109 C CG  . TRP F 2 92  ? -24.726 14.410  16.090  1.00 26.25 ? 92  TRP F CG  1 
ATOM   11110 C CD1 . TRP F 2 92  ? -24.160 15.649  16.112  1.00 26.08 ? 92  TRP F CD1 1 
ATOM   11111 C CD2 . TRP F 2 92  ? -23.822 13.542  16.780  1.00 26.20 ? 92  TRP F CD2 1 
ATOM   11112 N NE1 . TRP F 2 92  ? -22.963 15.614  16.782  1.00 26.37 ? 92  TRP F NE1 1 
ATOM   11113 C CE2 . TRP F 2 92  ? -22.731 14.331  17.206  1.00 26.39 ? 92  TRP F CE2 1 
ATOM   11114 C CE3 . TRP F 2 92  ? -23.832 12.174  17.091  1.00 25.87 ? 92  TRP F CE3 1 
ATOM   11115 C CZ2 . TRP F 2 92  ? -21.657 13.800  17.930  1.00 25.85 ? 92  TRP F CZ2 1 
ATOM   11116 C CZ3 . TRP F 2 92  ? -22.766 11.647  17.809  1.00 25.83 ? 92  TRP F CZ3 1 
ATOM   11117 C CH2 . TRP F 2 92  ? -21.692 12.461  18.220  1.00 26.02 ? 92  TRP F CH2 1 
ATOM   11118 N N   . THR F 2 93  ? -27.882 13.078  12.899  1.00 27.00 ? 93  THR F N   1 
ATOM   11119 C CA  . THR F 2 93  ? -29.003 12.356  12.287  1.00 26.75 ? 93  THR F CA  1 
ATOM   11120 C C   . THR F 2 93  ? -28.495 11.188  11.433  1.00 26.97 ? 93  THR F C   1 
ATOM   11121 O O   . THR F 2 93  ? -29.018 10.080  11.521  1.00 26.99 ? 93  THR F O   1 
ATOM   11122 C CB  . THR F 2 93  ? -29.900 13.304  11.454  1.00 26.68 ? 93  THR F CB  1 
ATOM   11123 O OG1 . THR F 2 93  ? -30.460 14.306  12.312  1.00 26.82 ? 93  THR F OG1 1 
ATOM   11124 C CG2 . THR F 2 93  ? -31.038 12.552  10.770  1.00 26.30 ? 93  THR F CG2 1 
ATOM   11125 N N   . TYR F 2 94  ? -27.464 11.442  10.632  1.00 27.17 ? 94  TYR F N   1 
ATOM   11126 C CA  . TYR F 2 94  ? -26.820 10.411  9.820   1.00 27.48 ? 94  TYR F CA  1 
ATOM   11127 C C   . TYR F 2 94  ? -26.202 9.316   10.688  1.00 27.85 ? 94  TYR F C   1 
ATOM   11128 O O   . TYR F 2 94  ? -26.397 8.135   10.417  1.00 28.05 ? 94  TYR F O   1 
ATOM   11129 C CB  . TYR F 2 94  ? -25.769 11.049  8.896   1.00 27.49 ? 94  TYR F CB  1 
ATOM   11130 C CG  . TYR F 2 94  ? -24.799 10.097  8.228   1.00 27.29 ? 94  TYR F CG  1 
ATOM   11131 C CD1 . TYR F 2 94  ? -24.998 9.665   6.913   1.00 27.44 ? 94  TYR F CD1 1 
ATOM   11132 C CD2 . TYR F 2 94  ? -23.660 9.655   8.897   1.00 27.44 ? 94  TYR F CD2 1 
ATOM   11133 C CE1 . TYR F 2 94  ? -24.089 8.797   6.294   1.00 26.96 ? 94  TYR F CE1 1 
ATOM   11134 C CE2 . TYR F 2 94  ? -22.757 8.789   8.295   1.00 27.38 ? 94  TYR F CE2 1 
ATOM   11135 C CZ  . TYR F 2 94  ? -22.972 8.365   6.998   1.00 27.45 ? 94  TYR F CZ  1 
ATOM   11136 O OH  . TYR F 2 94  ? -22.055 7.510   6.423   1.00 28.72 ? 94  TYR F OH  1 
ATOM   11137 N N   . ASN F 2 95  ? -25.459 9.711   11.723  1.00 28.26 ? 95  ASN F N   1 
ATOM   11138 C CA  . ASN F 2 95  ? -24.816 8.764   12.633  1.00 28.36 ? 95  ASN F CA  1 
ATOM   11139 C C   . ASN F 2 95  ? -25.826 7.827   13.287  1.00 28.62 ? 95  ASN F C   1 
ATOM   11140 O O   . ASN F 2 95  ? -25.638 6.612   13.294  1.00 28.60 ? 95  ASN F O   1 
ATOM   11141 C CB  . ASN F 2 95  ? -24.019 9.500   13.717  1.00 28.41 ? 95  ASN F CB  1 
ATOM   11142 C CG  . ASN F 2 95  ? -22.709 10.095  13.201  1.00 28.65 ? 95  ASN F CG  1 
ATOM   11143 O OD1 . ASN F 2 95  ? -22.121 10.962  13.850  1.00 30.05 ? 95  ASN F OD1 1 
ATOM   11144 N ND2 . ASN F 2 95  ? -22.243 9.627   12.050  1.00 27.80 ? 95  ASN F ND2 1 
ATOM   11145 N N   . ALA F 2 96  ? -26.898 8.407   13.823  1.00 28.89 ? 96  ALA F N   1 
ATOM   11146 C CA  . ALA F 2 96  ? -27.965 7.651   14.472  1.00 29.15 ? 96  ALA F CA  1 
ATOM   11147 C C   . ALA F 2 96  ? -28.632 6.679   13.506  1.00 29.43 ? 96  ALA F C   1 
ATOM   11148 O O   . ALA F 2 96  ? -28.738 5.483   13.796  1.00 29.66 ? 96  ALA F O   1 
ATOM   11149 C CB  . ALA F 2 96  ? -29.004 8.605   15.069  1.00 29.12 ? 96  ALA F CB  1 
ATOM   11150 N N   . GLU F 2 97  ? -29.070 7.200   12.361  1.00 29.51 ? 97  GLU F N   1 
ATOM   11151 C CA  . GLU F 2 97  ? -29.783 6.413   11.358  1.00 29.82 ? 97  GLU F CA  1 
ATOM   11152 C C   . GLU F 2 97  ? -28.921 5.312   10.757  1.00 29.63 ? 97  GLU F C   1 
ATOM   11153 O O   . GLU F 2 97  ? -29.379 4.183   10.612  1.00 29.81 ? 97  GLU F O   1 
ATOM   11154 C CB  . GLU F 2 97  ? -30.344 7.310   10.250  1.00 29.84 ? 97  GLU F CB  1 
ATOM   11155 C CG  . GLU F 2 97  ? -31.631 8.028   10.634  1.00 31.00 ? 97  GLU F CG  1 
ATOM   11156 C CD  . GLU F 2 97  ? -32.130 8.972   9.554   1.00 33.18 ? 97  GLU F CD  1 
ATOM   11157 O OE1 . GLU F 2 97  ? -31.637 8.904   8.407   1.00 35.31 ? 97  GLU F OE1 1 
ATOM   11158 O OE2 . GLU F 2 97  ? -33.021 9.791   9.847   1.00 33.45 ? 97  GLU F OE2 1 
ATOM   11159 N N   . LEU F 2 98  ? -27.678 5.644   10.420  1.00 29.64 ? 98  LEU F N   1 
ATOM   11160 C CA  . LEU F 2 98  ? -26.743 4.663   9.865   1.00 29.78 ? 98  LEU F CA  1 
ATOM   11161 C C   . LEU F 2 98  ? -26.349 3.561   10.855  1.00 29.75 ? 98  LEU F C   1 
ATOM   11162 O O   . LEU F 2 98  ? -26.233 2.401   10.465  1.00 29.57 ? 98  LEU F O   1 
ATOM   11163 C CB  . LEU F 2 98  ? -25.484 5.338   9.313   1.00 29.72 ? 98  LEU F CB  1 
ATOM   11164 C CG  . LEU F 2 98  ? -24.562 4.396   8.530   1.00 30.16 ? 98  LEU F CG  1 
ATOM   11165 C CD1 . LEU F 2 98  ? -25.162 4.054   7.149   1.00 30.68 ? 98  LEU F CD1 1 
ATOM   11166 C CD2 . LEU F 2 98  ? -23.151 4.962   8.403   1.00 29.49 ? 98  LEU F CD2 1 
ATOM   11167 N N   . LEU F 2 99  ? -26.134 3.923   12.120  1.00 29.68 ? 99  LEU F N   1 
ATOM   11168 C CA  . LEU F 2 99  ? -25.799 2.932   13.141  1.00 29.88 ? 99  LEU F CA  1 
ATOM   11169 C C   . LEU F 2 99  ? -26.943 1.927   13.347  1.00 30.11 ? 99  LEU F C   1 
ATOM   11170 O O   . LEU F 2 99  ? -26.703 0.726   13.481  1.00 29.99 ? 99  LEU F O   1 
ATOM   11171 C CB  . LEU F 2 99  ? -25.405 3.599   14.467  1.00 29.75 ? 99  LEU F CB  1 
ATOM   11172 C CG  . LEU F 2 99  ? -24.825 2.689   15.563  1.00 29.83 ? 99  LEU F CG  1 
ATOM   11173 C CD1 . LEU F 2 99  ? -23.600 1.927   15.075  1.00 29.42 ? 99  LEU F CD1 1 
ATOM   11174 C CD2 . LEU F 2 99  ? -24.498 3.460   16.838  1.00 29.88 ? 99  LEU F CD2 1 
ATOM   11175 N N   . VAL F 2 100 ? -28.179 2.422   13.355  1.00 30.33 ? 100 VAL F N   1 
ATOM   11176 C CA  . VAL F 2 100 ? -29.343 1.561   13.537  1.00 30.61 ? 100 VAL F CA  1 
ATOM   11177 C C   . VAL F 2 100 ? -29.528 0.630   12.337  1.00 30.90 ? 100 VAL F C   1 
ATOM   11178 O O   . VAL F 2 100 ? -29.800 -0.555  12.511  1.00 31.06 ? 100 VAL F O   1 
ATOM   11179 C CB  . VAL F 2 100 ? -30.625 2.373   13.839  1.00 30.73 ? 100 VAL F CB  1 
ATOM   11180 C CG1 . VAL F 2 100 ? -31.870 1.490   13.759  1.00 30.51 ? 100 VAL F CG1 1 
ATOM   11181 C CG2 . VAL F 2 100 ? -30.528 3.021   15.218  1.00 30.65 ? 100 VAL F CG2 1 
ATOM   11182 N N   . LEU F 2 101 ? -29.352 1.158   11.129  1.00 31.14 ? 101 LEU F N   1 
ATOM   11183 C CA  . LEU F 2 101 ? -29.406 0.336   9.918   1.00 31.40 ? 101 LEU F CA  1 
ATOM   11184 C C   . LEU F 2 101 ? -28.359 -0.777  9.911   1.00 31.52 ? 101 LEU F C   1 
ATOM   11185 O O   . LEU F 2 101 ? -28.687 -1.940  9.643   1.00 31.45 ? 101 LEU F O   1 
ATOM   11186 C CB  . LEU F 2 101 ? -29.272 1.204   8.662   1.00 31.44 ? 101 LEU F CB  1 
ATOM   11187 C CG  . LEU F 2 101 ? -30.526 1.473   7.817   1.00 31.85 ? 101 LEU F CG  1 
ATOM   11188 C CD1 . LEU F 2 101 ? -31.797 1.689   8.640   1.00 31.50 ? 101 LEU F CD1 1 
ATOM   11189 C CD2 . LEU F 2 101 ? -30.266 2.662   6.915   1.00 32.52 ? 101 LEU F CD2 1 
ATOM   11190 N N   . MET F 2 102 ? -27.113 -0.417  10.220  1.00 31.57 ? 102 MET F N   1 
ATOM   11191 C CA  . MET F 2 102 ? -25.999 -1.361  10.179  1.00 32.00 ? 102 MET F CA  1 
ATOM   11192 C C   . MET F 2 102 ? -26.100 -2.442  11.246  1.00 31.93 ? 102 MET F C   1 
ATOM   11193 O O   . MET F 2 102 ? -25.864 -3.618  10.959  1.00 31.86 ? 102 MET F O   1 
ATOM   11194 C CB  . MET F 2 102 ? -24.652 -0.638  10.277  1.00 32.32 ? 102 MET F CB  1 
ATOM   11195 C CG  . MET F 2 102 ? -24.295 0.172   9.031   1.00 33.58 ? 102 MET F CG  1 
ATOM   11196 S SD  . MET F 2 102 ? -22.649 0.907   9.102   1.00 36.46 ? 102 MET F SD  1 
ATOM   11197 C CE  . MET F 2 102 ? -21.669 -0.437  8.419   1.00 36.99 ? 102 MET F CE  1 
ATOM   11198 N N   . GLU F 2 103 ? -26.466 -2.043  12.463  1.00 31.94 ? 103 GLU F N   1 
ATOM   11199 C CA  . GLU F 2 103 ? -26.596 -2.986  13.572  1.00 31.95 ? 103 GLU F CA  1 
ATOM   11200 C C   . GLU F 2 103 ? -27.842 -3.873  13.475  1.00 31.78 ? 103 GLU F C   1 
ATOM   11201 O O   . GLU F 2 103 ? -27.798 -5.037  13.866  1.00 31.64 ? 103 GLU F O   1 
ATOM   11202 C CB  . GLU F 2 103 ? -26.519 -2.273  14.931  1.00 31.97 ? 103 GLU F CB  1 
ATOM   11203 C CG  . GLU F 2 103 ? -25.111 -1.797  15.318  1.00 32.82 ? 103 GLU F CG  1 
ATOM   11204 C CD  . GLU F 2 103 ? -24.075 -2.929  15.421  1.00 34.24 ? 103 GLU F CD  1 
ATOM   11205 O OE1 . GLU F 2 103 ? -24.463 -4.083  15.710  1.00 34.89 ? 103 GLU F OE1 1 
ATOM   11206 O OE2 . GLU F 2 103 ? -22.864 -2.665  15.208  1.00 34.45 ? 103 GLU F OE2 1 
ATOM   11207 N N   . ASN F 2 104 ? -28.939 -3.331  12.948  1.00 31.77 ? 104 ASN F N   1 
ATOM   11208 C CA  . ASN F 2 104 ? -30.121 -4.143  12.655  1.00 31.81 ? 104 ASN F CA  1 
ATOM   11209 C C   . ASN F 2 104 ? -29.784 -5.309  11.737  1.00 32.18 ? 104 ASN F C   1 
ATOM   11210 O O   . ASN F 2 104 ? -30.252 -6.426  11.953  1.00 32.15 ? 104 ASN F O   1 
ATOM   11211 C CB  . ASN F 2 104 ? -31.241 -3.303  12.038  1.00 31.60 ? 104 ASN F CB  1 
ATOM   11212 C CG  . ASN F 2 104 ? -32.046 -2.545  13.073  1.00 30.92 ? 104 ASN F CG  1 
ATOM   11213 O OD1 . ASN F 2 104 ? -31.765 -2.600  14.271  1.00 29.04 ? 104 ASN F OD1 1 
ATOM   11214 N ND2 . ASN F 2 104 ? -33.057 -1.826  12.610  1.00 30.38 ? 104 ASN F ND2 1 
ATOM   11215 N N   . GLU F 2 105 ? -28.965 -5.045  10.718  1.00 32.57 ? 105 GLU F N   1 
ATOM   11216 C CA  . GLU F 2 105 ? -28.477 -6.098  9.838   1.00 33.05 ? 105 GLU F CA  1 
ATOM   11217 C C   . GLU F 2 105 ? -27.656 -7.110  10.637  1.00 33.06 ? 105 GLU F C   1 
ATOM   11218 O O   . GLU F 2 105 ? -27.893 -8.315  10.540  1.00 33.21 ? 105 GLU F O   1 
ATOM   11219 C CB  . GLU F 2 105 ? -27.672 -5.510  8.666   1.00 33.24 ? 105 GLU F CB  1 
ATOM   11220 C CG  . GLU F 2 105 ? -27.253 -6.524  7.602   1.00 34.91 ? 105 GLU F CG  1 
ATOM   11221 C CD  . GLU F 2 105 ? -27.209 -5.925  6.194   1.00 38.54 ? 105 GLU F CD  1 
ATOM   11222 O OE1 . GLU F 2 105 ? -26.089 -5.661  5.697   1.00 39.82 ? 105 GLU F OE1 1 
ATOM   11223 O OE2 . GLU F 2 105 ? -28.288 -5.712  5.583   1.00 38.60 ? 105 GLU F OE2 1 
ATOM   11224 N N   . ARG F 2 106 ? -26.718 -6.614  11.443  1.00 32.93 ? 106 ARG F N   1 
ATOM   11225 C CA  . ARG F 2 106 ? -25.835 -7.475  12.227  1.00 33.09 ? 106 ARG F CA  1 
ATOM   11226 C C   . ARG F 2 106 ? -26.566 -8.297  13.292  1.00 32.98 ? 106 ARG F C   1 
ATOM   11227 O O   . ARG F 2 106 ? -26.125 -9.402  13.622  1.00 33.11 ? 106 ARG F O   1 
ATOM   11228 C CB  . ARG F 2 106 ? -24.698 -6.672  12.863  1.00 33.28 ? 106 ARG F CB  1 
ATOM   11229 C CG  . ARG F 2 106 ? -23.619 -6.219  11.884  1.00 34.40 ? 106 ARG F CG  1 
ATOM   11230 C CD  . ARG F 2 106 ? -22.340 -5.788  12.607  1.00 36.95 ? 106 ARG F CD  1 
ATOM   11231 N NE  . ARG F 2 106 ? -21.604 -6.930  13.159  1.00 38.92 ? 106 ARG F NE  1 
ATOM   11232 C CZ  . ARG F 2 106 ? -20.661 -7.611  12.506  1.00 40.26 ? 106 ARG F CZ  1 
ATOM   11233 N NH1 . ARG F 2 106 ? -20.317 -7.272  11.268  1.00 41.36 ? 106 ARG F NH1 1 
ATOM   11234 N NH2 . ARG F 2 106 ? -20.054 -8.635  13.091  1.00 40.68 ? 106 ARG F NH2 1 
ATOM   11235 N N   . THR F 2 107 ? -27.668 -7.759  13.823  1.00 32.66 ? 107 THR F N   1 
ATOM   11236 C CA  . THR F 2 107 ? -28.506 -8.465  14.795  1.00 32.39 ? 107 THR F CA  1 
ATOM   11237 C C   . THR F 2 107 ? -29.173 -9.687  14.156  1.00 32.47 ? 107 THR F C   1 
ATOM   11238 O O   . THR F 2 107 ? -29.055 -10.801 14.671  1.00 32.42 ? 107 THR F O   1 
ATOM   11239 C CB  . THR F 2 107 ? -29.583 -7.538  15.401  1.00 32.49 ? 107 THR F CB  1 
ATOM   11240 O OG1 . THR F 2 107 ? -28.955 -6.529  16.200  1.00 32.42 ? 107 THR F OG1 1 
ATOM   11241 C CG2 . THR F 2 107 ? -30.564 -8.324  16.279  1.00 32.46 ? 107 THR F CG2 1 
ATOM   11242 N N   . LEU F 2 108 ? -29.861 -9.472  13.034  1.00 32.12 ? 108 LEU F N   1 
ATOM   11243 C CA  . LEU F 2 108 ? -30.511 -10.557 12.294  1.00 32.00 ? 108 LEU F CA  1 
ATOM   11244 C C   . LEU F 2 108 ? -29.528 -11.669 11.917  1.00 31.74 ? 108 LEU F C   1 
ATOM   11245 O O   . LEU F 2 108 ? -29.879 -12.847 11.946  1.00 31.67 ? 108 LEU F O   1 
ATOM   11246 C CB  . LEU F 2 108 ? -31.221 -10.016 11.048  1.00 31.95 ? 108 LEU F CB  1 
ATOM   11247 C CG  . LEU F 2 108 ? -32.661 -9.483  11.137  1.00 32.63 ? 108 LEU F CG  1 
ATOM   11248 C CD1 . LEU F 2 108 ? -33.101 -9.031  12.541  1.00 32.43 ? 108 LEU F CD1 1 
ATOM   11249 C CD2 . LEU F 2 108 ? -32.871 -8.360  10.109  1.00 33.12 ? 108 LEU F CD2 1 
ATOM   11250 N N   . ASP F 2 109 ? -28.298 -11.290 11.584  1.00 31.43 ? 109 ASP F N   1 
ATOM   11251 C CA  . ASP F 2 109 ? -27.253 -12.263 11.305  1.00 31.35 ? 109 ASP F CA  1 
ATOM   11252 C C   . ASP F 2 109 ? -26.797 -12.963 12.583  1.00 30.90 ? 109 ASP F C   1 
ATOM   11253 O O   . ASP F 2 109 ? -26.499 -14.158 12.568  1.00 30.58 ? 109 ASP F O   1 
ATOM   11254 C CB  . ASP F 2 109 ? -26.072 -11.604 10.589  1.00 31.66 ? 109 ASP F CB  1 
ATOM   11255 C CG  . ASP F 2 109 ? -26.448 -11.059 9.210   1.00 32.92 ? 109 ASP F CG  1 
ATOM   11256 O OD1 . ASP F 2 109 ? -27.361 -11.622 8.566   1.00 33.15 ? 109 ASP F OD1 1 
ATOM   11257 O OD2 . ASP F 2 109 ? -25.821 -10.063 8.770   1.00 35.40 ? 109 ASP F OD2 1 
ATOM   11258 N N   . PHE F 2 110 ? -26.759 -12.215 13.683  1.00 30.50 ? 110 PHE F N   1 
ATOM   11259 C CA  . PHE F 2 110 ? -26.400 -12.759 14.991  1.00 30.34 ? 110 PHE F CA  1 
ATOM   11260 C C   . PHE F 2 110 ? -27.332 -13.925 15.362  1.00 30.21 ? 110 PHE F C   1 
ATOM   11261 O O   . PHE F 2 110 ? -26.865 -15.026 15.674  1.00 30.11 ? 110 PHE F O   1 
ATOM   11262 C CB  . PHE F 2 110 ? -26.426 -11.636 16.038  1.00 30.25 ? 110 PHE F CB  1 
ATOM   11263 C CG  . PHE F 2 110 ? -26.087 -12.072 17.434  1.00 29.91 ? 110 PHE F CG  1 
ATOM   11264 C CD1 . PHE F 2 110 ? -24.861 -12.669 17.724  1.00 29.92 ? 110 PHE F CD1 1 
ATOM   11265 C CD2 . PHE F 2 110 ? -26.982 -11.843 18.476  1.00 29.29 ? 110 PHE F CD2 1 
ATOM   11266 C CE1 . PHE F 2 110 ? -24.546 -13.058 19.030  1.00 28.78 ? 110 PHE F CE1 1 
ATOM   11267 C CE2 . PHE F 2 110 ? -26.673 -12.224 19.782  1.00 28.83 ? 110 PHE F CE2 1 
ATOM   11268 C CZ  . PHE F 2 110 ? -25.452 -12.831 20.057  1.00 28.36 ? 110 PHE F CZ  1 
ATOM   11269 N N   . HIS F 2 111 ? -28.640 -13.688 15.281  1.00 29.95 ? 111 HIS F N   1 
ATOM   11270 C CA  . HIS F 2 111 ? -29.643 -14.722 15.548  1.00 29.86 ? 111 HIS F CA  1 
ATOM   11271 C C   . HIS F 2 111 ? -29.498 -15.918 14.601  1.00 30.09 ? 111 HIS F C   1 
ATOM   11272 O O   . HIS F 2 111 ? -29.584 -17.074 15.022  1.00 29.87 ? 111 HIS F O   1 
ATOM   11273 C CB  . HIS F 2 111 ? -31.052 -14.148 15.430  1.00 29.52 ? 111 HIS F CB  1 
ATOM   11274 C CG  . HIS F 2 111 ? -31.390 -13.135 16.477  1.00 29.49 ? 111 HIS F CG  1 
ATOM   11275 N ND1 . HIS F 2 111 ? -31.290 -13.394 17.828  1.00 29.10 ? 111 HIS F ND1 1 
ATOM   11276 C CD2 . HIS F 2 111 ? -31.856 -11.869 16.370  1.00 28.46 ? 111 HIS F CD2 1 
ATOM   11277 C CE1 . HIS F 2 111 ? -31.673 -12.329 18.507  1.00 28.50 ? 111 HIS F CE1 1 
ATOM   11278 N NE2 . HIS F 2 111 ? -32.023 -11.390 17.646  1.00 28.21 ? 111 HIS F NE2 1 
ATOM   11279 N N   . ASP F 2 112 ? -29.282 -15.623 13.321  1.00 30.32 ? 112 ASP F N   1 
ATOM   11280 C CA  . ASP F 2 112 ? -29.069 -16.641 12.302  1.00 30.62 ? 112 ASP F CA  1 
ATOM   11281 C C   . ASP F 2 112 ? -27.881 -17.534 12.687  1.00 30.62 ? 112 ASP F C   1 
ATOM   11282 O O   . ASP F 2 112 ? -27.983 -18.759 12.675  1.00 30.60 ? 112 ASP F O   1 
ATOM   11283 C CB  . ASP F 2 112 ? -28.846 -15.965 10.944  1.00 30.55 ? 112 ASP F CB  1 
ATOM   11284 C CG  . ASP F 2 112 ? -29.003 -16.914 9.772   1.00 31.37 ? 112 ASP F CG  1 
ATOM   11285 O OD1 . ASP F 2 112 ? -29.572 -18.021 9.937   1.00 31.98 ? 112 ASP F OD1 1 
ATOM   11286 O OD2 . ASP F 2 112 ? -28.559 -16.540 8.667   1.00 32.07 ? 112 ASP F OD2 1 
ATOM   11287 N N   . SER F 2 113 ? -26.774 -16.895 13.058  1.00 30.93 ? 113 SER F N   1 
ATOM   11288 C CA  . SER F 2 113 ? -25.550 -17.567 13.498  1.00 30.96 ? 113 SER F CA  1 
ATOM   11289 C C   . SER F 2 113 ? -25.778 -18.457 14.722  1.00 31.03 ? 113 SER F C   1 
ATOM   11290 O O   . SER F 2 113 ? -25.250 -19.570 14.798  1.00 30.94 ? 113 SER F O   1 
ATOM   11291 C CB  . SER F 2 113 ? -24.470 -16.519 13.802  1.00 30.85 ? 113 SER F CB  1 
ATOM   11292 O OG  . SER F 2 113 ? -23.331 -17.093 14.420  1.00 31.29 ? 113 SER F OG  1 
ATOM   11293 N N   . ASN F 2 114 ? -26.557 -17.951 15.676  1.00 31.07 ? 114 ASN F N   1 
ATOM   11294 C CA  . ASN F 2 114 ? -26.862 -18.685 16.897  1.00 31.13 ? 114 ASN F CA  1 
ATOM   11295 C C   . ASN F 2 114 ? -27.694 -19.944 16.665  1.00 31.30 ? 114 ASN F C   1 
ATOM   11296 O O   . ASN F 2 114 ? -27.447 -20.969 17.300  1.00 31.42 ? 114 ASN F O   1 
ATOM   11297 C CB  . ASN F 2 114 ? -27.527 -17.768 17.931  1.00 30.99 ? 114 ASN F CB  1 
ATOM   11298 C CG  . ASN F 2 114 ? -26.580 -16.701 18.464  1.00 30.90 ? 114 ASN F CG  1 
ATOM   11299 O OD1 . ASN F 2 114 ? -27.014 -15.645 18.921  1.00 31.52 ? 114 ASN F OD1 1 
ATOM   11300 N ND2 . ASN F 2 114 ? -25.284 -16.970 18.398  1.00 29.82 ? 114 ASN F ND2 1 
ATOM   11301 N N   . VAL F 2 115 ? -28.666 -19.869 15.756  1.00 31.46 ? 115 VAL F N   1 
ATOM   11302 C CA  . VAL F 2 115 ? -29.461 -21.036 15.379  1.00 31.67 ? 115 VAL F CA  1 
ATOM   11303 C C   . VAL F 2 115 ? -28.560 -22.073 14.716  1.00 32.15 ? 115 VAL F C   1 
ATOM   11304 O O   . VAL F 2 115 ? -28.652 -23.266 15.020  1.00 32.37 ? 115 VAL F O   1 
ATOM   11305 C CB  . VAL F 2 115 ? -30.646 -20.668 14.442  1.00 31.81 ? 115 VAL F CB  1 
ATOM   11306 C CG1 . VAL F 2 115 ? -31.341 -21.919 13.911  1.00 31.03 ? 115 VAL F CG1 1 
ATOM   11307 C CG2 . VAL F 2 115 ? -31.650 -19.781 15.166  1.00 31.50 ? 115 VAL F CG2 1 
ATOM   11308 N N   . LYS F 2 116 ? -27.679 -21.609 13.831  1.00 32.50 ? 116 LYS F N   1 
ATOM   11309 C CA  . LYS F 2 116 ? -26.727 -22.487 13.150  1.00 33.03 ? 116 LYS F CA  1 
ATOM   11310 C C   . LYS F 2 116 ? -25.713 -23.149 14.099  1.00 33.27 ? 116 LYS F C   1 
ATOM   11311 O O   . LYS F 2 116 ? -25.372 -24.323 13.916  1.00 33.26 ? 116 LYS F O   1 
ATOM   11312 C CB  . LYS F 2 116 ? -26.047 -21.755 11.982  1.00 32.95 ? 116 LYS F CB  1 
ATOM   11313 C CG  . LYS F 2 116 ? -24.610 -22.151 11.725  1.00 33.88 ? 116 LYS F CG  1 
ATOM   11314 C CD  . LYS F 2 116 ? -24.346 -22.527 10.281  1.00 35.16 ? 116 LYS F CD  1 
ATOM   11315 C CE  . LYS F 2 116 ? -22.849 -22.711 10.068  1.00 35.81 ? 116 LYS F CE  1 
ATOM   11316 N NZ  . LYS F 2 116 ? -22.515 -23.918 9.262   1.00 36.28 ? 116 LYS F NZ  1 
ATOM   11317 N N   . ASN F 2 117 ? -25.250 -22.410 15.107  1.00 33.60 ? 117 ASN F N   1 
ATOM   11318 C CA  . ASN F 2 117 ? -24.332 -22.965 16.111  1.00 34.13 ? 117 ASN F CA  1 
ATOM   11319 C C   . ASN F 2 117 ? -24.981 -24.012 17.023  1.00 34.44 ? 117 ASN F C   1 
ATOM   11320 O O   . ASN F 2 117 ? -24.359 -25.018 17.360  1.00 34.15 ? 117 ASN F O   1 
ATOM   11321 C CB  . ASN F 2 117 ? -23.700 -21.856 16.956  1.00 34.05 ? 117 ASN F CB  1 
ATOM   11322 C CG  . ASN F 2 117 ? -22.721 -21.003 16.170  1.00 34.52 ? 117 ASN F CG  1 
ATOM   11323 O OD1 . ASN F 2 117 ? -22.138 -21.450 15.179  1.00 34.70 ? 117 ASN F OD1 1 
ATOM   11324 N ND2 . ASN F 2 117 ? -22.530 -19.761 16.616  1.00 34.59 ? 117 ASN F ND2 1 
ATOM   11325 N N   . LEU F 2 118 ? -26.231 -23.763 17.412  1.00 35.06 ? 118 LEU F N   1 
ATOM   11326 C CA  . LEU F 2 118 ? -26.995 -24.686 18.241  1.00 35.79 ? 118 LEU F CA  1 
ATOM   11327 C C   . LEU F 2 118 ? -27.280 -25.977 17.481  1.00 36.60 ? 118 LEU F C   1 
ATOM   11328 O O   . LEU F 2 118 ? -27.247 -27.063 18.063  1.00 36.79 ? 118 LEU F O   1 
ATOM   11329 C CB  . LEU F 2 118 ? -28.300 -24.035 18.702  1.00 35.71 ? 118 LEU F CB  1 
ATOM   11330 C CG  . LEU F 2 118 ? -29.191 -24.763 19.719  1.00 36.15 ? 118 LEU F CG  1 
ATOM   11331 C CD1 . LEU F 2 118 ? -28.524 -24.862 21.090  1.00 36.73 ? 118 LEU F CD1 1 
ATOM   11332 C CD2 . LEU F 2 118 ? -30.534 -24.067 19.840  1.00 35.73 ? 118 LEU F CD2 1 
ATOM   11333 N N   . TYR F 2 119 ? -27.553 -25.845 16.182  1.00 37.42 ? 119 TYR F N   1 
ATOM   11334 C CA  . TYR F 2 119 ? -27.785 -26.987 15.303  1.00 38.17 ? 119 TYR F CA  1 
ATOM   11335 C C   . TYR F 2 119 ? -26.527 -27.844 15.192  1.00 39.18 ? 119 TYR F C   1 
ATOM   11336 O O   . TYR F 2 119 ? -26.591 -29.068 15.277  1.00 39.05 ? 119 TYR F O   1 
ATOM   11337 C CB  . TYR F 2 119 ? -28.238 -26.519 13.910  1.00 37.85 ? 119 TYR F CB  1 
ATOM   11338 C CG  . TYR F 2 119 ? -28.390 -27.644 12.912  1.00 37.05 ? 119 TYR F CG  1 
ATOM   11339 C CD1 . TYR F 2 119 ? -29.594 -28.339 12.795  1.00 36.59 ? 119 TYR F CD1 1 
ATOM   11340 C CD2 . TYR F 2 119 ? -27.324 -28.030 12.096  1.00 36.10 ? 119 TYR F CD2 1 
ATOM   11341 C CE1 . TYR F 2 119 ? -29.735 -29.387 11.889  1.00 35.95 ? 119 TYR F CE1 1 
ATOM   11342 C CE2 . TYR F 2 119 ? -27.454 -29.075 11.191  1.00 35.87 ? 119 TYR F CE2 1 
ATOM   11343 C CZ  . TYR F 2 119 ? -28.664 -29.746 11.092  1.00 35.97 ? 119 TYR F CZ  1 
ATOM   11344 O OH  . TYR F 2 119 ? -28.801 -30.777 10.197  1.00 35.97 ? 119 TYR F OH  1 
ATOM   11345 N N   . ASP F 2 120 ? -25.388 -27.186 14.990  1.00 40.68 ? 120 ASP F N   1 
ATOM   11346 C CA  . ASP F 2 120 ? -24.101 -27.868 14.920  1.00 42.13 ? 120 ASP F CA  1 
ATOM   11347 C C   . ASP F 2 120 ? -23.700 -28.488 16.258  1.00 42.98 ? 120 ASP F C   1 
ATOM   11348 O O   . ASP F 2 120 ? -23.028 -29.516 16.281  1.00 43.13 ? 120 ASP F O   1 
ATOM   11349 C CB  . ASP F 2 120 ? -23.007 -26.925 14.408  1.00 42.06 ? 120 ASP F CB  1 
ATOM   11350 C CG  . ASP F 2 120 ? -23.015 -26.785 12.891  1.00 42.86 ? 120 ASP F CG  1 
ATOM   11351 O OD1 . ASP F 2 120 ? -23.751 -27.531 12.213  1.00 43.85 ? 120 ASP F OD1 1 
ATOM   11352 O OD2 . ASP F 2 120 ? -22.276 -25.927 12.368  1.00 44.26 ? 120 ASP F OD2 1 
ATOM   11353 N N   . LYS F 2 121 ? -24.132 -27.875 17.360  1.00 44.16 ? 121 LYS F N   1 
ATOM   11354 C CA  . LYS F 2 121 ? -23.819 -28.373 18.700  1.00 45.43 ? 121 LYS F CA  1 
ATOM   11355 C C   . LYS F 2 121 ? -24.413 -29.764 18.906  1.00 46.10 ? 121 LYS F C   1 
ATOM   11356 O O   . LYS F 2 121 ? -23.757 -30.656 19.447  1.00 46.25 ? 121 LYS F O   1 
ATOM   11357 C CB  . LYS F 2 121 ? -24.327 -27.410 19.779  1.00 45.44 ? 121 LYS F CB  1 
ATOM   11358 C CG  . LYS F 2 121 ? -23.634 -27.571 21.132  1.00 46.38 ? 121 LYS F CG  1 
ATOM   11359 C CD  . LYS F 2 121 ? -24.279 -26.720 22.234  1.00 47.56 ? 121 LYS F CD  1 
ATOM   11360 C CE  . LYS F 2 121 ? -25.462 -27.433 22.889  1.00 48.23 ? 121 LYS F CE  1 
ATOM   11361 N NZ  . LYS F 2 121 ? -25.988 -26.697 24.078  1.00 48.57 ? 121 LYS F NZ  1 
ATOM   11362 N N   . VAL F 2 122 ? -25.655 -29.939 18.466  1.00 47.00 ? 122 VAL F N   1 
ATOM   11363 C CA  . VAL F 2 122 ? -26.316 -31.236 18.516  1.00 47.72 ? 122 VAL F CA  1 
ATOM   11364 C C   . VAL F 2 122 ? -25.661 -32.168 17.499  1.00 48.42 ? 122 VAL F C   1 
ATOM   11365 O O   . VAL F 2 122 ? -25.258 -33.280 17.842  1.00 48.57 ? 122 VAL F O   1 
ATOM   11366 C CB  . VAL F 2 122 ? -27.835 -31.104 18.268  1.00 47.61 ? 122 VAL F CB  1 
ATOM   11367 C CG1 . VAL F 2 122 ? -28.474 -32.460 17.973  1.00 47.62 ? 122 VAL F CG1 1 
ATOM   11368 C CG2 . VAL F 2 122 ? -28.508 -30.448 19.462  1.00 47.26 ? 122 VAL F CG2 1 
ATOM   11369 N N   . ARG F 2 123 ? -25.524 -31.678 16.269  1.00 49.13 ? 123 ARG F N   1 
ATOM   11370 C CA  . ARG F 2 123 ? -24.980 -32.444 15.152  1.00 49.96 ? 123 ARG F CA  1 
ATOM   11371 C C   . ARG F 2 123 ? -23.741 -33.255 15.527  1.00 50.45 ? 123 ARG F C   1 
ATOM   11372 O O   . ARG F 2 123 ? -23.740 -34.478 15.395  1.00 50.62 ? 123 ARG F O   1 
ATOM   11373 C CB  . ARG F 2 123 ? -24.652 -31.503 13.987  1.00 50.06 ? 123 ARG F CB  1 
ATOM   11374 C CG  . ARG F 2 123 ? -24.877 -32.075 12.587  1.00 50.70 ? 123 ARG F CG  1 
ATOM   11375 C CD  . ARG F 2 123 ? -23.703 -32.908 12.069  1.00 52.75 ? 123 ARG F CD  1 
ATOM   11376 N NE  . ARG F 2 123 ? -22.452 -32.179 11.799  1.00 54.17 ? 123 ARG F NE  1 
ATOM   11377 C CZ  . ARG F 2 123 ? -22.336 -30.895 11.446  1.00 54.70 ? 123 ARG F CZ  1 
ATOM   11378 N NH1 . ARG F 2 123 ? -23.405 -30.120 11.295  1.00 54.79 ? 123 ARG F NH1 1 
ATOM   11379 N NH2 . ARG F 2 123 ? -21.129 -30.383 11.236  1.00 54.19 ? 123 ARG F NH2 1 
ATOM   11380 N N   . LEU F 2 124 ? -22.697 -32.586 16.004  1.00 51.08 ? 124 LEU F N   1 
ATOM   11381 C CA  . LEU F 2 124 ? -21.458 -33.278 16.347  1.00 51.82 ? 124 LEU F CA  1 
ATOM   11382 C C   . LEU F 2 124 ? -21.561 -34.085 17.638  1.00 52.27 ? 124 LEU F C   1 
ATOM   11383 O O   . LEU F 2 124 ? -20.721 -34.941 17.906  1.00 52.38 ? 124 LEU F O   1 
ATOM   11384 C CB  . LEU F 2 124 ? -20.283 -32.303 16.428  1.00 51.84 ? 124 LEU F CB  1 
ATOM   11385 C CG  . LEU F 2 124 ? -20.561 -30.817 16.228  1.00 52.21 ? 124 LEU F CG  1 
ATOM   11386 C CD1 . LEU F 2 124 ? -20.445 -30.093 17.557  1.00 52.97 ? 124 LEU F CD1 1 
ATOM   11387 C CD2 . LEU F 2 124 ? -19.587 -30.238 15.219  1.00 52.00 ? 124 LEU F CD2 1 
ATOM   11388 N N   . GLN F 2 125 ? -22.587 -33.810 18.436  1.00 57.75 ? 125 GLN F N   1 
ATOM   11389 C CA  . GLN F 2 125 ? -22.810 -34.561 19.668  1.00 58.25 ? 125 GLN F CA  1 
ATOM   11390 C C   . GLN F 2 125 ? -23.458 -35.917 19.401  1.00 58.56 ? 125 GLN F C   1 
ATOM   11391 O O   . GLN F 2 125 ? -23.356 -36.836 20.213  1.00 58.58 ? 125 GLN F O   1 
ATOM   11392 C CB  . GLN F 2 125 ? -23.671 -33.750 20.639  1.00 58.28 ? 125 GLN F CB  1 
ATOM   11393 C CG  . GLN F 2 125 ? -23.302 -33.937 22.102  1.00 58.75 ? 125 GLN F CG  1 
ATOM   11394 C CD  . GLN F 2 125 ? -23.928 -32.888 23.000  1.00 59.39 ? 125 GLN F CD  1 
ATOM   11395 O OE1 . GLN F 2 125 ? -23.467 -31.748 23.057  1.00 60.56 ? 125 GLN F OE1 1 
ATOM   11396 N NE2 . GLN F 2 125 ? -24.985 -33.270 23.707  1.00 58.96 ? 125 GLN F NE2 1 
ATOM   11397 N N   . LEU F 2 126 ? -24.124 -36.032 18.257  1.00 58.91 ? 126 LEU F N   1 
ATOM   11398 C CA  . LEU F 2 126 ? -24.807 -37.267 17.878  1.00 59.21 ? 126 LEU F CA  1 
ATOM   11399 C C   . LEU F 2 126 ? -24.017 -38.142 16.912  1.00 59.48 ? 126 LEU F C   1 
ATOM   11400 O O   . LEU F 2 126 ? -24.215 -39.357 16.881  1.00 59.53 ? 126 LEU F O   1 
ATOM   11401 C CB  . LEU F 2 126 ? -26.182 -36.963 17.277  1.00 59.15 ? 126 LEU F CB  1 
ATOM   11402 C CG  . LEU F 2 126 ? -27.239 -36.311 18.164  1.00 59.04 ? 126 LEU F CG  1 
ATOM   11403 C CD1 . LEU F 2 126 ? -28.537 -36.193 17.392  1.00 59.06 ? 126 LEU F CD1 1 
ATOM   11404 C CD2 . LEU F 2 126 ? -27.448 -37.093 19.449  1.00 59.04 ? 126 LEU F CD2 1 
ATOM   11405 N N   . ARG F 2 127 ? -23.145 -37.526 16.121  1.00 59.77 ? 127 ARG F N   1 
ATOM   11406 C CA  . ARG F 2 127 ? -22.362 -38.248 15.124  1.00 60.13 ? 127 ARG F CA  1 
ATOM   11407 C C   . ARG F 2 127 ? -23.263 -39.078 14.214  1.00 60.21 ? 127 ARG F C   1 
ATOM   11408 O O   . ARG F 2 127 ? -24.291 -38.592 13.748  1.00 60.22 ? 127 ARG F O   1 
ATOM   11409 C CB  . ARG F 2 127 ? -21.320 -39.138 15.799  1.00 60.20 ? 127 ARG F CB  1 
ATOM   11410 C CG  . ARG F 2 127 ? -20.691 -38.528 17.039  1.00 60.48 ? 127 ARG F CG  1 
ATOM   11411 C CD  . ARG F 2 127 ? -19.421 -37.768 16.701  1.00 61.21 ? 127 ARG F CD  1 
ATOM   11412 N NE  . ARG F 2 127 ? -18.369 -38.645 16.195  1.00 61.58 ? 127 ARG F NE  1 
ATOM   11413 C CZ  . ARG F 2 127 ? -17.549 -39.352 16.965  1.00 62.01 ? 127 ARG F CZ  1 
ATOM   11414 N NH1 . ARG F 2 127 ? -17.659 -39.293 18.284  1.00 61.91 ? 127 ARG F NH1 1 
ATOM   11415 N NH2 . ARG F 2 127 ? -16.619 -40.120 16.417  1.00 62.00 ? 127 ARG F NH2 1 
ATOM   11416 N N   . ASP F 2 128 ? -22.878 -40.326 13.960  1.00 60.42 ? 128 ASP F N   1 
ATOM   11417 C CA  . ASP F 2 128 ? -23.690 -41.211 13.117  1.00 60.50 ? 128 ASP F CA  1 
ATOM   11418 C C   . ASP F 2 128 ? -24.797 -41.975 13.866  1.00 60.45 ? 128 ASP F C   1 
ATOM   11419 O O   . ASP F 2 128 ? -25.539 -42.747 13.256  1.00 60.53 ? 128 ASP F O   1 
ATOM   11420 C CB  . ASP F 2 128 ? -22.812 -42.151 12.264  1.00 60.65 ? 128 ASP F CB  1 
ATOM   11421 C CG  . ASP F 2 128 ? -21.864 -43.021 13.093  1.00 60.93 ? 128 ASP F CG  1 
ATOM   11422 O OD1 . ASP F 2 128 ? -21.830 -42.910 14.338  1.00 61.38 ? 128 ASP F OD1 1 
ATOM   11423 O OD2 . ASP F 2 128 ? -21.137 -43.832 12.476  1.00 61.11 ? 128 ASP F OD2 1 
ATOM   11424 N N   . ASN F 2 129 ? -24.715 -41.737 15.065  1.00 50.76 ? 129 ASN F N   1 
ATOM   11425 C CA  . ASN F 2 129 ? -25.757 -42.343 15.892  1.00 50.35 ? 129 ASN F CA  1 
ATOM   11426 C C   . ASN F 2 129 ? -27.159 -41.954 15.429  1.00 50.04 ? 129 ASN F C   1 
ATOM   11427 O O   . ASN F 2 129 ? -28.133 -42.663 15.684  1.00 50.13 ? 129 ASN F O   1 
ATOM   11428 C CB  . ASN F 2 129 ? -25.564 -41.965 17.361  1.00 50.43 ? 129 ASN F CB  1 
ATOM   11429 C CG  . ASN F 2 129 ? -24.577 -42.872 18.071  1.00 50.75 ? 129 ASN F CG  1 
ATOM   11430 O OD1 . ASN F 2 129 ? -24.495 -42.878 19.299  1.00 50.68 ? 129 ASN F OD1 1 
ATOM   11431 N ND2 . ASN F 2 129 ? -23.822 -43.644 17.299  1.00 50.69 ? 129 ASN F ND2 1 
ATOM   11432 N N   . ALA F 2 130 ? -27.244 -40.819 14.746  1.00 49.57 ? 130 ALA F N   1 
ATOM   11433 C CA  . ALA F 2 130 ? -28.502 -40.292 14.224  1.00 49.11 ? 130 ALA F CA  1 
ATOM   11434 C C   . ALA F 2 130 ? -28.354 -39.855 12.769  1.00 48.81 ? 130 ALA F C   1 
ATOM   11435 O O   . ALA F 2 130 ? -27.256 -39.884 12.203  1.00 48.63 ? 130 ALA F O   1 
ATOM   11436 C CB  . ALA F 2 130 ? -29.015 -39.146 15.085  1.00 49.05 ? 130 ALA F CB  1 
ATOM   11437 N N   . LYS F 2 131 ? -29.471 -39.445 12.181  1.00 48.47 ? 131 LYS F N   1 
ATOM   11438 C CA  . LYS F 2 131 ? -29.554 -39.165 10.758  1.00 48.22 ? 131 LYS F CA  1 
ATOM   11439 C C   . LYS F 2 131 ? -29.974 -37.713 10.524  1.00 47.85 ? 131 LYS F C   1 
ATOM   11440 O O   . LYS F 2 131 ? -30.970 -37.253 11.087  1.00 47.77 ? 131 LYS F O   1 
ATOM   11441 C CB  . LYS F 2 131 ? -30.565 -40.131 10.138  1.00 48.26 ? 131 LYS F CB  1 
ATOM   11442 C CG  . LYS F 2 131 ? -30.607 -40.192 8.623   1.00 48.67 ? 131 LYS F CG  1 
ATOM   11443 C CD  . LYS F 2 131 ? -31.529 -41.329 8.179   1.00 49.79 ? 131 LYS F CD  1 
ATOM   11444 C CE  . LYS F 2 131 ? -32.978 -41.104 8.631   1.00 50.50 ? 131 LYS F CE  1 
ATOM   11445 N NZ  . LYS F 2 131 ? -33.702 -42.388 8.892   1.00 51.28 ? 131 LYS F NZ  1 
ATOM   11446 N N   . GLU F 2 132 ? -29.204 -36.996 9.707   1.00 47.47 ? 132 GLU F N   1 
ATOM   11447 C CA  . GLU F 2 132 ? -29.551 -35.633 9.305   1.00 47.33 ? 132 GLU F CA  1 
ATOM   11448 C C   . GLU F 2 132 ? -30.699 -35.653 8.297   1.00 47.01 ? 132 GLU F C   1 
ATOM   11449 O O   . GLU F 2 132 ? -30.532 -36.138 7.177   1.00 47.13 ? 132 GLU F O   1 
ATOM   11450 C CB  . GLU F 2 132 ? -28.350 -34.926 8.667   1.00 47.44 ? 132 GLU F CB  1 
ATOM   11451 C CG  . GLU F 2 132 ? -27.406 -34.204 9.612   1.00 47.88 ? 132 GLU F CG  1 
ATOM   11452 C CD  . GLU F 2 132 ? -26.548 -33.176 8.876   1.00 48.93 ? 132 GLU F CD  1 
ATOM   11453 O OE1 . GLU F 2 132 ? -25.415 -33.524 8.462   1.00 48.65 ? 132 GLU F OE1 1 
ATOM   11454 O OE2 . GLU F 2 132 ? -27.016 -32.028 8.692   1.00 48.55 ? 132 GLU F OE2 1 
ATOM   11455 N N   . LEU F 2 133 ? -31.854 -35.120 8.688   1.00 46.54 ? 133 LEU F N   1 
ATOM   11456 C CA  . LEU F 2 133 ? -33.007 -35.061 7.789   1.00 46.26 ? 133 LEU F CA  1 
ATOM   11457 C C   . LEU F 2 133 ? -32.943 -33.897 6.798   1.00 46.13 ? 133 LEU F C   1 
ATOM   11458 O O   . LEU F 2 133 ? -33.655 -33.897 5.789   1.00 46.38 ? 133 LEU F O   1 
ATOM   11459 C CB  . LEU F 2 133 ? -34.327 -35.049 8.575   1.00 46.22 ? 133 LEU F CB  1 
ATOM   11460 C CG  . LEU F 2 133 ? -34.698 -36.318 9.356   1.00 46.10 ? 133 LEU F CG  1 
ATOM   11461 C CD1 . LEU F 2 133 ? -35.997 -36.115 10.118  1.00 45.97 ? 133 LEU F CD1 1 
ATOM   11462 C CD2 . LEU F 2 133 ? -34.795 -37.547 8.451   1.00 45.60 ? 133 LEU F CD2 1 
ATOM   11463 N N   . GLY F 2 134 ? -32.090 -32.914 7.083   1.00 45.71 ? 134 GLY F N   1 
ATOM   11464 C CA  . GLY F 2 134 ? -31.876 -31.778 6.185   1.00 45.21 ? 134 GLY F CA  1 
ATOM   11465 C C   . GLY F 2 134 ? -32.843 -30.618 6.363   1.00 44.93 ? 134 GLY F C   1 
ATOM   11466 O O   . GLY F 2 134 ? -32.816 -29.659 5.591   1.00 44.84 ? 134 GLY F O   1 
ATOM   11467 N N   . ASN F 2 135 ? -33.691 -30.708 7.385   1.00 44.72 ? 135 ASN F N   1 
ATOM   11468 C CA  . ASN F 2 135 ? -34.688 -29.684 7.677   1.00 44.49 ? 135 ASN F CA  1 
ATOM   11469 C C   . ASN F 2 135 ? -34.558 -29.119 9.094   1.00 44.51 ? 135 ASN F C   1 
ATOM   11470 O O   . ASN F 2 135 ? -35.441 -28.402 9.569   1.00 44.37 ? 135 ASN F O   1 
ATOM   11471 C CB  . ASN F 2 135 ? -36.092 -30.261 7.474   1.00 44.57 ? 135 ASN F CB  1 
ATOM   11472 C CG  . ASN F 2 135 ? -36.402 -31.407 8.435   1.00 44.43 ? 135 ASN F CG  1 
ATOM   11473 O OD1 . ASN F 2 135 ? -35.501 -31.978 9.057   1.00 44.10 ? 135 ASN F OD1 1 
ATOM   11474 N ND2 . ASN F 2 135 ? -37.682 -31.740 8.564   1.00 43.36 ? 135 ASN F ND2 1 
ATOM   11475 N N   . GLY F 2 136 ? -33.455 -29.451 9.761   1.00 44.67 ? 136 GLY F N   1 
ATOM   11476 C CA  . GLY F 2 136 ? -33.234 -29.060 11.149  1.00 44.73 ? 136 GLY F CA  1 
ATOM   11477 C C   . GLY F 2 136 ? -33.456 -30.202 12.123  1.00 44.99 ? 136 GLY F C   1 
ATOM   11478 O O   . GLY F 2 136 ? -33.218 -30.056 13.322  1.00 44.94 ? 136 GLY F O   1 
ATOM   11479 N N   . CYS F 2 137 ? -33.906 -31.345 11.608  1.00 45.25 ? 137 CYS F N   1 
ATOM   11480 C CA  . CYS F 2 137 ? -34.234 -32.494 12.452  1.00 45.59 ? 137 CYS F CA  1 
ATOM   11481 C C   . CYS F 2 137 ? -33.246 -33.650 12.334  1.00 45.69 ? 137 CYS F C   1 
ATOM   11482 O O   . CYS F 2 137 ? -32.652 -33.886 11.280  1.00 45.44 ? 137 CYS F O   1 
ATOM   11483 C CB  . CYS F 2 137 ? -35.652 -32.992 12.163  1.00 45.67 ? 137 CYS F CB  1 
ATOM   11484 S SG  . CYS F 2 137 ? -36.947 -31.775 12.467  1.00 45.80 ? 137 CYS F SG  1 
ATOM   11485 N N   . PHE F 2 138 ? -33.079 -34.362 13.444  1.00 46.17 ? 138 PHE F N   1 
ATOM   11486 C CA  . PHE F 2 138 ? -32.248 -35.557 13.497  1.00 46.55 ? 138 PHE F CA  1 
ATOM   11487 C C   . PHE F 2 138 ? -33.115 -36.741 13.875  1.00 46.92 ? 138 PHE F C   1 
ATOM   11488 O O   . PHE F 2 138 ? -33.864 -36.673 14.849  1.00 46.94 ? 138 PHE F O   1 
ATOM   11489 C CB  . PHE F 2 138 ? -31.137 -35.390 14.532  1.00 46.39 ? 138 PHE F CB  1 
ATOM   11490 C CG  . PHE F 2 138 ? -30.184 -34.284 14.222  1.00 46.25 ? 138 PHE F CG  1 
ATOM   11491 C CD1 . PHE F 2 138 ? -29.030 -34.536 13.483  1.00 46.05 ? 138 PHE F CD1 1 
ATOM   11492 C CD2 . PHE F 2 138 ? -30.436 -32.987 14.664  1.00 45.97 ? 138 PHE F CD2 1 
ATOM   11493 C CE1 . PHE F 2 138 ? -28.135 -33.513 13.188  1.00 46.27 ? 138 PHE F CE1 1 
ATOM   11494 C CE2 . PHE F 2 138 ? -29.549 -31.953 14.375  1.00 46.30 ? 138 PHE F CE2 1 
ATOM   11495 C CZ  . PHE F 2 138 ? -28.394 -32.216 13.634  1.00 46.41 ? 138 PHE F CZ  1 
ATOM   11496 N N   . GLU F 2 139 ? -33.026 -37.819 13.101  1.00 47.38 ? 139 GLU F N   1 
ATOM   11497 C CA  . GLU F 2 139 ? -33.728 -39.050 13.451  1.00 47.92 ? 139 GLU F CA  1 
ATOM   11498 C C   . GLU F 2 139 ? -32.734 -40.061 14.011  1.00 48.19 ? 139 GLU F C   1 
ATOM   11499 O O   . GLU F 2 139 ? -31.792 -40.464 13.326  1.00 48.13 ? 139 GLU F O   1 
ATOM   11500 C CB  . GLU F 2 139 ? -34.491 -39.623 12.254  1.00 47.90 ? 139 GLU F CB  1 
ATOM   11501 C CG  . GLU F 2 139 ? -35.618 -40.572 12.653  1.00 48.27 ? 139 GLU F CG  1 
ATOM   11502 C CD  . GLU F 2 139 ? -36.411 -41.106 11.472  1.00 48.25 ? 139 GLU F CD  1 
ATOM   11503 O OE1 . GLU F 2 139 ? -37.656 -41.098 11.545  1.00 48.27 ? 139 GLU F OE1 1 
ATOM   11504 O OE2 . GLU F 2 139 ? -35.799 -41.542 10.474  1.00 49.00 ? 139 GLU F OE2 1 
ATOM   11505 N N   . PHE F 2 140 ? -32.951 -40.443 15.268  1.00 48.69 ? 140 PHE F N   1 
ATOM   11506 C CA  . PHE F 2 140 ? -32.068 -41.359 15.987  1.00 49.20 ? 140 PHE F CA  1 
ATOM   11507 C C   . PHE F 2 140 ? -32.084 -42.777 15.431  1.00 49.75 ? 140 PHE F C   1 
ATOM   11508 O O   . PHE F 2 140 ? -33.148 -43.362 15.208  1.00 49.60 ? 140 PHE F O   1 
ATOM   11509 C CB  . PHE F 2 140 ? -32.447 -41.409 17.468  1.00 49.12 ? 140 PHE F CB  1 
ATOM   11510 C CG  . PHE F 2 140 ? -32.070 -40.182 18.232  1.00 48.98 ? 140 PHE F CG  1 
ATOM   11511 C CD1 . PHE F 2 140 ? -30.763 -39.996 18.671  1.00 48.91 ? 140 PHE F CD1 1 
ATOM   11512 C CD2 . PHE F 2 140 ? -33.020 -39.214 18.526  1.00 48.74 ? 140 PHE F CD2 1 
ATOM   11513 C CE1 . PHE F 2 140 ? -30.408 -38.855 19.387  1.00 48.65 ? 140 PHE F CE1 1 
ATOM   11514 C CE2 . PHE F 2 140 ? -32.674 -38.071 19.241  1.00 48.36 ? 140 PHE F CE2 1 
ATOM   11515 C CZ  . PHE F 2 140 ? -31.367 -37.891 19.672  1.00 48.17 ? 140 PHE F CZ  1 
ATOM   11516 N N   . TYR F 2 141 ? -30.891 -43.329 15.230  1.00 50.56 ? 141 TYR F N   1 
ATOM   11517 C CA  . TYR F 2 141 ? -30.742 -44.739 14.889  1.00 51.39 ? 141 TYR F CA  1 
ATOM   11518 C C   . TYR F 2 141 ? -30.915 -45.645 16.117  1.00 52.28 ? 141 TYR F C   1 
ATOM   11519 O O   . TYR F 2 141 ? -30.585 -46.833 16.067  1.00 52.41 ? 141 TYR F O   1 
ATOM   11520 C CB  . TYR F 2 141 ? -29.382 -44.996 14.234  1.00 51.07 ? 141 TYR F CB  1 
ATOM   11521 C CG  . TYR F 2 141 ? -29.306 -44.631 12.770  1.00 50.49 ? 141 TYR F CG  1 
ATOM   11522 C CD1 . TYR F 2 141 ? -30.240 -45.123 11.856  1.00 49.74 ? 141 TYR F CD1 1 
ATOM   11523 C CD2 . TYR F 2 141 ? -28.284 -43.812 12.293  1.00 49.75 ? 141 TYR F CD2 1 
ATOM   11524 C CE1 . TYR F 2 141 ? -30.167 -44.794 10.509  1.00 49.22 ? 141 TYR F CE1 1 
ATOM   11525 C CE2 . TYR F 2 141 ? -28.202 -43.476 10.950  1.00 49.15 ? 141 TYR F CE2 1 
ATOM   11526 C CZ  . TYR F 2 141 ? -29.144 -43.972 10.062  1.00 49.01 ? 141 TYR F CZ  1 
ATOM   11527 O OH  . TYR F 2 141 ? -29.062 -43.648 8.729   1.00 48.35 ? 141 TYR F OH  1 
ATOM   11528 N N   . HIS F 2 142 ? -31.419 -45.080 17.214  1.00 53.30 ? 142 HIS F N   1 
ATOM   11529 C CA  . HIS F 2 142 ? -31.707 -45.850 18.426  1.00 54.46 ? 142 HIS F CA  1 
ATOM   11530 C C   . HIS F 2 142 ? -32.915 -45.310 19.189  1.00 55.59 ? 142 HIS F C   1 
ATOM   11531 O O   . HIS F 2 142 ? -33.550 -44.345 18.765  1.00 55.90 ? 142 HIS F O   1 
ATOM   11532 C CB  . HIS F 2 142 ? -30.473 -45.935 19.338  1.00 54.25 ? 142 HIS F CB  1 
ATOM   11533 C CG  . HIS F 2 142 ? -30.016 -44.615 19.882  1.00 53.49 ? 142 HIS F CG  1 
ATOM   11534 N ND1 . HIS F 2 142 ? -30.646 -43.984 20.935  1.00 52.77 ? 142 HIS F ND1 1 
ATOM   11535 C CD2 . HIS F 2 142 ? -28.978 -43.818 19.533  1.00 52.28 ? 142 HIS F CD2 1 
ATOM   11536 C CE1 . HIS F 2 142 ? -30.023 -42.849 21.200  1.00 52.45 ? 142 HIS F CE1 1 
ATOM   11537 N NE2 . HIS F 2 142 ? -29.007 -42.726 20.365  1.00 52.08 ? 142 HIS F NE2 1 
ATOM   11538 N N   . LYS F 2 143 ? -33.234 -45.950 20.309  1.00 56.99 ? 143 LYS F N   1 
ATOM   11539 C CA  . LYS F 2 143 ? -34.296 -45.486 21.190  1.00 58.48 ? 143 LYS F CA  1 
ATOM   11540 C C   . LYS F 2 143 ? -33.758 -44.344 22.061  1.00 59.27 ? 143 LYS F C   1 
ATOM   11541 O O   . LYS F 2 143 ? -32.725 -44.497 22.725  1.00 59.45 ? 143 LYS F O   1 
ATOM   11542 C CB  . LYS F 2 143 ? -34.810 -46.648 22.050  1.00 58.52 ? 143 LYS F CB  1 
ATOM   11543 C CG  . LYS F 2 143 ? -36.170 -46.421 22.703  1.00 59.44 ? 143 LYS F CG  1 
ATOM   11544 C CD  . LYS F 2 143 ? -36.566 -47.624 23.568  1.00 60.97 ? 143 LYS F CD  1 
ATOM   11545 C CE  . LYS F 2 143 ? -37.711 -47.295 24.529  1.00 61.93 ? 143 LYS F CE  1 
ATOM   11546 N NZ  . LYS F 2 143 ? -39.009 -47.064 23.826  1.00 62.41 ? 143 LYS F NZ  1 
ATOM   11547 N N   . CYS F 2 144 ? -34.444 -43.200 22.038  1.00 60.20 ? 144 CYS F N   1 
ATOM   11548 C CA  . CYS F 2 144 ? -34.018 -42.029 22.812  1.00 61.18 ? 144 CYS F CA  1 
ATOM   11549 C C   . CYS F 2 144 ? -35.104 -41.547 23.778  1.00 61.57 ? 144 CYS F C   1 
ATOM   11550 O O   . CYS F 2 144 ? -35.986 -40.760 23.417  1.00 61.61 ? 144 CYS F O   1 
ATOM   11551 C CB  . CYS F 2 144 ? -33.532 -40.900 21.890  1.00 61.28 ? 144 CYS F CB  1 
ATOM   11552 S SG  . CYS F 2 144 ? -32.732 -39.478 22.719  1.00 62.51 ? 144 CYS F SG  1 
ATOM   11553 N N   . ASP F 2 145 ? -35.017 -42.048 25.010  1.00 62.12 ? 145 ASP F N   1 
ATOM   11554 C CA  . ASP F 2 145 ? -35.941 -41.726 26.101  1.00 62.59 ? 145 ASP F CA  1 
ATOM   11555 C C   . ASP F 2 145 ? -35.858 -40.251 26.498  1.00 62.77 ? 145 ASP F C   1 
ATOM   11556 O O   . ASP F 2 145 ? -34.947 -39.547 26.068  1.00 62.89 ? 145 ASP F O   1 
ATOM   11557 C CB  . ASP F 2 145 ? -35.647 -42.626 27.313  1.00 62.69 ? 145 ASP F CB  1 
ATOM   11558 C CG  . ASP F 2 145 ? -34.154 -42.922 27.485  1.00 63.20 ? 145 ASP F CG  1 
ATOM   11559 O OD1 . ASP F 2 145 ? -33.578 -42.529 28.521  1.00 63.46 ? 145 ASP F OD1 1 
ATOM   11560 O OD2 . ASP F 2 145 ? -33.553 -43.545 26.580  1.00 63.92 ? 145 ASP F OD2 1 
ATOM   11561 N N   . ASN F 2 146 ? -36.807 -39.791 27.315  1.00 62.98 ? 146 ASN F N   1 
ATOM   11562 C CA  . ASN F 2 146 ? -36.847 -38.392 27.768  1.00 63.13 ? 146 ASN F CA  1 
ATOM   11563 C C   . ASN F 2 146 ? -35.551 -37.907 28.414  1.00 63.38 ? 146 ASN F C   1 
ATOM   11564 O O   . ASN F 2 146 ? -35.188 -36.736 28.282  1.00 63.39 ? 146 ASN F O   1 
ATOM   11565 C CB  . ASN F 2 146 ? -38.030 -38.146 28.713  1.00 63.04 ? 146 ASN F CB  1 
ATOM   11566 C CG  . ASN F 2 146 ? -39.340 -37.901 27.970  1.00 62.96 ? 146 ASN F CG  1 
ATOM   11567 O OD1 . ASN F 2 146 ? -39.388 -37.900 26.737  1.00 62.85 ? 146 ASN F OD1 1 
ATOM   11568 N ND2 . ASN F 2 146 ? -40.412 -37.690 28.725  1.00 62.45 ? 146 ASN F ND2 1 
ATOM   11569 N N   . GLU F 2 147 ? -34.861 -38.814 29.102  1.00 63.72 ? 147 GLU F N   1 
ATOM   11570 C CA  . GLU F 2 147 ? -33.580 -38.506 29.736  1.00 64.11 ? 147 GLU F CA  1 
ATOM   11571 C C   . GLU F 2 147 ? -32.433 -38.523 28.733  1.00 64.17 ? 147 GLU F C   1 
ATOM   11572 O O   . GLU F 2 147 ? -31.391 -37.907 28.963  1.00 64.16 ? 147 GLU F O   1 
ATOM   11573 C CB  . GLU F 2 147 ? -33.301 -39.465 30.898  1.00 64.21 ? 147 GLU F CB  1 
ATOM   11574 C CG  . GLU F 2 147 ? -33.890 -39.010 32.232  1.00 65.06 ? 147 GLU F CG  1 
ATOM   11575 C CD  . GLU F 2 147 ? -35.399 -39.192 32.319  1.00 66.24 ? 147 GLU F CD  1 
ATOM   11576 O OE1 . GLU F 2 147 ? -35.862 -40.354 32.386  1.00 67.05 ? 147 GLU F OE1 1 
ATOM   11577 O OE2 . GLU F 2 147 ? -36.121 -38.170 32.336  1.00 66.54 ? 147 GLU F OE2 1 
ATOM   11578 N N   . CYS F 2 148 ? -32.632 -39.238 27.629  1.00 64.39 ? 148 CYS F N   1 
ATOM   11579 C CA  . CYS F 2 148 ? -31.724 -39.187 26.486  1.00 64.68 ? 148 CYS F CA  1 
ATOM   11580 C C   . CYS F 2 148 ? -31.910 -37.855 25.753  1.00 65.01 ? 148 CYS F C   1 
ATOM   11581 O O   . CYS F 2 148 ? -30.936 -37.234 25.319  1.00 64.92 ? 148 CYS F O   1 
ATOM   11582 C CB  . CYS F 2 148 ? -31.990 -40.372 25.548  1.00 64.49 ? 148 CYS F CB  1 
ATOM   11583 S SG  . CYS F 2 148 ? -31.252 -40.270 23.888  1.00 64.46 ? 148 CYS F SG  1 
ATOM   11584 N N   . MET F 2 149 ? -33.166 -37.423 25.631  1.00 65.45 ? 149 MET F N   1 
ATOM   11585 C CA  . MET F 2 149 ? -33.508 -36.153 24.983  1.00 66.04 ? 149 MET F CA  1 
ATOM   11586 C C   . MET F 2 149 ? -32.959 -34.949 25.746  1.00 66.48 ? 149 MET F C   1 
ATOM   11587 O O   . MET F 2 149 ? -32.415 -34.021 25.144  1.00 66.49 ? 149 MET F O   1 
ATOM   11588 C CB  . MET F 2 149 ? -35.026 -36.017 24.805  1.00 65.98 ? 149 MET F CB  1 
ATOM   11589 C CG  . MET F 2 149 ? -35.613 -36.851 23.672  1.00 66.00 ? 149 MET F CG  1 
ATOM   11590 S SD  . MET F 2 149 ? -34.894 -36.479 22.058  1.00 66.12 ? 149 MET F SD  1 
ATOM   11591 C CE  . MET F 2 149 ? -35.862 -37.560 21.003  1.00 65.94 ? 149 MET F CE  1 
ATOM   11592 N N   . GLU F 2 150 ? -33.099 -34.974 27.071  1.00 66.92 ? 150 GLU F N   1 
ATOM   11593 C CA  . GLU F 2 150 ? -32.577 -33.907 27.922  1.00 67.23 ? 150 GLU F CA  1 
ATOM   11594 C C   . GLU F 2 150 ? -31.067 -34.017 28.096  1.00 67.14 ? 150 GLU F C   1 
ATOM   11595 O O   . GLU F 2 150 ? -30.442 -33.141 28.686  1.00 67.27 ? 150 GLU F O   1 
ATOM   11596 C CB  . GLU F 2 150 ? -33.286 -33.885 29.280  1.00 67.42 ? 150 GLU F CB  1 
ATOM   11597 C CG  . GLU F 2 150 ? -34.759 -33.480 29.196  1.00 68.45 ? 150 GLU F CG  1 
ATOM   11598 C CD  . GLU F 2 150 ? -35.289 -32.879 30.488  1.00 69.70 ? 150 GLU F CD  1 
ATOM   11599 O OE1 . GLU F 2 150 ? -34.943 -33.383 31.582  1.00 70.10 ? 150 GLU F OE1 1 
ATOM   11600 O OE2 . GLU F 2 150 ? -36.063 -31.899 30.405  1.00 69.79 ? 150 GLU F OE2 1 
ATOM   11601 N N   . SER F 2 151 ? -30.492 -35.095 27.571  1.00 67.17 ? 151 SER F N   1 
ATOM   11602 C CA  . SER F 2 151 ? -29.046 -35.292 27.577  1.00 67.21 ? 151 SER F CA  1 
ATOM   11603 C C   . SER F 2 151 ? -28.373 -34.388 26.542  1.00 67.21 ? 151 SER F C   1 
ATOM   11604 O O   . SER F 2 151 ? -27.355 -33.759 26.835  1.00 67.14 ? 151 SER F O   1 
ATOM   11605 C CB  . SER F 2 151 ? -28.705 -36.771 27.334  1.00 67.22 ? 151 SER F CB  1 
ATOM   11606 O OG  . SER F 2 151 ? -27.335 -36.958 27.019  1.00 67.20 ? 151 SER F OG  1 
ATOM   11607 N N   . VAL F 2 152 ? -28.949 -34.330 25.341  1.00 67.29 ? 152 VAL F N   1 
ATOM   11608 C CA  . VAL F 2 152 ? -28.434 -33.477 24.262  1.00 67.38 ? 152 VAL F CA  1 
ATOM   11609 C C   . VAL F 2 152 ? -28.797 -32.004 24.453  1.00 67.40 ? 152 VAL F C   1 
ATOM   11610 O O   . VAL F 2 152 ? -28.038 -31.119 24.053  1.00 67.29 ? 152 VAL F O   1 
ATOM   11611 C CB  . VAL F 2 152 ? -28.890 -33.949 22.857  1.00 67.41 ? 152 VAL F CB  1 
ATOM   11612 C CG1 . VAL F 2 152 ? -27.913 -34.958 22.293  1.00 67.44 ? 152 VAL F CG1 1 
ATOM   11613 C CG2 . VAL F 2 152 ? -30.299 -34.520 22.896  1.00 67.47 ? 152 VAL F CG2 1 
ATOM   11614 N N   . LYS F 2 153 ? -29.956 -31.759 25.064  1.00 67.54 ? 153 LYS F N   1 
ATOM   11615 C CA  . LYS F 2 153 ? -30.402 -30.413 25.430  1.00 67.76 ? 153 LYS F CA  1 
ATOM   11616 C C   . LYS F 2 153 ? -29.528 -29.811 26.533  1.00 68.15 ? 153 LYS F C   1 
ATOM   11617 O O   . LYS F 2 153 ? -29.272 -28.606 26.539  1.00 68.14 ? 153 LYS F O   1 
ATOM   11618 C CB  . LYS F 2 153 ? -31.865 -30.439 25.878  1.00 67.61 ? 153 LYS F CB  1 
ATOM   11619 C CG  . LYS F 2 153 ? -32.862 -30.669 24.752  1.00 67.22 ? 153 LYS F CG  1 
ATOM   11620 C CD  . LYS F 2 153 ? -34.207 -31.186 25.257  1.00 66.85 ? 153 LYS F CD  1 
ATOM   11621 C CE  . LYS F 2 153 ? -34.955 -30.156 26.086  1.00 66.79 ? 153 LYS F CE  1 
ATOM   11622 N NZ  . LYS F 2 153 ? -36.209 -30.724 26.645  1.00 66.70 ? 153 LYS F NZ  1 
ATOM   11623 N N   . ASN F 2 154 ? -29.086 -30.659 27.463  1.00 68.62 ? 154 ASN F N   1 
ATOM   11624 C CA  . ASN F 2 154 ? -28.136 -30.272 28.509  1.00 69.03 ? 154 ASN F CA  1 
ATOM   11625 C C   . ASN F 2 154 ? -26.707 -30.185 27.956  1.00 69.19 ? 154 ASN F C   1 
ATOM   11626 O O   . ASN F 2 154 ? -25.852 -29.512 28.533  1.00 69.25 ? 154 ASN F O   1 
ATOM   11627 C CB  . ASN F 2 154 ? -28.206 -31.262 29.684  1.00 69.09 ? 154 ASN F CB  1 
ATOM   11628 C CG  . ASN F 2 154 ? -27.654 -30.689 30.989  1.00 69.51 ? 154 ASN F CG  1 
ATOM   11629 O OD1 . ASN F 2 154 ? -26.845 -31.329 31.665  1.00 69.63 ? 154 ASN F OD1 1 
ATOM   11630 N ND2 . ASN F 2 154 ? -28.105 -29.493 31.357  1.00 69.92 ? 154 ASN F ND2 1 
ATOM   11631 N N   . GLY F 2 155 ? -26.465 -30.869 26.837  1.00 69.39 ? 155 GLY F N   1 
ATOM   11632 C CA  . GLY F 2 155 ? -25.167 -30.853 26.156  1.00 69.80 ? 155 GLY F CA  1 
ATOM   11633 C C   . GLY F 2 155 ? -24.222 -31.984 26.533  1.00 70.07 ? 155 GLY F C   1 
ATOM   11634 O O   . GLY F 2 155 ? -23.045 -31.963 26.166  1.00 70.00 ? 155 GLY F O   1 
ATOM   11635 N N   . THR F 2 156 ? -24.740 -32.977 27.253  1.00 70.40 ? 156 THR F N   1 
ATOM   11636 C CA  . THR F 2 156 ? -23.923 -34.070 27.791  1.00 70.76 ? 156 THR F CA  1 
ATOM   11637 C C   . THR F 2 156 ? -24.385 -35.441 27.286  1.00 70.94 ? 156 THR F C   1 
ATOM   11638 O O   . THR F 2 156 ? -25.042 -36.196 28.011  1.00 70.94 ? 156 THR F O   1 
ATOM   11639 C CB  . THR F 2 156 ? -23.919 -34.052 29.337  1.00 70.73 ? 156 THR F CB  1 
ATOM   11640 O OG1 . THR F 2 156 ? -25.256 -33.851 29.813  1.00 70.74 ? 156 THR F OG1 1 
ATOM   11641 C CG2 . THR F 2 156 ? -23.027 -32.930 29.862  1.00 70.93 ? 156 THR F CG2 1 
ATOM   11642 N N   . TYR F 2 157 ? -24.023 -35.754 26.043  1.00 71.12 ? 157 TYR F N   1 
ATOM   11643 C CA  . TYR F 2 157 ? -24.483 -36.968 25.371  1.00 71.23 ? 157 TYR F CA  1 
ATOM   11644 C C   . TYR F 2 157 ? -23.371 -38.001 25.233  1.00 71.67 ? 157 TYR F C   1 
ATOM   11645 O O   . TYR F 2 157 ? -22.224 -37.659 24.932  1.00 71.71 ? 157 TYR F O   1 
ATOM   11646 C CB  . TYR F 2 157 ? -25.061 -36.614 23.996  1.00 71.03 ? 157 TYR F CB  1 
ATOM   11647 C CG  . TYR F 2 157 ? -25.517 -37.788 23.149  1.00 70.09 ? 157 TYR F CG  1 
ATOM   11648 C CD1 . TYR F 2 157 ? -26.790 -38.334 23.302  1.00 69.56 ? 157 TYR F CD1 1 
ATOM   11649 C CD2 . TYR F 2 157 ? -24.682 -38.335 22.176  1.00 69.30 ? 157 TYR F CD2 1 
ATOM   11650 C CE1 . TYR F 2 157 ? -27.213 -39.406 22.517  1.00 68.80 ? 157 TYR F CE1 1 
ATOM   11651 C CE2 . TYR F 2 157 ? -25.095 -39.402 21.387  1.00 68.71 ? 157 TYR F CE2 1 
ATOM   11652 C CZ  . TYR F 2 157 ? -26.360 -39.932 21.562  1.00 68.47 ? 157 TYR F CZ  1 
ATOM   11653 O OH  . TYR F 2 157 ? -26.768 -40.988 20.780  1.00 68.41 ? 157 TYR F OH  1 
ATOM   11654 N N   . ASP F 2 158 ? -23.734 -39.264 25.444  1.00 72.13 ? 158 ASP F N   1 
ATOM   11655 C CA  . ASP F 2 158 ? -22.810 -40.392 25.325  1.00 72.54 ? 158 ASP F CA  1 
ATOM   11656 C C   . ASP F 2 158 ? -22.844 -41.036 23.938  1.00 72.69 ? 158 ASP F C   1 
ATOM   11657 O O   . ASP F 2 158 ? -23.714 -41.869 23.655  1.00 72.70 ? 158 ASP F O   1 
ATOM   11658 C CB  . ASP F 2 158 ? -23.138 -41.448 26.385  1.00 72.61 ? 158 ASP F CB  1 
ATOM   11659 C CG  . ASP F 2 158 ? -22.058 -41.586 27.443  1.00 72.87 ? 158 ASP F CG  1 
ATOM   11660 O OD1 . ASP F 2 158 ? -20.861 -41.412 27.121  1.00 73.15 ? 158 ASP F OD1 1 
ATOM   11661 O OD2 . ASP F 2 158 ? -22.414 -41.896 28.599  1.00 73.02 ? 158 ASP F OD2 1 
ATOM   11662 N N   . TYR F 2 159 ? -21.899 -40.655 23.080  1.00 72.88 ? 159 TYR F N   1 
ATOM   11663 C CA  . TYR F 2 159 ? -21.789 -41.268 21.754  1.00 73.12 ? 159 TYR F CA  1 
ATOM   11664 C C   . TYR F 2 159 ? -21.392 -42.748 21.819  1.00 73.22 ? 159 TYR F C   1 
ATOM   11665 O O   . TYR F 2 159 ? -22.010 -43.567 21.136  1.00 73.30 ? 159 TYR F O   1 
ATOM   11666 C CB  . TYR F 2 159 ? -20.834 -40.492 20.834  1.00 73.21 ? 159 TYR F CB  1 
ATOM   11667 C CG  . TYR F 2 159 ? -20.461 -41.241 19.562  1.00 73.59 ? 159 TYR F CG  1 
ATOM   11668 C CD1 . TYR F 2 159 ? -21.332 -41.282 18.470  1.00 73.68 ? 159 TYR F CD1 1 
ATOM   11669 C CD2 . TYR F 2 159 ? -19.240 -41.915 19.455  1.00 73.77 ? 159 TYR F CD2 1 
ATOM   11670 C CE1 . TYR F 2 159 ? -20.995 -41.971 17.305  1.00 73.53 ? 159 TYR F CE1 1 
ATOM   11671 C CE2 . TYR F 2 159 ? -18.895 -42.607 18.292  1.00 73.66 ? 159 TYR F CE2 1 
ATOM   11672 C CZ  . TYR F 2 159 ? -19.778 -42.630 17.224  1.00 73.53 ? 159 TYR F CZ  1 
ATOM   11673 O OH  . TYR F 2 159 ? -19.443 -43.308 16.075  1.00 73.53 ? 159 TYR F OH  1 
ATOM   11674 N N   . PRO F 2 160 ? -20.358 -43.095 22.623  1.00 73.28 ? 160 PRO F N   1 
ATOM   11675 C CA  . PRO F 2 160 ? -19.962 -44.509 22.691  1.00 73.16 ? 160 PRO F CA  1 
ATOM   11676 C C   . PRO F 2 160 ? -20.999 -45.425 23.356  1.00 72.95 ? 160 PRO F C   1 
ATOM   11677 O O   . PRO F 2 160 ? -21.156 -46.569 22.927  1.00 72.94 ? 160 PRO F O   1 
ATOM   11678 C CB  . PRO F 2 160 ? -18.658 -44.474 23.507  1.00 73.21 ? 160 PRO F CB  1 
ATOM   11679 C CG  . PRO F 2 160 ? -18.151 -43.070 23.358  1.00 73.30 ? 160 PRO F CG  1 
ATOM   11680 C CD  . PRO F 2 160 ? -19.400 -42.240 23.353  1.00 73.30 ? 160 PRO F CD  1 
ATOM   11681 N N   . GLN F 2 161 ? -21.710 -44.929 24.369  1.00 72.66 ? 161 GLN F N   1 
ATOM   11682 C CA  . GLN F 2 161 ? -22.675 -45.760 25.100  1.00 72.45 ? 161 GLN F CA  1 
ATOM   11683 C C   . GLN F 2 161 ? -23.904 -46.131 24.257  1.00 72.26 ? 161 GLN F C   1 
ATOM   11684 O O   . GLN F 2 161 ? -24.640 -47.059 24.596  1.00 72.32 ? 161 GLN F O   1 
ATOM   11685 C CB  . GLN F 2 161 ? -23.066 -45.109 26.441  1.00 72.50 ? 161 GLN F CB  1 
ATOM   11686 C CG  . GLN F 2 161 ? -24.467 -44.485 26.518  1.00 72.65 ? 161 GLN F CG  1 
ATOM   11687 C CD  . GLN F 2 161 ? -25.439 -45.274 27.392  1.00 72.87 ? 161 GLN F CD  1 
ATOM   11688 O OE1 . GLN F 2 161 ? -26.113 -44.707 28.254  1.00 72.60 ? 161 GLN F OE1 1 
ATOM   11689 N NE2 . GLN F 2 161 ? -25.515 -46.582 27.171  1.00 73.19 ? 161 GLN F NE2 1 
ATOM   11690 N N   . TYR F 2 162 ? -24.108 -45.417 23.153  1.00 72.00 ? 162 TYR F N   1 
ATOM   11691 C CA  . TYR F 2 162 ? -25.229 -45.694 22.258  1.00 71.70 ? 162 TYR F CA  1 
ATOM   11692 C C   . TYR F 2 162 ? -24.802 -46.285 20.911  1.00 71.68 ? 162 TYR F C   1 
ATOM   11693 O O   . TYR F 2 162 ? -25.634 -46.824 20.177  1.00 71.57 ? 162 TYR F O   1 
ATOM   11694 C CB  . TYR F 2 162 ? -26.074 -44.432 22.042  1.00 71.62 ? 162 TYR F CB  1 
ATOM   11695 C CG  . TYR F 2 162 ? -27.087 -44.161 23.134  1.00 70.95 ? 162 TYR F CG  1 
ATOM   11696 C CD1 . TYR F 2 162 ? -28.240 -44.938 23.250  1.00 70.38 ? 162 TYR F CD1 1 
ATOM   11697 C CD2 . TYR F 2 162 ? -26.899 -43.121 24.043  1.00 70.42 ? 162 TYR F CD2 1 
ATOM   11698 C CE1 . TYR F 2 162 ? -29.174 -44.691 24.248  1.00 70.15 ? 162 TYR F CE1 1 
ATOM   11699 C CE2 . TYR F 2 162 ? -27.828 -42.864 25.045  1.00 70.11 ? 162 TYR F CE2 1 
ATOM   11700 C CZ  . TYR F 2 162 ? -28.963 -43.654 25.141  1.00 70.21 ? 162 TYR F CZ  1 
ATOM   11701 O OH  . TYR F 2 162 ? -29.889 -43.406 26.129  1.00 70.28 ? 162 TYR F OH  1 
ATOM   11702 N N   . SER F 2 163 ? -23.510 -46.194 20.597  1.00 71.70 ? 163 SER F N   1 
ATOM   11703 C CA  . SER F 2 163 ? -22.989 -46.619 19.290  1.00 71.93 ? 163 SER F CA  1 
ATOM   11704 C C   . SER F 2 163 ? -23.221 -48.099 18.975  1.00 72.13 ? 163 SER F C   1 
ATOM   11705 O O   . SER F 2 163 ? -23.017 -48.535 17.838  1.00 72.14 ? 163 SER F O   1 
ATOM   11706 C CB  . SER F 2 163 ? -21.503 -46.263 19.148  1.00 71.91 ? 163 SER F CB  1 
ATOM   11707 O OG  . SER F 2 163 ? -20.744 -46.750 20.240  1.00 71.98 ? 163 SER F OG  1 
ATOM   11708 N N   . GLU F 2 164 ? -23.660 -48.853 19.985  1.00 72.29 ? 164 GLU F N   1 
ATOM   11709 C CA  . GLU F 2 164 ? -23.942 -50.281 19.855  1.00 72.36 ? 164 GLU F CA  1 
ATOM   11710 C C   . GLU F 2 164 ? -25.180 -50.552 18.994  1.00 72.24 ? 164 GLU F C   1 
ATOM   11711 O O   . GLU F 2 164 ? -25.056 -51.039 17.870  1.00 72.14 ? 164 GLU F O   1 
ATOM   11712 C CB  . GLU F 2 164 ? -24.094 -50.924 21.238  1.00 72.50 ? 164 GLU F CB  1 
ATOM   11713 C CG  . GLU F 2 164 ? -24.091 -52.456 21.224  1.00 73.14 ? 164 GLU F CG  1 
ATOM   11714 C CD  . GLU F 2 164 ? -24.815 -53.068 22.418  1.00 74.01 ? 164 GLU F CD  1 
ATOM   11715 O OE1 . GLU F 2 164 ? -25.069 -52.345 23.407  1.00 74.40 ? 164 GLU F OE1 1 
ATOM   11716 O OE2 . GLU F 2 164 ? -25.133 -54.278 22.368  1.00 74.25 ? 164 GLU F OE2 1 
ATOM   11717 N N   . GLU F 2 165 ? -26.365 -50.236 19.520  1.00 72.18 ? 165 GLU F N   1 
ATOM   11718 C CA  . GLU F 2 165 ? -27.624 -50.479 18.798  1.00 72.20 ? 165 GLU F CA  1 
ATOM   11719 C C   . GLU F 2 165 ? -27.790 -49.588 17.566  1.00 72.22 ? 165 GLU F C   1 
ATOM   11720 O O   . GLU F 2 165 ? -28.510 -49.942 16.630  1.00 72.23 ? 165 GLU F O   1 
ATOM   11721 C CB  . GLU F 2 165 ? -28.846 -50.363 19.726  1.00 72.18 ? 165 GLU F CB  1 
ATOM   11722 C CG  . GLU F 2 165 ? -28.931 -49.078 20.547  1.00 72.30 ? 165 GLU F CG  1 
ATOM   11723 C CD  . GLU F 2 165 ? -30.264 -48.914 21.274  1.00 72.48 ? 165 GLU F CD  1 
ATOM   11724 O OE1 . GLU F 2 165 ? -31.292 -49.434 20.789  1.00 72.08 ? 165 GLU F OE1 1 
ATOM   11725 O OE2 . GLU F 2 165 ? -30.286 -48.244 22.329  1.00 72.63 ? 165 GLU F OE2 1 
ATOM   11726 N N   . ALA F 2 166 ? -27.112 -48.441 17.578  1.00 72.25 ? 166 ALA F N   1 
ATOM   11727 C CA  . ALA F 2 166 ? -27.138 -47.498 16.468  1.00 72.16 ? 166 ALA F CA  1 
ATOM   11728 C C   . ALA F 2 166 ? -26.523 -48.099 15.205  1.00 72.16 ? 166 ALA F C   1 
ATOM   11729 O O   . ALA F 2 166 ? -27.167 -48.123 14.157  1.00 72.14 ? 166 ALA F O   1 
ATOM   11730 C CB  . ALA F 2 166 ? -26.431 -46.206 16.853  1.00 72.18 ? 166 ALA F CB  1 
ATOM   11731 N N   . ARG F 2 167 ? -25.290 -48.595 15.317  1.00 72.27 ? 167 ARG F N   1 
ATOM   11732 C CA  . ARG F 2 167 ? -24.583 -49.214 14.188  1.00 72.36 ? 167 ARG F CA  1 
ATOM   11733 C C   . ARG F 2 167 ? -25.367 -50.395 13.603  1.00 72.30 ? 167 ARG F C   1 
ATOM   11734 O O   . ARG F 2 167 ? -25.393 -50.587 12.387  1.00 72.31 ? 167 ARG F O   1 
ATOM   11735 C CB  . ARG F 2 167 ? -23.163 -49.649 14.596  1.00 72.44 ? 167 ARG F CB  1 
ATOM   11736 C CG  . ARG F 2 167 ? -23.111 -50.909 15.459  1.00 72.99 ? 167 ARG F CG  1 
ATOM   11737 C CD  . ARG F 2 167 ? -21.752 -51.153 16.101  1.00 73.95 ? 167 ARG F CD  1 
ATOM   11738 N NE  . ARG F 2 167 ? -21.903 -51.875 17.368  1.00 74.08 ? 167 ARG F NE  1 
ATOM   11739 C CZ  . ARG F 2 167 ? -20.927 -52.513 18.008  1.00 73.92 ? 167 ARG F CZ  1 
ATOM   11740 N NH1 . ARG F 2 167 ? -19.697 -52.546 17.510  1.00 73.88 ? 167 ARG F NH1 1 
ATOM   11741 N NH2 . ARG F 2 167 ? -21.187 -53.131 19.153  1.00 73.80 ? 167 ARG F NH2 1 
ATOM   11742 N N   . LEU F 2 168 ? -26.011 -51.164 14.482  1.00 72.15 ? 168 LEU F N   1 
ATOM   11743 C CA  . LEU F 2 168 ? -26.781 -52.349 14.104  1.00 72.03 ? 168 LEU F CA  1 
ATOM   11744 C C   . LEU F 2 168 ? -27.965 -51.971 13.215  1.00 71.86 ? 168 LEU F C   1 
ATOM   11745 O O   . LEU F 2 168 ? -28.197 -52.595 12.176  1.00 71.84 ? 168 LEU F O   1 
ATOM   11746 C CB  . LEU F 2 168 ? -27.249 -53.089 15.367  1.00 72.09 ? 168 LEU F CB  1 
ATOM   11747 C CG  . LEU F 2 168 ? -27.782 -54.524 15.294  1.00 72.26 ? 168 LEU F CG  1 
ATOM   11748 C CD1 . LEU F 2 168 ? -27.300 -55.329 16.496  1.00 72.08 ? 168 LEU F CD1 1 
ATOM   11749 C CD2 . LEU F 2 168 ? -29.308 -54.560 15.193  1.00 72.33 ? 168 LEU F CD2 1 
ATOM   11750 N N   . ASN F 2 169 ? -28.698 -50.939 13.628  1.00 71.66 ? 169 ASN F N   1 
ATOM   11751 C CA  . ASN F 2 169 ? -29.837 -50.436 12.868  1.00 71.48 ? 169 ASN F CA  1 
ATOM   11752 C C   . ASN F 2 169 ? -29.413 -49.737 11.578  1.00 71.49 ? 169 ASN F C   1 
ATOM   11753 O O   . ASN F 2 169 ? -30.032 -49.929 10.535  1.00 71.39 ? 169 ASN F O   1 
ATOM   11754 C CB  . ASN F 2 169 ? -30.683 -49.498 13.730  1.00 71.42 ? 169 ASN F CB  1 
ATOM   11755 C CG  . ASN F 2 169 ? -31.333 -50.208 14.907  1.00 71.11 ? 169 ASN F CG  1 
ATOM   11756 O OD1 . ASN F 2 169 ? -32.012 -51.222 14.740  1.00 70.87 ? 169 ASN F OD1 1 
ATOM   11757 N ND2 . ASN F 2 169 ? -31.137 -49.669 16.103  1.00 70.46 ? 169 ASN F ND2 1 
ATOM   11758 N N   . ARG F 2 170 ? -28.346 -48.944 11.659  1.00 71.54 ? 170 ARG F N   1 
ATOM   11759 C CA  . ARG F 2 170 ? -27.842 -48.171 10.521  1.00 71.70 ? 170 ARG F CA  1 
ATOM   11760 C C   . ARG F 2 170 ? -27.355 -49.061 9.373   1.00 71.96 ? 170 ARG F C   1 
ATOM   11761 O O   . ARG F 2 170 ? -27.545 -48.728 8.198   1.00 71.88 ? 170 ARG F O   1 
ATOM   11762 C CB  . ARG F 2 170 ? -26.715 -47.237 10.980  1.00 71.57 ? 170 ARG F CB  1 
ATOM   11763 C CG  . ARG F 2 170 ? -26.234 -46.220 9.940   1.00 71.01 ? 170 ARG F CG  1 
ATOM   11764 C CD  . ARG F 2 170 ? -24.778 -45.847 10.175  1.00 70.18 ? 170 ARG F CD  1 
ATOM   11765 N NE  . ARG F 2 170 ? -24.490 -45.650 11.595  1.00 69.73 ? 170 ARG F NE  1 
ATOM   11766 C CZ  . ARG F 2 170 ? -23.380 -46.057 12.205  1.00 69.21 ? 170 ARG F CZ  1 
ATOM   11767 N NH1 . ARG F 2 170 ? -22.435 -46.696 11.526  1.00 68.93 ? 170 ARG F NH1 1 
ATOM   11768 N NH2 . ARG F 2 170 ? -23.219 -45.833 13.502  1.00 68.90 ? 170 ARG F NH2 1 
ATOM   11769 N N   . GLU F 2 171 ? -26.728 -50.184 9.721   1.00 72.34 ? 171 GLU F N   1 
ATOM   11770 C CA  . GLU F 2 171 ? -26.207 -51.128 8.732   1.00 72.75 ? 171 GLU F CA  1 
ATOM   11771 C C   . GLU F 2 171 ? -27.329 -51.831 7.972   1.00 72.84 ? 171 GLU F C   1 
ATOM   11772 O O   . GLU F 2 171 ? -27.151 -52.232 6.821   1.00 72.83 ? 171 GLU F O   1 
ATOM   11773 C CB  . GLU F 2 171 ? -25.289 -52.163 9.395   1.00 72.88 ? 171 GLU F CB  1 
ATOM   11774 C CG  . GLU F 2 171 ? -23.930 -51.621 9.856   1.00 73.54 ? 171 GLU F CG  1 
ATOM   11775 C CD  . GLU F 2 171 ? -22.977 -51.310 8.707   1.00 74.55 ? 171 GLU F CD  1 
ATOM   11776 O OE1 . GLU F 2 171 ? -22.642 -50.119 8.516   1.00 74.86 ? 171 GLU F OE1 1 
ATOM   11777 O OE2 . GLU F 2 171 ? -22.563 -52.255 7.998   1.00 74.81 ? 171 GLU F OE2 1 
ATOM   11778 N N   . GLU F 2 172 ? -28.482 -51.967 8.624   1.00 73.06 ? 172 GLU F N   1 
ATOM   11779 C CA  . GLU F 2 172 ? -29.646 -52.624 8.030   1.00 73.40 ? 172 GLU F CA  1 
ATOM   11780 C C   . GLU F 2 172 ? -30.615 -51.643 7.358   1.00 73.48 ? 172 GLU F C   1 
ATOM   11781 O O   . GLU F 2 172 ? -31.263 -51.992 6.370   1.00 73.48 ? 172 GLU F O   1 
ATOM   11782 C CB  . GLU F 2 172 ? -30.366 -53.489 9.072   1.00 73.43 ? 172 GLU F CB  1 
ATOM   11783 C CG  . GLU F 2 172 ? -29.607 -54.773 9.439   1.00 73.77 ? 172 GLU F CG  1 
ATOM   11784 C CD  . GLU F 2 172 ? -29.965 -55.322 10.821  1.00 74.37 ? 172 GLU F CD  1 
ATOM   11785 O OE1 . GLU F 2 172 ? -30.605 -54.601 11.622  1.00 74.19 ? 172 GLU F OE1 1 
ATOM   11786 O OE2 . GLU F 2 172 ? -29.596 -56.484 11.107  1.00 74.38 ? 172 GLU F OE2 1 
ATOM   11787 N N   . ILE F 2 173 ? -30.702 -50.422 7.887   1.00 73.65 ? 173 ILE F N   1 
ATOM   11788 C CA  . ILE F 2 173 ? -31.572 -49.379 7.324   1.00 73.78 ? 173 ILE F CA  1 
ATOM   11789 C C   . ILE F 2 173 ? -30.989 -48.783 6.035   1.00 73.82 ? 173 ILE F C   1 
ATOM   11790 O O   . ILE F 2 173 ? -29.929 -48.154 6.042   1.00 73.86 ? 173 ILE F O   1 
ATOM   11791 C CB  . ILE F 2 173 ? -31.902 -48.263 8.368   1.00 73.78 ? 173 ILE F CB  1 
ATOM   11792 C CG1 . ILE F 2 173 ? -32.844 -48.811 9.450   1.00 73.83 ? 173 ILE F CG1 1 
ATOM   11793 C CG2 . ILE F 2 173 ? -32.518 -47.030 7.690   1.00 73.75 ? 173 ILE F CG2 1 
ATOM   11794 C CD1 . ILE F 2 173 ? -32.955 -47.949 10.699  1.00 73.82 ? 173 ILE F CD1 1 
HETATM 11795 C C1  . NAG G 3 .   ? -14.003 -3.582  32.437  1.00 20.00 ? 1   NAG A C1  1 
HETATM 11796 C C2  . NAG G 3 .   ? -14.963 -2.886  33.305  1.00 20.00 ? 1   NAG A C2  1 
HETATM 11797 C C3  . NAG G 3 .   ? -14.165 -1.632  33.522  1.00 20.00 ? 1   NAG A C3  1 
HETATM 11798 C C4  . NAG G 3 .   ? -12.840 -1.939  34.190  1.00 20.00 ? 1   NAG A C4  1 
HETATM 11799 C C5  . NAG G 3 .   ? -12.222 -3.249  33.751  1.00 20.00 ? 1   NAG A C5  1 
HETATM 11800 C C6  . NAG G 3 .   ? -11.252 -3.802  34.786  1.00 20.00 ? 1   NAG A C6  1 
HETATM 11801 C C7  . NAG G 3 .   ? -17.217 -3.293  32.478  1.00 20.00 ? 1   NAG A C7  1 
HETATM 11802 C C8  . NAG G 3 .   ? -18.259 -2.724  31.591  1.00 20.00 ? 1   NAG A C8  1 
HETATM 11803 N N2  . NAG G 3 .   ? -16.121 -2.586  32.530  1.00 20.00 ? 1   NAG A N2  1 
HETATM 11804 O O3  . NAG G 3 .   ? -14.892 -0.716  34.285  1.00 20.00 ? 1   NAG A O3  1 
HETATM 11805 O O4  . NAG G 3 .   ? -11.926 -0.939  33.842  1.00 20.00 ? 1   NAG A O4  1 
HETATM 11806 O O5  . NAG G 3 .   ? -13.230 -4.157  33.436  1.00 20.00 ? 1   NAG A O5  1 
HETATM 11807 O O6  . NAG G 3 .   ? -9.990  -3.207  34.578  1.00 20.00 ? 1   NAG A O6  1 
HETATM 11808 O O7  . NAG G 3 .   ? -17.410 -4.325  33.070  1.00 20.00 ? 1   NAG A O7  1 
HETATM 11809 C C1  . NAG H 3 .   ? 7.741   56.424  -0.160  1.00 51.42 ? 2   NAG A C1  1 
HETATM 11810 C C2  . NAG H 3 .   ? 6.687   57.018  -1.097  1.00 52.72 ? 2   NAG A C2  1 
HETATM 11811 C C3  . NAG H 3 .   ? 6.764   56.449  -2.509  1.00 53.87 ? 2   NAG A C3  1 
HETATM 11812 C C4  . NAG H 3 .   ? 8.193   56.385  -3.053  1.00 55.37 ? 2   NAG A C4  1 
HETATM 11813 C C5  . NAG H 3 .   ? 9.129   55.810  -1.982  1.00 54.37 ? 2   NAG A C5  1 
HETATM 11814 C C6  . NAG H 3 .   ? 10.593  55.698  -2.427  1.00 54.47 ? 2   NAG A C6  1 
HETATM 11815 C C7  . NAG H 3 .   ? 4.479   57.751  -0.364  1.00 51.70 ? 2   NAG A C7  1 
HETATM 11816 C C8  . NAG H 3 .   ? 3.123   57.295  0.080   1.00 51.50 ? 2   NAG A C8  1 
HETATM 11817 N N2  . NAG H 3 .   ? 5.339   56.771  -0.638  1.00 52.12 ? 2   NAG A N2  1 
HETATM 11818 O O3  . NAG H 3 .   ? 5.956   57.242  -3.350  1.00 53.92 ? 2   NAG A O3  1 
HETATM 11819 O O4  . NAG H 3 .   ? 8.181   55.550  -4.191  1.00 57.98 ? 2   NAG A O4  1 
HETATM 11820 O O5  . NAG H 3 .   ? 9.009   56.564  -0.784  1.00 53.18 ? 2   NAG A O5  1 
HETATM 11821 O O6  . NAG H 3 .   ? 11.157  56.957  -2.729  1.00 54.80 ? 2   NAG A O6  1 
HETATM 11822 O O7  . NAG H 3 .   ? 4.741   58.954  -0.440  1.00 50.60 ? 2   NAG A O7  1 
HETATM 11823 C C1  . NAG I 3 .   ? 8.479   56.255  -5.412  1.00 59.77 ? 327 NAG A C1  1 
HETATM 11824 C C2  . NAG I 3 .   ? 8.708   55.185  -6.478  1.00 60.89 ? 327 NAG A C2  1 
HETATM 11825 C C3  . NAG I 3 .   ? 8.966   55.803  -7.853  1.00 61.48 ? 327 NAG A C3  1 
HETATM 11826 C C4  . NAG I 3 .   ? 7.877   56.826  -8.182  1.00 61.73 ? 327 NAG A C4  1 
HETATM 11827 C C5  . NAG I 3 .   ? 7.738   57.825  -7.029  1.00 61.36 ? 327 NAG A C5  1 
HETATM 11828 C C6  . NAG I 3 .   ? 6.644   58.850  -7.296  1.00 61.81 ? 327 NAG A C6  1 
HETATM 11829 C C7  . NAG I 3 .   ? 9.571   53.084  -5.579  1.00 61.60 ? 327 NAG A C7  1 
HETATM 11830 C C8  . NAG I 3 .   ? 10.797  52.307  -5.192  1.00 61.49 ? 327 NAG A C8  1 
HETATM 11831 N N2  . NAG I 3 .   ? 9.792   54.309  -6.063  1.00 61.42 ? 327 NAG A N2  1 
HETATM 11832 O O3  . NAG I 3 .   ? 8.977   54.788  -8.831  1.00 61.80 ? 327 NAG A O3  1 
HETATM 11833 O O4  . NAG I 3 .   ? 8.173   57.502  -9.389  1.00 62.18 ? 327 NAG A O4  1 
HETATM 11834 O O5  . NAG I 3 .   ? 7.451   57.137  -5.825  1.00 60.51 ? 327 NAG A O5  1 
HETATM 11835 O O6  . NAG I 3 .   ? 7.138   59.783  -8.231  1.00 62.40 ? 327 NAG A O6  1 
HETATM 11836 O O7  . NAG I 3 .   ? 8.447   52.588  -5.445  1.00 61.17 ? 327 NAG A O7  1 
HETATM 11837 C C1  . GOL J 4 .   ? -12.333 -0.372  22.803  1.00 53.79 ? 328 GOL A C1  1 
HETATM 11838 O O1  . GOL J 4 .   ? -11.290 -1.311  22.957  1.00 52.92 ? 328 GOL A O1  1 
HETATM 11839 C C2  . GOL J 4 .   ? -11.978 0.958   23.461  1.00 54.48 ? 328 GOL A C2  1 
HETATM 11840 O O2  . GOL J 4 .   ? -11.215 0.715   24.619  1.00 54.72 ? 328 GOL A O2  1 
HETATM 11841 C C3  . GOL J 4 .   ? -13.244 1.726   23.844  1.00 55.15 ? 328 GOL A C3  1 
HETATM 11842 O O3  . GOL J 4 .   ? -13.853 2.297   22.698  1.00 56.13 ? 328 GOL A O3  1 
HETATM 11843 C C   . TAM K 5 .   ? 7.908   56.623  45.776  1.00 50.84 ? 329 TAM A C   1 
HETATM 11844 C C1  . TAM K 5 .   ? 6.935   57.257  44.765  1.00 50.86 ? 329 TAM A C1  1 
HETATM 11845 C C2  . TAM K 5 .   ? 9.340   56.567  45.236  1.00 50.88 ? 329 TAM A C2  1 
HETATM 11846 C C3  . TAM K 5 .   ? 7.401   55.225  46.168  1.00 50.80 ? 329 TAM A C3  1 
HETATM 11847 C C4  . TAM K 5 .   ? 7.335   58.629  44.211  1.00 50.89 ? 329 TAM A C4  1 
HETATM 11848 C C5  . TAM K 5 .   ? 10.237  57.744  45.635  1.00 50.71 ? 329 TAM A C5  1 
HETATM 11849 C C6  . TAM K 5 .   ? 6.320   55.239  47.258  1.00 51.02 ? 329 TAM A C6  1 
HETATM 11850 N N   . TAM K 5 .   ? 7.986   57.423  46.988  1.00 50.96 ? 329 TAM A N   1 
HETATM 11851 O O4  . TAM K 5 .   ? 6.491   58.948  43.098  1.00 51.54 ? 329 TAM A O4  1 
HETATM 11852 O O5  . TAM K 5 .   ? 11.197  58.001  44.599  1.00 50.89 ? 329 TAM A O5  1 
HETATM 11853 O O6  . TAM K 5 .   ? 5.582   54.005  47.290  1.00 50.59 ? 329 TAM A O6  1 
HETATM 11854 C C1  . NAG L 3 .   ? -3.541  -0.276  -6.240  1.00 65.01 ? 327 NAG C C1  1 
HETATM 11855 C C2  . NAG L 3 .   ? -2.263  0.189   -5.553  1.00 67.05 ? 327 NAG C C2  1 
HETATM 11856 C C3  . NAG L 3 .   ? -1.704  1.437   -6.226  1.00 67.54 ? 327 NAG C C3  1 
HETATM 11857 C C4  . NAG L 3 .   ? -1.651  1.263   -7.739  1.00 67.85 ? 327 NAG C C4  1 
HETATM 11858 C C5  . NAG L 3 .   ? -2.972  0.723   -8.273  1.00 67.73 ? 327 NAG C C5  1 
HETATM 11859 C C6  . NAG L 3 .   ? -2.893  0.473   -9.774  1.00 68.31 ? 327 NAG C C6  1 
HETATM 11860 C C7  . NAG L 3 .   ? -2.087  -0.363  -3.197  1.00 67.96 ? 327 NAG C C7  1 
HETATM 11861 C C8  . NAG L 3 .   ? -2.418  0.020   -1.785  1.00 67.98 ? 327 NAG C C8  1 
HETATM 11862 N N2  . NAG L 3 .   ? -2.522  0.455   -4.151  1.00 67.55 ? 327 NAG C N2  1 
HETATM 11863 O O3  . NAG L 3 .   ? -0.407  1.694   -5.737  1.00 67.88 ? 327 NAG C O3  1 
HETATM 11864 O O4  . NAG L 3 .   ? -1.371  2.505   -8.345  1.00 68.05 ? 327 NAG C O4  1 
HETATM 11865 O O5  . NAG L 3 .   ? -3.289  -0.482  -7.612  1.00 67.24 ? 327 NAG C O5  1 
HETATM 11866 O O6  . NAG L 3 .   ? -3.198  1.664   -10.466 1.00 68.41 ? 327 NAG C O6  1 
HETATM 11867 O O7  . NAG L 3 .   ? -1.446  -1.386  -3.433  1.00 67.75 ? 327 NAG C O7  1 
HETATM 11868 C C1  . NAG M 3 .   ? -45.312 56.970  3.012   1.00 39.93 ? 328 NAG C C1  1 
HETATM 11869 C C2  . NAG M 3 .   ? -45.481 57.172  4.523   1.00 40.30 ? 328 NAG C C2  1 
HETATM 11870 C C3  . NAG M 3 .   ? -46.720 56.440  5.037   1.00 41.45 ? 328 NAG C C3  1 
HETATM 11871 C C4  . NAG M 3 .   ? -47.972 56.783  4.239   1.00 42.46 ? 328 NAG C C4  1 
HETATM 11872 C C5  . NAG M 3 .   ? -47.657 56.515  2.763   1.00 41.31 ? 328 NAG C C5  1 
HETATM 11873 C C6  . NAG M 3 .   ? -48.846 56.733  1.817   1.00 40.56 ? 328 NAG C C6  1 
HETATM 11874 C C7  . NAG M 3 .   ? -43.755 57.341  6.259   1.00 39.04 ? 328 NAG C C7  1 
HETATM 11875 C C8  . NAG M 3 .   ? -42.646 56.629  6.976   1.00 37.80 ? 328 NAG C C8  1 
HETATM 11876 N N2  . NAG M 3 .   ? -44.368 56.650  5.293   1.00 39.41 ? 328 NAG C N2  1 
HETATM 11877 O O3  . NAG M 3 .   ? -46.923 56.729  6.400   1.00 41.71 ? 328 NAG C O3  1 
HETATM 11878 O O4  . NAG M 3 .   ? -49.005 55.945  4.718   1.00 45.18 ? 328 NAG C O4  1 
HETATM 11879 O O5  . NAG M 3 .   ? -46.537 57.298  2.369   1.00 40.88 ? 328 NAG C O5  1 
HETATM 11880 O O6  . NAG M 3 .   ? -49.193 58.095  1.699   1.00 39.60 ? 328 NAG C O6  1 
HETATM 11881 O O7  . NAG M 3 .   ? -44.047 58.497  6.572   1.00 38.73 ? 328 NAG C O7  1 
HETATM 11882 C C1  . NAG N 3 .   ? -50.164 56.673  5.182   1.00 47.57 ? 329 NAG C C1  1 
HETATM 11883 C C2  . NAG N 3 .   ? -51.367 55.729  5.172   1.00 48.66 ? 329 NAG C C2  1 
HETATM 11884 C C3  . NAG N 3 .   ? -52.647 56.422  5.656   1.00 49.21 ? 329 NAG C C3  1 
HETATM 11885 C C4  . NAG N 3 .   ? -52.438 57.236  6.944   1.00 49.94 ? 329 NAG C C4  1 
HETATM 11886 C C5  . NAG N 3 .   ? -51.085 57.972  6.969   1.00 49.65 ? 329 NAG C C5  1 
HETATM 11887 C C6  . NAG N 3 .   ? -50.749 58.432  8.387   1.00 49.68 ? 329 NAG C C6  1 
HETATM 11888 C C7  . NAG N 3 .   ? -51.053 53.962  3.479   1.00 49.48 ? 329 NAG C C7  1 
HETATM 11889 C C8  . NAG N 3 .   ? -51.374 53.525  2.081   1.00 49.86 ? 329 NAG C C8  1 
HETATM 11890 N N2  . NAG N 3 .   ? -51.566 55.140  3.854   1.00 49.01 ? 329 NAG C N2  1 
HETATM 11891 O O3  . NAG N 3 .   ? -53.628 55.428  5.879   1.00 49.01 ? 329 NAG C O3  1 
HETATM 11892 O O4  . NAG N 3 .   ? -53.451 58.221  7.123   1.00 51.31 ? 329 NAG C O4  1 
HETATM 11893 O O5  . NAG N 3 .   ? -50.004 57.183  6.490   1.00 48.76 ? 329 NAG C O5  1 
HETATM 11894 O O6  . NAG N 3 .   ? -49.847 59.513  8.329   1.00 49.87 ? 329 NAG C O6  1 
HETATM 11895 O O7  . NAG N 3 .   ? -50.353 53.243  4.196   1.00 49.37 ? 329 NAG C O7  1 
HETATM 11896 C C1  . BMA O 6 .   ? -54.064 57.862  8.344   1.00 20.00 ? 330 BMA C C1  1 
HETATM 11897 C C2  . BMA O 6 .   ? -55.094 58.964  8.603   1.00 20.00 ? 330 BMA C C2  1 
HETATM 11898 C C3  . BMA O 6 .   ? -55.732 58.738  9.977   1.00 20.00 ? 330 BMA C C3  1 
HETATM 11899 C C4  . BMA O 6 .   ? -56.280 57.308  10.032  1.00 20.00 ? 330 BMA C C4  1 
HETATM 11900 C C5  . BMA O 6 .   ? -55.160 56.331  9.666   1.00 20.00 ? 330 BMA C C5  1 
HETATM 11901 C C6  . BMA O 6 .   ? -55.688 54.898  9.753   1.00 20.00 ? 330 BMA C C6  1 
HETATM 11902 O O2  . BMA O 6 .   ? -56.101 58.924  7.592   1.00 20.00 ? 330 BMA C O2  1 
HETATM 11903 O O3  . BMA O 6 .   ? -56.798 59.671  10.169  1.00 20.00 ? 330 BMA C O3  1 
HETATM 11904 O O4  . BMA O 6 .   ? -56.749 57.026  11.351  1.00 20.00 ? 330 BMA C O4  1 
HETATM 11905 O O5  . BMA O 6 .   ? -54.708 56.591  8.340   1.00 20.00 ? 330 BMA C O5  1 
HETATM 11906 O O6  . BMA O 6 .   ? -54.643 53.984  9.416   1.00 20.00 ? 330 BMA C O6  1 
HETATM 11907 C C1  . GOL P 4 .   ? -12.267 3.924   -4.229  1.00 60.58 ? 2   GOL C C1  1 
HETATM 11908 O O1  . GOL P 4 .   ? -11.023 4.374   -3.742  1.00 61.08 ? 2   GOL C O1  1 
HETATM 11909 C C2  . GOL P 4 .   ? -13.122 3.455   -3.061  1.00 60.58 ? 2   GOL C C2  1 
HETATM 11910 O O2  . GOL P 4 .   ? -12.747 4.150   -1.893  1.00 60.91 ? 2   GOL C O2  1 
HETATM 11911 C C3  . GOL P 4 .   ? -12.903 1.964   -2.847  1.00 60.41 ? 2   GOL C C3  1 
HETATM 11912 O O3  . GOL P 4 .   ? -13.508 1.227   -3.886  1.00 60.40 ? 2   GOL C O3  1 
HETATM 11913 C C1  . NAG Q 3 .   ? -42.475 -0.006  3.810   1.00 58.14 ? 327 NAG E C1  1 
HETATM 11914 C C2  . NAG Q 3 .   ? -42.613 0.822   2.538   1.00 60.46 ? 327 NAG E C2  1 
HETATM 11915 C C3  . NAG Q 3 .   ? -43.398 2.102   2.802   1.00 61.02 ? 327 NAG E C3  1 
HETATM 11916 C C4  . NAG Q 3 .   ? -44.677 1.807   3.576   1.00 61.56 ? 327 NAG E C4  1 
HETATM 11917 C C5  . NAG Q 3 .   ? -44.395 0.909   4.775   1.00 61.88 ? 327 NAG E C5  1 
HETATM 11918 C C6  . NAG Q 3 .   ? -45.684 0.548   5.502   1.00 63.12 ? 327 NAG E C6  1 
HETATM 11919 C C7  . NAG Q 3 .   ? -40.755 0.440   1.024   1.00 61.33 ? 327 NAG E C7  1 
HETATM 11920 C C8  . NAG Q 3 .   ? -39.394 0.872   0.566   1.00 61.08 ? 327 NAG E C8  1 
HETATM 11921 N N2  . NAG Q 3 .   ? -41.301 1.145   2.011   1.00 60.86 ? 327 NAG E N2  1 
HETATM 11922 O O3  . NAG Q 3 .   ? -43.722 2.716   1.575   1.00 61.18 ? 327 NAG E O3  1 
HETATM 11923 O O4  . NAG Q 3 .   ? -45.247 3.018   4.020   1.00 61.78 ? 327 NAG E O4  1 
HETATM 11924 O O5  . NAG Q 3 .   ? -43.755 -0.270  4.339   1.00 61.21 ? 327 NAG E O5  1 
HETATM 11925 O O6  . NAG Q 3 .   ? -45.665 1.104   6.798   1.00 63.96 ? 327 NAG E O6  1 
HETATM 11926 O O7  . NAG Q 3 .   ? -41.316 -0.519  0.497   1.00 61.61 ? 327 NAG E O7  1 
HETATM 11927 C C1  . NAG R 3 .   ? -17.781 52.736  46.475  1.00 54.79 ? 328 NAG E C1  1 
HETATM 11928 C C2  . NAG R 3 .   ? -16.395 53.319  46.169  1.00 55.94 ? 328 NAG E C2  1 
HETATM 11929 C C3  . NAG R 3 .   ? -15.303 52.669  47.021  1.00 56.66 ? 328 NAG E C3  1 
HETATM 11930 C C4  . NAG R 3 .   ? -15.692 52.613  48.500  1.00 58.06 ? 328 NAG E C4  1 
HETATM 11931 C C5  . NAG R 3 .   ? -17.088 51.993  48.633  1.00 57.59 ? 328 NAG E C5  1 
HETATM 11932 C C6  . NAG R 3 .   ? -17.563 51.884  50.083  1.00 57.66 ? 328 NAG E C6  1 
HETATM 11933 C C7  . NAG R 3 .   ? -15.540 54.123  44.007  1.00 54.81 ? 328 NAG E C7  1 
HETATM 11934 C C8  . NAG R 3 .   ? -15.253 53.753  42.583  1.00 54.81 ? 328 NAG E C8  1 
HETATM 11935 N N2  . NAG R 3 .   ? -16.059 53.156  44.765  1.00 55.10 ? 328 NAG E N2  1 
HETATM 11936 O O3  . NAG R 3 .   ? -14.101 53.386  46.857  1.00 56.05 ? 328 NAG E O3  1 
HETATM 11937 O O4  . NAG R 3 .   ? -14.748 51.832  49.206  1.00 60.27 ? 328 NAG E O4  1 
HETATM 11938 O O5  . NAG R 3 .   ? -18.012 52.760  47.876  1.00 57.01 ? 328 NAG E O5  1 
HETATM 11939 O O6  . NAG R 3 .   ? -17.664 53.160  50.680  1.00 57.73 ? 328 NAG E O6  1 
HETATM 11940 O O7  . NAG R 3 .   ? -15.294 55.262  44.400  1.00 54.25 ? 328 NAG E O7  1 
HETATM 11941 C C1  . NAG S 3 .   ? -13.943 52.633  50.096  1.00 62.07 ? 329 NAG E C1  1 
HETATM 11942 C C2  . NAG S 3 .   ? -13.321 51.707  51.144  1.00 63.05 ? 329 NAG E C2  1 
HETATM 11943 C C3  . NAG S 3 .   ? -12.336 52.469  52.035  1.00 63.84 ? 329 NAG E C3  1 
HETATM 11944 C C4  . NAG S 3 .   ? -11.324 53.241  51.184  1.00 64.23 ? 329 NAG E C4  1 
HETATM 11945 C C5  . NAG S 3 .   ? -12.032 54.112  50.139  1.00 63.82 ? 329 NAG E C5  1 
HETATM 11946 C C6  . NAG S 3 .   ? -11.029 54.712  49.157  1.00 64.02 ? 329 NAG E C6  1 
HETATM 11947 C C7  . NAG S 3 .   ? -14.772 49.804  51.740  1.00 62.91 ? 329 NAG E C7  1 
HETATM 11948 C C8  . NAG S 3 .   ? -15.853 49.314  52.663  1.00 62.86 ? 329 NAG E C8  1 
HETATM 11949 N N2  . NAG S 3 .   ? -14.358 51.062  51.938  1.00 62.97 ? 329 NAG E N2  1 
HETATM 11950 O O3  . NAG S 3 .   ? -11.653 51.574  52.887  1.00 63.90 ? 329 NAG E O3  1 
HETATM 11951 O O4  . NAG S 3 .   ? -10.500 54.032  52.018  1.00 64.62 ? 329 NAG E O4  1 
HETATM 11952 O O5  . NAG S 3 .   ? -12.944 53.339  49.381  1.00 62.86 ? 329 NAG E O5  1 
HETATM 11953 O O6  . NAG S 3 .   ? -10.700 56.026  49.546  1.00 63.99 ? 329 NAG E O6  1 
HETATM 11954 O O7  . NAG S 3 .   ? -14.326 49.054  50.868  1.00 62.10 ? 329 NAG E O7  1 
HETATM 11955 C C1  . GOL T 4 .   ? -34.833 3.498   10.415  1.00 42.42 ? 330 GOL E C1  1 
HETATM 11956 O O1  . GOL T 4 .   ? -35.737 4.364   9.778   1.00 43.75 ? 330 GOL E O1  1 
HETATM 11957 C C2  . GOL T 4 .   ? -35.602 2.241   10.764  1.00 41.79 ? 330 GOL E C2  1 
HETATM 11958 O O2  . GOL T 4 .   ? -36.537 2.564   11.761  1.00 42.06 ? 330 GOL E O2  1 
HETATM 11959 C C3  . GOL T 4 .   ? -34.634 1.201   11.298  1.00 41.60 ? 330 GOL E C3  1 
HETATM 11960 O O3  . GOL T 4 .   ? -35.379 0.114   11.796  1.00 41.40 ? 330 GOL E O3  1 
HETATM 11961 O O   . HOH U 7 .   ? -11.708 46.798  19.749  1.00 40.63 ? 29  HOH A O   1 
HETATM 11962 O O   . HOH U 7 .   ? -3.546  39.844  26.580  1.00 29.94 ? 30  HOH A O   1 
HETATM 11963 O O   . HOH U 7 .   ? -3.358  63.459  9.058   1.00 35.04 ? 330 HOH A O   1 
HETATM 11964 O O   . HOH U 7 .   ? -7.164  -18.504 22.735  1.00 39.35 ? 331 HOH A O   1 
HETATM 11965 O O   . HOH U 7 .   ? -1.821  -7.848  29.163  1.00 48.84 ? 332 HOH A O   1 
HETATM 11966 O O   . HOH U 7 .   ? -5.824  3.334   25.321  1.00 29.85 ? 333 HOH A O   1 
HETATM 11967 O O   . HOH U 7 .   ? 9.921   39.566  32.721  1.00 29.73 ? 334 HOH A O   1 
HETATM 11968 O O   . HOH U 7 .   ? 7.543   39.437  33.190  1.00 25.44 ? 335 HOH A O   1 
HETATM 11969 O O   . HOH U 7 .   ? 12.268  32.733  20.888  1.00 30.87 ? 336 HOH A O   1 
HETATM 11970 O O   . HOH U 7 .   ? 3.664   32.827  30.460  1.00 39.37 ? 337 HOH A O   1 
HETATM 11971 O O   . HOH U 7 .   ? -5.407  45.396  27.078  1.00 36.83 ? 338 HOH A O   1 
HETATM 11972 O O   . HOH U 7 .   ? -6.863  50.667  15.778  1.00 41.98 ? 339 HOH A O   1 
HETATM 11973 O O   . HOH U 7 .   ? -10.625 43.066  17.799  1.00 20.59 ? 340 HOH A O   1 
HETATM 11974 O O   . HOH U 7 .   ? -13.381 38.976  13.469  1.00 22.86 ? 341 HOH A O   1 
HETATM 11975 O O   . HOH U 7 .   ? 8.066   69.638  17.401  1.00 36.99 ? 342 HOH A O   1 
HETATM 11976 O O   . HOH U 7 .   ? 1.265   63.557  33.356  1.00 38.78 ? 343 HOH A O   1 
HETATM 11977 O O   . HOH U 7 .   ? 6.053   59.920  27.670  1.00 26.49 ? 344 HOH A O   1 
HETATM 11978 O O   . HOH U 7 .   ? 9.502   60.281  28.216  1.00 48.31 ? 345 HOH A O   1 
HETATM 11979 O O   . HOH U 7 .   ? 0.149   64.991  23.213  1.00 17.37 ? 346 HOH A O   1 
HETATM 11980 O O   . HOH U 7 .   ? -5.289  50.175  6.557   1.00 34.63 ? 347 HOH A O   1 
HETATM 11981 O O   . HOH U 7 .   ? -12.072 67.991  14.635  1.00 36.65 ? 348 HOH A O   1 
HETATM 11982 O O   . HOH U 7 .   ? -12.082 58.116  20.458  1.00 38.11 ? 349 HOH A O   1 
HETATM 11983 O O   . HOH U 7 .   ? -13.243 59.469  18.723  1.00 33.16 ? 350 HOH A O   1 
HETATM 11984 O O   . HOH U 7 .   ? -2.440  51.365  7.068   1.00 27.23 ? 351 HOH A O   1 
HETATM 11985 O O   . HOH U 7 .   ? -4.270  47.369  9.573   1.00 38.58 ? 352 HOH A O   1 
HETATM 11986 O O   . HOH U 7 .   ? -5.778  50.061  10.116  1.00 30.77 ? 353 HOH A O   1 
HETATM 11987 O O   . HOH U 7 .   ? -0.158  50.787  4.372   1.00 26.00 ? 354 HOH A O   1 
HETATM 11988 O O   . HOH U 7 .   ? -7.751  36.207  18.470  1.00 37.27 ? 355 HOH A O   1 
HETATM 11989 O O   . HOH U 7 .   ? -11.022 45.154  21.641  1.00 25.23 ? 356 HOH A O   1 
HETATM 11990 O O   . HOH U 7 .   ? 6.703   64.211  27.662  1.00 37.20 ? 357 HOH A O   1 
HETATM 11991 O O   . HOH U 7 .   ? -15.854 40.623  13.639  1.00 25.07 ? 358 HOH A O   1 
HETATM 11992 O O   . HOH U 7 .   ? 1.650   36.487  30.185  1.00 33.99 ? 359 HOH A O   1 
HETATM 11993 O O   . HOH U 7 .   ? -2.539  49.133  3.325   1.00 43.02 ? 360 HOH A O   1 
HETATM 11994 O O   . HOH U 7 .   ? -9.517  -4.667  15.429  1.00 24.66 ? 361 HOH A O   1 
HETATM 11995 O O   . HOH U 7 .   ? 5.825   57.090  41.422  1.00 31.30 ? 362 HOH A O   1 
HETATM 11996 O O   . HOH U 7 .   ? 4.176   61.831  41.544  1.00 43.49 ? 363 HOH A O   1 
HETATM 11997 O O   . HOH U 7 .   ? 4.061   61.909  38.373  1.00 40.45 ? 364 HOH A O   1 
HETATM 11998 O O   . HOH U 7 .   ? 8.957   60.057  40.208  1.00 34.96 ? 365 HOH A O   1 
HETATM 11999 O O   . HOH V 7 .   ? -13.828 -32.917 14.863  1.00 37.55 ? 183 HOH B O   1 
HETATM 12000 O O   . HOH V 7 .   ? -16.280 -19.734 7.369   1.00 29.46 ? 184 HOH B O   1 
HETATM 12001 O O   . HOH V 7 .   ? -21.866 -20.360 12.172  1.00 35.33 ? 185 HOH B O   1 
HETATM 12002 O O   . HOH V 7 .   ? -11.973 -15.620 6.826   1.00 33.62 ? 186 HOH B O   1 
HETATM 12003 O O   . HOH V 7 .   ? -20.937 17.394  17.924  1.00 21.81 ? 187 HOH B O   1 
HETATM 12004 O O   . HOH V 7 .   ? -6.778  -24.709 19.980  1.00 45.37 ? 188 HOH B O   1 
HETATM 12005 O O   . HOH V 7 .   ? 5.556   -37.298 14.849  1.00 52.61 ? 189 HOH B O   1 
HETATM 12006 O O   . HOH V 7 .   ? -19.922 22.364  23.915  1.00 38.03 ? 190 HOH B O   1 
HETATM 12007 O O   . HOH V 7 .   ? -21.471 18.170  20.529  1.00 33.91 ? 191 HOH B O   1 
HETATM 12008 O O   . HOH V 7 .   ? -18.234 12.022  21.127  1.00 31.85 ? 192 HOH B O   1 
HETATM 12009 O O   . HOH V 7 .   ? -19.907 -11.195 16.098  1.00 40.71 ? 193 HOH B O   1 
HETATM 12010 O O   . HOH V 7 .   ? -21.296 -13.997 17.966  1.00 50.57 ? 194 HOH B O   1 
HETATM 12011 O O   . HOH V 7 .   ? -11.932 34.871  24.391  1.00 32.21 ? 195 HOH B O   1 
HETATM 12012 O O   . HOH V 7 .   ? -17.116 -19.167 17.871  1.00 42.18 ? 196 HOH B O   1 
HETATM 12013 O O   . HOH V 7 .   ? -20.984 41.883  18.906  1.00 21.92 ? 197 HOH B O   1 
HETATM 12014 O O   . HOH V 7 .   ? -19.709 40.495  17.239  1.00 33.68 ? 198 HOH B O   1 
HETATM 12015 O O   . HOH W 7 .   ? -14.391 7.152   -8.589  1.00 20.31 ? 331 HOH C O   1 
HETATM 12016 O O   . HOH W 7 .   ? -29.109 37.530  -16.549 1.00 24.98 ? 332 HOH C O   1 
HETATM 12017 O O   . HOH W 7 .   ? -9.998  52.976  -2.202  1.00 41.26 ? 333 HOH C O   1 
HETATM 12018 O O   . HOH W 7 .   ? -21.554 64.686  -9.161  1.00 25.86 ? 334 HOH C O   1 
HETATM 12019 O O   . HOH W 7 .   ? -22.615 65.138  -11.178 1.00 29.83 ? 335 HOH C O   1 
HETATM 12020 O O   . HOH W 7 .   ? -7.163  56.780  3.445   1.00 31.35 ? 336 HOH C O   1 
HETATM 12021 O O   . HOH W 7 .   ? -12.806 66.388  10.248  1.00 31.47 ? 337 HOH C O   1 
HETATM 12022 O O   . HOH W 7 .   ? -14.355 68.443  10.620  1.00 29.34 ? 338 HOH C O   1 
HETATM 12023 O O   . HOH W 7 .   ? -15.128 -15.042 -9.913  1.00 38.05 ? 339 HOH C O   1 
HETATM 12024 O O   . HOH W 7 .   ? -20.069 -3.121  -13.747 1.00 35.31 ? 340 HOH C O   1 
HETATM 12025 O O   . HOH W 7 .   ? -19.736 2.056   -12.859 1.00 36.74 ? 341 HOH C O   1 
HETATM 12026 O O   . HOH W 7 .   ? -15.768 41.055  -12.149 1.00 25.47 ? 342 HOH C O   1 
HETATM 12027 O O   . HOH W 7 .   ? -23.678 50.854  -13.799 1.00 32.57 ? 343 HOH C O   1 
HETATM 12028 O O   . HOH W 7 .   ? -25.424 50.898  -12.027 1.00 36.34 ? 344 HOH C O   1 
HETATM 12029 O O   . HOH W 7 .   ? -33.043 48.807  -14.238 1.00 23.06 ? 345 HOH C O   1 
HETATM 12030 O O   . HOH W 7 .   ? -31.722 42.839  -12.447 1.00 45.45 ? 346 HOH C O   1 
HETATM 12031 O O   . HOH W 7 .   ? -28.283 47.844  -12.923 1.00 34.86 ? 347 HOH C O   1 
HETATM 12032 O O   . HOH W 7 .   ? -15.858 43.303  -4.794  1.00 25.34 ? 348 HOH C O   1 
HETATM 12033 O O   . HOH W 7 .   ? -13.263 39.485  -5.893  1.00 48.53 ? 349 HOH C O   1 
HETATM 12034 O O   . HOH W 7 .   ? -14.488 47.767  -2.753  1.00 41.15 ? 350 HOH C O   1 
HETATM 12035 O O   . HOH W 7 .   ? -14.382 48.600  -0.393  1.00 36.43 ? 351 HOH C O   1 
HETATM 12036 O O   . HOH W 7 .   ? -10.017 51.564  -5.647  1.00 43.41 ? 352 HOH C O   1 
HETATM 12037 O O   . HOH W 7 .   ? -23.690 51.252  5.106   1.00 23.51 ? 353 HOH C O   1 
HETATM 12038 O O   . HOH W 7 .   ? -20.604 37.942  2.519   1.00 28.40 ? 354 HOH C O   1 
HETATM 12039 O O   . HOH W 7 .   ? -19.943 44.078  5.963   1.00 22.02 ? 355 HOH C O   1 
HETATM 12040 O O   . HOH W 7 .   ? -21.683 68.775  -8.508  1.00 47.12 ? 356 HOH C O   1 
HETATM 12041 O O   . HOH W 7 .   ? -22.207 67.984  -0.731  1.00 28.63 ? 357 HOH C O   1 
HETATM 12042 O O   . HOH W 7 .   ? -28.327 61.461  12.781  1.00 37.32 ? 358 HOH C O   1 
HETATM 12043 O O   . HOH W 7 .   ? -32.801 49.468  8.791   1.00 31.31 ? 359 HOH C O   1 
HETATM 12044 O O   . HOH W 7 .   ? -34.295 48.054  6.469   1.00 36.27 ? 360 HOH C O   1 
HETATM 12045 O O   . HOH W 7 .   ? -30.423 47.398  6.049   1.00 36.60 ? 361 HOH C O   1 
HETATM 12046 O O   . HOH W 7 .   ? -37.118 50.766  6.042   1.00 30.66 ? 362 HOH C O   1 
HETATM 12047 O O   . HOH W 7 .   ? -34.536 55.466  13.296  1.00 44.98 ? 363 HOH C O   1 
HETATM 12048 O O   . HOH W 7 .   ? -18.935 59.367  11.261  1.00 30.29 ? 364 HOH C O   1 
HETATM 12049 O O   . HOH W 7 .   ? -17.511 58.909  9.260   1.00 37.56 ? 365 HOH C O   1 
HETATM 12050 O O   . HOH W 7 .   ? -24.147 57.126  13.163  1.00 36.37 ? 366 HOH C O   1 
HETATM 12051 O O   . HOH W 7 .   ? -32.081 56.151  17.741  1.00 42.63 ? 367 HOH C O   1 
HETATM 12052 O O   . HOH W 7 .   ? -4.953  64.108  2.774   1.00 36.78 ? 368 HOH C O   1 
HETATM 12053 O O   . HOH W 7 .   ? -29.342 55.610  -3.941  1.00 16.48 ? 369 HOH C O   1 
HETATM 12054 O O   . HOH W 7 .   ? -10.501 12.900  -9.436  1.00 52.54 ? 370 HOH C O   1 
HETATM 12055 O O   . HOH W 7 .   ? -26.065 28.299  -3.549  1.00 29.94 ? 371 HOH C O   1 
HETATM 12056 O O   . HOH W 7 .   ? -22.735 33.626  -2.456  1.00 25.27 ? 372 HOH C O   1 
HETATM 12057 O O   . HOH W 7 .   ? -33.680 51.369  6.509   1.00 29.92 ? 373 HOH C O   1 
HETATM 12058 O O   . HOH X 7 .   ? -20.516 -2.601  -1.907  1.00 19.35 ? 183 HOH D O   1 
HETATM 12059 O O   . HOH X 7 .   ? -17.026 -12.296 -3.104  1.00 25.87 ? 184 HOH D O   1 
HETATM 12060 O O   . HOH X 7 .   ? -26.367 -14.812 2.584   1.00 21.05 ? 185 HOH D O   1 
HETATM 12061 O O   . HOH X 7 .   ? -22.639 35.460  0.775   1.00 37.46 ? 186 HOH D O   1 
HETATM 12062 O O   . HOH X 7 .   ? -10.049 8.871   -2.269  1.00 43.41 ? 187 HOH D O   1 
HETATM 12063 O O   . HOH X 7 .   ? -14.294 -17.656 0.690   1.00 31.60 ? 188 HOH D O   1 
HETATM 12064 O O   . HOH X 7 .   ? -17.568 -21.620 -10.356 1.00 28.73 ? 189 HOH D O   1 
HETATM 12065 O O   . HOH X 7 .   ? -13.589 18.126  10.625  1.00 29.86 ? 190 HOH D O   1 
HETATM 12066 O O   . HOH X 7 .   ? -32.632 -43.734 -11.646 1.00 40.28 ? 191 HOH D O   1 
HETATM 12067 O O   . HOH Y 7 .   ? -20.734 38.571  19.554  1.00 28.72 ? 1   HOH E O   1 
HETATM 12068 O O   . HOH Y 7 .   ? -18.943 62.073  33.460  1.00 23.36 ? 331 HOH E O   1 
HETATM 12069 O O   . HOH Y 7 .   ? -34.791 48.049  19.945  1.00 44.65 ? 332 HOH E O   1 
HETATM 12070 O O   . HOH Y 7 .   ? -32.501 48.620  18.851  1.00 35.81 ? 333 HOH E O   1 
HETATM 12071 O O   . HOH Y 7 .   ? -36.804 41.486  21.532  1.00 35.07 ? 334 HOH E O   1 
HETATM 12072 O O   . HOH Y 7 .   ? -24.656 50.358  25.637  1.00 32.16 ? 335 HOH E O   1 
HETATM 12073 O O   . HOH Y 7 .   ? -25.634 43.256  20.460  1.00 24.19 ? 336 HOH E O   1 
HETATM 12074 O O   . HOH Y 7 .   ? -32.772 65.726  29.532  1.00 36.31 ? 337 HOH E O   1 
HETATM 12075 O O   . HOH Y 7 .   ? -39.451 65.413  32.832  1.00 39.48 ? 338 HOH E O   1 
HETATM 12076 O O   . HOH Y 7 .   ? -13.240 54.082  31.868  1.00 31.20 ? 339 HOH E O   1 
HETATM 12077 O O   . HOH Y 7 .   ? -17.209 48.456  30.232  1.00 37.97 ? 340 HOH E O   1 
HETATM 12078 O O   . HOH Y 7 .   ? -48.537 41.880  30.190  1.00 33.68 ? 341 HOH E O   1 
HETATM 12079 O O   . HOH Y 7 .   ? -42.821 38.328  24.125  1.00 32.01 ? 342 HOH E O   1 
HETATM 12080 O O   . HOH Y 7 .   ? -47.060 63.656  21.122  1.00 38.48 ? 343 HOH E O   1 
HETATM 12081 O O   . HOH Y 7 .   ? -19.030 49.774  33.953  1.00 21.74 ? 344 HOH E O   1 
HETATM 12082 O O   . HOH Y 7 .   ? -44.986 37.004  17.395  1.00 43.35 ? 345 HOH E O   1 
HETATM 12083 O O   . HOH Y 7 .   ? -43.315 6.803   22.596  1.00 45.41 ? 346 HOH E O   1 
HETATM 12084 O O   . HOH Y 7 .   ? -30.390 -4.090  16.332  1.00 33.18 ? 347 HOH E O   1 
HETATM 12085 O O   . HOH Z 7 .   ? -23.241 -16.119 16.969  1.00 20.21 ? 183 HOH F O   1 
HETATM 12086 O O   . HOH Z 7 .   ? -37.969 -23.416 13.915  1.00 24.90 ? 184 HOH F O   1 
HETATM 12087 O O   . HOH Z 7 .   ? -28.137 36.507  21.637  1.00 39.21 ? 185 HOH F O   1 
HETATM 12088 O O   . HOH Z 7 .   ? -31.615 36.049  14.952  1.00 30.70 ? 186 HOH F O   1 
HETATM 12089 O O   . HOH Z 7 .   ? -30.206 44.398  6.196   1.00 45.01 ? 187 HOH F O   1 
HETATM 12090 O O   . HOH Z 7 .   ? -30.501 -17.926 6.705   1.00 30.61 ? 188 HOH F O   1 
HETATM 12091 O O   . HOH Z 7 .   ? -20.713 41.032  12.356  1.00 36.34 ? 189 HOH F O   1 
HETATM 12092 O O   . HOH Z 7 .   ? -22.185 39.368  10.405  1.00 27.41 ? 190 HOH F O   1 
HETATM 12093 O O   . HOH Z 7 .   ? -23.690 18.346  7.930   1.00 34.53 ? 191 HOH F 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   ASP 1   3   ?   ?   ?   A . n 
A 1 2   LEU 2   4   ?   ?   ?   A . n 
A 1 3   GLY 3   5   ?   ?   ?   A . n 
A 1 4   SER 4   6   ?   ?   ?   A . n 
A 1 5   ALA 5   7   ?   ?   ?   A . n 
A 1 6   ASP 6   8   ?   ?   ?   A . n 
A 1 7   PRO 7   9   9   PRO PRO A . n 
A 1 8   GLY 8   10  10  GLY GLY A . n 
A 1 9   ASP 9   11  11  ASP ASP A . n 
A 1 10  GLN 10  12  12  GLN GLN A . n 
A 1 11  ILE 11  13  13  ILE ILE A . n 
A 1 12  CYS 12  14  14  CYS CYS A . n 
A 1 13  ILE 13  15  15  ILE ILE A . n 
A 1 14  GLY 14  16  16  GLY GLY A . n 
A 1 15  TYR 15  17  17  TYR TYR A . n 
A 1 16  HIS 16  18  18  HIS HIS A . n 
A 1 17  ALA 17  19  19  ALA ALA A . n 
A 1 18  ASN 18  19  19  ASN ASN A A n 
A 1 19  ASN 19  20  20  ASN ASN A . n 
A 1 20  SER 20  21  21  SER SER A . n 
A 1 21  THR 21  22  22  THR THR A . n 
A 1 22  GLU 22  23  23  GLU GLU A . n 
A 1 23  GLN 23  24  24  GLN GLN A . n 
A 1 24  VAL 24  25  25  VAL VAL A . n 
A 1 25  ASP 25  26  26  ASP ASP A . n 
A 1 26  THR 26  27  27  THR THR A . n 
A 1 27  ILE 27  28  28  ILE ILE A . n 
A 1 28  MET 28  31  31  MET MET A . n 
A 1 29  GLU 29  32  32  GLU GLU A . n 
A 1 30  LYS 30  33  33  LYS LYS A . n 
A 1 31  ASN 31  34  34  ASN ASN A . n 
A 1 32  VAL 32  35  35  VAL VAL A . n 
A 1 33  THR 33  35  35  THR THR A A n 
A 1 34  VAL 34  36  36  VAL VAL A . n 
A 1 35  THR 35  37  37  THR THR A . n 
A 1 36  HIS 36  38  38  HIS HIS A . n 
A 1 37  ALA 37  39  39  ALA ALA A . n 
A 1 38  GLN 38  40  40  GLN GLN A . n 
A 1 39  ASP 39  41  41  ASP ASP A . n 
A 1 40  ILE 40  42  42  ILE ILE A . n 
A 1 41  LEU 41  43  43  LEU LEU A . n 
A 1 42  GLU 42  44  44  GLU GLU A . n 
A 1 43  LYS 43  45  45  LYS LYS A . n 
A 1 44  THR 44  46  46  THR THR A . n 
A 1 45  HIS 45  47  47  HIS HIS A . n 
A 1 46  ASN 46  48  48  ASN ASN A . n 
A 1 47  GLY 47  49  49  GLY GLY A . n 
A 1 48  LYS 48  50  50  LYS LYS A . n 
A 1 49  LEU 49  51  51  LEU LEU A . n 
A 1 50  CYS 50  52  52  CYS CYS A . n 
A 1 51  ASP 51  53  53  ASP ASP A . n 
A 1 52  LEU 52  53  53  LEU LEU A A n 
A 1 53  ASP 53  54  54  ASP ASP A . n 
A 1 54  GLY 54  55  55  GLY GLY A . n 
A 1 55  VAL 55  56  56  VAL VAL A . n 
A 1 56  LYS 56  57  57  LYS LYS A . n 
A 1 57  PRO 57  58  58  PRO PRO A . n 
A 1 58  LEU 58  59  59  LEU LEU A . n 
A 1 59  ILE 59  60  60  ILE ILE A . n 
A 1 60  LEU 60  61  61  LEU LEU A . n 
A 1 61  ARG 61  62  62  ARG ARG A . n 
A 1 62  ASP 62  63  63  ASP ASP A . n 
A 1 63  CYS 63  64  64  CYS CYS A . n 
A 1 64  SER 64  65  65  SER SER A . n 
A 1 65  VAL 65  66  66  VAL VAL A . n 
A 1 66  ALA 66  67  67  ALA ALA A . n 
A 1 67  GLY 67  68  68  GLY GLY A . n 
A 1 68  TRP 68  69  69  TRP TRP A . n 
A 1 69  LEU 69  70  70  LEU LEU A . n 
A 1 70  LEU 70  71  71  LEU LEU A . n 
A 1 71  GLY 71  72  72  GLY GLY A . n 
A 1 72  ASN 72  73  73  ASN ASN A . n 
A 1 73  PRO 73  74  74  PRO PRO A . n 
A 1 74  MET 74  75  75  MET MET A . n 
A 1 75  CYS 75  76  76  CYS CYS A . n 
A 1 76  ASP 76  77  77  ASP ASP A . n 
A 1 77  GLU 77  78  78  GLU GLU A . n 
A 1 78  PHE 78  79  79  PHE PHE A . n 
A 1 79  ILE 79  80  80  ILE ILE A . n 
A 1 80  ASN 80  81  81  ASN ASN A . n 
A 1 81  VAL 81  82  82  VAL VAL A . n 
A 1 82  PRO 82  82  82  PRO PRO A A n 
A 1 83  GLU 83  83  83  GLU GLU A . n 
A 1 84  TRP 84  84  84  TRP TRP A . n 
A 1 85  SER 85  85  85  SER SER A . n 
A 1 86  TYR 86  86  86  TYR TYR A . n 
A 1 87  ILE 87  87  87  ILE ILE A . n 
A 1 88  VAL 88  88  88  VAL VAL A . n 
A 1 89  GLU 89  89  89  GLU GLU A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  SER 92  92  92  SER SER A . n 
A 1 93  PRO 93  93  93  PRO PRO A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  LEU 97  96  96  LEU LEU A A n 
A 1 98  CYS 98  97  97  CYS CYS A . n 
A 1 99  TYR 99  98  98  TYR TYR A . n 
A 1 100 PRO 100 99  99  PRO PRO A . n 
A 1 101 GLY 101 100 100 GLY GLY A . n 
A 1 102 ASP 102 101 101 ASP ASP A . n 
A 1 103 PHE 103 102 102 PHE PHE A . n 
A 1 104 ASN 104 103 103 ASN ASN A . n 
A 1 105 ASN 105 104 104 ASN ASN A . n 
A 1 106 TYR 106 105 105 TYR TYR A . n 
A 1 107 GLU 107 106 106 GLU GLU A . n 
A 1 108 GLU 108 107 107 GLU GLU A . n 
A 1 109 LEU 109 108 108 LEU LEU A . n 
A 1 110 LYS 110 109 109 LYS LYS A . n 
A 1 111 HIS 111 110 110 HIS HIS A . n 
A 1 112 LEU 112 111 111 LEU LEU A . n 
A 1 113 LEU 113 112 112 LEU LEU A . n 
A 1 114 SER 114 113 113 SER SER A . n 
A 1 115 ARG 115 114 114 ARG ARG A . n 
A 1 116 THR 116 115 115 THR THR A . n 
A 1 117 ASN 117 116 116 ASN ASN A . n 
A 1 118 HIS 118 117 117 HIS HIS A . n 
A 1 119 PHE 119 118 118 PHE PHE A . n 
A 1 120 GLU 120 119 119 GLU GLU A . n 
A 1 121 LYS 121 120 120 LYS LYS A . n 
A 1 122 ILE 122 121 121 ILE ILE A . n 
A 1 123 GLN 123 122 122 GLN GLN A . n 
A 1 124 ILE 124 123 123 ILE ILE A . n 
A 1 125 ILE 125 124 124 ILE ILE A . n 
A 1 126 PRO 126 125 125 PRO PRO A . n 
A 1 127 LYS 127 125 125 LYS LYS A A n 
A 1 128 SER 128 125 125 SER SER A B n 
A 1 129 SER 129 126 126 SER SER A . n 
A 1 130 TRP 130 127 127 TRP TRP A . n 
A 1 131 SER 131 128 128 SER SER A . n 
A 1 132 ASN 132 129 129 ASN ASN A . n 
A 1 133 HIS 133 130 130 HIS HIS A . n 
A 1 134 ASP 134 131 131 ASP ASP A . n 
A 1 135 ALA 135 132 132 ALA ALA A . n 
A 1 136 SER 136 133 133 SER SER A . n 
A 1 137 SER 137 133 133 SER SER A A n 
A 1 138 GLY 138 134 134 GLY GLY A . n 
A 1 139 VAL 139 135 135 VAL VAL A . n 
A 1 140 SER 140 136 136 SER SER A . n 
A 1 141 SER 141 137 137 SER SER A . n 
A 1 142 ALA 142 138 138 ALA ALA A . n 
A 1 143 CYS 143 139 139 CYS CYS A . n 
A 1 144 PRO 144 140 140 PRO PRO A . n 
A 1 145 TYR 145 141 141 TYR TYR A . n 
A 1 146 HIS 146 142 142 HIS HIS A . n 
A 1 147 GLY 147 143 143 GLY GLY A . n 
A 1 148 LYS 148 144 144 LYS LYS A . n 
A 1 149 SER 149 145 145 SER SER A . n 
A 1 150 SER 150 146 146 SER SER A . n 
A 1 151 PHE 151 147 147 PHE PHE A . n 
A 1 152 PHE 152 148 148 PHE PHE A . n 
A 1 153 ARG 153 149 149 ARG ARG A . n 
A 1 154 ASN 154 150 150 ASN ASN A . n 
A 1 155 VAL 155 151 151 VAL VAL A . n 
A 1 156 VAL 156 152 152 VAL VAL A . n 
A 1 157 TRP 157 153 153 TRP TRP A . n 
A 1 158 LEU 158 154 154 LEU LEU A . n 
A 1 159 ILE 159 155 155 ILE ILE A . n 
A 1 160 LYS 160 156 156 LYS LYS A . n 
A 1 161 LYS 161 157 157 LYS LYS A . n 
A 1 162 ASN 162 158 158 ASN ASN A . n 
A 1 163 SER 163 159 159 SER SER A . n 
A 1 164 ALA 164 160 160 ALA ALA A . n 
A 1 165 TYR 165 161 161 TYR TYR A . n 
A 1 166 PRO 166 162 162 PRO PRO A . n 
A 1 167 THR 167 163 163 THR THR A . n 
A 1 168 ILE 168 164 164 ILE ILE A . n 
A 1 169 LYS 169 165 165 LYS LYS A . n 
A 1 170 ARG 170 166 166 ARG ARG A . n 
A 1 171 SER 171 167 167 SER SER A . n 
A 1 172 TYR 172 168 168 TYR TYR A . n 
A 1 173 ASN 173 169 169 ASN ASN A . n 
A 1 174 ASN 174 170 170 ASN ASN A . n 
A 1 175 THR 175 171 171 THR THR A . n 
A 1 176 ASN 176 172 172 ASN ASN A . n 
A 1 177 GLN 177 173 173 GLN GLN A . n 
A 1 178 GLU 178 174 174 GLU GLU A . n 
A 1 179 ASP 179 175 175 ASP ASP A . n 
A 1 180 LEU 180 176 176 LEU LEU A . n 
A 1 181 LEU 181 177 177 LEU LEU A . n 
A 1 182 VAL 182 178 178 VAL VAL A . n 
A 1 183 LEU 183 179 179 LEU LEU A . n 
A 1 184 TRP 184 180 180 TRP TRP A . n 
A 1 185 GLY 185 181 181 GLY GLY A . n 
A 1 186 ILE 186 182 182 ILE ILE A . n 
A 1 187 HIS 187 183 183 HIS HIS A . n 
A 1 188 HIS 188 184 184 HIS HIS A . n 
A 1 189 PRO 189 185 185 PRO PRO A . n 
A 1 190 ASN 190 186 186 ASN ASN A . n 
A 1 191 ASP 191 187 187 ASP ASP A . n 
A 1 192 ALA 192 188 188 ALA ALA A . n 
A 1 193 ALA 193 189 189 ALA ALA A . n 
A 1 194 GLU 194 190 190 GLU GLU A . n 
A 1 195 GLN 195 191 191 GLN GLN A . n 
A 1 196 THR 196 192 192 THR THR A . n 
A 1 197 LYS 197 193 193 LYS LYS A . n 
A 1 198 LEU 198 194 194 LEU LEU A . n 
A 1 199 TYR 199 195 195 TYR TYR A . n 
A 1 200 GLN 200 196 196 GLN GLN A . n 
A 1 201 ASN 201 197 197 ASN ASN A . n 
A 1 202 PRO 202 198 198 PRO PRO A . n 
A 1 203 THR 203 199 199 THR THR A . n 
A 1 204 THR 204 200 200 THR THR A . n 
A 1 205 TYR 205 201 201 TYR TYR A . n 
A 1 206 ILE 206 202 202 ILE ILE A . n 
A 1 207 SER 207 203 203 SER SER A . n 
A 1 208 VAL 208 204 204 VAL VAL A . n 
A 1 209 GLY 209 205 205 GLY GLY A . n 
A 1 210 THR 210 206 206 THR THR A . n 
A 1 211 SER 211 207 207 SER SER A . n 
A 1 212 THR 212 208 208 THR THR A . n 
A 1 213 LEU 213 209 209 LEU LEU A . n 
A 1 214 ASN 214 210 210 ASN ASN A . n 
A 1 215 GLN 215 211 211 GLN GLN A . n 
A 1 216 ARG 216 212 212 ARG ARG A . n 
A 1 217 LEU 217 213 213 LEU LEU A . n 
A 1 218 VAL 218 214 214 VAL VAL A . n 
A 1 219 PRO 219 215 215 PRO PRO A . n 
A 1 220 GLU 220 216 216 GLU GLU A . n 
A 1 221 ILE 221 217 217 ILE ILE A . n 
A 1 222 ALA 222 218 218 ALA ALA A . n 
A 1 223 THR 223 219 219 THR THR A . n 
A 1 224 ARG 224 220 220 ARG ARG A . n 
A 1 225 PRO 225 221 221 PRO PRO A . n 
A 1 226 LYS 226 222 222 LYS LYS A . n 
A 1 227 VAL 227 223 223 VAL VAL A . n 
A 1 228 ASN 228 224 224 ASN ASN A . n 
A 1 229 GLY 229 225 225 GLY GLY A . n 
A 1 230 GLN 230 226 226 GLN GLN A . n 
A 1 231 SER 231 227 227 SER SER A . n 
A 1 232 GLY 232 228 228 GLY GLY A . n 
A 1 233 ARG 233 229 229 ARG ARG A . n 
A 1 234 MET 234 230 230 MET MET A . n 
A 1 235 GLU 235 231 231 GLU GLU A . n 
A 1 236 PHE 236 232 232 PHE PHE A . n 
A 1 237 PHE 237 233 233 PHE PHE A . n 
A 1 238 TRP 238 234 234 TRP TRP A . n 
A 1 239 THR 239 235 235 THR THR A . n 
A 1 240 ILE 240 236 236 ILE ILE A . n 
A 1 241 LEU 241 237 237 LEU LEU A . n 
A 1 242 LYS 242 238 238 LYS LYS A . n 
A 1 243 PRO 243 239 239 PRO PRO A . n 
A 1 244 ASN 244 240 240 ASN ASN A . n 
A 1 245 ASP 245 241 241 ASP ASP A . n 
A 1 246 ALA 246 242 242 ALA ALA A . n 
A 1 247 ILE 247 243 243 ILE ILE A . n 
A 1 248 ASN 248 244 244 ASN ASN A . n 
A 1 249 PHE 249 245 245 PHE PHE A . n 
A 1 250 GLU 250 246 246 GLU GLU A . n 
A 1 251 SER 251 247 247 SER SER A . n 
A 1 252 ASN 252 248 248 ASN ASN A . n 
A 1 253 GLY 253 249 249 GLY GLY A . n 
A 1 254 ASN 254 250 250 ASN ASN A . n 
A 1 255 PHE 255 251 251 PHE PHE A . n 
A 1 256 ILE 256 252 252 ILE ILE A . n 
A 1 257 ALA 257 253 253 ALA ALA A . n 
A 1 258 PRO 258 254 254 PRO PRO A . n 
A 1 259 GLU 259 255 255 GLU GLU A . n 
A 1 260 TYR 260 256 256 TYR TYR A . n 
A 1 261 ALA 261 257 257 ALA ALA A . n 
A 1 262 TYR 262 258 258 TYR TYR A . n 
A 1 263 LYS 263 259 259 LYS LYS A . n 
A 1 264 ILE 264 260 260 ILE ILE A . n 
A 1 265 VAL 265 261 261 VAL VAL A . n 
A 1 266 LYS 266 262 262 LYS LYS A . n 
A 1 267 LYS 267 263 263 LYS LYS A . n 
A 1 268 GLY 268 264 264 GLY GLY A . n 
A 1 269 ASP 269 264 264 ASP ASP A A n 
A 1 270 SER 270 265 265 SER SER A . n 
A 1 271 ALA 271 266 266 ALA ALA A . n 
A 1 272 ILE 272 267 267 ILE ILE A . n 
A 1 273 MET 273 268 268 MET MET A . n 
A 1 274 LYS 274 269 269 LYS LYS A . n 
A 1 275 SER 275 270 270 SER SER A . n 
A 1 276 GLU 276 271 271 GLU GLU A . n 
A 1 277 LEU 277 272 272 LEU LEU A . n 
A 1 278 GLU 278 273 273 GLU GLU A . n 
A 1 279 TYR 279 274 274 TYR TYR A . n 
A 1 280 GLY 280 275 275 GLY GLY A . n 
A 1 281 ASN 281 276 276 ASN ASN A . n 
A 1 282 CYS 282 277 277 CYS CYS A . n 
A 1 283 ASN 283 278 278 ASN ASN A . n 
A 1 284 THR 284 279 279 THR THR A . n 
A 1 285 LYS 285 280 280 LYS LYS A . n 
A 1 286 CYS 286 281 281 CYS CYS A . n 
A 1 287 GLN 287 282 282 GLN GLN A . n 
A 1 288 THR 288 283 283 THR THR A . n 
A 1 289 PRO 289 284 284 PRO PRO A . n 
A 1 290 MET 290 285 285 MET MET A . n 
A 1 291 GLY 291 286 286 GLY GLY A . n 
A 1 292 ALA 292 287 287 ALA ALA A . n 
A 1 293 ILE 293 288 288 ILE ILE A . n 
A 1 294 ASN 294 289 289 ASN ASN A . n 
A 1 295 SER 295 290 290 SER SER A . n 
A 1 296 SER 296 291 291 SER SER A . n 
A 1 297 MET 297 292 292 MET MET A . n 
A 1 298 PRO 298 293 293 PRO PRO A . n 
A 1 299 PHE 299 294 294 PHE PHE A . n 
A 1 300 HIS 300 295 295 HIS HIS A . n 
A 1 301 ASN 301 296 296 ASN ASN A . n 
A 1 302 ILE 302 297 297 ILE ILE A . n 
A 1 303 HIS 303 298 298 HIS HIS A . n 
A 1 304 PRO 304 299 299 PRO PRO A . n 
A 1 305 LEU 305 300 300 LEU LEU A . n 
A 1 306 THR 306 301 301 THR THR A . n 
A 1 307 ILE 307 302 302 ILE ILE A . n 
A 1 308 GLY 308 303 303 GLY GLY A . n 
A 1 309 GLU 309 304 304 GLU GLU A . n 
A 1 310 CYS 310 305 305 CYS CYS A . n 
A 1 311 PRO 311 306 306 PRO PRO A . n 
A 1 312 LYS 312 307 307 LYS LYS A . n 
A 1 313 TYR 313 308 308 TYR TYR A . n 
A 1 314 VAL 314 309 309 VAL VAL A . n 
A 1 315 LYS 315 310 310 LYS LYS A . n 
A 1 316 SER 316 311 311 SER SER A . n 
A 1 317 ASN 317 312 312 ASN ASN A . n 
A 1 318 ARG 318 313 313 ARG ARG A . n 
A 1 319 LEU 319 314 314 LEU LEU A . n 
A 1 320 VAL 320 315 315 VAL VAL A . n 
A 1 321 LEU 321 316 316 LEU LEU A . n 
A 1 322 ALA 322 317 317 ALA ALA A . n 
A 1 323 THR 323 318 318 THR THR A . n 
A 1 324 GLY 324 319 319 GLY GLY A . n 
A 1 325 LEU 325 320 320 LEU LEU A . n 
A 1 326 ARG 326 321 321 ARG ARG A . n 
A 1 327 ASN 327 322 322 ASN ASN A . n 
A 1 328 THR 328 323 323 THR THR A . n 
A 1 329 PRO 329 324 ?   ?   ?   A . n 
A 1 330 GLN 330 325 ?   ?   ?   A . n 
A 1 331 ARG 331 326 ?   ?   ?   A . n 
B 2 1   GLY 1   1   1   GLY GLY B . n 
B 2 2   LEU 2   2   2   LEU LEU B . n 
B 2 3   PHE 3   3   3   PHE PHE B . n 
B 2 4   GLY 4   4   4   GLY GLY B . n 
B 2 5   ALA 5   5   5   ALA ALA B . n 
B 2 6   ILE 6   6   6   ILE ILE B . n 
B 2 7   ALA 7   7   7   ALA ALA B . n 
B 2 8   GLY 8   8   8   GLY GLY B . n 
B 2 9   PHE 9   9   9   PHE PHE B . n 
B 2 10  ILE 10  10  10  ILE ILE B . n 
B 2 11  GLU 11  11  11  GLU GLU B . n 
B 2 12  GLY 12  12  12  GLY GLY B . n 
B 2 13  GLY 13  13  13  GLY GLY B . n 
B 2 14  TRP 14  14  14  TRP TRP B . n 
B 2 15  GLN 15  15  15  GLN GLN B . n 
B 2 16  GLY 16  16  16  GLY GLY B . n 
B 2 17  MET 17  17  17  MET MET B . n 
B 2 18  VAL 18  18  18  VAL VAL B . n 
B 2 19  ASP 19  19  19  ASP ASP B . n 
B 2 20  GLY 20  20  20  GLY GLY B . n 
B 2 21  TRP 21  21  21  TRP TRP B . n 
B 2 22  TYR 22  22  22  TYR TYR B . n 
B 2 23  GLY 23  23  23  GLY GLY B . n 
B 2 24  TYR 24  24  24  TYR TYR B . n 
B 2 25  HIS 25  25  25  HIS HIS B . n 
B 2 26  HIS 26  26  26  HIS HIS B . n 
B 2 27  SER 27  27  27  SER SER B . n 
B 2 28  ASN 28  28  28  ASN ASN B . n 
B 2 29  GLU 29  29  29  GLU GLU B . n 
B 2 30  GLN 30  30  30  GLN GLN B . n 
B 2 31  GLY 31  31  31  GLY GLY B . n 
B 2 32  SER 32  32  32  SER SER B . n 
B 2 33  GLY 33  33  33  GLY GLY B . n 
B 2 34  TYR 34  34  34  TYR TYR B . n 
B 2 35  ALA 35  35  35  ALA ALA B . n 
B 2 36  ALA 36  36  36  ALA ALA B . n 
B 2 37  ASP 37  37  37  ASP ASP B . n 
B 2 38  LYS 38  38  38  LYS LYS B . n 
B 2 39  GLU 39  39  39  GLU GLU B . n 
B 2 40  SER 40  40  40  SER SER B . n 
B 2 41  THR 41  41  41  THR THR B . n 
B 2 42  GLN 42  42  42  GLN GLN B . n 
B 2 43  LYS 43  43  43  LYS LYS B . n 
B 2 44  ALA 44  44  44  ALA ALA B . n 
B 2 45  ILE 45  45  45  ILE ILE B . n 
B 2 46  ASP 46  46  46  ASP ASP B . n 
B 2 47  GLY 47  47  47  GLY GLY B . n 
B 2 48  VAL 48  48  48  VAL VAL B . n 
B 2 49  THR 49  49  49  THR THR B . n 
B 2 50  ASN 50  50  50  ASN ASN B . n 
B 2 51  LYS 51  51  51  LYS LYS B . n 
B 2 52  VAL 52  52  52  VAL VAL B . n 
B 2 53  ASN 53  53  53  ASN ASN B . n 
B 2 54  SER 54  54  54  SER SER B . n 
B 2 55  ILE 55  55  55  ILE ILE B . n 
B 2 56  ILE 56  56  56  ILE ILE B . n 
B 2 57  ASP 57  57  57  ASP ASP B . n 
B 2 58  LYS 58  58  58  LYS LYS B . n 
B 2 59  MET 59  59  59  MET MET B . n 
B 2 60  ASN 60  60  60  ASN ASN B . n 
B 2 61  THR 61  61  61  THR THR B . n 
B 2 62  GLN 62  62  62  GLN GLN B . n 
B 2 63  PHE 63  63  63  PHE PHE B . n 
B 2 64  GLU 64  64  64  GLU GLU B . n 
B 2 65  ALA 65  65  65  ALA ALA B . n 
B 2 66  VAL 66  66  66  VAL VAL B . n 
B 2 67  GLY 67  67  67  GLY GLY B . n 
B 2 68  ARG 68  68  68  ARG ARG B . n 
B 2 69  GLU 69  69  69  GLU GLU B . n 
B 2 70  PHE 70  70  70  PHE PHE B . n 
B 2 71  ASN 71  71  71  ASN ASN B . n 
B 2 72  ASN 72  72  72  ASN ASN B . n 
B 2 73  LEU 73  73  73  LEU LEU B . n 
B 2 74  GLU 74  74  74  GLU GLU B . n 
B 2 75  ARG 75  75  75  ARG ARG B . n 
B 2 76  ARG 76  76  76  ARG ARG B . n 
B 2 77  ILE 77  77  77  ILE ILE B . n 
B 2 78  GLU 78  78  78  GLU GLU B . n 
B 2 79  ASN 79  79  79  ASN ASN B . n 
B 2 80  LEU 80  80  80  LEU LEU B . n 
B 2 81  ASN 81  81  81  ASN ASN B . n 
B 2 82  LYS 82  82  82  LYS LYS B . n 
B 2 83  LYS 83  83  83  LYS LYS B . n 
B 2 84  MET 84  84  84  MET MET B . n 
B 2 85  GLU 85  85  85  GLU GLU B . n 
B 2 86  ASP 86  86  86  ASP ASP B . n 
B 2 87  GLY 87  87  87  GLY GLY B . n 
B 2 88  PHE 88  88  88  PHE PHE B . n 
B 2 89  LEU 89  89  89  LEU LEU B . n 
B 2 90  ASP 90  90  90  ASP ASP B . n 
B 2 91  VAL 91  91  91  VAL VAL B . n 
B 2 92  TRP 92  92  92  TRP TRP B . n 
B 2 93  THR 93  93  93  THR THR B . n 
B 2 94  TYR 94  94  94  TYR TYR B . n 
B 2 95  ASN 95  95  95  ASN ASN B . n 
B 2 96  ALA 96  96  96  ALA ALA B . n 
B 2 97  GLU 97  97  97  GLU GLU B . n 
B 2 98  LEU 98  98  98  LEU LEU B . n 
B 2 99  LEU 99  99  99  LEU LEU B . n 
B 2 100 VAL 100 100 100 VAL VAL B . n 
B 2 101 LEU 101 101 101 LEU LEU B . n 
B 2 102 MET 102 102 102 MET MET B . n 
B 2 103 GLU 103 103 103 GLU GLU B . n 
B 2 104 ASN 104 104 104 ASN ASN B . n 
B 2 105 GLU 105 105 105 GLU GLU B . n 
B 2 106 ARG 106 106 106 ARG ARG B . n 
B 2 107 THR 107 107 107 THR THR B . n 
B 2 108 LEU 108 108 108 LEU LEU B . n 
B 2 109 ASP 109 109 109 ASP ASP B . n 
B 2 110 PHE 110 110 110 PHE PHE B . n 
B 2 111 HIS 111 111 111 HIS HIS B . n 
B 2 112 ASP 112 112 112 ASP ASP B . n 
B 2 113 SER 113 113 113 SER SER B . n 
B 2 114 ASN 114 114 114 ASN ASN B . n 
B 2 115 VAL 115 115 115 VAL VAL B . n 
B 2 116 LYS 116 116 116 LYS LYS B . n 
B 2 117 ASN 117 117 117 ASN ASN B . n 
B 2 118 LEU 118 118 118 LEU LEU B . n 
B 2 119 TYR 119 119 119 TYR TYR B . n 
B 2 120 ASP 120 120 120 ASP ASP B . n 
B 2 121 LYS 121 121 121 LYS LYS B . n 
B 2 122 VAL 122 122 122 VAL VAL B . n 
B 2 123 ARG 123 123 123 ARG ARG B . n 
B 2 124 LEU 124 124 124 LEU LEU B . n 
B 2 125 GLN 125 125 125 GLN GLN B . n 
B 2 126 LEU 126 126 126 LEU LEU B . n 
B 2 127 ARG 127 127 127 ARG ARG B . n 
B 2 128 ASP 128 128 128 ASP ASP B . n 
B 2 129 ASN 129 129 129 ASN ASN B . n 
B 2 130 ALA 130 130 130 ALA ALA B . n 
B 2 131 LYS 131 131 131 LYS LYS B . n 
B 2 132 GLU 132 132 132 GLU GLU B . n 
B 2 133 LEU 133 133 133 LEU LEU B . n 
B 2 134 GLY 134 134 134 GLY GLY B . n 
B 2 135 ASN 135 135 135 ASN ASN B . n 
B 2 136 GLY 136 136 136 GLY GLY B . n 
B 2 137 CYS 137 137 137 CYS CYS B . n 
B 2 138 PHE 138 138 138 PHE PHE B . n 
B 2 139 GLU 139 139 139 GLU GLU B . n 
B 2 140 PHE 140 140 140 PHE PHE B . n 
B 2 141 TYR 141 141 141 TYR TYR B . n 
B 2 142 HIS 142 142 142 HIS HIS B . n 
B 2 143 LYS 143 143 143 LYS LYS B . n 
B 2 144 CYS 144 144 144 CYS CYS B . n 
B 2 145 ASP 145 145 145 ASP ASP B . n 
B 2 146 ASN 146 146 146 ASN ASN B . n 
B 2 147 GLU 147 147 147 GLU GLU B . n 
B 2 148 CYS 148 148 148 CYS CYS B . n 
B 2 149 MET 149 149 149 MET MET B . n 
B 2 150 GLU 150 150 150 GLU GLU B . n 
B 2 151 SER 151 151 151 SER SER B . n 
B 2 152 VAL 152 152 152 VAL VAL B . n 
B 2 153 LYS 153 153 153 LYS LYS B . n 
B 2 154 ASN 154 154 154 ASN ASN B . n 
B 2 155 GLY 155 155 155 GLY GLY B . n 
B 2 156 THR 156 156 156 THR THR B . n 
B 2 157 TYR 157 157 157 TYR TYR B . n 
B 2 158 ASP 158 158 158 ASP ASP B . n 
B 2 159 TYR 159 159 159 TYR TYR B . n 
B 2 160 PRO 160 160 160 PRO PRO B . n 
B 2 161 GLN 161 161 161 GLN GLN B . n 
B 2 162 TYR 162 162 162 TYR TYR B . n 
B 2 163 SER 163 163 163 SER SER B . n 
B 2 164 GLU 164 164 164 GLU GLU B . n 
B 2 165 GLU 165 165 165 GLU GLU B . n 
B 2 166 ALA 166 166 166 ALA ALA B . n 
B 2 167 ARG 167 167 167 ARG ARG B . n 
B 2 168 LEU 168 168 168 LEU LEU B . n 
B 2 169 ASN 169 169 169 ASN ASN B . n 
B 2 170 ARG 170 170 170 ARG ARG B . n 
B 2 171 GLU 171 171 ?   ?   ?   B . n 
B 2 172 GLU 172 172 ?   ?   ?   B . n 
B 2 173 ILE 173 173 ?   ?   ?   B . n 
B 2 174 SER 174 174 ?   ?   ?   B . n 
B 2 175 GLY 175 175 ?   ?   ?   B . n 
B 2 176 VAL 176 176 ?   ?   ?   B . n 
B 2 177 ARG 177 177 ?   ?   ?   B . n 
B 2 178 SER 178 178 ?   ?   ?   B . n 
B 2 179 LEU 179 179 ?   ?   ?   B . n 
B 2 180 VAL 180 180 ?   ?   ?   B . n 
B 2 181 PRO 181 181 ?   ?   ?   B . n 
B 2 182 ARG 182 182 ?   ?   ?   B . n 
C 1 1   ASP 1   3   ?   ?   ?   C . n 
C 1 2   LEU 2   4   ?   ?   ?   C . n 
C 1 3   GLY 3   5   ?   ?   ?   C . n 
C 1 4   SER 4   6   ?   ?   ?   C . n 
C 1 5   ALA 5   7   ?   ?   ?   C . n 
C 1 6   ASP 6   8   ?   ?   ?   C . n 
C 1 7   PRO 7   9   ?   ?   ?   C . n 
C 1 8   GLY 8   10  10  GLY GLY C . n 
C 1 9   ASP 9   11  11  ASP ASP C . n 
C 1 10  GLN 10  12  12  GLN GLN C . n 
C 1 11  ILE 11  13  13  ILE ILE C . n 
C 1 12  CYS 12  14  14  CYS CYS C . n 
C 1 13  ILE 13  15  15  ILE ILE C . n 
C 1 14  GLY 14  16  16  GLY GLY C . n 
C 1 15  TYR 15  17  17  TYR TYR C . n 
C 1 16  HIS 16  18  18  HIS HIS C . n 
C 1 17  ALA 17  19  19  ALA ALA C . n 
C 1 18  ASN 18  19  19  ASN ASN C A n 
C 1 19  ASN 19  20  20  ASN ASN C . n 
C 1 20  SER 20  21  21  SER SER C . n 
C 1 21  THR 21  22  22  THR THR C . n 
C 1 22  GLU 22  23  23  GLU GLU C . n 
C 1 23  GLN 23  24  24  GLN GLN C . n 
C 1 24  VAL 24  25  25  VAL VAL C . n 
C 1 25  ASP 25  26  26  ASP ASP C . n 
C 1 26  THR 26  27  27  THR THR C . n 
C 1 27  ILE 27  28  28  ILE ILE C . n 
C 1 28  MET 28  31  31  MET MET C . n 
C 1 29  GLU 29  32  32  GLU GLU C . n 
C 1 30  LYS 30  33  33  LYS LYS C . n 
C 1 31  ASN 31  34  34  ASN ASN C . n 
C 1 32  VAL 32  35  35  VAL VAL C . n 
C 1 33  THR 33  35  35  THR THR C A n 
C 1 34  VAL 34  36  36  VAL VAL C . n 
C 1 35  THR 35  37  37  THR THR C . n 
C 1 36  HIS 36  38  38  HIS HIS C . n 
C 1 37  ALA 37  39  39  ALA ALA C . n 
C 1 38  GLN 38  40  40  GLN GLN C . n 
C 1 39  ASP 39  41  41  ASP ASP C . n 
C 1 40  ILE 40  42  42  ILE ILE C . n 
C 1 41  LEU 41  43  43  LEU LEU C . n 
C 1 42  GLU 42  44  44  GLU GLU C . n 
C 1 43  LYS 43  45  45  LYS LYS C . n 
C 1 44  THR 44  46  46  THR THR C . n 
C 1 45  HIS 45  47  47  HIS HIS C . n 
C 1 46  ASN 46  48  48  ASN ASN C . n 
C 1 47  GLY 47  49  49  GLY GLY C . n 
C 1 48  LYS 48  50  50  LYS LYS C . n 
C 1 49  LEU 49  51  51  LEU LEU C . n 
C 1 50  CYS 50  52  52  CYS CYS C . n 
C 1 51  ASP 51  53  53  ASP ASP C . n 
C 1 52  LEU 52  53  53  LEU LEU C A n 
C 1 53  ASP 53  54  54  ASP ASP C . n 
C 1 54  GLY 54  55  55  GLY GLY C . n 
C 1 55  VAL 55  56  56  VAL VAL C . n 
C 1 56  LYS 56  57  57  LYS LYS C . n 
C 1 57  PRO 57  58  58  PRO PRO C . n 
C 1 58  LEU 58  59  59  LEU LEU C . n 
C 1 59  ILE 59  60  60  ILE ILE C . n 
C 1 60  LEU 60  61  61  LEU LEU C . n 
C 1 61  ARG 61  62  62  ARG ARG C . n 
C 1 62  ASP 62  63  63  ASP ASP C . n 
C 1 63  CYS 63  64  64  CYS CYS C . n 
C 1 64  SER 64  65  65  SER SER C . n 
C 1 65  VAL 65  66  66  VAL VAL C . n 
C 1 66  ALA 66  67  67  ALA ALA C . n 
C 1 67  GLY 67  68  68  GLY GLY C . n 
C 1 68  TRP 68  69  69  TRP TRP C . n 
C 1 69  LEU 69  70  70  LEU LEU C . n 
C 1 70  LEU 70  71  71  LEU LEU C . n 
C 1 71  GLY 71  72  72  GLY GLY C . n 
C 1 72  ASN 72  73  73  ASN ASN C . n 
C 1 73  PRO 73  74  74  PRO PRO C . n 
C 1 74  MET 74  75  75  MET MET C . n 
C 1 75  CYS 75  76  76  CYS CYS C . n 
C 1 76  ASP 76  77  77  ASP ASP C . n 
C 1 77  GLU 77  78  78  GLU GLU C . n 
C 1 78  PHE 78  79  79  PHE PHE C . n 
C 1 79  ILE 79  80  80  ILE ILE C . n 
C 1 80  ASN 80  81  81  ASN ASN C . n 
C 1 81  VAL 81  82  82  VAL VAL C . n 
C 1 82  PRO 82  82  82  PRO PRO C A n 
C 1 83  GLU 83  83  83  GLU GLU C . n 
C 1 84  TRP 84  84  84  TRP TRP C . n 
C 1 85  SER 85  85  85  SER SER C . n 
C 1 86  TYR 86  86  86  TYR TYR C . n 
C 1 87  ILE 87  87  87  ILE ILE C . n 
C 1 88  VAL 88  88  88  VAL VAL C . n 
C 1 89  GLU 89  89  89  GLU GLU C . n 
C 1 90  LYS 90  90  90  LYS LYS C . n 
C 1 91  ALA 91  91  91  ALA ALA C . n 
C 1 92  SER 92  92  92  SER SER C . n 
C 1 93  PRO 93  93  93  PRO PRO C . n 
C 1 94  ALA 94  94  94  ALA ALA C . n 
C 1 95  ASN 95  95  95  ASN ASN C . n 
C 1 96  ASP 96  96  96  ASP ASP C . n 
C 1 97  LEU 97  96  96  LEU LEU C A n 
C 1 98  CYS 98  97  97  CYS CYS C . n 
C 1 99  TYR 99  98  98  TYR TYR C . n 
C 1 100 PRO 100 99  99  PRO PRO C . n 
C 1 101 GLY 101 100 100 GLY GLY C . n 
C 1 102 ASP 102 101 101 ASP ASP C . n 
C 1 103 PHE 103 102 102 PHE PHE C . n 
C 1 104 ASN 104 103 103 ASN ASN C . n 
C 1 105 ASN 105 104 104 ASN ASN C . n 
C 1 106 TYR 106 105 105 TYR TYR C . n 
C 1 107 GLU 107 106 106 GLU GLU C . n 
C 1 108 GLU 108 107 107 GLU GLU C . n 
C 1 109 LEU 109 108 108 LEU LEU C . n 
C 1 110 LYS 110 109 109 LYS LYS C . n 
C 1 111 HIS 111 110 110 HIS HIS C . n 
C 1 112 LEU 112 111 111 LEU LEU C . n 
C 1 113 LEU 113 112 112 LEU LEU C . n 
C 1 114 SER 114 113 113 SER SER C . n 
C 1 115 ARG 115 114 114 ARG ARG C . n 
C 1 116 THR 116 115 115 THR THR C . n 
C 1 117 ASN 117 116 116 ASN ASN C . n 
C 1 118 HIS 118 117 117 HIS HIS C . n 
C 1 119 PHE 119 118 118 PHE PHE C . n 
C 1 120 GLU 120 119 119 GLU GLU C . n 
C 1 121 LYS 121 120 120 LYS LYS C . n 
C 1 122 ILE 122 121 121 ILE ILE C . n 
C 1 123 GLN 123 122 122 GLN GLN C . n 
C 1 124 ILE 124 123 123 ILE ILE C . n 
C 1 125 ILE 125 124 124 ILE ILE C . n 
C 1 126 PRO 126 125 125 PRO PRO C . n 
C 1 127 LYS 127 125 125 LYS LYS C A n 
C 1 128 SER 128 125 125 SER SER C B n 
C 1 129 SER 129 126 126 SER SER C . n 
C 1 130 TRP 130 127 127 TRP TRP C . n 
C 1 131 SER 131 128 128 SER SER C . n 
C 1 132 ASN 132 129 129 ASN ASN C . n 
C 1 133 HIS 133 130 130 HIS HIS C . n 
C 1 134 ASP 134 131 131 ASP ASP C . n 
C 1 135 ALA 135 132 132 ALA ALA C . n 
C 1 136 SER 136 133 133 SER SER C . n 
C 1 137 SER 137 133 133 SER SER C A n 
C 1 138 GLY 138 134 134 GLY GLY C . n 
C 1 139 VAL 139 135 135 VAL VAL C . n 
C 1 140 SER 140 136 136 SER SER C . n 
C 1 141 SER 141 137 137 SER SER C . n 
C 1 142 ALA 142 138 138 ALA ALA C . n 
C 1 143 CYS 143 139 139 CYS CYS C . n 
C 1 144 PRO 144 140 140 PRO PRO C . n 
C 1 145 TYR 145 141 141 TYR TYR C . n 
C 1 146 HIS 146 142 142 HIS HIS C . n 
C 1 147 GLY 147 143 143 GLY GLY C . n 
C 1 148 LYS 148 144 144 LYS LYS C . n 
C 1 149 SER 149 145 145 SER SER C . n 
C 1 150 SER 150 146 146 SER SER C . n 
C 1 151 PHE 151 147 147 PHE PHE C . n 
C 1 152 PHE 152 148 148 PHE PHE C . n 
C 1 153 ARG 153 149 149 ARG ARG C . n 
C 1 154 ASN 154 150 150 ASN ASN C . n 
C 1 155 VAL 155 151 151 VAL VAL C . n 
C 1 156 VAL 156 152 152 VAL VAL C . n 
C 1 157 TRP 157 153 153 TRP TRP C . n 
C 1 158 LEU 158 154 154 LEU LEU C . n 
C 1 159 ILE 159 155 155 ILE ILE C . n 
C 1 160 LYS 160 156 156 LYS LYS C . n 
C 1 161 LYS 161 157 157 LYS LYS C . n 
C 1 162 ASN 162 158 158 ASN ASN C . n 
C 1 163 SER 163 159 159 SER SER C . n 
C 1 164 ALA 164 160 160 ALA ALA C . n 
C 1 165 TYR 165 161 161 TYR TYR C . n 
C 1 166 PRO 166 162 162 PRO PRO C . n 
C 1 167 THR 167 163 163 THR THR C . n 
C 1 168 ILE 168 164 164 ILE ILE C . n 
C 1 169 LYS 169 165 165 LYS LYS C . n 
C 1 170 ARG 170 166 166 ARG ARG C . n 
C 1 171 SER 171 167 167 SER SER C . n 
C 1 172 TYR 172 168 168 TYR TYR C . n 
C 1 173 ASN 173 169 169 ASN ASN C . n 
C 1 174 ASN 174 170 170 ASN ASN C . n 
C 1 175 THR 175 171 171 THR THR C . n 
C 1 176 ASN 176 172 172 ASN ASN C . n 
C 1 177 GLN 177 173 173 GLN GLN C . n 
C 1 178 GLU 178 174 174 GLU GLU C . n 
C 1 179 ASP 179 175 175 ASP ASP C . n 
C 1 180 LEU 180 176 176 LEU LEU C . n 
C 1 181 LEU 181 177 177 LEU LEU C . n 
C 1 182 VAL 182 178 178 VAL VAL C . n 
C 1 183 LEU 183 179 179 LEU LEU C . n 
C 1 184 TRP 184 180 180 TRP TRP C . n 
C 1 185 GLY 185 181 181 GLY GLY C . n 
C 1 186 ILE 186 182 182 ILE ILE C . n 
C 1 187 HIS 187 183 183 HIS HIS C . n 
C 1 188 HIS 188 184 184 HIS HIS C . n 
C 1 189 PRO 189 185 185 PRO PRO C . n 
C 1 190 ASN 190 186 186 ASN ASN C . n 
C 1 191 ASP 191 187 187 ASP ASP C . n 
C 1 192 ALA 192 188 188 ALA ALA C . n 
C 1 193 ALA 193 189 189 ALA ALA C . n 
C 1 194 GLU 194 190 190 GLU GLU C . n 
C 1 195 GLN 195 191 191 GLN GLN C . n 
C 1 196 THR 196 192 192 THR THR C . n 
C 1 197 LYS 197 193 193 LYS LYS C . n 
C 1 198 LEU 198 194 194 LEU LEU C . n 
C 1 199 TYR 199 195 195 TYR TYR C . n 
C 1 200 GLN 200 196 196 GLN GLN C . n 
C 1 201 ASN 201 197 197 ASN ASN C . n 
C 1 202 PRO 202 198 198 PRO PRO C . n 
C 1 203 THR 203 199 199 THR THR C . n 
C 1 204 THR 204 200 200 THR THR C . n 
C 1 205 TYR 205 201 201 TYR TYR C . n 
C 1 206 ILE 206 202 202 ILE ILE C . n 
C 1 207 SER 207 203 203 SER SER C . n 
C 1 208 VAL 208 204 204 VAL VAL C . n 
C 1 209 GLY 209 205 205 GLY GLY C . n 
C 1 210 THR 210 206 206 THR THR C . n 
C 1 211 SER 211 207 207 SER SER C . n 
C 1 212 THR 212 208 208 THR THR C . n 
C 1 213 LEU 213 209 209 LEU LEU C . n 
C 1 214 ASN 214 210 210 ASN ASN C . n 
C 1 215 GLN 215 211 211 GLN GLN C . n 
C 1 216 ARG 216 212 212 ARG ARG C . n 
C 1 217 LEU 217 213 213 LEU LEU C . n 
C 1 218 VAL 218 214 214 VAL VAL C . n 
C 1 219 PRO 219 215 215 PRO PRO C . n 
C 1 220 GLU 220 216 216 GLU GLU C . n 
C 1 221 ILE 221 217 217 ILE ILE C . n 
C 1 222 ALA 222 218 218 ALA ALA C . n 
C 1 223 THR 223 219 219 THR THR C . n 
C 1 224 ARG 224 220 220 ARG ARG C . n 
C 1 225 PRO 225 221 221 PRO PRO C . n 
C 1 226 LYS 226 222 222 LYS LYS C . n 
C 1 227 VAL 227 223 223 VAL VAL C . n 
C 1 228 ASN 228 224 224 ASN ASN C . n 
C 1 229 GLY 229 225 225 GLY GLY C . n 
C 1 230 GLN 230 226 226 GLN GLN C . n 
C 1 231 SER 231 227 227 SER SER C . n 
C 1 232 GLY 232 228 228 GLY GLY C . n 
C 1 233 ARG 233 229 229 ARG ARG C . n 
C 1 234 MET 234 230 230 MET MET C . n 
C 1 235 GLU 235 231 231 GLU GLU C . n 
C 1 236 PHE 236 232 232 PHE PHE C . n 
C 1 237 PHE 237 233 233 PHE PHE C . n 
C 1 238 TRP 238 234 234 TRP TRP C . n 
C 1 239 THR 239 235 235 THR THR C . n 
C 1 240 ILE 240 236 236 ILE ILE C . n 
C 1 241 LEU 241 237 237 LEU LEU C . n 
C 1 242 LYS 242 238 238 LYS LYS C . n 
C 1 243 PRO 243 239 239 PRO PRO C . n 
C 1 244 ASN 244 240 240 ASN ASN C . n 
C 1 245 ASP 245 241 241 ASP ASP C . n 
C 1 246 ALA 246 242 242 ALA ALA C . n 
C 1 247 ILE 247 243 243 ILE ILE C . n 
C 1 248 ASN 248 244 244 ASN ASN C . n 
C 1 249 PHE 249 245 245 PHE PHE C . n 
C 1 250 GLU 250 246 246 GLU GLU C . n 
C 1 251 SER 251 247 247 SER SER C . n 
C 1 252 ASN 252 248 248 ASN ASN C . n 
C 1 253 GLY 253 249 249 GLY GLY C . n 
C 1 254 ASN 254 250 250 ASN ASN C . n 
C 1 255 PHE 255 251 251 PHE PHE C . n 
C 1 256 ILE 256 252 252 ILE ILE C . n 
C 1 257 ALA 257 253 253 ALA ALA C . n 
C 1 258 PRO 258 254 254 PRO PRO C . n 
C 1 259 GLU 259 255 255 GLU GLU C . n 
C 1 260 TYR 260 256 256 TYR TYR C . n 
C 1 261 ALA 261 257 257 ALA ALA C . n 
C 1 262 TYR 262 258 258 TYR TYR C . n 
C 1 263 LYS 263 259 259 LYS LYS C . n 
C 1 264 ILE 264 260 260 ILE ILE C . n 
C 1 265 VAL 265 261 261 VAL VAL C . n 
C 1 266 LYS 266 262 262 LYS LYS C . n 
C 1 267 LYS 267 263 263 LYS LYS C . n 
C 1 268 GLY 268 264 264 GLY GLY C . n 
C 1 269 ASP 269 264 264 ASP ASP C A n 
C 1 270 SER 270 265 265 SER SER C . n 
C 1 271 ALA 271 266 266 ALA ALA C . n 
C 1 272 ILE 272 267 267 ILE ILE C . n 
C 1 273 MET 273 268 268 MET MET C . n 
C 1 274 LYS 274 269 269 LYS LYS C . n 
C 1 275 SER 275 270 270 SER SER C . n 
C 1 276 GLU 276 271 271 GLU GLU C . n 
C 1 277 LEU 277 272 272 LEU LEU C . n 
C 1 278 GLU 278 273 273 GLU GLU C . n 
C 1 279 TYR 279 274 274 TYR TYR C . n 
C 1 280 GLY 280 275 275 GLY GLY C . n 
C 1 281 ASN 281 276 276 ASN ASN C . n 
C 1 282 CYS 282 277 277 CYS CYS C . n 
C 1 283 ASN 283 278 278 ASN ASN C . n 
C 1 284 THR 284 279 279 THR THR C . n 
C 1 285 LYS 285 280 280 LYS LYS C . n 
C 1 286 CYS 286 281 281 CYS CYS C . n 
C 1 287 GLN 287 282 282 GLN GLN C . n 
C 1 288 THR 288 283 283 THR THR C . n 
C 1 289 PRO 289 284 284 PRO PRO C . n 
C 1 290 MET 290 285 285 MET MET C . n 
C 1 291 GLY 291 286 286 GLY GLY C . n 
C 1 292 ALA 292 287 287 ALA ALA C . n 
C 1 293 ILE 293 288 288 ILE ILE C . n 
C 1 294 ASN 294 289 289 ASN ASN C . n 
C 1 295 SER 295 290 290 SER SER C . n 
C 1 296 SER 296 291 291 SER SER C . n 
C 1 297 MET 297 292 292 MET MET C . n 
C 1 298 PRO 298 293 293 PRO PRO C . n 
C 1 299 PHE 299 294 294 PHE PHE C . n 
C 1 300 HIS 300 295 295 HIS HIS C . n 
C 1 301 ASN 301 296 296 ASN ASN C . n 
C 1 302 ILE 302 297 297 ILE ILE C . n 
C 1 303 HIS 303 298 298 HIS HIS C . n 
C 1 304 PRO 304 299 299 PRO PRO C . n 
C 1 305 LEU 305 300 300 LEU LEU C . n 
C 1 306 THR 306 301 301 THR THR C . n 
C 1 307 ILE 307 302 302 ILE ILE C . n 
C 1 308 GLY 308 303 303 GLY GLY C . n 
C 1 309 GLU 309 304 304 GLU GLU C . n 
C 1 310 CYS 310 305 305 CYS CYS C . n 
C 1 311 PRO 311 306 306 PRO PRO C . n 
C 1 312 LYS 312 307 307 LYS LYS C . n 
C 1 313 TYR 313 308 308 TYR TYR C . n 
C 1 314 VAL 314 309 309 VAL VAL C . n 
C 1 315 LYS 315 310 310 LYS LYS C . n 
C 1 316 SER 316 311 311 SER SER C . n 
C 1 317 ASN 317 312 312 ASN ASN C . n 
C 1 318 ARG 318 313 313 ARG ARG C . n 
C 1 319 LEU 319 314 314 LEU LEU C . n 
C 1 320 VAL 320 315 315 VAL VAL C . n 
C 1 321 LEU 321 316 316 LEU LEU C . n 
C 1 322 ALA 322 317 317 ALA ALA C . n 
C 1 323 THR 323 318 318 THR THR C . n 
C 1 324 GLY 324 319 319 GLY GLY C . n 
C 1 325 LEU 325 320 320 LEU LEU C . n 
C 1 326 ARG 326 321 321 ARG ARG C . n 
C 1 327 ASN 327 322 322 ASN ASN C . n 
C 1 328 THR 328 323 323 THR THR C . n 
C 1 329 PRO 329 324 ?   ?   ?   C . n 
C 1 330 GLN 330 325 ?   ?   ?   C . n 
C 1 331 ARG 331 326 ?   ?   ?   C . n 
D 2 1   GLY 1   1   1   GLY GLY D . n 
D 2 2   LEU 2   2   2   LEU LEU D . n 
D 2 3   PHE 3   3   3   PHE PHE D . n 
D 2 4   GLY 4   4   4   GLY GLY D . n 
D 2 5   ALA 5   5   5   ALA ALA D . n 
D 2 6   ILE 6   6   6   ILE ILE D . n 
D 2 7   ALA 7   7   7   ALA ALA D . n 
D 2 8   GLY 8   8   8   GLY GLY D . n 
D 2 9   PHE 9   9   9   PHE PHE D . n 
D 2 10  ILE 10  10  10  ILE ILE D . n 
D 2 11  GLU 11  11  11  GLU GLU D . n 
D 2 12  GLY 12  12  12  GLY GLY D . n 
D 2 13  GLY 13  13  13  GLY GLY D . n 
D 2 14  TRP 14  14  14  TRP TRP D . n 
D 2 15  GLN 15  15  15  GLN GLN D . n 
D 2 16  GLY 16  16  16  GLY GLY D . n 
D 2 17  MET 17  17  17  MET MET D . n 
D 2 18  VAL 18  18  18  VAL VAL D . n 
D 2 19  ASP 19  19  19  ASP ASP D . n 
D 2 20  GLY 20  20  20  GLY GLY D . n 
D 2 21  TRP 21  21  21  TRP TRP D . n 
D 2 22  TYR 22  22  22  TYR TYR D . n 
D 2 23  GLY 23  23  23  GLY GLY D . n 
D 2 24  TYR 24  24  24  TYR TYR D . n 
D 2 25  HIS 25  25  25  HIS HIS D . n 
D 2 26  HIS 26  26  26  HIS HIS D . n 
D 2 27  SER 27  27  27  SER SER D . n 
D 2 28  ASN 28  28  28  ASN ASN D . n 
D 2 29  GLU 29  29  29  GLU GLU D . n 
D 2 30  GLN 30  30  30  GLN GLN D . n 
D 2 31  GLY 31  31  31  GLY GLY D . n 
D 2 32  SER 32  32  32  SER SER D . n 
D 2 33  GLY 33  33  33  GLY GLY D . n 
D 2 34  TYR 34  34  34  TYR TYR D . n 
D 2 35  ALA 35  35  35  ALA ALA D . n 
D 2 36  ALA 36  36  36  ALA ALA D . n 
D 2 37  ASP 37  37  37  ASP ASP D . n 
D 2 38  LYS 38  38  38  LYS LYS D . n 
D 2 39  GLU 39  39  39  GLU GLU D . n 
D 2 40  SER 40  40  40  SER SER D . n 
D 2 41  THR 41  41  41  THR THR D . n 
D 2 42  GLN 42  42  42  GLN GLN D . n 
D 2 43  LYS 43  43  43  LYS LYS D . n 
D 2 44  ALA 44  44  44  ALA ALA D . n 
D 2 45  ILE 45  45  45  ILE ILE D . n 
D 2 46  ASP 46  46  46  ASP ASP D . n 
D 2 47  GLY 47  47  47  GLY GLY D . n 
D 2 48  VAL 48  48  48  VAL VAL D . n 
D 2 49  THR 49  49  49  THR THR D . n 
D 2 50  ASN 50  50  50  ASN ASN D . n 
D 2 51  LYS 51  51  51  LYS LYS D . n 
D 2 52  VAL 52  52  52  VAL VAL D . n 
D 2 53  ASN 53  53  53  ASN ASN D . n 
D 2 54  SER 54  54  54  SER SER D . n 
D 2 55  ILE 55  55  55  ILE ILE D . n 
D 2 56  ILE 56  56  56  ILE ILE D . n 
D 2 57  ASP 57  57  57  ASP ASP D . n 
D 2 58  LYS 58  58  58  LYS LYS D . n 
D 2 59  MET 59  59  59  MET MET D . n 
D 2 60  ASN 60  60  60  ASN ASN D . n 
D 2 61  THR 61  61  61  THR THR D . n 
D 2 62  GLN 62  62  62  GLN GLN D . n 
D 2 63  PHE 63  63  63  PHE PHE D . n 
D 2 64  GLU 64  64  64  GLU GLU D . n 
D 2 65  ALA 65  65  65  ALA ALA D . n 
D 2 66  VAL 66  66  66  VAL VAL D . n 
D 2 67  GLY 67  67  67  GLY GLY D . n 
D 2 68  ARG 68  68  68  ARG ARG D . n 
D 2 69  GLU 69  69  69  GLU GLU D . n 
D 2 70  PHE 70  70  70  PHE PHE D . n 
D 2 71  ASN 71  71  71  ASN ASN D . n 
D 2 72  ASN 72  72  72  ASN ASN D . n 
D 2 73  LEU 73  73  73  LEU LEU D . n 
D 2 74  GLU 74  74  74  GLU GLU D . n 
D 2 75  ARG 75  75  75  ARG ARG D . n 
D 2 76  ARG 76  76  76  ARG ARG D . n 
D 2 77  ILE 77  77  77  ILE ILE D . n 
D 2 78  GLU 78  78  78  GLU GLU D . n 
D 2 79  ASN 79  79  79  ASN ASN D . n 
D 2 80  LEU 80  80  80  LEU LEU D . n 
D 2 81  ASN 81  81  81  ASN ASN D . n 
D 2 82  LYS 82  82  82  LYS LYS D . n 
D 2 83  LYS 83  83  83  LYS LYS D . n 
D 2 84  MET 84  84  84  MET MET D . n 
D 2 85  GLU 85  85  85  GLU GLU D . n 
D 2 86  ASP 86  86  86  ASP ASP D . n 
D 2 87  GLY 87  87  87  GLY GLY D . n 
D 2 88  PHE 88  88  88  PHE PHE D . n 
D 2 89  LEU 89  89  89  LEU LEU D . n 
D 2 90  ASP 90  90  90  ASP ASP D . n 
D 2 91  VAL 91  91  91  VAL VAL D . n 
D 2 92  TRP 92  92  92  TRP TRP D . n 
D 2 93  THR 93  93  93  THR THR D . n 
D 2 94  TYR 94  94  94  TYR TYR D . n 
D 2 95  ASN 95  95  95  ASN ASN D . n 
D 2 96  ALA 96  96  96  ALA ALA D . n 
D 2 97  GLU 97  97  97  GLU GLU D . n 
D 2 98  LEU 98  98  98  LEU LEU D . n 
D 2 99  LEU 99  99  99  LEU LEU D . n 
D 2 100 VAL 100 100 100 VAL VAL D . n 
D 2 101 LEU 101 101 101 LEU LEU D . n 
D 2 102 MET 102 102 102 MET MET D . n 
D 2 103 GLU 103 103 103 GLU GLU D . n 
D 2 104 ASN 104 104 104 ASN ASN D . n 
D 2 105 GLU 105 105 105 GLU GLU D . n 
D 2 106 ARG 106 106 106 ARG ARG D . n 
D 2 107 THR 107 107 107 THR THR D . n 
D 2 108 LEU 108 108 108 LEU LEU D . n 
D 2 109 ASP 109 109 109 ASP ASP D . n 
D 2 110 PHE 110 110 110 PHE PHE D . n 
D 2 111 HIS 111 111 111 HIS HIS D . n 
D 2 112 ASP 112 112 112 ASP ASP D . n 
D 2 113 SER 113 113 113 SER SER D . n 
D 2 114 ASN 114 114 114 ASN ASN D . n 
D 2 115 VAL 115 115 115 VAL VAL D . n 
D 2 116 LYS 116 116 116 LYS LYS D . n 
D 2 117 ASN 117 117 117 ASN ASN D . n 
D 2 118 LEU 118 118 118 LEU LEU D . n 
D 2 119 TYR 119 119 119 TYR TYR D . n 
D 2 120 ASP 120 120 120 ASP ASP D . n 
D 2 121 LYS 121 121 121 LYS LYS D . n 
D 2 122 VAL 122 122 122 VAL VAL D . n 
D 2 123 ARG 123 123 123 ARG ARG D . n 
D 2 124 LEU 124 124 124 LEU LEU D . n 
D 2 125 GLN 125 125 125 GLN GLN D . n 
D 2 126 LEU 126 126 126 LEU LEU D . n 
D 2 127 ARG 127 127 127 ARG ARG D . n 
D 2 128 ASP 128 128 128 ASP ASP D . n 
D 2 129 ASN 129 129 129 ASN ASN D . n 
D 2 130 ALA 130 130 130 ALA ALA D . n 
D 2 131 LYS 131 131 131 LYS LYS D . n 
D 2 132 GLU 132 132 132 GLU GLU D . n 
D 2 133 LEU 133 133 133 LEU LEU D . n 
D 2 134 GLY 134 134 134 GLY GLY D . n 
D 2 135 ASN 135 135 135 ASN ASN D . n 
D 2 136 GLY 136 136 136 GLY GLY D . n 
D 2 137 CYS 137 137 137 CYS CYS D . n 
D 2 138 PHE 138 138 138 PHE PHE D . n 
D 2 139 GLU 139 139 139 GLU GLU D . n 
D 2 140 PHE 140 140 140 PHE PHE D . n 
D 2 141 TYR 141 141 141 TYR TYR D . n 
D 2 142 HIS 142 142 142 HIS HIS D . n 
D 2 143 LYS 143 143 143 LYS LYS D . n 
D 2 144 CYS 144 144 144 CYS CYS D . n 
D 2 145 ASP 145 145 145 ASP ASP D . n 
D 2 146 ASN 146 146 146 ASN ASN D . n 
D 2 147 GLU 147 147 147 GLU GLU D . n 
D 2 148 CYS 148 148 148 CYS CYS D . n 
D 2 149 MET 149 149 149 MET MET D . n 
D 2 150 GLU 150 150 150 GLU GLU D . n 
D 2 151 SER 151 151 151 SER SER D . n 
D 2 152 VAL 152 152 152 VAL VAL D . n 
D 2 153 LYS 153 153 153 LYS LYS D . n 
D 2 154 ASN 154 154 154 ASN ASN D . n 
D 2 155 GLY 155 155 155 GLY GLY D . n 
D 2 156 THR 156 156 156 THR THR D . n 
D 2 157 TYR 157 157 157 TYR TYR D . n 
D 2 158 ASP 158 158 158 ASP ASP D . n 
D 2 159 TYR 159 159 159 TYR TYR D . n 
D 2 160 PRO 160 160 160 PRO PRO D . n 
D 2 161 GLN 161 161 161 GLN GLN D . n 
D 2 162 TYR 162 162 162 TYR TYR D . n 
D 2 163 SER 163 163 163 SER SER D . n 
D 2 164 GLU 164 164 164 GLU GLU D . n 
D 2 165 GLU 165 165 165 GLU GLU D . n 
D 2 166 ALA 166 166 166 ALA ALA D . n 
D 2 167 ARG 167 167 167 ARG ARG D . n 
D 2 168 LEU 168 168 168 LEU LEU D . n 
D 2 169 ASN 169 169 169 ASN ASN D . n 
D 2 170 ARG 170 170 170 ARG ARG D . n 
D 2 171 GLU 171 171 171 GLU GLU D . n 
D 2 172 GLU 172 172 172 GLU GLU D . n 
D 2 173 ILE 173 173 ?   ?   ?   D . n 
D 2 174 SER 174 174 ?   ?   ?   D . n 
D 2 175 GLY 175 175 ?   ?   ?   D . n 
D 2 176 VAL 176 176 ?   ?   ?   D . n 
D 2 177 ARG 177 177 ?   ?   ?   D . n 
D 2 178 SER 178 178 ?   ?   ?   D . n 
D 2 179 LEU 179 179 ?   ?   ?   D . n 
D 2 180 VAL 180 180 ?   ?   ?   D . n 
D 2 181 PRO 181 181 ?   ?   ?   D . n 
D 2 182 ARG 182 182 ?   ?   ?   D . n 
E 1 1   ASP 1   3   ?   ?   ?   E . n 
E 1 2   LEU 2   4   ?   ?   ?   E . n 
E 1 3   GLY 3   5   ?   ?   ?   E . n 
E 1 4   SER 4   6   ?   ?   ?   E . n 
E 1 5   ALA 5   7   ?   ?   ?   E . n 
E 1 6   ASP 6   8   ?   ?   ?   E . n 
E 1 7   PRO 7   9   9   PRO PRO E . n 
E 1 8   GLY 8   10  10  GLY GLY E . n 
E 1 9   ASP 9   11  11  ASP ASP E . n 
E 1 10  GLN 10  12  12  GLN GLN E . n 
E 1 11  ILE 11  13  13  ILE ILE E . n 
E 1 12  CYS 12  14  14  CYS CYS E . n 
E 1 13  ILE 13  15  15  ILE ILE E . n 
E 1 14  GLY 14  16  16  GLY GLY E . n 
E 1 15  TYR 15  17  17  TYR TYR E . n 
E 1 16  HIS 16  18  18  HIS HIS E . n 
E 1 17  ALA 17  19  19  ALA ALA E . n 
E 1 18  ASN 18  19  19  ASN ASN E A n 
E 1 19  ASN 19  20  20  ASN ASN E . n 
E 1 20  SER 20  21  21  SER SER E . n 
E 1 21  THR 21  22  22  THR THR E . n 
E 1 22  GLU 22  23  23  GLU GLU E . n 
E 1 23  GLN 23  24  24  GLN GLN E . n 
E 1 24  VAL 24  25  25  VAL VAL E . n 
E 1 25  ASP 25  26  26  ASP ASP E . n 
E 1 26  THR 26  27  27  THR THR E . n 
E 1 27  ILE 27  28  28  ILE ILE E . n 
E 1 28  MET 28  31  31  MET MET E . n 
E 1 29  GLU 29  32  32  GLU GLU E . n 
E 1 30  LYS 30  33  33  LYS LYS E . n 
E 1 31  ASN 31  34  34  ASN ASN E . n 
E 1 32  VAL 32  35  35  VAL VAL E . n 
E 1 33  THR 33  35  35  THR THR E A n 
E 1 34  VAL 34  36  36  VAL VAL E . n 
E 1 35  THR 35  37  37  THR THR E . n 
E 1 36  HIS 36  38  38  HIS HIS E . n 
E 1 37  ALA 37  39  39  ALA ALA E . n 
E 1 38  GLN 38  40  40  GLN GLN E . n 
E 1 39  ASP 39  41  41  ASP ASP E . n 
E 1 40  ILE 40  42  42  ILE ILE E . n 
E 1 41  LEU 41  43  43  LEU LEU E . n 
E 1 42  GLU 42  44  44  GLU GLU E . n 
E 1 43  LYS 43  45  45  LYS LYS E . n 
E 1 44  THR 44  46  46  THR THR E . n 
E 1 45  HIS 45  47  47  HIS HIS E . n 
E 1 46  ASN 46  48  48  ASN ASN E . n 
E 1 47  GLY 47  49  49  GLY GLY E . n 
E 1 48  LYS 48  50  50  LYS LYS E . n 
E 1 49  LEU 49  51  51  LEU LEU E . n 
E 1 50  CYS 50  52  52  CYS CYS E . n 
E 1 51  ASP 51  53  53  ASP ASP E . n 
E 1 52  LEU 52  53  53  LEU LEU E A n 
E 1 53  ASP 53  54  54  ASP ASP E . n 
E 1 54  GLY 54  55  55  GLY GLY E . n 
E 1 55  VAL 55  56  56  VAL VAL E . n 
E 1 56  LYS 56  57  57  LYS LYS E . n 
E 1 57  PRO 57  58  58  PRO PRO E . n 
E 1 58  LEU 58  59  59  LEU LEU E . n 
E 1 59  ILE 59  60  60  ILE ILE E . n 
E 1 60  LEU 60  61  61  LEU LEU E . n 
E 1 61  ARG 61  62  62  ARG ARG E . n 
E 1 62  ASP 62  63  63  ASP ASP E . n 
E 1 63  CYS 63  64  64  CYS CYS E . n 
E 1 64  SER 64  65  65  SER SER E . n 
E 1 65  VAL 65  66  66  VAL VAL E . n 
E 1 66  ALA 66  67  67  ALA ALA E . n 
E 1 67  GLY 67  68  68  GLY GLY E . n 
E 1 68  TRP 68  69  69  TRP TRP E . n 
E 1 69  LEU 69  70  70  LEU LEU E . n 
E 1 70  LEU 70  71  71  LEU LEU E . n 
E 1 71  GLY 71  72  72  GLY GLY E . n 
E 1 72  ASN 72  73  73  ASN ASN E . n 
E 1 73  PRO 73  74  74  PRO PRO E . n 
E 1 74  MET 74  75  75  MET MET E . n 
E 1 75  CYS 75  76  76  CYS CYS E . n 
E 1 76  ASP 76  77  77  ASP ASP E . n 
E 1 77  GLU 77  78  78  GLU GLU E . n 
E 1 78  PHE 78  79  79  PHE PHE E . n 
E 1 79  ILE 79  80  80  ILE ILE E . n 
E 1 80  ASN 80  81  81  ASN ASN E . n 
E 1 81  VAL 81  82  82  VAL VAL E . n 
E 1 82  PRO 82  82  82  PRO PRO E A n 
E 1 83  GLU 83  83  83  GLU GLU E . n 
E 1 84  TRP 84  84  84  TRP TRP E . n 
E 1 85  SER 85  85  85  SER SER E . n 
E 1 86  TYR 86  86  86  TYR TYR E . n 
E 1 87  ILE 87  87  87  ILE ILE E . n 
E 1 88  VAL 88  88  88  VAL VAL E . n 
E 1 89  GLU 89  89  89  GLU GLU E . n 
E 1 90  LYS 90  90  90  LYS LYS E . n 
E 1 91  ALA 91  91  91  ALA ALA E . n 
E 1 92  SER 92  92  92  SER SER E . n 
E 1 93  PRO 93  93  93  PRO PRO E . n 
E 1 94  ALA 94  94  94  ALA ALA E . n 
E 1 95  ASN 95  95  95  ASN ASN E . n 
E 1 96  ASP 96  96  96  ASP ASP E . n 
E 1 97  LEU 97  96  96  LEU LEU E A n 
E 1 98  CYS 98  97  97  CYS CYS E . n 
E 1 99  TYR 99  98  98  TYR TYR E . n 
E 1 100 PRO 100 99  99  PRO PRO E . n 
E 1 101 GLY 101 100 100 GLY GLY E . n 
E 1 102 ASP 102 101 101 ASP ASP E . n 
E 1 103 PHE 103 102 102 PHE PHE E . n 
E 1 104 ASN 104 103 103 ASN ASN E . n 
E 1 105 ASN 105 104 104 ASN ASN E . n 
E 1 106 TYR 106 105 105 TYR TYR E . n 
E 1 107 GLU 107 106 106 GLU GLU E . n 
E 1 108 GLU 108 107 107 GLU GLU E . n 
E 1 109 LEU 109 108 108 LEU LEU E . n 
E 1 110 LYS 110 109 109 LYS LYS E . n 
E 1 111 HIS 111 110 110 HIS HIS E . n 
E 1 112 LEU 112 111 111 LEU LEU E . n 
E 1 113 LEU 113 112 112 LEU LEU E . n 
E 1 114 SER 114 113 113 SER SER E . n 
E 1 115 ARG 115 114 114 ARG ARG E . n 
E 1 116 THR 116 115 115 THR THR E . n 
E 1 117 ASN 117 116 116 ASN ASN E . n 
E 1 118 HIS 118 117 117 HIS HIS E . n 
E 1 119 PHE 119 118 118 PHE PHE E . n 
E 1 120 GLU 120 119 119 GLU GLU E . n 
E 1 121 LYS 121 120 120 LYS LYS E . n 
E 1 122 ILE 122 121 121 ILE ILE E . n 
E 1 123 GLN 123 122 122 GLN GLN E . n 
E 1 124 ILE 124 123 123 ILE ILE E . n 
E 1 125 ILE 125 124 124 ILE ILE E . n 
E 1 126 PRO 126 125 125 PRO PRO E . n 
E 1 127 LYS 127 125 125 LYS LYS E A n 
E 1 128 SER 128 125 125 SER SER E B n 
E 1 129 SER 129 126 126 SER SER E . n 
E 1 130 TRP 130 127 127 TRP TRP E . n 
E 1 131 SER 131 128 128 SER SER E . n 
E 1 132 ASN 132 129 129 ASN ASN E . n 
E 1 133 HIS 133 130 130 HIS HIS E . n 
E 1 134 ASP 134 131 131 ASP ASP E . n 
E 1 135 ALA 135 132 132 ALA ALA E . n 
E 1 136 SER 136 133 133 SER SER E . n 
E 1 137 SER 137 133 133 SER SER E A n 
E 1 138 GLY 138 134 134 GLY GLY E . n 
E 1 139 VAL 139 135 135 VAL VAL E . n 
E 1 140 SER 140 136 136 SER SER E . n 
E 1 141 SER 141 137 137 SER SER E . n 
E 1 142 ALA 142 138 138 ALA ALA E . n 
E 1 143 CYS 143 139 139 CYS CYS E . n 
E 1 144 PRO 144 140 140 PRO PRO E . n 
E 1 145 TYR 145 141 141 TYR TYR E . n 
E 1 146 HIS 146 142 142 HIS HIS E . n 
E 1 147 GLY 147 143 143 GLY GLY E . n 
E 1 148 LYS 148 144 144 LYS LYS E . n 
E 1 149 SER 149 145 145 SER SER E . n 
E 1 150 SER 150 146 146 SER SER E . n 
E 1 151 PHE 151 147 147 PHE PHE E . n 
E 1 152 PHE 152 148 148 PHE PHE E . n 
E 1 153 ARG 153 149 149 ARG ARG E . n 
E 1 154 ASN 154 150 150 ASN ASN E . n 
E 1 155 VAL 155 151 151 VAL VAL E . n 
E 1 156 VAL 156 152 152 VAL VAL E . n 
E 1 157 TRP 157 153 153 TRP TRP E . n 
E 1 158 LEU 158 154 154 LEU LEU E . n 
E 1 159 ILE 159 155 155 ILE ILE E . n 
E 1 160 LYS 160 156 156 LYS LYS E . n 
E 1 161 LYS 161 157 157 LYS LYS E . n 
E 1 162 ASN 162 158 158 ASN ASN E . n 
E 1 163 SER 163 159 159 SER SER E . n 
E 1 164 ALA 164 160 160 ALA ALA E . n 
E 1 165 TYR 165 161 161 TYR TYR E . n 
E 1 166 PRO 166 162 162 PRO PRO E . n 
E 1 167 THR 167 163 163 THR THR E . n 
E 1 168 ILE 168 164 164 ILE ILE E . n 
E 1 169 LYS 169 165 165 LYS LYS E . n 
E 1 170 ARG 170 166 166 ARG ARG E . n 
E 1 171 SER 171 167 167 SER SER E . n 
E 1 172 TYR 172 168 168 TYR TYR E . n 
E 1 173 ASN 173 169 169 ASN ASN E . n 
E 1 174 ASN 174 170 170 ASN ASN E . n 
E 1 175 THR 175 171 171 THR THR E . n 
E 1 176 ASN 176 172 172 ASN ASN E . n 
E 1 177 GLN 177 173 173 GLN GLN E . n 
E 1 178 GLU 178 174 174 GLU GLU E . n 
E 1 179 ASP 179 175 175 ASP ASP E . n 
E 1 180 LEU 180 176 176 LEU LEU E . n 
E 1 181 LEU 181 177 177 LEU LEU E . n 
E 1 182 VAL 182 178 178 VAL VAL E . n 
E 1 183 LEU 183 179 179 LEU LEU E . n 
E 1 184 TRP 184 180 180 TRP TRP E . n 
E 1 185 GLY 185 181 181 GLY GLY E . n 
E 1 186 ILE 186 182 182 ILE ILE E . n 
E 1 187 HIS 187 183 183 HIS HIS E . n 
E 1 188 HIS 188 184 184 HIS HIS E . n 
E 1 189 PRO 189 185 185 PRO PRO E . n 
E 1 190 ASN 190 186 186 ASN ASN E . n 
E 1 191 ASP 191 187 187 ASP ASP E . n 
E 1 192 ALA 192 188 188 ALA ALA E . n 
E 1 193 ALA 193 189 189 ALA ALA E . n 
E 1 194 GLU 194 190 190 GLU GLU E . n 
E 1 195 GLN 195 191 191 GLN GLN E . n 
E 1 196 THR 196 192 192 THR THR E . n 
E 1 197 LYS 197 193 193 LYS LYS E . n 
E 1 198 LEU 198 194 194 LEU LEU E . n 
E 1 199 TYR 199 195 195 TYR TYR E . n 
E 1 200 GLN 200 196 196 GLN GLN E . n 
E 1 201 ASN 201 197 197 ASN ASN E . n 
E 1 202 PRO 202 198 198 PRO PRO E . n 
E 1 203 THR 203 199 199 THR THR E . n 
E 1 204 THR 204 200 200 THR THR E . n 
E 1 205 TYR 205 201 201 TYR TYR E . n 
E 1 206 ILE 206 202 202 ILE ILE E . n 
E 1 207 SER 207 203 203 SER SER E . n 
E 1 208 VAL 208 204 204 VAL VAL E . n 
E 1 209 GLY 209 205 205 GLY GLY E . n 
E 1 210 THR 210 206 206 THR THR E . n 
E 1 211 SER 211 207 207 SER SER E . n 
E 1 212 THR 212 208 208 THR THR E . n 
E 1 213 LEU 213 209 209 LEU LEU E . n 
E 1 214 ASN 214 210 210 ASN ASN E . n 
E 1 215 GLN 215 211 211 GLN GLN E . n 
E 1 216 ARG 216 212 212 ARG ARG E . n 
E 1 217 LEU 217 213 213 LEU LEU E . n 
E 1 218 VAL 218 214 214 VAL VAL E . n 
E 1 219 PRO 219 215 215 PRO PRO E . n 
E 1 220 GLU 220 216 216 GLU GLU E . n 
E 1 221 ILE 221 217 217 ILE ILE E . n 
E 1 222 ALA 222 218 218 ALA ALA E . n 
E 1 223 THR 223 219 219 THR THR E . n 
E 1 224 ARG 224 220 220 ARG ARG E . n 
E 1 225 PRO 225 221 221 PRO PRO E . n 
E 1 226 LYS 226 222 222 LYS LYS E . n 
E 1 227 VAL 227 223 223 VAL VAL E . n 
E 1 228 ASN 228 224 224 ASN ASN E . n 
E 1 229 GLY 229 225 225 GLY GLY E . n 
E 1 230 GLN 230 226 226 GLN GLN E . n 
E 1 231 SER 231 227 227 SER SER E . n 
E 1 232 GLY 232 228 228 GLY GLY E . n 
E 1 233 ARG 233 229 229 ARG ARG E . n 
E 1 234 MET 234 230 230 MET MET E . n 
E 1 235 GLU 235 231 231 GLU GLU E . n 
E 1 236 PHE 236 232 232 PHE PHE E . n 
E 1 237 PHE 237 233 233 PHE PHE E . n 
E 1 238 TRP 238 234 234 TRP TRP E . n 
E 1 239 THR 239 235 235 THR THR E . n 
E 1 240 ILE 240 236 236 ILE ILE E . n 
E 1 241 LEU 241 237 237 LEU LEU E . n 
E 1 242 LYS 242 238 238 LYS LYS E . n 
E 1 243 PRO 243 239 239 PRO PRO E . n 
E 1 244 ASN 244 240 240 ASN ASN E . n 
E 1 245 ASP 245 241 241 ASP ASP E . n 
E 1 246 ALA 246 242 242 ALA ALA E . n 
E 1 247 ILE 247 243 243 ILE ILE E . n 
E 1 248 ASN 248 244 244 ASN ASN E . n 
E 1 249 PHE 249 245 245 PHE PHE E . n 
E 1 250 GLU 250 246 246 GLU GLU E . n 
E 1 251 SER 251 247 247 SER SER E . n 
E 1 252 ASN 252 248 248 ASN ASN E . n 
E 1 253 GLY 253 249 249 GLY GLY E . n 
E 1 254 ASN 254 250 250 ASN ASN E . n 
E 1 255 PHE 255 251 251 PHE PHE E . n 
E 1 256 ILE 256 252 252 ILE ILE E . n 
E 1 257 ALA 257 253 253 ALA ALA E . n 
E 1 258 PRO 258 254 254 PRO PRO E . n 
E 1 259 GLU 259 255 255 GLU GLU E . n 
E 1 260 TYR 260 256 256 TYR TYR E . n 
E 1 261 ALA 261 257 257 ALA ALA E . n 
E 1 262 TYR 262 258 258 TYR TYR E . n 
E 1 263 LYS 263 259 259 LYS LYS E . n 
E 1 264 ILE 264 260 260 ILE ILE E . n 
E 1 265 VAL 265 261 261 VAL VAL E . n 
E 1 266 LYS 266 262 262 LYS LYS E . n 
E 1 267 LYS 267 263 263 LYS LYS E . n 
E 1 268 GLY 268 264 264 GLY GLY E . n 
E 1 269 ASP 269 264 264 ASP ASP E A n 
E 1 270 SER 270 265 265 SER SER E . n 
E 1 271 ALA 271 266 266 ALA ALA E . n 
E 1 272 ILE 272 267 267 ILE ILE E . n 
E 1 273 MET 273 268 268 MET MET E . n 
E 1 274 LYS 274 269 269 LYS LYS E . n 
E 1 275 SER 275 270 270 SER SER E . n 
E 1 276 GLU 276 271 271 GLU GLU E . n 
E 1 277 LEU 277 272 272 LEU LEU E . n 
E 1 278 GLU 278 273 273 GLU GLU E . n 
E 1 279 TYR 279 274 274 TYR TYR E . n 
E 1 280 GLY 280 275 275 GLY GLY E . n 
E 1 281 ASN 281 276 276 ASN ASN E . n 
E 1 282 CYS 282 277 277 CYS CYS E . n 
E 1 283 ASN 283 278 278 ASN ASN E . n 
E 1 284 THR 284 279 279 THR THR E . n 
E 1 285 LYS 285 280 280 LYS LYS E . n 
E 1 286 CYS 286 281 281 CYS CYS E . n 
E 1 287 GLN 287 282 282 GLN GLN E . n 
E 1 288 THR 288 283 283 THR THR E . n 
E 1 289 PRO 289 284 284 PRO PRO E . n 
E 1 290 MET 290 285 285 MET MET E . n 
E 1 291 GLY 291 286 286 GLY GLY E . n 
E 1 292 ALA 292 287 287 ALA ALA E . n 
E 1 293 ILE 293 288 288 ILE ILE E . n 
E 1 294 ASN 294 289 289 ASN ASN E . n 
E 1 295 SER 295 290 290 SER SER E . n 
E 1 296 SER 296 291 291 SER SER E . n 
E 1 297 MET 297 292 292 MET MET E . n 
E 1 298 PRO 298 293 293 PRO PRO E . n 
E 1 299 PHE 299 294 294 PHE PHE E . n 
E 1 300 HIS 300 295 295 HIS HIS E . n 
E 1 301 ASN 301 296 296 ASN ASN E . n 
E 1 302 ILE 302 297 297 ILE ILE E . n 
E 1 303 HIS 303 298 298 HIS HIS E . n 
E 1 304 PRO 304 299 299 PRO PRO E . n 
E 1 305 LEU 305 300 300 LEU LEU E . n 
E 1 306 THR 306 301 301 THR THR E . n 
E 1 307 ILE 307 302 302 ILE ILE E . n 
E 1 308 GLY 308 303 303 GLY GLY E . n 
E 1 309 GLU 309 304 304 GLU GLU E . n 
E 1 310 CYS 310 305 305 CYS CYS E . n 
E 1 311 PRO 311 306 306 PRO PRO E . n 
E 1 312 LYS 312 307 307 LYS LYS E . n 
E 1 313 TYR 313 308 308 TYR TYR E . n 
E 1 314 VAL 314 309 309 VAL VAL E . n 
E 1 315 LYS 315 310 310 LYS LYS E . n 
E 1 316 SER 316 311 311 SER SER E . n 
E 1 317 ASN 317 312 312 ASN ASN E . n 
E 1 318 ARG 318 313 313 ARG ARG E . n 
E 1 319 LEU 319 314 314 LEU LEU E . n 
E 1 320 VAL 320 315 315 VAL VAL E . n 
E 1 321 LEU 321 316 316 LEU LEU E . n 
E 1 322 ALA 322 317 317 ALA ALA E . n 
E 1 323 THR 323 318 318 THR THR E . n 
E 1 324 GLY 324 319 319 GLY GLY E . n 
E 1 325 LEU 325 320 320 LEU LEU E . n 
E 1 326 ARG 326 321 321 ARG ARG E . n 
E 1 327 ASN 327 322 322 ASN ASN E . n 
E 1 328 THR 328 323 323 THR THR E . n 
E 1 329 PRO 329 324 ?   ?   ?   E . n 
E 1 330 GLN 330 325 ?   ?   ?   E . n 
E 1 331 ARG 331 326 ?   ?   ?   E . n 
F 2 1   GLY 1   1   1   GLY GLY F . n 
F 2 2   LEU 2   2   2   LEU LEU F . n 
F 2 3   PHE 3   3   3   PHE PHE F . n 
F 2 4   GLY 4   4   4   GLY GLY F . n 
F 2 5   ALA 5   5   5   ALA ALA F . n 
F 2 6   ILE 6   6   6   ILE ILE F . n 
F 2 7   ALA 7   7   7   ALA ALA F . n 
F 2 8   GLY 8   8   8   GLY GLY F . n 
F 2 9   PHE 9   9   9   PHE PHE F . n 
F 2 10  ILE 10  10  10  ILE ILE F . n 
F 2 11  GLU 11  11  11  GLU GLU F . n 
F 2 12  GLY 12  12  12  GLY GLY F . n 
F 2 13  GLY 13  13  13  GLY GLY F . n 
F 2 14  TRP 14  14  14  TRP TRP F . n 
F 2 15  GLN 15  15  15  GLN GLN F . n 
F 2 16  GLY 16  16  16  GLY GLY F . n 
F 2 17  MET 17  17  17  MET MET F . n 
F 2 18  VAL 18  18  18  VAL VAL F . n 
F 2 19  ASP 19  19  19  ASP ASP F . n 
F 2 20  GLY 20  20  20  GLY GLY F . n 
F 2 21  TRP 21  21  21  TRP TRP F . n 
F 2 22  TYR 22  22  22  TYR TYR F . n 
F 2 23  GLY 23  23  23  GLY GLY F . n 
F 2 24  TYR 24  24  24  TYR TYR F . n 
F 2 25  HIS 25  25  25  HIS HIS F . n 
F 2 26  HIS 26  26  26  HIS HIS F . n 
F 2 27  SER 27  27  27  SER SER F . n 
F 2 28  ASN 28  28  28  ASN ASN F . n 
F 2 29  GLU 29  29  29  GLU GLU F . n 
F 2 30  GLN 30  30  30  GLN GLN F . n 
F 2 31  GLY 31  31  31  GLY GLY F . n 
F 2 32  SER 32  32  32  SER SER F . n 
F 2 33  GLY 33  33  33  GLY GLY F . n 
F 2 34  TYR 34  34  34  TYR TYR F . n 
F 2 35  ALA 35  35  35  ALA ALA F . n 
F 2 36  ALA 36  36  36  ALA ALA F . n 
F 2 37  ASP 37  37  37  ASP ASP F . n 
F 2 38  LYS 38  38  38  LYS LYS F . n 
F 2 39  GLU 39  39  39  GLU GLU F . n 
F 2 40  SER 40  40  40  SER SER F . n 
F 2 41  THR 41  41  41  THR THR F . n 
F 2 42  GLN 42  42  42  GLN GLN F . n 
F 2 43  LYS 43  43  43  LYS LYS F . n 
F 2 44  ALA 44  44  44  ALA ALA F . n 
F 2 45  ILE 45  45  45  ILE ILE F . n 
F 2 46  ASP 46  46  46  ASP ASP F . n 
F 2 47  GLY 47  47  47  GLY GLY F . n 
F 2 48  VAL 48  48  48  VAL VAL F . n 
F 2 49  THR 49  49  49  THR THR F . n 
F 2 50  ASN 50  50  50  ASN ASN F . n 
F 2 51  LYS 51  51  51  LYS LYS F . n 
F 2 52  VAL 52  52  52  VAL VAL F . n 
F 2 53  ASN 53  53  53  ASN ASN F . n 
F 2 54  SER 54  54  54  SER SER F . n 
F 2 55  ILE 55  55  55  ILE ILE F . n 
F 2 56  ILE 56  56  56  ILE ILE F . n 
F 2 57  ASP 57  57  57  ASP ASP F . n 
F 2 58  LYS 58  58  58  LYS LYS F . n 
F 2 59  MET 59  59  59  MET MET F . n 
F 2 60  ASN 60  60  60  ASN ASN F . n 
F 2 61  THR 61  61  61  THR THR F . n 
F 2 62  GLN 62  62  62  GLN GLN F . n 
F 2 63  PHE 63  63  63  PHE PHE F . n 
F 2 64  GLU 64  64  64  GLU GLU F . n 
F 2 65  ALA 65  65  65  ALA ALA F . n 
F 2 66  VAL 66  66  66  VAL VAL F . n 
F 2 67  GLY 67  67  67  GLY GLY F . n 
F 2 68  ARG 68  68  68  ARG ARG F . n 
F 2 69  GLU 69  69  69  GLU GLU F . n 
F 2 70  PHE 70  70  70  PHE PHE F . n 
F 2 71  ASN 71  71  71  ASN ASN F . n 
F 2 72  ASN 72  72  72  ASN ASN F . n 
F 2 73  LEU 73  73  73  LEU LEU F . n 
F 2 74  GLU 74  74  74  GLU GLU F . n 
F 2 75  ARG 75  75  75  ARG ARG F . n 
F 2 76  ARG 76  76  76  ARG ARG F . n 
F 2 77  ILE 77  77  77  ILE ILE F . n 
F 2 78  GLU 78  78  78  GLU GLU F . n 
F 2 79  ASN 79  79  79  ASN ASN F . n 
F 2 80  LEU 80  80  80  LEU LEU F . n 
F 2 81  ASN 81  81  81  ASN ASN F . n 
F 2 82  LYS 82  82  82  LYS LYS F . n 
F 2 83  LYS 83  83  83  LYS LYS F . n 
F 2 84  MET 84  84  84  MET MET F . n 
F 2 85  GLU 85  85  85  GLU GLU F . n 
F 2 86  ASP 86  86  86  ASP ASP F . n 
F 2 87  GLY 87  87  87  GLY GLY F . n 
F 2 88  PHE 88  88  88  PHE PHE F . n 
F 2 89  LEU 89  89  89  LEU LEU F . n 
F 2 90  ASP 90  90  90  ASP ASP F . n 
F 2 91  VAL 91  91  91  VAL VAL F . n 
F 2 92  TRP 92  92  92  TRP TRP F . n 
F 2 93  THR 93  93  93  THR THR F . n 
F 2 94  TYR 94  94  94  TYR TYR F . n 
F 2 95  ASN 95  95  95  ASN ASN F . n 
F 2 96  ALA 96  96  96  ALA ALA F . n 
F 2 97  GLU 97  97  97  GLU GLU F . n 
F 2 98  LEU 98  98  98  LEU LEU F . n 
F 2 99  LEU 99  99  99  LEU LEU F . n 
F 2 100 VAL 100 100 100 VAL VAL F . n 
F 2 101 LEU 101 101 101 LEU LEU F . n 
F 2 102 MET 102 102 102 MET MET F . n 
F 2 103 GLU 103 103 103 GLU GLU F . n 
F 2 104 ASN 104 104 104 ASN ASN F . n 
F 2 105 GLU 105 105 105 GLU GLU F . n 
F 2 106 ARG 106 106 106 ARG ARG F . n 
F 2 107 THR 107 107 107 THR THR F . n 
F 2 108 LEU 108 108 108 LEU LEU F . n 
F 2 109 ASP 109 109 109 ASP ASP F . n 
F 2 110 PHE 110 110 110 PHE PHE F . n 
F 2 111 HIS 111 111 111 HIS HIS F . n 
F 2 112 ASP 112 112 112 ASP ASP F . n 
F 2 113 SER 113 113 113 SER SER F . n 
F 2 114 ASN 114 114 114 ASN ASN F . n 
F 2 115 VAL 115 115 115 VAL VAL F . n 
F 2 116 LYS 116 116 116 LYS LYS F . n 
F 2 117 ASN 117 117 117 ASN ASN F . n 
F 2 118 LEU 118 118 118 LEU LEU F . n 
F 2 119 TYR 119 119 119 TYR TYR F . n 
F 2 120 ASP 120 120 120 ASP ASP F . n 
F 2 121 LYS 121 121 121 LYS LYS F . n 
F 2 122 VAL 122 122 122 VAL VAL F . n 
F 2 123 ARG 123 123 123 ARG ARG F . n 
F 2 124 LEU 124 124 124 LEU LEU F . n 
F 2 125 GLN 125 125 125 GLN GLN F . n 
F 2 126 LEU 126 126 126 LEU LEU F . n 
F 2 127 ARG 127 127 127 ARG ARG F . n 
F 2 128 ASP 128 128 128 ASP ASP F . n 
F 2 129 ASN 129 129 129 ASN ASN F . n 
F 2 130 ALA 130 130 130 ALA ALA F . n 
F 2 131 LYS 131 131 131 LYS LYS F . n 
F 2 132 GLU 132 132 132 GLU GLU F . n 
F 2 133 LEU 133 133 133 LEU LEU F . n 
F 2 134 GLY 134 134 134 GLY GLY F . n 
F 2 135 ASN 135 135 135 ASN ASN F . n 
F 2 136 GLY 136 136 136 GLY GLY F . n 
F 2 137 CYS 137 137 137 CYS CYS F . n 
F 2 138 PHE 138 138 138 PHE PHE F . n 
F 2 139 GLU 139 139 139 GLU GLU F . n 
F 2 140 PHE 140 140 140 PHE PHE F . n 
F 2 141 TYR 141 141 141 TYR TYR F . n 
F 2 142 HIS 142 142 142 HIS HIS F . n 
F 2 143 LYS 143 143 143 LYS LYS F . n 
F 2 144 CYS 144 144 144 CYS CYS F . n 
F 2 145 ASP 145 145 145 ASP ASP F . n 
F 2 146 ASN 146 146 146 ASN ASN F . n 
F 2 147 GLU 147 147 147 GLU GLU F . n 
F 2 148 CYS 148 148 148 CYS CYS F . n 
F 2 149 MET 149 149 149 MET MET F . n 
F 2 150 GLU 150 150 150 GLU GLU F . n 
F 2 151 SER 151 151 151 SER SER F . n 
F 2 152 VAL 152 152 152 VAL VAL F . n 
F 2 153 LYS 153 153 153 LYS LYS F . n 
F 2 154 ASN 154 154 154 ASN ASN F . n 
F 2 155 GLY 155 155 155 GLY GLY F . n 
F 2 156 THR 156 156 156 THR THR F . n 
F 2 157 TYR 157 157 157 TYR TYR F . n 
F 2 158 ASP 158 158 158 ASP ASP F . n 
F 2 159 TYR 159 159 159 TYR TYR F . n 
F 2 160 PRO 160 160 160 PRO PRO F . n 
F 2 161 GLN 161 161 161 GLN GLN F . n 
F 2 162 TYR 162 162 162 TYR TYR F . n 
F 2 163 SER 163 163 163 SER SER F . n 
F 2 164 GLU 164 164 164 GLU GLU F . n 
F 2 165 GLU 165 165 165 GLU GLU F . n 
F 2 166 ALA 166 166 166 ALA ALA F . n 
F 2 167 ARG 167 167 167 ARG ARG F . n 
F 2 168 LEU 168 168 168 LEU LEU F . n 
F 2 169 ASN 169 169 169 ASN ASN F . n 
F 2 170 ARG 170 170 170 ARG ARG F . n 
F 2 171 GLU 171 171 171 GLU GLU F . n 
F 2 172 GLU 172 172 172 GLU GLU F . n 
F 2 173 ILE 173 173 173 ILE ILE F . n 
F 2 174 SER 174 174 ?   ?   ?   F . n 
F 2 175 GLY 175 175 ?   ?   ?   F . n 
F 2 176 VAL 176 176 ?   ?   ?   F . n 
F 2 177 ARG 177 177 ?   ?   ?   F . n 
F 2 178 SER 178 178 ?   ?   ?   F . n 
F 2 179 LEU 179 179 ?   ?   ?   F . n 
F 2 180 VAL 180 180 ?   ?   ?   F . n 
F 2 181 PRO 181 181 ?   ?   ?   F . n 
F 2 182 ARG 182 182 ?   ?   ?   F . n 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A ASN 31  A ASN 34  ? ASN 'GLYCOSYLATION SITE' 
2 E ASN 31  E ASN 34  ? ASN 'GLYCOSYLATION SITE' 
3 C ASN 31  C ASN 34  ? ASN 'GLYCOSYLATION SITE' 
4 E ASN 173 E ASN 169 ? ASN 'GLYCOSYLATION SITE' 
5 A ASN 173 A ASN 169 ? ASN 'GLYCOSYLATION SITE' 
6 C ASN 173 C ASN 169 ? ASN 'GLYCOSYLATION SITE' 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   hexameric 
_pdbx_struct_assembly.oligomeric_count     6 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 31210 ? 
1 MORE         -120  ? 
1 'SSA (A^2)'  61720 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2011-12-14 
2 'Structure model' 1 1 2012-03-28 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_phasing_MR.entry_id                     3S11 
_pdbx_phasing_MR.method_rotation              ? 
_pdbx_phasing_MR.method_translation           ? 
_pdbx_phasing_MR.model_details                'Phaser MODE: MR_AUTO' 
_pdbx_phasing_MR.R_factor                     49.040 
_pdbx_phasing_MR.R_rigid_body                 ? 
_pdbx_phasing_MR.correlation_coeff_Fo_to_Fc   ? 
_pdbx_phasing_MR.correlation_coeff_Io_to_Ic   ? 
_pdbx_phasing_MR.d_res_high_rotation          3.440 
_pdbx_phasing_MR.d_res_low_rotation           49.120 
_pdbx_phasing_MR.d_res_high_translation       3.440 
_pdbx_phasing_MR.d_res_low_translation        49.120 
_pdbx_phasing_MR.packing                      ? 
_pdbx_phasing_MR.reflns_percent_rotation      ? 
_pdbx_phasing_MR.reflns_percent_translation   ? 
_pdbx_phasing_MR.sigma_F_rotation             ? 
_pdbx_phasing_MR.sigma_F_translation          ? 
_pdbx_phasing_MR.sigma_I_rotation             ? 
_pdbx_phasing_MR.sigma_I_translation          ? 
# 
_phasing.method   MR 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 SCALEPACK   .     ?                          program 'Zbyszek Otwinowski' hkl@hkl-xray.com            'data scaling'    
http://www.hkl-xray.com/                     ?          ? 
2 PHASER      2.1.4 'Wed Oct 28 14:30:30 2009' program 'Randy J. Read'      cimr-phaser@lists.cam.ac.uk phasing           
http://www-structmed.cimr.cam.ac.uk/phaser/  ?          ? 
3 REFMAC      .     ?                          program 'Garib N. Murshudov' garib@ysbl.york.ac.uk       refinement        
http://www.ccp4.ac.uk/dist/html/refmac5.html Fortran_77 ? 
4 PDB_EXTRACT 3.10  'June 10, 2010'            package PDB                  deposit@deposit.rcsb.org    'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/    C++        ? 
5 HKL-2000    .     ?                          ?       ?                    ?                           'data collection' ? ? ? 
6 HKL-2000    .     ?                          ?       ?                    ?                           'data reduction'  ? ? ? 
# 
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 ARG A 62  ? ? 58.57   -117.26 
2  1 ASP A 96  ? ? -111.19 -91.85  
3  1 GLN A 196 ? ? 73.40   -59.35  
4  1 THR A 206 ? ? -108.71 -168.92 
5  1 GLU A 255 ? ? -125.90 -51.35  
6  1 ALA B 5   ? ? -100.81 -63.89  
7  1 THR B 61  ? ? -107.25 43.09   
8  1 ARG B 127 ? ? 53.13   -132.41 
9  1 ASN B 129 ? ? -67.55  2.56    
10 1 PRO B 160 ? ? -71.03  25.39   
11 1 ARG C 62  ? ? 52.10   -115.99 
12 1 ASP C 96  ? ? -110.20 -87.40  
13 1 TYR C 141 ? ? -101.71 -69.99  
14 1 HIS C 142 ? ? -86.53  -75.59  
15 1 SER C 146 ? ? -139.59 -159.62 
16 1 GLN C 196 ? ? 67.02   -59.98  
17 1 THR C 206 ? ? -120.42 -160.00 
18 1 ASN C 240 ? ? 81.65   -6.73   
19 1 HIS C 298 ? ? -170.06 139.54  
20 1 ASN D 28  ? ? -111.26 -160.83 
21 1 ARG D 127 ? ? 53.60   -122.33 
22 1 ARG E 62  ? ? 55.69   -114.60 
23 1 ASP E 96  ? ? -111.36 -91.03  
24 1 TYR E 141 ? ? -113.05 -90.12  
25 1 HIS E 142 ? ? -105.41 69.98   
26 1 SER E 159 ? ? 49.52   29.06   
27 1 GLN E 196 ? ? 69.09   -49.96  
28 1 ASN E 240 ? ? 78.47   -4.64   
29 1 ASN E 250 ? ? 58.83   16.80   
30 1 ALA F 5   ? ? -106.00 -65.87  
31 1 ARG F 127 ? ? 53.10   -134.88 
32 1 GLU F 164 ? ? -69.81  -71.10  
# 
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 ASP 3   ? A ASP 1   
2  1 Y 1 A LEU 4   ? A LEU 2   
3  1 Y 1 A GLY 5   ? A GLY 3   
4  1 Y 1 A SER 6   ? A SER 4   
5  1 Y 1 A ALA 7   ? A ALA 5   
6  1 Y 1 A ASP 8   ? A ASP 6   
7  1 Y 1 A PRO 324 ? A PRO 329 
8  1 Y 1 A GLN 325 ? A GLN 330 
9  1 Y 1 A ARG 326 ? A ARG 331 
10 1 Y 1 B GLU 171 ? B GLU 171 
11 1 Y 1 B GLU 172 ? B GLU 172 
12 1 Y 1 B ILE 173 ? B ILE 173 
13 1 Y 1 B SER 174 ? B SER 174 
14 1 Y 1 B GLY 175 ? B GLY 175 
15 1 Y 1 B VAL 176 ? B VAL 176 
16 1 Y 1 B ARG 177 ? B ARG 177 
17 1 Y 1 B SER 178 ? B SER 178 
18 1 Y 1 B LEU 179 ? B LEU 179 
19 1 Y 1 B VAL 180 ? B VAL 180 
20 1 Y 1 B PRO 181 ? B PRO 181 
21 1 Y 1 B ARG 182 ? B ARG 182 
22 1 Y 1 C ASP 3   ? C ASP 1   
23 1 Y 1 C LEU 4   ? C LEU 2   
24 1 Y 1 C GLY 5   ? C GLY 3   
25 1 Y 1 C SER 6   ? C SER 4   
26 1 Y 1 C ALA 7   ? C ALA 5   
27 1 Y 1 C ASP 8   ? C ASP 6   
28 1 Y 1 C PRO 9   ? C PRO 7   
29 1 Y 1 C PRO 324 ? C PRO 329 
30 1 Y 1 C GLN 325 ? C GLN 330 
31 1 Y 1 C ARG 326 ? C ARG 331 
32 1 Y 1 D ILE 173 ? D ILE 173 
33 1 Y 1 D SER 174 ? D SER 174 
34 1 Y 1 D GLY 175 ? D GLY 175 
35 1 Y 1 D VAL 176 ? D VAL 176 
36 1 Y 1 D ARG 177 ? D ARG 177 
37 1 Y 1 D SER 178 ? D SER 178 
38 1 Y 1 D LEU 179 ? D LEU 179 
39 1 Y 1 D VAL 180 ? D VAL 180 
40 1 Y 1 D PRO 181 ? D PRO 181 
41 1 Y 1 D ARG 182 ? D ARG 182 
42 1 Y 1 E ASP 3   ? E ASP 1   
43 1 Y 1 E LEU 4   ? E LEU 2   
44 1 Y 1 E GLY 5   ? E GLY 3   
45 1 Y 1 E SER 6   ? E SER 4   
46 1 Y 1 E ALA 7   ? E ALA 5   
47 1 Y 1 E ASP 8   ? E ASP 6   
48 1 Y 1 E PRO 324 ? E PRO 329 
49 1 Y 1 E GLN 325 ? E GLN 330 
50 1 Y 1 E ARG 326 ? E ARG 331 
51 1 Y 1 F SER 174 ? F SER 174 
52 1 Y 1 F GLY 175 ? F GLY 175 
53 1 Y 1 F VAL 176 ? F VAL 176 
54 1 Y 1 F ARG 177 ? F ARG 177 
55 1 Y 1 F SER 178 ? F SER 178 
56 1 Y 1 F LEU 179 ? F LEU 179 
57 1 Y 1 F VAL 180 ? F VAL 180 
58 1 Y 1 F PRO 181 ? F PRO 181 
59 1 Y 1 F ARG 182 ? F ARG 182 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 N-ACETYL-D-GLUCOSAMINE           NAG 
4 GLYCEROL                         GOL 
5 'TRIS(HYDROXYETHYL)AMINOMETHANE' TAM 
6 BETA-D-MANNOSE                   BMA 
7 water                            HOH 
# 
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 
G 3 NAG 1  1   1   NAG NAG A . 
H 3 NAG 1  2   2   NAG NAG A . 
I 3 NAG 2  327 327 NAG NAG A . 
J 4 GOL 1  328 328 GOL GOL A . 
K 5 TAM 1  329 329 TAM TAM A . 
L 3 NAG 1  327 327 NAG NAG C . 
M 3 NAG 1  328 328 NAG NAG C . 
N 3 NAG 2  329 329 NAG NAG C . 
O 6 BMA 3  330 330 BMA BMA C . 
P 4 GOL 1  2   2   GOL GOL C . 
Q 3 NAG 1  327 327 NAG NAG E . 
R 3 NAG 1  328 328 NAG NAG E . 
S 3 NAG 2  329 329 NAG NAG E . 
T 4 GOL 1  330 330 GOL GOL E . 
U 7 HOH 1  29  29  HOH HOH A . 
U 7 HOH 2  30  30  HOH HOH A . 
U 7 HOH 3  330 330 HOH HOH A . 
U 7 HOH 4  331 331 HOH HOH A . 
U 7 HOH 5  332 332 HOH HOH A . 
U 7 HOH 6  333 333 HOH HOH A . 
U 7 HOH 7  334 334 HOH HOH A . 
U 7 HOH 8  335 335 HOH HOH A . 
U 7 HOH 9  336 336 HOH HOH A . 
U 7 HOH 10 337 337 HOH HOH A . 
U 7 HOH 11 338 338 HOH HOH A . 
U 7 HOH 12 339 339 HOH HOH A . 
U 7 HOH 13 340 340 HOH HOH A . 
U 7 HOH 14 341 341 HOH HOH A . 
U 7 HOH 15 342 342 HOH HOH A . 
U 7 HOH 16 343 343 HOH HOH A . 
U 7 HOH 17 344 344 HOH HOH A . 
U 7 HOH 18 345 345 HOH HOH A . 
U 7 HOH 19 346 346 HOH HOH A . 
U 7 HOH 20 347 347 HOH HOH A . 
U 7 HOH 21 348 348 HOH HOH A . 
U 7 HOH 22 349 349 HOH HOH A . 
U 7 HOH 23 350 350 HOH HOH A . 
U 7 HOH 24 351 351 HOH HOH A . 
U 7 HOH 25 352 352 HOH HOH A . 
U 7 HOH 26 353 353 HOH HOH A . 
U 7 HOH 27 354 354 HOH HOH A . 
U 7 HOH 28 355 355 HOH HOH A . 
U 7 HOH 29 356 356 HOH HOH A . 
U 7 HOH 30 357 357 HOH HOH A . 
U 7 HOH 31 358 358 HOH HOH A . 
U 7 HOH 32 359 359 HOH HOH A . 
U 7 HOH 33 360 360 HOH HOH A . 
U 7 HOH 34 361 361 HOH HOH A . 
U 7 HOH 35 362 362 HOH HOH A . 
U 7 HOH 36 363 363 HOH HOH A . 
U 7 HOH 37 364 364 HOH HOH A . 
U 7 HOH 38 365 365 HOH HOH A . 
V 7 HOH 1  183 183 HOH HOH B . 
V 7 HOH 2  184 184 HOH HOH B . 
V 7 HOH 3  185 185 HOH HOH B . 
V 7 HOH 4  186 186 HOH HOH B . 
V 7 HOH 5  187 187 HOH HOH B . 
V 7 HOH 6  188 188 HOH HOH B . 
V 7 HOH 7  189 189 HOH HOH B . 
V 7 HOH 8  190 190 HOH HOH B . 
V 7 HOH 9  191 191 HOH HOH B . 
V 7 HOH 10 192 192 HOH HOH B . 
V 7 HOH 11 193 193 HOH HOH B . 
V 7 HOH 12 194 194 HOH HOH B . 
V 7 HOH 13 195 195 HOH HOH B . 
V 7 HOH 14 196 196 HOH HOH B . 
V 7 HOH 15 197 197 HOH HOH B . 
V 7 HOH 16 198 198 HOH HOH B . 
W 7 HOH 1  331 331 HOH HOH C . 
W 7 HOH 2  332 332 HOH HOH C . 
W 7 HOH 3  333 333 HOH HOH C . 
W 7 HOH 4  334 334 HOH HOH C . 
W 7 HOH 5  335 335 HOH HOH C . 
W 7 HOH 6  336 336 HOH HOH C . 
W 7 HOH 7  337 337 HOH HOH C . 
W 7 HOH 8  338 338 HOH HOH C . 
W 7 HOH 9  339 339 HOH HOH C . 
W 7 HOH 10 340 340 HOH HOH C . 
W 7 HOH 11 341 341 HOH HOH C . 
W 7 HOH 12 342 342 HOH HOH C . 
W 7 HOH 13 343 343 HOH HOH C . 
W 7 HOH 14 344 344 HOH HOH C . 
W 7 HOH 15 345 345 HOH HOH C . 
W 7 HOH 16 346 346 HOH HOH C . 
W 7 HOH 17 347 347 HOH HOH C . 
W 7 HOH 18 348 348 HOH HOH C . 
W 7 HOH 19 349 349 HOH HOH C . 
W 7 HOH 20 350 350 HOH HOH C . 
W 7 HOH 21 351 351 HOH HOH C . 
W 7 HOH 22 352 352 HOH HOH C . 
W 7 HOH 23 353 353 HOH HOH C . 
W 7 HOH 24 354 354 HOH HOH C . 
W 7 HOH 25 355 355 HOH HOH C . 
W 7 HOH 26 356 356 HOH HOH C . 
W 7 HOH 27 357 357 HOH HOH C . 
W 7 HOH 28 358 358 HOH HOH C . 
W 7 HOH 29 359 359 HOH HOH C . 
W 7 HOH 30 360 360 HOH HOH C . 
W 7 HOH 31 361 361 HOH HOH C . 
W 7 HOH 32 362 362 HOH HOH C . 
W 7 HOH 33 363 363 HOH HOH C . 
W 7 HOH 34 364 364 HOH HOH C . 
W 7 HOH 35 365 365 HOH HOH C . 
W 7 HOH 36 366 366 HOH HOH C . 
W 7 HOH 37 367 367 HOH HOH C . 
W 7 HOH 38 368 368 HOH HOH C . 
W 7 HOH 39 369 369 HOH HOH C . 
W 7 HOH 40 370 370 HOH HOH C . 
W 7 HOH 41 371 371 HOH HOH C . 
W 7 HOH 42 372 372 HOH HOH C . 
W 7 HOH 43 373 373 HOH HOH C . 
X 7 HOH 1  183 183 HOH HOH D . 
X 7 HOH 2  184 184 HOH HOH D . 
X 7 HOH 3  185 185 HOH HOH D . 
X 7 HOH 4  186 186 HOH HOH D . 
X 7 HOH 5  187 187 HOH HOH D . 
X 7 HOH 6  188 188 HOH HOH D . 
X 7 HOH 7  189 189 HOH HOH D . 
X 7 HOH 8  190 190 HOH HOH D . 
X 7 HOH 9  191 191 HOH HOH D . 
Y 7 HOH 1  1   1   HOH HOH E . 
Y 7 HOH 2  331 331 HOH HOH E . 
Y 7 HOH 3  332 332 HOH HOH E . 
Y 7 HOH 4  333 333 HOH HOH E . 
Y 7 HOH 5  334 334 HOH HOH E . 
Y 7 HOH 6  335 335 HOH HOH E . 
Y 7 HOH 7  336 336 HOH HOH E . 
Y 7 HOH 8  337 337 HOH HOH E . 
Y 7 HOH 9  338 338 HOH HOH E . 
Y 7 HOH 10 339 339 HOH HOH E . 
Y 7 HOH 11 340 340 HOH HOH E . 
Y 7 HOH 12 341 341 HOH HOH E . 
Y 7 HOH 13 342 342 HOH HOH E . 
Y 7 HOH 14 343 343 HOH HOH E . 
Y 7 HOH 15 344 344 HOH HOH E . 
Y 7 HOH 16 345 345 HOH HOH E . 
Y 7 HOH 17 346 346 HOH HOH E . 
Y 7 HOH 18 347 347 HOH HOH E . 
Z 7 HOH 1  183 183 HOH HOH F . 
Z 7 HOH 2  184 184 HOH HOH F . 
Z 7 HOH 3  185 185 HOH HOH F . 
Z 7 HOH 4  186 186 HOH HOH F . 
Z 7 HOH 5  187 187 HOH HOH F . 
Z 7 HOH 6  188 188 HOH HOH F . 
Z 7 HOH 7  189 189 HOH HOH F . 
Z 7 HOH 8  190 190 HOH HOH F . 
Z 7 HOH 9  191 191 HOH HOH F . 
# 
